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  • Cell Line  (89)
  • Amino Acid Sequence  (61)
  • AERODYNAMICS
  • Chemistry
  • Pflanzenkrankheit
  • American Association for the Advancement of Science (AAAS)  (143)
  • Iranian Fisheries Science Research Institute
  • 2020-2022
  • 2005-2009  (143)
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  • 2005  (143)
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  • 2020-2022
  • 2005-2009  (143)
  • 1945-1949
  • 1935-1939
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  • 1
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    Proposition 71. Proposed legislation threatens to slow California stem cell rush (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1857.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790821" target="_blank"〉PubMed〈/a〉
    Keywords: California ; Cell Line ; Cloning, Organism ; *Embryo Research/economics/legislation & jurisprudence ; Embryo, Mammalian/*cytology ; Humans ; *Research Support as Topic/legislation & jurisprudence ; *Stem Cells ; Tissue Donors/legislation & jurisprudence
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-19
    Description: Deregulation of Akt/protein kinase B (PKB) is implicated in the pathogenesis of cancer and diabetes. Akt/PKB activation requires the phosphorylation of Thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (PDK1) and Ser473 within the carboxyl-terminal hydrophobic motif by an unknown kinase. We show that in Drosophila and human cells the target of rapamycin (TOR) kinase and its associated protein rictor are necessary for Ser473 phosphorylation and that a reduction in rictor or mammalian TOR (mTOR) expression inhibited an Akt/PKB effector. The rictor-mTOR complex directly phosphorylated Akt/PKB on Ser473 in vitro and facilitated Thr308 phosphorylation by PDK1. Rictor-mTOR may serve as a drug target in tumors that have lost the expression of PTEN, a tumor suppressor that opposes Akt/PKB activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sarbassov, D D -- Guertin, David A -- Ali, Siraj M -- Sabatini, David M -- R01 AI47389/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 18;307(5712):1098-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research and Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15718470" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Adaptor Proteins, Signal Transducing ; Animals ; Carrier Proteins/*metabolism ; Cell Line ; Cell Line, Tumor ; Drosophila Proteins/*metabolism ; Drosophila melanogaster ; Enzyme Activation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Immunoprecipitation ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Proteins/metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; RNA Interference ; Serine/metabolism ; TOR Serine-Threonine Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Micropylar pollen tube guidance by egg apparatus 1 of maize (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Ant nestmate and non-nestmate discrimination by a chemosensory sensillum (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Achieving stability of lipopolysaccharide-induced NF-kappaB activation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Electronic ISSN: 1095-9203
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  • 7
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    Toll-like receptor 8-mediated reversal of CD4+ regulatory T cell function (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 8
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    A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 9
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    DISC1 and PDE4B are interacting genetic factors in schizophrenia that regulate cAMP signaling (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    Print ISSN: 0036-8075
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  • 10
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    SLC24A5, a putative cation exchanger, affects pigmentation in zebrafish and humans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 11
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    Public health. Pandemic or not, experts welcome Bush flu plan (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):952-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284148" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*supply & distribution ; Cell Line ; *Disease Outbreaks/prevention & control ; Financing, Government ; Humans ; Influenza A Virus, H5N1 Subtype/growth & development/immunology/pathogenicity ; Influenza A virus/growth & development/immunology ; Influenza Vaccines/*economics ; Influenza, Human/drug therapy/*epidemiology/prevention & control/*virology ; United States ; Virus Cultivation
    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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  • 12
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    Toward high-resolution de novo structure prediction for small proteins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-17
    Description: The prediction of protein structure from amino acid sequence is a grand challenge of computational molecular biology. By using a combination of improved low- and high-resolution conformational sampling methods, improved atomically detailed potential functions that capture the jigsaw puzzle-like packing of protein cores, and high-performance computing, high-resolution structure prediction (〈1.5 angstroms) can be achieved for small protein domains (〈85 residues). The primary bottleneck to consistent high-resolution prediction appears to be conformational sampling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradley, Philip -- Misura, Kira M S -- Baker, David -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Washington, Department of Biochemistry, and Howard Hughes Medical Institute, Box 357350, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemistry, Physical ; *Computational Biology ; Computer Simulation ; Hydrogen Bonding ; Models, Molecular ; Monte Carlo Method ; Physicochemical Phenomena ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry ; Sequence Alignment ; Thermodynamics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    Functional genomic analysis of the Wnt-wingless signaling pathway (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-09
    Description: The Wnt-Wingless (Wg) pathway is one of a core set of evolutionarily conserved signaling pathways that regulates many aspects of metazoan development. Aberrant Wnt signaling has been linked to human disease. In the present study, we used a genomewide RNA interference (RNAi) screen in Drosophila cells to screen for regulators of the Wnt pathway. We identified 238 potential regulators, which include known pathway components, genes with functions not previously linked to this pathway, and genes with no previously assigned functions. Reciprocal-Best-Blast analyses reveal that 50% of the genes identified in the screen have human orthologs, of which approximately 18% are associated with human disease. Functional assays of selected genes from the cell-based screen in Drosophila, mammalian cells, and zebrafish embryos demonstrated that these genes have evolutionarily conserved functions in Wnt signaling. High-throughput RNAi screens in cultured cells, followed by functional analyses in model organisms, prove to be a rapid means of identifying regulators of signaling pathways implicated in development and disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DasGupta, Ramanuj -- Kaykas, Ajamete -- Moon, Randall T -- Perrimon, Norbert -- New York, N.Y. -- Science. 2005 May 6;308(5723):826-33. Epub 2005 Apr 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Howard Hughes Medical Institute (HHMI), Harvard Medical School, New Research Building, No. 339, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. rdasgupt@genetics.med.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15817814" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Line ; Cloning, Molecular ; Computational Biology ; Cytoskeletal Proteins/metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/*genetics/metabolism ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; Epistasis, Genetic ; *Gene Expression Regulation ; Genes, Insect ; Genes, Reporter ; *Genomics ; Mutation ; Phenotype ; Phosphorylation ; Protein Kinases/metabolism ; Proteins/metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; *RNA Interference ; *Signal Transduction ; Trans-Activators/metabolism ; Transcription Factors/chemistry/genetics/metabolism ; Transfection ; Wnt Proteins ; Wnt1 Protein ; Wnt3 Protein ; Zebrafish ; Zebrafish Proteins ; beta Catenin ; rab5 GTP-Binding Proteins/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 15
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    Ethics: Moral issues of human-non-human primate neural grafting (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greene, Mark -- Schill, Kathryn -- Takahashi, Shoji -- Bateman-House, Alison -- Beauchamp, Tom -- Bok, Hilary -- Cheney, Dorothy -- Coyle, Joseph -- Deacon, Terrence -- Dennett, Daniel -- Donovan, Peter -- Flanagan, Owen -- Goldman, Steven -- Greely, Henry -- Martin, Lee -- Miller, Earl -- Mueller, Dawn -- Siegel, Andrew -- Solter, Davor -- Gearhart, John -- McKhann, Guy -- Faden, Ruth -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):385-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Philosophy, University of Delaware, Newark, DE 19716, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020716" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Animal Experimentation/*ethics ; Animals ; Brain/anatomy & histology/physiology ; Cell Line ; *Ethics, Research ; Humans ; Mental Processes ; Moral Obligations ; *Morals ; Neurons/cytology/physiology/*transplantation ; *Primates/psychology ; Stem Cell Transplantation/*ethics ; Transplantation Chimera ; Transplantation, Heterologous/*ethics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Dependence of self-tolerance on TRAF6-directed development of thymic stroma (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Chromosome alignment and segregation regulated by ubiquitination of survivin (2005)
    American Association for the Advancement of Science (AAAS)
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    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    Crystal structure of the malaria vaccine candidate apical membrane antigen 1 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 19
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    Nodulation signaling in legumes requires NSP2, a member of the GRAS family of transcriptional regulators (2005)
    American Association for the Advancement of Science (AAAS)
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    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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  • 20
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    Circadian clock control by SUMOylation of BMAL1 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 21
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    Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination (2005)
    American Association for the Advancement of Science (AAAS)
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    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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  • 22
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    Stimulus specificity of gene expression programs determined by temporal control of IKK activity (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 23
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    PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-02
    Description: Activation of the transcription factor NF-kappaB after engagement of the T cell receptor (TCR) is important for T cell proliferation and activation during the adaptive immune response. Recent reports have elucidated a signaling pathway that involves the protein kinase C (PKC), the scaffold protein CARD11 (also called CARMA-1), the caspase recruitment domain (CARD)-containing protein Bcl10, and the paracaspase (protease related to caspases) MALT1 as critical intermediates linking the TCR to the IkappaB kinase (IKK) complex. However, the events proximal to the TCR that initiate the activation of this signaling pathway remain poorly defined. We demonstrate that 3-phosphoinositide-dependent kinase 1 (PDK1) has an essential role in this pathway by regulating the activation of PKC and through signal-dependent recruiting of both PKC and CARD11 to lipid rafts. PDK1-associated PKC recruits the IKK complex, whereas PDK1-associated CARD11 recruits the Bcl10-MALT1 complex, thereby allowing activation of the IKK complex through Bcl10-MALT1-dependent ubiquitination of the IKK complex subunit known as NEMO (NF-kappaB essential modifier). Hence, PDK1 plays a critical role by nucleating the TCR-induced NF-kappaB activation pathway in T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Ki-Young -- D'Acquisto, Fulvio -- Hayden, Matthew S -- Shim, Jae-Hyuck -- Ghosh, Sankar -- R37 AI033443/AI/NIAID NIH HHS/ -- R37-AI33443/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 1;308(5718):114-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Department of Molecular Biophysics and Biochemistry, 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/15802604" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Adaptor Proteins, Signal Transducing/metabolism ; Apoptosis Regulatory Proteins ; CARD Signaling Adaptor Proteins ; Carrier Proteins/metabolism ; Caspases ; Cell Line ; Cell Line, Tumor ; Enzyme Activation ; Guanylate Cyclase/metabolism ; Humans ; I-kappa B Kinase ; Isoenzymes/genetics/*metabolism ; Jurkat Cells ; Lymphocyte Activation ; Lymphoma, B-Cell, Marginal Zone/metabolism ; Membrane Microdomains/metabolism ; Membrane Proteins/metabolism ; Models, Biological ; NF-kappa B/*metabolism ; Neoplasm Proteins/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation ; Protein Kinase C/genetics/*metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; RNA Interference ; Receptors, Antigen, T-Cell/immunology/*metabolism ; *Signal Transduction ; T-Lymphocytes/enzymology/immunology/*metabolism ; Transfection
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    Bacterial injectisomes: needle length does matter (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Contact-dependent inhibition of growth in Escherichia coli (2005)
    American Association for the Advancement of Science (AAAS)
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    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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    Prostaglandin E2 promotes colon cancer cell growth through a Gs-axin-beta-catenin signaling axis (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: How cyclooxygenase-2 (COX-2) and its proinflammatory metabolite prostaglandin E2 (PGE2) enhance colon cancer progression remains poorly understood. We show that PGE2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor, EP2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase Akt by free G protein betagamma subunits and the direct association of the G protein alphas subunit with the regulator of G protein signaling (RGS) domain of axin. This leads to the inactivation and release of glycogen synthase kinase 3beta from its complex with axin, thereby relieving the inhibitory phosphorylation of beta-catenin and activating its signaling pathway. These findings may provide a molecular framework for the future evaluation of chemopreventive strategies for colorectal cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castellone, Maria Domenica -- Teramoto, Hidemi -- Williams, Bart O -- Druey, Kirk M -- Gutkind, J Silvio -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1504-10. Epub 2005 Nov 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892-4340, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293724" target="_blank"〉PubMed〈/a〉
    Keywords: Axin Protein ; Cell Line ; Cell Proliferation ; Colonic Neoplasms/*pathology ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dinoprostone/*physiology ; GTP-Binding Protein alpha Subunits, Gs/*metabolism ; Genes, Reporter ; Humans ; RGS Proteins/metabolism ; Receptors, Prostaglandin E/metabolism ; Receptors, Prostaglandin E, EP2 Subtype ; Repressor Proteins/*metabolism ; *Signal Transduction ; beta Catenin/*metabolism
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    Structure of SARS coronavirus spike receptor-binding domain complexed with receptor (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection (2005)
    American Association for the Advancement of Science (AAAS)
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    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The beta-glucuronidase klotho hydrolyzes and activates the TRPV5 channel (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Structural insights into the activity of enhancer-binding proteins (2005)
    American Association for the Advancement of Science (AAAS)
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    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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    A strategy for probing the function of noncoding RNAs finds a repressor of NFAT (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Human embryonic stem cells (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilmut, Ian -- West, Michael D -- Lanza, Robert P -- Gearhart, John D -- Smith, Austin -- Colman, Alan -- Trounson, Alan O -- Campbell, Keith H -- New York, N.Y. -- Science. 2005 Dec 23;310(5756):1903. Epub 2005 Dec 13.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16352868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/cytology ; Cell Line ; *Cloning, Organism ; Embryo, Mammalian/*cytology ; Humans ; Nuclear Transfer Techniques ; *Stem Cells
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    A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA (2005)
    American Association for the Advancement of Science (AAAS)
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    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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    A transmembrane intracellular estrogen receptor mediates rapid cell signaling (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-12
    Description: The steroid hormone estrogen regulates many functionally unrelated processes in numerous tissues. Although it is traditionally thought to control transcriptional activation through the classical nuclear estrogen receptors, it also initiates many rapid nongenomic signaling events. We found that of all G protein-coupled receptors characterized to date, GPR30 is uniquely localized to the endoplasmic reticulum, where it specifically binds estrogen and fluorescent estrogen derivatives. Activating GPR30 by estrogen resulted in intracellular calcium mobilization and synthesis of phosphatidylinositol 3,4,5-trisphosphate in the nucleus. Thus, GPR30 represents an intracellular transmembrane estrogen receptor that may contribute to normal estrogen physiology as well as pathophysiology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Revankar, Chetana M -- Cimino, Daniel F -- Sklar, Larry A -- Arterburn, Jeffrey B -- Prossnitz, Eric R -- 1 S10 RR14668/RR/NCRR NIH HHS/ -- AI36357/AI/NIAID NIH HHS/ -- EB00264/EB/NIBIB NIH HHS/ -- P20 RR11830/RR/NCRR NIH HHS/ -- R24 CA88339/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1625-30. Epub 2005 Feb 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, University of New Mexico Health Sciences Center, Albuquerque, NM 87131, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15705806" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antisense Elements (Genetics) ; Calcium/metabolism ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; Endoplasmic Reticulum/*metabolism ; Estradiol/metabolism ; Estrogen Receptor alpha/metabolism ; Estrogens/*metabolism ; Humans ; Nuclear Envelope/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Protein Transport ; Receptor, Epidermal Growth Factor/metabolism ; Receptors, Estrogen/*metabolism ; Receptors, G-Protein-Coupled/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transfection
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    RNA polymerase IV directs silencing of endogenous DNA (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Cyberinfrastructure for e-Science (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-10
    Description: Here we describe the requirements of an e-Infrastructure to enable faster, better, and different scientific research capabilities. We use two application exemplars taken from the United Kingdom's e-Science Programme to illustrate these requirements and make the case for a service-oriented infrastructure. We provide a brief overview of the UK "plug-and-play composable services" vision and the role of semantics in such an e-Infrastructure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hey, Tony -- Trefethen, Anne E -- New York, N.Y. -- Science. 2005 May 6;308(5723):817-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Engineering and Physical Sciences Research Council, Polaris House, North Star Avenue, Swindon SN2 1ET, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879209" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Combinatorial Chemistry Techniques ; *Computational Biology ; *Computer Communication Networks ; *Computing Methodologies ; Databases as Topic ; Graves Disease/genetics ; *Internet ; *Research ; *Software ; Williams Syndrome/genetics
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    Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Reciprocal interference between specific CJD and scrapie agents in neural cell cultures (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Small CTD phosphatases function in silencing neuronal gene expression (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    TLR11 activation of dendritic cells by a protozoan profilin-like protein (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Crystal structure of human toll-like receptor 3 (TLR3) ectodomain (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Functional interaction between beta-catenin and FOXO in oxidative stress signaling (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    The floral regulator LEAFY evolves by substitutions in the DNA binding domain (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-04-12
    Description: The plant-specific transcription factor LEAFY controls general aspects of the life cycle in a basal plant, the moss Physcomitrella patens. In contrast, LEAFY has more specialized functions in angiosperms, where it specifically induces floral fate during the reproductive phase. This raises the question of a concomitant change in the biochemical function of LEAFY during the evolution of land plants. We report that the DNA binding domain of LEAFY, although largely conserved, has diverged in activity. On the contrary, other, more rapidly evolving portions of the protein have few effects on LEAFY activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maizel, Alexis -- Busch, Maximilian A -- Tanahashi, Takako -- Perkovic, Josip -- Kato, Masahiro -- Hasebe, Mitsuyasu -- Weigel, Detlef -- New York, N.Y. -- Science. 2005 Apr 8;308(5719):260-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Max Planck Institute for Developmental Biology, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15821093" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; DNA, Plant/metabolism ; *Evolution, Molecular ; Flowers/*growth & development ; Phylogeny ; Plant Proteins/*genetics/metabolism ; Plants/genetics ; Transcription Factors/*genetics/metabolism
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    Marine fish egg hydration is aquaporin-mediated (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    TAZ, a transcriptional modulator of mesenchymal stem cell differentiation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Stem cells. Cloning researcher says work is flawed but claims results stand (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- Vogel, Gretchen -- Holden, Constance -- New York, N.Y. -- Science. 2005 Dec 23;310(5756):1886-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16373544" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Cloning, Organism ; *Embryo Research ; Female ; Humans ; Korea ; Peer Review, Research ; Retraction of Publication as Topic ; *Stem Cells
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    Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-02
    Description: The existence of specialized molecular chaperones that interact directly with ribosomes is well established in microorganisms. Such proteins bind polypeptides exiting the ribosomal tunnel and provide a physical link between translation and protein folding. We report that ribosome-associated molecular chaperones have been maintained throughout eukaryotic evolution, as illustrated by Mpp11, the human ortholog of the yeast ribosome-associated J protein Zuo. When expressed in yeast, Mpp11 partially substituted for Zuo by partnering with the multipurpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multifunctional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hundley, Heather A -- Walter, William -- Bairstow, Shawn -- Craig, Elizabeth A -- R01GM031107/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 13;308(5724):1032-4. Epub 2005 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802566" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Substitution ; Binding Sites ; Cell Line ; DNA-Binding Proteins/chemistry/*metabolism ; HSC70 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/chemistry/*metabolism ; Oncogene Proteins/chemistry/*metabolism ; Potassium Chloride/pharmacology ; Protein Structure, Tertiary ; Ribosomes/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/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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    Virology. Culture systems for hepatitis C virus in sight at last (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1539-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947152" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Genes, Viral ; Hepacivirus/*genetics/*growth & development/isolation & purification ; Hepatitis C/virology ; Humans ; Liver ; Mutation ; RNA, Viral/genetics ; *Replicon ; Transfection ; Viral Nonstructural Proteins/genetics ; Virus Cultivation/*methods ; Virus Replication
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    Widespread parallel evolution in sticklebacks by repeated fixation of Ectodysplasin alleles (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: Major phenotypic changes evolve in parallel in nature by molecular mechanisms that are largely unknown. Here, we use positional cloning methods to identify the major chromosome locus controlling armor plate patterning in wild threespine sticklebacks. Mapping, sequencing, and transgenic studies show that the Ectodysplasin (EDA) signaling pathway plays a key role in evolutionary change in natural populations and that parallel evolution of stickleback low-plated phenotypes at most freshwater locations around the world has occurred by repeated selection of Eda alleles derived from an ancestral low-plated haplotype that first appeared more than two million years ago. Members of this clade of low-plated alleles are present at low frequencies in marine fish, which suggests that standing genetic variation can provide a molecular basis for rapid, parallel evolution of dramatic phenotypic change in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colosimo, Pamela F -- Hosemann, Kim E -- Balabhadra, Sarita -- Villarreal, Guadalupe Jr -- Dickson, Mark -- Grimwood, Jane -- Schmutz, Jeremy -- Myers, Richard M -- Schluter, Dolph -- Kingsley, David M -- 1P50HG02568/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1928-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305-5329, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790847" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; *Biological Evolution ; Body Patterning ; Chromosome Walking ; Cloning, Molecular ; Ectodysplasins ; Fresh Water ; Gene Frequency ; Genetic Variation ; Haplotypes ; Linkage Disequilibrium ; Membrane Proteins/*genetics/physiology ; Molecular Sequence Data ; Mutation ; Phenotype ; Phylogeny ; Polymorphism, Single Nucleotide ; Seawater ; Selection, Genetic ; Sequence Analysis, DNA ; Signal Transduction ; Smegmamorpha/*anatomy & histology/classification/*genetics/growth & development
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    Protein synthesis upon acute nutrient restriction relies on proteasome function (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-24
    Description: The mechanisms that protect mammalian cells against amino acid deprivation are only partially understood. We found that during an acute decrease in external amino acid supply, before up-regulation of the autophagosomal-lysosomal pathway, efficient translation was ensured by proteasomal protein degradation. Amino acids for the synthesis of new proteins were supplied by the degradation of preexisting proteins, whereas nascent and newly formed polypeptides remained largely protected from proteolysis. Proteasome inhibition during nutrient deprivation caused rapid amino acid depletion and marked impairment of translation. Thus, the proteasome plays a crucial role in cell survival after acute disruption of amino acid supply.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vabulas, Ramunas M -- Hartl, F Ulrich -- New York, N.Y. -- Science. 2005 Dec 23;310(5756):1960-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany. vabulas@biochem.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16373576" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*metabolism ; Azetidinecarboxylic Acid/metabolism ; Cell Line ; Green Fluorescent Proteins/genetics ; HeLa Cells ; Humans ; Proteasome Endopeptidase Complex/*physiology ; Proteasome Inhibitors ; Protein Biosynthesis/*physiology ; Protein Kinases/metabolism ; Ubiquitin/genetics
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    Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-04
    Description: Closely related signals often lead to very different cellular outcomes. We found that the differentiation of human mesenchymal stem cells into bone-forming cells is stimulated by epidermal growth factor (EGF) but not platelet-derived growth factor (PDGF). We used mass spectrometry-based proteomics to comprehensively compare proteins that were tyrosine phosphorylated in response to EGF and PDGF and their associated partners. More than 90% of these signaling proteins were used by both ligands, whereas the phosphatidylinositol 3-kinase (PI3K) pathway was exclusively activated by PDGF, implicating it as a possible control point. Indeed, chemical inhibition of PI3K in PDGF-stimulated cells removed the differential effect of the two growth factors, bestowing full differentiation effect onto PDGF. Thus, quantitative proteomics can directly compare entire signaling networks and discover critical differences capable of changing cell fate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kratchmarova, Irina -- Blagoev, Blagoy -- Haack-Sorensen, Mandana -- Kassem, Moustapha -- Mann, Matthias -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1472-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Experimental BioInformatics (CEBI), Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933201" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Differentiation ; Cell Line ; Epidermal Growth Factor/*physiology ; Fibroblast Growth Factors/physiology ; Humans ; MAP Kinase Signaling System ; Mesoderm/*cytology ; Nerve Growth Factor/physiology ; Osteoblasts/cytology ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/*physiology ; Proteins/metabolism ; Proteomics ; Signal Transduction ; Stem Cells/*cytology ; Tyrosine/metabolism
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    Computational thermostabilization of an enzyme (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-10
    Description: Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412875/" 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/PMC3412875/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korkegian, Aaron -- Black, Margaret E -- Baker, David -- Stoddard, Barry L -- CA85939/CA/NCI NIH HHS/ -- CA97328/CA/NCI NIH HHS/ -- GM49857/GM/NIGMS NIH HHS/ -- GM59224/GM/NIGMS NIH HHS/ -- R01 CA097328/CA/NCI NIH HHS/ -- R01 GM049857/GM/NIGMS NIH HHS/ -- T32-GM08268/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 6;308(5723):857-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center (FHCRC), 1100 Fairview Avenue North, Seattle, WA 98109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Catalysis ; Circular Dichroism ; *Computer Simulation ; Crystallography, X-Ray ; Cytosine Deaminase/*chemistry/*metabolism ; Enzyme Stability ; Escherichia coli/genetics/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Monte Carlo Method ; Mutagenesis, Site-Directed ; Point Mutation ; Protein Conformation ; Protein Denaturation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Software ; Temperature ; Thermodynamics ; Transformation, Genetic ; Yeasts/enzymology
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    Stem cells. Collaborators split over ethics allegations (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1100.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293726" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cloning, Organism/*ethics ; Cooperative Behavior ; Embryo Research/*ethics ; Female ; Humans ; Korea ; Oocytes/cytology ; Pennsylvania ; *Politics ; *Stem Cells ; Tissue and Organ Procurement/ethics
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    Suppression of aging in mice by the hormone Klotho (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-27
    Description: A defect in Klotho gene expression in mice accelerates the degeneration of multiple age-sensitive traits. Here, we show that overexpression of Klotho in mice extends life span. Klotho protein functions as a circulating hormone that binds to a cell-surface receptor and represses intracellular signals of insulin and insulin-like growth factor 1 (IGF1), an evolutionarily conserved mechanism for extending life span. Alleviation of aging-like phenotypes in Klotho-deficient mice was observed by perturbing insulin and IGF1 signaling, suggesting that Klotho-mediated inhibition of insulin and IGF1 signaling contributes to its anti-aging properties. Klotho protein may function as an anti-aging hormone in mammals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2536606/" 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/PMC2536606/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurosu, Hiroshi -- Yamamoto, Masaya -- Clark, Jeremy D -- Pastor, Johanne V -- Nandi, Animesh -- Gurnani, Prem -- McGuinness, Owen P -- Chikuda, Hirotaka -- Yamaguchi, Masayuki -- Kawaguchi, Hiroshi -- Shimomura, Iichiro -- Takayama, Yoshiharu -- Herz, Joachim -- Kahn, C Ronald -- Rosenblatt, Kevin P -- Kuro-o, Makoto -- R01 AG019712/AG/NIA NIH HHS/ -- R01 AG019712-05/AG/NIA NIH HHS/ -- R01 AG025326/AG/NIA NIH HHS/ -- R01 AG025326-03/AG/NIA NIH HHS/ -- R01AG19712/AG/NIA NIH HHS/ -- R01AG25326/AG/NIA NIH HHS/ -- R37 HL063762/HL/NHLBI NIH HHS/ -- U24 DK059637/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1829-33. Epub 2005 Aug 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Texas (UT) Southwestern Medical Center at Dallas, 5323 Harry Hines Bouleuvard, Dallas, TX 75390-9072, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16123266" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics/*physiology ; Animals ; Blood Glucose/analysis ; Cell Line ; Cell Line, Tumor ; Eating ; Female ; Glucuronidase ; Insulin/blood/metabolism ; Insulin Resistance ; Insulin-Like Growth Factor I/metabolism/pharmacology ; Ligands ; Longevity/genetics/*physiology ; Male ; Membrane Proteins/chemistry/*genetics/pharmacology/*physiology ; Mice ; Mice, Transgenic ; Myoblasts/metabolism ; Oxygen Consumption ; Peptide Fragments/chemistry/pharmacology ; Phosphorylation ; Receptor, IGF Type 1/metabolism ; Receptor, Insulin/metabolism ; Receptors, Cell Surface/metabolism ; Recombinant Proteins/chemistry/isolation & purification/metabolism ; Signal Transduction
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    Stem cells. Scientists chase after immortality in a petri dish (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-09-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2005 Sep 23;309(5743):1982-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16179446" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication ; Cell Differentiation ; Cell Line ; Cells, Cultured ; Embryo, Mammalian/*cytology ; Female ; Genomic Imprinting ; Humans ; Male ; Meiosis ; *Oocytes/cytology/physiology ; Ovary/cytology/physiology ; *Spermatozoa/cytology/physiology ; *Stem Cells/cytology/physiology ; Testis/cytology/physiology
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    Nuclear reprogramming of somatic cells after fusion with human embryonic stem cells (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-08-27
    Description: We have explored the use of embryonic stem cells as an alternative to oocytes for reprogramming human somatic nuclei. Human embryonic stem (hES) cells were fused with human fibroblasts, resulting in hybrid cells that maintain a stable tetraploid DNA content and have morphology, growth rate, and antigen expression patterns characteristic of hES cells. Differentiation of hybrid cells in vitro and in vivo yielded cell types from each embryonic germ layer. Analysis of genome-wide transcriptional activity, reporter gene activation, allele-specific gene expression, and DNA methylation showed that the somatic genome was reprogrammed to an embryonic state. These results establish that hES cells can reprogram the transcriptional state of somatic nuclei and provide a system for investigating the underlying mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cowan, Chad A -- Atienza, Jocelyn -- Melton, Douglas A -- Eggan, Kevin -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1369-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Harvard Stem Cell Institute, Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16123299" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Biomarkers/analysis ; Cell Cycle ; Cell Differentiation ; *Cell Fusion ; Cell Line ; Cell Nucleus/*physiology ; Cell Shape ; Cell Transplantation ; Chromosomes, Human/genetics ; Embryo, Mammalian/*cytology ; Epigenesis, Genetic ; Female ; Fibroblasts/cytology/*physiology ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Humans ; Hybrid Cells/cytology/*physiology ; Male ; Mice ; Mice, Nude ; Phenotype ; Pluripotent Stem Cells/cytology/*physiology ; Polyploidy ; Teratoma/pathology ; Transcription, Genetic ; Transcriptional Activation ; Transfection
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    Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: Apolipoprotein L-I is the trypanolytic factor of human serum. Here we show that this protein contains a membrane pore-forming domain functionally similar to that of bacterial colicins, flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein L-I formed anion channels. In Trypanosoma brucei, apolipoprotein L-I was targeted to the lysosomal membrane and triggered depolarization of this membrane, continuous influx of chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perez-Morga, David -- Vanhollebeke, Benoit -- Paturiaux-Hanocq, Francoise -- Nolan, Derek P -- Lins, Laurence -- Homble, Fabrice -- Vanhamme, Luc -- Tebabi, Patricia -- Pays, Annette -- Poelvoorde, Philippe -- Jacquet, Alain -- Brasseur, Robert -- Pays, Etienne -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):469-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Parasitology, IBMM, Universite Libre de Bruxelles, 12, rue des Profs Jeener et Brachet, B6041 Gosselies, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020735" target="_blank"〉PubMed〈/a〉
    Keywords: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid/pharmacology ; Amino Acid Sequence ; Animals ; Anions/metabolism ; Apolipoproteins/*chemistry/genetics/*metabolism/pharmacology ; Cells, Immobilized ; Chlorides/metabolism ; Colicins/chemistry/pharmacology ; Escherichia coli/drug effects/growth & development ; Humans ; Intracellular Membranes/drug effects/*metabolism/ultrastructure ; Ion Channels/metabolism ; Lipid Bilayers/chemistry ; Lipoproteins, HDL/*chemistry/genetics/*metabolism/pharmacology ; Lysosomes/drug effects/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Permeability ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/metabolism ; Trypanosoma brucei brucei/drug effects/*metabolism/ultrastructure
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    Antigen recognition determinants of gammadelta T cell receptors (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-12
    Description: The molecular basis of gammadelta T cell receptor (TCR) recognition is poorly understood. Here, we analyze the TCR sequences of a natural gammadelta T cell population specific for the major histocompatibility complex class Ib molecule T22. We find that T22 recognition correlates strongly with a somatically recombined TCRdelta complementarity-determining region 3 (CDR3) motif derived from germ line-encoded residues. Sequence diversity around these residues modulates TCR ligand-binding affinities, whereas V gene usage correlates mainly with tissue origin. These results show how an antigen-specific gammadelta TCR repertoire can be generated at a high frequency and suggest that gammadelta T cells recognize a limited number of antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shin, Sunny -- El-Diwany, Ramy -- Schaffert, Steven -- Adams, Erin J -- Garcia, K Christopher -- Pereira, Pablo -- Chien, Yueh-Hsiu -- AI33431/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 8;308(5719):252-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15821090" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens ; Binding Sites ; Gene Rearrangement, gamma-Chain T-Cell Antigen Receptor ; Histocompatibility Antigens Class I/*immunology ; Humans ; Jurkat Cells ; Ligands ; Protein Conformation ; Proteins/*immunology ; Receptors, Antigen, T-Cell, gamma-delta/genetics/*immunology ; T-Lymphocytes/*immunology
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    Treatment of autoimmune neuroinflammation with a synthetic tryptophan metabolite (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-08
    Description: Local catabolism of the amino acid tryptophan (Trp) by indoleamine 2,3-dioxygenase (IDO) is considered an important mechanism of regulating T cell immunity. We show that IDO transcription was increased when myelin-specific T cells were stimulated with tolerogenic altered self-peptides. Catabolites of Trp suppressed proliferation of myelin-specific T cells and inhibited production of proinflammatory T helper-1 (T(H)1) cytokines. N-(3,4,-Dimethoxycinnamoyl) anthranilic acid (3,4-DAA), an orally active synthetic derivative of the Trp metabolite anthranilic acid, reversed paralysis in mice with experimental autoimmune encephalomyelitis, a model of multiple sclerosis (MS). Trp catabolites and their derivatives offer a new strategy for treating T(H)1-mediated autoimmune diseases such as MS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Platten, Michael -- Ho, Peggy P -- Youssef, Sawsan -- Fontoura, Paulo -- Garren, Hideki -- Hur, Eun Mi -- Gupta, Rohit -- Lee, Lowen Y -- Kidd, Brian A -- Robinson, William H -- Sobel, Raymond A -- Selley, Michael L -- Steinman, Lawrence -- New York, N.Y. -- Science. 2005 Nov 4;310(5749):850-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Neurological Sciences, Beckman Center for Molecular Medicine, Stanford University, Stanford, CA 94305, USA. michael.platten@uni-tuebingen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16272121" target="_blank"〉PubMed〈/a〉
    Keywords: Adoptive Transfer ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/administration & ; dosage/pharmacology/*therapeutic use ; Antigen-Presenting Cells/drug effects/immunology ; Brain/pathology ; Cell Line ; Cytokines/biosynthesis ; Disease Models, Animal ; Encephalomyelitis, Autoimmune, Experimental/*drug therapy/immunology ; Female ; Histocompatibility Antigens Class II/immunology/metabolism ; Immune Tolerance ; Immunosuppressive Agents/pharmacology/therapeutic use ; Indoleamine-Pyrrole 2,3,-Dioxygenase/genetics/metabolism ; Interferon-gamma/immunology ; Lymphocyte Activation ; Mice ; Mice, Transgenic ; Microglia/drug effects/immunology ; Multiple Sclerosis/drug therapy/immunology/pathology ; Myelin Proteins/immunology ; Signal Transduction ; Spinal Cord/pathology ; T-Lymphocytes/immunology ; Th1 Cells/immunology ; Th2 Cells/immunology ; Tryptophan/*metabolism ; ortho-Aminobenzoates/administration & dosage/pharmacology/*therapeutic use
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    Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: Ubiquitination controls a broad range of cellular functions. The last step of the ubiquitination pathway is regulated by enzyme type 3 (E3) ubiquitin ligases. E3 enzymes are responsible for substrate specificity and catalyze the formation of an isopeptide bond between a lysine residue of the substrate (or the N terminus of the substrate) and ubiquitin. MIR1 and MIR2 are two E3 ubiquitin ligases encoded by Kaposi's sarcoma-associated herpesvirus that mediate the ubiquitination of major histocompatibility complex class I (MHC I) molecules and subsequent internalization. Here, we found that MIR1, but not MIR2, promoted down-regulation of MHC I molecules lacking lysine residues in their intracytoplasmic domain. In the presence of MIR1, these MHC I molecules were ubiquitinated, and their association with ubiquitin was sensitive to beta2-mercaptoethanol, unlike lysine-ubiquitin bonds. This form of ubiquitination required a cysteine residue in the intracytoplasmic tail of MHC I molecules. An MHC I molecule containing a single cysteine residue in an artificial glycine and alanine intracytoplasmic domain was endocytosed and degraded in the presence of MIR1. Thus, ubiquitination can occur on proteins lacking accessible lysines or an accessible N terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cadwell, Ken -- Coscoy, Laurent -- 1R01CA108447-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):127-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, 142 Life Sciences Addition Room 3200, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; CHO Cells ; Cell Line ; Cricetinae ; Cysteine/chemistry/metabolism ; Down-Regulation ; Endocytosis ; HLA-B7 Antigen/chemistry/genetics/*metabolism ; Herpesvirus 8, Human/*enzymology ; Humans ; Lysine/metabolism ; Mutation ; Protein Structure, Tertiary ; Serine/chemistry/metabolism ; Transduction, Genetic ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligases/*metabolism
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    Cell biology. Human embryonic stem cells may be toxicology's new best friends (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sinha, Gunjan -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1538.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947151" target="_blank"〉PubMed〈/a〉
    Keywords: Animal Testing Alternatives ; Animals ; Cell Differentiation ; Cell Line ; Embryo, Mammalian/*cytology ; Europe ; Hepatocytes ; Humans ; Myocytes, Cardiac ; *Stem Cells ; Toxicity Tests/*methods
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    A cellular microRNA mediates antiviral defense in human cells (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-04-23
    Description: In eukaryotes, 21- to 24-nucleotide-long RNAs engage in sequence-specific interactions that inhibit gene expression by RNA silencing. This process has regulatory roles involving microRNAs and, in plants and insects, it also forms the basis of a defense mechanism directed by small interfering RNAs that derive from replicative or integrated viral genomes. We show that a cellular microRNA effectively restricts the accumulation of the retrovirus primate foamy virus type 1 (PFV-1) in human cells. PFV-1 also encodes a protein, Tas, that suppresses microRNA-directed functions in mammalian cells and displays cross-kingdom antisilencing activities. Therefore, through fortuitous recognition of foreign nucleic acids, cellular microRNAs have direct antiviral effects in addition to their regulatory functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lecellier, Charles-Henri -- Dunoyer, Patrice -- Arar, Khalil -- Lehmann-Che, Jacqueline -- Eyquem, Stephanie -- Himber, Christophe -- Saib, Ali -- Voinnet, Olivier -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):557-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS Unite Propre de Recherche (UPR) 2357, Institut de Biologie Moleculaire des Plantes, 12 rue du General Zimmer, 67084 Strasbourg Cedex, France. charles.lecellier@infobiogen.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15845854" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiviral Agents/*physiology ; Arabidopsis/genetics ; Cell Line ; Cricetinae ; DNA-Binding Proteins/genetics/metabolism ; Genes, Reporter ; Green Fluorescent Proteins/genetics ; HeLa Cells ; Humans ; MicroRNAs/*physiology ; Oligonucleotides, Antisense ; Plants, Genetically Modified ; Protein Biosynthesis ; *RNA Interference ; RNA, Viral ; Retroviridae Proteins/genetics/metabolism ; Spumavirus/*genetics/*physiology ; Trans-Activators/genetics/metabolism ; Transfection ; Virus Replication
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    RNA polymerase II is required for RNAi-dependent heterochromatin assembly (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-11
    Description: In Schizosaccharomyces pombe, the RNA interference (RNAi) machinery converts pericentromeric transcripts into small interfering RNAs (siRNAs) and is required for the assembly of pericentromeric heterochromatin. Here we describe a mutation in the second largest subunit of RNA polymerase II (RNAPII). Both wild-type and mutant RNAPII localized to the pericentromere. However, the mutation resulted in the loss of heterochromatic histone modifications and in the accumulation of pericentromeric transcripts, accompanied by the loss of siRNAs. This phenotype resembles mutants in RNAi and suggests that RNAPII couples pericentromeric transcription with siRNA processing and heterochromatin assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kato, Hiroaki -- Goto, Derek B -- Martienssen, Robert A -- Urano, Takeshi -- Furukawa, Koichi -- Murakami, Yota -- R01-GM067014/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):467-9. Epub 2005 Jun 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Viral Oncology, Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947136" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Centromere/metabolism ; Chromosome Segregation ; Gene Expression Regulation, Fungal ; Heterochromatin/*metabolism ; Histones/metabolism ; Methylation ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Point Mutation ; *RNA Interference ; RNA Polymerase II/chemistry/genetics/*metabolism ; RNA, Fungal/metabolism ; RNA, Messenger/metabolism ; RNA, Small Interfering/*metabolism ; Schizosaccharomyces/enzymology/genetics/*metabolism ; Transcription, Genetic
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    NSP1 of the GRAS protein family is essential for rhizobial Nod factor-induced transcription (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-18
    Description: Rhizobial Nod factors induce in their legume hosts the expression of many genes and set in motion developmental processes leading to root nodule formation. Here we report the identification of the Medicago GRAS-type protein Nodulation signaling pathway 1 (NSP1), which is essential for all known Nod factor-induced changes in gene expression. NSP1 is constitutively expressed, and so it acts as a primary transcriptional regulator mediating all known Nod factor-induced transcriptional responses, and therefore, we named it a Nod factor response factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smit, Patrick -- Raedts, John -- Portyanko, Vladimir -- Debelle, Frederic -- Gough, Clare -- Bisseling, Ton -- Geurts, Rene -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Science, Laboratory of Molecular Biology, Wageningen University, Wageningen 6703 HA, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961669" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; 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 ; Plant Proteins/chemistry/genetics/*metabolism ; Plant Roots/metabolism/microbiology ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; Signal Transduction ; Sinorhizobium meliloti/*physiology ; Symbiosis ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic
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    Orphan enzymes? (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-01-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lespinet, Olivier -- Labedan, Bernard -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637255" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Databases, Protein ; Enzymes/*chemistry/classification/metabolism
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    A role for the phagosome in cytokine secretion (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-11-12
    Description: Membrane traffic in activated macrophages is required for two critical events in innate immunity: proinflammatory cytokine secretion and phagocytosis of pathogens. We found a joint trafficking pathway linking both actions, which may economize membrane transport and augment the immune response. Tumor necrosis factor alpha (TNFalpha) is trafficked from the Golgi to the recycling endosome (RE), where vesicle-associated membrane protein 3 mediates its delivery to the cell surface at the site of phagocytic cup formation. Fusion of the RE at the cup simultaneously allows rapid release of TNFalpha and expands the membrane for phagocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murray, Rachael Z -- Kay, Jason G -- Sangermani, Daniele G -- Stow, Jennifer L -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1492-5. Epub 2005 Nov 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16282525" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Candida albicans/immunology ; Cell Line ; Cell Membrane/metabolism ; Cytoplasmic Vesicles/metabolism ; Endosomes/metabolism ; Interferon-gamma/metabolism ; Macrophage Activation ; Macrophages/immunology/*secretion ; Mice ; Phagocytosis ; Phagosomes/*physiology ; Qa-SNARE Proteins/metabolism ; Tumor Necrosis Factor-alpha/*secretion ; Vesicle-Associated Membrane Protein 3/physiology ; rab GTP-Binding Proteins/biosynthesis
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    Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-02
    Description: The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murata, Takeshi -- Yamato, Ichiro -- Kakinuma, Yoshimi -- Leslie, Andrew G W -- Walker, John E -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):654-9. Epub 2005 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802565" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Detergents/metabolism ; Enterococcus/*enzymology ; Ion Transport ; Models, Biological ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Molecular Sequence Data ; Phospholipids/chemistry/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Sodium/metabolism ; Static Electricity ; Water
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    Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-15
    Description: Enhancer of Zeste homolog 2 (EZH2) is a methyltransferase that plays an important role in many biological processes through its ability to trimethylate lysine 27 in histone H3. Here, we show that Akt phosphorylates EZH2 at serine 21 and suppresses its methyltransferase activity by impeding EZH2 binding to histone H3, which results in a decrease of lysine 27 trimethylation and derepression of silenced genes. Our results imply that Akt regulates the methylation activity, through phosphorylation of EZH2, which may contribute to oncogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cha, Tai-Lung -- Zhou, Binhua P -- Xia, Weiya -- Wu, Yadi -- Yang, Cheng-Chieh -- Chen, Chun-Te -- Ping, Bo -- Otte, Arie P -- Hung, Mien-Chie -- P01 099031/PHS HHS/ -- R01 109311/PHS HHS/ -- New York, N.Y. -- Science. 2005 Oct 14;310(5746):306-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Oncology, the University of Texas M. D. Anderson Cancer Center, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16224021" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; COS Cells ; Cell Line ; Cell Transformation, Neoplastic ; Cercopithecus aethiops ; Chromones/pharmacology ; DNA-Binding Proteins ; Enzyme Inhibitors/pharmacology ; Gene Expression Regulation ; HeLa Cells ; Histone-Lysine N-Methyltransferase/metabolism ; Histones/*metabolism ; Homeodomain Proteins/genetics ; Humans ; Lysine/*metabolism ; Methylation ; Mice ; Molecular Sequence Data ; Morpholines/pharmacology ; Phosphorylation ; Polycomb Repressive Complex 2 ; Protein Binding ; Protein Methyltransferases ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/*metabolism ; Proteins/*metabolism ; Proto-Oncogene Proteins/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins c-akt ; Serine/metabolism ; Transcription Factors
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    A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-10
    Description: Focal and segmental glomerulosclerosis (FSGS) is a kidney disorder of unknown etiology, and up to 20% of patients on dialysis have been diagnosed with it. Here we show that a large family with hereditary FSGS carries a missense mutation in the TRPC6 gene on chromosome 11q, encoding the ion-channel protein transient receptor potential cation channel 6 (TRPC6). The proline-to-glutamine substitution at position 112, which occurs in a highly conserved region of the protein, enhances TRPC6-mediated calcium signals in response to agonists such as angiotensin II and appears to alter the intracellular distribution of TRPC6 protein. Previous work has emphasized the importance of cytoskeletal and structural proteins in proteinuric kidney diseases. Our findings suggest an alternative mechanism for the pathogenesis of glomerular disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winn, Michelle P -- Conlon, Peter J -- Lynn, Kelvin L -- Farrington, Merry Kay -- Creazzo, Tony -- Hawkins, April F -- Daskalakis, Nikki -- Kwan, Shu Ying -- Ebersviller, Seth -- Burchette, James L -- Pericak-Vance, Margaret A -- Howell, David N -- Vance, Jeffery M -- Rosenberg, Paul B -- R01 DK074748/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1801-4. Epub 2005 May 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA. michelle.winn@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879175" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Angiotensin II/metabolism/pharmacology ; Calcium/metabolism ; Calcium Channels/chemistry/*genetics/metabolism ; Calcium Signaling ; Carbachol/pharmacology ; Cell Line ; Cell Membrane/metabolism ; Chromosomes, Human, Pair 11/genetics ; Exons ; Female ; GTP-Binding Protein alpha Subunits, Gq-G11/metabolism ; Glomerulosclerosis, Focal Segmental/*genetics ; Haplotypes ; Humans ; Kidney/metabolism ; Kidney Glomerulus/metabolism ; Kidney Tubules/metabolism ; Male ; *Mutation, Missense ; Patch-Clamp Techniques ; Pedigree ; Receptor, Angiotensin, Type 1/genetics/metabolism ; Sequence Analysis, DNA ; Sodium/metabolism ; TRPC Cation Channels ; Transfection ; Uridine Triphosphate/metabolism/pharmacology
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    SMEDWI-2 is a PIWI-like protein that regulates planarian stem cells (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-29
    Description: We have identified two genes, smedwi-1 and smedwi-2, expressed in the dividing adult stem cells (neoblasts) of the planarian Schmidtea mediterranea. Both genes encode proteins that belong to the Argonaute/PIWI protein family and that share highest homology with those proteins defined by Drosophila PIWI. RNA interference (RNAi) of smedwi-2 blocks regeneration, even though neoblasts are present, irradiation-sensitive, and capable of proliferating in response to wounding; smedwi-2(RNAi) neoblast progeny migrate to sites of cell turnover but, unlike normal cells, fail at replacing aged tissue. We suggest that SMEDWI-2 functions within dividing neoblasts to support the generation of cells that promote regeneration and homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddien, Peter W -- Oviedo, Nestor J -- Jennings, Joya R -- Jenkin, James C -- Sanchez Alvarado, Alejandro -- R0-1 GM57260/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 25;310(5752):1327-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Neurobiology and Anatomy, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16311336" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Count ; Cell Differentiation ; Cell Division ; Cell Movement ; Cell Separation ; Cell Shape ; Cyclin B/genetics ; Flow Cytometry ; Gene Expression ; *Genes, Helminth ; Helminth Proteins/genetics/*physiology ; Homeostasis ; Mitosis ; Molecular Sequence Data ; Phenotype ; Planarians/chemistry/*cytology/genetics/*physiology ; RNA Interference ; Regeneration ; Stem Cells/cytology/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Dependence of olfactory bulb neurogenesis on prokineticin 2 signaling (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-25
    Description: Neurogenesis persists in the olfactory bulb (OB) of the adult mammalian brain. New interneurons are continually added to the OB from the subventricular zone (SVZ) via the rostral migratory stream (RMS). Here we show that secreted prokineticin 2 (PK2) functions as a chemoattractant for SVZ-derived neuronal progenitors. Within the OB, PK2 may also act as a detachment signal for chain-migrating progenitors arriving from the RMS. PK2 deficiency in mice leads to a marked reduction in OB size, loss of normal OB architecture, and the accumulation of neuronal progenitors in the RMS. These findings define an essential role for G protein-coupled PK2 signaling in postnatal and adult OB neurogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ng, Kwan L -- Li, Jia-Da -- Cheng, Michelle Y -- Leslie, Frances M -- Lee, Alex G -- Zhou, Qun-Yong -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1923-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California-Irvine (UCI), Irvine, CA 92697, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976302" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Brain/cytology/growth & development/metabolism ; Cell Adhesion ; Cell Count ; Cell Line ; Cell Proliferation ; Cerebral Ventricles/cytology/*physiology ; Chemotactic Factors/physiology ; Chemotaxis ; Coculture Techniques ; Dopamine/physiology ; Gastrointestinal Hormones/*metabolism ; Gene Expression ; Interneurons/cytology/*physiology ; Mice ; Mice, Inbred C57BL ; Neurons/cytology/*physiology ; Neuropeptides/*metabolism ; Olfactory Bulb/*cytology/growth & development/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, G-Protein-Coupled/genetics/metabolism ; *Signal Transduction ; Stem Cells/*physiology
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    Recognition of host immune activation by Pseudomonas aeruginosa (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-30
    Description: It is generally reasoned that lethal infections caused by opportunistic pathogens develop permissively by invading a host that is both physiologically stressed and immunologically compromised. However, an alternative hypothesis might be that opportunistic pathogens actively sense alterations in host immune function and respond by enhancing their virulence phenotype. We demonstrate that interferon-gamma binds to an outer membrane protein in Pseudomonas aeruginosa, OprF, resulting in the expression of a quorum-sensing dependent virulence determinant, the PA-I lectin. These observations provide details of the mechanisms by which prokaryotic organisms are directly signaled by immune activation in their eukaryotic host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Licheng -- Estrada, Oscar -- Zaborina, Olga -- Bains, Manjeet -- Shen, Le -- Kohler, Jonathan E -- Patel, Nachiket -- Musch, Mark W -- Chang, Eugene B -- Fu, Yang-Xin -- Jacobs, Michael A -- Nishimura, Michael I -- Hancock, Robert E W -- Turner, Jerrold R -- Alverdy, John C -- 2-RO1 GM062344-05/GM/NIGMS NIH HHS/ -- DK-38510/DK/NIDDK NIH HHS/ -- DK-47722/DK/NIDDK NIH HHS/ -- R01DK61931/DK/NIDDK NIH HHS/ -- R01DK68271/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):774-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, University of Chicago, Pritzker School of Medicine, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051797" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/*biosynthesis ; Animals ; Cell Line ; Cell Line, Tumor ; Cells, Cultured ; Cytokines/immunology/metabolism/pharmacology ; Humans ; Interferon-gamma/immunology/*metabolism/pharmacology ; Lectins/*biosynthesis ; Lymphocyte Activation ; Porins/isolation & purification/*metabolism ; Protein Binding ; Pseudomonas aeruginosa/growth & development/*immunology/metabolism/*pathogenicity ; Pyocyanine/biosynthesis ; Recombinant Proteins/pharmacology ; Signal Transduction ; T-Lymphocytes/*immunology ; Up-Regulation ; Virulence
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Divergent immunoglobulin g subclass activity through selective Fc receptor binding (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-03
    Description: Subclasses of immunoglobulin G (IgG) display substantial differences in their ability to mediate effector responses, contributing to variable activity of antibodies against microbes and tumors. We demonstrate that the mechanism underlying this long-standing observation of subclass dominance in function is provided by the differential affinities of IgG subclasses for specific activating IgG Fc receptors compared with their affinities for the inhibitory IgG Fc receptor. The significant differences in the ratios of activating-to-inhibitory receptor binding predicted the in vivo activity. We suggest that these highly predictable functions assigned by Fc binding will be an important consideration in the design of therapeutic antibodies and vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nimmerjahn, Falk -- Ravetch, Jeffrey V -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1510-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322460" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Platelets/immunology ; Cell Line ; Female ; Immunoglobulin G/*immunology/*metabolism ; Melanosomes/immunology ; Mice ; Mice, Inbred C57BL ; Protein Binding ; Receptors, IgG/classification/*metabolism
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    Control of excitatory and inhibitory synapse formation by neuroligins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-01
    Description: The normal function of neural networks depends on a delicate balance between excitatory and inhibitory synaptic inputs. Synapse formation is thought to be regulated by bidirectional signaling between pre- and postsynaptic cells. We demonstrate that members of the Neuroligin family promote postsynaptic differentiation in cultured rat hippocampal neurons. Down-regulation of neuroligin isoform expression by RNA interference results in a loss of excitatory and inhibitory synapses. Electrophysiological analysis revealed a predominant reduction of inhibitory synaptic function. Thus, neuroligins control the formation and functional balance of excitatory and inhibitory synapses in hippocampal neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chih, Ben -- Engelman, Holly -- Scheiffele, Peter -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1324-8. Epub 2005 Jan 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Cellular Biophysics, Center for Neurobiology and Behavior, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681343" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Cell Adhesion Molecules, Neuronal ; Cell Line ; Cells, Cultured ; Dendrites/physiology/ultrastructure ; Down-Regulation ; Evoked Potentials ; Excitatory Postsynaptic Potentials ; Hippocampus/cytology ; Membrane Proteins/genetics/*metabolism ; Membrane Transport Proteins/metabolism ; Mutation ; Nerve Tissue Proteins/genetics/*metabolism ; Neural Inhibition ; Neurons/physiology ; Presynaptic Terminals/*physiology ; Protein Isoforms ; RNA Interference ; Rats ; Receptors, AMPA/metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/*physiology ; Synaptic Membranes/*physiology ; Synaptic Transmission ; Transfection ; Vesicular Glutamate Transport Protein 1 ; Vesicular Inhibitory Amino Acid Transport Proteins
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    An acylation cycle regulates localization and activity of palmitoylated Ras isoforms (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-12
    Description: We show that the specific subcellular distribution of H- and Nras guanosine triphosphate-binding proteins is generated by a constitutive de/reacylation cycle that operates on palmitoylated proteins, driving their rapid exchange between the plasma membrane (PM) and the Golgi apparatus. Depalmitoylation redistributes farnesylated Ras in all membranes, followed by repalmitoylation and trapping of Ras at the Golgi, from where it is redirected to the PM via the secretory pathway. This continuous cycle prevents Ras from nonspecific residence on endomembranes, thereby maintaining the specific intracellular compartmentalization. The de/reacylation cycle also initiates Ras activation at the Golgi by transport of PM-localized Ras guanosine triphosphate. Different de/repalmitoylation kinetics account for isoform-specific activation responses to growth factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rocks, Oliver -- Peyker, Anna -- Kahms, Martin -- Verveer, Peter J -- Koerner, Carolin -- Lumbierres, Maria -- Kuhlmann, Jurgen -- Waldmann, Herbert -- Wittinghofer, Alfred -- Bastiaens, Philippe I H -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1746-52. Epub 2005 Feb 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Max Planck Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15705808" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Animals ; COS Cells ; Cell Line ; Cell Membrane/*metabolism ; Cercopithecus aethiops ; Dogs ; Golgi Apparatus/*metabolism ; Guanosine Triphosphate/metabolism ; Kinetics ; Models, Biological ; Molecular Sequence Data ; Palmitic Acid/*metabolism ; Protein Isoforms/chemistry/metabolism ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Protein Transport ; Proto-Oncogene Proteins p21(ras)/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    Ethics. Issues in oocyte donation for stem cell research (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Magnus, David -- Cho, Mildred K -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1747-8. Epub 2005 May 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford Center for Biomedical Ethics and Department of Pediatrics, Stanford University, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905363" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Embryo Research/*ethics ; Embryo, Mammalian/cytology ; Ethics Committees, Research ; Ethics, Research ; Female ; Humans ; Informed Consent ; International Cooperation ; Oocyte Donation/*ethics ; Oocytes ; Patient Selection/ethics ; Publishing/ethics ; Research Embryo Creation/ethics ; *Research Subjects ; Risk ; *Stem Cells ; Tissue Donors/*ethics ; United States
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    High-throughput mapping of a dynamic signaling network in mammalian cells (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: Signaling pathways transmit information through protein interaction networks that are dynamically regulated by complex extracellular cues. We developed LUMIER (for luminescence-based mammalian interactome mapping), an automated high-throughput technology, to map protein-protein interaction networks systematically in mammalian cells and applied it to the transforming growth factor-beta (TGFbeta) pathway. Analysis using self-organizing maps and k-means clustering identified links of the TGFbeta pathway to the p21-activated kinase (PAK) network, to the polarity complex, and to Occludin, a structural component of tight junctions. We show that Occludin regulates TGFbeta type I receptor localization for efficient TGFbeta-dependent dissolution of tight junctions during epithelial-to-mesenchymal transitions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrios-Rodiles, Miriam -- Brown, Kevin R -- Ozdamar, Barish -- Bose, Rohit -- Liu, Zhong -- Donovan, Robert S -- Shinjo, Fukiko -- Liu, Yongmei -- Dembowy, Joanna -- Taylor, Ian W -- Luga, Valbona -- Przulj, Natasa -- Robinson, Mark -- Suzuki, Harukazu -- Hayashizaki, Yoshihide -- Jurisica, Igor -- Wrana, Jeffrey L -- P50 GM-62413/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1621-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada, M5G 1X5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761153" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/metabolism ; Animals ; Cell Line ; Cell Polarity ; DNA-Binding Proteins/metabolism ; Epithelial Cells/cytology/physiology ; Humans ; Immunoprecipitation ; Luciferases ; Membrane Proteins/metabolism ; Mesoderm/cytology ; Mice ; Occludin ; Phosphorylation ; *Protein Interaction Mapping ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Transforming Growth Factor beta/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Smad2 Protein ; Smad4 Protein ; Tight Junctions/ultrastructure ; Trans-Activators/metabolism ; Transforming Growth Factor beta/*metabolism ; p21-Activated Kinases
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    Obestatin, a peptide encoded by the ghrelin gene, opposes ghrelin's effects on food intake (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-11-15
    Description: Ghrelin, a circulating appetite-inducing hormone, is derived from a prohormone by posttranslational processing. On the basis of the bioinformatic prediction that another peptide also derived from proghrelin exists, we isolated a hormone from rat stomach and named it obestatin-a contraction of obese, from the Latin "obedere," meaning to devour, and "statin," denoting suppression. Contrary to the appetite-stimulating effects of ghrelin, treatment of rats with obestatin suppressed food intake, inhibited jejunal contraction, and decreased body-weight gain. Obestatin bound to the orphan G protein-coupled receptor GPR39. Thus, two peptide hormones with opposing action in weight regulation are derived from the same ghrelin gene. After differential modification, these hormones activate distinct receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Jian V -- Ren, Pei-Gen -- Avsian-Kretchmer, Orna -- Luo, Ching-Wei -- Rauch, Rami -- Klein, Cynthia -- Hsueh, Aaron J W -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):996-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Reproductive Biology, Department of Obstetrics and Gynecology, Stanford University School of Medicine, Stanford, CA 94305-5317, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284174" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Computational Biology ; Conserved Sequence ; Cricetinae ; *Eating/drug effects ; Fasting ; Gastric Emptying/drug effects ; Gastrointestinal Motility/drug effects ; Ghrelin ; Humans ; In Vitro Techniques ; Ligands ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptide Hormones/blood/chemistry/*genetics/metabolism/pharmacology/*physiology ; Protein Binding ; Protein Precursors/*genetics ; Radioimmunoassay ; Rats ; Rats, Sprague-Dawley ; Receptors, G-Protein-Coupled/metabolism ; Receptors, Ghrelin ; Signal Transduction ; Weight Gain/drug effects
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    Golgin tethers define subpopulations of COPI vesicles (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-19
    Description: Coiled-coil proteins of the golgin family have been implicated in intra-Golgi transport through tethering coat protein complex I (COPI) vesicles. The p115-golgin tether is the best studied, and here we characterize the golgin-84-CASP tether. The vesicles bound by this tether were strikingly different from those bound by the p115-golgin tether in that they lacked members of the p24 family of putative cargo receptors and contained enzymes instead of anterograde cargo. Microinjected golgin-84 or CASP also inhibited Golgi-enzyme transport to the endoplasmic reticulum, further implicating this tether in retrograde transport. These and other golgins may modulate the flow patterns within the Golgi stack.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malsam, Jorg -- Satoh, Ayano -- Pelletier, Laurence -- Warren, Graham -- New York, N.Y. -- Science. 2005 Feb 18;307(5712):1095-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15718469" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantigens/*metabolism ; Binding, Competitive ; COP-Coated Vesicles/*metabolism ; Cell Fractionation ; Cell Line ; Cytoskeletal Proteins/*metabolism ; DNA-Binding Proteins ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/chemistry/enzymology/*metabolism ; Humans ; Immunoprecipitation ; Membrane Glycoproteins/metabolism ; Membrane Proteins/*metabolism ; Microscopy, Electron ; Protein Transport ; Rats ; Recombinant Fusion Proteins/metabolism ; Transcription Factors ; Viral Envelope Proteins/metabolism
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    Parallel patterns of evolution in the genomes and transcriptomes of humans and chimpanzees (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-06
    Description: The determination of the chimpanzee genome sequence provides a means to study both structural and functional aspects of the evolution of the human genome. Here we compare humans and chimpanzees with respect to differences in expression levels and protein-coding sequences for genes active in brain, heart, liver, kidney, and testis. We find that the patterns of differences in gene expression and gene sequences are markedly similar. In particular, there is a gradation of selective constraints among the tissues so that the brain shows the least differences between the species whereas liver shows the most. Furthermore, expression levels as well as amino acid sequences of genes active in more tissues have diverged less between the species than have genes active in fewer tissues. In general, these patterns are consistent with a model of neutral evolution with negative selection. However, for X-chromosomal genes expressed in testis, patterns suggestive of positive selection on sequence changes as well as expression changes are seen. Furthermore, although genes expressed in the brain have changed less than have genes expressed in other tissues, in agreement with previous work we find that genes active in brain have accumulated more changes on the human than on the chimpanzee lineage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khaitovich, Philipp -- Hellmann, Ines -- Enard, Wolfgang -- Nowick, Katja -- Leinweber, Marcus -- Franz, Henriette -- Weiss, Gunter -- Lachmann, Michael -- Paabo, Svante -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1850-4. Epub 2005 Sep 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Evolutionary Anthropology, Deutscher Platz 6, D-04103 Leipzig, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16141373" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Amino Acid Sequence ; Animals ; Base Sequence ; Child ; Chromosomes, Human, X/genetics ; Chromosomes, Mammalian/genetics ; *Evolution, Molecular ; Female ; *Gene Expression ; Gene Expression Profiling ; Gene Expression Regulation ; *Genome ; *Genome, Human ; Heart/physiology ; Humans ; Kidney/physiology ; Liver/physiology ; Male ; Middle Aged ; Models, Genetic ; Oligonucleotide Array Sequence Analysis ; Organ Specificity ; Pan troglodytes/*genetics ; Prefrontal Cortex/physiology ; Promoter Regions, Genetic ; Proteins/genetics ; Selection, Genetic ; Sequence Analysis, DNA ; Species Specificity ; Testis/physiology ; *Transcription, Genetic ; X Chromosome/genetics
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    Structure of a V3-containing HIV-1 gp120 core (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-11-15
    Description: The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is immunodominant and contains features essential for coreceptor binding. We determined the structure of V3 in the context of an HIV-1 gp120 core complexed to the CD4 receptor and to the X5 antibody at 3.5 angstrom resolution. Binding of gp120 to cell-surface CD4 would position V3 so that its coreceptor-binding tip protrudes 30 angstroms from the core toward the target cell membrane. The extended nature and antibody accessibility of V3 explain its immunodominance. Together, the results provide a structural rationale for the role of V3 in HIV entry and neutralization.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2408531/" 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/PMC2408531/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Chih-chin -- Tang, Min -- Zhang, Mei-Yun -- Majeed, Shahzad -- Montabana, Elizabeth -- Stanfield, Robyn L -- Dimitrov, Dimiter S -- Korber, Bette -- Sodroski, Joseph -- Wilson, Ian A -- Wyatt, Richard -- Kwong, Peter D -- AI24755/AI/NIAID NIH HHS/ -- AI31783/AI/NIAID NIH HHS/ -- AI39429/AI/NIAID NIH HHS/ -- AI40895/AI/NIAID NIH HHS/ -- GM46192/GM/NIGMS NIH HHS/ -- Z99 AI999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):1025-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD4/chemistry/*metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; HIV Antibodies/immunology ; HIV Envelope Protein gp120/*chemistry/immunology/metabolism ; HIV-1/*chemistry/immunology/metabolism ; Humans ; Hydrogen Bonding ; Immunodominant Epitopes ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments/*chemistry/immunology/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, CCR5/chemistry/metabolism ; Receptors, CXCR4/chemistry/metabolism
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    Cell biology. Wnt signaling glows with RNAi (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fearon, Eric R -- Cadigan, Ken M -- New York, N.Y. -- Science. 2005 May 6;308(5723):801-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Center, University of Michigan, Ann Arbor, MI 48109, USA. fearon@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879199" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cytoskeletal Proteins/metabolism ; Drosophila Proteins/*metabolism ; Drosophila melanogaster/*genetics/metabolism ; *Gene Expression Regulation ; Genes, Insect ; Genes, Reporter ; *Genomics ; Intercellular Signaling Peptides and Proteins/metabolism ; Models, Biological ; Mutation ; Phosphorylation ; Proto-Oncogene Proteins/*metabolism ; *RNA Interference ; RNA, Double-Stranded/genetics/metabolism ; *Signal Transduction ; Trans-Activators/metabolism ; Transcription Factors/genetics/metabolism ; Wings, Animal/metabolism ; Wnt Proteins ; Wnt1 Protein ; beta Catenin
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    Small-molecule inhibitor of Vibrio cholerae virulence and intestinal colonization (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-15
    Description: Increasing antibiotic resistance requires the development of new approaches to combating infection. Virulence gene expression in vivo represents a target for antibiotic discovery that has not yet been explored. A high-throughput, phenotypic screen was used to identify a small molecule 4-[N-(1,8-naphthalimide)]-n-butyric acid, virstatin, that inhibits virulence regulation in Vibrio cholerae. By inhibiting the transcriptional regulator ToxT, virstatin prevents expression of two critical V. cholerae virulence factors, cholera toxin and the toxin coregulated pilus. Orogastric administration of virstatin protects infant mice from intestinal colonization by V. cholerae.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hung, Deborah T -- Shakhnovich, Elizabeth A -- Pierson, Emily -- Mekalanos, John J -- AI26289/AI/NIAID NIH HHS/ -- K08 AI060708-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):670-4. Epub 2005 Oct 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA. dhung@partners.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16223984" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/*pharmacology ; Bacterial Proteins/biosynthesis/drug effects ; Butyrates/*pharmacology ; Cell Line ; Cholera/microbiology ; Cholera Toxin/biosynthesis ; Fimbriae, Bacterial/drug effects ; Gene Expression Regulation, Bacterial/drug effects ; Intestine, Small/*microbiology ; Mice ; Microbial Sensitivity Tests ; Naphthalenes/*pharmacology ; Naphthalimides ; Transcription Factors/biosynthesis/drug effects ; Vibrio cholerae/*drug effects/pathogenicity ; Virulence/drug effects ; Virulence Factors/biosynthesis
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    An aneuploid mouse strain carrying human chromosome 21 with Down syndrome phenotypes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-24
    Description: Aneuploidies are common chromosomal defects that result in growth and developmental deficits and high levels of lethality in humans. To gain insight into the biology of aneuploidies, we manipulated mouse embryonic stem cells and generated a trans-species aneuploid mouse line that stably transmits a freely segregating, almost complete human chromosome 21 (Hsa21). This "transchromosomic" mouse line, Tc1, is a model of trisomy 21, which manifests as Down syndrome (DS) in humans, and has phenotypic alterations in behavior, synaptic plasticity, cerebellar neuronal number, heart development, and mandible size that relate to human DS. Transchromosomic mouse lines such as Tc1 may represent useful genetic tools for dissecting other human aneuploidies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1378183/" 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/PMC1378183/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Doherty, Aideen -- Ruf, Sandra -- Mulligan, Claire -- Hildreth, Victoria -- Errington, Mick L -- Cooke, Sam -- Sesay, Abdul -- Modino, Sonie -- Vanes, Lesley -- Hernandez, Diana -- Linehan, Jacqueline M -- Sharpe, Paul T -- Brandner, Sebastian -- Bliss, Timothy V P -- Henderson, Deborah J -- Nizetic, Dean -- Tybulewicz, Victor L J -- Fisher, Elizabeth M C -- 076700/Wellcome Trust/United Kingdom -- MC_U117512674/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Sep 23;309(5743):2033-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurodegenerative Disease, Institute of Neurology, Queen Square, London WC1N 3BG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16179473" target="_blank"〉PubMed〈/a〉
    Keywords: *Aneuploidy ; Animals ; Behavior, Animal ; Brain/pathology ; Cell Count ; Cell Line ; Chimera ; *Chromosomes, Human, Pair 21 ; *Disease Models, Animal ; *Down Syndrome/genetics/physiopathology ; Embryo, Mammalian/cytology ; Facial Bones/pathology ; Female ; Gene Expression ; *Genetic Engineering ; Genetic Markers ; Heart Defects, Congenital/embryology ; Hippocampus/physiopathology ; Humans ; Long-Term Potentiation ; Lymphocyte Activation ; Male ; Maze Learning ; Memory ; Mice ; Mice, Inbred Strains ; *Mice, Transgenic ; Neurons/cytology ; Oligonucleotide Array Sequence Analysis ; Phenotype ; Skull/pathology ; Stem Cells ; Synaptic Transmission ; T-Lymphocytes/immunology
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    Evolution of oxygen secretion in fishes and the emergence of a complex physiological system (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: We have reconstructed the events that led to the evolution of a key physiological innovation underpinning the large adaptive radiation of fishes, namely their unique ability to secrete molecular oxygen (O2). We show that O2 secretion into the swimbladder evolved some 100 million years after another O2-secreting system in the eye. We unravel the likely sequence in which the functional components of both systems evolved. These components include ocular and swimbladder countercurrent exchangers, the Bohr and Root effects, the buffering power and surface histidine content of hemoglobins, and red blood cell Na+/H+ exchange activity. Our synthesis reveals the dynamics of gains and losses of these multiple traits over time, accounting for part of the huge diversity of form and function in living fishes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berenbrink, Michael -- Koldkjaer, Pia -- Kepp, Oliver -- Cossins, Andrew R -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1752-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK. michaelb@liv.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774753" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Air Sacs/blood supply/*physiology ; Amino Acid Sequence ; Animals ; *Biological Evolution ; Buffers ; Capillaries/physiology ; Choroid/blood supply/physiology ; Diffusion ; Environment ; Erythrocytes/physiology ; Fishes/anatomy & histology/classification/*physiology ; Hemoglobins/chemistry/*metabolism ; Histidine/analysis ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Oxygen/*metabolism ; Oxyhemoglobins/metabolism ; Phylogeny ; Sodium-Hydrogen Antiporter/blood/metabolism ; Species Specificity
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    Mechanism of JCV entry into oligodendrocytes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santagata, Sandro -- Kinney, Hannah C -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):381-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020715" target="_blank"〉PubMed〈/a〉
    Keywords: Astrocytes/metabolism/virology ; Cell Line ; Humans ; JC Virus/*physiology ; Leukoencephalopathy, Progressive Multifocal/virology ; Oligodendroglia/metabolism/*virology ; Receptor, Serotonin, 5-HT2A/physiology ; Receptors, Virus/physiology ; Serotonin 5-HT2 Receptor Antagonists
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    Wingless signaling at synapses is through cleavage and nuclear import of receptor DFrizzled2 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-29
    Description: Wingless secretion provides pivotal signals during development by activating transcription of target genes. At Drosophila synapses, Wingless is secreted from presynaptic terminals and is required for synaptic growth and differentiation. Wingless binds the seven-pass transmembrane DFrizzled2 receptor, but the ensuing events at synapses are not known. We show that DFrizzled2 is endocytosed from the postsynaptic membrane and transported to the nucleus. The C terminus of DFrizzled2 is cleaved and translocated into the nucleus; the N-terminal region remains just outside the nucleus. Translocation of DFrizzled2-C into the nucleus, but not its cleavage and transport, depends on Wingless signaling. We conclude that, at synapses, Wingless signal transduction occurs through the nuclear localization of DFrizzled2-C for potential transcriptional regulation of synapse development.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3535279/" 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/PMC3535279/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathew, Dennis -- Ataman, Bulent -- Chen, Jinyun -- Zhang, Yali -- Cumberledge, Susan -- Budnik, Vivian -- GM R01 HD36000/GM/NIGMS NIH HHS/ -- R01 MH070000/MH/NIMH NIH HHS/ -- R01 MH70000/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 25;310(5752):1344-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16311339" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Nucleus/*metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/genetics/*metabolism ; Endocytosis ; Frizzled Receptors ; Molecular Sequence Data ; Muscle Cells/metabolism ; Mutagenesis, Site-Directed ; Neuromuscular Junction/*metabolism ; Protein Binding ; Proto-Oncogene Proteins/*metabolism ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter/chemistry/genetics/*metabolism ; *Signal Transduction ; Synaptic Membranes/metabolism ; Transfection ; Transgenes ; Wnt1 Protein
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    The kaposin B protein of KSHV activates the p38/MK2 pathway and stabilizes cytokine mRNAs (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-05
    Description: Cytokine production plays a critical role in diseases caused by Kaposi's sarcoma-associated herpesvirus (KSHV). Here we show that a latent KSHV gene product, kaposin B, increases the expression of cytokines by blocking the degradation of their messenger RNAs (mRNAs). Cytokine transcripts are normally unstable because they contain AU-rich elements (AREs) in their 3' noncoding regions that target them for degradation. Kaposin B reverses this instability by binding to and activating the kinase MK2, a target of the p38 mitogen-activated protein kinase signaling pathway and a known inhibitor of ARE-mRNA decay. These findings define an important mechanism linking latent KSHV infection to cytokine production, and also illustrate a distinctive mode by which viruses can selectively modulate mRNA turnover.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, Craig -- Ganem, Don -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):739-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Microbiology and Immunology, and Department of Medicine, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692053" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cytokines/*genetics/*metabolism ; Cytosol/metabolism ; Enzyme Activation ; HeLa Cells ; Herpesvirus 8, Human/*physiology ; Humans ; Intracellular Signaling Peptides and Proteins ; *MAP Kinase Signaling System ; Models, Biological ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; *RNA Stability ; RNA, Messenger/*metabolism ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic ; Transfection ; Two-Hybrid System Techniques ; Viral Proteins/*metabolism ; Virus Latency ; p38 Mitogen-Activated Protein Kinases/genetics/*metabolism
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    Tubulin polyglutamylase enzymes are members of the TTL domain protein family (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-14
    Description: Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase-like (TTLL) protein, TTLL1. TTLL1 is a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates. In the model protist Tetrahymena thermophila, two conserved types of polyglutamylases were characterized that differ in substrate preference and subcellular localization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janke, Carsten -- Rogowski, Krzysztof -- Wloga, Dorota -- Regnard, Catherine -- Kajava, Andrey V -- Strub, Jean-Marc -- Temurak, Nevzat -- van Dijk, Juliette -- Boucher, Dominique -- van Dorsselaer, Alain -- Suryavanshi, Swati -- Gaertig, Jacek -- Edde, Bernard -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1758-62. Epub 2005 May 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Recherches de Biochimie Macromoleculaire, CNRS, 34293 Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890843" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Brain/enzymology ; *Catalytic Domain ; Cilia/physiology ; Humans ; Mice ; Microtubules/metabolism ; Models, Molecular ; Molecular Sequence Data ; Movement ; Peptide Synthases/*chemistry/genetics/isolation & purification/*metabolism ; Phylogeny ; Polyglutamic Acid/*chemistry/genetics/isolation & purification/*metabolism ; Protein Conformation ; Protein Subunits/chemistry/isolation & purification/metabolism ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Tetrahymena thermophila/*enzymology/genetics/metabolism ; Tubulin/*chemistry/genetics/isolation & purification/*metabolism
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    Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-30
    Description: In the crystal structure of the membrane-embedded rotor ring of the sodium ion-translocating adenosine 5'-triphosphate (ATP) synthase of Ilyobacter tartaricus at 2.4 angstrom resolution, 11 c subunits are assembled into an hourglass-shaped cylinder with 11-fold symmetry. Sodium ions are bound in a locked conformation close to the outer surface of the cylinder near the middle of the membrane. The structure supports an ion-translocation mechanism in the intact ATP synthase in which the binding site converts from the locked conformation into one that opens toward subunit a as the rotor ring moves through the subunit a/c interface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meier, Thomas -- Polzer, Patrick -- Diederichs, Kay -- Welte, Wolfram -- Dimroth, Peter -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):659-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Mikrobiologie, Eidgenossische Technische Hochschule (ETH), Zurich Honggerberg, Wolfgang-Pauli-Str. 10, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860619" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Cytoplasm/metabolism ; Fusobacteria/*enzymology ; Glutamic Acid/chemistry/metabolism ; Hydrophobic and Hydrophilic Interactions ; Ion Transport ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Sodium/metabolism
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    Glycine-rich antifreeze proteins from snow fleas (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-22
    Description: We purified antifreeze proteins from winter-active snow fleas, Hypogastrura harveyi. These 6.5- and 15.7-kilodalton thermolabile proteins are glycine-rich (45% of the residues), and the short isoform is composed of the tripeptide repeat Gly-X-X. This makes them very different from other antifreeze proteins, including two from insects, suggesting independent adaptation to freezing environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Graham, Laurie A -- Davies, Peter L -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):461.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Queen's University, Kingston, ON K7L 3N6, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; Antifreeze Proteins/*chemistry/isolation & purification ; Arthropods/*chemistry ; Circular Dichroism ; Evolution, Molecular ; Glycine/*analysis ; Ice ; Molecular Sequence Data ; Molecular Weight ; Snow
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    Cell biology. Korean team speeds up creation of cloned human stem cells (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2005 May 20;308(5725):1096-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905368" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Blastocyst/*cytology ; Cell Line ; Child ; Child, Preschool ; *Cloning, Organism/ethics/methods ; Embryo Research/ethics ; Female ; Humans ; Korea ; Male ; Middle Aged ; Oocytes ; Politics ; *Research Embryo Creation/ethics/methods ; *Stem Cells ; Tissue Donors ; United States
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    Structure of a gammadelta T cell receptor in complex with the nonclassical MHC T22 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-12
    Description: Gammadelta T cell receptors (TCRs), alphabeta TCRs, and antibodies are the three lineages of somatically recombined antigen receptors. The structural basis for ligand recognition is well defined for alphabeta TCR and antibodies but is lacking for gammadelta TCRs. We present the 3.4 A structure of the murine gammadelta TCR G8 bound to its major histocompatibility complex (MHC) class Ib ligand, T22. G8 predominantly uses germline-encoded residues of its delta chain complementarity-determining region 3 (CDR3) loop to bind T22 in an orientation substantially different from that seen in alphabeta TCR/peptide-MHC. That junctionally encoded G8 residues play an ancillary role in binding suggests a fusion of innate and adaptive recognition strategies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adams, Erin J -- Chien, Yueh-Hsiu -- Garcia, K Christopher -- AI048540/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 8;308(5719):227-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Fairchild D319, 299 Campus Drive, Stanford, CA 94035-5124, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15821084" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Line ; Cloning, Molecular ; Crystallography, X-Ray ; Dimerization ; Histocompatibility Antigens Class I/*chemistry ; Humans ; Insects ; Mice ; Protein Binding ; Protein Conformation ; Proteins/*chemistry/immunology ; Receptors, Antigen, T-Cell, gamma-delta/*chemistry/immunology ; Recombinant Proteins/chemistry ; T-Lymphocytes/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Extensive diversity of Ig-superfamily proteins in the immune system of insects (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-20
    Description: The extensive somatic diversification of immune receptors is a hallmark of higher vertebrates. However, whether molecular diversity contributes to immune protection in invertebrates is unknown. We present evidence that Drosophila immune-competent cells have the potential to express more than 18,000 isoforms of the immunoglobulin (Ig)-superfamily receptor Down syndrome cell adhesion molecule (Dscam). Secreted protein isoforms of Dscam were detected in the hemolymph, and hemocyte-specific loss of Dscam impaired the efficiency of phagocytic uptake of bacteria, possibly due to reduced bacterial binding. Importantly, the molecular diversity of Dscam transcripts generated through a mechanism of alternative splicing is highly conserved across major insect orders, suggesting an unsuspected molecular complexity of the innate immune system of insects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, Fiona L -- Puttmann-Holgado, Roland -- Thomas, Franziska -- Lamar, David L -- Hughes, Michael -- Kondo, Masahiro -- Rebel, Vivienne I -- Schmucker, Dietmar -- 1RO1-NS46747-01/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1874-8. Epub 2005 Aug 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Dana Farber Cancer Institute, Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16109846" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Brain/metabolism ; Cell Adhesion Molecules ; Cell Line ; Drosophila Proteins/chemistry/*genetics/*immunology/metabolism ; Drosophila melanogaster/*genetics/*immunology/metabolism ; Escherichia coli/immunology/metabolism ; Fat Body/metabolism ; Hemocytes/immunology/*metabolism ; Hemolymph/chemistry ; Immunity, Innate ; Immunoglobulins/chemistry ; Insects/chemistry/genetics ; Molecular Sequence Data ; Neurons/metabolism ; Oligonucleotide Array Sequence Analysis ; Phagocytosis ; Protein Isoforms/chemistry/genetics/metabolism ; Protein Structure, Tertiary ; RNA Interference ; Receptors, Immunologic/immunology/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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  • 95
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    ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: The ataxia-telangiectasia mutated (ATM) kinase signals the presence of DNA double-strand breaks in mammalian cells by phosphorylating proteins that initiate cell-cycle arrest, apoptosis, and DNA repair. We show that the Mre11-Rad50-Nbs1 (MRN) complex acts as a double-strand break sensor for ATM and recruits ATM to broken DNA molecules. Inactive ATM dimers were activated in vitro with DNA in the presence of MRN, leading to phosphorylation of the downstream cellular targets p53 and Chk2. ATM autophosphorylation was not required for monomerization of ATM by MRN. The unwinding of DNA ends by MRN was essential for ATM stimulation, which is consistent with the central role of single-stranded DNA as an evolutionarily conserved signal for DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Ji-Hoon -- Paull, Tanya T -- CA094008/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):551-4. Epub 2005 Mar 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, 1 University Station, A4800, Austin, TX 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790808" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Cell Line ; DNA/chemistry/*metabolism ; *DNA Damage ; DNA Repair ; DNA Repair Enzymes/genetics/*metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; Enzyme Activation ; Humans ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Nucleic Acid Conformation ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Recombinant Proteins/metabolism ; Serine ; Signal Transduction ; Transfection ; Tumor Suppressor Proteins/chemistry/*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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  • 96
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    Regulation of X-chromosome counting by Tsix and Xite sequences (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-30
    Description: In mammals, X-inactivation establishes X-chromosome dosage parity between males and females. How X-chromosome counting regulates this process remains elusive, because neither the hypothesized inactivation "blocking factor" nor the required cis-elements have been defined. Here, a mouse knockout and transgenic analysis identified DNA sequences within the noncoding Tsix and Xite genes as numerators. Homozygous deficiency of Tsix resulted in "chaotic choice" and a variable number of inactive X's, whereas overdosage of Tsix/Xite inhibited X-inactivation. Thus, counting was affected by specific Tsix/Xite mutations, suggesting that counting is genetically separable from but molecularly coupled to choice. The mutations affect XX and XY cells differently, demonstrating that counting and choice are regulated not by one "blocking factor," but by both a "blocking" and a "competence" factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Jeannie T -- R01-GM58839/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):768-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology, Massachusetts General Hospital, Department of Genetics, Harvard Medical School Boston, MA 02114, USA. lee@molbio.mgh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051795" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blastocyst ; Cell Death ; Cell Differentiation ; Cell Line ; Chromosomes, Mammalian/genetics ; *DNA, Intergenic ; *Dosage Compensation, Genetic ; Female ; Gene Dosage ; Gene Silencing ; In Situ Hybridization, Fluorescence ; Male ; Mice ; Mice, Knockout ; Mice, Transgenic ; Models, Genetic ; RNA, Long Noncoding ; RNA, Untranslated/*genetics/physiology ; X Chromosome/*genetics
    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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  • 97
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    Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pufall, Miles A -- Lee, Gregory M -- Nelson, Mary L -- Kang, Hyun-Seo -- Velyvis, Algirdas -- Kay, Lewis E -- McIntosh, Lawrence P -- Graves, Barbara J -- GM08537/GM/NIGMS NIH HHS/ -- P01-CA24014/CA/NCI NIH HHS/ -- R01 GM38663/GM/NIGMS NIH HHS/ -- T32-CA93247/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):142-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Huntsman Cancer Institute, Department of Oncological Sciences, University of Utah, Salt Lake City, UT 84112-5550, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994560" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; DNA/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/*chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-ets ; Signal Transduction ; Transcription Factors/*chemistry/genetics/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    A mitotic septin scaffold required for Mammalian chromosome congression and segregation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: Coordination of cytokinesis with chromosome congression and segregation is critical for proper cell division, but the mechanism is unknown. Here, septins, a conserved family of polymerizing guanosine triphosphate-binding proteins, localized to the metaphase plate during mitosis. Septin depletion resulted in chromosome loss from the metaphase plate, lack of chromosome segregation and spindle elongation, and incomplete cytokinesis upon delayed mitotic exit. These defects correlated with loss of the mitotic motor and the checkpoint regulator centromere-associated protein E (CENP-E) from the kinetochores of congressing chromosomes. Mammalian septins may thus form a mitotic scaffold for CENP-E and other effectors to coordinate cytokinesis with chromosome congression and segregation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3368603/" 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/PMC3368603/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spiliotis, Elias T -- Kinoshita, Makoto -- Nelson, W James -- GM35527/GM/NIGMS NIH HHS/ -- R01 GM035527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1781-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Beckman Center for Molecular and Genetic Medicine, Stanford University School of Medicine, Stanford, CA 94305-5435, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774761" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chromosomal Proteins, Non-Histone/metabolism ; *Chromosome Segregation ; Chromosomes, Human/*physiology/ultrastructure ; Chromosomes, Mammalian/*physiology/ultrastructure ; Cytokinesis ; Cytoskeletal Proteins ; Dogs ; GTP-Binding Proteins/metabolism ; HeLa Cells ; Humans ; Kinesin/metabolism ; Kinetochores/metabolism ; Metaphase ; Microtubules/metabolism ; *Mitosis ; Phosphoric Monoester Hydrolases/immunology/*metabolism ; RNA Interference ; Septins ; Spindle Apparatus/metabolism/ultrastructure
    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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  • 99
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    Spindle multipolarity is prevented by centrosomal clustering (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: Most tumor cells are characterized by increased genomic instability and chromosome segregational defects, often associated with hyperamplification of the centrosome and the formation of multipolar spindles. However, extra centrosomes do not always lead to multipolarity. Here, we describe a process of centrosomal clustering that prevented the formation of multipolar spindles in noncancer cells. Noncancer cells needed to overcome this clustering mechanism to allow multipolar spindles to form at a high frequency. The microtubule motor cytoplasmic dynein was a critical part of this coalescing machinery, and in some tumor cells overexpression of the spindle protein NuMA interfered with dynein localization, promoting multipolarity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Quintyne, Nicholas J -- Reing, Janet E -- Hoffelder, Diane R -- Gollin, Susanne M -- Saunders, William S -- DE016086/DE/NIDCR NIH HHS/ -- P60DE13059/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Pittsburgh, 4249 Fifth Avenue, Pittsburgh, PA 15260, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637283" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Nuclear ; Cell Line ; Cell Line, Tumor ; Centrosome/*physiology ; Demecolcine/pharmacology ; Dyneins/*metabolism ; Humans ; Microtubule-Associated Proteins/metabolism ; Nuclear Matrix-Associated Proteins ; Nuclear Proteins/genetics/metabolism ; RNA, Small Interfering/metabolism ; Spindle Apparatus/*physiology ; Transfection
    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
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    Bats are natural reservoirs of SARS-like coronaviruses (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: Severe acute respiratory syndrome (SARS) emerged in 2002 to 2003 in southern China. The origin of its etiological agent, the SARS coronavirus (SARS-CoV), remains elusive. Here we report that species of bats are a natural host of coronaviruses closely related to those responsible for the SARS outbreak. These viruses, termed SARS-like coronaviruses (SL-CoVs), display greater genetic variation than SARS-CoV isolated from humans or from civets. The human and civet isolates of SARS-CoV nestle phylogenetically within the spectrum of SL-CoVs, indicating that the virus responsible for the SARS outbreak was a member of this coronavirus group.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Wendong -- Shi, Zhengli -- Yu, Meng -- Ren, Wuze -- Smith, Craig -- Epstein, Jonathan H -- Wang, Hanzhong -- Crameri, Gary -- Hu, Zhihong -- Zhang, Huajun -- Zhang, Jianhong -- McEachern, Jennifer -- Field, Hume -- Daszak, Peter -- Eaton, Bryan T -- Zhang, Shuyi -- Wang, Lin-Fa -- R01-TW05869/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):676-9. Epub 2005 Sep 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Zoology, Chinese Academy of Sciences (CAS), Beijing, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195424" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cercopithecus aethiops ; China/epidemiology ; Chiroptera/*virology ; Communicable Diseases, Emerging ; *Coronavirus/classification ; Disease Outbreaks ; *Disease Reservoirs ; Genetic Variation ; Genome, Viral ; Henipavirus/classification ; Humans ; Molecular Sequence Data ; Mutation ; Phylogeny ; Polymerase Chain Reaction ; *SARS Virus/classification ; Sequence Analysis, DNA ; Severe Acute Respiratory Syndrome/epidemiology/transmission/virology ; Vero Cells ; Viverridae/virology
    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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