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  • 1
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    MARF1 regulates essential oogenic processes in mice (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-24
    Description: Development of fertilization-competent oocytes depends on integrated processes controlling meiosis, cytoplasmic development, and maintenance of genomic integrity. We show that meiosis arrest female 1 (MARF1) is required for these processes in mammalian oocytes. Mutations of Marf1 cause female infertility characterized by up-regulation of a cohort of transcripts, increased retrotransposon expression, defective cytoplasmic maturation, and meiotic arrest. Up-regulation of protein phosphatase 2 catalytic subunit (PPP2CB) is key to the meiotic arrest phenotype. Moreover, Iap and Line1 retrotransposon messenger RNAs are also up-regulated, and, concomitantly, DNA double-strand breaks are elevated in mutant oocytes. Therefore MARF1, by suppressing levels of specific transcripts, is an essential regulator of important oogenic processes leading to female fertility and the development of healthy offspring.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3612990/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3612990/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, You-Qiang -- Sugiura, Koji -- Sun, Fengyun -- Pendola, Janice K -- Cox, Gregory A -- Handel, Mary Ann -- Schimenti, John C -- Eppig, John J -- CA34196/CA/NCI NIH HHS/ -- HD42137/HD/NICHD NIH HHS/ -- P01 HD042137/HD/NICHD NIH HHS/ -- P30 CA034196/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2012 Mar 23;335(6075):1496-9. doi: 10.1126/science.1214680.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Jackson Laboratory, Bar Harbor, ME 04609, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22442484" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; DNA Breaks, Double-Stranded ; Embryonic Development ; Female ; *Fertility ; Meiosis ; Mice ; Molecular Sequence Data ; Mutation ; Oocytes/*physiology ; *Oogenesis ; Phenotype ; Protein Phosphatase 2/genetics/metabolism ; Protein Structure, Tertiary ; RNA, Messenger/genetics/metabolism ; Retroelements ; Transcription, Genetic ; Transcriptome ; Up-Regulation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    The ancient drug salicylate directly activates AMP-activated protein kinase (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-04-21
    Description: Salicylate, a plant product, has been in medicinal use since ancient times. More recently, it has been replaced by synthetic derivatives such as aspirin and salsalate, both of which are rapidly broken down to salicylate in vivo. At concentrations reached in plasma after administration of salsalate or of aspirin at high doses, salicylate activates adenosine monophosphate-activated protein kinase (AMPK), a central regulator of cell growth and metabolism. Salicylate binds at the same site as the synthetic activator A-769662 to cause allosteric activation and inhibition of dephosphorylation of the activating phosphorylation site, threonine-172. In AMPK knockout mice, effects of salicylate to increase fat utilization and to lower plasma fatty acids in vivo were lost. Our results suggest that AMPK activation could explain some beneficial effects of salsalate and aspirin in humans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399766/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399766/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hawley, Simon A -- Fullerton, Morgan D -- Ross, Fiona A -- Schertzer, Jonathan D -- Chevtzoff, Cyrille -- Walker, Katherine J -- Peggie, Mark W -- Zibrova, Darya -- Green, Kevin A -- Mustard, Kirsty J -- Kemp, Bruce E -- Sakamoto, Kei -- Steinberg, Gregory R -- Hardie, D Grahame -- 080982/Wellcome Trust/United Kingdom -- 097726/Wellcome Trust/United Kingdom -- MC_U127088492/Medical Research Council/United Kingdom -- Canadian Institutes of Health Research/Canada -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2012 May 18;336(6083):918-22. doi: 10.1126/science.1215327. Epub 2012 Apr 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cell Signalling and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22517326" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases/genetics/*metabolism ; Amino Acid Substitution ; Animals ; Aspirin/pharmacology ; Binding Sites ; Carbohydrate Metabolism/drug effects ; Cell Line ; Enzyme Activation ; Enzyme Activators/pharmacology ; HEK293 Cells ; Humans ; Lipid Metabolism/drug effects ; Liver/drug effects/metabolism ; Mice ; Mice, Knockout ; Mutation ; Oxygen Consumption/drug effects ; Phosphorylation ; Pyrones/pharmacology ; Rats ; Salicylates/blood/*metabolism/*pharmacology ; Thiophenes/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Airborne transmission of influenza A/H5N1 virus between ferrets (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: Highly pathogenic avian influenza A/H5N1 virus can cause morbidity and mortality in humans but thus far has not acquired the ability to be transmitted by aerosol or respiratory droplet ("airborne transmission") between humans. To address the concern that the virus could acquire this ability under natural conditions, we genetically modified A/H5N1 virus by site-directed mutagenesis and subsequent serial passage in ferrets. The genetically modified A/H5N1 virus acquired mutations during passage in ferrets, ultimately becoming airborne transmissible in ferrets. None of the recipient ferrets died after airborne infection with the mutant A/H5N1 viruses. Four amino acid substitutions in the host receptor-binding protein hemagglutinin, and one in the polymerase complex protein basic polymerase 2, were consistently present in airborne-transmitted viruses. The transmissible viruses were sensitive to the antiviral drug oseltamivir and reacted well with antisera raised against H5 influenza vaccine strains. Thus, avian A/H5N1 influenza viruses can acquire the capacity for airborne transmission between mammals without recombination in an intermediate host and therefore constitute a risk for human pandemic influenza.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herfst, Sander -- Schrauwen, Eefje J A -- Linster, Martin -- Chutinimitkul, Salin -- de Wit, Emmie -- Munster, Vincent J -- Sorrell, Erin M -- Bestebroer, Theo M -- Burke, David F -- Smith, Derek J -- Rimmelzwaan, Guus F -- Osterhaus, Albert D M E -- Fouchier, Ron A M -- DP1-OD000490-01/OD/NIH HHS/ -- HHSN266200700010C/PHS HHS/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1534-41. doi: 10.1126/science.1213362.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Virology, Erasmus Medical Center, Rotterdam, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723413" target="_blank"〉PubMed〈/a〉
    Keywords: Air Microbiology ; Amino Acid Substitution ; Animals ; Antiviral Agents/pharmacology ; Containment of Biohazards ; Disease Models, Animal ; Female ; *Ferrets ; Hemagglutinin Glycoproteins, Influenza ; Virus/chemistry/genetics/immunology/metabolism ; Humans ; Immune Sera ; Influenza A Virus, H5N1 Subtype/drug effects/*genetics/*pathogenicity/physiology ; Influenza in Birds/epidemiology/virology ; Influenza, Human/epidemiology/transmission/*virology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Orthomyxoviridae Infections/transmission/*virology ; Oseltamivir/pharmacology ; Pandemics ; Poultry ; RNA Replicase/chemistry/genetics ; Reassortant Viruses/pathogenicity ; Receptors, Virus/metabolism ; Respiratory System/*virology ; Reverse Genetics ; Serial Passage ; Sialic Acids/metabolism ; Viral Proteins/chemistry/genetics ; Virulence ; Virus Replication ; Virus Shedding
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Elfn1 regulates target-specific release probability at CA1-interneuron synapses (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-10-09
    Description: Although synaptic transmission may be unidirectional, the establishment of synaptic connections with specific properties can involve bidirectional signaling. Pyramidal neurons in the hippocampus form functionally distinct synapses onto two types of interneurons. Excitatory synapses onto oriens-lacunosum moleculare (O-LM) interneurons are facilitating and have a low release probability, whereas synapses onto parvalbumin interneurons are depressing and have a high release probability. Here, we show that the extracellular leucine-rich repeat fibronectin containing 1 (Elfn1) protein is selectively expressed by O-LM interneurons and regulates presynaptic release probability to direct the formation of highly facilitating pyramidal-O-LM synapses. Thus, postsynaptic expression of Elfn1 in O-LM interneurons regulates presynaptic release probability, which confers target-specific synaptic properties to pyramidal cell axons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sylwestrak, Emily L -- Ghosh, Anirvan -- R01 NS067216/NS/NINDS NIH HHS/ -- R01NS067216/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2012 Oct 26;338(6106):536-40. doi: 10.1126/science.1222482. Epub 2012 Oct 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurobiology Section, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093-0366, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23042292" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/metabolism ; CA1 Region, Hippocampal/*metabolism ; Cells, Cultured ; Gene Knockdown Techniques ; Green Fluorescent Proteins/genetics/metabolism ; HEK293 Cells ; Humans ; Interneurons/*metabolism ; Mice ; Nerve Tissue Proteins/genetics/*metabolism ; RNA, Small Interfering/metabolism ; Rats ; Rats, Inbred LEC ; Synapses/genetics/*metabolism ; Synaptic Transmission
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Mysteries of the brain. How are memories retrieved? (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-10-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2012 Oct 5;338(6103):30-1. doi: 10.1126/science.338.6103.30-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23042864" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*physiology ; Hippocampus/physiology ; Humans ; *Mental Recall ; Neuronal Plasticity ; Rats
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Secreted kinase phosphorylates extracellular proteins that regulate biomineralization (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-15
    Description: Protein phosphorylation is a fundamental mechanism regulating nearly every aspect of cellular life. Several secreted proteins are phosphorylated, but the kinases responsible are unknown. We identified a family of atypical protein kinases that localize within the Golgi apparatus and are secreted. Fam20C appears to be the Golgi casein kinase that phosphorylates secretory pathway proteins within S-x-E motifs. Fam20C phosphorylates the caseins and several secreted proteins implicated in biomineralization, including the small integrin-binding ligand, N-linked glycoproteins (SIBLINGs). Consequently, mutations in Fam20C cause an osteosclerotic bone dysplasia in humans known as Raine syndrome. Fam20C is thus a protein kinase dedicated to the phosphorylation of extracellular proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3754843/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3754843/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tagliabracci, Vincent S -- Engel, James L -- Wen, Jianzhong -- Wiley, Sandra E -- Worby, Carolyn A -- Kinch, Lisa N -- Xiao, Junyu -- Grishin, Nick V -- Dixon, Jack E -- DK018024-37/DK/NIDDK NIH HHS/ -- DK018849-36/DK/NIDDK NIH HHS/ -- GM094575/GM/NIGMS NIH HHS/ -- R01 DK018849/DK/NIDDK NIH HHS/ -- R37 DK018024/DK/NIDDK NIH HHS/ -- T32 CA009523/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Jun 1;336(6085):1150-3. doi: 10.1126/science.1217817. Epub 2012 May 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0721, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22582013" target="_blank"〉PubMed〈/a〉
    Keywords: Abnormalities, Multiple/genetics/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Casein Kinase I ; Casein Kinases/metabolism ; Caseins/*metabolism ; Cattle ; Cell Line, Tumor ; Cleft Palate/genetics/metabolism ; Exophthalmos/genetics/metabolism ; Extracellular Matrix Proteins/chemistry/genetics/*metabolism/secretion ; Glycoproteins/metabolism ; Golgi Apparatus/*enzymology ; HEK293 Cells ; HeLa Cells ; Humans ; Microcephaly/genetics/metabolism ; Milk/enzymology ; Molecular Sequence Data ; Mutation ; Osteopontin ; Osteosclerosis/genetics/metabolism ; Phosphorylation ; Protein Sorting Signals ; Recombinant Fusion Proteins/chemistry/metabolism/secretion ; *Secretory Pathway ; Substrate Specificity
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Alzheimer's research. How to talk about Alzheimer's risk (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-08-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2012 Aug 17;337(6096):792. doi: 10.1126/science.337.6096.792.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22903992" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*diagnosis/*genetics ; Apolipoprotein E4/genetics ; Clinical Trials as Topic ; Genetic Predisposition to Disease ; Humans ; Mutation ; *Patient Selection ; Risk ; Risk Assessment
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Locally synchronized synaptic inputs (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-01-24
    Description: Synaptic inputs on dendrites are nonlinearly converted to action potential outputs, yet the spatiotemporal patterns of dendritic activation remain to be elucidated at single-synapse resolution. In rodents, we optically imaged synaptic activities from hundreds of dendritic spines in hippocampal and neocortical pyramidal neurons ex vivo and in vivo. Adjacent spines were frequently synchronized in spontaneously active networks, thereby forming dendritic foci that received locally convergent inputs from presynaptic cell assemblies. This precise subcellular geometry manifested itself during N-methyl-D-aspartate receptor-dependent circuit remodeling. Thus, clustered synaptic plasticity is innately programmed to compartmentalize correlated inputs along dendrites and may reify nonlinear synaptic integration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, Naoya -- Kitamura, Kazuo -- Matsuo, Naoki -- Mayford, Mark -- Kano, Masanobu -- Matsuki, Norio -- Ikegaya, Yuji -- New York, N.Y. -- Science. 2012 Jan 20;335(6066):353-6. doi: 10.1126/science.1210362.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Pharmacology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22267814" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; CA3 Region, Hippocampal/cytology/physiology ; Calcium/metabolism ; Dendritic Spines/*physiology/ultrastructure ; Excitatory Postsynaptic Potentials ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Nerve Net/*physiology ; Neuronal Plasticity ; Organ Culture Techniques ; Patch-Clamp Techniques ; Pyramidal Cells/*physiology ; Rats ; Rats, Wistar ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/metabolism ; Somatosensory Cortex/cytology/physiology ; Synapses/*physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Gene loops enhance transcriptional directionality (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-29
    Description: Eukaryotic genomes are extensively transcribed, forming both messenger RNAs (mRNAs) and noncoding RNAs (ncRNAs). ncRNAs made by RNA polymerase II often initiate from bidirectional promoters (nucleosome-depleted chromatin) that synthesize mRNA and ncRNA in opposite directions. We demonstrate that, by adopting a gene-loop conformation, actively transcribed mRNA encoding genes restrict divergent transcription of ncRNAs. Because gene-loop formation depends on a protein factor (Ssu72) that coassociates with both the promoter and the terminator, the inactivation of Ssu72 leads to increased synthesis of promoter-associated divergent ncRNAs, referred to as Ssu72-restricted transcripts (SRTs). Similarly, inactivation of individual gene loops by gene mutation enhances SRT synthesis. We demonstrate that gene-loop conformation enforces transcriptional directionality on otherwise bidirectional promoters.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3563069/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3563069/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tan-Wong, Sue Mei -- Zaugg, Judith B -- Camblong, Jurgi -- Xu, Zhenyu -- Zhang, David W -- Mischo, Hannah E -- Ansari, Aseem Z -- Luscombe, Nicholas M -- Steinmetz, Lars M -- Proudfoot, Nick J -- 091805/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2012 Nov 2;338(6107):671-5. doi: 10.1126/science.1224350. Epub 2012 Sep 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23019609" target="_blank"〉PubMed〈/a〉
    Keywords: Exosome Multienzyme Ribonuclease Complex/metabolism ; *Genes, Fungal ; Genome, Fungal ; Mutation ; Nucleic Acid Conformation ; Phosphoprotein Phosphatases/metabolism ; Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; RNA Stability ; RNA, Fungal/genetics/metabolism ; RNA, Messenger/*genetics/metabolism ; RNA, Untranslated/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; *Transcription, Genetic ; mRNA Cleavage and Polyadenylation Factors/metabolism
    Print ISSN: 0036-8075
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  • 10
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    Membrane fusion intermediates via directional and full assembly of the SNARE complex (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-02
    Description: Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677693/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677693/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hernandez, Javier M -- Stein, Alexander -- Behrmann, Elmar -- Riedel, Dietmar -- Cypionka, Anna -- Farsi, Zohreh -- Walla, Peter J -- Raunser, Stefan -- Jahn, Reinhard -- 3P01GM072694-05S1/GM/NIGMS NIH HHS/ -- P01 GM072694/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1581-4. doi: 10.1126/science.1221976. Epub 2012 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22653732" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Lipid Bilayers/chemistry/*metabolism ; *Liposomes/chemistry/metabolism ; *Membrane Fusion ; Protein Binding ; Protein Conformation ; Rats ; SNARE Proteins/chemistry/*metabolism ; Vesicle-Associated Membrane Protein 2/metabolism
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  • 11
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    Erasure of a spinal memory trace of pain by a brief, high-dose opioid administration (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-01-17
    Description: Painful stimuli activate nociceptive C fibers and induce synaptic long-term potentiation (LTP) at their spinal terminals. LTP at C-fiber synapses represents a cellular model for pain amplification (hyperalgesia) and for a memory trace of pain. mu-Opioid receptor agonists exert a powerful but reversible depression at C-fiber synapses that renders the continuous application of low opioid doses the gold standard in pain therapy. We discovered that brief application of a high opioid dose reversed various forms of activity-dependent LTP at C-fiber synapses. Depotentiation involved Ca(2+)-dependent signaling and normalization of the phosphorylation state of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors. This also reversed hyperalgesia in behaving animals. Opioids thus not only temporarily dampen pain but may also erase a spinal memory trace of pain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drdla-Schutting, Ruth -- Benrath, Justus -- Wunderbaldinger, Gabriele -- Sandkuhler, Jurgen -- New York, N.Y. -- Science. 2012 Jan 13;335(6065):235-8. doi: 10.1126/science.1211726.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, Center for Brain Research, Medical University of Vienna, A-1090 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22246779" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesics, Opioid/*administration & dosage ; Animals ; Calcium Signaling ; Evoked Potentials ; Hyperalgesia/chemically induced/drug therapy ; Long-Term Potentiation/*drug effects ; Male ; Naloxone/administration & dosage ; Nerve Fibers, Unmyelinated/*drug effects/physiology ; Nociceptive Pain/*drug therapy/physiopathology ; Phosphorylation ; Piperidines/*administration & dosage ; Protein Kinase C/antagonists & inhibitors/metabolism ; Protein Phosphatase 1/antagonists & inhibitors/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/metabolism ; Receptors, Opioid, mu/agonists/metabolism ; Sciatic Nerve/*drug effects/physiology ; Somatostatin/administration & dosage/analogs & derivatives ; Spinal Cord/physiology ; Synapses/*drug effects/physiology
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  • 12
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    Medicine. The ultimate genetic test (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drmanac, Radoje -- New York, N.Y. -- Science. 2012 Jun 1;336(6085):1110-2. doi: 10.1126/science.1221037.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Complete Genomics, Inc., Mountain View, CA 94043, USA. rdrmanac@completegenomics.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22654043" target="_blank"〉PubMed〈/a〉
    Keywords: Genetic Predisposition to Disease ; Genetic Privacy ; *Genetic Testing/economics/methods/standards ; *Genetic Variation ; *Genome, Human ; Humans ; Mutation ; Precision Medicine ; Public Policy ; *Sequence Analysis, DNA/economics/methods/standards
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  • 13
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    Cancer research. Unraveling the obesity-cancer connection (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-01-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, Gary -- New York, N.Y. -- Science. 2012 Jan 6;335(6064):28, 30-2. doi: 10.1126/science.335.6064.28.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22223787" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Proliferation ; Diabetes Mellitus, Type 2/complications/*metabolism ; Diet ; Glucose/metabolism ; Humans ; Insulin/blood/*metabolism ; Mutation ; Neoplasms/*etiology/genetics/metabolism/pathology ; Obesity/complications/*metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Receptor, Insulin/metabolism ; Receptors, Somatomedin/metabolism ; Signal Transduction ; Somatomedins/*metabolism
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  • 14
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    IBI series winner. A mutant search--Caenorhabditis elegans and gene discovery (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-11-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaRue, Candace C -- Padilla, Pamela A -- New York, N.Y. -- Science. 2012 Oct 26;338(6106):487-8. doi: 10.1126/science.1215229.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of North Texas, Denton TX 76203, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23112325" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; Caenorhabditis elegans Proteins/*genetics ; DNA Mutational Analysis ; *Genetic Association Studies ; Genetic Research ; *Genetic Testing ; Genetics/*education ; Mutation ; Texas ; Universities
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  • 15
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    The biology of genomes. Single-cell sequencing tackles basic and biomedical questions (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 2012 May 25;336(6084):976-7. doi: 10.1126/science.336.6084.976.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22628633" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/genetics ; Cell Line, Tumor ; Female ; Genes, Neoplasm ; *Genome, Human ; Humans ; Lab-On-A-Chip Devices ; Male ; Mutation ; Recombination, Genetic ; Sequence Analysis, DNA/*methods ; *Single-Cell Analysis ; Spermatozoa
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  • 16
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    Sedlin controls the ER export of procollagen by regulating the Sar1 cycle (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-29
    Description: Newly synthesized proteins exit the endoplasmic reticulum (ER) via coat protein complex II (COPII) vesicles. Procollagen (PC), however, forms prefibrils that are too large to fit into typical COPII vesicles; PC thus needs large transport carriers, which we term megacarriers. TANGO1 assists PC packing, but its role in promoting the growth of megacarriers is not known. We found that TANGO1 recruited Sedlin, a TRAPP component that is defective in spondyloepiphyseal dysplasia tarda (SEDT), and that Sedlin was required for the ER export of PC. Sedlin bound and promoted efficient cycling of Sar1, a guanosine triphosphatase that can constrict membranes, and thus allowed nascent carriers to grow and incorporate PC prefibrils. This joint action of TANGO1 and Sedlin sustained the ER export of PC, and its derangement may explain the defective chondrogenesis underlying SEDT.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3471527/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3471527/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venditti, Rossella -- Scanu, Tiziana -- Santoro, Michele -- Di Tullio, Giuseppe -- Spaar, Alexander -- Gaibisso, Renato -- Beznoussenko, Galina V -- Mironov, Alexander A -- Mironov, Alexander Jr -- Zelante, Leopoldo -- Piemontese, Maria Rosaria -- Notarangelo, Angelo -- Malhotra, Vivek -- Vertel, Barbara M -- Wilson, Cathal -- De Matteis, Maria Antonietta -- AR053696/AR/NIAMS NIH HHS/ -- GGP06166/Telethon/Italy -- GGP07075/Telethon/Italy -- GSP08002/Telethon/Italy -- GTF08001/Telethon/Italy -- New York, N.Y. -- Science. 2012 Sep 28;337(6102):1668-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Telethon Institute of Genetics and Medicine, Naples, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23019651" target="_blank"〉PubMed〈/a〉
    Keywords: Aryl Hydrocarbon Receptor Nuclear Translocator/*metabolism ; COP-Coated Vesicles/metabolism ; Cell Line ; Chondrogenesis/genetics ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/metabolism ; Humans ; Membrane Transport Proteins/genetics/*metabolism ; Monomeric GTP-Binding Proteins/*metabolism ; Mutation ; Osteochondrodysplasias/genetics/metabolism ; Procollagen/*metabolism ; Protein Transport ; Transcription Factors/genetics/*metabolism
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  • 17
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    Pigment pattern formation by contact-dependent depolarization (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-11
    Description: Although recent experimental studies have suggested that the interactions among the pigment cells play a key role in the skin pattern formation, details of the mechanism remain largely unknown. By using an in vitro cell culture system, we have detected interactions between the two pigment cell types, melanophores and xanthophores, in the zebrafish skin. During primary culture, the melanophore membrane transiently depolarizes when contacted with the dendrites of a xanthophore. This depolarization triggers melanophore migration to avoid further contact with the xanthophores. Cell depolarization and repulsive movement were not observed in pigment cells with the jaguar mutant, which shows defective segregation of melanophores and xanthophores. The depolarization-repulsion of wild-type pigment cells may explain the pigment cell behaviors generating the stripe pattern of zebrafish.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inaba, Masafumi -- Yamanaka, Hiroaki -- Kondo, Shigeru -- New York, N.Y. -- Science. 2012 Feb 10;335(6069):677. doi: 10.1126/science.1212821.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22323812" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication ; Cell Movement ; Cells, Cultured ; Chromatophores/*physiology ; Melanophores/*physiology ; Membrane Potentials ; Mutation ; Skin/cytology ; *Skin Pigmentation ; Zebrafish/*anatomy & histology/physiology
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  • 18
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    Extremely long-lived nuclear pore proteins in the rat brain (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-04
    Description: To combat the functional decline of the proteome, cells use the process of protein turnover to replace potentially impaired polypeptides with new functional copies. We found that extremely long-lived proteins (ELLPs) did not turn over in postmitotic cells of the rat central nervous system. These ELLPs were associated with chromatin and the nuclear pore complex, the central transport channels that mediate all molecular trafficking in and out of the nucleus. The longevity of these proteins would be expected to expose them to potentially harmful metabolites, putting them at risk of accumulating damage over extended periods of time. Thus, it is possible that failure to maintain proper levels and functional integrity of ELLPs in nonproliferative cells might contribute to age-related deterioration in cell and tissue function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3296478/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3296478/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Savas, Jeffrey N -- Toyama, Brandon H -- Xu, Tao -- Yates, John R 3rd -- Hetzer, Martin W -- F32 AG039127/AG/NIA NIH HHS/ -- F32 AG039127-01A1/AG/NIA NIH HHS/ -- F32AG039127/AG/NIA NIH HHS/ -- HHSN268201000035C/PHS HHS/ -- P01 AG031097/AG/NIA NIH HHS/ -- P01 AG031097-03/AG/NIA NIH HHS/ -- P30 CA014195/CA/NCI NIH HHS/ -- P30 CA014195-35/CA/NCI NIH HHS/ -- P41 RR011823/RR/NCRR NIH HHS/ -- P41 RR011823-14/RR/NCRR NIH HHS/ -- R01 MH067880/MH/NIMH NIH HHS/ -- R01 MH067880-08/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2012 Feb 24;335(6071):942. doi: 10.1126/science.1217421. Epub 2012 Feb 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22300851" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/*metabolism ; Cell Aging ; Chromatin/metabolism ; Female ; Half-Life ; Liver/metabolism ; Mitosis ; Nuclear Pore/*metabolism ; Nuclear Pore Complex Proteins/*metabolism ; Proteome/metabolism ; Rats ; Rats, Sprague-Dawley ; Time Factors
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  • 19
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    GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to autophagy (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-04-28
    Description: In metazoans, cells depend on extracellular growth factors for energy homeostasis. We found that glycogen synthase kinase-3 (GSK3), when deinhibited by default in cells deprived of growth factors, activates acetyltransferase TIP60 through phosphorylating TIP60-Ser(86), which directly acetylates and stimulates the protein kinase ULK1, which is required for autophagy. Cells engineered to express TIP60(S86A) that cannot be phosphorylated by GSK3 could not undergo serum deprivation-induced autophagy. An acetylation-defective mutant of ULK1 failed to rescue autophagy in ULK1(-/-) mouse embryonic fibroblasts. Cells used signaling from GSK3 to TIP60 and ULK1 to regulate autophagy when deprived of serum but not glucose. These findings uncover an activating pathway that integrates protein phosphorylation and acetylation to connect growth factor deprivation to autophagy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Shu-Yong -- Li, Terytty Yang -- Liu, Qing -- Zhang, Cixiong -- Li, Xiaotong -- Chen, Yan -- Zhang, Shi-Meng -- Lian, Guili -- Liu, Qi -- Ruan, Ka -- Wang, Zhen -- Zhang, Chen-Song -- Chien, Kun-Yi -- Wu, Jiawei -- Li, Qinxi -- Han, Jiahuai -- Lin, Sheng-Cai -- New York, N.Y. -- Science. 2012 Apr 27;336(6080):477-81. doi: 10.1126/science.1217032.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Fujian, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22539723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Autophagy ; Cell Line ; Cell Line, Tumor ; Culture Media ; Culture Media, Serum-Free ; Glucose/metabolism ; Glycogen Synthase Kinase 3/genetics/*metabolism ; HEK293 Cells ; Histone Acetyltransferases/genetics/*metabolism ; Humans ; Intercellular Signaling Peptides and Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/genetics/*metabolism ; Mice ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Rats ; *Signal Transduction ; Trans-Activators/genetics/metabolism
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    Hippocampal place fields emerge upon single-cell manipulation of excitability during behavior (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-08-21
    Description: The origin of the spatial receptive fields of hippocampal place cells has not been established. A hippocampal CA1 pyramidal cell receives thousands of synaptic inputs, mostly from other spatially tuned neurons; however, how the postsynaptic neuron's cellular properties determine the response to these inputs during behavior is unknown. We discovered that, contrary to expectations from basic models of place cells and neuronal integration, a small, spatially uniform depolarization of the spatially untuned somatic membrane potential of a silent cell leads to the sudden and reversible emergence of a spatially tuned subthreshold response and place-field spiking. Such gating of inputs by postsynaptic neuronal excitability reveals a cellular mechanism for receptive field origin and may be critical for the formation of hippocampal memory representations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Doyun -- Lin, Bei-Jung -- Lee, Albert K -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Aug 17;337(6096):849-53. doi: 10.1126/science.1221489.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Janelia Farm Research Campus, Ashburn, VA 20147, USA. leed@janelia.hhmi.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22904011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CA1 Region, Hippocampal/cytology/*physiology ; *Excitatory Postsynaptic Potentials ; *Memory ; Pyramidal Cells/*physiology ; Rats ; *Spatial Behavior ; Synapses/*physiology
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  • 21
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    An overlapping protein-coding region in influenza A virus segment 3 modulates the host response (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-06-30
    Description: Influenza A virus (IAV) infection leads to variable and imperfectly understood pathogenicity. We report that segment 3 of the virus contains a second open reading frame ("X-ORF"), accessed via ribosomal frameshifting. The frameshift product, termed PA-X, comprises the endonuclease domain of the viral PA protein with a C-terminal domain encoded by the X-ORF and functions to repress cellular gene expression. PA-X also modulates IAV virulence in a mouse infection model, acting to decrease pathogenicity. Loss of PA-X expression leads to changes in the kinetics of the global host response, which notably includes increases in inflammatory, apoptotic, and T lymphocyte-signaling pathways. Thus, we have identified a previously unknown IAV protein that modulates the host response to infection, a finding with important implications for understanding IAV pathogenesis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3552242/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3552242/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jagger, B W -- Wise, H M -- Kash, J C -- Walters, K-A -- Wills, N M -- Xiao, Y-L -- Dunfee, R L -- Schwartzman, L M -- Ozinsky, A -- Bell, G L -- Dalton, R M -- Lo, A -- Efstathiou, S -- Atkins, J F -- Firth, A E -- Taubenberger, J K -- Digard, P -- 073126/Wellcome Trust/United Kingdom -- 088789/Wellcome Trust/United Kingdom -- G0700815/Medical Research Council/United Kingdom -- G0700815(82260)/Medical Research Council/United Kingdom -- G9800943/Medical Research Council/United Kingdom -- MR/J002232/1/Medical Research Council/United Kingdom -- Biotechnology and Biological Sciences Research Council/United Kingdom -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2012 Jul 13;337(6091):199-204. doi: 10.1126/science.1222213. Epub 2012 Jun 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22745253" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Codon ; Conserved Sequence ; Female ; *Frameshifting, Ribosomal ; Gene Expression Regulation ; Genome, Viral ; HEK293 Cells ; Humans ; Influenza A Virus, H1N1 Subtype/*genetics/growth & development/pathogenicity ; Influenza A virus/*genetics/metabolism ; Lung/pathology/virology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutation ; *Open Reading Frames ; Orthomyxoviridae Infections/genetics/immunology/pathology/*virology ; Protein Interaction Domains and Motifs ; Proteome ; RNA Replicase/chemistry/*genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Viral/genetics/metabolism ; Reassortant Viruses/genetics ; Repressor Proteins/chemistry/*genetics/*metabolism ; Viral Nonstructural Proteins/chemistry/*genetics/*metabolism ; Viral Proteins/biosynthesis/chemistry/*genetics/*metabolism ; Virus Replication
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  • 22
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    Benefits and risks of influenza research: lessons learned (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-06-23
    Description: Given the yearly challenge of seasonal influenza and the potential catastrophic consequences of future pandemics, the need for intensive basic and clinical influenza research is unquestionable. Although the fruits of decades of research have enabled dramatic improvements in our ability to prevent and treat influenza, many fundamental questions remain, including those related to the complex factors associated with host switching and transmission of influenza viruses. Recent public concern over two H5N1 influenza manuscripts that studied the transmissibility of influenza viruses has triggered intense discussion on dual-use research and the way forward.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fauci, Anthony S -- Collins, Francis S -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1522-3. doi: 10.1126/science.1224305.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institutes of Health, Bethesda, MD 20892, USA. afauci@niaid.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723407" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Animals ; *Biomedical Research ; Bioterrorism ; Disease Models, Animal ; Evolution, Molecular ; Ferrets ; Humans ; Influenza A Virus, H5N1 Subtype/*genetics/*pathogenicity ; Influenza, Human/mortality/transmission/*virology ; Mutation ; National Institutes of Health (U.S.) ; Orthomyxoviridae Infections/transmission/*virology ; Public Health ; Public Policy ; *Publishing ; Reassortant Viruses/genetics/pathogenicity ; Risk Assessment ; Security Measures ; United States
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    A core metabolic enzyme mediates resistance to phosphine gas (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-11-10
    Description: Phosphine is a small redox-active gas that is used to protect global grain reserves, which are threatened by the emergence of phosphine resistance in pest insects. We find that polymorphisms responsible for genetic resistance cluster around the redox-active catalytic disulfide or the dimerization interface of dihydrolipoamide dehydrogenase (DLD) in insects (Rhyzopertha dominica and Tribolium castaneum) and nematodes (Caenorhabditis elegans). DLD is a core metabolic enzyme representing a new class of resistance factor for a redox-active metabolic toxin. It participates in four key steps of core metabolism, and metabolite profiles indicate that phosphine exposure in mutant and wild-type animals affects these steps differently. Mutation of DLD in C. elegans increases arsenite sensitivity. This specific vulnerability may be exploited to control phosphine-resistant insects and safeguard food security.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlipalius, David I -- Valmas, Nicholas -- Tuck, Andrew G -- Jagadeesan, Rajeswaran -- Ma, Li -- Kaur, Ramandeep -- Goldinger, Anita -- Anderson, Cameron -- Kuang, Jujiao -- Zuryn, Steven -- Mau, Yosep S -- Cheng, Qiang -- Collins, Patrick J -- Nayak, Manoj K -- Schirra, Horst Joachim -- Hilliard, Massimo A -- Ebert, Paul R -- R01NS060129/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 9;338(6108):807-10. doi: 10.1126/science.1224951.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Agri-Science Queensland, Department of Agriculture, Fisheries and Forestry, Ecosciences Precinct, Brisbane, QLD 4001, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23139334" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arsenicals/pharmacology ; Arsenites/pharmacology ; Beetles/drug effects/*enzymology/genetics/metabolism ; Caenorhabditis elegans/drug effects/*enzymology/genetics/metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/metabolism ; Catalytic Domain ; Dihydrolipoamide Dehydrogenase/chemistry/*genetics/metabolism ; Insect Proteins/chemistry/genetics/metabolism ; Insecticide Resistance/*genetics ; *Insecticides/pharmacology ; Metabolic Networks and Pathways ; Molecular Sequence Data ; Mutation ; Oxidation-Reduction ; Pesticides ; *Phosphines/pharmacology ; Polymorphism, Genetic ; Protein Multimerization ; Tribolium/drug effects/*enzymology/genetics/metabolism
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    Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-15
    Description: Human UBIAD1 localizes to mitochondria and converts vitamin K(1) to vitamin K(2). Vitamin K(2) is best known as a cofactor in blood coagulation, but in bacteria it is a membrane-bound electron carrier. Whether vitamin K(2) exerts a similar carrier function in eukaryotic cells is unknown. We identified Drosophila UBIAD1/Heix as a modifier of pink1, a gene mutated in Parkinson's disease that affects mitochondrial function. We found that vitamin K(2) was necessary and sufficient to transfer electrons in Drosophila mitochondria. Heix mutants showed severe mitochondrial defects that were rescued by vitamin K(2), and, similar to ubiquinone, vitamin K(2) transferred electrons in Drosophila mitochondria, resulting in more efficient adenosine triphosphate (ATP) production. Thus, mitochondrial dysfunction was rescued by vitamin K(2) that serves as a mitochondrial electron carrier, helping to maintain normal ATP production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vos, Melissa -- Esposito, Giovanni -- Edirisinghe, Janaka N -- Vilain, Sven -- Haddad, Dominik M -- Slabbaert, Jan R -- Van Meensel, Stefanie -- Schaap, Onno -- De Strooper, Bart -- Meganathan, R -- Morais, Vanessa A -- Verstreken, Patrik -- New York, N.Y. -- Science. 2012 Jun 8;336(6086):1306-10. doi: 10.1126/science.1218632. Epub 2012 May 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉VIB Center for the Biology of Disease, Leuven, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22582012" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Drosophila/genetics/*metabolism ; Drosophila Proteins/deficiency/*genetics/*metabolism ; *Electron Transport ; Escherichia coli/metabolism ; Flight, Animal ; Genes, Insect ; Membrane Potential, Mitochondrial ; Mitochondria/*metabolism/ultrastructure ; Mitochondria, Muscle/metabolism/ultrastructure ; Mutation ; Oxygen Consumption ; Protein-Serine-Threonine Kinases/deficiency/*genetics/*metabolism ; Ubiquinone/metabolism ; Ubiquitin-Protein Ligases/genetics ; Vitamin K 2/*metabolism/pharmacology
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    Structural biology. Versatility from protein disorder (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-09-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babu, M Madan -- Kriwacki, Richard W -- Pappu, Rohit V -- MC_U105185859/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2012 Sep 21;337(6101):1460-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. madanm@mrc-lmb.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22997313" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Computer Simulation ; Evolution, Molecular ; Mutation ; Protein Binding ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Proteins/*chemistry/genetics/*metabolism
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    Mechanism of voltage gating in potassium channels (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-04-14
    Description: The mechanism of ion channel voltage gating-how channels open and close in response to voltage changes-has been debated since Hodgkin and Huxley's seminal discovery that the crux of nerve conduction is ion flow across cellular membranes. Using all-atom molecular dynamics simulations, we show how a voltage-gated potassium channel (KV) switches between activated and deactivated states. On deactivation, pore hydrophobic collapse rapidly halts ion flow. Subsequent voltage-sensing domain (VSD) relaxation, including inward, 15-angstrom S4-helix motion, completes the transition. On activation, outward S4 motion tightens the VSD-pore linker, perturbing linker-S6-helix packing. Fluctuations allow water, then potassium ions, to reenter the pore; linker-S6 repacking stabilizes the open pore. We propose a mechanistic model for the sodium/potassium/calcium voltage-gated ion channel superfamily that reconciles apparently conflicting experimental data.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jensen, Morten O -- Jogini, Vishwanath -- Borhani, David W -- Leffler, Abba E -- Dror, Ron O -- Shaw, David E -- New York, N.Y. -- Science. 2012 Apr 13;336(6078):229-33. doi: 10.1126/science.1216533.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉D E Shaw Research, New York, NY 10036, USA. morten.jensen@DEShawResearch.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22499946" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Hydrophobic and Hydrophilic Interactions ; *Ion Channel Gating ; Kv1.2 Potassium Channel/*chemistry/*metabolism ; Membrane Potentials ; Models, Biological ; Models, Molecular ; Molecular Dynamics Simulation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Shab Potassium Channels/*chemistry/*metabolism
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    Avian influenza. For young scientists, a wild ride (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, Martin -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1495. doi: 10.1126/science.336.6088.1495.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723388" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cough ; Ferrets ; *Influenza A Virus, H5N1 Subtype/genetics/pathogenicity ; Mutation ; Orthomyxoviridae Infections/transmission/*virology ; Publishing ; *Research Personnel ; Sneezing
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    Orbitofrontal cortex supports behavior and learning using inferred but not cached values (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-11-20
    Description: Computational and learning theory models propose that behavioral control reflects value that is both cached (computed and stored during previous experience) and inferred (estimated on the fly on the basis of knowledge of the causal structure of the environment). The latter is thought to depend on the orbitofrontal cortex. Yet some accounts propose that the orbitofrontal cortex contributes to behavior by signaling "economic" value, regardless of the associative basis of the information. We found that the orbitofrontal cortex is critical for both value-based behavior and learning when value must be inferred but not when a cached value is sufficient. The orbitofrontal cortex is thus fundamental for accessing model-based representations of the environment to compute value rather than for signaling value per se.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3592380/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3592380/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Joshua L -- Esber, Guillem R -- McDannald, Michael A -- Gruber, Aaron J -- Hernandez, Alex -- Mirenzi, Aaron -- Schoenbaum, Geoffrey -- F32 DA031517/DA/NIDA NIH HHS/ -- F32-031517/PHS HHS/ -- R01 DA015718/DA/NIDA NIH HHS/ -- R01-DA015718/DA/NIDA NIH HHS/ -- ZIA DA000587-01/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 16;338(6109):953-6. doi: 10.1126/science.1227489.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, University of Maryland School of Medicine, 20 Penn Street, Baltimore, MD 21201, USA. josh.jones@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23162000" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; Conditioning (Psychology) ; Cues ; Frontal Lobe/*physiology ; *Learning ; Male ; Rats ; Rats, Inbred LEC
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    Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-11-01
    Description: Aberrant signaling through the class I phosphatidylinositol 3-kinase (PI3K)-Akt axis is frequent in human cancer. Here, we show that Beclin 1, an essential autophagy and tumor suppressor protein, is a target of the protein kinase Akt. Expression of a Beclin 1 mutant resistant to Akt-mediated phosphorylation increased autophagy, reduced anchorage-independent growth, and inhibited Akt-driven tumorigenesis. Akt-mediated phosphorylation of Beclin 1 enhanced its interactions with 14-3-3 and vimentin intermediate filament proteins, and vimentin depletion increased autophagy and inhibited Akt-driven transformation. Thus, Akt-mediated phosphorylation of Beclin 1 functions in autophagy inhibition, oncogenesis, and the formation of an autophagy-inhibitory Beclin 1/14-3-3/vimentin intermediate filament complex. These findings have broad implications for understanding the role of Akt signaling and intermediate filament proteins in autophagy and cancer.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3507442/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3507442/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Richard C -- Wei, Yongjie -- An, Zhenyi -- Zou, Zhongju -- Xiao, Guanghua -- Bhagat, Govind -- White, Michael -- Reichelt, Julia -- Levine, Beth -- K08 CA164047/CA/NCI NIH HHS/ -- P30 CA142543/CA/NCI NIH HHS/ -- R01 CA071443/CA/NCI NIH HHS/ -- R01 CA084254/CA/NCI NIH HHS/ -- R01 CA109618/CA/NCI NIH HHS/ -- R01 CA129451/CA/NCI NIH HHS/ -- R01 CA84254-S1/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Nov 16;338(6109):956-9. doi: 10.1126/science.1225967. Epub 2012 Oct 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23112296" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis Regulatory Proteins/genetics/*metabolism ; *Autophagy ; Cell Line, Tumor ; Cell Transformation, Neoplastic/genetics/*metabolism ; Fibroblasts/metabolism/pathology ; HeLa Cells ; Humans ; Membrane Proteins/genetics/*metabolism ; Mice ; Phosphorylation ; Proto-Oncogene Proteins c-akt/genetics/*metabolism ; RNA, Small Interfering/genetics ; Rats ; Transduction, Genetic ; Vimentin/genetics ; Xenograft Model Antitumor Assays
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    Circadian rhythm of redox state regulates excitability in suprachiasmatic nucleus neurons (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-08-04
    Description: Daily rhythms of mammalian physiology, metabolism, and behavior parallel the day-night cycle. They are orchestrated by a central circadian clock in the brain, the suprachiasmatic nucleus (SCN). Transcription of clock genes is sensitive to metabolic changes in reduction and oxidation (redox); however, circadian cycles in protein oxidation have been reported in anucleate cells, where no transcription occurs. We investigated whether the SCN also expresses redox cycles and how such metabolic oscillations might affect neuronal physiology. We detected self-sustained circadian rhythms of SCN redox state that required the molecular clockwork. The redox oscillation could determine the excitability of SCN neurons through nontranscriptional modulation of multiple potassium (K(+)) channels. Thus, dynamic regulation of SCN excitability appears to be closely tied to metabolism that engages the clockwork machinery.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3490628/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3490628/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Tongfei A -- Yu, Yanxun V -- Govindaiah, Gubbi -- Ye, Xiaoying -- Artinian, Liana -- Coleman, Todd P -- Sweedler, Jonathan V -- Cox, Charles L -- Gillette, Martha U -- EY014024/EY/NEI NIH HHS/ -- P30 DA018310/DA/NIDA NIH HHS/ -- P30DA018310/DA/NIDA NIH HHS/ -- R01 EY014024/EY/NEI NIH HHS/ -- R01 HL086870/HL/NHLBI NIH HHS/ -- R01 HL092571/HL/NHLBI NIH HHS/ -- R01HL086870/HL/NHLBI NIH HHS/ -- R01HL092571/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2012 Aug 17;337(6096):839-42. doi: 10.1126/science.1222826. Epub 2012 Aug 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Integrative Physiology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22859819" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors/genetics ; Animals ; *Circadian Rhythm ; Fluorometry ; Glutathione/metabolism ; Membrane Potentials ; Mice ; Mice, Mutant Strains ; NADP/metabolism ; Neurons/metabolism/*physiology ; Oxidation-Reduction ; Potassium Channels/metabolism ; Rats ; Suprachiasmatic Nucleus/cytology/metabolism/*physiology
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    Personalized medicine. New cystic fibrosis drug offers hope, at a price (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-02-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2012 Feb 10;335(6069):645. doi: 10.1126/science.335.6069.645.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22323790" target="_blank"〉PubMed〈/a〉
    Keywords: Aminophenols/economics/*therapeutic use ; Cystic Fibrosis/*drug therapy/*genetics ; Cystic Fibrosis Transmembrane Conductance ; Regulator/chemistry/*genetics/metabolism ; Drug Approval ; Drug Costs ; Humans ; Molecular Targeted Therapy ; Mutation ; Precision Medicine ; Quinolones/economics/*therapeutic use ; Small Molecule Libraries ; United States ; United States Food and Drug Administration
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    The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-06-02
    Description: C99 is the transmembrane carboxyl-terminal domain of the amyloid precursor protein that is cleaved by gamma-secretase to release the amyloid-beta polypeptides, which are associated with Alzheimer's disease. Nuclear magnetic resonance and electron paramagnetic resonance spectroscopy show that the extracellular amino terminus of C99 includes a surface-embedded "N-helix" followed by a short "N-loop" connecting to the transmembrane domain (TMD). The TMD is a flexibly curved alpha helix, making it well suited for processive cleavage by gamma-secretase. Titration of C99 reveals a binding site for cholesterol, providing mechanistic insight into how cholesterol promotes amyloidogenesis. Membrane-buried GXXXG motifs (G, Gly; X, any amino acid), which have an established role in oligomerization, were also shown to play a key role in cholesterol binding. The structure and cholesterol binding properties of C99 may aid in the design of Alzheimer's therapeutics.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3528355/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3528355/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrett, Paul J -- Song, Yuanli -- Van Horn, Wade D -- Hustedt, Eric J -- Schafer, Johanna M -- Hadziselimovic, Arina -- Beel, Andrew J -- Sanders, Charles R -- F31 NS077681/NS/NINDS NIH HHS/ -- P01 GM080513/GM/NIGMS NIH HHS/ -- T32 GM008320/GM/NIGMS NIH HHS/ -- T32 GM08320/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 1;336(6085):1168-71. doi: 10.1126/science.1219988.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Center for Structural Biology and Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22654059" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Amyloid beta-Protein Precursor/*chemistry/genetics/*metabolism ; Binding Sites ; Cholesterol/*metabolism ; Electron Spin Resonance Spectroscopy ; Humans ; Micelles ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Peptide Fragments/*chemistry/genetics/*metabolism ; Protein Binding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    The transcription factor c-Maf controls touch receptor development and function (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-02-22
    Description: The sense of touch relies on detection of mechanical stimuli by specialized mechanosensory neurons. The scarcity of molecular data has made it difficult to analyze development of mechanoreceptors and to define the basis of their diversity and function. We show that the transcription factor c-Maf/c-MAF is crucial for mechanosensory function in mice and humans. The development and function of several rapidly adapting mechanoreceptor types are disrupted in c-Maf mutant mice. In particular, Pacinian corpuscles, a type of mechanoreceptor specialized to detect high-frequency vibrations, are severely atrophied. In line with this, sensitivity to high-frequency vibration is reduced in humans carrying a dominant mutation in the c-MAF gene. Thus, our work identifies a key transcription factor specifying development and function of mechanoreceptors and their end organs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wende, Hagen -- Lechner, Stefan G -- Cheret, Cyril -- Bourane, Steeve -- Kolanczyk, Maria E -- Pattyn, Alexandre -- Reuter, Katja -- Munier, Francis L -- Carroll, Patrick -- Lewin, Gary R -- Birchmeier, Carmen -- New York, N.Y. -- Science. 2012 Mar 16;335(6074):1373-6. doi: 10.1126/science.1214314. Epub 2012 Feb 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Developmental Biology, Max Delbruck Center (MDC) for Molecular Medicine, Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22345400" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ganglia, Spinal/cytology/embryology ; Gene Expression Regulation, Developmental ; Humans ; Maf Transcription Factors, Large/genetics/metabolism ; Mechanoreceptors/*cytology/*physiology ; Mice ; Mutation ; Pacinian Corpuscles/cytology/physiology ; Proto-Oncogene Proteins c-maf/genetics/*metabolism ; Proto-Oncogene Proteins c-ret/genetics/metabolism ; Skin/innervation ; *Touch ; Vibration
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    Assembly of an evolutionarily new pathway for alpha-pyrone biosynthesis in Arabidopsis (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-08-28
    Description: Plants possess arrays of functionally diverse specialized metabolites, many of which are distributed taxonomically. Here, we describe the evolution of a class of substituted alpha-pyrone metabolites in Arabidopsis, which we have named arabidopyrones. The biosynthesis of arabidopyrones requires a cytochrome P450 enzyme (CYP84A4) to generate the catechol-substituted substrate for an extradiol ring-cleavage dioxygenase (AtLigB). Unlike other ring-cleavage-derived plant metabolites made from tyrosine, arabidopyrones are instead derived from phenylalanine through the early steps of phenylpropanoid metabolism. Whereas CYP84A4, an Arabidopsis-specific paralog of the lignin-biosynthetic enzyme CYP84A1, has neofunctionalized relative to its ancestor, AtLigB homologs are widespread among land plants and many bacteria. This study exemplifies the rapid evolution of a biochemical pathway formed by the addition of a new biological activity into an existing metabolic infrastructure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weng, Jing-Ke -- Li, Yi -- Mo, Huaping -- Chapple, Clint -- New York, N.Y. -- Science. 2012 Aug 24;337(6097):960-4. doi: 10.1126/science.1221614.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22923580" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/enzymology/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Base Sequence ; Biosynthetic Pathways ; Catalytic Domain ; Cytochrome P-450 Enzyme System/chemistry/genetics/*metabolism ; Dioxygenases/genetics/metabolism ; Evolution, Molecular ; Gene Duplication ; Genome, Plant ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Phenylalanine/metabolism ; Phylogeny ; Plant Stems/metabolism ; Plants, Genetically Modified ; Pyrones/chemistry/*metabolism
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    The cellular basis of GABA(B)-mediated interhemispheric inhibition (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-01
    Description: Interhemispheric inhibition is thought to mediate cortical rivalry between the two hemispheres through callosal input. The long-lasting form of this inhibition is believed to operate via gamma-aminobutyric acid type B (GABA(B)) receptors, but the process is poorly understood at the cellular level. We found that the firing of layer 5 pyramidal neurons in rat somatosensory cortex due to contralateral sensory stimulation was inhibited for hundreds of milliseconds when paired with ipsilateral stimulation. The inhibition acted directly on apical dendrites via layer 1 interneurons but was silent in the absence of pyramidal cell firing, relying on metabotropic inhibition of active dendritic currents recruited during neuronal activity. The results not only reveal the microcircuitry underlying interhemispheric inhibition but also demonstrate the importance of active dendritic properties for cortical output.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palmer, Lucy M -- Schulz, Jan M -- Murphy, Sean C -- Ledergerber, Debora -- Murayama, Masanori -- Larkum, Matthew E -- New York, N.Y. -- Science. 2012 Feb 24;335(6071):989-93. doi: 10.1126/science.1217276.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physiologisches Institut, Universitat Bern, Buhlplatz 5, CH-3012 Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22363012" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/metabolism ; Cerebrum/*physiology ; Corpus Callosum/physiology ; Dendrites/*physiology ; Electric Stimulation ; Hindlimb ; Interneurons/physiology ; *Neural Inhibition ; Patch-Clamp Techniques ; Pyramidal Cells/*physiology ; Rats ; Rats, Wistar ; Receptors, GABA-B/*metabolism ; Somatosensory Cortex/cytology/*physiology
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    Tricking the guard: exploiting plant defense for disease susceptibility (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-10-23
    Description: Typically, pathogens deploy virulence effectors to disable defense. Plants defeat effectors with resistance proteins that guard effector targets. We found that a pathogen exploits a resistance protein by activating it to confer susceptibility in Arabidopsis. The guard mechanism of plant defense is recapitulated by interactions among victorin (an effector produced by the necrotrophic fungus Cochliobolus victoriae), TRX-h5 (a defense-associated thioredoxin), and LOV1 (an Arabidopsis susceptibility protein). In LOV1's absence, victorin inhibits TRX-h5, resulting in compromised defense but not disease by C. victoriae. In LOV1's presence, victorin binding to TRX-h5 activates LOV1 and elicits a resistance-like response that confers disease susceptibility. We propose that victorin is, or mimics, a conventional pathogen virulence effector that was defeated by LOV1 and confers virulence to C. victoriae solely because it incites defense.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4125361/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4125361/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lorang, J -- Kidarsa, T -- Bradford, C S -- Gilbert, B -- Curtis, M -- Tzeng, S-C -- Maier, C S -- Wolpert, T J -- BB/D016541/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/H008039/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- P30 ES000210/ES/NIEHS NIH HHS/ -- P30ES200210/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 2;338(6107):659-62. doi: 10.1126/science.1226743. Epub 2012 Oct 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology and Center for Genome Research and Biocomputing, Oregon State University, Corvallis, OR 97331, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23087001" target="_blank"〉PubMed〈/a〉
    Keywords: *Arabidopsis/immunology/metabolism/microbiology ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Ascomycota/metabolism/*pathogenicity ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Disease Susceptibility ; Fungal Proteins/*metabolism ; Mutation ; Mycotoxins/*metabolism ; Oxidation-Reduction ; *Plant Diseases/immunology/microbiology ; *Plant Immunity ; Protein Binding ; Protein Interaction Domains and Motifs ; Thioredoxins/genetics/*metabolism ; Tobacco/genetics/metabolism ; Virulence Factors/*metabolism
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    Network resets in medial prefrontal cortex mark the onset of behavioral uncertainty (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-10-09
    Description: Regions within the prefrontal cortex are thought to process beliefs about the world, but little is known about the circuit dynamics underlying the formation and modification of these beliefs. Using a task that permits dissociation between the activity encoding an animal's internal state and that encoding aspects of behavior, we found that transient increases in the volatility of activity in the rat medial prefrontal cortex accompany periods when an animal's belief is modified after an environmental change. Activity across the majority of sampled neurons underwent marked, abrupt, and coordinated changes when prior belief was abandoned in favor of exploration of alternative strategies. These dynamics reflect network switches to a state of instability, which diminishes over the period of exploration as new stable representations are formed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karlsson, Mattias P -- Tervo, Dougal G R -- Karpova, Alla Y -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Oct 5;338(6103):135-9. doi: 10.1126/science.1226518.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Janelia Farm Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, VA 20147, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23042898" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; Male ; Nerve Net/cytology/*physiology ; Neurons/physiology ; Prefrontal Cortex/cytology/*physiology ; Rats ; Rats, Long-Evans ; Rejection (Psychology) ; Reward ; *Uncertainty
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    Population genomics of early events in the ecological differentiation of bacteria (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-04-12
    Description: Genetic exchange is common among bacteria, but its effect on population diversity during ecological differentiation remains controversial. A fundamental question is whether advantageous mutations lead to selection of clonal genomes or, as in sexual eukaryotes, sweep through populations on their own. Here, we show that in two recently diverged populations of ocean bacteria, ecological differentiation has occurred akin to a sexual mechanism: A few genome regions have swept through subpopulations in a habitat-specific manner, accompanied by gradual separation of gene pools as evidenced by increased habitat specificity of the most recent recombinations. These findings reconcile previous, seemingly contradictory empirical observations of the genetic structure of bacterial populations and point to a more unified process of differentiation in bacteria and sexual eukaryotes than previously thought.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3337212/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3337212/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shapiro, B Jesse -- Friedman, Jonathan -- Cordero, Otto X -- Preheim, Sarah P -- Timberlake, Sonia C -- Szabo, Gitta -- Polz, Martin F -- Alm, Eric J -- U54 GM088558/GM/NIGMS NIH HHS/ -- U54 GM088558-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Apr 6;336(6077):48-51. doi: 10.1126/science.1218198.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Computational and Systems Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22491847" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosomes, Bacterial/genetics ; *Ecosystem ; *Evolution, Molecular ; Gene Flow ; Gene Transfer, Horizontal ; Genes, Bacterial ; Genetic Variation ; *Genome, Bacterial ; Models, Genetic ; Molecular Sequence Data ; Mutation ; Oceans and Seas ; Phylogeny ; Polymorphism, Single Nucleotide ; *Recombination, Genetic ; Seawater/*microbiology ; *Selection, Genetic ; Vibrio/classification/*genetics
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    Neuroscience. All eyes on RNA (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-12-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garber, Ken -- New York, N.Y. -- Science. 2012 Dec 7;338(6112):1282-3. doi: 10.1126/science.338.6112.1282.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23224536" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*genetics/metabolism ; Chromosomes, Human, Pair 9/genetics ; DNA-Binding Proteins/genetics/metabolism ; Dementia/genetics/metabolism ; Humans ; Motor Neurons/metabolism/pathology ; Mutation ; Proteins/genetics ; RNA/*metabolism ; RNA-Binding Protein FUS/genetics/metabolism ; RNA-Binding Proteins/*genetics/metabolism
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    Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-11-10
    Description: Millions of molecules of lipopolysaccharide (LPS) must be assembled on the Escherichia coli cell surface each time the cell divides. The biogenesis of LPS requires seven essential lipopolysaccharide transport (Lpt) proteins to move LPS from the inner membrane through the periplasm to the cell surface. However, no intermediate transport states have been observed. We developed methods to observe intermediate LPS molecules bound to Lpt proteins in the process of being transported in vivo. Movement of individual LPS molecules along these binding sites required multiple rounds of adenosine triphosphate (ATP) hydrolysis in vitro, which suggests that ATP is used to push a continuous stream of LPS through a transenvelope bridge in discrete steps against a concentration gradient.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3552488/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3552488/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Okuda, Suguru -- Freinkman, Elizaveta -- Kahne, Daniel -- AI081059/AI/NIAID NIH HHS/ -- GM066174/GM/NIGMS NIH HHS/ -- R01 AI081059/AI/NIAID NIH HHS/ -- R01 GM066174/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 30;338(6111):1214-7. doi: 10.1126/science.1228984. Epub 2012 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23138981" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/chemistry/metabolism ; Adenosine Triphosphate/*metabolism ; Bacterial Proteins/chemistry/metabolism ; Biological Transport ; Carrier Proteins/chemistry/genetics/metabolism ; Cytoplasm/*metabolism ; Escherichia coli/*metabolism ; Escherichia coli Proteins/chemistry/genetics/metabolism ; Hydrolysis ; Lipopolysaccharides/*metabolism ; Membrane Proteins/chemistry/genetics/metabolism ; Mutation ; Periplasm/*metabolism ; Protein Conformation
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    Glacial survival of boreal trees in northern Scandinavia (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-03-03
    Description: It is commonly believed that trees were absent in Scandinavia during the last glaciation and first recolonized the Scandinavian Peninsula with the retreat of its ice sheet some 9000 years ago. Here, we show the presence of a rare mitochondrial DNA haplotype of spruce that appears unique to Scandinavia and with its highest frequency to the west-an area believed to sustain ice-free refugia during most of the last ice age. We further show the survival of DNA from this haplotype in lake sediments and pollen of Trondelag in central Norway dating back ~10,300 years and chloroplast DNA of pine and spruce in lake sediments adjacent to the ice-free Andoya refugium in northwestern Norway as early as ~22,000 and 17,700 years ago, respectively. Our findings imply that conifer trees survived in ice-free refugia of Scandinavia during the last glaciation, challenging current views on survival and spread of trees as a response to climate changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parducci, Laura -- Jorgensen, Tina -- Tollefsrud, Mari Mette -- Elverland, Ellen -- Alm, Torbjorn -- Fontana, Sonia L -- Bennett, K D -- Haile, James -- Matetovici, Irina -- Suyama, Yoshihisa -- Edwards, Mary E -- Andersen, Kenneth -- Rasmussen, Morten -- Boessenkool, Sanne -- Coissac, Eric -- Brochmann, Christian -- Taberlet, Pierre -- Houmark-Nielsen, Michael -- Larsen, Nicolaj Krog -- Orlando, Ludovic -- Gilbert, M Thomas P -- Kjaer, Kurt H -- Alsos, Inger Greve -- Willerslev, Eske -- New York, N.Y. -- Science. 2012 Mar 2;335(6072):1083-6. doi: 10.1126/science.1216043.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Genetics, Evolutionary Biology Centre, Uppsala University, Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22383845" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Chloroplast/genetics ; DNA, Mitochondrial/genetics ; *Ecosystem ; Europe ; *Fossils ; Geologic Sediments ; Haplotypes ; *Ice Cover ; Molecular Sequence Data ; Mutation ; Norway ; *Picea/genetics ; *Pinus/genetics ; Scandinavian and Nordic Countries ; Time
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    Cell biology. The unusual case of Porcupine (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-08-28
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4314091/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4314091/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lum, Lawrence -- Clevers, Hans -- R21 HD061303/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2012 Aug 24;337(6097):922-3. doi: 10.1126/science.1228179.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA. lawrence.lum@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22923569" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/pharmacology/*therapeutic use ; Clinical Trials, Phase I as Topic ; DNA-Binding Proteins/genetics ; Drug Discovery ; Enzyme Inhibitors/pharmacology/*therapeutic use ; Humans ; Membrane Proteins/*antagonists & inhibitors/genetics/*metabolism ; Molecular Targeted Therapy ; Mutation ; Neoplasms/*drug therapy/genetics/metabolism ; Oncogene Proteins/genetics ; Palmitic Acid/metabolism ; Protein-Serine-Threonine Kinases/genetics ; Wnt Proteins/*metabolism ; Wnt Signaling Pathway/*drug effects
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    IBI* series winner. Adapting to osmotic stress and the process of science (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gasper, Brittany J -- Minchella, Dennis J -- Weaver, Gabriela C -- Csonka, Laszlo N -- Gardner, Stephanie M -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Mar 30;335(6076):1590-1. doi: 10.1126/science.1215582.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22461603" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; Awards and Prizes ; Bacterial Proteins/genetics/metabolism ; Genetics, Microbial/*education ; Mutation ; Osmotic Pressure ; Research/*education ; Salmonella typhimurium/*genetics/physiology ; *Stress, Physiological ; Symporters/genetics/metabolism ; Universities
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    dSarm/Sarm1 is required for activation of an injury-induced axon death pathway (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-06-09
    Description: Axonal and synaptic degeneration is a hallmark of peripheral neuropathy, brain injury, and neurodegenerative disease. Axonal degeneration has been proposed to be mediated by an active autodestruction program, akin to apoptotic cell death; however, loss-of-function mutations capable of potently blocking axon self-destruction have not been described. Here, we show that loss of the Drosophila Toll receptor adaptor dSarm (sterile alpha/Armadillo/Toll-Interleukin receptor homology domain protein) cell-autonomously suppresses Wallerian degeneration for weeks after axotomy. Severed mouse Sarm1 null axons exhibit remarkable long-term survival both in vivo and in vitro, indicating that Sarm1 prodegenerative signaling is conserved in mammals. Our results provide direct evidence that axons actively promote their own destruction after injury and identify dSarm/Sarm1 as a member of an ancient axon death signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Osterloh, Jeannette M -- Yang, Jing -- Rooney, Timothy M -- Fox, A Nicole -- Adalbert, Robert -- Powell, Eric H -- Sheehan, Amy E -- Avery, Michelle A -- Hackett, Rachel -- Logan, Mary A -- MacDonald, Jennifer M -- Ziegenfuss, Jennifer S -- Milde, Stefan -- Hou, Ying-Ju -- Nathan, Carl -- Ding, Aihao -- Brown, Robert H Jr -- Conforti, Laura -- Coleman, Michael -- Tessier-Lavigne, Marc -- Zuchner, Stephan -- Freeman, Marc R -- 5R01-NS050557-05/NS/NINDS NIH HHS/ -- AI030165/AI/NIAID NIH HHS/ -- R01NS059991/NS/NINDS NIH HHS/ -- R01NS072248/NS/NINDS NIH HHS/ -- RC2-NS070-342/NS/NINDS NIH HHS/ -- U54NS065712/NS/NINDS NIH HHS/ -- Biotechnology and Biological Sciences Research Council/United Kingdom -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Jul 27;337(6093):481-4. doi: 10.1126/science.1223899. Epub 2012 Jun 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22678360" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Apoptosis ; Armadillo Domain Proteins/analysis/*genetics/*physiology ; Axons/*physiology/ultrastructure ; Axotomy ; Cell Survival ; Cells, Cultured ; Cytoskeletal Proteins/analysis/*genetics/*physiology ; Denervation ; Drosophila/embryology/genetics/physiology ; Drosophila Proteins/analysis/*genetics/*physiology ; Mice ; Mutation ; Neurons/*physiology ; Sciatic Nerve/injuries/physiology ; Signal Transduction ; Superior Cervical Ganglion/cytology ; Tissue Culture Techniques ; *Wallerian Degeneration
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    Recent explosive human population growth has resulted in an excess of rare genetic variants (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-15
    Description: Human populations have experienced recent explosive growth, expanding by at least three orders of magnitude over the past 400 generations. This departure from equilibrium skews patterns of genetic variation and distorts basic principles of population genetics. We characterized the empirical signatures of explosive growth on the site frequency spectrum and found that the discrepancy in rare variant abundance across demographic modeling studies is mostly due to differences in sample size. Rapid recent growth increases the load of rare variants and is likely to play a role in the individual genetic burden of complex disease risk. Hence, the extreme recent human population growth needs to be taken into consideration in studying the genetics of complex diseases and traits.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3586590/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3586590/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keinan, Alon -- Clark, Andrew G -- GM065509/GM/NIGMS NIH HHS/ -- HL102419/HL/NHLBI NIH HHS/ -- R01 HG003229/HG/NHGRI NIH HHS/ -- RC2 HL102419/HL/NHLBI NIH HHS/ -- U01 HG005715/HG/NHGRI NIH HHS/ -- U01-HG005715/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2012 May 11;336(6082):740-3. doi: 10.1126/science.1217283.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Statistics and Computational Biology, Cornell University, Ithaca, NY 14853, USA. ak735@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22582263" target="_blank"〉PubMed〈/a〉
    Keywords: Asian Continental Ancestry Group/genetics ; European Continental Ancestry Group/genetics ; Gene Frequency ; Genetic Association Studies ; Genetic Predisposition to Disease ; *Genetic Variation ; Genetics, Population/methods ; Genome, Human ; Haplotypes ; Heterozygote ; Humans ; Models, Genetic ; Mutation ; Polymorphism, Single Nucleotide ; *Population Density ; *Population Growth ; Sample Size ; Sequence Analysis, DNA
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    SNARE proteins: one to fuse and three to keep the nascent fusion pore open (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-17
    Description: Neurotransmitters are released through nascent fusion pores, which ordinarily dilate after bilayer fusion, preventing consistent biochemical studies. We used lipid bilayer nanodiscs as fusion partners; their rigid protein framework prevents dilation and reveals properties of the fusion pore induced by SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). We found that although only one SNARE per nanodisc is required for maximum rates of bilayer fusion, efficient release of content on the physiologically relevant time scale of synaptic transmission apparently requires three or more SNARE complexes (SNAREpins) and the native transmembrane domain of vesicle-associated membrane protein 2 (VAMP2). We suggest that several SNAREpins simultaneously zippering their SNARE transmembrane helices within the freshly fused bilayers provide a radial force that prevents the nascent pore from resealing during synchronous neurotransmitter release.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3736847/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3736847/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, Lei -- Shen, Qing-Tao -- Kiel, Alexander -- Wang, Jing -- Wang, Hong-Wei -- Melia, Thomas J -- Rothman, James E -- Pincet, Frederic -- R01 DK027044/DK/NIDDK NIH HHS/ -- R37 DK027044/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2012 Mar 16;335(6074):1355-9. doi: 10.1126/science.1214984.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, School of Medicine, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22422984" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Diffusion ; *Lipid Bilayers ; Liposomes ; *Membrane Fusion ; Membrane Proteins/chemistry/metabolism ; Mice ; Neurotransmitter Agents/metabolism ; Protein Structure, Tertiary ; Proteolipids/chemistry ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; SNARE Proteins/*chemistry/*metabolism ; Synaptic Transmission ; Synaptic Vesicles/*chemistry/metabolism ; Synaptosomal-Associated Protein 25/chemistry/metabolism ; Syntaxin 1/chemistry/metabolism ; Vesicle-Associated Membrane Protein 2/*chemistry/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 47
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    The structure and catalytic cycle of a sodium-pumping pyrophosphatase (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-07-28
    Description: Membrane-integral pyrophosphatases (M-PPases) are crucial for the survival of plants, bacteria, and protozoan parasites. They couple pyrophosphate hydrolysis or synthesis to Na(+) or H(+) pumping. The 2.6-angstrom structure of Thermotoga maritima M-PPase in the resting state reveals a previously unknown solution for ion pumping. The hydrolytic center, 20 angstroms above the membrane, is coupled to the gate formed by the conserved Asp(243), Glu(246), and Lys(707) by an unusual "coupling funnel" of six alpha helices. Comparison with our 4.0-angstrom resolution structure of the product complex suggests that helix 12 slides down upon substrate binding to open the gate by a simple binding-change mechanism. Below the gate, four helices form the exit channel. Superimposing helices 3 to 6, 9 to 12, and 13 to 16 suggests that M-PPases arose through gene triplication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellosalo, Juho -- Kajander, Tommi -- Kogan, Konstantin -- Pokharel, Kisun -- Goldman, Adrian -- New York, N.Y. -- Science. 2012 Jul 27;337(6093):473-6. doi: 10.1126/science.1222505.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology and Biophysics Program, Institute of Biotechnology, Post Office Box 65, University of Helsinki, FIN-00014, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22837527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/metabolism ; Biocatalysis ; Calcium/chemistry ; Catalytic Domain ; Cell Membrane/enzymology ; Crystallography, X-Ray ; Diphosphates/*metabolism ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Ion Channel Gating ; Magnesium/chemistry ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Multimerization ; Protein Structure, Secondary ; Pyrophosphatases/*chemistry/genetics/*metabolism ; Sodium/*metabolism ; Sodium-Potassium-Exchanging ATPase/*chemistry/genetics/metabolism ; Thermotoga maritima/*enzymology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Closed-loop control of epilepsy by transcranial electrical stimulation (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-08-11
    Description: Many neurological and psychiatric diseases are associated with clinically detectable, altered brain dynamics. The aberrant brain activity, in principle, can be restored through electrical stimulation. In epilepsies, abnormal patterns emerge intermittently, and therefore, a closed-loop feedback brain control that leaves other aspects of brain functions unaffected is desirable. Here, we demonstrate that seizure-triggered, feedback transcranial electrical stimulation (TES) can dramatically reduce spike-and-wave episodes in a rodent model of generalized epilepsy. Closed-loop TES can be an effective clinical tool to reduce pathological brain patterns in drug-resistant patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berenyi, Antal -- Belluscio, Mariano -- Mao, Dun -- Buzsaki, Gyorgy -- MH54671/MH/NIMH NIH HHS/ -- NS074015/NS/NINDS NIH HHS/ -- NS34994/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2012 Aug 10;337(6095):735-7. doi: 10.1126/science.1223154.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular and Behavioral Neuroscience, Rutgers University, Newark, NJ 07102, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22879515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Brain Waves ; Cerebral Cortex/physiopathology ; *Deep Brain Stimulation ; Electric Stimulation ; Electrodes, Implanted ; Epilepsy, Absence/physiopathology/*therapy ; Feedback, Physiological ; Male ; Rats ; Rats, Long-Evans ; Thalamus/physiopathology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Natural variation in a chloride channel subunit confers avermectin resistance in C. elegans (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-04
    Description: Resistance of nematodes to anthelmintics such as avermectins has emerged as a major global health and agricultural problem, but genes conferring natural resistance to avermectins are unknown. We show that a naturally occurring four-amino-acid deletion in the ligand-binding domain of GLC-1, the alpha-subunit of a glutamate-gated chloride channel, confers resistance to avermectins in the model nematode Caenorhabditis elegans. We also find that the same variant confers resistance to the avermectin-producing bacterium Streptomyces avermitilis. Population-genetic analyses identified two highly divergent haplotypes at the glc-1 locus that have been maintained at intermediate frequencies by long-term balancing selection. These results implicate variation in glutamate-gated chloride channels in avermectin resistance and provide a mechanism by which such resistance can be maintained.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3273849/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3273849/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, Rajarshi -- Andersen, Erik C -- Shapiro, Joshua A -- Gerke, Justin P -- Kruglyak, Leonid -- P50-GM071508/GM/NIGMS NIH HHS/ -- R01 HG004321/HG/NHGRI NIH HHS/ -- R01 HG004321-03/HG/NHGRI NIH HHS/ -- R01-HG004321/HG/NHGRI NIH HHS/ -- R37- MH59520/MH/NIMH NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Feb 3;335(6068):574-8. doi: 10.1126/science.1214318.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lewis-Sigler Institute for Integrative Genomics, Department of Ecology and Evolutionary Biology, and Howard Hughes Medical Institute, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22301316" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Antinematodal Agents/*pharmacology ; Caenorhabditis elegans/*drug effects/*genetics/physiology ; Caenorhabditis elegans Proteins/chemistry/*genetics/metabolism ; Chloride Channels/chemistry/*genetics/metabolism ; Crosses, Genetic ; Drug Resistance/genetics ; Genes, Helminth ; Genome-Wide Association Study ; Ivermectin/*analogs & derivatives/*pharmacology ; Ligands ; Molecular Sequence Data ; Mutation ; Polymorphism, Single Nucleotide ; Protein Structure, Tertiary ; Quantitative Trait Loci ; Selection, Genetic ; Streptomyces/physiology
    Print ISSN: 0036-8075
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    ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-04
    Description: Eukaryotic secretory proteins exit the endoplasmic reticulum (ER) via transport vesicles generated by the essential coat protein complex II (COPII) proteins. The outer coat complex, Sec13-Sec31, forms a scaffold that is thought to enforce curvature. By exploiting yeast bypass-of-sec-thirteen (bst) mutants, where Sec13p is dispensable, we probed the relationship between a compromised COPII coat and the cellular context in which it could still function. Genetic and biochemical analyses suggested that Sec13p was required to generate vesicles from membranes that contained asymmetrically distributed cargoes that were likely to confer opposing curvature. Thus, Sec13p may rigidify the COPII cage and increase its membrane-bending capacity; this function could be bypassed when a bst mutation renders the membrane more deformable.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3306526/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3306526/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Copic, Alenka -- Latham, Catherine F -- Horlbeck, Max A -- D'Arcangelo, Jennifer G -- Miller, Elizabeth A -- GM078186/GM/NIGMS NIH HHS/ -- GM085089/GM/NIGMS NIH HHS/ -- R01 GM078186/GM/NIGMS NIH HHS/ -- R01 GM078186-05/GM/NIGMS NIH HHS/ -- R01 GM085089/GM/NIGMS NIH HHS/ -- R01 GM085089-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Mar 16;335(6074):1359-62. doi: 10.1126/science.1215909. Epub 2012 Feb 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22300850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; COP-Coated Vesicles/*chemistry/metabolism/ultrastructure ; Endoplasmic Reticulum/*metabolism ; Genes, Fungal ; Models, Biological ; Models, Molecular ; Mutant Proteins/chemistry/metabolism ; Mutation ; Nuclear Pore Complex Proteins/chemistry/genetics/*metabolism ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Protein Transport ; Saccharomyces cerevisiae/genetics/*metabolism/ultrastructure ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Vesicular Transport Proteins/chemistry/metabolism
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    Mitochondrial fission, fusion, and stress (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-09-01
    Description: Mitochondrial fission and fusion play critical roles in maintaining functional mitochondria when cells experience metabolic or environmental stresses. Fusion helps mitigate stress by mixing the contents of partially damaged mitochondria as a form of complementation. Fission is needed to create new mitochondria, but it also contributes to quality control by enabling the removal of damaged mitochondria and can facilitate apoptosis during high levels of cellular stress. Disruptions in these processes affect normal development, and they have been implicated in neurodegenerative diseases, such as Parkinson's.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4762028/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4762028/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Youle, Richard J -- van der Bliek, Alexander M -- GM051866/GM/NIGMS NIH HHS/ -- Z99 NS999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2012 Aug 31;337(6098):1062-5. doi: 10.1126/science.1219855.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA. youler@ninds.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22936770" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autophagy ; DNA, Mitochondrial/genetics ; Humans ; *Membrane Fusion ; Mice ; Mitochondria/genetics/*physiology ; Mitochondrial Diseases/metabolism ; Mitochondrial Proteins/genetics/metabolism ; Mutation ; Neurodegenerative Diseases/metabolism ; Parkinson Disease/metabolism ; *Stress, Physiological
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    Neuroscience. The emerging biology of autism spectrum disorders (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-18
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3657753/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3657753/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉State, Matthew W -- Sestan, Nenad -- P50MH081756/MH/NIMH NIH HHS/ -- R01 NS054273/NS/NINDS NIH HHS/ -- R01MH081754/MH/NIMH NIH HHS/ -- R01NS054273/NS/NINDS NIH HHS/ -- RC2MH089956/MH/NIMH NIH HHS/ -- U01 MH081896/MH/NIMH NIH HHS/ -- U01MH081896/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2012 Sep 14;337(6100):1301-3. doi: 10.1126/science.1224989.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Child Study Center and Department of Psychiatry, Yale University School of Medicine, New Haven, CT 06510, USA. matthew.state@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22984058" target="_blank"〉PubMed〈/a〉
    Keywords: Child Development Disorders, Pervasive/*genetics ; Child, Preschool ; Gene Expression Profiling ; *Gene Expression Regulation, Developmental ; Genetic Loci ; Humans ; Mutation ; Neocortex/*growth & development/metabolism
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    A memory retrieval-extinction procedure to prevent drug craving and relapse (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-04-14
    Description: Drug use and relapse involve learned associations between drug-associated environmental cues and drug effects. Extinction procedures in the clinic can suppress conditioned responses to drug cues, but the extinguished responses typically reemerge after exposure to the drug itself (reinstatement), the drug-associated environment (renewal), or the passage of time (spontaneous recovery). We describe a memory retrieval-extinction procedure that decreases conditioned drug effects and drug seeking in rat models of relapse, and drug craving in abstinent heroin addicts. In rats, daily retrieval of drug-associated memories 10 minutes or 1 hour but not 6 hours before extinction sessions attenuated drug-induced reinstatement, spontaneous recovery, and renewal of conditioned drug effects and drug seeking. In heroin addicts, retrieval of drug-associated memories 10 minutes before extinction sessions attenuated cue-induced heroin craving 1, 30, and 180 days later. The memory retrieval-extinction procedure is a promising nonpharmacological method for decreasing drug craving and relapse during abstinence.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3695463/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3695463/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xue, Yan-Xue -- Luo, Yi-Xiao -- Wu, Ping -- Shi, Hai-Shui -- Xue, Li-Fen -- Chen, Chen -- Zhu, Wei-Li -- Ding, Zeng-Bo -- Bao, Yan-ping -- Shi, Jie -- Epstein, David H -- Shaham, Yavin -- Lu, Lin -- Z99 DA999999/Intramural NIH HHS/ -- ZIA DA000434-12/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2012 Apr 13;336(6078):241-5. doi: 10.1126/science.1215070.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute on Drug Dependence, Peking University, Beijing, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22499948" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/enzymology ; Animals ; Behavior, Addictive/*prevention & control ; Cocaine/administration & dosage ; Cocaine-Related Disorders/*psychology/therapy ; Conditioning, Classical ; Conditioning, Operant ; Cues ; *Extinction, Psychological ; Heroin/administration & dosage ; Heroin Dependence/*psychology/therapy ; Humans ; Male ; *Memory ; Mental Recall ; Models, Animal ; Prefrontal Cortex/enzymology ; Protein Kinase C/metabolism ; Rats ; Rats, Sprague-Dawley ; Recurrence ; Self Administration ; Time Factors
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    A mutation in EGF repeat-8 of Notch discriminates between Serrate/Jagged and Delta family ligands (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-12-01
    Description: Notch signaling affects many developmental and cellular processes and has been implicated in congenital disorders, stroke, and numerous cancers. The Notch receptor binds its ligands Delta and Serrate and is able to discriminate between them in different contexts. However, the specific domains in Notch responsible for this selectivity are poorly defined. Through genetic screens in Drosophila, we isolated a mutation, Notch(jigsaw), that affects Serrate- but not Delta-dependent signaling. Notch(jigsaw) carries a missense mutation in epidermal growth factor repeat-8 (EGFr-8) and is defective in Serrate binding. A homologous point mutation in mammalian Notch2 also exhibits defects in signaling of a mammalian Serrate homolog, Jagged1. Hence, an evolutionarily conserved valine in EGFr-8 is essential for ligand selectivity and provides a molecular handle to study numerous Notch-dependent signaling events.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3663443/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3663443/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamoto, Shinya -- Charng, Wu-Lin -- Rana, Nadia A -- Kakuda, Shinako -- Jaiswal, Manish -- Bayat, Vafa -- Xiong, Bo -- Zhang, Ke -- Sandoval, Hector -- David, Gabriela -- Wang, Hao -- Haltiwanger, Robert S -- Bellen, Hugo J -- 1RC4GM096355-01/GM/NIGMS NIH HHS/ -- 5K12GM084897/GM/NIGMS NIH HHS/ -- 5P30HD024064/HD/NICHD NIH HHS/ -- 5R01GM061126-12/GM/NIGMS NIH HHS/ -- 5R01GM067858/GM/NIGMS NIH HHS/ -- 5T32-HD055200/HD/NICHD NIH HHS/ -- K12 GM084897/GM/NIGMS NIH HHS/ -- P30 HD024064/HD/NICHD NIH HHS/ -- R01 GM061126/GM/NIGMS NIH HHS/ -- R01 GM067858/GM/NIGMS NIH HHS/ -- RC4 GM096355/GM/NIGMS NIH HHS/ -- T32 HD055200/HD/NICHD NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Nov 30;338(6111):1229-32. doi: 10.1126/science.1228745.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Developmental Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23197537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Calcium-Binding Proteins/*metabolism ; Cells, Cultured ; DNA Mutational Analysis ; Drosophila Proteins/*genetics/*metabolism ; Drosophila melanogaster/genetics/*metabolism ; Epidermal Growth Factor/genetics ; Evolution, Molecular ; Humans ; Intercellular Signaling Peptides and Proteins/*metabolism ; Intracellular Signaling Peptides and Proteins/*metabolism ; Ligands ; Male ; Membrane Proteins/*metabolism ; Methionine/genetics ; Molecular Sequence Data ; Mutation ; Receptor, Notch2/genetics/metabolism ; Receptors, Notch/*genetics/*metabolism ; Tandem Repeat Sequences/genetics ; Valine/genetics ; X Chromosome/genetics
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    Bacterial quorum sensing and metabolic incentives to cooperate (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-10-16
    Description: The opportunistic pathogen Pseudomonas aeruginosa uses a cell-cell communication system termed "quorum sensing" to control production of public goods, extracellular products that can be used by any community member. Not all individuals respond to quorum-sensing signals and synthesize public goods. Such social cheaters enjoy the benefits of the products secreted by cooperators. There are some P. aeruginosa cellular enzymes controlled by quorum sensing, and we show that quorum sensing-controlled expression of such private goods can put a metabolic constraint on social cheating and prevent a tragedy of the commons. Metabolic constraint of social cheating provides an explanation for private-goods regulation by a cooperative system and has general implications for population biology, infection control, and stabilization of quorum-sensing circuits in synthetic biology.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587168/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587168/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dandekar, Ajai A -- Chugani, Sudha -- Greenberg, E Peter -- GM-59026/GM/NIGMS NIH HHS/ -- P30 DK 89507/DK/NIDDK NIH HHS/ -- P30 DK089507/DK/NIDDK NIH HHS/ -- R01 GM059026/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Oct 12;338(6104):264-6. doi: 10.1126/science.1227289.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Pulmonary and Critical Care Medicine, University of Washington School of Medicine, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23066081" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl-Butyrolactones/metabolism ; Adenosine/*metabolism ; Bacterial Proteins/genetics/metabolism ; Caseins/metabolism ; Culture Media/metabolism ; Microarray Analysis ; Mutation ; Pseudomonas aeruginosa/genetics/*growth & development/*metabolism ; Quorum Sensing/genetics/*physiology ; Signal Transduction ; Social Behavior ; Trans-Activators/genetics/metabolism
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    Evolutionary dynamics of gene and isoform regulation in Mammalian tissues (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-12-22
    Description: Most mammalian genes produce multiple distinct messenger RNAs through alternative splicing, but the extent of splicing conservation is not clear. To assess tissue-specific transcriptome variation across mammals, we sequenced complementary DNA from nine tissues from four mammals and one bird in biological triplicate, at unprecedented depth. We find that while tissue-specific gene expression programs are largely conserved, alternative splicing is well conserved in only a subset of tissues and is frequently lineage-specific. Thousands of previously unknown, lineage-specific, and conserved alternative exons were identified; widely conserved alternative exons had signatures of binding by MBNL, PTB, RBFOX, STAR, and TIA family splicing factors, implicating them as ancestral mammalian splicing regulators. Our data also indicate that alternative splicing often alters protein phosphorylatability, delimiting the scope of kinase signaling.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3568499/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3568499/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merkin, Jason -- Russell, Caitlin -- Chen, Ping -- Burge, Christopher B -- OD011092/OD/NIH HHS/ -- R01 HG002439/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2012 Dec 21;338(6114):1593-9. doi: 10.1126/science.1228186.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23258891" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Animals ; Biological Evolution ; Cattle ; Chickens ; Conserved Sequence ; DNA, Complementary ; DNA-Binding Proteins/metabolism ; *Evolution, Molecular ; Exons ; Gene Expression Profiling ; *Gene Expression Regulation ; Introns ; Macaca mulatta ; Male ; Mammals/*genetics ; Mice ; Models, Genetic ; Phosphorylation ; Phylogeny ; Protein Isoforms/chemistry/*genetics/metabolism ; Protein Kinases/genetics/metabolism ; RNA Splice Sites ; RNA Splicing ; RNA-Binding Proteins/metabolism ; Rats ; Sequence Analysis, DNA ; *Transcriptome
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    Structure and allostery of the PKA RIIbeta tetrameric holoenzyme (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-11
    Description: In its physiological state, cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) is a tetramer that contains a regulatory (R) subunit dimer and two catalytic (C) subunits. We describe here the 2.3 angstrom structure of full-length tetrameric RIIbeta(2):C(2) holoenzyme. This structure showing a dimer of dimers provides a mechanistic understanding of allosteric activation by cAMP. The heterodimers are anchored together by an interface created by the beta4-beta5 loop in the RIIbeta subunit, which docks onto the carboxyl-terminal tail of the adjacent C subunit, thereby forcing the C subunit into a fully closed conformation in the absence of nucleotide. Diffusion of magnesium adenosine triphosphate (ATP) into these crystals trapped not ATP, but the reaction products, adenosine diphosphate and the phosphorylated RIIbeta subunit. This complex has implications for the dissociation-reassociation cycling of PKA. The quaternary structure of the RIIbeta tetramer differs appreciably from our model of the RIalpha tetramer, confirming the small-angle x-ray scattering prediction that the structures of each PKA tetramer are different.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985767/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985767/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Ping -- Smith-Nguyen, Eric V -- Keshwani, Malik M -- Deal, Michael S -- Kornev, Alexandr P -- Taylor, Susan S -- GM34921/GM/NIGMS NIH HHS/ -- R01 GM034921/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Feb 10;335(6069):712-6. doi: 10.1126/science.1213979.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0654, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22323819" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Allosteric Regulation ; Allosteric Site ; Amino Acid Sequence ; Animals ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinase Catalytic Subunits/*chemistry/*metabolism ; Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit/*chemistry/*metabolism ; Holoenzymes/chemistry/metabolism ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Protein Binding ; Protein Folding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Rats
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    Sex-specific adaptation drives early sex chromosome evolution in Drosophila (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-07-24
    Description: Most species' sex chromosomes are derived from ancient autosomes and show few signatures of their origins. We studied the sex chromosomes of Drosophila miranda, where a neo-Y chromosome originated only approximately 1 million years ago. Whole-genome and transcriptome analysis reveals massive degeneration of the neo-Y, that male-beneficial genes on the neo-Y are more likely to undergo accelerated protein evolution, and that neo-Y genes evolve biased expression toward male-specific tissues--the shrinking gene content of the neo-Y becomes masculinized. In contrast, although older X chromosomes show a paucity of genes expressed in male tissues, neo-X genes highly expressed in male-specific tissues undergo increased rates of protein evolution if haploid in males. Thus, the response to sex-specific selection can shift at different stages of X differentiation, resulting in masculinization or demasculinization of the X-chromosomal gene content.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4107656/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4107656/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Qi -- Bachtrog, Doris -- R01 GM076007/GM/NIGMS NIH HHS/ -- R01 GM093182/GM/NIGMS NIH HHS/ -- R01GM076007/GM/NIGMS NIH HHS/ -- R01GM093182/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jul 20;337(6092):341-5. doi: 10.1126/science.1225385.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrative Biology, University of California Berkeley, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22822149" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological/*genetics ; Animals ; Drosophila/genetics/*physiology ; *Evolution, Molecular ; Female ; Gene Expression Regulation ; *Genes, Insect ; Genome-Wide Association Study ; Male ; Mutation ; Open Reading Frames ; Sex Factors ; Testis ; X Chromosome/*genetics ; Y Chromosome/*genetics
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    Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-12-22
    Description: Neurotransmitter release depends critically on Munc18-1, Munc13, the Ca(2+) sensor synaptotagmin-1, and the soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs) syntaxin-1, synaptobrevin, and SNAP-25. In vitro reconstitutions have shown that syntaxin-1-SNAP-25 liposomes fuse efficiently with synaptobrevin liposomes in the presence of synaptotagmin-1-Ca(2+), but neurotransmitter release also requires Munc18-1 and Munc13 in vivo. We found that Munc18-1 could displace SNAP-25 from syntaxin-1 and that fusion of syntaxin-1-Munc18-1 liposomes with synaptobrevin liposomes required Munc13, in addition to SNAP-25 and synaptotagmin-1-Ca(2+). Moreover, when starting with syntaxin-1-SNAP-25 liposomes, NSF-alpha-SNAP disassembled the syntaxin-1-SNAP-25 heterodimers and abrogated fusion, which then required Munc18-1 and Munc13. We propose that fusion does not proceed through syntaxin-1-SNAP-25 heterodimers but starts with the syntaxin-1-Munc18-1 complex; Munc18-1 and Munc13 then orchestrate membrane fusion together with the SNAREs and synaptotagmin-1-Ca(2+) in an NSF- and SNAP-resistant manner.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3733786/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3733786/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ma, Cong -- Su, Lijing -- Seven, Alpay B -- Xu, Yibin -- Rizo, Josep -- NS37200/NS/NINDS NIH HHS/ -- NS40944/NS/NINDS NIH HHS/ -- R01 NS037200/NS/NINDS NIH HHS/ -- R01 NS040944/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2013 Jan 25;339(6118):421-5. doi: 10.1126/science.1230473. Epub 2012 Dec 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Key Laboratory of Molecular Biophysics, Ministry of Education, and Institute of Biophysics and Biochemistry, Huazhong University of Science and Technology, Wuhan 430074, China. cong.ma7@gmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23258414" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Humans ; Liposomes ; *Membrane Fusion ; Models, Biological ; Munc18 Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Neurotransmitter Agents/*metabolism ; Protein Binding ; Protein Multimerization ; R-SNARE Proteins/metabolism ; Rats ; Synaptic Vesicles/*metabolism ; Synaptosomal-Associated Protein 25/metabolism ; Synaptotagmin I/metabolism ; Syntaxin 1/metabolism
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    Actin, spectrin, and associated proteins form a periodic cytoskeletal structure in axons (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-12-15
    Description: Actin and spectrin play important roles in neurons, but their organization in axons and dendrites remains unclear. We used stochastic optical reconstruction microscopy to study the organization of actin, spectrin, and associated proteins in neurons. Actin formed ringlike structures that wrapped around the circumference of axons and were evenly spaced along axonal shafts with a periodicity of ~180 to 190 nanometers. This periodic structure was not observed in dendrites, which instead contained long actin filaments running along dendritic shafts. Adducin, an actin-capping protein, colocalized with the actin rings. Spectrin exhibited periodic structures alternating with those of actin and adducin, and the distance between adjacent actin-adducin rings was comparable to the length of a spectrin tetramer. Sodium channels in axons were distributed in a periodic pattern coordinated with the underlying actin-spectrin-based cytoskeleton.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815867/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815867/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, Ke -- Zhong, Guisheng -- Zhuang, Xiaowei -- R01 GM096450/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 Jan 25;339(6118):452-6. doi: 10.1126/science.1232251. Epub 2012 Dec 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23239625" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Capping Proteins/chemistry/ultrastructure ; Actin Cytoskeleton/chemistry/ultrastructure ; Actins/chemistry/*ultrastructure ; Animals ; Axons/*chemistry/*ultrastructure ; Calmodulin-Binding Proteins/chemistry/*ultrastructure ; Cells, Cultured ; Cytoskeleton/*chemistry/*ultrastructure ; Dendrites/chemistry/ultrastructure ; Hippocampus/ultrastructure ; Image Processing, Computer-Assisted ; Microscopy, Fluorescence/methods ; Neurons/chemistry/ultrastructure ; Protein Multimerization ; Rats ; Rats, Wistar ; Sodium Channels/chemistry/ultrastructure ; Spectrin/chemistry/*ultrastructure
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    Neural representations of location composed of spatially periodic bands (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-08-21
    Description: The mammalian hippocampal formation provides neuronal representations of environmental location, but the underlying mechanisms are poorly understood. Here, we report a class of cells whose spatially periodic firing patterns are composed of plane waves (or bands) drawn from a discrete set of orientations and wavelengths. The majority of cells recorded in parasubicular and medial entorhinal cortices of freely moving rats belonged to this class and included grid cells, an important subset that corresponds to three bands at 60 degrees orientations and has the most stable firing pattern. Occasional changes between hexagonal and nonhexagonal patterns imply a common underlying mechanism. Our results indicate a Fourier-like spatial analysis underlying neuronal representations of location, and suggest that path integration is performed by integrating displacement along a restricted set of directions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4576732/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4576732/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krupic, Julija -- Burgess, Neil -- O'Keefe, John -- 082507/Wellcome Trust/United Kingdom -- 095811/Wellcome Trust/United Kingdom -- G1000854/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2012 Aug 17;337(6096):853-7. doi: 10.1126/science.1222403.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, University College London, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22904012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Entorhinal Cortex/cytology/*physiology ; Fourier Analysis ; Hippocampus/cytology/*physiology ; Male ; Neurons/*physiology ; Rats
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    A histone acetyltransferase regulates active DNA demethylation in Arabidopsis (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-06-16
    Description: Active DNA demethylation is an important part of epigenetic regulation in plants and animals. How active DNA demethylation is regulated and its relationship with histone modification patterns are unclear. Here, we report the discovery of IDM1, a regulator of DNA demethylation in Arabidopsis. IDM1 is required for preventing DNA hypermethylation of highly homologous multicopy genes and other repetitive sequences that are normally targeted for active DNA demethylation by Repressor of Silencing 1 and related 5-methylcytosine DNA glycosylases. IDM1 binds methylated DNA at chromatin sites lacking histone H3K4 di- or trimethylation and acetylates H3 to create a chromatin environment permissible for 5-methylcytosine DNA glycosylases to function. Our study reveals how some genes are indicated by multiple epigenetic marks for active DNA demethylation and protection from silencing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575687/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575687/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Qian, Weiqiang -- Miki, Daisuke -- Zhang, Heng -- Liu, Yunhua -- Zhang, Xi -- Tang, Kai -- Kan, Yunchao -- La, Honggui -- Li, Xiaojie -- Li, Shaofang -- Zhu, Xiaohong -- Shi, Xiaobing -- Zhang, Kangling -- Pontes, Olga -- Chen, Xuemei -- Liu, Renyi -- Gong, Zhizhong -- Zhu, Jian-Kang -- R01 GM059138/GM/NIGMS NIH HHS/ -- R01 GM070795/GM/NIGMS NIH HHS/ -- R01GM059138/GM/NIGMS NIH HHS/ -- R01GM070795/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 15;336(6087):1445-8. doi: 10.1126/science.1219416.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Shanghai Center for Plant Stress Biology and Shanghai Institute of Plant Physiology and Ecology, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22700931" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Arabidopsis/*genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Chromatin/metabolism ; DNA Glycosylases/metabolism ; *DNA Methylation ; DNA, Plant/*metabolism ; Gene Silencing ; Genes, Plant ; Histone Acetyltransferases/chemistry/genetics/*metabolism ; Histones/metabolism ; Methylation ; Mutation ; Nuclear Proteins/genetics/metabolism ; Protein Structure, Tertiary ; Transgenes
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    Processing and subcellular trafficking of ER-tethered EIN2 control response to ethylene gas (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-01
    Description: Ethylene gas is essential for many developmental processes and stress responses in plants. ETHYLENE INSENSITIVE2 (EIN2), an NRAMP-like integral membrane protein, plays an essential role in ethylene signaling, but its function remains enigmatic. Here we report that phosphorylation-regulated proteolytic processing of EIN2 triggers its endoplasmic reticulum (ER)-to-nucleus translocation. ER-tethered EIN2 shows CONSTITUTIVE TRIPLE RESPONSE1 (CTR1) kinase-dependent phosphorylation. Ethylene triggers dephosphorylation at several sites and proteolytic cleavage at one of these sites, resulting in nuclear translocation of a carboxyl-terminal EIN2 fragment (EIN2-C'). Mutations that mimic EIN2 dephosphorylation, or inactivate CTR1, show constitutive cleavage and nuclear localization of EIN2-C' and EIN3 and EIN3-LIKE1-dependent activation of ethylene responses. These findings uncover a mechanism of subcellular communication whereby ethylene stimulates phosphorylation-dependent cleavage and nuclear movement of the EIN2-C' peptide, linking hormone perception and signaling components in the ER with nuclear-localized transcriptional regulators.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3523706/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3523706/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Qiao, Hong -- Shen, Zhouxin -- Huang, Shao-shan Carol -- Schmitz, Robert J -- Urich, Mark A -- Briggs, Steven P -- Ecker, Joseph R -- F32 HG004830/HG/NHGRI NIH HHS/ -- F32-HG004830/HG/NHGRI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Oct 19;338(6105):390-3. doi: 10.1126/science.1225974. Epub 2012 Aug 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22936567" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Arabidopsis/drug effects/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Cell Nucleus/*metabolism ; Endoplasmic Reticulum/*metabolism ; Ethylenes/*metabolism/pharmacology ; Gases/metabolism/pharmacology ; Mutation ; Nuclear Localization Signals/genetics/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Proteolysis ; Receptors, Cell Surface/genetics/*metabolism
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    Mysteries of the brain. Why is mental illness so hard to treat? (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-10-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2012 Oct 5;338(6103):32-3. doi: 10.1126/science.338.6103.32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23042865" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antipsychotic Agents ; Brain/drug effects/*physiopathology ; Disease Models, Animal ; Drug Discovery/history/*trends ; Gene Expression Profiling ; Genome, Human ; History, 20th Century ; History, 21st Century ; Humans ; Intellectual Disability ; Mental Disorders/drug therapy/genetics/*therapy ; Mice ; Neural Pathways ; Neuroimaging ; Neurons/metabolism/physiology ; Rats
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Coagulation factor X activates innate immunity to human species C adenovirus (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-29
    Description: Although coagulation factors play a role in host defense for "living fossils" such as horseshoe crabs, the role of the coagulation system in immunity in higher organisms remains unclear. We modeled the interface of human species C adenovirus (HAdv) interaction with coagulation factor X (FX) and introduced a mutation that abrogated formation of the HAdv-FX complex. In vivo genome-wide transcriptional profiling revealed that FX-binding-ablated virus failed to activate a distinct network of nuclear factor kappaB-dependent early-response genes that are activated by HAdv-FX complex downstream of TLR4/MyD88/TRIF/TRAF6 signaling. Our study implicates host factor "decoration" of the virus as a mechanism to trigger an innate immune sensor that responds to a misplacement of coagulation FX from the blood into intracellular macrophage compartments upon virus entry into the cell.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4762479/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4762479/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doronin, Konstantin -- Flatt, Justin W -- Di Paolo, Nelson C -- Khare, Reeti -- Kalyuzhniy, Oleksandr -- Acchione, Mauro -- Sumida, John P -- Ohto, Umeharu -- Shimizu, Toshiyuki -- Akashi-Takamura, Sachiko -- Miyake, Kensuke -- MacDonald, James W -- Bammler, Theo K -- Beyer, Richard P -- Farin, Frederico M -- Stewart, Phoebe L -- Shayakhmetov, Dmitry M -- AI065429/AI/NIAID NIH HHS/ -- CA141439/CA/NCI NIH HHS/ -- P30ES07033/ES/NIEHS NIH HHS/ -- R01 AI065429/AI/NIAID NIH HHS/ -- R01 CA141439/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 9;338(6108):795-8. doi: 10.1126/science.1226625. Epub 2012 Sep 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23019612" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae Infections/*immunology/metabolism/virology ; Adenoviruses, Human/genetics/*immunology/*metabolism ; Animals ; CHO Cells ; Capsid Proteins/chemistry/genetics/metabolism ; Cell Line, Tumor ; Cricetinae ; Cricetulus ; Cryoelectron Microscopy ; Cytokines/metabolism ; Factor X/chemistry/*metabolism ; Gene Expression Profiling ; Gene Expression Regulation ; Hepatocytes/virology ; Humans ; *Immunity, Innate ; Macrophages/metabolism/virology ; Mice ; Mice, Inbred C57BL ; Molecular Dynamics Simulation ; Mutation ; NF-kappa B/metabolism ; Signal Transduction ; Virus Internalization
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    Real-time evolution of new genes by innovation, amplification, and divergence (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-10-23
    Description: Gene duplications allow evolution of genes with new functions. Here, we describe the innovation-amplification-divergence (IAD) model in which the new function appears before duplication and functionally distinct new genes evolve under continuous selection. One example fitting this model is a preexisting parental gene in Salmonella enterica that has low levels of two distinct activities. This gene is amplified to a high copy number, and the amplified gene copies accumulate mutations that provide enzymatic specialization of different copies and faster growth. Selection maintains the initial amplification and beneficial mutant alleles but is relaxed for other less improved gene copies, allowing their loss. This rapid process, completed in fewer than 3000 generations, shows the efficacy of the IAD model and allows the study of gene evolution in real time.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4392837/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4392837/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nasvall, Joakim -- Sun, Lei -- Roth, John R -- Andersson, Dan I -- GM27068/GM/NIGMS NIH HHS/ -- R01 GM027068/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Oct 19;338(6105):384-7. doi: 10.1126/science.1226521.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23087246" target="_blank"〉PubMed〈/a〉
    Keywords: *Evolution, Molecular ; *Gene Amplification ; Gene Dosage ; *Genetic Variation ; Histidine/genetics ; *Models, Genetic ; Mutation ; Salmonella enterica/*genetics ; Selection, Genetic ; Time
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    Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-01-10
    Description: Posttranslational modification of alpha-dystroglycan (alpha-DG) by the like-acetylglucosaminyltransferase (LARGE) is required for it to function as an extracellular matrix (ECM) receptor. Mutations in the LARGE gene have been identified in congenital muscular dystrophy patients with brain abnormalities. However, the precise function of LARGE remains unclear. Here we found that LARGE could act as a bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, which produced repeating units of [-3-xylose-alpha1,3-glucuronic acid-beta1-]. This modification allowed alpha-DG to bind laminin-G domain-containing ECM ligands.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3702376/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3702376/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inamori, Kei-ichiro -- Yoshida-Moriguchi, Takako -- Hara, Yuji -- Anderson, Mary E -- Yu, Liping -- Campbell, Kevin P -- 1U54NS053672/NS/NINDS NIH HHS/ -- U54 NS053672/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Jan 6;335(6064):93-6. doi: 10.1126/science.1214115.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Physiology and Biophysics, University of Iowa Roy J. and Lucille A. Carver College of Medicine, 4283 Carver Biomedical Research Building, 285 Newton Road, Iowa City, IA 52242-1101, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22223806" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; CHO Cells ; Carbohydrate Conformation ; Catalytic Domain ; Cricetinae ; Dystroglycans/chemistry/*metabolism ; Glucuronic Acid/metabolism ; Glucuronosyltransferase/metabolism ; Glycosaminoglycans/metabolism ; Glycosylation ; HEK293 Cells ; Humans ; Laminin/metabolism ; Ligands ; Mice ; Mutation ; N-Acetylglucosaminyltransferases/chemistry/genetics/*metabolism ; Pentosyltransferases/metabolism ; Polysaccharides/*metabolism ; Protein Processing, Post-Translational ; Recombinant Proteins/metabolism ; Xylose/metabolism
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    MORC family ATPases required for heterochromatin condensation and gene silencing (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-05
    Description: Transposable elements (TEs) and DNA repeats are commonly targeted by DNA and histone methylation to achieve epigenetic gene silencing. We isolated mutations in two Arabidopsis genes, AtMORC1 and AtMORC6, which cause derepression of DNA-methylated genes and TEs but no losses of DNA or histone methylation. AtMORC1 and AtMORC6 are members of the conserved Microrchidia (MORC) adenosine triphosphatase (ATPase) family, which are predicted to catalyze alterations in chromosome superstructure. The atmorc1 and atmorc6 mutants show decondensation of pericentromeric heterochromatin, increased interaction of pericentromeric regions with the rest of the genome, and transcriptional defects that are largely restricted to loci residing in pericentromeric regions. Knockdown of the single MORC homolog in Caenorhabditis elegans also impairs transgene silencing. We propose that the MORC ATPases are conserved regulators of gene silencing in eukaryotes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3376212/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3376212/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moissiard, Guillaume -- Cokus, Shawn J -- Cary, Joshua -- Feng, Suhua -- Billi, Allison C -- Stroud, Hume -- Husmann, Dylan -- Zhan, Ye -- Lajoie, Bryan R -- McCord, Rachel Patton -- Hale, Christopher J -- Feng, Wei -- Michaels, Scott D -- Frand, Alison R -- Pellegrini, Matteo -- Dekker, Job -- Kim, John K -- Jacobsen, Steven E -- F32 GM100617/GM/NIGMS NIH HHS/ -- F32GM100617/GM/NIGMS NIH HHS/ -- GM007185/GM/NIGMS NIH HHS/ -- GM075060/GM/NIGMS NIH HHS/ -- GM088565/GM/NIGMS NIH HHS/ -- GM60398/GM/NIGMS NIH HHS/ -- HG003143/HG/NHGRI NIH HHS/ -- R01 GM075060/GM/NIGMS NIH HHS/ -- R01 GM088565/GM/NIGMS NIH HHS/ -- R01 HG003143/HG/NHGRI NIH HHS/ -- R37 GM060398/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Jun 15;336(6087):1448-51. doi: 10.1126/science.1221472. Epub 2012 May 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cell, and Developmental Biology, University of California at Los Angeles, Terasaki Life Sciences Building, 610 Charles Young Drive East, Los Angeles, CA 90095-723905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22555433" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry/genetics/*metabolism ; Animals ; Arabidopsis/enzymology/*genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/genetics/metabolism ; Centromere ; DNA Methylation ; DNA Transposable Elements ; *Gene Silencing ; Genes, Plant ; Heterochromatin/*metabolism/ultrastructure ; Histones/metabolism ; Methylation ; Mutation ; RNA, Small Interfering/metabolism ; Transcription, Genetic ; Transgenes ; Up-Regulation
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    Cost-benefit tradeoffs in engineered lac operons (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-19
    Description: Cells must balance the cost and benefit of protein expression to optimize organismal fitness. The lac operon of the bacterium Escherichia coli has been a model for quantifying the physiological impact of costly protein production and for elucidating the resulting regulatory mechanisms. We report quantitative fitness measurements in 27 redesigned operons that suggested that protein production is not the primary origin of fitness costs. Instead, we discovered that the lac permease activity, which relates linearly to cost, is the major physiological burden to the cell. These findings explain control points in the lac operon that minimize the cost of lac permease activity, not protein expression. Characterizing similar relationships in other systems will be important to map the impact of cost/benefit tradeoffs on cell physiology and regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eames, Matt -- Kortemme, Tanja -- New York, N.Y. -- Science. 2012 May 18;336(6083):911-5. doi: 10.1126/science.1219083.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Group in Biophysics, MC 2530, University of California, San Francisco, CA 94158-2330, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22605776" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biocatalysis ; Biological Transport ; Escherichia coli/*genetics/growth & development/metabolism ; Escherichia coli Proteins/*genetics/*metabolism ; Gene Expression Regulation, Bacterial ; Gene Knockout Techniques ; Genetic Engineering ; Isopropyl Thiogalactoside/metabolism ; *Lac Operon ; Lac Repressors ; Lactose/metabolism ; Models, Biological ; Molecular Sequence Data ; Monosaccharide Transport Proteins/*genetics/*metabolism ; Mutation ; Symporters/*genetics/*metabolism ; beta-Galactosidase/*genetics/*metabolism
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    Neurexin and neuroligin mediate retrograde synaptic inhibition in C. elegans (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-08-04
    Description: The synaptic adhesion molecules neurexin and neuroligin alter the development and function of synapses and are linked to autism in humans. Here, we found that Caenorhabditis elegans neurexin (NRX-1) and neuroligin (NLG-1) mediated a retrograde synaptic signal that inhibited neurotransmitter release at neuromuscular junctions. Retrograde signaling was induced in mutants lacking a muscle microRNA (miR-1) and was blocked in mutants lacking NLG-1 or NRX-1. Release was rapid and abbreviated when the retrograde signal was on, whereas release was slow and prolonged when retrograde signaling was blocked. The retrograde signal adjusted release kinetics by inhibiting exocytosis of synaptic vesicles (SVs) that are distal to the site of calcium entry. Inhibition of release was mediated by increased presynaptic levels of tomosyn, an inhibitor of SV fusion.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791080/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791080/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, Zhitao -- Hom, Sabrina -- Kudze, Tambudzai -- Tong, Xia-Jing -- Choi, Seungwon -- Aramuni, Gayane -- Zhang, Weiqi -- Kaplan, Joshua M -- NS32196/NS/NINDS NIH HHS/ -- R37 NS032196/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2012 Aug 24;337(6097):980-4. doi: 10.1126/science.1224896. Epub 2012 Aug 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22859820" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Caenorhabditis elegans Proteins/genetics/*metabolism ; Cell Adhesion Molecules, Neuronal/genetics/*metabolism ; Cholinergic Neurons/physiology ; Excitatory Postsynaptic Potentials ; Exocytosis ; Kinetics ; Mice ; MicroRNAs/genetics/metabolism ; Motor Neurons/physiology ; Mutation ; Neural Inhibition ; Neuromuscular Junction/*physiology ; Neurotransmitter Agents/metabolism ; *Synaptic Transmission ; Synaptic Vesicles/physiology ; Transcription Factors/genetics/metabolism ; Transfection
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    Landscape of somatic retrotransposition in human cancers (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-30
    Description: Transposable elements (TEs) are abundant in the human genome, and some are capable of generating new insertions through RNA intermediates. In cancer, the disruption of cellular mechanisms that normally suppress TE activity may facilitate mutagenic retrotranspositions. We performed single-nucleotide resolution analysis of TE insertions in 43 high-coverage whole-genome sequencing data sets from five cancer types. We identified 194 high-confidence somatic TE insertions, as well as thousands of polymorphic TE insertions in matched normal genomes. Somatic insertions were present in epithelial tumors but not in blood or brain cancers. Somatic L1 insertions tend to occur in genes that are commonly mutated in cancer, disrupt the expression of the target genes, and are biased toward regions of cancer-specific DNA hypomethylation, highlighting their potential impact in tumorigenesis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3656569/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3656569/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Eunjung -- Iskow, Rebecca -- Yang, Lixing -- Gokcumen, Omer -- Haseley, Psalm -- Luquette, Lovelace J 3rd -- Lohr, Jens G -- Harris, Christopher C -- Ding, Li -- Wilson, Richard K -- Wheeler, David A -- Gibbs, Richard A -- Kucherlapati, Raju -- Lee, Charles -- Kharchenko, Peter V -- Park, Peter J -- Cancer Genome Atlas Research Network -- F32 AG039979/AG/NIA NIH HHS/ -- F32AG039979/AG/NIA NIH HHS/ -- K25 AG037596/AG/NIA NIH HHS/ -- K25AG037596/AG/NIA NIH HHS/ -- R01 GM082798/GM/NIGMS NIH HHS/ -- R01GM082798/GM/NIGMS NIH HHS/ -- RC1HG005482/HG/NHGRI NIH HHS/ -- T32 CA009172/CA/NCI NIH HHS/ -- U01 HG005725/HG/NHGRI NIH HHS/ -- U01HG005209/HG/NHGRI NIH HHS/ -- U01HG005725/HG/NHGRI NIH HHS/ -- U24 CA144025/CA/NCI NIH HHS/ -- U24CA144025/CA/NCI NIH HHS/ -- U54 HG003273/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2012 Aug 24;337(6097):967-71. doi: 10.1126/science.1222077. Epub 2012 Jun 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biomedical Informatics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22745252" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Transformation, Neoplastic ; Colorectal Neoplasms/*genetics ; DNA Methylation ; Female ; Gene Expression Regulation, Neoplastic ; Genes, Neoplasm ; Genome, Human ; Glioblastoma/*genetics ; Humans ; Long Interspersed Nucleotide Elements ; Male ; Microsatellite Instability ; Molecular Sequence Annotation ; Molecular Sequence Data ; Multiple Myeloma/*genetics ; Mutagenesis, Insertional ; Mutation ; Ovarian Neoplasms/*genetics ; Prostatic Neoplasms/*genetics ; *Retroelements ; Sequence Analysis, DNA
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    Physico-genetic determinants in the evolution of development (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-10-16
    Description: Animal bodies and the embryos that generate them exhibit an assortment of stereotypic morphological motifs that first appeared more than half a billion years ago. During development, cells arrange themselves into tissues with interior cavities and multiple layers with immiscible boundaries, containing patterned arrangements of cell types. These tissues go on to elongate, fold, segment, and form appendages. Their motifs are similar to the outcomes of physical processes generic to condensed, chemically excitable, viscoelastic materials, although the embryonic mechanisms that generate them are typically much more complex. I propose that the origins of animal development lay in the mobilization of physical organizational effects that resulted when certain gene products of single-celled ancestors came to operate on the spatial scale of multicellular aggregates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, Stuart A -- New York, N.Y. -- Science. 2012 Oct 12;338(6104):217-9. doi: 10.1126/science.1222003.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, New York Medical College, Valhalla, NY 10595, USA. newman@nymc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23066074" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Body Patterning/*genetics ; Chimerism/embryology ; Cleavage Stage, Ovum ; Invertebrates/embryology ; Mutation ; Physical Phenomena ; *Physical Processes ; Vertebrates/embryology
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    AIDS/HIV. HIV interplay with SAMHD1 (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaller, Torsten -- Goujon, Caroline -- Malim, Michael H -- G0401570/Medical Research Council/United Kingdom -- G1000196/Medical Research Council/United Kingdom -- G1001081/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2012 Mar 16;335(6074):1313-4. doi: 10.1126/science.1221057.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Infectious Diseases, King's College London School of Medicine, Guy's Hospital, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22422971" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptive Immunity ; Animals ; Autoimmune Diseases of the Nervous System/genetics ; DNA, Complementary/metabolism ; Genes, Viral ; HIV Infections/immunology/*virology ; HIV-1/*immunology/pathogenicity/*physiology ; HIV-2/pathogenicity ; Humans ; Immunity, Innate ; Monomeric GTP-Binding Proteins/chemistry/genetics/*metabolism ; Mutation ; Myeloid Cells/*virology ; Nervous System Malformations/genetics ; Nucleotides/metabolism ; Simian Immunodeficiency Virus/pathogenicity ; Viral Regulatory and Accessory Proteins/genetics/metabolism ; Virus Replication
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    Chloroplast biogenesis is regulated by direct action of the ubiquitin-proteasome system (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-11-03
    Description: Development of chloroplasts and other plastids depends on the import of thousands of nucleus-encoded proteins from the cytosol. Import is initiated by TOC (translocon at the outer envelope of chloroplasts) complexes in the plastid outer membrane that incorporate multiple, client-specific receptors. Modulation of import is thought to control the plastid's proteome, developmental fate, and functions. Using forward genetics, we identified Arabidopsis SP1, which encodes a RING-type ubiquitin E3 ligase of the chloroplast outer membrane. The SP1 protein associated with TOC complexes and mediated ubiquitination of TOC components, promoting their degradation. Mutant sp1 plants performed developmental transitions that involve plastid proteome changes inefficiently, indicating a requirement for reorganization of the TOC machinery. Thus, the ubiquitin-proteasome system acts on plastids to control their development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ling, Qihua -- Huang, Weihua -- Baldwin, Amy -- Jarvis, Paul -- BB/D016541/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/H008039/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2012 Nov 2;338(6107):655-9. doi: 10.1126/science.1225053.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Leicester, Leicester LE1 7RH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23118188" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis Regulatory Proteins/chemistry/*genetics/*metabolism ; Arabidopsis/genetics/growth & development/*metabolism/ultrastructure ; Arabidopsis Proteins/chemistry/*genetics/*metabolism ; Chloroplast Proteins/*metabolism ; Chloroplasts/*metabolism/ultrastructure ; Membrane Proteins/genetics/metabolism ; Mutation ; Proteasome Endopeptidase Complex/*metabolism ; Protein Precursors/genetics/metabolism ; Protein Transport ; Proteome ; RING Finger Domains ; Ubiquitin-Protein Ligases/chemistry/*genetics/*metabolism ; Ubiquitination
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    Awake hippocampal sharp-wave ripples support spatial memory (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-05
    Description: The hippocampus is critical for spatial learning and memory. Hippocampal neurons in awake animals exhibit place field activity that encodes current location, as well as sharp-wave ripple (SWR) activity during which representations based on past experiences are often replayed. The relationship between these patterns of activity and the memory functions of the hippocampus is poorly understood. We interrupted awake SWRs in animals learning a spatial alternation task. We observed a specific learning and performance deficit that persisted throughout training. This deficit was associated with awake SWR activity, as SWR interruption left place field activity and post-experience SWR reactivation intact. These results provide a link between awake SWRs and hippocampal memory processes, which suggests that awake replay of memory-related information during SWRs supports learning and memory-guided decision-making.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4441285/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4441285/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jadhav, Shantanu P -- Kemere, Caleb -- German, P Walter -- Frank, Loren M -- R01 MH080283/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 15;336(6087):1454-8. doi: 10.1126/science.1217230. Epub 2012 May 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Center for Integrative Neuroscience, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22555434" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Waves/*physiology ; CA1 Region, Hippocampal/*physiology ; Decision Making ; Electric Stimulation ; Hippocampus/*physiology ; Male ; Maze Learning ; Memory/*physiology ; Memory, Short-Term ; Nerve Net/physiology ; Rats ; Rats, Long-Evans ; Space Perception ; Synaptic Potentials ; Wakefulness/*physiology
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    Evolution, safety, and highly pathogenic influenza viruses (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: Experience with influenza has shown that predictions of virus phenotype or fitness from nucleotide sequence are imperfect and that predicting the timing and course of evolution is extremely difficult. Such uncertainty means that the risk of experiments with mammalian-transmissible, possibly highly virulent influenza viruses remains high even if some aspects of their laboratory biology are reassuring; it also implies limitations on the ability of laboratory observations to guide interpretation of surveillance of strains in the field. Thus, we propose that future experiments with virulent pathogens whose accidental or deliberate release could lead to extensive spread in human populations should be limited by explicit risk-benefit considerations.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3467308/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3467308/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lipsitch, Marc -- Plotkin, Joshua B -- Simonsen, Lone -- Bloom, Barry -- U54 GM088558/GM/NIGMS NIH HHS/ -- U54GM088558/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1529-31. doi: 10.1126/science.1223204.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Communicable Disease Dynamics and Department of Epidemiology, Harvard School of Public Health, Boston, MA 02115, USA. mlipsitc@hsph.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723411" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigenic Variation ; Antigens, Viral ; Antiviral Agents/pharmacology/therapeutic use ; Biohazard Release ; *Containment of Biohazards ; Drug Resistance, Viral ; *Evolution, Molecular ; Ferrets ; Humans ; Influenza A Virus, H5N1 Subtype/genetics/*pathogenicity ; Influenza A virus/drug effects/genetics/immunology/*pathogenicity ; Influenza, Human/drug therapy/transmission/*virology ; Laboratory Infection/epidemiology ; Mutation ; Orthomyxoviridae Infections/transmission/*virology ; Public Policy ; Risk Assessment ; *Safety ; Security Measures ; United States/epidemiology
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    Evolutionarily assembled cis-regulatory module at a human ciliopathy locus (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-01-28
    Description: Neighboring genes are often coordinately expressed within cis-regulatory modules, but evidence that nonparalogous genes share functions in mammals is lacking. Here, we report that mutation of either TMEM138 or TMEM216 causes a phenotypically indistinguishable human ciliopathy, Joubert syndrome. Despite a lack of sequence homology, the genes are aligned in a head-to-tail configuration and joined by chromosomal rearrangement at the amphibian-to-reptile evolutionary transition. Expression of the two genes is mediated by a conserved regulatory element in the noncoding intergenic region. Coordinated expression is important for their interdependent cellular role in vesicular transport to primary cilia. Hence, during vertebrate evolution of genes involved in ciliogenesis, nonparalogous genes were arranged to a functional gene cluster with shared regulatory elements.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3671610/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3671610/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Jeong Ho -- Silhavy, Jennifer L -- Lee, Ji Eun -- Al-Gazali, Lihadh -- Thomas, Sophie -- Davis, Erica E -- Bielas, Stephanie L -- Hill, Kiley J -- Iannicelli, Miriam -- Brancati, Francesco -- Gabriel, Stacey B -- Russ, Carsten -- Logan, Clare V -- Sharif, Saghira Malik -- Bennett, Christopher P -- Abe, Masumi -- Hildebrandt, Friedhelm -- Diplas, Bill H -- Attie-Bitach, Tania -- Katsanis, Nicholas -- Rajab, Anna -- Koul, Roshan -- Sztriha, Laszlo -- Waters, Elizabeth R -- Ferro-Novick, Susan -- Woods, C Geoffrey -- Johnson, Colin A -- Valente, Enza Maria -- Zaki, Maha S -- Gleeson, Joseph G -- DK068306/DK/NIDDK NIH HHS/ -- DK072301/DK/NIDDK NIH HHS/ -- DK075972/DK/NIDDK NIH HHS/ -- DK090917/DK/NIDDK NIH HHS/ -- EY021872/EY/NEI NIH HHS/ -- G0700073/Medical Research Council/United Kingdom -- GGP08145/Telethon/Italy -- HD042601/HD/NICHD NIH HHS/ -- NS04843/NS/NINDS NIH HHS/ -- NS052455/NS/NINDS NIH HHS/ -- P30 CA023100/CA/NCI NIH HHS/ -- P30NS047101/NS/NINDS NIH HHS/ -- R01 DK068306/DK/NIDDK NIH HHS/ -- R01 DK072301/DK/NIDDK NIH HHS/ -- R01 DK075972/DK/NIDDK NIH HHS/ -- R01 EY021872/EY/NEI NIH HHS/ -- R01 HD042601/HD/NICHD NIH HHS/ -- R01 NS048453/NS/NINDS NIH HHS/ -- R01 NS052455/NS/NINDS NIH HHS/ -- U54 HG003067/HG/NHGRI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Feb 24;335(6071):966-9. doi: 10.1126/science.1213506. Epub 2012 Jan 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurogenetics Laboratory, Howard Hughes Medical Institute (HHMI), Department of Neurosciences, University of California, San Diego, CA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22282472" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cerebellar Diseases/*genetics/metabolism/pathology ; Cilia/metabolism/*ultrastructure ; Conserved Sequence ; DNA, Intergenic ; *Evolution, Molecular ; Eye Abnormalities/*genetics/metabolism/pathology ; Gene Expression Profiling ; *Gene Expression Regulation ; Genetic Heterogeneity ; *Genetic Loci ; Humans ; Kidney Diseases, Cystic/*genetics/metabolism/pathology ; Membrane Proteins/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Mutation ; Mutation, Missense ; Phenotype ; Protein Transport ; *Regulatory Sequences, Nucleic Acid ; Retina/abnormalities/metabolism/pathology ; Transport Vesicles/metabolism/ultrastructure
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    Cotranscriptional role for Arabidopsis DICER-LIKE 4 in transcription termination (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-31
    Description: Transcription termination is emerging as an important component of gene regulation necessary to partition the genome and minimize transcriptional interference. We have discovered a role for the Arabidopsis RNA silencing enzyme DICER-LIKE 4 (DCL4) in transcription termination of an endogenous Arabidopsis gene, FCA. DCL4 directly associates with FCA chromatin in the 3' region and promotes cleavage of the nascent transcript in a domain downstream of the canonical polyA site. In a dcl4 mutant, the resulting transcriptional read-through triggers an RNA interference-mediated gene silencing of a transgene containing the same 3' region. We conclude that DCL4 promotes transcription termination of the Arabidopsis FCA gene, reducing the amount of aberrant RNA produced from the locus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Fuquan -- Bakht, Saleha -- Dean, Caroline -- BB/D010799/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/G01406X/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2012 Mar 30;335(6076):1621-3. doi: 10.1126/science.1214402.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22461611" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/metabolism ; Arabidopsis Proteins/*genetics/metabolism ; Base Sequence ; Chromatin/genetics/metabolism ; Chromatin Immunoprecipitation ; *Gene Expression Regulation, Plant ; MADS Domain Proteins/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Polyadenylation ; Protein Structure, Tertiary ; RNA Interference ; RNA, Messenger/genetics/metabolism ; RNA, Plant/*genetics/metabolism ; RNA-Binding Proteins/*genetics/metabolism ; Ribonuclease III/chemistry/genetics/*metabolism ; *Transcription, Genetic ; Transgenes
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    The potential for respiratory droplet-transmissible A/H5N1 influenza virus to evolve in a mammalian host (2012)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2012-06-23
    Description: Avian A/H5N1 influenza viruses pose a pandemic threat. As few as five amino acid substitutions, or four with reassortment, might be sufficient for mammal-to-mammal transmission through respiratory droplets. From surveillance data, we found that two of these substitutions are common in A/H5N1 viruses, and thus, some viruses might require only three additional substitutions to become transmissible via respiratory droplets between mammals. We used a mathematical model of within-host virus evolution to study factors that could increase and decrease the probability of the remaining substitutions evolving after the virus has infected a mammalian host. These factors, combined with the presence of some of these substitutions in circulating strains, make a virus evolving in nature a potentially serious threat. These results highlight critical areas in which more data are needed for assessing, and potentially averting, this threat.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3426314/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3426314/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, Colin A -- Fonville, Judith M -- Brown, Andre E X -- Burke, David F -- Smith, David L -- James, Sarah L -- Herfst, Sander -- van Boheemen, Sander -- Linster, Martin -- Schrauwen, Eefje J -- Katzelnick, Leah -- Mosterin, Ana -- Kuiken, Thijs -- Maher, Eileen -- Neumann, Gabriele -- Osterhaus, Albert D M E -- Kawaoka, Yoshihiro -- Fouchier, Ron A M -- Smith, Derek J -- DP1 OD000490/OD/NIH HHS/ -- DP1-OD000490-01/OD/NIH HHS/ -- HHSN266200700010C/AI/NIAID NIH HHS/ -- HHSN266200700010C/PHS HHS/ -- R01 AI 069274/AI/NIAID NIH HHS/ -- R56 AI069274/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1541-7. doi: 10.1126/science.1222526.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723414" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Air Microbiology ; Amino Acid Substitution ; Animals ; Birds ; *Evolution, Molecular ; Genetic Fitness ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus/*genetics/metabolism ; High-Throughput Nucleotide Sequencing ; Humans ; Influenza A Virus, H5N1 Subtype/*genetics/*pathogenicity ; Influenza in Birds/virology ; Influenza, Human/immunology/transmission/*virology ; Mammals ; Models, Biological ; Mutation ; Orthomyxoviridae Infections/transmission/*virology ; Probability ; RNA Replicase/*genetics ; Receptors, Virus/metabolism ; Respiratory System/*virology ; Selection, Genetic ; Sialic Acids/metabolism ; Viral Proteins/*genetics
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    Molecular biology. Genetic events that shape the cancer epigenome (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ryan, Russell J H -- Bernstein, Bradley E -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1513-4. doi: 10.1126/science.1223730.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Pathology and Center for Cancer Research, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723401" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/chemistry/*metabolism/ultrastructure ; DNA Methylation ; Enhancer Elements, Genetic ; *Epigenesis, Genetic ; *Gene Expression Regulation, Neoplastic ; Gene Silencing ; *Genome, Human ; Histones/genetics/*metabolism ; Humans ; Methylation ; Mutation ; Neoplasms/*genetics/metabolism ; Promoter Regions, Genetic ; Transcription Factors/*metabolism ; *Transcription, Genetic
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    The path from beta-carotene to carlactone, a strigolactone-like plant hormone (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-17
    Description: Strigolactones, phytohormones with diverse signaling activities, have a common structure consisting of two lactones connected by an enol-ether bridge. Strigolactones derive from carotenoids via a pathway involving the carotenoid cleavage dioxygenases 7 and 8 (CCD7 and CCD8) and the iron-binding protein D27. We show that D27 is a beta-carotene isomerase that converts all-trans-beta-carotene into 9-cis-beta-carotene, which is cleaved by CCD7 into a 9-cis-configured aldehyde. CCD8 incorporates three oxygens into 9-cis-beta-apo-10'-carotenal and performs molecular rearrangement, linking carotenoids with strigolactones and producing carlactone, a compound with strigolactone-like biological activities. Knowledge of the structure of carlactone will be crucial for understanding the biology of strigolactones and may have applications in combating parasitic weeds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alder, Adrian -- Jamil, Muhammad -- Marzorati, Mattia -- Bruno, Mark -- Vermathen, Martina -- Bigler, Peter -- Ghisla, Sandro -- Bouwmeester, Harro -- Beyer, Peter -- Al-Babili, Salim -- New York, N.Y. -- Science. 2012 Mar 16;335(6074):1348-51. doi: 10.1126/science.1218094.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Biology, University of Freiburg, Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22422982" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/genetics/metabolism ; Biosynthetic Pathways ; Carotenoids/chemistry/metabolism ; Dioxygenases/genetics/metabolism ; Germination ; Isomerases/genetics/metabolism ; Lactones/chemistry/*metabolism/pharmacology ; Molecular Structure ; Mutation ; Oryza/genetics/*metabolism ; Peas/genetics/*metabolism ; Phenotype ; Plant Growth Regulators/*biosynthesis/chemistry ; Plant Proteins/genetics/metabolism ; Stereoisomerism ; Striga/growth & development ; beta Carotene/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Function, targets, and evolution of Caenorhabditis elegans piRNAs (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-16
    Description: Piwi-interacting RNAs (piRNAs) are small RNAs required to maintain germline integrity and fertility, but their mechanism of action is poorly understood. Here we demonstrate that Caenorhabditis elegans piRNAs silence transcripts in trans through imperfectly complementary sites. Target silencing is independent of Piwi endonuclease activity or "slicing." Instead, piRNAs initiate a localized secondary endogenous small interfering RNA (endo-siRNA) response. Endogenous protein-coding gene and transposon transcripts exhibit Piwi-dependent endo-siRNAs at sites complementary to piRNAs and are derepressed in Piwi mutants. Genomic loci of piRNA biogenesis are depleted of protein-coding genes and tend to overlap the start and end of transposons in sense and antisense, respectively. Our data suggest that nematode piRNA clusters are evolving to generate piRNAs against active mobile elements. Thus, piRNAs provide heritable, sequence-specific triggers for RNA interference in C. elegans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3951736/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3951736/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bagijn, Marloes P -- Goldstein, Leonard D -- Sapetschnig, Alexandra -- Weick, Eva-Maria -- Bouasker, Samir -- Lehrbach, Nicolas J -- Simard, Martin J -- Miska, Eric A -- 092096/Wellcome Trust/United Kingdom -- 11832/Cancer Research UK/United Kingdom -- A14492/Cancer Research UK/United Kingdom -- Wellcome Trust/United Kingdom -- Cancer Research UK/United Kingdom -- Canadian Institutes of Health Research/Canada -- New York, N.Y. -- Science. 2012 Aug 3;337(6094):574-8. doi: 10.1126/science.1220952. Epub 2012 Jun 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gurdon Institute and Department of Biochemistry, University of Cambridge, The Henry Wellcome Building of Cancer and Developmental Biology, Tennis Court Road, Cambridge CB2 1QN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22700655" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Argonaute Proteins/genetics ; Caenorhabditis elegans/*genetics ; Caenorhabditis elegans Proteins/genetics ; Evolution, Molecular ; Mutation ; *RNA Interference ; RNA, Double-Stranded/biosynthesis/genetics ; RNA, Small Interfering/genetics/*metabolism ; *Transcription, Genetic
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    Restoring voluntary control of locomotion after paralyzing spinal cord injury (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-02
    Description: Half of human spinal cord injuries lead to chronic paralysis. Here, we introduce an electrochemical neuroprosthesis and a robotic postural interface designed to encourage supraspinally mediated movements in rats with paralyzing lesions. Despite the interruption of direct supraspinal pathways, the cortex regained the capacity to transform contextual information into task-specific commands to execute refined locomotion. This recovery relied on the extensive remodeling of cortical projections, including the formation of brainstem and intraspinal relays that restored qualitative control over electrochemically enabled lumbosacral circuitries. Automated treadmill-restricted training, which did not engage cortical neurons, failed to promote translesional plasticity and recovery. By encouraging active participation under functional states, our training paradigm triggered a cortex-dependent recovery that may improve function after similar injuries in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van den Brand, Rubia -- Heutschi, Janine -- Barraud, Quentin -- DiGiovanna, Jack -- Bartholdi, Kay -- Huerlimann, Michele -- Friedli, Lucia -- Vollenweider, Isabel -- Moraud, Eduardo Martin -- Duis, Simone -- Dominici, Nadia -- Micera, Silvestro -- Musienko, Pavel -- Courtine, Gregoire -- New York, N.Y. -- Science. 2012 Jun 1;336(6085):1182-5. doi: 10.1126/science.1217416.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurology Department, University of Zurich, CH-8008 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22654062" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology ; Brain Stem/physiology ; Dopamine Agonists/administration & dosage ; Electric Stimulation ; Female ; Gait ; Hindlimb/*physiology ; *Locomotion ; Motor Cortex/*physiology ; Nerve Fibers/physiology ; Neuronal Plasticity ; Neurons/physiology ; Paralysis/physiopathology/*rehabilitation ; Pyramidal Tracts/cytology/*physiology ; Rats ; Rats, Inbred Lew ; Recovery of Function ; *Robotics ; Serotonin Receptor Agonists/administration & dosage ; Spinal Cord/cytology/physiology ; Spinal Cord Injuries/physiopathology/*rehabilitation
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Influenza. One H5N1 paper finally goes to press; second greenlighted (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, Martin -- Cohen, Jon -- New York, N.Y. -- Science. 2012 May 4;336(6081):529-30. doi: 10.1126/science.336.6081.529.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22556223" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites/genetics ; Containment of Biohazards ; Ferrets ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/*genetics/metabolism ; Humans ; Influenza A Virus, H5N1 Subtype/genetics/*pathogenicity ; Influenza, Human/transmission/virology ; Mutation ; Orthomyxoviridae Infections/transmission/virology ; *Publishing ; Receptors, Virus/metabolism ; Virus Internalization
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Mutations in BCKD-kinase lead to a potentially treatable form of autism with epilepsy (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-08
    Description: Autism spectrum disorders are a genetically heterogeneous constellation of syndromes characterized by impairments in reciprocal social interaction. Available somatic treatments have limited efficacy. We have identified inactivating mutations in the gene BCKDK (Branched Chain Ketoacid Dehydrogenase Kinase) in consanguineous families with autism, epilepsy, and intellectual disability. The encoded protein is responsible for phosphorylation-mediated inactivation of the E1alpha subunit of branched-chain ketoacid dehydrogenase (BCKDH). Patients with homozygous BCKDK mutations display reductions in BCKDK messenger RNA and protein, E1alpha phosphorylation, and plasma branched-chain amino acids. Bckdk knockout mice show abnormal brain amino acid profiles and neurobehavioral deficits that respond to dietary supplementation. Thus, autism presenting with intellectual disability and epilepsy caused by BCKDK mutations represents a potentially treatable syndrome.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3704165/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3704165/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Novarino, Gaia -- El-Fishawy, Paul -- Kayserili, Hulya -- Meguid, Nagwa A -- Scott, Eric M -- Schroth, Jana -- Silhavy, Jennifer L -- Kara, Majdi -- Khalil, Rehab O -- Ben-Omran, Tawfeg -- Ercan-Sencicek, A Gulhan -- Hashish, Adel F -- Sanders, Stephan J -- Gupta, Abha R -- Hashem, Hebatalla S -- Matern, Dietrich -- Gabriel, Stacey -- Sweetman, Larry -- Rahimi, Yasmeen -- Harris, Robert A -- State, Matthew W -- Gleeson, Joseph G -- K08 MH087639/MH/NIMH NIH HHS/ -- K08MH087639/MH/NIMH NIH HHS/ -- P01 HD070494/HD/NICHD NIH HHS/ -- P01HD070494/HD/NICHD NIH HHS/ -- P30 NS047101/NS/NINDS NIH HHS/ -- P30NS047101/NS/NINDS NIH HHS/ -- R01 NS041537/NS/NINDS NIH HHS/ -- R01 NS048453/NS/NINDS NIH HHS/ -- R01NS048453/NS/NINDS NIH HHS/ -- R25 MH077823/MH/NIMH NIH HHS/ -- RC2 MH089956/MH/NIMH NIH HHS/ -- RC2MH089956/MH/NIMH NIH HHS/ -- T32MH018268/MH/NIMH NIH HHS/ -- U54HG003067/HG/NHGRI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Oct 19;338(6105):394-7. doi: 10.1126/science.1224631. Epub 2012 Sep 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurogenetics Laboratory, Howard Hughes Medical Institute, Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093, USA. gnovarino@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22956686" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)/*administration & ; dosage/deficiency/*genetics ; Adolescent ; Amino Acids, Branched-Chain/administration & dosage/blood/deficiency ; Animals ; Arginine/genetics ; Autistic Disorder/*diet therapy/enzymology/*genetics ; Base Sequence ; Brain/metabolism ; Child ; Child, Preschool ; Diet ; Epilepsy/*diet therapy/enzymology/*genetics ; Female ; Homozygote ; Humans ; Intellectual Disability/diet therapy/enzymology/genetics ; Male ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; Pedigree ; Phosphorylation ; Protein Folding ; Protein Structure, Tertiary ; RNA, Messenger/metabolism ; Young Adult
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    The fission yeast FANCM ortholog directs non-crossover recombination during meiosis (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: The formation of healthy gametes depends on programmed DNA double-strand breaks (DSBs), which are each repaired as a crossover (CO) or non-crossover (NCO) from a homologous template. Although most of these DSBs are repaired without giving COs, little is known about the genetic requirements of NCO-specific recombination. We show that Fml1, the Fanconi anemia complementation group M (FANCM)-ortholog of Schizosaccharomyces pombe, directs the formation of NCOs during meiosis in competition with the Mus81-dependent pro-CO pathway. We also define the Rad51/Dmc1-mediator Swi5-Sfr1 as a major determinant in biasing the recombination process in favor of Mus81, to ensure the appropriate amount of COs to guide meiotic chromosome segregation. The conservation of these proteins from yeast to humans suggests that this interplay may be a general feature of meiotic recombination.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399777/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399777/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lorenz, Alexander -- Osman, Fekret -- Sun, Weili -- Nandi, Saikat -- Steinacher, Roland -- Whitby, Matthew C -- 090767/Wellcome Trust/United Kingdom -- 090767/Z/09/Z/Wellcome Trust/United Kingdom -- J 2489/Austrian Science Fund FWF/Austria -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1585-8. doi: 10.1126/science.1220111.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Oxford, Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723423" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Segregation ; Chromosomes, Fungal/physiology ; *Crossing Over, Genetic ; DNA Breaks, Double-Stranded ; DNA Helicases/genetics/*metabolism ; DNA Repair ; DNA, Fungal/chemistry/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Endonucleases/genetics/metabolism ; *Homologous Recombination ; *Meiosis ; Mutation ; Recombinases/genetics/metabolism ; Schizosaccharomyces/*genetics/physiology ; Schizosaccharomyces pombe Proteins/genetics/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Type 6 secretion dynamics within and between bacterial cells (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-07-07
    Description: The bacterial type 6 secretion system (T6SS) functions as a virulence factor capable of attacking both eukaryotic and prokaryotic target cells by a process that involves protein transport through a contractile bacteriophage tail-like structure. The T6SS apparatus is composed, in part, of an exterior sheath wrapped around an interior tube. Here, we report that in living cells the cytoplasmic adenosine triphosphatase called ClpV specifically recognizes the contracted T6SS sheath structure, causing its disassembly within seconds. ClpV imaging allowed spatial and temporal documentation of cell-cell interactions (termed T6SS dueling) that likely mark the location of repeated T6SS-mediated protein translocation events between bacterial cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3557511/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3557511/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Basler, M -- Mekalanos, J J -- AI-018045/AI/NIAID NIH HHS/ -- AI-26289/AI/NIAID NIH HHS/ -- R01 AI018045/AI/NIAID NIH HHS/ -- R01 AI026289/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2012 Aug 17;337(6096):815. doi: 10.1126/science.1222901. Epub 2012 Jul 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunobiology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22767897" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/genetics/metabolism ; Amino Acid Substitution ; Bacterial Proteins/genetics/*metabolism ; *Bacterial Secretion Systems ; Green Fluorescent Proteins/genetics/metabolism ; Microscopy, Fluorescence/methods ; Molecular Imaging/methods ; Mutation ; Protein Transport ; Pseudomonas aeruginosa/metabolism/*physiology ; Recombinant Fusion Proteins/genetics/metabolism ; Tyrosine/genetics/metabolism ; Vibrio cholerae/metabolism/*physiology
    Print ISSN: 0036-8075
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    Immunology. Orchestrating inflammasomes (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-18
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4340476/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4340476/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Franchi, Luigi -- Nunez, Gabriel -- R01 DK091191/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2012 Sep 14;337(6100):1299-300. doi: 10.1126/science.1229010.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22984056" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CARD Signaling Adaptor Proteins/genetics/*metabolism ; Calcium-Binding Proteins/genetics/*metabolism ; Enzyme Activation ; Gram-Negative Bacteria/*immunology ; Gram-Negative Bacterial Infections/enzymology/*immunology ; Humans ; Inflammasomes/*metabolism ; Mice ; Mice, Mutant Strains ; Mutation ; Phosphorylation ; Protein Kinase C-delta/*metabolism ; Serine/genetics/metabolism
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    Multiple spectral inputs improve motion discrimination in the Drosophila visual system (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-19
    Description: Color and motion information are thought to be channeled through separate neural pathways, but it remains unclear whether and how these pathways interact to improve motion perception. In insects, such as Drosophila, it has long been believed that motion information is fed exclusively by one spectral class of photoreceptor, so-called R1 to R6 cells; whereas R7 and R8 photoreceptors, which exist in multiple spectral classes, subserve color vision. Here, we report that R7 and R8 also contribute to the motion pathway. By using electrophysiological, optical, and behavioral assays, we found that R7/R8 information converge with and shape the motion pathway output, explaining flies' broadly tuned optomotor behavior by its composite responses. Our results demonstrate that inputs from photoreceptors of different spectral sensitivities improve motion discrimination, increasing robustness of perception.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wardill, Trevor J -- List, Olivier -- Li, Xiaofeng -- Dongre, Sidhartha -- McCulloch, Marie -- Ting, Chun-Yuan -- O'Kane, Cahir J -- Tang, Shiming -- Lee, Chi-Hon -- Hardie, Roger C -- Juusola, Mikko -- BB/D007585/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/F012071/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/G006865/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/H013849/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2012 May 18;336(6083):925-31. doi: 10.1126/science.1215317.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Science, University of Sheffield, Sheffield S10 2TN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22605779" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Color Vision ; Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Flight, Animal ; Gap Junctions/physiology ; Genes, Insect ; Light ; Models, Neurological ; *Motion Perception ; Mutation ; Neurons/physiology ; Opsins/metabolism ; Optic Lobe, Nonmammalian/cytology/physiology ; Patch-Clamp Techniques ; Photoreceptor Cells, Invertebrate/*physiology/ultrastructure ; Transgenes ; Ultraviolet Rays ; Visual Pathways
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    Preventing Alzheimer's disease (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-22
    Description: Despite intensive laboratory and clinical research over three decades, an effective treatment to delay the onset and progression of Alzheimer's disease is not at hand. Recent clinical trial failures suggest that we must treat the disease earlier than in its mild to moderate stages, and major progress in validating presymptomatic biomarkers now makes secondary prevention trials possible. We will learn more about the natural history of the disease and any partial therapeutic responses from detailed analyses of recent trial results. This process will likely position the field for success, but only with much greater investment in all aspects of Alzheimer research and with careful design of future trials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selkoe, Dennis J -- New York, N.Y. -- Science. 2012 Sep 21;337(6101):1488-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. dselkoe@rics.bwh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22997326" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/diagnosis/etiology/*prevention & control/therapy ; Amyloid beta-Peptides/cerebrospinal fluid/genetics/metabolism ; Animals ; Apolipoproteins E/genetics ; Biomarkers/analysis/cerebrospinal fluid ; Clinical Trials as Topic ; Disease Progression ; Genetic Predisposition to Disease ; Humans ; Life Style ; Mutation ; Peptide Fragments/cerebrospinal fluid ; Secondary Prevention
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Avian influenza. Surprising twist in debate over lab-made H5N1 (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2012 Mar 9;335(6073):1155-6. doi: 10.1126/science.335.6073.1155.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22403358" target="_blank"〉PubMed〈/a〉
    Keywords: Access to Information ; Animals ; Containment of Biohazards ; Disease Models, Animal ; Ferrets ; Humans ; Influenza A Virus, H5N1 Subtype/genetics/*pathogenicity ; Influenza, Human/epidemiology/transmission/*virology ; Mutation ; Orthomyxoviridae Infections/transmission/*virology ; Pandemics ; Publishing
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Influence of synaptic vesicle position on release probability and exocytotic fusion mode (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-22
    Description: Neurotransmission depends on movements of transmitter-laden synaptic vesicles, but accurate, nanometer-scale monitoring of vesicle dynamics in presynaptic terminals has remained elusive. Here, we report three-dimensional, real-time tracking of quantum dot-loaded single synaptic vesicles with an accuracy of 20 to 30 nanometers, less than a vesicle diameter. Determination of the time, position, and mode of fusion, aided by trypan blue quenching of Qdot fluorescence, revealed that vesicles starting close to their ultimate fusion sites tended to fuse earlier than those positioned farther away. The mode of fusion depended on the prior motion of vesicles, with long-dwelling vesicles preferring kiss-and-run rather than full-collapse fusion. Kiss-and-run fusion events were concentrated near the center of the synapse, whereas full-collapse fusion events were broadly spread.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3776413/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3776413/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Hyokeun -- Li, Yulong -- Tsien, Richard W -- R01 MH064070/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2012 Mar 16;335(6074):1362-6. doi: 10.1126/science.1216937. Epub 2012 Feb 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22345401" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; *Exocytosis ; Imaging, Three-Dimensional ; *Membrane Fusion ; Microscopy, Fluorescence ; Neurons/physiology/ultrastructure ; Presynaptic Terminals/*physiology/ultrastructure ; Rats ; Synaptic Transmission ; Synaptic Vesicles/*physiology/ultrastructure ; Trypan Blue
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Avian influenza. The limits of avian flu studies in ferrets (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2012 Feb 3;335(6068):512-3. doi: 10.1126/science.335.6068.512.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22301288" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens ; *Disease Models, Animal ; *Ferrets ; Humans ; Influenza A Virus, H1N1 Subtype/pathogenicity ; Influenza A Virus, H5N1 Subtype/genetics/*pathogenicity ; Influenza in Birds/epidemiology ; Influenza, Human/epidemiology/transmission/*virology ; Mutation ; Orthomyxoviridae Infections/transmission/*virology ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Animal cognition. 'Killjoys' challenge claims of clever animals (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2012 Mar 2;335(6072):1036-7. doi: 10.1126/science.335.6072.1036.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22383823" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; Birds ; *Cognition ; Empathy ; Humans ; Learning ; Pan troglodytes ; Rats ; Theory of Mind
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    Avian influenza. On second thought, flu papers get go-ahead (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- Malakoff, David -- New York, N.Y. -- Science. 2012 Apr 6;336(6077):19-20. doi: 10.1126/science.336.6077.19.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22491833" target="_blank"〉PubMed〈/a〉
    Keywords: *Access to Information ; Advisory Committees ; Animals ; Birds ; Humans ; Influenza A Virus, H5N1 Subtype/genetics/*pathogenicity ; Influenza in Birds/transmission/*virology ; Influenza, Human/transmission/virology ; Mammals ; Mutation ; National Institutes of Health (U.S.) ; Netherlands ; Orthomyxoviridae Infections/*virology ; Public Policy ; *Publishing ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Public health and biosecurity. Life sciences at a crossroads: respiratory transmissible H5N1 (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Osterholm, Michael T -- Henderson, Donald A -- New York, N.Y. -- Science. 2012 Feb 17;335(6070):801-2. doi: 10.1126/science.1218612. Epub 2012 Jan 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Infectious Disease Research and Division of Environmental Health Sciences, Medical School, University of Minnesota, Minneapolis, MN 55455, USA. mto@umn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22267584" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds ; *Containment of Biohazards ; Humans ; Influenza A Virus, H5N1 Subtype/genetics/*pathogenicity ; Influenza Vaccines ; Influenza in Birds/epidemiology/transmission ; Influenza, Human/prevention & control/*transmission/virology ; *Information Dissemination/ethics ; Mutation ; Pandemics ; Public Health ; Publishing/ethics ; *Security Measures
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    FKF1 conveys timing information for CONSTANS stabilization in photoperiodic flowering (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-26
    Description: Plants use day-length information to coordinate flowering time with the appropriate season to maximize reproduction. In Arabidopsis, the long day-specific expression of CONSTANS (CO) protein is crucial for flowering induction. Although light signaling regulates CO protein stability, the mechanism by which CO is stabilized in the long-day afternoon has remained elusive. Here, we demonstrate that FLAVIN-BINDING, KELCH REPEAT, F-BOX 1 (FKF1) protein stabilizes CO protein in the afternoon in long days. FKF1 interacts with CO through its LOV domain, and blue light enhances this interaction. In addition, FKF1 simultaneously removes CYCLING DOF FACTOR 1 (CDF1), which represses CO and FLOWERING LOCUS T (FT) transcription. Together with CO transcriptional regulation, FKF1 protein controls robust FT mRNA induction through multiple feedforward mechanisms that accurately control flowering timing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737243/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737243/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, Young Hun -- Smith, Robert W -- To, Benjamin J -- Millar, Andrew J -- Imaizumi, Takato -- BB/F005237/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/F59011/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/G019621/Biotechnology and Biological Sciences Research Council/United Kingdom -- GM079712/GM/NIGMS NIH HHS/ -- R01 GM079712/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 May 25;336(6084):1045-9. doi: 10.1126/science.1219644.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22628657" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/growth & development/metabolism/*physiology ; Arabidopsis Proteins/chemistry/*genetics/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Flowers/*growth & development ; Gene Expression Regulation, Plant ; Light ; Models, Biological ; Mutation ; *Photoperiod ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Stability ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Repressor Proteins/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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  • 98
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    Function and molecular mechanism of acetylation in autophagy regulation (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-04-28
    Description: Protein acetylation emerged as a key regulatory mechanism for many cellular processes. We used genetic analysis of Saccharomyces cerevisiae to identify Esa1 as a histone acetyltransferase required for autophagy. We further identified the autophagy signaling component Atg3 as a substrate for Esa1. Specifically, acetylation of K19 and K48 of Atg3 regulated autophagy by controlling Atg3 and Atg8 interaction and lipidation of Atg8. Starvation induced transient K19-K48 acetylation through spatial and temporal regulation of the localization of acetylase Esa1 and the deacetylase Rpd3 on pre-autophagosomal structures (PASs) and their interaction with Atg3. Attenuation of K19-K48 acetylation was associated with attenuation of autophagy. Increased K19-K48 acetylation after deletion of the deacetylase Rpd3 caused increased autophagy. Thus, protein acetylation contributes to control of autophagy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yi, Cong -- Ma, Meisheng -- Ran, Leili -- Zheng, Jingxiang -- Tong, Jingjing -- Zhu, Jing -- Ma, Chengying -- Sun, Yufen -- Zhang, Shaojin -- Feng, Wenzhi -- Zhu, Liyuan -- Le, Yan -- Gong, Xingqi -- Yan, Xianghua -- Hong, Bing -- Jiang, Fen-Jun -- Xie, Zhiping -- Miao, Di -- Deng, Haiteng -- Yu, Li -- New York, N.Y. -- Science. 2012 Apr 27;336(6080):474-7. doi: 10.1126/science.1216990.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22539722" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; *Autophagy ; Carbohydrate Epimerases/genetics/metabolism ; Histone Acetyltransferases/genetics/*metabolism ; Histone Deacetylases/genetics/metabolism ; Microtubule-Associated Proteins/metabolism ; Mutation ; Phagosomes/metabolism ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/enzymology/genetics/*physiology ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Ubiquitin-Conjugating Enzymes/chemistry/genetics/*metabolism
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  • 99
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    FANCM limits meiotic crossovers (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: The number of meiotic crossovers (COs) is tightly regulated within a narrow range, despite a large excess of molecular precursors. The factors that limit COs remain largely unknown. Here, using a genetic screen in Arabidopsis thaliana, we identified the highly conserved FANCM helicase, which is required for genome stability in humans and yeasts, as a major factor limiting meiotic CO formation. The fancm mutant has a threefold-increased CO frequency as compared to the wild type. These extra COs arise not from the pathway that accounts for most of the COs in wild type, but from an alternate, normally minor pathway. Thus, FANCM is a key factor imposing an upper limit on the number of meiotic COs, and its manipulation holds much promise for plant breeding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crismani, Wayne -- Girard, Chloe -- Froger, Nicole -- Pradillo, Monica -- Santos, Juan Luis -- Chelysheva, Liudmila -- Copenhaver, Gregory P -- Horlow, Christine -- Mercier, Raphael -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1588-90. doi: 10.1126/science.1220381.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Recherche Agronomique (INRA), UMR1318, Institut Jean-Pierre Bourgin, Versailles, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22723424" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/growth & development/physiology ; Arabidopsis Proteins/genetics/*metabolism ; Cation Transport Proteins/genetics/metabolism ; Chromosome Segregation ; Chromosomes, Plant/physiology/ultrastructure ; *Crossing Over, Genetic ; DNA Helicases/genetics/*metabolism ; Endonucleases/genetics/metabolism ; Genetic Complementation Test ; Homologous Recombination ; In Situ Hybridization, Fluorescence ; *Meiosis ; Mutation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Cilia at the node of mouse embryos sense fluid flow for left-right determination via Pkd2 (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-18
    Description: Unidirectional fluid flow plays an essential role in the breaking of left-right (L-R) symmetry in mouse embryos, but it has remained unclear how the flow is sensed by the embryo. We report that the Ca(2+) channel Polycystin-2 (Pkd2) is required specifically in the perinodal crown cells for sensing the nodal flow. Examination of mutant forms of Pkd2 shows that the ciliary localization of Pkd2 is essential for correct L-R patterning. Whereas Kif3a mutant embryos, which lack all cilia, failed to respond to an artificial flow, restoration of primary cilia in crown cells rescued the response to the flow. Our results thus suggest that nodal flow is sensed in a manner dependent on Pkd2 by the cilia of crown cells located at the edge of the node.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711115/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711115/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshiba, Satoko -- Shiratori, Hidetaka -- Kuo, Ivana Y -- Kawasumi, Aiko -- Shinohara, Kyosuke -- Nonaka, Shigenori -- Asai, Yasuko -- Sasaki, Genta -- Belo, Jose Antonio -- Sasaki, Hiroshi -- Nakai, Junichi -- Dworniczak, Bernd -- Ehrlich, Barbara E -- Pennekamp, Petra -- Hamada, Hiroshi -- P30 DK090744/DK/NIDDK NIH HHS/ -- P50 DK057328/DK/NIDDK NIH HHS/ -- R01 DK087844/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2012 Oct 12;338(6104):226-31. doi: 10.1126/science.1222538. Epub 2012 Sep 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Developmental Genetics Group, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, 565-0871 Osaka, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22983710" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Fluids/physiology ; *Body Patterning ; Calcium/metabolism ; Cilia/metabolism/physiology ; Embryo, Mammalian/anatomy & histology/cytology/*physiology ; Gene Expression Regulation, Developmental ; Intercellular Signaling Peptides and Proteins/metabolism ; Kinesin/genetics ; Left-Right Determination Factors/genetics/*metabolism ; Mice ; Mice, Mutant Strains ; Mutation ; Organizers, Embryonic/cytology/*physiology ; Signal Transduction ; TRPP Cation Channels/genetics/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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