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  • Mice  (249)
  • Rats  (208)
  • Molecular Sequence Data  (86)
  • Adult  (65)
  • American Association for the Advancement of Science (AAAS)  (563)
  • 2005-2009  (304)
  • 1980-1984  (259)
  • 2005  (304)
  • 1981  (259)
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  • American Association for the Advancement of Science (AAAS)  (563)
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  • 2005-2009  (304)
  • 1980-1984  (259)
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  • 1
    Publication Date: 2005-12-03
    Description: Macrophages and dendritic cells (DCs) are crucial for immune and inflammatory responses and belong to a network of cells that has been termed the mononuclear phagocyte system (MPS). However, the origin and lineage of these cells remain poorly understood. Here, we describe the isolation and clonal analysis of a mouse bone marrow progenitor that is specific for monocytes, several macrophage subsets, and resident spleen DCs in vivo. It was also possible to recapitulate this differentiation in vitro by using treatment with the cytokines macrophage colony-stimulating factor and granulocyte-macrophage colony-stimulating factor. Thus, macrophages and DCs appear to renew from a common progenitor, providing a cellular and molecular basis for the concept of the MPS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fogg, Darin K -- Sibon, Claire -- Miled, Chaouki -- Jung, Steffen -- Aucouturier, Pierre -- Littman, Dan R -- Cumano, Ana -- Geissmann, Frederic -- A133856/PHS HHS/ -- G0900867/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):83-7. Epub 2005 Dec 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM, Laboratory of Mononuclear Phagocyte Biology, Avenir Team, Necker Enfants Malades Institute, 75015 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322423" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Lineage ; Cell Separation ; Clone Cells ; Colony-Stimulating Factors/pharmacology ; Dendritic Cells/*cytology ; Flow Cytometry ; Granulocyte Colony-Stimulating Factor/pharmacology ; Hematopoietic Stem Cell Transplantation ; Macrophage Colony-Stimulating Factor/pharmacology ; Macrophages/*cytology ; Mice ; Mice, Inbred C57BL ; Myeloid Progenitor Cells/*cytology/immunology ; Proto-Oncogene Proteins c-kit/analysis ; Receptors, Cytokine/analysis ; Receptors, HIV/analysis ; Recombinant Proteins ; Spleen/cytology
    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
    Publication Date: 2005-02-26
    Description: The genomic diversity and relative importance of distinct genotypes within natural bacterial populations have remained largely unknown. Here, we analyze the diversity and annual dynamics of a group of coastal bacterioplankton (greater than 99% 16S ribosomal RNA identity to Vibrio splendidus). We show that this group consists of at least a thousand distinct genotypes, each occurring at extremely low environmental concentrations (on average less than one cell per milliliter). Overall, the genomes show extensive allelic diversity and size variation. Individual genotypes rarely recurred in samples, and allelic distribution did not show spatial or temporal substructure. Ecological considerations suggest that much genotypic and possibly phenotypic variation within natural populations should be considered neutral.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, Janelle R -- Pacocha, Sarah -- Pharino, Chanathip -- Klepac-Ceraj, Vanja -- Hunt, Dana E -- Benoit, Jennifer -- Sarma-Rupavtarm, Ramahi -- Distel, Daniel L -- Polz, Martin F -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1311-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Civil and Environmental Engineering, Massachusetts Institute of Technology (MIT), Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731455" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Chaperonin 60/genetics ; *Ecosystem ; Electrophoresis, Gel, Pulsed-Field ; *Genetic Variation ; Genome, Bacterial ; Genotype ; Molecular Sequence Data ; Plankton/classification/*genetics/growth & development/isolation & purification ; Polymerase Chain Reaction ; Ribotyping ; Seawater/*microbiology ; Time Factors ; Vibrio/classification/*genetics/isolation & purification
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-10-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Jean -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):43-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autophagy ; Brain-Derived Neurotrophic Factor/metabolism ; Cells, Cultured ; Clinical Trials as Topic ; Corpus Striatum/pathology ; Disease Models, Animal ; Gene Expression Regulation ; Humans ; Huntington Disease/*drug therapy/genetics/pathology/*physiopathology ; Mice ; Mitochondria/metabolism ; Mutation ; Nerve Tissue Proteins/chemistry/*genetics/metabolism/*physiology ; Neurons/*physiology ; Nuclear Proteins/chemistry/*genetics/metabolism/*physiology ; Peptides ; Transcription Factors/metabolism ; Trinucleotide Repeat Expansion
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  • 4
    Publication Date: 2005-02-01
    Description: Pollen tube guidance precedes the double fertilization of flowering plants. Here, we report the identification of a small maize protein of 94 amino acids involved in short-range signaling required for pollen tube attraction by the female gametophyte. ZmEA1 is exclusively expressed in the egg apparatus, consisting of the egg cell and two synergids. Chimeric ZmEA1 fused to green fluorescent protein (ZmEA1:GFP) was first visible within the filiform apparatus and later was localized to nucellar cell walls below the micropylar opening of the ovule. Transgenic down-regulation of the ZmEA1 gene led to ovule sterility caused by loss of close-range pollen tube guidance to the micropyle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marton, Mihaela L -- Cordts, Simone -- Broadhvest, Jean -- Dresselhaus, Thomas -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biocenter Klein Flottbek, Developmental Biology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, D-22609 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antisense Elements (Genetics) ; Crosses, Genetic ; DNA, Complementary ; Flowers/growth & development/*physiology ; Genes, Plant ; Green Fluorescent Proteins/metabolism ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/*physiology ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Reproduction ; Seeds/physiology ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Zea mays/*genetics/*physiology
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  • 5
    Publication Date: 2005-10-29
    Description: Recurrent chromosomal rearrangements have not been well characterized in common carcinomas. We used a bioinformatics approach to discover candidate oncogenic chromosomal aberrations on the basis of outlier gene expression. Two ETS transcription factors, ERG and ETV1, were identified as outliers in prostate cancer. We identified recurrent gene fusions of the 5' untranslated region of TMPRSS2 to ERG or ETV1 in prostate cancer tissues with outlier expression. By using fluorescence in situ hybridization, we demonstrated that 23 of 29 prostate cancer samples harbor rearrangements in ERG or ETV1. Cell line experiments suggest that the androgen-responsive promoter elements of TMPRSS2 mediate the overexpression of ETS family members in prostate cancer. These results have implications in the development of carcinomas and the molecular diagnosis and treatment of prostate cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomlins, Scott A -- Rhodes, Daniel R -- Perner, Sven -- Dhanasekaran, Saravana M -- Mehra, Rohit -- Sun, Xiao-Wei -- Varambally, Sooryanarayana -- Cao, Xuhong -- Tchinda, Joelle -- Kuefer, Rainer -- Lee, Charles -- Montie, James E -- Shah, Rajal B -- Pienta, Kenneth J -- Rubin, Mark A -- Chinnaiyan, Arul M -- 5P30 CA46592/CA/NCI NIH HHS/ -- P50CA69568/CA/NCI NIH HHS/ -- R01 CA97063/CA/NCI NIH HHS/ -- R01AG21404/AG/NIA NIH HHS/ -- UO1 CA111275-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):644-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Michigan Medical School, 1301 Catherine Street, Ann Arbor, MI 48109-0602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16254181" target="_blank"〉PubMed〈/a〉
    Keywords: Androgens/metabolism ; Cell Line, Tumor ; DNA-Binding Proteins/*genetics ; Gene Expression Regulation, Neoplastic ; Gene Rearrangement ; Humans ; In Situ Hybridization, Fluorescence ; Male ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Neoplasm Proteins/*genetics ; Oncogene Proteins, Fusion/*genetics ; Polymerase Chain Reaction ; Prostatic Neoplasms/*genetics ; Serine Endopeptidases/*genetics ; Trans-Activators/*genetics ; Transcription Factors/*genetics ; Translocation, Genetic
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  • 6
    Publication Date: 2005-05-28
    Description: Searles Lake is a salt-saturated, alkaline brine unusually rich in the toxic element arsenic. Arsenic speciation changed from arsenate [As(V)] to arsenite [As(III)] with sediment depth. Incubated anoxic sediment slurries displayed dissimilatory As(V)-reductase activity that was markedly stimulated by H2 or sulfide, whereas aerobic slurries had rapid As(III)-oxidase activity. An anaerobic, extremely haloalkaliphilic bacterium was isolated from the sediment that grew via As(V) respiration, using either lactate or sulfide as its electron donor. Hence, a full biogeochemical cycle of arsenic occurs in Searles Lake, driven in part by inorganic electron donors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oremland, Ronald S -- Kulp, Thomas R -- Blum, Jodi Switzer -- Hoeft, Shelley E -- Baesman, Shaun -- Miller, Laurence G -- Stolz, John F -- New York, N.Y. -- Science. 2005 May 27;308(5726):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Geological Survey, ms 480, 345 Middlefield Road, Menlo Park, CA 94025, USA. roremlan@usgs.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15919992" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Anaerobiosis ; Arsenates/*metabolism ; Arsenites/*metabolism ; Bacteria, Anaerobic/classification/growth & development/*isolation & ; purification/*metabolism ; Bicarbonates/metabolism ; California ; Ecosystem ; Electron Transport ; Genes, rRNA ; Geologic Sediments/*microbiology ; Hydrogen-Ion Concentration ; Lactic Acid/metabolism ; Molecular Sequence Data ; Oxidation-Reduction ; Phylogeny ; *Salts ; Sodium Chloride ; Sulfides/metabolism ; Water/chemistry ; *Water Microbiology
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-09-06
    Description: Large numbers of noncoding RNA transcripts (ncRNAs) are being revealed by complementary DNA cloning and genome tiling array studies in animals. The big and as yet largely unanswered question is whether these transcripts are relevant. A paper by Willingham et al. shows the way forward by developing a strategy for large-scale functional screening of ncRNAs, involving small interfering RNA knockdowns in cell-based screens, which identified a previously unidentified ncRNA repressor of the transcription factor NFAT. It appears likely that ncRNAs constitute a critical hidden layer of gene regulation in complex organisms, the understanding of which requires new approaches in functional genomics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mattick, John S -- New York, N.Y. -- Science. 2005 Sep 2;309(5740):1527-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Australian Research Council Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia. j.mattick@imb.uq.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16141063" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Conserved Sequence ; DNA-Binding Proteins/antagonists & inhibitors ; *Genomics ; Humans ; Mice ; NFATC Transcription Factors ; Nuclear Proteins/antagonists & inhibitors ; *RNA Interference ; RNA, Untranslated/antagonists & inhibitors/genetics/*physiology ; Transcription Factors/antagonists & inhibitors ; beta Karyopherins/metabolism
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  • 8
    Publication Date: 2005-06-11
    Description: In animal societies, chemical communication plays an important role in conflict and cooperation. For ants, cuticular hydrocarbon (CHC) blends produced by non-nestmates elicit overt aggression. We describe a sensory sensillum on the antennae of the carpenter ant Camponotus japonicus that functions in nestmate discrimination. This sensillum is multiporous and responds only to non-nestmate CHC blends. This suggests a role for a peripheral recognition mechanism in detecting colony-specific chemical signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ozaki, Mamiko -- Wada-Katsumata, Ayako -- Fujikawa, Kazuyo -- Iwasaki, Masayuki -- Yokohari, Fumio -- Satoji, Yuji -- Nisimura, Tomoyosi -- Yamaoka, Ryohei -- New York, N.Y. -- Science. 2005 Jul 8;309(5732):311-4. Epub 2005 Jun 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan. mamiko@kit.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947139" target="_blank"〉PubMed〈/a〉
    Keywords: Aggression ; Amino Acid Sequence ; Animals ; Ants/*physiology ; Base Sequence ; *Behavior, Animal ; Carrier Proteins/chemistry/isolation & purification/metabolism ; Chemoreceptor Cells/*physiology ; Cues ; Electrophysiology ; *Hydrocarbons ; Insect Proteins/chemistry/isolation & purification/metabolism ; Microscopy, Electron, Scanning ; Molecular Sequence Data ; Neurons, Afferent/*physiology ; Sense Organs/physiology ; Social Behavior
    Print ISSN: 0036-8075
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  • 9
    Publication Date: 2005-12-17
    Description: Translesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of poleta and poliota to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of poleta is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bienko, Marzena -- Green, Catherine M -- Crosetto, Nicola -- Rudolf, Fabian -- Zapart, Grzegorz -- Coull, Barry -- Kannouche, Patricia -- Wider, Gerhard -- Peter, Matthias -- Lehmann, Alan R -- Hofmann, Kay -- Dikic, Ivan -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1821-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biochemistry II, Goethe University Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Line ; Computational Biology ; DNA/*biosynthesis ; *DNA Damage ; DNA Repair ; DNA Replication ; DNA-Directed DNA Polymerase/*chemistry/genetics/*metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Point Mutation ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Binding ; Protein Conformation ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Transfection ; Ubiquitin/*metabolism ; Xeroderma Pigmentosum/genetics ; Zinc Fingers
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  • 10
    Publication Date: 2005-04-23
    Description: The CLOCK transcription factor is a key component of the molecular circadian clock within pacemaker neurons of the hypothalamic suprachiasmatic nucleus. We found that homozygous Clock mutant mice have a greatly attenuated diurnal feeding rhythm, are hyperphagic and obese, and develop a metabolic syndrome of hyperleptinemia, hyperlipidemia, hepatic steatosis, hyperglycemia, and hypoinsulinemia. Expression of transcripts encoding selected hypothalamic peptides associated with energy balance was attenuated in the Clock mutant mice. These results suggest that the circadian clock gene network plays an important role in mammalian energy balance.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3764501/" 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/PMC3764501/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turek, Fred W -- Joshu, Corinne -- Kohsaka, Akira -- Lin, Emily -- Ivanova, Ganka -- McDearmon, Erin -- Laposky, Aaron -- Losee-Olson, Sue -- Easton, Amy -- Jensen, Dalan R -- Eckel, Robert H -- Takahashi, Joseph S -- Bass, Joseph -- AG11412/AG/NIA NIH HHS/ -- AG18200/AG/NIA NIH HHS/ -- DK02675/DK/NIDDK NIH HHS/ -- DK26356/DK/NIDDK NIH HHS/ -- HL59598/HL/NHLBI NIH HHS/ -- HL75029/HL/NHLBI NIH HHS/ -- K08 DK002675/DK/NIDDK NIH HHS/ -- P01 AG011412/AG/NIA NIH HHS/ -- R01 AG018200/AG/NIA NIH HHS/ -- R01 DK026356/DK/NIDDK NIH HHS/ -- R01 HL059598/HL/NHLBI NIH HHS/ -- R01 HL075029/HL/NHLBI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2005 May 13;308(5724):1043-5. Epub 2005 Apr 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15845877" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/pathology ; Animals ; Body Weight ; Brain/metabolism ; CLOCK Proteins ; *Circadian Rhythm ; Dietary Fats/administration & dosage ; Energy Intake ; *Energy Metabolism ; *Feeding Behavior ; Hepatocytes/pathology ; Hyperglycemia ; Hyperlipidemias ; Insulin/blood ; Leptin/blood ; Metabolic Syndrome X/genetics/*physiopathology ; Mice ; Mice, Inbred C57BL ; Motor Activity ; Mutation ; Neuropeptides/genetics/metabolism ; Obesity/genetics/*physiopathology ; Trans-Activators/*genetics/*physiology ; Weight Gain
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  • 11
    Publication Date: 2005-10-01
    Description: Monocular deprivation normally alters ocular dominance in the visual cortex only during a postnatal critical period (20 to 32 days postnatal in mice). We find that mutations in the Nogo-66 receptor (NgR) affect cessation of ocular dominance plasticity. In NgR-/- mice, plasticity during the critical period is normal, but it continues abnormally such that ocular dominance at 45 or 120 days postnatal is subject to the same plasticity as at juvenile ages. Thus, physiological NgR signaling from myelin-derived Nogo, MAG, and OMgp consolidates the neural circuitry established during experience-dependent plasticity. After pathological trauma, similar NgR signaling limits functional recovery and axonal regeneration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856689/" 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/PMC2856689/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGee, Aaron W -- Yang, Yupeng -- Fischer, Quentin S -- Daw, Nigel W -- Strittmatter, Stephen M -- R01 NS039962/NS/NINDS NIH HHS/ -- R01 NS039962-10/NS/NINDS NIH HHS/ -- R01 NS042304/NS/NINDS NIH HHS/ -- R01 NS042304-08/NS/NINDS NIH HHS/ -- R01 NS056485/NS/NINDS NIH HHS/ -- R01 NS056485-04/NS/NINDS NIH HHS/ -- R37 NS033020/NS/NINDS NIH HHS/ -- R37 NS033020-15/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2222-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Yale University School of Medicine, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195464" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chondroitin Sulfate Proteoglycans/metabolism ; Darkness ; Dominance, Ocular/*physiology ; Electrophysiology ; GPI-Linked Proteins ; Gene Targeting ; Mice ; Mice, Inbred C57BL ; Mutation ; Myelin Basic Protein/metabolism ; Myelin Proteins/genetics/metabolism/*physiology ; Myelin Sheath/*physiology ; Myelin-Associated Glycoprotein/metabolism ; Neurites/physiology ; Neuronal Plasticity/*physiology ; Neurons/*physiology ; Photic Stimulation ; Receptors, Cell Surface/genetics/*physiology ; Signal Transduction ; Visual Cortex/cytology/growth & development/*physiology ; gamma-Aminobutyric Acid/physiology
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  • 12
    Publication Date: 2005-02-05
    Description: The gene encoding the Nod2 protein is frequently mutated in Crohn's disease (CD) patients, although the physiological function of Nod2 in the intestine remains elusive. Here we show that protective immunity mediated by Nod2 recognition of bacterial muramyl dipeptide is abolished in Nod2-deficient mice. These animals are susceptible to bacterial infection via the oral route but not through intravenous or peritoneal delivery. Nod2 is required for the expression of a subgroup of intestinal anti-microbial peptides, known as cryptdins. The Nod2 protein is thus a critical regulator of bacterial immunity within the intestine, providing a possible mechanism for Nod2 mutations in CD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobayashi, Koichi S -- Chamaillard, Mathias -- Ogura, Yasunori -- Henegariu, Octavian -- Inohara, Naohiro -- Nunez, Gabriel -- Flavell, Richard A -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692051" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylmuramyl-Alanyl-Isoglutamine/*immunology ; Animals ; *Antibody Formation ; Female ; Gene Expression ; Gene Targeting ; Ileum/*immunology/microbiology ; *Immunity, Innate ; Immunity, Mucosal ; Immunoglobulins/biosynthesis ; Interleukins/biosynthesis ; Intestinal Diseases/immunology/microbiology ; Intestinal Mucosa/immunology/microbiology ; Intracellular Signaling Peptides and Proteins/*physiology ; Ligands ; Lipopolysaccharides/toxicity ; Listeria monocytogenes/growth & development/immunology/isolation & purification ; Listeriosis/*immunology/microbiology ; Liver/microbiology ; Macrophages/immunology ; Male ; Membrane Glycoproteins/physiology ; Mice ; Nod2 Signaling Adaptor Protein ; Oligonucleotide Array Sequence Analysis ; Protein Precursors/biosynthesis/genetics ; Receptors, Cell Surface/physiology ; Serum Albumin/immunology ; Signal Transduction ; Spleen/microbiology ; Toll-Like Receptors ; Tumor Necrosis Factor-alpha/biosynthesis ; alpha-Defensins/*biosynthesis/genetics
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1310-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16123271" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Blood Glucose/analysis ; Female ; Glucuronidase ; Insulin/blood/metabolism ; Insulin Resistance ; Insulin-Like Growth Factor I/metabolism ; Longevity/*genetics ; Male ; Membrane Proteins/blood/*genetics/*physiology ; Mice ; Mutation ; Signal Transduction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
    Publication Date: 2005-07-16
    Description: Leishmania species cause a spectrum of human diseases in tropical and subtropical regions of the world. We have sequenced the 36 chromosomes of the 32.8-megabase haploid genome of Leishmania major (Friedlin strain) and predict 911 RNA genes, 39 pseudogenes, and 8272 protein-coding genes, of which 36% can be ascribed a putative function. These include genes involved in host-pathogen interactions, such as proteolytic enzymes, and extensive machinery for synthesis of complex surface glycoconjugates. The organization of protein-coding genes into long, strand-specific, polycistronic clusters and lack of general transcription factors in the L. major, Trypanosoma brucei, and Trypanosoma cruzi (Tritryp) genomes suggest that the mechanisms regulating RNA polymerase II-directed transcription are distinct from those operating in other eukaryotes, although the trypanosomatids appear capable of chromatin remodeling. Abundant RNA-binding proteins are encoded in the Tritryp genomes, consistent with active posttranscriptional regulation of gene expression.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1470643/" 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/PMC1470643/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivens, Alasdair C -- Peacock, Christopher S -- Worthey, Elizabeth A -- Murphy, Lee -- Aggarwal, Gautam -- Berriman, Matthew -- Sisk, Ellen -- Rajandream, Marie-Adele -- Adlem, Ellen -- Aert, Rita -- Anupama, Atashi -- Apostolou, Zina -- Attipoe, Philip -- Bason, Nathalie -- Bauser, Christopher -- Beck, Alfred -- Beverley, Stephen M -- Bianchettin, Gabriella -- Borzym, Katja -- Bothe, Gordana -- Bruschi, Carlo V -- Collins, Matt -- Cadag, Eithon -- Ciarloni, Laura -- Clayton, Christine -- Coulson, Richard M R -- Cronin, Ann -- Cruz, Angela K -- Davies, Robert M -- De Gaudenzi, Javier -- Dobson, Deborah E -- Duesterhoeft, Andreas -- Fazelina, Gholam -- Fosker, Nigel -- Frasch, Alberto Carlos -- Fraser, Audrey -- Fuchs, Monika -- Gabel, Claudia -- Goble, Arlette -- Goffeau, Andre -- Harris, David -- Hertz-Fowler, Christiane -- Hilbert, Helmut -- Horn, David -- Huang, Yiting -- Klages, Sven -- Knights, Andrew -- Kube, Michael -- Larke, Natasha -- Litvin, Lyudmila -- Lord, Angela -- Louie, Tin -- Marra, Marco -- Masuy, David -- Matthews, Keith -- Michaeli, Shulamit -- Mottram, Jeremy C -- Muller-Auer, Silke -- Munden, Heather -- Nelson, Siri -- Norbertczak, Halina -- Oliver, Karen -- O'neil, Susan -- Pentony, Martin -- Pohl, Thomas M -- Price, Claire -- Purnelle, Benedicte -- Quail, Michael A -- Rabbinowitsch, Ester -- Reinhardt, Richard -- Rieger, Michael -- Rinta, Joel -- Robben, Johan -- Robertson, Laura -- Ruiz, Jeronimo C -- Rutter, Simon -- Saunders, David -- Schafer, Melanie -- Schein, Jacquie -- Schwartz, David C -- Seeger, Kathy -- Seyler, Amber -- Sharp, Sarah -- Shin, Heesun -- Sivam, Dhileep -- Squares, Rob -- Squares, Steve -- Tosato, Valentina -- Vogt, Christy -- Volckaert, Guido -- Wambutt, Rolf -- Warren, Tim -- Wedler, Holger -- Woodward, John -- Zhou, Shiguo -- Zimmermann, Wolfgang -- Smith, Deborah F -- Blackwell, Jenefer M -- Stuart, Kenneth D -- Barrell, Bart -- Myler, Peter J -- R01 AI040599/AI/NIAID NIH HHS/ -- R01 AI053667/AI/NIAID NIH HHS/ -- U01 AI040599/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):436-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire CB10 1SA, UK. alicat@sanger.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020728" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/genetics/metabolism ; Gene Expression Regulation ; Genes, Protozoan ; Genes, rRNA ; *Genome, Protozoan ; Glycoconjugates/biosynthesis/metabolism ; Leishmania major/chemistry/*genetics/metabolism ; Leishmaniasis, Cutaneous/parasitology ; Lipid Metabolism ; Membrane Proteins/biosynthesis/chemistry/genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Protein Biosynthesis ; Protein Processing, Post-Translational ; Protozoan Proteins/biosynthesis/chemistry/genetics/metabolism ; RNA Processing, Post-Transcriptional ; RNA Splicing ; RNA, Protozoan/genetics/metabolism ; *Sequence Analysis, DNA ; Transcription, Genetic
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  • 15
    Publication Date: 2005-09-17
    Description: The activation dynamics of the transcription factor NF-kappaB exhibit damped oscillatory behavior when cells are stimulated by tumor necrosis factor-alpha (TNFalpha) but stable behavior when stimulated by lipopolysaccharide (LPS). LPS binding to Toll-like receptor 4 (TLR4) causes activation of NF-kappaB that requires two downstream pathways, each of which when isolated exhibits damped oscillatory behavior. Computational modeling of the two TLR4-dependent signaling pathways suggests that one pathway requires a time delay to establish early anti-phase activation of NF-kappaB by the two pathways. The MyD88-independent pathway required Inferon regulatory factor 3-dependent expression of TNFalpha to activate NF-kappaB, and the time required for TNFalpha synthesis established the delay.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Covert, Markus W -- Leung, Thomas H -- Gaston, Jahlionais E -- Baltimore, David -- GM039458-21/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1854-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166516" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Vesicular Transport/deficiency/physiology ; Animals ; Antigens, Differentiation/physiology ; Cell Line ; Cells, Cultured ; Computer Simulation ; Cycloheximide/pharmacology ; DNA-Binding Proteins/genetics/physiology ; Gene Expression Profiling ; Gene Expression Regulation ; I-kappa B Kinase ; I-kappa B Proteins/biosynthesis/genetics/metabolism ; Interferon Regulatory Factor-3 ; Kinetics ; Lipopolysaccharides/*immunology/metabolism ; Mice ; Models, Biological ; Myeloid Differentiation Factor 88 ; NF-kappa B/*metabolism ; Oligonucleotide Array Sequence Analysis ; Protein Synthesis Inhibitors/pharmacology ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Immunologic/deficiency/metabolism/physiology ; Signal Transduction ; Time Factors ; Toll-Like Receptor 4 ; Transcription Factors/genetics/physiology ; Tumor Necrosis Factor-alpha/biosynthesis/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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  • 16
    Publication Date: 2005-07-16
    Description: Mutations in mitochondrial DNA (mtDNA) accumulate in tissues of mammalian species and have been hypothesized to contribute to aging. We show that mice expressing a proofreading-deficient version of the mitochondrial DNA polymerase g (POLG) accumulate mtDNA mutations and display features of accelerated aging. Accumulation of mtDNA mutations was not associated with increased markers of oxidative stress or a defect in cellular proliferation, but was correlated with the induction of apoptotic markers, particularly in tissues characterized by rapid cellular turnover. The levels of apoptotic markers were also found to increase during aging in normal mice. Thus, accumulation of mtDNA mutations that promote apoptosis may be a central mechanism driving mammalian aging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kujoth, G C -- Hiona, A -- Pugh, T D -- Someya, S -- Panzer, K -- Wohlgemuth, S E -- Hofer, T -- Seo, A Y -- Sullivan, R -- Jobling, W A -- Morrow, J D -- Van Remmen, H -- Sedivy, J M -- Yamasoba, T -- Tanokura, M -- Weindruch, R -- Leeuwenburgh, C -- Prolla, T A -- AG021905/AG/NIA NIH HHS/ -- AG16694/AG/NIA NIH HHS/ -- AG17994/AG/NIA NIH HHS/ -- AG18922/AG/NIA NIH HHS/ -- AG21042/AG/NIA NIH HHS/ -- DK48831/DK/NIDDK NIH HHS/ -- RR00095/RR/NCRR NIH HHS/ -- T32 AG00213/AG/NIA NIH HHS/ -- T32 GM07601/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):481-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Genetics and Medical Genetics, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020738" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Amino Acid Substitution ; Animals ; *Apoptosis ; Caspase 3 ; Caspases/metabolism ; Cloning, Molecular ; DNA Damage ; DNA Fragmentation ; DNA, Mitochondrial/*genetics ; DNA-Directed DNA Polymerase/genetics ; Gene Targeting ; Humans ; Hydrogen Peroxide/metabolism ; Lipid Peroxidation ; Liver/metabolism ; Mice ; Mitochondria, Heart/metabolism ; Mitochondria, Liver/metabolism ; Muscle, Skeletal/metabolism ; *Mutation ; Myocardium/metabolism ; *Oxidative Stress ; Phenotype ; Presbycusis/etiology ; Reactive Oxygen Species/metabolism
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  • 17
    Publication Date: 2005-08-27
    Description: CD4+ regulatory T (Treg) cells have a profound ability to suppress host immune responses, yet little is understood about how these cells are regulated. We describe a mechanism linking Toll-like receptor (TLR) 8 signaling to the control of Treg cell function, in which synthetic and natural ligands for human TLR8 can reverse Treg cell function. This effect was independent of dendritic cells but required functional TLR8-MyD88-IRAK4 signaling in Treg cells. Adoptive transfer of TLR8 ligand-stimulated Treg cells into tumor-bearing mice enhanced anti-tumor immunity. These results suggest that TLR8 signaling could play a critical role in controlling immune responses to cancer and other diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peng, Guangyong -- Guo, Zhong -- Kiniwa, Yukiko -- Voo, Kui Shin -- Peng, Weiyi -- Fu, Tihui -- Wang, Daniel Y -- Li, Yanchun -- Wang, Helen Y -- Wang, Rong-Fu -- P01CA94237/CA/NCI NIH HHS/ -- P50 CA093459/CA/NCI NIH HHS/ -- P50CA58204/CA/NCI NIH HHS/ -- R01CA101795/CA/NCI NIH HHS/ -- R01CA90327/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1380-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cell and Gene Therapy and Department of Immunology, 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/16123302" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Adoptive Transfer ; Animals ; Antigens, Differentiation/genetics/physiology ; CD4-Positive T-Lymphocytes/*immunology ; Cell Line ; Cell Line, Tumor ; Humans ; Immune Tolerance ; Interleukin-1 Receptor-Associated Kinases ; Killer Cells, Natural/immunology ; Ligands ; Lymphocyte Activation ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Myeloid Differentiation Factor 88 ; Neoplasm Transplantation ; Neoplasms, Experimental/immunology/pathology ; Oligodeoxyribonucleotides/immunology ; Phosphotransferases (Alcohol Group Acceptor)/genetics/physiology ; Poly G/immunology ; RNA Interference ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Immunologic/genetics/physiology ; *Signal Transduction ; T-Lymphocyte Subsets/*immunology ; Toll-Like Receptor 8 ; Toll-Like Receptors
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  • 18
    Publication Date: 2005-02-12
    Description: Most protein phosphatases have little intrinsic substrate specificity, making selective pharmacological inhibition of specific dephosphorylation reactions a challenging problem. In a screen for small molecules that protect cells from endoplasmic reticulum (ER) stress, we identified salubrinal, a selective inhibitor of cellular complexes that dephosphorylate eukaryotic translation initiation factor 2 subunit alpha (eIF2alpha). Salubrinal also blocks eIF2alpha dephosphorylation mediated by a herpes simplex virus protein and inhibits viral replication. These results suggest that selective chemical inhibitors of eIF2alpha dephosphorylation may be useful in diseases involving ER stress or viral infection. More broadly, salubrinal demonstrates the feasibility of selective pharmacological targeting of cellular dephosphorylation events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boyce, Michael -- Bryant, Kevin F -- Jousse, Celine -- Long, Kai -- Harding, Heather P -- Scheuner, Donalyn -- Kaufman, Randal J -- Ma, Dawei -- Coen, Donald M -- Ron, David -- Yuan, Junying -- AI19838/AI/NIAID NIH HHS/ -- AI26077/AI/NIAID NIH HHS/ -- DDK42394/DK/NIDDK NIH HHS/ -- DK47119/DK/NIDDK NIH HHS/ -- ES08681/ES/NIEHS NIH HHS/ -- GM64703/GM/NIGMS NIH HHS/ -- NS35138/NS/NINDS NIH HHS/ -- R37-AG012859/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 11;307(5711):935-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15705855" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Differentiation ; Apoptosis/*drug effects ; Cell Cycle Proteins ; Cell Line ; Cinnamates/*pharmacology/toxicity ; *Cytoprotection ; Dose-Response Relationship, Drug ; Endoplasmic Reticulum/*metabolism ; Enzyme Inhibitors/pharmacology ; Eukaryotic Initiation Factor-2/*metabolism ; Genes, Reporter ; Herpesvirus 1, Human/drug effects/physiology ; Keratitis, Herpetic/drug therapy/virology ; Male ; Mice ; Oxazoles/pharmacology/toxicity ; PC12 Cells ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Folding ; Protein Kinases/metabolism ; Protein Phosphatase 1 ; Proteins/metabolism ; Rats ; Thiourea/*analogs & derivatives/*pharmacology/toxicity ; Tunicamycin/pharmacology ; Viral Proteins/metabolism ; Virus Replication/drug effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
    Publication Date: 2005-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1761.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357241" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axin Protein ; Body Patterning/drug effects/genetics ; *DNA Methylation ; DNA Transposable Elements ; *Dietary Supplements ; Embryonic Development/drug effects/*genetics ; *Epigenesis, Genetic ; Female ; Folic Acid/*administration & dosage/pharmacology ; Gene Expression Regulation, Developmental/*drug effects ; Mice ; Pregnancy ; Repressor Proteins/genetics ; Tail/embryology ; Vitamin B Complex/*administration & dosage/pharmacology
    Print ISSN: 0036-8075
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  • 20
    Publication Date: 2005-08-20
    Description: The SAR11 clade consists of very small, heterotrophic marine alpha-proteobacteria that are found throughout the oceans, where they account for about 25% of all microbial cells. Pelagibacter ubique, the first cultured member of this clade, has the smallest genome and encodes the smallest number of predicted open reading frames known for a free-living microorganism. In contrast to parasitic bacteria and archaea with small genomes, P. ubique has complete biosynthetic pathways for all 20 amino acids and all but a few cofactors. P. ubique has no pseudogenes, introns, transposons, extrachromosomal elements, or inteins; few paralogs; and the shortest intergenic spacers yet observed for any cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giovannoni, Stephen J -- Tripp, H James -- Givan, Scott -- Podar, Mircea -- Vergin, Kevin L -- Baptista, Damon -- Bibbs, Lisa -- Eads, Jonathan -- Richardson, Toby H -- Noordewier, Michiel -- Rappe, Michael S -- Short, Jay M -- Carrington, James C -- Mathur, Eric J -- New York, N.Y. -- Science. 2005 Aug 19;309(5738):1242-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Oregon State University, Corvallis, OR 97331, USA. steve.giovannoni@oregonstate.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16109880" target="_blank"〉PubMed〈/a〉
    Keywords: Alphaproteobacteria/classification/*genetics/isolation & purification/physiology ; Bacterial Proteins/genetics/metabolism ; Base Composition ; Biological Evolution ; Carbon/metabolism ; Computational Biology ; DNA, Bacterial/chemistry/genetics ; DNA, Intergenic ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; *Genome, Bacterial ; Membrane Transport Proteins/genetics/metabolism ; Molecular Sequence Data ; Oceans and Seas ; Phosphates/metabolism ; Phylogeny ; Seawater/*microbiology ; Selection, Genetic ; Sigma Factor/genetics ; Thymidylate Synthase/genetics
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-10-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):602.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16254156" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Proliferation/*drug effects ; Ciliary Neurotrophic Factor/*pharmacology ; Humans ; Hypothalamus/cytology/*drug effects ; Mice ; Neurons/cytology/*drug effects ; Weight Loss/*drug effects
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  • 22
    Publication Date: 2005-05-21
    Description: Gene marking with replication-defective retroviral vectors has been used for more than 20 years to track the in vivo fate of cell clones. We demonstrate that retroviral integrations themselves may trigger nonmalignant clonal expansion in murine long-term hematopoiesis. All 29 insertions recovered from clones dominating in serially transplanted recipients affected loci with an established or potential role in the self-renewal or survival of hematopoietic stem cells. Transcriptional dysregulation occurred in all 12 insertion sites analyzed. These findings have major implications for diagnostic gene marking and the discovery of genes regulating stem cell turnover.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kustikova, Olga -- Fehse, Boris -- Modlich, Ute -- Yang, Min -- Dullmann, Jochen -- Kamino, Kenji -- von Neuhoff, Nils -- Schlegelberger, Brigitte -- Li, Zhixiong -- Baum, Christopher -- New York, N.Y. -- Science. 2005 May 20;308(5725):1171-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bone Marrow Transplantation, University Hospital Eppendorf, Martinistrasse 52, 20251 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905401" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD34/genetics ; Bone Marrow Transplantation ; DNA-Binding Proteins/genetics ; Down-Regulation ; *Genetic Vectors ; *Hematopoiesis ; *Hematopoietic Stem Cell Transplantation ; Hematopoietic Stem Cells/*physiology ; Humans ; Ligase Chain Reaction ; Mice ; Mice, Inbred C57BL ; *Mutagenesis, Insertional ; Polymerase Chain Reaction ; Proto-Oncogenes/genetics ; Retroviridae/*genetics ; Transcription Factors/genetics ; Transcription, Genetic ; Transgenes ; Up-Regulation ; *Virus Integration
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  • 23
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-10-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):416-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/cytology ; *Cell Line ; Embryo Implantation ; Embryo Research/economics/*ethics ; Embryo, Mammalian/*cytology ; Female ; Financing, Government ; Humans ; Mice ; Nuclear Transfer Techniques ; *Pluripotent Stem Cells ; Research Support as Topic ; *Stem Cells ; United States
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  • 24
    Publication Date: 2005-11-19
    Description: The disrupted in schizophrenia 1 (DISC1) gene is a candidate susceptibility factor for schizophrenia, but its mechanistic role in the disorder is unknown. Here we report that the gene encoding phosphodiesterase 4B (PDE4B) is disrupted by a balanced translocation in a subject diagnosed with schizophrenia and a relative with chronic psychiatric illness. The PDEs inactivate adenosine 3',5'-monophosphate (cAMP), a second messenger implicated in learning, memory, and mood. We show that DISC1 interacts with the UCR2 domain of PDE4B and that elevation of cellular cAMP leads to dissociation of PDE4B from DISC1 and an increase in PDE4B activity. We propose a mechanistic model whereby DISC1 sequesters PDE4B in resting cells and releases it in an activated state in response to elevated cAMP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Millar, J Kirsty -- Pickard, Benjamin S -- Mackie, Shaun -- James, Rachel -- Christie, Sheila -- Buchanan, Sebastienne R -- Malloy, M Pat -- Chubb, Jennifer E -- Huston, Elaine -- Baillie, George S -- Thomson, Pippa A -- Hill, Elaine V -- Brandon, Nicholas J -- Rain, Jean-Christophe -- Camargo, L Miguel -- Whiting, Paul J -- Houslay, Miles D -- Blackwood, Douglas H R -- Muir, Walter J -- Porteous, David J -- G8604010/Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1187-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Genetics Section, Molecular Medicine Centre, University of Edinburgh, Edinburgh EH4 2XU, UK. Kirsty.Millar@ed.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293762" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/*genetics/metabolism ; Adult ; Affective Disorders, Psychotic/genetics/metabolism ; Animals ; Cadherins/genetics ; Cell Line ; Chromosomes, Human, Pair 1 ; Chromosomes, Human, Pair 16 ; Cyclic AMP/*metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Enzyme Activation ; Genetic Predisposition to Disease ; Humans ; Male ; Nerve Tissue Proteins/*genetics/metabolism ; Protein Binding ; Rats ; Schizophrenia/enzymology/*genetics/metabolism ; *Signal Transduction ; Translocation, Genetic
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  • 25
    Publication Date: 2005-12-17
    Description: Lighter variations of pigmentation in humans are associated with diminished number, size, and density of melanosomes, the pigmented organelles of melanocytes. Here we show that zebrafish golden mutants share these melanosomal changes and that golden encodes a putative cation exchanger slc24a5 (nckx5) that localizes to an intracellular membrane, likely the melanosome or its precursor. The human ortholog is highly similar in sequence and functional in zebrafish. The evolutionarily conserved ancestral allele of a human coding polymorphism predominates in African and East Asian populations. In contrast, the variant allele is nearly fixed in European populations, is associated with a substantial reduction in regional heterozygosity, and correlates with lighter skin pigmentation in admixed populations, suggesting a key role for the SLC24A5 gene in human pigmentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lamason, Rebecca L -- Mohideen, Manzoor-Ali P K -- Mest, Jason R -- Wong, Andrew C -- Norton, Heather L -- Aros, Michele C -- Jurynec, Michael J -- Mao, Xianyun -- Humphreville, Vanessa R -- Humbert, Jasper E -- Sinha, Soniya -- Moore, Jessica L -- Jagadeeswaran, Pudur -- Zhao, Wei -- Ning, Gang -- Makalowska, Izabela -- McKeigue, Paul M -- O'donnell, David -- Kittles, Rick -- Parra, Esteban J -- Mangini, Nancy J -- Grunwald, David J -- Shriver, Mark D -- Canfield, Victor A -- Cheng, Keith C -- CA73935/CA/NCI NIH HHS/ -- EY11308/EY/NEI NIH HHS/ -- HD37572/HD/NICHD NIH HHS/ -- HD40179/HD/NICHD NIH HHS/ -- HG002154/HG/NHGRI NIH HHS/ -- HL077910/HL/NHLBI NIH HHS/ -- RR017441/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jake Gittlen Cancer Research Foundation, Department of Pathology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357253" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/genetics ; African Continental Ancestry Group/genetics ; Alanine/genetics ; Alleles ; Amino Acid Sequence ; Animals ; Antiporters/chemistry/*genetics/physiology ; Asian Continental Ancestry Group/genetics ; Biological Evolution ; Calcium/metabolism ; European Continental Ancestry Group/genetics ; Gene Frequency ; Genes ; Genetic Variation ; Haplotypes ; Heterozygote ; Humans ; Ion Transport ; Melanins/analysis ; Melanosomes/chemistry/ultrastructure ; Mice ; Molecular Sequence Data ; Multifactorial Inheritance ; Mutation ; Pigment Epithelium of Eye/chemistry/ultrastructure ; Polymorphism, Single Nucleotide ; Selection, Genetic ; Skin Pigmentation/*genetics ; Threonine/genetics ; Zebrafish/embryology/*genetics/metabolism ; Zebrafish Proteins/chemistry/*genetics/physiology
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-10-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):28-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210501" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Animals ; Bioterrorism ; Chick Embryo/virology ; Containment of Biohazards ; Disease Outbreaks/history ; Editorial Policies ; *Genes, Viral ; Genome, Viral ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/*metabolism ; History, 20th Century ; Humans ; Influenza A virus/*genetics/*pathogenicity/physiology ; Influenza, Human/epidemiology/history/*virology ; Mice ; Neuraminidase/genetics/metabolism ; Publishing ; RNA Replicase/genetics/metabolism ; United States ; Virulence ; Virus Replication
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  • 27
    Publication Date: 2005-12-17
    Description: Electrical synapses are common between inhibitory neurons in the mammalian thalamus and neocortex. Synaptic modulation, which allows flexibility of communication between neurons, has been studied extensively at chemical synapses, but modulation of electrical synapses in the mammalian brain has barely been examined. We found that the activation of metabotropic glutamate receptors, via endogenous neurotransmitter or by agonist, causes long-term reduction of electrical synapse strength between the inhibitory neurons of the rat thalamic reticular nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landisman, Carole E -- Connors, Barry W -- NS050434/NS/NINDS NIH HHS/ -- NS25983/NS/NINDS NIH HHS/ -- NS40528/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1809-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Division of Biology and Medicine, Brown University, Providence, RI 02912, USA. Carole_Landisman@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357260" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Cycloleucine/analogs & derivatives/pharmacology ; Electric Conductivity ; Electric Stimulation ; Excitatory Postsynaptic Potentials ; Gap Junctions/*physiology ; Glycine/analogs & derivatives/pharmacology ; In Vitro Techniques ; Intralaminar Thalamic Nuclei/cytology/*physiology ; Membrane Potentials ; Neocortex/physiology ; Neurons/*physiology ; Neurotransmitter Agents/pharmacology ; Patch-Clamp Techniques ; Rats ; Rats, Sprague-Dawley ; Receptors, Metabotropic Glutamate/agonists/antagonists & inhibitors/*physiology ; Synapses/physiology
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):194.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15653478" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Birds/anatomy & histology/*embryology/metabolism ; Chick Embryo ; Dinosaurs/*anatomy & histology ; Forelimb/*anatomy & histology ; Homeodomain Proteins/metabolism ; Mice ; Transcription Factors/metabolism ; Wings, Animal/anatomy & histology/*embryology/metabolism
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  • 29
    Publication Date: 2005-04-30
    Description: The clock proteins PERIOD1 (PER1) and PERIOD2 (PER2) play essential roles in a negative transcriptional feedback loop that generates circadian rhythms in mammalian cells. We identified two PER1-associated factors, NONO and WDR5, that modulate PER activity. The reduction of NONO expression by RNA interference (RNAi) attenuated circadian rhythms in mammalian cells, and fruit flies carrying a hypomorphic allele were nearly arrhythmic. WDR5, a subunit of histone methyltransferase complexes, augmented PER-mediated transcriptional repression, and its reduction by RNAi diminished circadian histone methylations at the promoter of a clock gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, Steven A -- Ripperger, Juergen -- Kadener, Sebastian -- Fleury-Olela, Fabienne -- Vilbois, Francis -- Rosbash, Michael -- Schibler, Ueli -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):693-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and National Centres of Competence in Research (NCCR) Frontiers in Genetics, Sciences III, University of Geneva, 30 Quai Ernest Ansermet, CH-1211 Geneva-4, Switzerland. steven.brown@molbio.unige.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860628" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Carrier Proteins/genetics/*metabolism ; Cell Cycle Proteins ; Cell Line ; *Circadian Rhythm ; DNA-Binding Proteins/genetics/metabolism ; Drosophila/genetics/physiology ; Drosophila Proteins/genetics/physiology ; Female ; Gene Expression Regulation ; Histones/metabolism ; Immunoprecipitation ; Male ; Methylation ; Mice ; Mice, Inbred BALB C ; Nuclear Proteins/genetics/*metabolism/physiology ; Nuclear Receptor Subfamily 1, Group D, Member 1 ; Period Circadian Proteins ; Promoter Regions, Genetic ; Proteins/genetics/*metabolism ; RNA Interference ; Rats ; Receptors, Cytoplasmic and Nuclear/genetics/metabolism ; Transcription Factors ; Transcription, Genetic ; Transfection
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  • 30
    Publication Date: 2005-01-18
    Description: Amyloid fibrils commonly exhibit multiple distinct morphologies in electron microscope and atomic force microscope images, often within a single image field. By using electron microscopy and solid-state nuclear magnetic resonance measurements on fibrils formed by the 40-residue beta-amyloid peptide of Alzheimer's disease (Abeta(1-40)), we show that different fibril morphologies have different underlying molecular structures, that the predominant structure can be controlled by subtle variations in fibril growth conditions, and that both morphology and molecular structure are self-propagating when fibrils grow from preformed seeds. Different Abeta(1-40) fibril morphologies also have significantly different toxicities in neuronal cell cultures. These results have implications for the mechanism of amyloid formation, the phenomenon of strains in prion diseases, the role of amyloid fibrils in amyloid diseases, and the development of amyloid-based nano-materials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petkova, Aneta T -- Leapman, Richard D -- Guo, Zhihong -- Yau, Wai-Ming -- Mattson, Mark P -- Tycko, Robert -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):262-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health (NIH), Bethesda, MD 20892-0520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15653506" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amyloid beta-Peptides/*chemistry/toxicity/*ultrastructure ; Animals ; Cells, Cultured ; Chemistry, Physical ; Hippocampus/cytology ; Humans ; Hydrogen Bonding ; Microscopy, Atomic Force ; Microscopy, Electron, Transmission ; Molecular Structure ; Neurons/cytology/drug effects ; Nuclear Magnetic Resonance, Biomolecular ; Peptide Fragments/*chemistry/toxicity/*ultrastructure ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Secondary ; Rats
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  • 31
    Publication Date: 2005-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Timothy M -- Cleveland, Don W -- R37 NS027036/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):361-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research and the Department of Medicine and Neurosciences, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15661995" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*drug therapy ; Animals ; Anti-Bacterial Agents/pharmacology/*therapeutic use ; Brain/metabolism ; Ceftriaxone/pharmacology/*therapeutic use ; Clinical Trials as Topic ; Drug Evaluation, Preclinical ; Excitatory Amino Acid Transporter 2/genetics/metabolism ; Glutamic Acid/metabolism ; Humans ; Mice ; Motor Neurons/physiology ; Neurodegenerative Diseases/*drug therapy ; Spinal Cord/metabolism ; Synapses/physiology ; Synaptic Transmission ; beta-Lactams/pharmacology/*therapeutic use
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  • 32
    Publication Date: 2005-02-12
    Description: The microenvironments of the thymus are generated by thymic epithelial cells (TECs) and are essential for inducing immune self-tolerance or developing T cells. However, the molecular mechanisms that underlie the differentiation of TECs and thymic compartmentalization are not fully understood. Here we show that deficiency in the tumor necrosis factor receptor-associated factor (TRAF) 6 results in disorganized distribution of medullary TECs (mTECs) and the absence of mature mTECs. Engraftment of thymic stroma of TRAF6(-/-) embryos into athymic nude mice induced autoimmunity. Thus, TRAF6 directs the development of thymic stroma and represents a critical point of regulation for self-tolerance and autoimmunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akiyama, Taishin -- Maeda, Shiori -- Yamane, Sayaka -- Ogino, Kaori -- Kasai, Michiyuki -- Kajiura, Fumiko -- Matsumoto, Mitsuru -- Inoue, Jun-ichiro -- New York, N.Y. -- Science. 2005 Apr 8;308(5719):248-51. Epub 2005 Feb 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular and Molecular Biology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15705807" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoimmunity ; Cell Line ; Epithelial Cells/immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Nude ; Organ Culture Techniques ; Proto-Oncogene Proteins/physiology ; *Self Tolerance ; T-Lymphocytes/immunology ; TNF Receptor-Associated Factor 6/immunology/*physiology ; Thymus Gland/cytology/embryology/*immunology ; Transcription Factor RelB ; Transcription Factors/physiology
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  • 33
    Publication Date: 2005-12-03
    Description: Proper chromosome segregation requires the attachment of sister kinetochores to microtubules from opposite spindle poles to form bi-oriented chromosomes on the metaphase spindle. The chromosome passenger complex containing Survivin and the kinase Aurora B regulates this process from the centromeres. We report that a de-ubiquitinating enzyme, hFAM, regulates chromosome alignment and segregation by controlling both the dynamic association of Survivin with centromeres and the proper targeting of Survivin and Aurora B to centromeres. Survivin is ubiquitinated in mitosis through both Lys(48) and Lys(63) ubiquitin linkages. Lys(63) de-ubiquitination mediated by hFAM is required for the dissociation of Survivin from centromeres, whereas Lys(63) ubiquitination mediated by the ubiquitin binding protein Ufd1 is required for the association of Survivin with centromeres. Thus, ubiquitinaton regulates dynamic protein-protein interactions and chromosome segregation independently of protein degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vong, Queenie P -- Cao, Kan -- Li, Hoi Y -- Iglesias, Pablo A -- Zheng, Yixian -- GM56312/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1499-504.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Embryology, Carnegie Institution of Washington and Howard Hughes Medical Institute, 3520 San Martin Drive, Baltimore, MD 21218, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322459" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aurora Kinase B ; Aurora Kinases ; Centromere/*metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation/*physiology ; Egg Proteins/metabolism ; Endopeptidases/metabolism ; HeLa Cells ; Humans ; Inhibitor of Apoptosis Proteins ; Lysine/metabolism ; Microtubule-Associated Proteins/metabolism ; Molecular Sequence Data ; Neoplasm Proteins/metabolism ; Protein Binding ; Protein-Serine-Threonine Kinases/metabolism ; Ubiquitin/*metabolism ; Ubiquitin Thiolesterase ; Xenopus ; Xenopus Proteins/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buzsaki, Gyorgy -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):568-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular and Behavioral Neuroscience, Rutgers University, Newark, NJ 07102, USA. buzsaki@axon.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16040697" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Mapping ; Cues ; Electrophysiology ; Hippocampus/cytology/*physiology ; Interneurons/physiology ; Memory/*physiology ; Nerve Net/*physiology ; Neural Inhibition ; Neurons/*physiology ; Orientation/*physiology ; Perception/physiology ; Pyramidal Cells/*physiology ; Rats ; Space Perception/*physiology
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1544-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761128" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Animals ; *Clinical Trials as Topic ; Genetic Diseases, X-Linked/*therapy ; *Genetic Therapy/adverse effects ; Genetic Vectors ; Haplorhini ; Humans ; Infant ; Leukemia, T-Cell/etiology ; Mice ; Oncogenes ; Retroviridae/genetics ; Severe Combined Immunodeficiency/*therapy ; United States
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  • 36
    Publication Date: 2005-11-15
    Description: The ancestry of modern Europeans is a subject of debate among geneticists, archaeologists, and anthropologists. A crucial question is the extent to which Europeans are descended from the first European farmers in the Neolithic Age 7500 years ago or from Paleolithic hunter-gatherers who were present in Europe since 40,000 years ago. Here we present an analysis of ancient DNA from early European farmers. We successfully extracted and sequenced intact stretches of maternally inherited mitochondrial DNA (mtDNA) from 24 out of 57 Neolithic skeletons from various locations in Germany, Austria, and Hungary. We found that 25% of the Neolithic farmers had one characteristic mtDNA type and that this type formerly was widespread among Neolithic farmers in Central Europe. Europeans today have a 150-times lower frequency (0.2%) of this mtDNA type, revealing that these first Neolithic farmers did not have a strong genetic influence on modern European female lineages. Our finding lends weight to a proposed Paleolithic ancestry for modern Europeans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haak, Wolfgang -- Forster, Peter -- Bramanti, Barbara -- Matsumura, Shuichi -- Brandt, Guido -- Tanzer, Marc -- Villems, Richard -- Renfrew, Colin -- Gronenborn, Detlef -- Alt, Kurt Werner -- Burger, Joachim -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):1016-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Anthropologie, Johannes Gutenberg Universitat Mainz, Saarstrasse 21, D-55099 Mainz, Germany. haakw@uni-mainz.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284177" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture/*history ; Austria ; Base Sequence ; Computer Simulation ; Cultural Evolution ; DNA, Mitochondrial/chemistry/classification/*genetics/history ; Emigration and Immigration ; Europe ; European Continental Ancestry Group/*genetics/history ; Female ; Gene Frequency ; Genetic Drift ; Genetics, Population ; Germany ; Haplotypes ; History, Ancient ; Humans ; Hungary ; Male ; Molecular Sequence Data ; Population Dynamics
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  • 37
    Publication Date: 2005-02-26
    Description: Apical membrane antigen 1 from Plasmodium is a leading malaria vaccine candidate. The protein is essential for host-cell invasion, but its molecular function is unknown. The crystal structure of the three domains comprising the ectoplasmic region of the antigen from P. vivax, solved at 1.8 angstrom resolution, shows that domains I and II belong to the PAN motif, which defines a superfamily of protein folds implicated in receptor binding. We also mapped the epitope of an invasion-inhibitory monoclonal antibody specific for the P. falciparum ortholog and modeled this to the structure. The location of the epitope and current knowledge on structure-function correlations for PAN domains together suggest a receptor-binding role during invasion in which domain II plays a critical part. These results are likely to aid vaccine and drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizarro, Juan Carlos -- Vulliez-Le Normand, Brigitte -- Chesne-Seck, Marie-Laure -- Collins, Christine R -- Withers-Martinez, Chrislaine -- Hackett, Fiona -- Blackman, Michael J -- Faber, Bart W -- Remarque, Edmond J -- Kocken, Clemens H M -- Thomas, Alan W -- Bentley, Graham A -- MC_U117532063/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):408-11. Epub 2005 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite d'Immunologie Structurale, Centre National de la Recherche Scientifique, URA 2185, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731407" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Protozoan/*chemistry/immunology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Epitope Mapping ; Epitopes ; Heparin/metabolism ; Malaria Vaccines ; Membrane Proteins/*chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Plasmodium falciparum/chemistry/immunology ; Plasmodium vivax/chemistry/*immunology ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protozoan Proteins/*chemistry/immunology ; Recombinant Proteins/chemistry ; Sequence Alignment
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-09-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guzman, Maria G -- New York, N.Y. -- Science. 2005 Sep 2;309(5740):1495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Virology Department, PAHO/WHO Collaborating Center for Viral Diseases, Instituto de Medicina Tropical "Pedro Kouri" Autopista Novia del Mediodia, Km 1/2, Post Office Box Mariano 13, Habana, Cuba. lupe@ipk.sld.cu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16141052" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Cuba/epidemiology ; Dengue/epidemiology/prevention & control/virology ; Dengue Virus/chemistry/immunology ; Humans ; Risk Factors ; Severe Dengue/*epidemiology ; Viral Vaccines
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poucet, Bruno -- Save, Etienne -- New York, N.Y. -- Science. 2005 May 6;308(5723):799-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Neurobiology and Cognition, CNRS-Universite Aix-Marseille, Centre Saint-Charles, 13331 Marseille Cedex 3, France. bpoucet@up.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879197" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Cues ; Environment ; Form Perception ; Hippocampus/*cytology/*physiology ; Learning ; Memory/*physiology ; Orientation ; Pattern Recognition, Visual ; Pyramidal Cells/*physiology ; Rats ; Space Perception
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  • 40
    Publication Date: 2005-06-18
    Description: Rhizobial bacteria enter a symbiotic interaction with legumes, activating diverse responses in roots through the lipochito oligosaccharide signaling molecule Nod factor. Here, we show that NSP2 from Medicago truncatula encodes a GRAS protein essential for Nod-factor signaling. NSP2 functions downstream of Nod-factor-induced calcium spiking and a calcium/calmodulin-dependent protein kinase. We show that NSP2-GFP expressed from a constitutive promoter is localized to the endoplasmic reticulum/nuclear envelope and relocalizes to the nucleus after Nod-factor elicitation. This work provides evidence that a GRAS protein transduces calcium signals in plants and provides a possible regulator of Nod-factor-inducible gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalo, Peter -- Gleason, Cynthia -- Edwards, Anne -- Marsh, John -- Mitra, Raka M -- Hirsch, Sibylle -- Jakab, Julia -- Sims, Sarah -- Long, Sharon R -- Rogers, Jane -- Kiss, Gyorgy B -- Downie, J Allan -- Oldroyd, Giles E D -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1786-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Disease and Stress Biology and Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961668" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Calcium/metabolism ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/metabolism ; Cell Nucleus/metabolism ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; Lipopolysaccharides/*metabolism ; Medicago/genetics/*metabolism/*microbiology ; Molecular Sequence Data ; Mutation ; Oligonucleotide Array Sequence Analysis ; Peas/genetics/metabolism ; Plant Proteins/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Sinorhizobium meliloti/*physiology ; Symbiosis ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic
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  • 41
    Publication Date: 2005-08-20
    Description: The molecular machinery that governs circadian rhythmicity is based on clock proteins organized in regulatory feedback loops. Although posttranslational modification of clock proteins is likely to finely control their circadian functions, only limited information is available to date. Here, we show that BMAL1, an essential transcription factor component of the clock mechanism, is SUMOylated on a highly conserved lysine residue (Lys259) in vivo. BMAL1 shows a circadian pattern of SUMOylation that parallels its activation in the mouse liver. SUMOylation of BMAL1 requires and is induced by CLOCK, the heterodimerization partner of BMAL1. Ectopic expression of a SUMO-deficient BMAL1 demonstrates that SUMOylation plays an important role in BMAL1 circadian expression and clock rhythmicity. This reveals an additional level of regulation within the core mechanism of the circadian clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cardone, Luca -- Hirayama, Jun -- Giordano, Francesca -- Tamaru, Teruya -- Palvimo, Jorma J -- Sassone-Corsi, Paolo -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1390-4. Epub 2005 Aug 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire, 1 rue Laurent Fries, 67404 Illkirch, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16109848" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; CLOCK Proteins ; COS Cells ; Cell Cycle Proteins ; Cell Line ; *Circadian Rhythm ; Dimerization ; Ethylmaleimide/pharmacology ; Gene Expression Regulation ; Liver/metabolism ; Lysine/metabolism ; Mice ; Mutation ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; SUMO-1 Protein/*metabolism ; Trans-Activators/genetics/metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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  • 42
    Publication Date: 2005-07-30
    Description: To study adaptation, it is essential to identify multiple adaptive mutations and to characterize their molecular, phenotypic, selective, and ecological consequences. Here we describe a genomic screen for adaptive insertions of transposable elements in Drosophila. Using a pilot application of this screen, we have identified an adaptive transposable element insertion, which truncates a gene and apparently generates a functional protein in the process. The insertion of this transposable element confers increased resistance to an organophosphate pesticide and has spread in D. melanogaster recently.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aminetzach, Yael T -- Macpherson, J Michael -- Petrov, Dmitri A -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):764-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, 371 Serra Mall, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051794" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Alleles ; Amino Acid Substitution ; Animals ; Azinphosmethyl/pharmacology ; Base Sequence ; Choline/metabolism ; Crosses, Genetic ; *DNA Transposable Elements ; Drosophila/drug effects/genetics/physiology ; Drosophila Proteins/chemistry/*genetics/physiology ; Drosophila melanogaster/drug effects/*genetics/physiology ; *Evolution, Molecular ; Exons ; Female ; Gene Expression ; *Genes, Insect ; Haplotypes ; Insecticide Resistance/*genetics ; Insecticides/pharmacology ; Introns ; Long Interspersed Nucleotide Elements ; Molecular Sequence Data ; Mutation ; Polymorphism, Genetic ; Recombination, Genetic ; Selection, Genetic
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  • 43
    Publication Date: 2005-09-24
    Description: Mammalian tooth crowns have precise functional requirements but cannot be substantially remodeled after eruption. In developing teeth, epithelial signaling centers, the enamel knots, form at future cusp positions and are the first signs of cusp patterns that distinguish species. We report that ectodin, a secreted bone morphogenetic protein (BMP) inhibitor, is expressed as a "negative" image of mouse enamel knots. Furthermore, we show that ectodin-deficient mice have enlarged enamel knots, highly altered cusp patterns, and extra teeth. Unlike in normal teeth, excess BMP accelerates patterning in ectodin-deficient teeth. We propose that ectodin is critical for robust spatial delineation of enamel knots and cusps.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kassai, Yoshiaki -- Munne, Pauliina -- Hotta, Yuhei -- Penttila, Enni -- Kavanagh, Kathryn -- Ohbayashi, Norihiko -- Takada, Shinji -- Thesleff, Irma -- Jernvall, Jukka -- Itoh, Nobuyuki -- New York, N.Y. -- Science. 2005 Sep 23;309(5743):2067-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetic Biochemistry, Kyoto University Graduate School of Pharmaceutical Sciences, Kyoto 606-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16179481" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Bone Morphogenetic Protein 4 ; Bone Morphogenetic ; Proteins/biosynthesis/genetics/metabolism/pharmacology/*physiology ; Cell Cycle Proteins/biosynthesis/genetics/physiology ; Chimera ; Cyclin-Dependent Kinase Inhibitor p21 ; Dental Enamel/embryology ; Gene Expression Regulation, Developmental ; Hedgehog Proteins ; Heterozygote ; Mice ; Mice, Inbred C57BL ; Microscopy, Confocal ; Molar/embryology/metabolism ; Mutation ; *Odontogenesis ; Organ Culture Techniques ; Tooth Crown/*embryology ; Trans-Activators/biosynthesis/genetics
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  • 44
    Publication Date: 2005-10-01
    Description: Chlorinated natural products include vancomycin and cryptophycin A. Their biosynthesis involves regioselective chlorination by flavin-dependent halogenases. We report the structural characterization of tryptophan 7-halogenase (PrnA), which regioselectively chlorinates tryptophan. Tryptophan and flavin adenine dinucleotide (FAD) are separated by a 10 angstrom-long tunnel and bound by distinct enzyme modules. The FAD module is conserved in halogenases and is related to flavin-dependent monooxygenases. On the basis of biochemical studies, crystal structures, and by analogy with monooxygenases, we predict that FADH2 reacts with O2 to make peroxyflavin, which is decomposed by Cl-. The resulting HOCl is guided through the tunnel to tryptophan, where it is activated to participate in electrophilic aromatic substitution.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315827/" 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/PMC3315827/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, Changjiang -- Flecks, Silvana -- Unversucht, Susanne -- Haupt, Caroline -- van Pee, Karl-Heinz -- Naismith, James H -- BB/C000080/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BBS/B/14426/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2216-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Biomolecular Sciences, EaStchem, University of St. Andrews, St. Andrews KY16 9ST, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195462" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Chlorides/*metabolism ; Crystallography, X-Ray ; Dimerization ; Flavin-Adenine Dinucleotide/analogs & derivatives/metabolism ; Hydrogen Bonding ; Hypochlorous Acid/metabolism ; Indoles/metabolism ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/*chemistry/isolation & purification/metabolism ; Oxygen/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pseudomonas fluorescens/*enzymology ; Tryptophan/analogs & derivatives/metabolism
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  • 45
    Publication Date: 2005-09-17
    Description: A small number of mammalian signaling pathways mediate a myriad of distinct physiological responses to diverse cellular stimuli. Temporal control of the signaling module that contains IkappaB kinase (IKK), its substrate inhibitor of NF-kappaB (IkappaB), and the key inflammatory transcription factor NF-kappaB can allow for selective gene activation. We have demonstrated that different inflammatory stimuli induce distinct IKK profiles, and we examined the underlying molecular mechanisms. Although tumor necrosis factor-alpha (TNFalpha)-induced IKK activity was rapidly attenuated by negative feedback, lipopolysaccharide (LPS) signaling and LPS-specific gene expression programs were dependent on a cytokine-mediated positive feedback mechanism. Thus, the distinct biological responses to LPS and TNFalpha depend on signaling pathway-specific mechanisms that regulate the temporal profile of IKK activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Werner, Shannon L -- Barken, Derren -- Hoffmann, Alexander -- GM071573/GM/NIGMS NIH HHS/ -- GM72024/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1857-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Signaling Systems Laboratory, Department of Chemistry and Biochemistry, 9500 Gilman Drive, Mailcode 0375, La Jolla, CA 92093-0375, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166517" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Autocrine Communication ; Cell Line ; Cells, Cultured ; Computer Simulation ; Cytokines/genetics ; Feedback, Physiological ; Gene Expression Profiling ; *Gene Expression Regulation ; I-kappa B Kinase ; I-kappa B Proteins/metabolism ; Lipopolysaccharides/immunology/metabolism/pharmacology ; Mice ; Models, Biological ; NF-kappa B/deficiency/metabolism ; Oligonucleotide Array Sequence Analysis ; Protein-Serine-Threonine Kinases/*metabolism ; Receptors, Immunologic/metabolism ; Signal Transduction ; Toll-Like Receptor 4 ; Transcriptional Activation ; Tumor Necrosis Factor-alpha/deficiency/immunology/metabolism/pharmacology
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  • 46
    Publication Date: 2005-03-19
    Description: The adherence of Candida glabrata to host cells is mediated, at least in part, by the EPA genes, a family of adhesins encoded at subtelomeric loci, where they are subject to transcriptional silencing. We show that normally silent EPA genes are expressed during murine urinary tract infection (UTI) and that the inducing signal is the limitation of nicotinic acid (NA), a precursor of nicotinamide adenine dinucleotide (NAD+). C. glabrata is an NA auxotroph, and NA-induced EPA expression is likely the result of a reduction in NAD+ availability for the NAD+-dependent histone deacetylase Sir2p. The adaptation of C. glabrata to the host, therefore, involves a loss of metabolic capacity and exploitation of the resulting auxotrophy to signal a particular host environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Domergue, Renee -- Castano, Irene -- De Las Penas, Alejandro -- Zupancic, Margaret -- Lockatell, Virginia -- Hebel, J Richard -- Johnson, David -- Cormack, Brendan P -- 2PO1DK49720/DK/NIDDK NIH HHS/ -- R01AI46223/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 May 6;308(5723):866-70. Epub 2005 Mar 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Candida glabrata/*genetics/growth & development/*pathogenicity/physiology ; Candidiasis/*microbiology ; Cell Adhesion ; Culture Media ; Female ; Gene Expression Regulation, Fungal ; *Gene Silencing ; Genes, Fungal ; Histone Deacetylases/genetics/metabolism ; Lectins/*genetics ; Mice ; Mice, Inbred BALB C ; Mice, Inbred CBA ; NAD/metabolism ; Niacin/administration & dosage/*metabolism/pharmacology/urine ; Niacinamide/pharmacology/urine ; Sirtuins/genetics/metabolism ; Transcription, Genetic ; Urinary Bladder/microbiology ; Urinary Tract Infections/*microbiology ; Urine/microbiology ; Urothelium/microbiology ; Virulence
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  • 47
    Publication Date: 2005-03-05
    Description: Unexpected, biologically salient stimuli elicit a short-latency, phasic response in midbrain dopaminergic (DA) neurons. Although this signal is important for reinforcement learning, the information it conveys to forebrain target structures remains uncertain. One way to decode the phasic DA signal would be to determine the perceptual properties of sensory inputs to DA neurons. After local disinhibition of the superior colliculus in anesthetized rats, DA neurons became visually responsive, whereas disinhibition of the visual cortex was ineffective. As the primary source of visual afferents, the limited processing capacities of the colliculus may constrain the visual information content of phasic DA responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dommett, Eleanor -- Coizet, Veronique -- Blaha, Charles D -- Martindale, John -- Lefebvre, Veronique -- Walton, Natalie -- Mayhew, John E W -- Overton, Paul G -- Redgrave, Peter -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1476-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, University of Sheffield, Sheffield, S10 2TP, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746431" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bicuculline/pharmacology ; Dopamine/*metabolism ; Electrochemistry ; Evoked Potentials, Visual ; Habituation, Psychophysiologic ; Neostriatum/physiology ; Neural Inhibition ; Neurons/*physiology ; *Photic Stimulation ; Rats ; *Reaction Time ; Reinforcement (Psychology) ; Reward ; Substantia Nigra/*physiology ; Superior Colliculi/*physiology ; Ventral Tegmental Area/*physiology ; Visual Cortex/physiology ; Visual Pathways/physiology
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  • 48
    Publication Date: 2005-02-26
    Description: Many pathogenic bacteria use a type III secretion nanomachine (an injectisome) to deliver virulence proteins into the cytosol of their eukaryotic host cells. Most injectisomes possess a stiff needlelike structure of a genetically defined length. We found that a minimal needle length was required for efficient functioning of the Yersinia enterocolitica injectisome. This minimal needle length correlated with the length of the major adhesin at the bacterial surface. The needle may be required for triggering type III secretion, and its length may have evolved to match specific structures at the bacterial and host cell surfaces.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mota, Luis Jaime -- Journet, Laure -- Sorg, Isabel -- Agrain, Celine -- Cornelis, Guy R -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1278.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum, Universitat Basel, 4056 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731447" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/*metabolism ; Animals ; Bacterial Outer Membrane Proteins/metabolism ; Bacterial Proteins/chemistry/genetics/metabolism ; Cell Line ; Macrophages/metabolism/microbiology ; Mice ; Plasmids ; Protein-Serine-Threonine Kinases/metabolism ; Virulence ; Virulence Factors/metabolism ; Yersinia enterocolitica/genetics/*metabolism/*pathogenicity
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  • 49
    Publication Date: 2005-06-11
    Description: Repetitive microsatellites mutate at relatively high rates and may contribute to the rapid evolution of species-typical traits. We show that individual alleles of a repetitive polymorphic microsatellite in the 5' region of the prairie vole vasopressin 1a receptor (avpr1a) gene modify gene expression in vitro. In vivo, we observe that this regulatory polymorphism predicts both individual differences in receptor distribution patterns and socio-behavioral traits. These data suggest that individual differences in gene expression patterns may be conferred via polymorphic microsatellites in the cis-regulatory regions of genes and may contribute to normal variation in behavioral traits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammock, Elizabeth A D -- Young, Larry J -- MH56897/MH/NIMH NIH HHS/ -- MH64692/MH/NIMH NIH HHS/ -- MH67397/MH/NIMH NIH HHS/ -- RR00165/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1630-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry and Behavioral Sciences, Center for Behavioral Neuroscience, Yerkes National Primate Research Center, Emory University, Atlanta, GA 30329, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947188" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Anxiety ; Arvicolinae/*genetics/physiology/psychology ; Base Sequence ; *Behavior, Animal ; Brain/metabolism ; *Gene Expression Regulation ; Genes, Reporter ; Genetic Variation ; Genotype ; Grooming ; Male ; *Microsatellite Repeats ; Molecular Sequence Data ; Odors ; Pair Bond ; Paternal Behavior ; Receptors, Vasopressin/*genetics/metabolism ; *Social Behavior
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  • 50
    Publication Date: 2005-03-19
    Description: Recognizing a deficiency of indispensable amino acids (IAAs) for protein synthesis is vital for dietary selection in metazoans, including humans. Cells in the brain's anterior piriform cortex (APC) are sensitive to IAA deficiency, signaling diet rejection and foraging for complementary IAA sources, but the mechanism is unknown. Here we report that the mechanism for recognizing IAA-deficient foods follows the conserved general control (GC) system, wherein uncharged transfer RNA induces phosphorylation of eukaryotic initiation factor 2 (eIF2) via the GC nonderepressing 2 (GCN2) kinase. Thus, a basic mechanism of nutritional stress management functions in mammalian brain to guide food selection for survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hao, Shuzhen -- Sharp, James W -- Ross-Inta, Catherine M -- McDaniel, Brent J -- Anthony, Tracy G -- Wek, Ronald C -- Cavener, Douglas R -- McGrath, Barbara C -- Rudell, John B -- Koehnle, Thomas J -- Gietzen, Dorothy W -- GM49164/GM/NIGMS NIH HHS/ -- NS043231/NS/NINDS NIH HHS/ -- NS33347/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1776-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Veterinary Medicine, Department of Anatomy, Physiology and Cell Biology, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774759" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acids, Essential/*administration & dosage/analysis/*deficiency ; Animals ; Diet ; Eating ; Eukaryotic Initiation Factor-2/*metabolism ; *Food ; Food Preferences ; Leucine/administration & dosage/*analogs & derivatives/pharmacology ; Mice ; Mice, Inbred C57BL ; Olfactory Pathways/*metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases ; RNA, Transfer/*metabolism ; Rats ; Stereoisomerism ; Threonine/administration & dosage ; eIF-2 Kinase/metabolism
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  • 51
    Publication Date: 2005-08-20
    Description: Bacteria have developed mechanisms to communicate and compete with each other for limited environmental resources. We found that certain Escherichia coli, including uropathogenic strains, contained a bacterial growth-inhibition system that uses direct cell-to-cell contact. Inhibition was conditional, dependent upon the growth state of the inhibitory cell and the pili expression state of the target cell. Both a large cell-surface protein designated Contact-dependent inhibitor A (CdiA) and two-partner secretion family member CdiB were required for growth inhibition. The CdiAB system may function to regulate the growth of specific cells within a differentiated bacterial population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aoki, Stephanie K -- Pamma, Rupinderjit -- Hernday, Aaron D -- Bickham, Jessica E -- Braaten, Bruce A -- Low, David A -- AI23348/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 19;309(5738):1245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular, Cellular, and Developmental Biology, University of California-Santa Barbara (UCSB), Santa Barbara, CA 93106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16109881" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Computational Biology ; Contact Inhibition ; Culture Media, Conditioned ; Escherichia coli/genetics/*growth & development/pathogenicity/physiology ; Escherichia coli K12/genetics/*growth & development/physiology ; Escherichia coli Proteins/chemistry/genetics/*physiology ; Fimbriae, Bacterial/metabolism ; Genes, Bacterial ; Genetic Complementation Test ; Genomic Islands ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Virulence
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  • 52
    Publication Date: 2005-09-17
    Description: The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Fang -- Li, Wenhui -- Farzan, Michael -- Harrison, Stephen C -- AI061601/AI/NIAID NIH HHS/ -- CA13202/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1864-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166518" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antibodies, Viral/immunology ; Binding Sites ; Carboxypeptidases/*chemistry/metabolism ; Cell Line ; Crystallography, X-Ray ; Disease Outbreaks ; Epitopes ; Glycosylation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/*chemistry/genetics/immunology/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Peptidyl-Dipeptidase A ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*chemistry/metabolism ; SARS Virus/*chemistry/genetics/physiology ; Severe Acute Respiratory Syndrome/transmission/*virology ; Species Specificity ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/*chemistry/genetics/immunology/*metabolism ; Viral Vaccines ; Viverridae/virology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 53
    Publication Date: 2005-02-01
    Description: Obesity occurs when energy intake exceeds energy expenditure. Humans expend energy through purposeful exercise and through changes in posture and movement that are associated with the routines of daily life [called nonexercise activity thermogenesis (NEAT)]. To examine NEAT's role in obesity, we recruited 10 lean and 10 mildly obese sedentary volunteers and measured their body postures and movements every half-second for 10 days. Obese individuals were seated, on average, 2 hours longer per day than lean individuals. Posture allocation did not change when the obese individuals lost weight or when lean individuals gained weight, suggesting that it is biologically determined. If obese individuals adopted the NEAT-enhanced behaviors of their lean counterparts, they might expend an additional 350 calories (kcal) per day.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levine, James A -- Lanningham-Foster, Lorraine M -- McCrady, Shelly K -- Krizan, Alisa C -- Olson, Leslie R -- Kane, Paul H -- Jensen, Michael D -- Clark, Matthew M -- DK56650/DK/NIDDK NIH HHS/ -- DK63226/DK/NIDDK NIH HHS/ -- DK66270/DK/NIDDK NIH HHS/ -- M01 RR00585/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):584-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrine Research Unit, Mayo Clinic, Rochester, MN 55905, USA. Jim@Mayo.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681386" target="_blank"〉PubMed〈/a〉
    Keywords: Activities of Daily Living ; Adult ; *Body Weight ; Energy Intake ; *Energy Metabolism ; Female ; Humans ; Locomotion ; Male ; Middle Aged ; *Motor Activity ; *Movement ; Obesity/*physiopathology ; Overnutrition ; Pilot Projects ; *Posture ; *Thermogenesis ; Weight Gain ; Weight Loss
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  • 54
    Publication Date: 2005-04-16
    Description: Ebola virus (EboV) causes rapidly fatal hemorrhagic fever in humans and there is currently no effective treatment. We found that the infection of African green monkey kidney (Vero) cells by vesicular stomatitis viruses bearing the EboV glycoprotein (GP) requires the activity of endosomal cysteine proteases. Using selective protease inhibitors and protease-deficient cell lines, we identified an essential role for cathepsin B (CatB) and an accessory role for cathepsin L (CatL) in EboV GP-dependent entry. Biochemical studies demonstrate that CatB and CatL mediate entry by carrying out proteolysis of the EboV GP subunit GP1 and support a multistep mechanism that explains the relative contributions of these enzymes to infection. CatB and CatB/CatL inhibitors diminish the multiplication of infectious EboV-Zaire in cultured cells and may merit investigation as anti-EboV drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandran, Kartik -- Sullivan, Nancy J -- Felbor, Ute -- Whelan, Sean P -- Cunningham, James M -- R01 AI059371/AI/NIAID NIH HHS/ -- R01 AI059371-01A1/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1643-5. Epub 2005 Apr 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15831716" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cathepsin B/antagonists & inhibitors/*metabolism ; Cathepsin L ; Cathepsins/antagonists & inhibitors/*metabolism ; Cell Line ; Cells, Cultured ; Cercopithecus aethiops ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Ebolavirus/metabolism/*physiology ; Endosomes/*metabolism ; Hydrogen-Ion Concentration ; Mice ; Vero Cells ; Vesicular stomatitis Indiana virus/genetics/physiology ; Viral Envelope Proteins/*metabolism ; Virion/physiology
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  • 55
    Publication Date: 2005-10-22
    Description: Blood calcium concentration is maintained within a narrow range despite large variations in dietary input and body demand. The Transient Receptor Potential ion channel TRPV5 has been implicated in this process. We report here that TRPV5 is stimulated by the mammalian hormone klotho. Klotho, a beta-glucuronidase, hydrolyzes extracellular sugar residues on TRPV5, entrapping the channel in the plasma membrane. This maintains durable calcium channel activity and membrane calcium permeability in kidney. Thus, klotho activates a cell surface channel by hydrolysis of its extracellular N-linked oligosaccharides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Q -- Hoefs, S -- van der Kemp, A W -- Topala, C N -- Bindels, R J -- Hoenderop, J G -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):490-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, 6500 HB Nijmegen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239475" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Channels/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cells, Cultured ; Glucuronidase/antagonists & inhibitors/metabolism ; Glycosylation ; Humans ; Hydrolysis ; Kidney/cytology/metabolism ; Membrane Proteins/*metabolism ; Mice ; Mice, Inbred C57BL ; Mutation ; Patch-Clamp Techniques ; Protein Transport ; Rabbits ; Sodium/metabolism ; TRPV Cation Channels/genetics/*metabolism ; Transfection
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  • 56
    Publication Date: 2005-03-26
    Description: Activators of bacterial sigma54-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic electron microscopy (cryo-EM) a 20 angstrom resolution structure of an activator, phage shock protein F [PspF(1-275)], which is bound to an ATP transition state analog in complex with its basal factor, sigma54. By fitting the crystal structure of PspF(1-275) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma54. Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma54.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2756573/" 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/PMC2756573/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rappas, Mathieu -- Schumacher, Jorg -- Beuron, Fabienne -- Niwa, Hajime -- Bordes, Patricia -- Wigneshweraraj, Sivaramesh -- Keetch, Catherine A -- Robinson, Carol V -- Buck, Martin -- Zhang, Xiaodong -- B17129/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1972-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Imperial College London, London, SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790859" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Cryoelectron Microscopy ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/metabolism ; DNA-Directed RNA Polymerases/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; PII Nitrogen Regulatory Proteins ; *Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Polymerase Sigma 54 ; Sigma Factor/chemistry/metabolism ; Trans-Activators/*chemistry/*metabolism ; Transcription Factors/chemistry/metabolism
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  • 57
    Publication Date: 2005-09-06
    Description: Noncoding RNA molecules (ncRNAs) have been implicated in numerous biological processes including transcriptional regulation and the modulation of protein function. Yet, in spite of the apparent abundance of ncRNA, little is known about the biological role of the projected thousands of ncRNA genes present in the human genome. To facilitate functional analysis of these RNAs, we have created an arrayed library of short hairpin RNAs (shRNAs) directed against 512 evolutionarily conserved putative ncRNAs and, via cell-based assays, we have begun to determine their roles in cellular pathways. Using this system, we have identified an ncRNA repressor of the nuclear factor of activated T cells (NFAT), which interacts with multiple proteins including members of the importin-beta superfamily and likely functions as a specific regulator of NFAT nuclear trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willingham, A T -- Orth, A P -- Batalov, S -- Peters, E C -- Wen, B G -- Aza-Blanc, P -- Hogenesch, J B -- Schultz, P G -- New York, N.Y. -- Science. 2005 Sep 2;309(5740):1570-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, 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/16141075" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; DNA-Binding Proteins/*antagonists & inhibitors ; Humans ; Mice ; NFATC Transcription Factors ; Nuclear Proteins/*antagonists & inhibitors ; *RNA Interference ; RNA, Long Noncoding ; RNA, Untranslated/antagonists & inhibitors/genetics/*physiology ; Transcription Factors/*antagonists & inhibitors ; beta Karyopherins/metabolism
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  • 58
    Publication Date: 2005-06-04
    Description: Fluoroquinolones are gaining increasing importance in the treatment of tuberculosis. The expression of MfpA, a member of the pentapeptide repeat family of proteins from Mycobacterium tuberculosis, causes resistance to ciprofloxacin and sparfloxacin. This protein binds to DNA gyrase and inhibits its activity. Its three-dimensional structure reveals a fold, which we have named the right-handed quadrilateral beta helix, that exhibits size, shape, and electrostatic similarity to B-form DNA. This represents a form of DNA mimicry and explains both its inhibitory effect on DNA gyrase and fluoroquinolone resistance resulting from the protein's expression in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hegde, Subray S -- Vetting, Matthew W -- Roderick, Steven L -- Mitchenall, Lesley A -- Maxwell, Anthony -- Takiff, Howard E -- Blanchard, John S -- AI33696/AI/NIAID NIH HHS/ -- AI60899/AI/NIAID NIH HHS/ -- T32 AI007501/AI/NIAID NIH HHS/ -- T32 AI07501/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1480-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933203" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antitubercular Agents/chemistry/*pharmacology ; Bacterial Proteins/chemistry/*physiology ; Ciprofloxacin/pharmacology ; Crystallography, X-Ray ; DNA Gyrase/metabolism ; DNA, Bacterial/*chemistry ; DNA, Superhelical/chemistry ; *Drug Resistance, Bacterial ; Drug Resistance, Microbial/*physiology ; Enzyme Inhibitors/chemistry ; Escherichia coli/enzymology ; Fluoroquinolones/antagonists & inhibitors/chemistry/*pharmacology ; Models, Molecular ; *Molecular Mimicry ; Molecular Sequence Data ; Monomeric GTP-Binding Proteins ; Mycobacterium tuberculosis/drug effects/*physiology ; Protein Conformation ; Protein Folding ; Structure-Activity Relationship ; Topoisomerase II Inhibitors
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, Martin -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1758.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357238" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cricetinae ; Humans ; Mice ; PrPC Proteins/*chemistry ; PrPSc Proteins/*chemistry/*pathogenicity ; Prion Diseases/*etiology ; Protein Folding
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  • 60
    Publication Date: 2005-12-13
    Description: Sir2 (silent information regulator 2) is a nicotinamide adenine dinucleotide-dependent deacetylase required for longevity due to calorie restriction in yeast and Drosophila. In mammals, calorie restriction induces a complex pattern of physiological and behavioral changes. Here we report that the mammalian Sir2 ortholog, Sirt1, is required for the induction of a phenotype by calorie restriction in mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Danica -- Steele, Andrew D -- Lindquist, Susan -- Guarente, Leonard -- AG11119/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1641.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339438" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Caloric Restriction ; Eating ; Mice ; Mice, Knockout ; *Motor Activity ; Movement ; Sirtuin 1 ; Sirtuins/genetics/*physiology
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  • 61
    Publication Date: 2005-09-06
    Description: Twin-ribozyme introns are formed by two ribozymes belonging to the group I family and occur in some ribosomal RNA transcripts. The group I-like ribozyme, GIR1, liberates the 5' end of a homing endonuclease messenger RNA in the slime mold Didymium iridis. We demonstrate that this cleavage occurs by a transesterification reaction with the joining of the first and the third nucleotide of the messenger by a 2',5'-phosphodiester linkage. Thus, a group I-like ribozyme catalyzes an RNA branching reaction similar to the first step of splicing in group II introns and spliceosomal introns. The resulting short lariat, by forming a protective 5' cap, might have been useful in a primitive RNA world.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nielsen, Henrik -- Westhof, Eric -- Johansen, Steinar -- New York, N.Y. -- Science. 2005 Sep 2;309(5740):1584-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Biochemistry and Genetics, Panum Institute, University of Copenhagen, DK-2200N Copenhagen, Denmark. hamra@imbg.ku.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16141078" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; Endonucleases/biosynthesis/*genetics ; Esterification ; *Introns ; Molecular Sequence Data ; RNA Caps/*chemistry ; *RNA Splicing ; RNA, Catalytic/chemistry/*metabolism
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  • 62
    Publication Date: 2005-01-18
    Description: Dendritic cells (DCs) and macrophages are critical to innate and adaptive immunity to the intestinal bacterial microbiota. Here, we identify a myeloid-derived mucosal DC in mice, which populates the entire lamina propria of the small intestine. Lamina propria DCs were found to depend on the chemokine receptor CX3CR1 to form transepithelial dendrites, which enable the cells to directly sample luminal antigens. CX3CR1 was also found to control the clearance of entero-invasive pathogens by DCs. Thus, CX3CR1-dependent processes, which control host interactions of specialized DCs with commensal and pathogenic bacteria, may regulate immunological tolerance and inflammation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Niess, Jan Hendrik -- Brand, Stephan -- Gu, Xiubin -- Landsman, Limor -- Jung, Steffen -- McCormick, Beth A -- Vyas, Jatin M -- Boes, Marianne -- Ploegh, Hidde L -- Fox, James G -- Littman, Dan R -- Reinecker, Hans-Christian -- AI33856/AI/NIAID NIH HHS/ -- DK33506/DK/NIDDK NIH HHS/ -- DK54427/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):254-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gastrointestinal Unit, Massachusetts General Hospital and Harvard Medical School, 55 Fruit Street, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15653504" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chemokine CX3CL1 ; Chemokines, CX3C/metabolism ; Dendritic Cells/cytology/*immunology/microbiology ; Escherichia coli/*immunology/isolation & purification ; Gene Deletion ; Green Fluorescent Proteins/metabolism ; Ileum/cytology/immunology ; *Immunity, Mucosal ; Intestinal Mucosa/*immunology/microbiology ; Intestine, Small/immunology/microbiology ; Lymphoid Tissue/cytology/immunology ; Membrane Proteins/metabolism ; Mice ; Mice, Transgenic ; Peyer's Patches/immunology/microbiology ; Phagocytosis ; Receptors, Chemokine/genetics/metabolism/*physiology ; Salmonella Infections, Animal/*immunology/microbiology ; Salmonella typhimurium/*immunology/isolation & purification
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  • 63
    Publication Date: 2005-02-05
    Description: Plants encode subunits for a fourth RNA polymerase (Pol IV) in addition to the well-known DNA-dependent RNA polymerases I, II, and III. By mutation of the two largest subunits (NRPD1a and NRPD2), we show that Pol IV silences certain transposons and repetitive DNA in a short interfering RNA pathway involving RNA-dependent RNA polymerase 2 and Dicer-like 3. The existence of this distinct silencing polymerase may explain the paradoxical involvement of an RNA silencing pathway in maintenance of transcriptional silencing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herr, A J -- Jensen, M B -- Dalmay, T -- Baulcombe, D C -- New York, N.Y. -- Science. 2005 Apr 1;308(5718):118-20. Epub 2005 Feb 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692015" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*enzymology/genetics ; Arabidopsis Proteins/chemistry/genetics/metabolism ; Base Sequence ; Chromatin/metabolism ; DNA Methylation ; DNA Transposable Elements ; DNA, Plant/*genetics/metabolism ; DNA-Directed RNA Polymerases/chemistry/genetics/*metabolism ; *Gene Silencing ; Genes, Plant ; Genetic Complementation Test ; Green Fluorescent Proteins/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Oryza/enzymology/genetics ; Plants, Genetically Modified ; Protein Subunits/chemistry/genetics/metabolism ; RNA Interference ; RNA Polymerase II/metabolism ; RNA, Plant/metabolism ; RNA, Small Interfering/metabolism ; Repetitive Sequences, Nucleic Acid ; Transgenes
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  • 64
    Publication Date: 2005-04-16
    Description: Microglial cells represent the immune system of the mammalian brain and therefore are critically involved in various injuries and diseases. Little is known about their role in the healthy brain and their immediate reaction to brain damage. By using in vivo two-photon imaging in neocortex, we found that microglial cells are highly active in their presumed resting state, continually surveying their microenvironment with extremely motile processes and protrusions. Furthermore, blood-brain barrier disruption provoked immediate and focal activation of microglia, switching their behavior from patroling to shielding of the injured site. Microglia thus are busy and vigilant housekeepers in the adult brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nimmerjahn, Axel -- Kirchhoff, Frank -- Helmchen, Fritjof -- New York, N.Y. -- Science. 2005 May 27;308(5726):1314-8. Epub 2005 Apr 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung Zellphysiologie, Max Planck Institut fur Medizinische Forschung, Jahnstrasse 29, 69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15831717" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/physiology/ultrastructure ; Bicuculline/pharmacology ; Blood-Brain Barrier ; Brain Injuries/physiopathology ; Capillaries/injuries ; Cell Movement ; Cell Surface Extensions/*physiology/ultrastructure ; GABA Antagonists/pharmacology ; Green Fluorescent Proteins ; Lasers ; Lipopolysaccharides/pharmacology ; Mice ; Mice, Transgenic ; Microglia/cytology/*physiology/*ultrastructure ; Microscopy, Fluorescence ; Neocortex/*cytology/*physiology ; Pseudopodia/physiology ; Sodium Channel Blockers/pharmacology ; Tetrodotoxin/pharmacology
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  • 65
    Publication Date: 2005-01-08
    Description: The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of control-topological, conformational, and covalent-until its release from the membrane is triggered by the P1 holin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, Min -- Arulandu, Arockiasamy -- Struck, Douglas K -- Swanson, Stephanie -- Sacchettini, James C -- Young, Ry -- GM27099/GM/NIGMS NIH HHS/ -- GM62410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):113-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637279" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage P1/*enzymology ; Binding Sites ; Catalytic Domain ; Cell Membrane/enzymology ; Chemistry, Physical ; Crystallography, X-Ray ; Cysteine/chemistry ; Enzyme Activation ; Escherichia coli/enzymology/virology ; Isomerism ; Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Muramidase/*chemistry/genetics/*metabolism ; Mutation ; Physicochemical Phenomena ; Protein Conformation ; Protein Sorting Signals ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism
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  • 66
    Publication Date: 2005-02-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):507.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681361" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/drug effects/embryology ; Female ; Humans ; Maximum Allowable Concentration ; National Academy of Sciences (U.S.) ; Perchlorates/administration & dosage/*toxicity ; Pregnancy ; Rats ; Risk Assessment ; Thyroid Gland/drug effects ; Thyroid Hormones/metabolism ; Toxicity Tests ; United States ; United States Environmental Protection Agency ; Water Pollutants, Chemical/administration & dosage/*toxicity ; *Water Supply
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  • 67
    Publication Date: 2005-10-22
    Description: Infection of mice with an attenuated Creutzfeldt-Jakob disease agent (SY-CJD) interferes with superinfection by a more virulent human-derived CJD agent (FU-CJD) and does not require pathological prion protein (PrPres). Using a rapid coculture system, we found that a neural cell line free of immune system cells similarly supported substantial CJD agent interference without PrPres. In addition, SY-CJD prevented superinfection by sheep-derived Chandler (Ch) and 22L scrapie agents. However, only 22L and not Ch prevented FU-CJD infection, even though both scrapie strains provoked abundant PrPres. This relationship between particular strains of sheep- and human-derived agents is likely to affect their prevalence and epidemic spread.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishida, Noriuki -- Katamine, Shigeru -- Manuelidis, Laura -- NS12674/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):493-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale Medical School, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239476" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Coculture Techniques ; *Creutzfeldt-Jakob Syndrome ; Humans ; Mice ; Neurons/metabolism/*physiology ; PrPSc Proteins/metabolism/*pathogenicity ; Prions/metabolism/*pathogenicity/*physiology ; Scrapie ; Sheep ; Species Specificity ; Virulence
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  • 68
    Publication Date: 2005-02-01
    Description: Neuronal gene transcription is repressed in non-neuronal cells by the repressor element 1 (RE-1)-silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) complex. To understand how this silencing is achieved, we examined a family of class-C RNA polymerase II (RNAPII) carboxyl-terminal domain (CTD) phosphatases [small CTD phosphatases (SCPs) 1 to 3], whose expression is restricted to non-neuronal tissues. We show that REST/NRSF recruits SCPs to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. Phosphatase-inactive forms of SCP interfere with REST/NRSF function and promote neuronal differentiation of P19 stem cells. Likewise, small interfering RNA directed to the single Drosophila SCP unmasks neuronal gene expression in S2 cells. Thus, SCP activity is an evolutionarily conserved transcriptional regulator that acts globally to silence neuronal genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeo, Michele -- Lee, Soo-Kyung -- Lee, Bora -- Ruiz, Esmeralda C -- Pfaff, Samuel L -- Gill, Gordon N -- DK13149/DK/NIDDK NIH HHS/ -- NS37116/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):596-600.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681389" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Basic Helix-Loop-Helix Transcription Factors ; Cell Differentiation ; Cell Line ; Chromatin Immunoprecipitation ; DNA-Binding Proteins/metabolism ; Down-Regulation ; Drosophila/genetics/metabolism ; Drosophila Proteins/genetics/metabolism ; Gene Expression Profiling ; Gene Expression Regulation ; *Gene Silencing ; Humans ; In Situ Hybridization ; Mice ; Nerve Tissue Proteins/metabolism ; Neurons/cytology/*physiology ; Nuclear Proteins ; Phosphoprotein Phosphatases/genetics/*metabolism ; Phosphorylation ; RNA Interference ; Regulatory Sequences, Nucleic Acid ; Repressor Proteins/*metabolism ; TCF Transcription Factors ; Transcription Factor 7-Like 1 Protein ; Transcription Factors/*metabolism ; Tretinoin/pharmacology
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  • 69
    Publication Date: 2005-04-02
    Description: We analyzed the mortality impacts and greenhouse gas (GHG) emissions produced by household energy use in Africa. Under a business-as-usual (BAU) scenario, household indoor air pollution will cause an estimated 9.8 million premature deaths by the year 2030. Gradual and rapid transitions to charcoal would delay 1.0 million and 2.8 million deaths, respectively; similar transitions to petroleum fuels would delay 1.3 million and 3.7 million deaths. Cumulative BAU GHG emissions will be 6.7 billion tons of carbon by 2050, which is 5.6% of Africa's total emissions. Large shifts to the use of fossil fuels would reduce GHG emissions by 1 to 10%. Charcoal-intensive future scenarios using current practices increase emissions by 140 to 190%; the increase can be reduced to 5 to 36% using currently available technologies for sustainable production or potentially reduced even more with investment in technological innovation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bailis, Robert -- Ezzati, Majid -- Kammen, Daniel M -- P01-AG17625/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 1;308(5718):98-103.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Energy and Resources Group, University of California, Berkeley, CA 94720-3050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802601" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Africa South of the Sahara ; *Air Pollution, Indoor/adverse effects/prevention & control ; *Biomass ; Carbon Dioxide ; Charcoal ; Child ; Costs and Cost Analysis ; Databases, Factual ; *Energy-Generating Resources/economics ; Female ; Forecasting ; Fossil Fuels ; *Greenhouse Effect ; Humans ; Mortality/trends ; *Petroleum ; Public Health/trends ; Pulmonary Disease, Chronic Obstructive/*mortality ; Respiratory Tract Infections/*mortality ; Rural Population ; Urban Population ; Wood
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  • 70
    Publication Date: 2005-10-29
    Description: Hypothalamic neurons that express neuropeptide Y (NPY) and agouti-related protein (AgRP) are thought to be critical regulators of feeding behavior and body weight. To determine whether NPY/AgRP neurons are essential in mice, we targeted the human diphtheria toxin receptor to the Agrp locus, which allows temporally controlled ablation of NPY/AgRP neurons to occur after an injection of diphtheria toxin. Neonatal ablation of NPY/AgRP neurons had minimal effects on feeding, whereas their ablation in adults caused rapid starvation. These results suggest that network-based compensatory mechanisms can develop after the ablation of NPY/AgRP neurons in neonates but do not readily occur when these neurons become essential in adults.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luquet, Serge -- Perez, Francisco A -- Hnasko, Thomas S -- Palmiter, Richard D -- K01 DA026504/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):683-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Washington, Box 357370, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16254186" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/physiology ; Agouti-Related Protein ; Animals ; Animals, Newborn ; Arcuate Nucleus of Hypothalamus/cytology ; Body Weight/physiology ; Diphtheria Toxin ; Feeding Behavior/*physiology ; Heparin-binding EGF-like Growth Factor ; Humans ; Intercellular Signaling Peptides and Proteins ; Mice ; Neurons/metabolism/*physiology ; Neuropeptide Y/*metabolism ; Proteins/*metabolism ; Receptors, Cell Surface/genetics
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  • 71
    Publication Date: 2005-04-30
    Description: Mammalian Toll-like receptors (TLRs) play an important role in the innate recognition of pathogens by dendritic cells (DCs). Although TLRs are clearly involved in the detection of bacteria and viruses, relatively little is known about their function in the innate response to eukaryotic microorganisms. Here we identify a profilin-like molecule from the protozoan parasite Toxoplasma gondii that generates a potent interleukin-12 (IL-12) response in murine DCs that is dependent on myeloid differentiation factor 88. T. gondii profilin activates DCs through TLR11 and is the first chemically defined ligand for this TLR. Moreover, TLR11 is required in vivo for parasite-induced IL-12 production and optimal resistance to infection, thereby establishing a role for the receptor in host recognition of protozoan pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yarovinsky, Felix -- Zhang, Dekai -- Andersen, John F -- Bannenberg, Gerard L -- Serhan, Charles N -- Hayden, Matthew S -- Hieny, Sara -- Sutterwala, Fayyaz S -- Flavell, Richard A -- Ghosh, Sankar -- Sher, Alan -- 1R01AI045806-01A1/AI/NIAID NIH HHS/ -- AI05093/AI/NIAID NIH HHS/ -- R01-AI59440/AI/NIAID NIH HHS/ -- R01-GM38765/GM/NIGMS NIH HHS/ -- Intramural NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1626-9. Epub 2005 Apr 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunobiology Section, Laboratory of Parasitic Diseases; National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA. fyarovinsky@niaid.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860593" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antigens, Differentiation/genetics/metabolism ; Contractile Proteins/chemistry/*immunology/isolation & purification/metabolism ; Dendritic Cells/*immunology ; Genes, Protozoan ; Immunity, Innate ; Interleukin-12/biosynthesis/blood ; Ligands ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Inbred C57BL ; Microfilament Proteins/chemistry/*immunology/isolation & purification/metabolism ; Molecular Sequence Data ; Myeloid Differentiation Factor 88 ; NF-kappa B/metabolism ; Profilins ; Protozoan Proteins/chemistry/*immunology/isolation & purification/metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Immunologic/genetics/metabolism ; Recombinant Proteins/immunology ; Signal Transduction ; Toll-Like Receptors ; Toxoplasma/genetics/*immunology ; Toxoplasmosis, Animal/*immunology ; Transfection
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  • 72
    Publication Date: 2005-08-16
    Description: Microorganisms living in anoxic rice soils contribute 10 to 25% of global methane emissions. The most important carbon source for CH4 production is plant-derived carbon that enters soil as root exudates and debris. Pulse labeling of rice plants with 13CO2 resulted in incorporation of 13C into the ribosomal RNA of Rice Cluster I Archaea in the soil, indicating that this archaeal group plays a key role in CH4 production from plant-derived carbon. This group of microorganisms has not yet been isolated but appears to be of global environmental importance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Yahai -- Conrad, Ralf -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1088-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Resources and Environmental Sciences, China Agricultural University, Beijing 100094, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099988" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/classification/genetics/growth & development/*metabolism ; Carbon Dioxide/metabolism ; Carbon Isotopes/*metabolism ; Cloning, Molecular ; *Ecosystem ; Hydrogen/metabolism ; Methane/*metabolism ; Molecular Sequence Data ; Oryza/metabolism/*microbiology ; Photosynthesis ; Phylogeny ; Plant Roots/metabolism/microbiology ; Polymorphism, Restriction Fragment Length ; RNA, Archaeal/metabolism ; RNA, Ribosomal, 16S/genetics/metabolism ; *Soil Microbiology
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  • 73
    Publication Date: 2005-06-04
    Description: Despite the greater information content of genomic DNA, ancient DNA studies have largely been limited to the amplification of mitochondrial sequences. Here we describe metagenomic libraries constructed with unamplified DNA extracted from skeletal remains of two 40,000-year-old extinct cave bears. Analysis of approximately 1 megabase of sequence from each library showed that despite significant microbial contamination, 5.8 and 1.1% of clones contained cave bear inserts, yielding 26,861 base pairs of cave bear genome sequence. Comparison of cave bear and modern bear sequences revealed the evolutionary relationship of these lineages. The metagenomic approach used here establishes the feasibility of ancient DNA genome sequencing programs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noonan, James P -- Hofreiter, Michael -- Smith, Doug -- Priest, James R -- Rohland, Nadin -- Rabeder, Gernot -- Krause, Johannes -- Detter, J Chris -- Paabo, Svante -- Rubin, Edward M -- T32 HL07279/HL/NHLBI NIH HHS/ -- U1 HL66681B/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):597-9. Epub 2005 Jun 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉United States Department of Energy Joint Genome Institute, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933159" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Computational Biology ; DNA/genetics/history ; Dogs/genetics ; *Genome ; Genomic Library ; History, Ancient ; Molecular Sequence Data ; Phylogeny ; Sequence Alignment ; *Sequence Analysis, DNA ; Ursidae/*genetics
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuspa, Stuart H -- Epstein, Ervin H Jr -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1727-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. sy12j@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774745" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma, Squamous Cell/etiology/genetics/pathology/*physiopathology ; Cell Adhesion Molecules/metabolism ; Cell Transformation, Neoplastic ; Collagen Type VII/chemistry/*genetics/*physiology ; Disease Susceptibility ; Epidermolysis Bullosa Dystrophica/complications/*genetics/metabolism/pathology ; Genes, ras ; Humans ; I-kappa B Proteins/genetics/metabolism ; Keratinocytes/*metabolism/pathology ; Mice ; Mutation ; Neoplasm Invasiveness ; Protein Structure, Tertiary ; Skin Neoplasms/etiology/genetics/pathology/*physiopathology ; Transduction, Genetic ; Transforming Growth Factor beta/metabolism
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  • 75
    Publication Date: 2005-06-18
    Description: Toll-like receptors (TLRs) play key roles in activating immune responses during infection. The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs). Asparagines conserved in the 24-residue LRR motif contribute extensive hydrogen-bonding networks for solenoid stabilization. TLR3 is largely masked by carbohydrate, but one face is glycosylation-free, which suggests its potential role in ligand binding and oligomerization. Highly conserved surface residues and a TLR3-specific LRR insertion form a homodimer interface in the crystal, whereas two patches of positively charged residues and a second insertion would provide an appropriate binding site for double-stranded RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choe, Jungwoo -- Kelker, Matthew S -- Wilson, Ian A -- AI-42266/AI/NIAID NIH HHS/ -- CA-58896/CA/NCI NIH HHS/ -- T32 AI077606/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):581-5. Epub 2005 Jun 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute (TSRI), 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/15961631" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; Glycosylation ; Humans ; Hydrogen Bonding ; Leucine/chemistry ; Ligands ; Membrane Glycoproteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Double-Stranded/metabolism ; Receptors, Cell Surface/*chemistry/metabolism ; Repetitive Sequences, Amino Acid ; Signal Transduction ; Static Electricity ; Surface Properties ; Toll-Like Receptor 3 ; Toll-Like Receptors
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  • 76
    Publication Date: 2005-05-21
    Description: beta-Catenin is a multifunctional protein that mediates Wnt signaling by binding to members of the T cell factor (TCF) family of transcription factors. Here, we report an evolutionarily conserved interaction of beta-catenin with FOXO transcription factors, which are regulated by insulin and oxidative stress signaling. beta-Catenin binds directly to FOXO and enhances FOXO transcriptional activity in mammalian cells. In Caenorhabditis elegans, loss of the beta-catenin BAR-1 reduces the activity of the FOXO ortholog DAF-16 in dauer formation and life span. Association of beta-catenin with FOXO was enhanced in cells exposed to oxidative stress. Furthermore, BAR-1 was required for the oxidative stress-induced expression of the DAF-16 target gene sod-3 and for resistance to oxidative damage. These results demonstrate a role for beta-catenin in regulating FOXO function that is particularly important under conditions of oxidative stress.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Essers, Marieke A G -- de Vries-Smits, Lydia M M -- Barker, Nick -- Polderman, Paulien E -- Burgering, Boudewijn M T -- Korswagen, Hendrik C -- New York, N.Y. -- Science. 2005 May 20;308(5725):1181-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry and Center for Biomedical Genetics, University Medical Center, Universiteitsweg 100, 3584 CG Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905404" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/genetics/*metabolism/physiology ; Caenorhabditis elegans Proteins/genetics/*metabolism ; Carrier Proteins/genetics/metabolism ; Cell Cycle ; Cell Line ; Cell Line, Tumor ; Cyclin-Dependent Kinase Inhibitor p27 ; Cytoskeletal Proteins/chemistry/genetics/*metabolism ; DNA-Binding Proteins/metabolism ; Forkhead Transcription Factors ; Humans ; Hydrogen Peroxide/pharmacology ; Immunoprecipitation ; Insulin/pharmacology ; Intracellular Signaling Peptides and Proteins/genetics/metabolism ; Lithium Chloride/pharmacology ; Longevity ; Mice ; Mutation ; *Oxidative Stress ; Receptor, Insulin/genetics/metabolism ; *Signal Transduction ; Superoxide Dismutase/metabolism ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/*metabolism ; Transfection ; beta Catenin
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  • 77
    Publication Date: 2005-02-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2005 Feb 18;307(5712):1027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15718437" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Asia, Southeastern/epidemiology ; Cambodia/epidemiology ; Disease Outbreaks/veterinary ; Female ; Humans ; *Influenza A virus ; Influenza in Birds/*epidemiology ; Influenza, Human/*epidemiology/transmission/*virology ; Male ; *Population Surveillance ; Poultry
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  • 78
    Publication Date: 2005-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmerberg, Joshua -- Chernomordik, Leonid V -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1626-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biophysics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-1855, USA. joshz@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339436" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Exocytosis ; Fatty Acids/*metabolism ; Hydrolysis ; Lipid Bilayers ; Lysophospholipids/*metabolism ; Membrane Fusion ; Membrane Lipids/analysis/metabolism ; Mice ; Micelles ; Neuromuscular Junction/drug effects/physiology ; Neurotoxins/metabolism/toxicity ; Neurotransmitter Agents/metabolism ; Phospholipases A/*metabolism/toxicity ; Synaptic Membranes/chemistry/*physiology ; Synaptic Vesicles/physiology
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  • 79
    Publication Date: 2005-02-01
    Description: The positive buoyancy of marine fish eggs in sea water, allowed by hydration of the oocyte, is critical for their survival and dispersion in the ocean. We isolated an aquaporin, SaAQP1o, that belongs to a unique subfamily of aquaporin-1-like channels specifically evolved in teleosts and mainly expressed in the ovary. We further show that hormone-induced fish oocyte hydration is a highly controlled process based on the interplay between protein hydrolysis and the translocation of SaAQP1o to the plasma membrane, indicating a specialized physiological role for this aquaporin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fabra, Mercedes -- Raldua, Demetrio -- Power, Deborah M -- Deen, Peter M T -- Cerda, Joan -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):545.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center of Aquaculture-Institut de Recerca i Tecnologia Agroalimentaries, Tarragona, Spain, and Reference Center in Aquaculture, Barcelona, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681377" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aquaporin 1 ; Aquaporins/chemistry/classification/genetics/*physiology ; Biological Evolution ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; DNA, Complementary ; Female ; Fishes/genetics/physiology ; Mercuric Chloride/pharmacology ; Microvilli/metabolism ; Molecular Sequence Data ; Oocytes/*physiology ; Ovary ; Permeability ; Phylogeny ; Recombinant Proteins/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Sea Bream/genetics/*physiology ; Water/*metabolism ; Xenopus laevis/genetics
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  • 80
    Publication Date: 2005-08-16
    Description: Mesenchymal stem cells (MSCs) are a pluripotent cell type that can differentiate into several distinct lineages. Two key transcription factors, Runx2 and peroxisome proliferator-activated receptor gamma (PPARgamma), drive MSCs to differentiate into either osteoblasts or adipocytes, respectively. How these two transcription factors are regulated in order to specify these alternate cell fates remains a pivotal question. Here we report that a 14-3-3-binding protein, TAZ (transcriptional coactivator with PDZ-binding motif), coactivates Runx2-dependent gene transcription while repressing PPARgamma-dependent gene transcription. By modulating TAZ expression in model cell lines, mouse embryonic fibroblasts, and primary MSCs in culture and in zebrafish in vivo, we observed alterations in osteogenic versus adipogenic potential. These results indicate that TAZ functions as a molecular rheostat that modulates MSC differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hong, Jeong-Ho -- Hwang, Eun Sook -- McManus, Michael T -- Amsterdam, Adam -- Tian, Yu -- Kalmukova, Ralitsa -- Mueller, Elisabetta -- Benjamin, Thomas -- Spiegelman, Bruce M -- Sharp, Phillip A -- Hopkins, Nancy -- Yaffe, Michael B -- CA042063/CA/NCI NIH HHS/ -- GM60594/GM/NIGMS NIH HHS/ -- GM68762/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1074-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research, Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, E18-580, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099986" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/*cytology ; Animals ; Bone Morphogenetic Protein 2 ; Bone Morphogenetic Proteins/pharmacology ; Cell Differentiation ; Cell Line ; Core Binding Factor Alpha 1 Subunit ; Gene Expression Regulation, Developmental ; Humans ; Mesenchymal Stromal Cells/*cytology/physiology ; Mice ; Neoplasm Proteins/metabolism ; Oligonucleotides, Antisense ; Osteoblasts/*cytology ; Osteocalcin/genetics ; Osteogenesis ; PPAR gamma/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Proteins/chemistry/genetics/*physiology ; RNA, Small Interfering ; Transcription Factors/chemistry/genetics/metabolism/*physiology ; Transcriptional Activation ; Transfection ; Transforming Growth Factor beta/pharmacology ; Zebrafish ; Zebrafish Proteins/genetics/physiology
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  • 81
    Publication Date: 2005-03-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mann, Charles C -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1716-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774742" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Age Factors ; Aged ; Body Mass Index ; Child ; Female ; Humans ; Incidence ; Life Expectancy/*trends ; Male ; Mortality ; Obesity/complications/*epidemiology ; Public Health ; United States/epidemiology
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  • 82
    Publication Date: 2005-12-13
    Description: Much is known about how people make decisions under varying levels of probability (risk). Less is known about the neural basis of decision-making when probabilities are uncertain because of missing information (ambiguity). In decision theory, ambiguity about probabilities should not affect choices. Using functional brain imaging, we show that the level of ambiguity in choices correlates positively with activation in the amygdala and orbitofrontal cortex, and negatively with a striatal system. Moreover, striatal activity correlates positively with expected reward. Neurological subjects with orbitofrontal lesions were insensitive to the level of ambiguity and risk in behavioral choices. These data suggest a general neural circuit responding to degrees of uncertainty, contrary to decision theory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, Ming -- Bhatt, Meghana -- Adolphs, Ralph -- Tranel, Daniel -- Camerer, Colin F -- P01 NS19632/NS/NINDS NIH HHS/ -- R01 MH067681/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1680-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Humanities and Social Sciences, 228-77, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339445" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amygdala/physiology ; Brain/*physiology ; Brain Diseases/physiopathology/psychology ; Brain Mapping ; Confidence Intervals ; Corpus Striatum/physiology ; *Decision Making ; Decision Theory ; Female ; Frontal Lobe/physiology ; Games, Experimental ; Humans ; Likelihood Functions ; Magnetic Resonance Imaging ; Male ; *Mental Processes ; Probability ; Reward ; Risk ; *Uncertainty
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-09-06
    Description: Recent studies showing that most "messenger" RNAs do not encode proteins finally explain the long-standing discrepancy between the small number of protein-coding genes found in vertebrate genomes and the much larger and ever-increasing number of polyadenylated transcripts identified by tag-sampling or microarray-based methods. Exploring the role and diversity of these numerous noncoding RNAs now constitutes a main challenge in transcription research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Claverie, Jean-Michel -- New York, N.Y. -- Science. 2005 Sep 2;309(5740):1529-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural and Genomics Information Laboratory, CNRS UPR 2589, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, Marseille 13402, France. jean-michel.claverie@igs.cnrs-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16141064" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Genes ; *Genome, Human ; Genomics ; Humans ; Mice ; Proteins/genetics ; RNA, Untranslated/*biosynthesis/physiology ; *Transcription, Genetic
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-05-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beghi, Ettore -- Bendotti, Caterina -- Mennini, Tiziana -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):632-3; author reply 632-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15864832" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Transport System X-AG/biosynthesis ; Amyotrophic Lateral Sclerosis/*drug therapy ; Animals ; Anti-Bacterial Agents/pharmacology/*therapeutic use ; Biological Transport/drug effects ; Ceftriaxone/pharmacology/*therapeutic use ; Clinical Trials as Topic ; Glutamic Acid/metabolism ; Humans ; Rats ; Spinal Cord/drug effects/metabolism
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  • 85
    Publication Date: 2005-11-19
    Description: Nodes of Ranvier are regularly placed, nonmyelinated axon segments along myelinated nerves. Here we show that nodal membranes isolated from the central nervous system (CNS) of mammals restricted neurite outgrowth of cultured neurons. Proteomic analysis of these membranes revealed several inhibitors of neurite outgrowth, including the oligodendrocyte myelin glycoprotein (OMgp). In rat spinal cord, OMgp was not localized to compact myelin, as previously thought, but to oligodendroglia-like cells, whose processes converge to form a ring that completely encircles the nodes. In OMgp-null mice, CNS nodes were abnormally wide and collateral sprouting was observed. Nodal ensheathment in the CNS may stabilize the node and prevent axonal sprouting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Jeffrey K -- Phillips, Greg R -- Roth, Alejandro D -- Pedraza, Liliana -- Shan, Weisong -- Belkaid, Wiam -- Mi, Sha -- Fex-Svenningsen, Asa -- Florens, Laurence -- Yates, John R 3rd -- Colman, David R -- NS20147/NS/NINDS NIH HHS/ -- P41 RR11823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1813-7. Epub 2005 Nov 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fishberg Department of Neuroscience, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/analysis ; Axons/*physiology/ultrastructure ; Cattle ; Cell Surface Extensions/chemistry/*physiology/ultrastructure ; Cells, Cultured ; GPI-Linked Proteins ; Ganglia, Spinal/physiology/ultrastructure ; Humans ; Mice ; Myelin Proteins ; Myelin Sheath/chemistry ; Myelin-Associated Glycoprotein/analysis ; Myelin-Oligodendrocyte Glycoprotein ; Neurites/*physiology/ultrastructure ; Neuroglia/chemistry/*physiology/*ultrastructure ; Oligodendroglia/chemistry/physiology/ultrastructure ; Proteoglycans/analysis ; Proteomics ; Ranvier's Nodes/chemistry/*physiology/ultrastructure ; Rats ; Spinal Cord/cytology
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  • 86
    Publication Date: 2005-03-05
    Description: To elucidate molecular, cellular, and circuit changes that occur in the brain during learning, we investigated the role of a glutamate receptor subtype in fear conditioning. In this form of learning, animals associate two stimuli, such as a tone and a shock. Here we report that fear conditioning drives AMPA-type glutamate receptors into the synapse of a large fraction of postsynaptic neurons in the lateral amygdala, a brain structure essential for this learning process. Furthermore, memory was reduced if AMPA receptor synaptic incorporation was blocked in as few as 10 to 20% of lateral amygdala neurons. Thus, the encoding of memories in the lateral amygdala is mediated by AMPA receptor trafficking, is widely distributed, and displays little redundancy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rumpel, Simon -- LeDoux, Joseph -- Zador, Anthony -- Malinow, Roberto -- New York, N.Y. -- Science. 2005 Apr 1;308(5718):83-8. Epub 2005 Mar 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746389" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/cytology/metabolism/*physiology/virology ; Animals ; Association Learning/*physiology ; Conditioning (Psychology) ; Electrophysiology ; Fear ; Female ; Genetic Vectors ; Green Fluorescent Proteins/metabolism ; Long-Term Potentiation ; Male ; Memory/*physiology ; Neural Pathways/physiology ; *Neuronal Plasticity ; Neurons/metabolism/*physiology/virology ; Patch-Clamp Techniques ; Protein Transport ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/*metabolism ; Recombinant Fusion Proteins/metabolism ; Simplexvirus/genetics ; Synapses/metabolism/*physiology ; Synaptic Transmission ; Thalamus/physiology
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  • 87
    Publication Date: 2005-07-30
    Description: The plague is caused by the bacterium Yersinia pestis. Plague bacteria are thought to inject effector Yop proteins into host cells via the type III pathway. The identity of the host cells targeted for injection during plague infection is unknown. We found, using Yop beta-lactamase hybrids and fluorescent staining of live cells from plague-infected animals, that Y. pestis selected immune cells for injection. In vivo, dendritic cells, macrophages, and neutrophils were injected most frequently, whereas B and T lymphocytes were rarely selected. Thus, it appears that Y. pestis disables these cell populations to annihilate host immune responses during plague.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3210820/" 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/PMC3210820/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marketon, Melanie M -- DePaolo, R William -- DeBord, Kristin L -- Jabri, Bana -- Schneewind, Olaf -- 1-U54-AI-057153/AI/NIAID NIH HHS/ -- U54 AI057153/AI/NIAID NIH HHS/ -- U54 AI057153-01/AI/NIAID NIH HHS/ -- U54 AI057153-02/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 9;309(5741):1739-41. Epub 2005 Jul 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051750" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology/metabolism/microbiology ; Bacterial Outer Membrane Proteins/genetics/*metabolism ; Dendritic Cells/immunology/metabolism/*microbiology ; Flow Cytometry ; Fluorescence ; HeLa Cells ; Humans ; Macrophages/immunology/metabolism/*microbiology ; Macrophages, Peritoneal/microbiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Microscopy, Fluorescence ; Neutrophils/immunology/metabolism/*microbiology ; Plague/immunology/*microbiology ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/immunology/metabolism/microbiology ; Transformation, Bacterial ; Yersinia pestis/metabolism/*pathogenicity
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  • 88
    Publication Date: 2005-07-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russo, Tommaso -- Volterra, Virginia -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):56; author reply 56.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Philosophy, University of Calabria, Via Piero Bucci, 87036 Rende (CS), Italy. t.russo@mclink.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994513" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Child ; Communication ; Deafness ; Gestures ; Humans ; Language ; *Learning ; Linguistics ; Nicaragua ; *Sign Language ; Speech
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  • 89
    Publication Date: 2005-04-12
    Description: Vasopressin and oxytocin strongly modulate autonomic fear responses, through mechanisms that are still unclear. We describe how these neuropeptides excite distinct neuronal populations in the central amygdala, which provides the major output of the amygdaloid complex to the autonomic nervous system. We identified these two neuronal populations as part of an inhibitory network, through which vasopressin and oxytocin modulate the integration of excitatory information from the basolateral amygdala and cerebral cortex in opposite manners. Through this network, the expression and endogenous activation of vasopressin and oxytocin receptors may regulate the autonomic expression of fear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, Daniel -- Veinante, Pierre -- Stoop, Ron -- New York, N.Y. -- Science. 2005 Apr 8;308(5719):245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biology and Morphology, Centre Hospitalier Universitaire Vaudois, University of Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15821089" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/cytology/drug effects/*physiology ; Animals ; Antidiuretic Hormone Receptor Antagonists ; Autoradiography ; Fear/physiology ; In Vitro Techniques ; Neurons/*physiology ; Oxytocin/*analogs & derivatives/pharmacology/*physiology ; Patch-Clamp Techniques ; Rats ; Rats, Sprague-Dawley ; Receptors, Oxytocin/agonists/antagonists & inhibitors/metabolism ; Receptors, Vasopressin/agonists/metabolism ; Tetrodotoxin/pharmacology ; Vasopressins/*physiology ; gamma-Aminobutyric Acid/metabolism
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-07-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fetler, Luc -- Amigorena, Sebastian -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):392-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire Physico-Chimie Curie, CNRS UMR 168, Institut Curie, Paris, France. luc.fetler@curie.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020721" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Astrocytes/metabolism ; Brain/blood supply/*cytology/pathology/*physiology ; Brain Injuries/immunology/pathology/*physiopathology ; Capillaries/injuries ; Cell Surface Extensions/physiology/ultrastructure ; Cells, Cultured ; Mice ; Mice, Transgenic ; Microglia/cytology/*physiology/*ultrastructure ; Microscopy/methods ; Movement ; Phagocytosis ; Photons ; Receptors, Purinergic P2/metabolism
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  • 91
    Publication Date: 2005-07-16
    Description: Neurotransmitter release is triggered by calcium ions and depends critically on the correct function of three types of SNARE [soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor] proteins. With use of the large calyx of Held presynaptic terminal from rats, we found that cleavage of different SNARE proteins by clostridial neurotoxins caused distinct kinetic changes in neurotransmitter release. When elevating calcium ion concentration directly at the presynaptic terminal with the use of caged calcium, cleavage of SNAP-25 by botulinum toxin A (BoNT/A) produced a strong reduction in the calcium sensitivity for release, whereas cleavage of syntaxin using BoNT/C1 and synaptobrevin using tetanus toxin (TeNT) produced an all-or-nothing block without changing the kinetics of remaining vesicles. When stimulating release by calcium influx through channels, a difference between BoNT/C1 and TeNT emerged, which suggests that cleavage of synaptobrevin modifies the coupling between channels and release-competent vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sakaba, Takeshi -- Stein, Alexander -- Jahn, Reinhard -- Neher, Erwin -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):491-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Department of Membrane Biophysics, Max Planck Institute for Biophysical Chemistry, Gottingen 37077, Germany. tsakaba@gwdg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020741" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Botulinum Toxins/metabolism/pharmacology ; Botulinum Toxins, Type A/metabolism/pharmacology ; Calcium/metabolism ; Calcium Channels/metabolism ; Excitatory Postsynaptic Potentials ; In Vitro Techniques ; Kinetics ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Neurotransmitter Agents/*metabolism ; Patch-Clamp Techniques ; Presynaptic Terminals/*metabolism ; Qa-SNARE Proteins ; R-SNARE Proteins ; Rats ; Synaptic Vesicles/metabolism ; Synaptosomal-Associated Protein 25 ; Tetanus Toxin/metabolism/pharmacology
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  • 92
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-02-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hussain, Natasha K -- Sheng, Morgan -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1207-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Picower Center for Learning and Memory, RIKEN-MIT Neuroscience Research Center, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. natashah@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731430" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Adhesion Molecules, Neuronal ; Cells, Cultured ; Glutamic Acid/metabolism ; Hippocampus/cytology ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Neural Inhibition ; Neurons/physiology ; Presynaptic Terminals/*physiology ; Protein Binding ; Rats ; Synapses/*physiology ; Synaptic Membranes/*physiology ; gamma-Aminobutyric Acid/metabolism
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  • 93
    Publication Date: 2005-12-03
    Description: Taste receptor cells detect chemicals in the oral cavity and transmit this information to taste nerves, but the neurotransmitter(s) have not been identified. We report that adenosine 5'-triphosphate (ATP) is the key neurotransmitter in this system. Genetic elimination of ionotropic purinergic receptors (P2X2 and P2X3) eliminates taste responses in the taste nerves, although the nerves remain responsive to touch, temperature, and menthol. Similarly, P2X-knockout mice show greatly reduced behavioral responses to sweeteners, glutamate, and bitter substances. Finally, stimulation of taste buds in vitro evokes release of ATP. Thus, ATP fulfils the criteria for a neurotransmitter linking taste buds to the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finger, Thomas E -- Danilova, Vicktoria -- Barrows, Jennell -- Bartel, Dianna L -- Vigers, Alison J -- Stone, Leslie -- Hellekant, Goran -- Kinnamon, Sue C -- P30 DC04657/DC/NIDCD NIH HHS/ -- R01 DC00766/DC/NIDCD NIH HHS/ -- R01 DC06070/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1495-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rocky Mountain Taste and Smell Center, Aurora CO 80045, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322458" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/*metabolism ; Animals ; Chorda Tympani Nerve/*metabolism ; Glossopharyngeal Nerve/*metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurotransmitter Agents/metabolism ; Receptors, Purinergic P2/genetics/metabolism ; Receptors, Purinergic P2X2 ; Receptors, Purinergic P2X3 ; Receptors, Serotonin, 5-HT3/genetics/metabolism ; *Signal Transduction ; Taste Buds/*metabolism
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  • 94
    Publication Date: 2005-10-01
    Description: Intraoperative electrical stimulation, which temporarily inactivates restricted regions during brain surgery, can map cognitive functions in humans with spatiotemporal resolution unmatched by other methods. Using this technique, we found that stimulation of the right inferior parietal lobule or the caudal superior temporal gyrus, but not of its rostral portion, determined rightward deviations on line bisection. However, the strongest shifts occurred with subcortical stimulation. Fiber tracking identified the stimulated site as a section of the superior occipitofrontal fasciculus, a poorly known parietal-frontal pathway. These findings suggest that parietal-frontal communication is necessary for the symmetrical processing of the visual scene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thiebaut de Schotten, Michel -- Urbanski, Marika -- Duffau, Hugues -- Volle, Emmanuelle -- Levy, Richard -- Dubois, Bruno -- Bartolomeo, Paolo -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2226-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM Unit 610, Assistance Publique-Hopitaux de Paris, Hopital de la Salpetriere, 75013 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195465" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Awareness/*physiology ; Brain Mapping ; Brain Neoplasms/surgery ; Electric Stimulation ; Female ; Frontal Lobe/*physiology ; Glioma/surgery ; Humans ; Male ; Nerve Net/*physiology ; Neural Pathways/*physiology ; Parietal Lobe/*physiology ; Perceptual Disorders/physiopathology ; Space Perception/*physiology ; Temporal Lobe/physiology
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  • 95
    Publication Date: 2005-01-22
    Description: Cell lineage specification depends on both gene activation and gene silencing, and in the differentiation of T helper progenitors to Th1 or Th2 effector cells, this requires the action of two opposing transcription factors, T-bet and GATA-3. T-bet is essential for the development of Th1 cells, and GATA-3 performs an equivalent role in Th2 development. We report that T-bet represses Th2 lineage commitment through tyrosine kinase-mediated interaction between the two transcription factors that interferes with the binding of GATA-3 to its target DNA. These results provide a novel function for tyrosine phosphorylation of a transcription factor in specifying alternate fates of a common progenitor cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, Eun Sook -- Szabo, Susanne J -- Schwartzberg, Pamela L -- Glimcher, Laurie H -- AI48126/AI/NIAID NIH HHS/ -- AI56296/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Lineage ; Cytokines/pharmacology/physiology ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; GATA3 Transcription Factor ; Interleukin-5/genetics ; Mice ; Mice, Inbred BALB C ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/metabolism ; T-Box Domain Proteins ; T-Lymphocytes, Helper-Inducer/cytology/*physiology ; Th1 Cells/cytology/physiology ; Th2 Cells/cytology/*physiology ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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  • 96
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, Scott M -- New York, N.Y. -- Science. 2005 May 6;308(5723):800-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201-1559, USA. sthom003@umaryland.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879198" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/*metabolism ; Calcium Channels/metabolism ; Calcium Signaling ; Cell Communication ; Exocytosis ; Interneurons/*physiology ; Neuronal Plasticity ; Neurotransmitter Agents/*metabolism ; Patch-Clamp Techniques ; Probability ; Pyramidal Cells/*physiology ; Rats ; Receptors, N-Methyl-D-Aspartate/physiology ; Somatosensory Cortex/cytology/*physiology ; Synapses/*physiology ; Synaptic Vesicles/physiology ; gamma-Aminobutyric Acid/metabolism
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-08-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):860.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16081704" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/*prevention & control ; Adult ; Biomedical Research/ethics ; *Circumcision, Male ; Global Health ; Humans ; Male ; Publishing/standards ; South Africa
    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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  • 98
    Publication Date: 2005-07-16
    Description: Neurofibrillary tangles (NFTs) are the most common intraneuronal inclusion in the brains of patients with neurodegenerative diseases and have been implicated in mediating neuronal death and cognitive deficits. Here, we found that mice expressing a repressible human tau variant developed progressive age-related NFTs, neuronal loss, and behavioral impairments. After the suppression of transgenic tau, memory function recovered, and neuron numbers stabilized, but to our surprise, NFTs continued to accumulate. Thus, NFTs are not sufficient to cause cognitive decline or neuronal death in this model of tauopathy.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1574647/" 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/PMC1574647/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santacruz, K -- Lewis, J -- Spires, T -- Paulson, J -- Kotilinek, L -- Ingelsson, M -- Guimaraes, A -- DeTure, M -- Ramsden, M -- McGowan, E -- Forster, C -- Yue, M -- Orne, J -- Janus, C -- Mariash, A -- Kuskowski, M -- Hyman, B -- Hutton, M -- Ashe, K H -- P01 AG015453/AG/NIA NIH HHS/ -- P01-AG15453/AG/NIA NIH HHS/ -- R01 AG008487/AG/NIA NIH HHS/ -- R01 AG026249/AG/NIA NIH HHS/ -- R01 AG026252/AG/NIA NIH HHS/ -- R01 NS033249/NS/NINDS NIH HHS/ -- R01 NS046355/NS/NINDS NIH HHS/ -- R01-026252/PHS HHS/ -- R01-AG08487/AG/NIA NIH HHS/ -- R01-AG26249/AG/NIA NIH HHS/ -- R01-NS46355/NS/NINDS NIH HHS/ -- T31-AG00277/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):476-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Laboratory Medicine and Pathology, University of Minnesota Medical School, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020737" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Atrophy ; Brain/*metabolism/pathology ; Cognition ; Disease Progression ; Doxycycline/pharmacology ; Hippocampus/metabolism/pathology ; Humans ; Maze Learning ; *Memory ; Mice ; Mice, Transgenic ; Neurodegenerative Diseases/metabolism/*pathology/*physiopathology ; Neurofibrillary Tangles/metabolism/*pathology ; Neuronal Plasticity ; Neurons/metabolism/pathology ; Organ Size ; Phosphorylation ; RNA, Messenger/genetics/metabolism ; Solubility ; tau Proteins/chemistry/genetics/*metabolism
    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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  • 99
    Publication Date: 2005-07-23
    Description: A key process in organ homeostasis is the mobilization of stem cells out of their niches. We show through analysis of mouse models that telomere length, as well as the catalytic component of telomerase, Tert, are critical determinants in the mobilization of epidermal stem cells. Telomere shortening inhibited mobilization of stem cells out of their niche, impaired hair growth, and resulted in suppression of stem cell proliferative capacity in vitro. In contrast, Tert overexpression in the absence of changes in telomere length promoted stem cell mobilization, hair growth, and stem cell proliferation in vitro. The effects of telomeres and telomerase on stem cell biology anticipate their role in cancer and aging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flores, Ignacio -- Cayuela, Maria L -- Blasco, Maria A -- New York, N.Y. -- Science. 2005 Aug 19;309(5738):1253-6. Epub 2005 Jul 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Telomeres and Telomerase Group, Molecular Oncology Program, Spanish National Cancer Centre (CNIO), Melchor Fernandez Almagro 3, Madrid E-28029, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16037417" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Count ; Cell Differentiation ; Cell Movement ; Cell Proliferation ; Clone Cells ; Epidermis/*cytology ; Hair Follicle/cytology ; Keratinocytes/*cytology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Multipotent Stem Cells/cytology/*physiology ; Telomerase/genetics/*metabolism ; Telomere/*physiology/ultrastructure ; Tetradecanoylphorbol Acetate/pharmacology ; 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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  • 100
    Publication Date: 2005-04-16
    Description: The Drosophila cuticle is essential for maintaining the surface barrier defenses of the fly. Integral to cuticle resilience is the transcription factor grainy head, which regulates production of the enzyme required for covalent cross-linking of the cuticular structural components. We report that formation and maintenance of the epidermal barrier in mice are dependent on a mammalian homolog of grainy head, Grainy head-like 3. Mice lacking this factor display defective skin barrier function and deficient wound repair, accompanied by reduced expression of transglutaminase 1, the key enzyme involved in cross-linking the structural components of the superficial epidermis. These findings suggest that the functional mechanisms involving protein cross-linking that maintain the epidermal barrier and induce tissue repair are conserved across 700 million years of evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ting, Stephen B -- Caddy, Jacinta -- Hislop, Nikki -- Wilanowski, Tomasz -- Auden, Alana -- Zhao, Lin-Lin -- Ellis, Sarah -- Kaur, Pritinder -- Uchida, Yoshikazu -- Holleran, Walter M -- Elias, Peter M -- Cunningham, John M -- Jane, Stephen M -- P01 HL53749-03/HL/NHLBI NIH HHS/ -- P01-AR39448/AR/NIAMS NIH HHS/ -- P30 CA 21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):411-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rotary Bone Marrow Research Laboratories, c/o Royal Melbourne Hospital Post Office, Grattan Street, Parkville, Victoria, Australia 3050.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15831758" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biological Evolution ; DNA-Binding Proteins/*genetics/metabolism/*physiology ; Embryo, Mammalian/physiology ; Embryonic Development ; Epidermis/*embryology/*physiology ; Epithelium/physiology ; Gene Expression ; Kruppel-Like Transcription Factors ; Mice ; Mutation ; Permeability ; Transcription Factors/*genetics/metabolism/*physiology ; Transglutaminases/genetics/metabolism ; Wound Healing/*physiology
    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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