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  • Signal Transduction  (81)
  • Crystallography, X-Ray
  • American Association for the Advancement of Science (AAAS)  (115)
  • American Meteorological Society
  • PANGAEA
  • 2015-2019
  • 2000-2004  (115)
  • 1995-1999
  • 2002  (115)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (115)
  • American Meteorological Society
  • PANGAEA
Years
  • 2015-2019
  • 2000-2004  (115)
  • 1995-1999
Year
  • 1
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    Cancer. BRCA2 enters the fray (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, John H -- Elledge, Stephen J -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1822-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228708" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BRCA1 Protein/metabolism ; BRCA2 Protein/*chemistry/*metabolism ; Binding Sites ; Breast Neoplasms/genetics ; Crystallography, X-Ray ; DNA/*metabolism ; DNA Damage ; *DNA Repair ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/metabolism ; Female ; Genes, BRCA1 ; Genes, BRCA2 ; Genetic Predisposition to Disease ; Humans ; Mice ; Ovarian Neoplasms/genetics ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rad51 Recombinase ; Rats ; Recombination, Genetic ; Replication Protein A
    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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    Visualization and functional analysis of RNA-dependent RNA polymerase lattices (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Positive-strand RNA viruses such as poliovirus replicate their genomes on intracellular membranes of their eukaryotic hosts. Electron microscopy has revealed that purified poliovirus RNA-dependent RNA polymerase forms planar and tubular oligomeric arrays. The structural integrity of these arrays correlates with cooperative RNA binding and RNA elongation and is sensitive to mutations that disrupt intermolecular contacts predicted by the polymerase structure. Membranous vesicles isolated from poliovirus-infected cells contain structures consistent with the presence of two-dimensional polymerase arrays on their surfaces during infection. Therefore, host cytoplasmic membranes may function as physical foundations for two-dimensional polymerase arrays, conferring the advantages of surface catalysis to viral RNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyle, John M -- Bullitt, Esther -- Bienz, Kurt -- Kirkegaard, Karla -- AI-42119/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2218-22.〈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/12077417" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Inclusion Bodies, Viral/metabolism/ultrastructure ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Poliovirus/*enzymology/physiology ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; RNA Replicase/*chemistry/isolation & purification/*metabolism/ultrastructure ; RNA, Viral/biosynthesis/*metabolism ; Viral Core Proteins/metabolism ; Virus Replication
    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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    Enhanced and delayed stress-induced alcohol drinking in mice lacking functional CRH1 receptors (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: There is a relation between stress and alcohol drinking. We show that the corticotropin-releasing hormone (CRH) system that mediates endocrine and behavioral responses to stress plays a role in the control of long-term alcohol drinking. In mice lacking a functional CRH1 receptor, stress leads to enhanced and progressively increasing alcohol intake. The effect of repeated stress on alcohol drinking behavior appeared with a delay and persisted throughout life. It was associated with an up-regulation of the N-methyl-d-aspartate receptor subunit NR2B. Alterations in the CRH1 receptor gene and adaptional changes in NR2B subunits may constitute a genetic risk factor for stress-induced alcohol drinking and alcoholism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sillaber, Inge -- Rammes, Gerhard -- Zimmermann, Stephan -- Mahal, Beatrice -- Zieglgansberger, Walter -- Wurst, Wolfgang -- Holsboer, Florian -- Spanagel, Rainer -- New York, N.Y. -- Science. 2002 May 3;296(5569):931-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Psychiatry, Kraepelinstrasse 2-10, 80804 Munich, Germany. sillaber@mpipsykl.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988580" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; *Alcohol Drinking ; Alcoholism/*etiology/genetics ; Animals ; Brain/metabolism ; Corticotropin-Releasing Hormone/physiology ; Ethanol/blood ; Female ; Hippocampus/physiology ; In Vitro Techniques ; Male ; Mice ; Mice, Knockout ; Models, Animal ; Mutation ; Receptors, AMPA/metabolism ; Receptors, Corticotropin-Releasing Hormone/*genetics/*physiology ; Receptors, Kainic Acid/metabolism ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Signal Transduction ; Stress, Physiological/physiopathology ; Stress, Psychological/*physiopathology ; Up-Regulation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Stromal effects on mammary gland development and breast cancer (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: Breast cancer manifests itself in the mammary epithelium, yet there is a growing recognition that mammary stromal cells also play an important role in tumorigenesis. During its developmental cycle, the mammary gland displays many of the properties associated with breast cancer, and many of the stromal factors necessary for mammary development also promote or protect against breast cancer. Here we review our present knowledge of the specific factors and cell types that contribute to epithelial-stromal crosstalk during mammary development. To find cures for diseases like breast cancer that rely on epithelial-stromal crosstalk, we must understand how these different cell types communicate with each other.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2788989/" 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/PMC2788989/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wiseman, Bryony S -- Werb, Zena -- CA57621/CA/NCI NIH HHS/ -- R01 CA057621/CA/NCI NIH HHS/ -- R01 CA057621-07/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 May 10;296(5570):1046-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, University of California, 513 Parnassus Avenue, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004111" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/cytology/physiology ; Animals ; Apoptosis ; Breast/cytology/embryology/*growth & development/physiology ; Breast Neoplasms/pathology/*physiopathology ; Cell Communication ; Epithelial Cells/physiology ; Extracellular Matrix/physiology ; Female ; Humans ; Mammary Glands, Animal/cytology/embryology/*growth & development/physiology ; Mammary Neoplasms, Animal/pathology/*physiopathology ; Morphogenesis ; Neoplasm Metastasis ; Pregnancy ; Signal Transduction ; Stromal Cells/*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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  • 5
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    BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: Mutations in the BRCA2 (breast cancer susceptibility gene 2) tumor suppressor lead to chromosomal instability due to defects in the repair of double-strand DNA breaks (DSBs) by homologous recombination, but BRCA2's role in this process has been unclear. Here, we present the 3.1 angstrom crystal structure of a approximately 90-kilodalton BRCA2 domain bound to DSS1, which reveals three oligonucleotide-binding (OB) folds and a helix-turn-helix (HTH) motif. We also (i) demonstrate that this BRCA2 domain binds single-stranded DNA, (ii) present its 3.5 angstrom structure bound to oligo(dT)9, (iii) provide data that implicate the HTH motif in dsDNA binding, and (iv) show that BRCA2 stimulates RAD51-mediated recombination in vitro. These findings establish that BRCA2 functions directly in homologous recombination and provide a structural and biochemical basis for understanding the loss of recombination-mediated DSB repair in BRCA2-associated cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Haijuan -- Jeffrey, Philip D -- Miller, Julie -- Kinnucan, Elspeth -- Sun, Yutong -- Thoma, Nicolas H -- Zheng, Ning -- Chen, Phang-Lang -- Lee, Wen-Hwa -- Pavletich, Nikola P -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1837-48.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Sloan-Kettering Division, Joan and Sanford I. Weill Graduate School of Medical Sciences, Cornell University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228710" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; BRCA2 Protein/*chemistry/genetics/*metabolism ; Binding Sites ; Crystallography, X-Ray ; DNA/metabolism ; *DNA Repair ; DNA, Single-Stranded/*metabolism ; DNA-Binding Proteins/metabolism ; Genes, BRCA2 ; Helix-Turn-Helix Motifs ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Mice ; Molecular Sequence Data ; Mutation ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/chemistry/*metabolism ; Rad51 Recombinase ; Rats ; *Recombination, Genetic
    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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    Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-24
    Description: A current view is that cytotoxic stress, such as DNA damage, induces apoptosis by regulating the permeability of mitochondria. Mitochondria sequester several proteins that, if released, kill by activating caspases, the proteases that disassemble the cell. Cytokines activate caspases in a different way, by assembling receptor complexes that activate caspases directly; in this case, the subsequent mitochondrial permeabilization accelerates cell disassembly by amplifying caspase activity. We found that cytotoxic stress causes activation of caspase-2, and that this caspase is required for the permeabilization of mitochondria. Therefore, we argue that cytokine-induced and stress-induced apoptosis act through conceptually similar pathways in which mitochondria are amplifiers of caspase activity rather than initiators of caspase activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lassus, Patrice -- Opitz-Araya, Ximena -- Lazebnik, Yuri -- CA-13106-31/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1352-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193789" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Apoptotic Protease-Activating Factor 1 ; Caspase 2 ; Caspases/genetics/*metabolism ; Cell Line, Transformed ; Cytochrome c Group/metabolism ; *DNA Damage ; Enzyme Activation ; Enzyme Repression ; Etoposide/pharmacology ; Humans ; Mitochondria/metabolism/*physiology ; Permeability ; Protein Transport ; Proteins/genetics/metabolism ; Proto-Oncogene Proteins/metabolism ; *Proto-Oncogene Proteins c-bcl-2 ; RNA, Small Interfering ; RNA, Untranslated ; Signal Transduction ; Transfection ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/pharmacology ; bcl-2-Associated X Protein
    Print ISSN: 0036-8075
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  • 7
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    Extension of life-span in Caenorhabditis elegans by a diet lacking coenzyme Q (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: The isoprenylated benzoquinone coenzyme Q is a redox-active lipid essential for electron transport in aerobic respiration. Here, we show that withdrawal of coenzyme Q (Q) from the diet of wild-type nematodes extends adult life-span by approximately 60%. The longevity of clk-1, daf-2, daf-12, and daf-16 mutants is also extended by a Q-less diet. These results establish the importance of Q in life-span determination. The findings suggest that Q and the daf-2 pathway intersect at the mitochondria and imply that a concerted production coupled with enhanced scavenging of reactive oxygen species contributes to the substantial life-span extension.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Larsen, Pamela L -- Clarke, Catherine F -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, 607 Charles E. Young Drive East, Box 951569, University of California, Los Angeles, CA 90095, USA. larsen@chem.ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778046" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Animals ; Caenorhabditis elegans/genetics/growth & development/metabolism/*physiology ; Caenorhabditis elegans Proteins/genetics/metabolism ; Diet ; Escherichia coli/genetics/metabolism ; Fermentation ; Forkhead Transcription Factors ; Genes, Helminth ; Helminth Proteins/genetics/metabolism ; Larva/growth & development/metabolism ; *Longevity ; Mitochondria/metabolism ; Models, Biological ; Mutation ; Oxidation-Reduction ; Oxygen Consumption ; Phenotype ; Reactive Oxygen Species/metabolism ; Receptor, Insulin/genetics/metabolism ; Receptors, Cytoplasmic and Nuclear/genetics/metabolism ; Signal Transduction ; Transcription Factors/genetics/metabolism ; Ubiquinone/administration & dosage/*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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  • 8
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    Toll-like receptor 4-dependent activation of dendritic cells by beta-defensin 2 (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-02
    Description: beta-Defensins are small antimicrobial peptides of the innate immune system produced in response to microbial infection of mucosal tissue and skin. We demonstrate that murine beta-defensin 2 (mDF2beta) acts directly on immature dendritic cells as an endogenous ligand for Toll-like receptor 4 (TLR-4), inducing up-regulation of costimulatory molecules and dendritic cell maturation. These events, in turn, trigger robust, type 1 polarized adaptive immune responses in vivo, suggesting that mDF2beta may play an important role in immunosurveillance against pathogens and, possibly, self antigens or tumor antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biragyn, Arya -- Ruffini, Pier Adelchi -- Leifer, Cynthia A -- Klyushnenkova, Elena -- Shakhov, Alexander -- Chertov, Oleg -- Shirakawa, Aiko K -- Farber, Joshua M -- Segal, David M -- Oppenheim, Joost J -- Kwak, Larry W -- N0L-CO-12400/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1025-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Transplantation and Immunology Branch, National Cancer Institute, Bethesda, MD 20892, USA. arya@mail.ncifcrf.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411706" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Neoplasm/immunology ; Cancer Vaccines/immunology ; Cell Line ; Cytokines/biosynthesis ; Dendritic Cells/*immunology ; *Drosophila Proteins ; Female ; Humans ; Interferon-alpha/physiology ; Ligands ; Lipopolysaccharides/immunology/pharmacology ; Lymphocyte Culture Test, Mixed ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Neoplasms/immunology/therapy ; Receptors, CCR6 ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Chemokine/metabolism ; Recombinant Fusion Proteins/pharmacology ; Signal Transduction ; Toll-Like Receptor 4 ; Toll-Like Receptors ; Transfection ; beta-Defensins/pharmacology/*physiology
    Print ISSN: 0036-8075
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  • 9
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    Endocrinology. This hormone has been relaxin' too long! (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivell, Richard -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):637-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Hormone and Fertility Research, University of Hamburg, Grandweg 64, 22529 Hamburg, Germany. ivell@ihf.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809958" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclic AMP/metabolism ; Endometrium/metabolism ; Endothelial Growth Factors/metabolism ; Female ; Humans ; Insulin ; Leydig Cells/metabolism ; Lymphokines/metabolism ; Male ; *Membrane Proteins ; Neovascularization, Physiologic ; Ovary/metabolism ; Pregnancy ; Proteins/chemistry/physiology ; Receptors, Cell Surface/chemistry/*physiology ; *Receptors, G-Protein-Coupled ; Receptors, Peptide/chemistry/*physiology ; Relaxin/blood/*physiology ; Reproduction ; Signal Transduction ; Testis/physiology ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors ; Vasodilation
    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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  • 10
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    Structural insights into group II intron catalysis and branch-site selection (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: Group II self-splicing introns catalyze autoexcision from precursor RNA transcripts by a mechanism strikingly similar to that of the spliceosome, an RNA-protein assembly responsible for splicing together the protein-coding parts of most eukaryotic pre-mRNAs. Splicing in both cases initiates via nucleophilic attack at the 5' splice site by the 2' OH of a conserved intron adenosine residue, creating a branched (lariat) intermediate. Here, we describe the crystal structure at 3.0 A resolution of a 70-nucleotide RNA containing the catalytically essential domains 5 and 6 of the yeast ai5gamma group II self-splicing intron, revealing an unexpected two-nucleotide bulged structure around the branch-point adenosine in domain 6.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Lan -- Doudna, Jennifer A -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2084-8. Epub 2002 Feb 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry and, Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859154" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/chemistry/metabolism ; Base Pairing ; Binding Sites ; CME-Carbodiimide/*analogs & derivatives ; Catalysis ; Cobalt/metabolism ; Crystallization ; Crystallography, X-Ray ; *Introns ; Magnesium/metabolism ; Manganese/metabolism ; *Nucleic Acid Conformation ; Point Mutation ; RNA Precursors/chemistry/metabolism ; *RNA Splicing ; RNA, Fungal/*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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  • 11
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    A heat-sensitive TRP channel expressed in keratinocytes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: Mechanical and thermal cues stimulate a specialized group of sensory neurons that terminate in the skin. Three members of the transient receptor potential (TRP) family of channels are expressed in subsets of these neurons and are activated at distinct physiological temperatures. Here, we describe the cloning and characterization of a novel thermosensitive TRP channel. TRPV3 has a unique threshold: It is activated at innocuous (warm) temperatures and shows an increased response at noxious temperatures. TRPV3 is specifically expressed in keratinocytes; hence, skin cells are capable of detecting heat via molecules similar to those in heat-sensing neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peier, Andrea M -- Reeve, Alison J -- Andersson, David A -- Moqrich, Aziz -- Earley, Taryn J -- Hergarden, Anne C -- Story, Gina M -- Colley, Sian -- Hogenesch, John B -- McIntyre, Peter -- Bevan, Stuart -- Patapoutian, Ardem -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2046-9. Epub 2002 May 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016205" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Newborn ; Blotting, Northern ; CHO Cells ; Capsaicin/*analogs & derivatives/pharmacology ; *Cation Transport Proteins ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Cricetinae ; Epidermis/cytology/innervation/metabolism ; Ganglia, Spinal/metabolism ; *Hot Temperature ; Humans ; In Situ Hybridization ; Ion Channels/chemistry/genetics/*metabolism ; Keratinocytes/*metabolism ; Membrane Potentials ; Mice ; Molecular Sequence Data ; Nerve Endings/physiology ; Neurons/physiology ; Patch-Clamp Techniques ; RNA, Messenger/genetics/metabolism ; Ruthenium Red/pharmacology ; Signal Transduction ; Spinal Cord/metabolism ; TRPV Cation Channels ; Temperature
    Print ISSN: 0036-8075
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  • 12
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    Development. Putting the brakes on regeneration (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKerracher, Lisa -- Ellezam, Benjamin -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1819-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Pathologie et Biologie Cellulaire, Universite de Montreal, 2900 Edouard-Montpetit, Montreal, Quebec, H3T 1J4 Canada. mckerral@patho.umontreal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052945" target="_blank"〉PubMed〈/a〉
    Keywords: Amacrine Cells/*physiology ; Animals ; Axonal Transport ; Axons/*physiology ; *Cell Communication ; Cell Differentiation ; Cell Polarity ; Cells, Cultured ; Coculture Techniques ; Dendrites/*physiology ; Embryo, Mammalian ; Nerve Crush ; *Nerve Regeneration ; Optic Nerve/cytology/physiology ; Peripheral Nerves/transplantation ; Rats ; Retinal Ganglion Cells/*physiology ; Signal Transduction ; Spinal Cord/cytology/physiology
    Print ISSN: 0036-8075
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  • 13
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    Molecular basis of proton motive force generation: structure of formate dehydrogenase-N (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jormakka, Mika -- Tornroth, Susanna -- Byrne, Bernadette -- Iwata, So -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1863-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biomedical Sciences, Imperial College, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884747" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Catalytic Domain ; Cell Membrane/enzymology ; Crystallography, X-Ray ; Electron Transport ; Escherichia coli/*enzymology ; Formate Dehydrogenases/*chemistry/metabolism ; Formates/metabolism ; Guanine Nucleotides/chemistry/metabolism ; Hydrogen Bonding ; Iron-Sulfur Proteins/chemistry/metabolism ; Membrane Potentials ; Models, Molecular ; Nitrate Reductases/chemistry/metabolism ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; *Proton-Motive Force ; Protons ; Pterins/chemistry/metabolism ; Vitamin K 2/chemistry/metabolism
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  • 14
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    Meiotic arrest in the mouse follicle maintained by a Gs protein in the oocyte (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-24
    Description: The mammalian ovarian follicle consists of a multilayered complex of somatic cells that surround the oocyte. A signal from the follicle cells keeps the oocyte cell cycle arrested at prophase of meiosis I until luteinizing hormone from the pituitary acts on the follicle cells to release the arrest, causing meiosis to continue. Here we show that meiotic arrest can be released in mice by microinjecting the oocyte within the follicle with an antibody that inhibits the stimulatory heterotrimeric GTP-binding protein Gs. This indicates that Gs activity in the oocyte is required to maintain meiotic arrest within the ovarian follicle and suggests that the follicle may keep the cell cycle arrested by activating Gs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mehlmann, Lisa M -- Jones, Teresa L Z -- Jaffe, Laurinda A -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1343-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Connecticut Health Center, Farmington, CT 06032, USA. lmehlman@neuron.uchc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193786" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/immunology ; Cells, Cultured ; Cyclic AMP/metabolism ; Female ; GTP-Binding Protein alpha Subunits, Gi-Go/immunology/physiology ; GTP-Binding Protein alpha Subunits, Gs/antagonists & ; inhibitors/immunology/*physiology ; Hypoxanthine/pharmacology ; *Meiosis ; Mice ; Oocytes/drug effects/metabolism/*physiology ; Ovarian Follicle/*physiology ; Signal Transduction
    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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    Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: When bound by extracellular ligands, receptor tyrosine kinases (RTKs) on the cell surface transmit critical signals to the cell interior. Although signal termination is less well understood, protein tyrosine phosphatase-1B (PTP1B) is implicated in the dephosphorylation and inactivation of several RTKs. However, PTP1B resides on the cytoplasmic surface of the endoplasmic reticulum (ER), so how and when it accesses RTKs has been unclear. Using fluorescence resonance energy transfer (FRET) methods, we monitored interactions between the epidermal- and platelet-derived growth factor receptors and PTP1B. PTP1B-catalyzed dephosphorylation required endocytosis of the receptors and occurred at specific sites on the surface of the ER. Most of the RTKs activated at the cell surface showed interaction with PTP1B after internalization, establishing that RTK activation and inactivation are spatially and temporally partitioned within cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haj, Fawaz G -- Verveer, Peter J -- Squire, Anthony -- Neel, Benjamin G -- Bastiaens, Philippe I H -- R01 CA49152/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1708-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Biology Program, Division of Hematology-Oncology, Department of Medicine, Beth Israel-Deaconess Medical Center, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872838" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Catalytic Domain ; Cell Membrane/enzymology ; Cells, Cultured ; *Endocytosis ; Endoplasmic Reticulum/*enzymology ; Energy Transfer ; Epidermal Growth Factor/metabolism/pharmacology ; Fluorescence ; Mice ; Microscopy, Confocal ; Microscopy, Fluorescence ; Phosphorylation ; Platelet-Derived Growth Factor/metabolism/pharmacology ; Protein Transport ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 ; Protein Tyrosine Phosphatases/chemistry/genetics/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Receptors, Platelet-Derived Growth Factor/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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  • 16
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    Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of alpha-ketoacid dehydrogenase complexes that are central to intermediary metabolism. We find that Lpd and SucB support Mtb's antioxidant defense. The peroxiredoxin alkyl hydroperoxide reductase (AhpC) is linked to Lpd and SucB by an adaptor protein, AhpD. The 2.0 angstrom AhpD crystal structure reveals a thioredoxin-like active site that is responsive to lipoamide. We propose that Lpd, SucB (the only lipoyl protein detected in Mtb), AhpD, and AhpC together constitute a nicotinamide adenine dinucleotide (reduced)-dependent peroxidase and peroxynitrite reductase. AhpD thus represents a class of thioredoxin-like molecules that enables an antioxidant defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bryk, R -- Lima, C D -- Erdjument-Bromage, H -- Tempst, P -- Nathan, C -- HL61241/HL/NHLBI NIH HHS/ -- P30 CA08748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1073-7. Epub 2002 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799204" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/*metabolism ; Amino Acid Sequence ; Antioxidants ; Binding Sites ; Catalysis ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; Dihydrolipoamide Dehydrogenase/*metabolism ; Hydrogen Bonding ; Hydrogen Peroxide/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mycobacterium tuberculosis/*enzymology/genetics/metabolism ; NAD/metabolism ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Peroxidases/*chemistry/*metabolism ; Peroxiredoxins ; Peroxynitrous Acid/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Thioctic Acid/*analogs & derivatives/metabolism ; Thioredoxins/chemistry/metabolism
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  • 17
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    Induction of T helper type 2 immunity by a point mutation in the LAT adaptor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-18
    Description: The transmembrane protein LAT (linker for activation of T cells) couples the T cell receptor (TCR) to downstream signaling effectors. Mice homozygous for a mutation of a single LAT tyrosine residue showed impeded T cell development. However, later they accumulated polyclonal helper T (TH) cells that chronically produced type 2 cytokines in large amounts. This exaggerated TH2 differentiation caused tissue eosinophilia and massive maturation of plasma cells secreting to immunoglobulins of the E and G1 isotypes. This paradoxical phenotype establishes an unanticipated inhibitory function for LAT that is critical for the differentiation and homeostasis of TH cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aguado, Enrique -- Richelme, Sylvie -- Nunez-Cruz, Selene -- Miazek, Arkadiusz -- Mura, Anne-Marie -- Richelme, Mireille -- Guo, Xiao-Jun -- Sainty, Danielle -- He, Hai-Tao -- Malissen, Bernard -- Malissen, Marie -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2036-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre d'Immunologie de Marseille-Luminy, INSERM- and CNRS-Universite de la Mediterranee, Parc Scientifique de Luminy, 13288 Marseille Cedex 9, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065839" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antigens, CD5/analysis/metabolism ; B-Lymphocytes/immunology/physiology ; CD4-Positive T-Lymphocytes/immunology/physiology ; CD8-Positive T-Lymphocytes/immunology/physiology ; Carrier Proteins/*genetics/*physiology ; Cell Cycle ; Cell Differentiation ; Eosinophilia ; Eosinophils/physiology ; Histocompatibility Antigens Class II/immunology ; Immunoglobulin E/blood ; Immunoglobulin G/blood ; Interferon-gamma/genetics/metabolism ; Interleukins/genetics/metabolism ; Leukocyte Count ; Lymphocyte Activation ; Lymphoid Tissue/cytology/immunology ; *Membrane Proteins ; Mice ; Mice, Inbred BALB C ; Phenotype ; Phosphoproteins/*genetics/*physiology ; *Point Mutation ; Receptors, Antigen, T-Cell/analysis ; Signal Transduction ; T-Lymphocyte Subsets/immunology/physiology ; Th2 Cells/*immunology/physiology ; Thymus Gland/cytology/immunology
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  • 18
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    Antioxidants in photosynthesis and human nutrition (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-12-14
    Description: The harnessing of solar energy by photosynthesis depends on a safety valve that effectively eliminates hazardous excess energy and prevents oxidative damage to the plant cells. Many of the compounds that protect plant cells also protect human cells. Improving plant resistance to stress may thus have the beneficial side effect of also improving the nutritional quality of plants in the human diet. The pathways that synthesize these compounds are becoming amenable to genetic manipulation, which may yield benefits as widespread as improved plant stress tolerance and improved human physical and mental health.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Demmig-Adams, Barbara -- Adams, William W 3rd -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2149-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental, Population, and Organismic Biology, University of Colorado, Boulder, CO 80309-0334, USA. barbara.demmig-adams@colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481128" target="_blank"〉PubMed〈/a〉
    Keywords: Antioxidants/*administration & dosage/*metabolism ; Carotenoids/administration & dosage/metabolism ; *Diet ; Genetic Engineering ; Humans ; Light ; *Nutritional Physiological Phenomena ; Nutritive Value ; Oxidative Stress ; *Photosynthesis ; Photosynthetic Reaction Center Complex Proteins/metabolism ; *Photosystem II Protein Complex ; Plant Development ; *Plant Proteins ; Plants/genetics/*metabolism ; Signal Transduction ; Vitamin E/administration & dosage/metabolism
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  • 19
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    Role of the isthmus and FGFs in resolving the paradox of neural crest plasticity and prepatterning (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-16
    Description: Cranial neural crest cells generate the distinctive bone and connective tissues in the vertebrate head. Classical models of craniofacial development argue that the neural crest is prepatterned or preprogrammed to make specific head structures before its migration from the neural tube. In contrast, recent studies in several vertebrates have provided evidence for plasticity in patterning neural crest populations. Using tissue transposition and molecular analyses in avian embryos, we reconcile these findings by demonstrating that classical manipulation experiments, which form the basis of the prepatterning model, involved transplantation of a local signaling center, the isthmic organizer. FGF8 signaling from the isthmus alters Hoxa2 expression and consequently branchial arch patterning, demonstrating that neural crest cells are patterned by environmental signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trainor, Paul A -- Ariza-McNaughton, Linda -- Krumlauf, Robb -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847340" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Brain/cytology/*embryology/metabolism ; Brain Tissue Transplantation ; Branchial Region/*embryology/metabolism ; Cartilage/embryology ; Cell Movement ; Central Nervous System/embryology ; Chick Embryo ; Culture Techniques ; Fibroblast Growth Factor 8 ; Fibroblast Growth Factors/pharmacology/*physiology ; Gene Expression Regulation, Developmental ; Homeodomain Proteins/genetics/metabolism ; Mesencephalon/embryology/metabolism ; Morphogenesis ; Neural Crest/cytology/*embryology/metabolism/physiology ; Phenotype ; Rhombencephalon/embryology/metabolism ; Signal Transduction
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  • 20
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    The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-16
    Description: Plant disease resistance (R) genes trigger innate immune responses upon pathogen attack. RAR1 is an early convergence point in a signaling pathway engaged by multiple R genes. Here, we show that RAR1 interacts with plant orthologs of the yeast protein SGT1, an essential regulator in the cell cycle. Silencing the barley gene Sgt1 reveals its role in R gene-triggered, Rar1-dependent disease resistance. SGT1 associates with SKP1 and CUL1, subunits of the SCF (Skp1-Cullin-F-box) ubiquitin ligase complex. Furthermore, the RAR1-SGT1 complex also interacts with two COP9 signalosome components. The interactions among RAR1, SGT1, SCF, and signalosome subunits indicate a link between disease resistance and ubiquitination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Azevedo, Cristina -- Sadanandom, Ari -- Kitagawa, Katsumi -- Freialdenhoven, Andreas -- Shirasu, Ken -- Schulze-Lefert, Paul -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2073-6. Epub 2002 Feb 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Sainsbury Laboratory, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847307" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/chemistry/genetics/metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Gene Silencing ; Genes, Fungal ; *Genes, Plant ; Hordeum/chemistry/genetics/metabolism ; Immunity, Innate ; Molecular Sequence Data ; Multiprotein Complexes ; Peptide Hydrolases ; Peptide Synthases/metabolism ; *Plant Diseases ; Plant Proteins/genetics/metabolism ; Protein Structure, Tertiary ; Proteins/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; SKP Cullin F-Box Protein Ligases ; Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism ; Sequence Alignment ; Signal Transduction ; Two-Hybrid System Techniques ; Ubiquitin/metabolism
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  • 21
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    Regulation of mitochondrial biogenesis in skeletal muscle by CaMK (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-16
    Description: Endurance exercise training promotes mitochondrial biogenesis in skeletal muscle and enhances muscle oxidative capacity, but the signaling mechanisms involved are poorly understood. To investigate this adaptive process, we generated transgenic mice that selectively express in skeletal muscle a constitutively active form of calcium/calmodulin-dependent protein kinase IV (CaMKIV*). Skeletal muscles from these mice showed augmented mitochondrial DNA replication and mitochondrial biogenesis, up-regulation of mitochondrial enzymes involved in fatty acid metabolism and electron transport, and reduced susceptibility to fatigue during repetitive contractions. CaMK induced expression of peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-1), a master regulator of mitochondrial biogenesis in vivo, and activated the PGC-1 gene promoter in cultured myocytes. Thus, a calcium-regulated signaling pathway controls mitochondrial biogenesis in mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Hai -- Kanatous, Shane B -- Thurmond, Frederick A -- Gallardo, Teresa -- Isotani, Eiji -- Bassel-Duby, Rhonda -- Williams, R Sanders -- AR40849/AR/NIAMS NIH HHS/ -- HL06296/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11951046" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; DNA Replication ; DNA, Mitochondrial/biosynthesis ; Electron Transport ; Fatty Acids/metabolism ; Gene Expression ; Gene Expression Profiling ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mitochondria, Muscle/enzymology/*metabolism ; Muscle Contraction ; Muscle Fatigue ; Muscle Fibers, Skeletal/ultrastructure ; Muscle, Skeletal/enzymology/*metabolism/ultrastructure ; Oligonucleotide Array Sequence Analysis ; Promoter Regions, Genetic ; Signal Transduction ; Transcription Factors/genetics/metabolism ; Transgenes ; Up-Regulation
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  • 22
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    Maneuvering in the complex path from genotype to phenotype (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-27
    Description: Human disease phenotypes are controlled not only by genes but by lawful self-organizing networks that display system-wide dynamics. These networks range from metabolic pathways to signaling pathways that regulate hormone action. When perturbed, networks alter their output of matter and energy which, depending on the environmental context, can produce either a pathological or a normal phenotype. Study of the dynamics of these networks by approaches such as metabolic control analysis may provide new insights into the pathogenesis and treatment of complex diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strohman, Richard -- New York, N.Y. -- Science. 2002 Apr 26;296(5568):701-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, 229 Stanley Hall, No. 3206, University of California at Berkeley, Berkeley, CA 94720-3206, USA. E-mail: strohman@uclink4.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976445" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism ; *Disease ; Genomics ; *Genotype ; Humans ; *Metabolism ; Molecular Biology ; Parkinson Disease/metabolism ; *Phenotype ; Proteins/metabolism ; Research Support as Topic ; Signal Transduction
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  • 23
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    Structure of a cofactor-deficient nitrogenase MoFe protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-16
    Description: One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous alpha and beta subunits. In this structure, one of the three alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmid, Benedikt -- Ribbe, Markus W -- Einsle, Oliver -- Yoshida, Mika -- Thomas, Leonard M -- Dean, Dennis R -- Rees, Douglas C -- Burgess, Barbara K -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):352-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, Mail Code 147-75CH, Howard Hughes Medical Institute, 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/11951047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Azotobacter vinelandii/*enzymology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Molybdoferredoxin/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Static Electricity ; Surface Properties
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  • 24
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    Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-09-21
    Description: To make messenger RNA transcripts, bacteriophage T7 RNA polymerase (T7 RNAP) undergoes a transition from an initiation phase, which only makes short RNA fragments, to a stable elongation phase. We have determined at 2.1 angstrom resolution the crystal structure of a T7 RNAP elongation complex with 30 base pairs of duplex DNA containing a "transcription bubble" interacting with a 17-nucleotide RNA transcript. The transition from an initiation to an elongation complex is accompanied by a major refolding of the amino-terminal 300 residues. This results in loss of the promoter binding site, facilitating promoter clearance, and creates a tunnel that surrounds the RNA transcript after it peels off a seven-base pair heteroduplex. Formation of the exit tunnel explains the enhanced processivity of the elongation complex. Downstream duplex DNA binds to the fingers domain, and its orientation relative to upstream DNA in the initiation complex implies an unwinding that could facilitate formation of the open promoter complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yin, Y Whitney -- Steitz, Thomas A -- GM57510/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1387-95. Epub 2002 Sep 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242451" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T7/enzymology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/genetics/*metabolism ; Models, Molecular ; Mutation ; N-Acetylmuramoyl-L-alanine Amidase/metabolism ; Nucleic Acid Heteroduplexes ; Promoter Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; RNA Polymerase II/chemistry ; RNA, Messenger/*chemistry/metabolism ; Taq Polymerase/chemistry ; Templates, Genetic ; Transcription Initiation Site ; *Transcription, Genetic ; Viral Proteins
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    Neurobiology. Learning more about NMDA receptor regulation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, Anirvan -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):449-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. aghosh@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799227" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Ephrin-B2 ; Glutamic Acid/metabolism ; Hippocampus/metabolism/physiology ; Ligands ; Membrane Proteins/*metabolism/pharmacology ; Mice ; *Neuronal Plasticity ; Neurons/metabolism/physiology ; Phosphorylation ; Protein Structure, Tertiary ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptor, EphB4 ; Receptors, Eph Family ; Receptors, N-Methyl-D-Aspartate/chemistry/*metabolism ; Signal Transduction ; Synapses/*metabolism ; Synaptic Membranes/metabolism ; src-Family Kinases/metabolism
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    Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: The chromodomain of the HP1 family of proteins recognizes histone tails with specifically methylated lysines. Here, we present structural, energetic, and mutational analyses of the complex between the Drosophila HP1 chromodomain and the histone H3 tail with a methyllysine at residue 9, a modification associated with epigenetic silencing. The histone tail inserts as a beta strand, completing the beta-sandwich architecture of the chromodomain. The methylammonium group is caged by three aromatic side chains, whereas adjacent residues form discerning contacts with one face of the chromodomain. Comparison of dimethyl- and trimethyllysine-containing complexes suggests a role for cation-pi and van der Waals interactions, with trimethylation slightly improving the binding affinity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, Steven A -- Khorasanizadeh, Sepideh -- GM63959-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2080-3. Epub 2002 Feb 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908-0733, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859155" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Chromosomal Proteins, Non-Histone/*chemistry/genetics/*metabolism ; Crystallography, X-Ray ; Drosophila Proteins/chemistry/metabolism ; Histones/*chemistry/genetics/*metabolism ; Hydrogen Bonding ; Lysine/*analogs & derivatives/chemistry/*metabolism ; Methylation ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Peptides/chemistry/metabolism ; Point Mutation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment
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    Pituitary development: regulatory codes in mammalian organogenesis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: During mammalian pituitary gland development, distinct cell types emerge from a common primordium. Appearance of specific cell types occurs in response to opposing signaling gradients that emanate from distinct organizing centers. These signals induce expression of interacting transcriptional regulators, including DNA binding-dependent activators and DNA binding-independent transrepressors, in temporally and spatially overlapping patterns. Together they synergistically regulate precursor proliferation and induction of distinct cell types. Terminal cell type differentiation requires selective gene activation strategies and long-term active repression, mediated by cell type-specific and promoter-specific recruitment of coregulatory complexes. These mechanisms imply the potential for flexibility in the ultimate identity of differentiated cell types.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scully, Kathleen M -- Rosenfeld, Michael G -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2231-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, School of Medicine, University of California, San Diego, 9500 Gilman Drive, Room 345, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910101" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; *Cell Lineage ; *Gene Expression Regulation, Developmental ; Homeodomain Proteins/metabolism ; Mammals/embryology ; Pituitary Gland/*cytology/*embryology/metabolism ; Pro-Opiomelanocortin/metabolism ; Signal Transduction ; Transcription Factors/*metabolism ; Transcriptional Activation
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    Intercellular communication in the mammalian ovary: oocytes carry the conversation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: The production of functional female gametes is essential for the propagation of all vertebrate species. The growth of oocytes within ovarian follicles and their development to mature eggs have fascinated biologists for centuries, and scientists have long realized the importance of the ovarian follicle's somatic cells in nurturing oogenesis and delivering the oocyte to the oviduct by ovulation. Recent studies have revealed key roles of the oocyte in folliculogenesis and established that bidirectional communication between the oocyte and companion somatic cells is essential for development of an egg competent to undergo fertilization and embryogenesis. The challenge for the future is to identify the factors that participate in this communication and their mechanisms of action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matzuk, Martin M -- Burns, Kathleen H -- Viveiros, Maria M -- Eppig, John J -- CA60651/CA/NCI NIH HHS/ -- CA62392/CA/NCI NIH HHS/ -- EY07102/EY/NEI NIH HHS/ -- GM07330/GM/NIGMS NIH HHS/ -- HD07495/HD/NICHD NIH HHS/ -- HD23839/HD/NICHD NIH HHS/ -- HD32067/HD/NICHD NIH HHS/ -- HD33438/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2178-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA. mmatzuk@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077402" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Communication ; Embryonic and Fetal Development ; Female ; Granulosa Cells/physiology ; Oocytes/*physiology ; *Oogenesis ; Ovarian Follicle/*physiology ; Signal Transduction
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    Aging. Dietary advice on Q (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tatar, Marc -- Rand, David M -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):54-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Brown University, Providence, RI 02912, USA. marc_tatar@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778030" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Animals ; Caenorhabditis elegans/genetics/growth & development/metabolism/*physiology ; Caenorhabditis elegans Proteins/genetics/physiology ; Cell Nucleus/metabolism ; Diet ; Electron Transport ; Energy Metabolism ; Escherichia coli/metabolism ; Fermentation ; Helminth Proteins/genetics/physiology ; Insulin/metabolism ; Larva/growth & development/metabolism ; *Longevity ; Mitochondria/metabolism ; Mutation ; Reactive Oxygen Species/metabolism ; Receptor, Insulin/genetics/physiology ; Receptors, Cytoplasmic and Nuclear/genetics/physiology ; Signal Transduction ; Ubiquinone/administration & dosage/*metabolism
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    C-cadherin ectodomain structure and implications for cell adhesion mechanisms (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative "classical" cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boggon, Titus J -- Murray, John -- Chappuis-Flament, Sophie -- Wong, Ellen -- Gumbiner, Barry M -- Shapiro, Lawrence -- NCI-P30-CA-08784/CI/NCPDCID CDC HHS/ -- R01 GM062270/GM/NIGMS NIH HHS/ -- R01 GM52717/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1308-13. Epub 2002 Apr 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Columbia University College of Physicians and Surgeons, 630 West 168th Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964443" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; CHO Cells ; Cadherins/*chemistry/genetics/metabolism ; *Cell Adhesion ; Cricetinae ; Crystallography, X-Ray ; Dimerization ; Glycosylation ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry ; Tryptophan/chemistry ; Xenopus Proteins
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    Amacrine-signaled loss of intrinsic axon growth ability by retinal ganglion cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: The central nervous system (CNS) loses the ability to regenerate early during development, but it is not known why. The retina has long served as a simple model system for study of CNS regeneration. Here we show that amacrine cells signal neonatal rat retinal ganglion cells (RGCs) to undergo a profound and apparently irreversible loss of intrinsic axon growth ability. Concurrently, retinal maturation triggers RGCs to greatly increase their dendritic growth ability. These results suggest that adult CNS neurons fail to regenerate not only because of CNS glial inhibition but also because of a loss of intrinsic axon growth ability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldberg, Jeffrey L -- Klassen, Matthew P -- Hua, Ying -- Barres, Ben A -- 2T32GM07365/GM/NIGMS NIH HHS/ -- R01 EY11030/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1860-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University School of Medicine, Department of Neurobiology, Sherman Fairchild Science Building D231, 299 Campus Drive, Stanford, CA 94305-5125, USA. jlgoldbe@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052959" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Amacrine Cells/*physiology ; Animals ; Animals, Newborn ; Axons/*physiology/ultrastructure ; Cell Aging ; *Cell Communication ; Cell Separation ; Cells, Cultured ; Culture Media, Conditioned ; Culture Techniques ; Cyclic AMP/metabolism ; Dendrites/physiology/ultrastructure ; Embryo, Mammalian ; Nerve Regeneration ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Rats ; Retina/cytology ; Retinal Ganglion Cells/*physiology/transplantation/ultrastructure ; Signal Transduction ; Superior Colliculi/physiology
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    Progression of vertebrate limb development through SHH-mediated counteraction of GLI3 (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: Distal limb development and specification of digit identities in tetrapods are under the control of a mesenchymal organizer called the polarizing region. Sonic Hedgehog (SHH) is the morphogenetic signal produced by the polarizing region in the posterior limb bud. Ectopic anterior SHH signaling induces digit duplications and has been suspected as a major cause underlying congenital malformations that result in digit polydactyly. Here, we report that the polydactyly of Gli3-deficient mice arises independently of SHH signaling. Disruption of one or both Gli3 alleles in mouse embryos lacking Shh progressively restores limb distal development and digit formation. Our genetic analysis indicates that SHH signaling counteracts GLI3-mediated repression of key regulator genes, cell survival, and distal progression of limb bud development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉te Welscher, Pascal -- Zuniga, Aimee -- Kuijper, Sanne -- Drenth, Thijs -- Goedemans, Hans J -- Meijlink, Frits -- Zeller, Rolf -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):827-30. Epub 2002 Sep 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Faculty of Biology, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215652" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Basic Helix-Loop-Helix Transcription Factors ; Cell Death ; DNA-Binding Proteins/genetics/*physiology ; Extremities/*embryology ; Fibroblast Growth Factors/genetics/metabolism ; Gene Expression Regulation, Developmental ; Genes, Homeobox ; Hedgehog Proteins ; Homeodomain Proteins/genetics/metabolism ; *Intercellular Signaling Peptides and Proteins ; Kruppel-Like Transcription Factors ; Limb Buds/cytology/embryology/metabolism ; Membrane Proteins/genetics/metabolism ; Mice ; Mutation ; *Nerve Tissue Proteins ; Oncogene Proteins/genetics/metabolism ; Polydactyly/genetics ; Proteins/genetics/physiology ; Receptors, Cell Surface ; Signal Transduction ; Trans-Activators/genetics/*physiology ; Transcription Factors/genetics/metabolism/*physiology ; Zebrafish Proteins
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    Combinatorial synthesis of genetic networks (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-25
    Description: A central problem in biology is determining how genes interact as parts of functional networks. Creation and analysis of synthetic networks, composed of well-characterized genetic elements, provide a framework for theoretical modeling. Here, with the use of a combinatorial method, a library of networks with varying connectivity was generated in Escherichia coli. These networks were composed of genes encoding the transcriptional regulators LacI, TetR, and lambda CI, as well as the corresponding promoters. They displayed phenotypic behaviors resembling binary logical circuits, with two chemical "inputs" and a fluorescent protein "output." Within this simple system, diverse computational functions arose through changes in network connectivity. Combinatorial synthesis provides an alternative approach for studying biological networks, as well as an efficient method for producing diverse phenotypes in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guet, Calin C -- Elowitz, Michael B -- Hsing, Weihong -- Leibler, Stanislas -- New York, N.Y. -- Science. 2002 May 24;296(5572):1466-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029133" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/metabolism ; Bacteriophage lambda/genetics ; Escherichia coli/*genetics/*metabolism ; *Escherichia coli Proteins ; Feedback, Physiological ; Fluorescence ; *Gene Expression Regulation, Bacterial ; Gene Library ; Genes, Regulator ; Green Fluorescent Proteins ; Lac Repressors ; Luminescent Proteins/genetics/metabolism ; Phenotype ; Plasmids ; *Promoter Regions, Genetic ; Repressor Proteins/*genetics/metabolism ; Signal Transduction ; Transformation, Bacterial
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    Neurobiology. A glial spin on neurotrophins (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hempstead, Barbara L -- Salzer, James L -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1184-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Weill Medical College of Cornell University, New York, NY 10021, USA. blhempst@med.Cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424359" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology ; Brain-Derived Neurotrophic Factor/pharmacology/*physiology ; Central Nervous System/physiology ; Ligands ; Mice ; Models, Neurological ; Myelin Sheath/*physiology ; Nerve Regeneration ; Neurotrophin 3/pharmacology/*physiology ; Oligodendroglia/physiology ; Paracrine Communication ; Peripheral Nervous System/physiology ; Receptor, Nerve Growth Factor ; Receptor, trkC/*physiology ; Receptors, Nerve Growth Factor/*physiology ; Schwann Cells/*physiology ; Signal Transduction
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    Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Einsle, Oliver -- Tezcan, F Akif -- Andrade, Susana L A -- Schmid, Benedikt -- Yoshida, Mika -- Howard, James B -- Rees, Douglas C -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1696-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Division of Chemistry and Chemical Engineering, California Institute of Technology, Mail Code 147-75CH, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215645" target="_blank"〉PubMed〈/a〉
    Keywords: Azotobacter vinelandii/enzymology ; Coenzymes/*chemistry/metabolism ; Crystallography, X-Ray ; Ligands ; Models, Molecular ; Molybdoferredoxin/*chemistry/metabolism ; Nitrogen/chemistry ; Nitrogenase/*chemistry/metabolism ; Protein Conformation
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    Retrograde support of neuronal survival without retrograde transport of nerve growth factor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Application of nerve growth factor (NGF) covalently cross-linked to beads increased the phosphorylation of TrkA and Akt, but not of mitogen-activated protein kinase, in cultured rat sympathetic neurons. NGF beads or iodine-125-labeled NGF beads supplied to distal axons resulted in the survival of over 80% of the neurons for 30 hours, with little or no retrograde transport of iodine-125-labeled NGF; whereas application of free iodine-125-labeled NGF (0.5 nanograms per milliliter) produced 20-fold more retrograde transport, but only 29% of the neurons survived. Thus, in contrast to widely accepted theory, a neuronal survival signal can reach the cell bodies unaccompanied by the NGF that initiated it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacInnis, Bronwyn L -- Campenot, Robert B -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1536-9. Epub 2002 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, 6-14 Medical Sciences Building, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799202" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*metabolism ; Cell Survival/drug effects ; Cells, Cultured ; Chromones/pharmacology ; Cross-Linking Reagents ; Enzyme Inhibitors/pharmacology ; Iodine Radioisotopes ; Microspheres ; Mitogen-Activated Protein Kinases/metabolism ; Morpholines/pharmacology ; Nerve Growth Factor/*metabolism/pharmacology ; Neurons/metabolism/*physiology ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors/metabolism ; Phosphorylation ; Protein Transport ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Rats, Sprague-Dawley ; Receptor, trkA/metabolism ; Signal Transduction ; Superior Cervical Ganglion
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Myeloperoxidase, a leukocyte-derived vascular NO oxidase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-29
    Description: Myeloperoxidase (MPO) is an abundant mammalian phagocyte hemoprotein thought to primarily mediate host defense reactions. Although its microbicidal functions are well established in vitro, humans deficient in MPO are not at unusual risk of infection. MPO was observed herein to modulate the vascular signaling and vasodilatory functions of nitric oxide (NO) during acute inflammation. After leukocyte degranulation, MPO localized in and around vascular endothelial cells in a rodent model of acute endotoxemia and impaired endothelium-dependent relaxant responses, to which MPO-deficient mice were resistant. Altered vascular responsiveness was due to catalytic consumption of NO by substrate radicals generated by MPO. Thus MPO can directly modulate vascular inflammatory responses by regulating NO bioavailability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eiserich, Jason P -- Baldus, Stephan -- Brennan, Marie-Luise -- Ma, Wenxin -- Zhang, Chunxiang -- Tousson, Albert -- Castro, Laura -- Lusis, Aldons J -- Nauseef, William M -- White, C Roger -- Freeman, Bruce A -- I01 BX000513/BX/BLRD VA/ -- R01 HL067930/HL/NHLBI NIH HHS/ -- R03 TW005682/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2391-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Division of Nephrology, University of California, Davis, CA 95616, USA. jpeiserich@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta ; Catalysis ; Cattle ; Cells, Cultured ; Chromans/metabolism/pharmacology ; Coculture Techniques ; Cyclic GMP/metabolism ; Endothelium, Vascular/enzymology/*physiology ; Endotoxemia/enzymology ; Humans ; Hydrogen Peroxide/metabolism/pharmacology ; Inflammation/*enzymology/physiopathology ; Leukocytes/*enzymology ; Mice ; Mice, Inbred C57BL ; Muscle, Smooth, Vascular/metabolism ; Mutation ; Nitric Oxide/*metabolism ; Oxidation-Reduction ; Peroxidase/genetics/*metabolism ; Rats ; Rats, Sprague-Dawley ; Signal Transduction ; Transfection ; Tumor Cells, Cultured ; *Vasodilation
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    The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: The ABC transporters are ubiquitous membrane proteins that couple adenosine triphosphate (ATP) hydrolysis to the translocation of diverse substrates across cell membranes. Clinically relevant examples are associated with cystic fibrosis and with multidrug resistance of pathogenic bacteria and cancer cells. Here, we report the crystal structure at 3.2 angstrom resolution of the Escherichia coli BtuCD protein, an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and appears to represent a conserved motif among the ABC transporters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Locher, Kaspar P -- Lee, Allen T -- Rees, Douglas C -- New York, N.Y. -- Science. 2002 May 10;296(5570):1091-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, Mail Code 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA. locher@caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004122" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Biological Transport ; Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/metabolism ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Vitamin B 12/*metabolism
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    Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: The crystal structure of the initiating form of Thermus aquaticus RNA polymerase, containing core RNA polymerase (alpha2betabeta'omega) and the promoter specificity sigma subunit, has been determined at 4 angstrom resolution. Important structural features of the RNA polymerase and their roles in positioning sigma within the initiation complex are delineated, as well as the role played by sigma in modulating the opening of the RNA polymerase active-site channel. The two carboxyl-terminal domains of sigma are separated by 45 angstroms on the surface of the RNA polymerase, but are linked by an extended loop. The loop winds near the RNA polymerase active site, where it may play a role in initiating nucleotide substrate binding, and out through the RNA exit channel. The advancing RNA transcript must displace the loop, leading to abortive initiation and ultimately to sigma release.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murakami, Katsuhiko S -- Masuda, Shoko -- Darst, Seth A -- GM53759/GM/NIGMS NIH HHS/ -- GM61898/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1280-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/12016306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/*chemistry/*metabolism ; Eukaryotic Cells/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Bacterial/metabolism ; RNA, Messenger/metabolism ; Sigma Factor/metabolism ; Thermus/*enzymology ; *Transcription, Genetic
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    Eppendorf & Science Prize. Essays on science and society. Making a bigger brain by regulating cell cycle exit (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chenn, Anjen -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):766-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Northwestern University, The Feinberg School of Medicine, Chicago, IL 60611-3008, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399574" target="_blank"〉PubMed〈/a〉
    Keywords: Adherens Junctions/physiology/ultrastructure ; Animals ; Apoptosis ; Awards and Prizes ; *Cell Cycle ; Cell Differentiation ; Cell Division ; Cerebral Cortex/anatomy & histology/*growth & development ; Cytoskeletal Proteins/*metabolism ; Humans ; Mice ; Mice, Transgenic ; Neurons/*cytology/physiology ; Signal Transduction ; Stem Cells/cytology/*physiology ; Trans-Activators/*metabolism ; beta Catenin
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    Hijacking of host cell IKK signalosomes by the transforming parasite Theileria (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-02
    Description: Parasites have evolved a plethora of mechanisms to ensure their propagation and evade antagonistic host responses. The intracellular protozoan parasite Theileria is the only eukaryote known to induce uncontrolled host cell proliferation. Survival of Theileria-transformed leukocytes depends strictly on constitutive nuclear factor kappa B (NF-kappaB) activity. We found that this was mediated by recruitment of the multisubunit IkappaB kinase (IKK) into large, activated foci on the parasite surface. IKK signalosome assembly was specific for the transforming schizont stage of the parasite and was down-regulated upon differentiation into the nontransforming merozoite stage. Our findings provide insights into IKK activation and how pathogens subvert host-cell signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heussler, Volker T -- Rottenberg, Sven -- Schwab, Rebekka -- Kuenzi, Peter -- Fernandez, Paula C -- McKellar, Susan -- Shiels, Brian -- Chen, Zhijian J -- Orth, Kim -- Wallach, David -- Dobbelaere, Dirk A E -- GM63692/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1033-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Pathology, Institute of Animal Pathology, University of Bern, CH-3012 Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411708" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Antiprotozoal Agents/pharmacology ; Apoptosis ; Cattle ; Cell Cycle ; Cell Division ; Cell Line, Transformed ; Cell Nucleus/metabolism ; Down-Regulation ; I-kappa B Kinase ; I-kappa B Proteins/metabolism ; Leukocytes/enzymology/*parasitology/physiology ; Microscopy, Confocal ; NF-kappa B/metabolism ; Naphthoquinones/pharmacology ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Signal Transduction ; Theileria/growth & development/metabolism/*pathogenicity
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  • 42
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    Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (alpha2betabeta'omegasigmaA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel. All sequence-specific contacts with core promoter elements are mediated by the sigma subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the sigma subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced -10 and -35 elements and provides the basis for models of the closed and open promoter complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murakami, Katsuhiko S -- Masuda, Shoko -- Campbell, Elizabeth A -- Muzzin, Oriana -- Darst, Seth A -- GM20470/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- GM61898/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1285-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/12016307" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA, Bacterial/*chemistry/genetics/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Subunits ; Sigma Factor/*chemistry/metabolism ; Templates, Genetic ; Thermus/*enzymology ; *Transcription, Genetic
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    A LAT mutation that inhibits T cell development yet induces lymphoproliferation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-18
    Description: Mice homozygous for a single tyrosine mutation in LAT (linker for activation of T cells) exhibited an early block in T cell maturation but later developed a polyclonal lymphoproliferative disorder and signs of autoimmune disease. T cell antigen receptor (TCR)-induced activation of phospholipase C-gamma1 (PLC-gamma1) and of nuclear factor of activated T cells, calcium influx, interleukin-2 production, and cell death were reduced or abrogated in T cells from LAT mutant mice. In contrast, TCR-induced Erk activation was intact. These results identify a critical role for integrated PLC-gamma1 and Ras-Erk signaling through LAT in T cell development and homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sommers, Connie L -- Park, Cheung-Seog -- Lee, Jan -- Feng, Chiguang -- Fuller, Claudette L -- Grinberg, Alexander -- Hildebrand, Jay A -- Lacana, Emanuela -- Menon, Rashmi K -- Shores, Elizabeth W -- Samelson, Lawrence E -- Love, Paul E -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2040-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065840" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antibodies, Antinuclear/blood ; Antigens, CD5/analysis ; Autoimmune Diseases/immunology ; CD4-Positive T-Lymphocytes/immunology/physiology ; Calcium/metabolism ; Calcium Signaling ; Carrier Proteins/*genetics/*physiology ; Cell Division ; Interleukin-2/biosynthesis ; Isoenzymes/*metabolism ; Lymphocyte Activation ; Lymphoproliferative Disorders/*etiology/immunology/pathology ; MAP Kinase Signaling System ; *Membrane Proteins ; Mice ; Mice, Inbred C57BL ; Mitogen-Activated Protein Kinases/metabolism ; Phenotype ; Phospholipase C gamma ; Phosphoproteins/*genetics/*physiology ; Phosphorylation ; *Point Mutation ; Receptors, Antigen, T-Cell/immunology/metabolism ; Signal Transduction ; T-Lymphocyte Subsets/immunology/physiology ; T-Lymphocytes/*immunology/physiology ; Thymus Gland/cytology/immunology/pathology ; Transcription Factors/metabolism ; Type C Phospholipases/*metabolism ; ras Proteins/metabolism
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    Germline stem cells anchored by adherens junctions in the Drosophila ovary niches (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: How stem cells are recruited to and maintained in their niches is crucial to understanding their regulation and use in regenerative medicine. Here, we demonstrate that DE-cadherin-mediated cell adhesion is required for anchoring germline stem cells (GSCs) in their niches in the Drosophila ovary. Two major components of this adhesion process, DE-cadherin and Armadillo/beta-catenin, accumulate at high levels in the junctions between GSCs and cap cells, one of the niche components. Removal of these proteins from GSCs results in stem cell loss. Furthermore, DE-cadherin is required for recruiting GSCs to their niche. Our study demonstrates that anchorage of GSCs in their niche by DE-cadherin-mediated adhesion is important for stem cell maintenance and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, Xiaoqing -- Zhu, Chun-Hong -- Doan, Chuong -- Xie, Ting -- 1R01 GM64428-01/GM/NIGMS NIH HHS/ -- HD 17608/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1855-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052957" target="_blank"〉PubMed〈/a〉
    Keywords: Adherens Junctions/*physiology ; Alleles ; Animals ; Armadillo Domain Proteins ; Cadherins/genetics/*physiology ; Cell Adhesion ; Cell Differentiation ; Drosophila/cytology/genetics/growth & development/*physiology ; *Drosophila Proteins ; Female ; Insect Proteins/genetics/physiology ; Larva/physiology ; Mutation ; Oocytes/*cytology/physiology/ultrastructure ; Ovary/cytology/growth & development/physiology ; Proto-Oncogene Proteins/genetics/physiology ; Signal Transduction ; Stem Cells/cytology/*physiology/ultrastructure ; *Trans-Activators ; Transcription Factors ; Wnt1 Protein
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  • 45
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    Loss of sex discrimination and male-male aggression in mice deficient for TRP2 (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-02-02
    Description: The mouse vomeronasal organ (VNO) is thought to mediate social behaviors and neuroendocrine changes elicited by pheromonal cues. The molecular mechanisms underlying the sensory response to pheromones and the behavioral repertoire induced through the VNO are not fully characterized. Using the tools of mouse genetics and multielectrode recording, we demonstrate that the sensory activation of VNO neurons requires TRP2, a putative ion channel of the transient receptor potential family that is expressed exclusively in these neurons. Moreover, we show that male mice deficient in TRP2 expression fail to display male-male aggression, and they initiate sexual and courtship behaviors toward both males and females. Our study suggests that, in the mouse, sensory activation of the VNO is essential for sex discrimination of conspecifics and thus ensures gender-specific behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stowers, Lisa -- Holy, Timothy E -- Meister, Markus -- Dulac, Catherine -- Koentges, Georgy -- DC03903/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1493-500. Epub 2002 Jan 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823606" target="_blank"〉PubMed〈/a〉
    Keywords: *Aggression ; Animals ; Chemoreceptor Cells/*physiology ; Crosses, Genetic ; Cues ; Electrophysiology ; Electroporation ; Female ; Gene Targeting ; Male ; Maternal Behavior ; Membrane Proteins/*genetics/*physiology ; Mice ; Mice, Inbred C57BL ; Mutation ; Neurons, Afferent/*physiology ; Odors ; Olfactory Bulb/physiology ; Olfactory Mucosa/physiology ; Pheromones/*physiology/urine ; Sex Characteristics ; *Sexual Behavior, Animal ; Signal Transduction ; TRPC Cation Channels ; Video Recording ; Vomeronasal Organ/*innervation/physiology
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    Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: The structural basis for the divalent cation-dependent binding of heterodimeric alphabeta integrins to their ligands, which contain the prototypical Arg-Gly-Asp sequence, is unknown. Interaction with ligands triggers tertiary and quaternary structural rearrangements in integrins that are needed for cell signaling. Here we report the crystal structure of the extracellular segment of integrin alphaVbeta3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence. The ligand binds at the major interface between the alphaV and beta3 subunits and makes extensive contacts with both. Both tertiary and quaternary changes are observed in the presence of ligand. The tertiary rearrangements take place in betaA, the ligand-binding domain of beta3; in the complex, betaA acquires two cations, one of which contacts the ligand Asp directly and the other stabilizes the ligand-binding surface. Ligand binding induces small changes in the orientation of alphaV relative to beta3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiong, Jian-Ping -- Stehle, Thilo -- Zhang, Rongguang -- Joachimiak, Andrzej -- Frech, Matthias -- Goodman, Simon L -- Arnaout, M Amin -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):151-5. Epub 2002 Mar 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Renal Unit, Leukocyte Biology and Inflammation Program, Structural Biology Program, Massachusetts General Hospital, 149 13th Street, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884718" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Ligands ; Manganese/chemistry ; Models, Molecular ; Oligopeptides/chemistry/*metabolism ; Peptides, Cyclic/chemistry/*metabolism ; *Protein Structure, Quaternary ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Receptors, Vitronectin/*chemistry/*metabolism
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    Role of Hec1 in spindle checkpoint signaling and kinetochore recruitment of Mad1/Mad2 (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: The spindle checkpoint delays sister chromatid separation until all chromosomes have undergone bipolar spindle attachment. Checkpoint failure may result in chromosome mis-segregation and may contribute to tumorigenesis. We showed that the human protein Hec1 was required for the recruitment of Mps1 kinase and Mad1/Mad2 complexes to kinetochores. Depletion of Hec1 impaired chromosome congression and caused persistent activation of the spindle checkpoint, indicating that high steady-state levels of Mad1/Mad2 complexes at kinetochores were not essential for checkpoint signaling. Simultaneous depletion of Hec1 and Mad2 caused catastrophic mitotic exit, making Hec1 an attractive target for the selective elimination of spindle checkpoint-deficient cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin-Lluesma, Silvia -- Stucke, Volker M -- Nigg, Erich A -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2267-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351790" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium-Binding Proteins/*metabolism ; *Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone/physiology ; Chromosomes, Human/physiology/ultrastructure ; Gene Silencing ; HeLa Cells ; Humans ; Kinetochores/*metabolism ; Mad2 Proteins ; Microtubule-Associated Proteins/*metabolism ; Microtubules/metabolism ; *Mitosis ; Nuclear Proteins/*metabolism ; Phenotype ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases ; RNA, Small Interfering ; RNA, Untranslated/metabolism ; Repressor Proteins ; Signal Transduction ; Spindle Apparatus/*physiology/ultrastructure ; Two-Hybrid System Techniques
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    A stem cell molecular signature (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: Mechanisms regulating self-renewal and cell fate decisions in mammalian stem cells are poorly understood. We determined global gene expression profiles for mouse and human hematopoietic stem cells and other stages of the hematopoietic hierarchy. Murine and human hematopoietic stem cells share a number of expressed gene products, which define key conserved regulatory pathways in this developmental system. Moreover, in the mouse, a portion of the genetic program of hematopoietic stem cells is shared with embryonic and neural stem cells. This overlapping set of gene products represents a molecular signature of stem cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivanova, Natalia B -- Dimos, John T -- Schaniel, Christoph -- Hackney, Jason A -- Moore, Kateri A -- Lemischka, Ihor R -- DK42989/DK/NIDDK NIH HHS/ -- DK54493/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):601-4. Epub 2002 Sep 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228721" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Cell Communication ; Cell Cycle ; Cell Differentiation ; Cell Line ; Cell Lineage ; Cell Separation ; Cells, Cultured ; Computational Biology ; Embryo, Mammalian/cytology ; Expressed Sequence Tags ; *Gene Expression ; *Gene Expression Profiling ; Genes, Homeobox ; Hematopoiesis ; Hematopoietic Stem Cell Transplantation ; Hematopoietic Stem Cells/*physiology ; Humans ; Mice ; Neurons/cytology ; Oligonucleotide Array Sequence Analysis ; Signal Transduction ; Stem Cells/*physiology ; Totipotent Stem Cells/*physiology ; Transcription, Genetic
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    S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: Matrix metalloproteinases (MMPs) are implicated in the pathogenesis of neurodegenerative diseases and stroke. However, the mechanism of MMP activation remains unclear. We report that MMP activation involves S-nitrosylation. During cerebral ischemia in vivo, MMP-9 colocalized with neuronal nitric oxide synthase. S-Nitrosylation activated MMP-9 in vitro and induced neuronal apoptosis. Mass spectrometry identified the active derivative of MMP-9, both in vitro and in vivo, as a stable sulfinic or sulfonic acid, whose formation was triggered by S-nitrosylation. These findings suggest a potential extracellular proteolysis pathway to neuronal cell death in which S-nitrosylation activates MMPs, and further oxidation results in a stable posttranslational modification with pathological activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Zezong -- Kaul, Marcus -- Yan, Boxu -- Kridel, Steven J -- Cui, Jiankun -- Strongin, Alex -- Smith, Jeffrey W -- Liddington, Robert C -- Lipton, Stuart A -- AR08505/AR/NIAMS NIH HHS/ -- P01 HD29587/HD/NICHD NIH HHS/ -- R01 AR42750/AR/NIAMS NIH HHS/ -- R01 CA 69306/CA/NCI NIH HHS/ -- R01 EY05477/EY/NEI NIH HHS/ -- R01 EY09024/EY/NEI NIH HHS/ -- R01 NS41207/NS/NINDS NIH HHS/ -- T32 AG00252/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1186-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neuroscience and Aging, Program in Cell Adhesion and Extracellular Matrix Biology, The Burnham Institute, 10901 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/12183632" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Brain Ischemia/*enzymology/pathology ; Cell Line ; Cells, Cultured ; Cerebral Cortex/blood supply/*enzymology/pathology ; Cysteine/*analogs & derivatives/metabolism/pharmacology ; Enzyme Activation ; Enzyme Precursors/genetics/metabolism ; Humans ; Matrix Metalloproteinase 9/chemistry/*metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Models, Molecular ; Neurons/*physiology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/antagonists & inhibitors/metabolism ; Nitric Oxide Synthase Type I ; Oxidation-Reduction ; Phenylmercuric Acetate/*analogs & derivatives/pharmacology ; Rats ; Recombinant Proteins/metabolism ; Reperfusion ; S-Nitrosothiols/*metabolism/pharmacology ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Immunology. The immunological synapse--a multitasking system (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Der Merwe, P Anton -- Davis, Simon J -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1479-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK. anton.vandermerwe@path.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859183" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigen-Presenting Cells/*immunology ; Antigens, CD ; Antigens, CD28/immunology/metabolism ; Antigens, CD80/immunology/metabolism ; Antigens, Differentiation/metabolism ; CD4-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/immunology ; CTLA-4 Antigen ; Dimerization ; Histocompatibility Antigens Class II/metabolism ; *Immunoconjugates ; Immunoglobulin alpha-Chains/immunology/metabolism ; Intercellular Junctions/*immunology ; Ligands ; Lipid Bilayers ; Lymphocyte Activation ; Mice ; Peptides/immunology/metabolism ; Receptor Aggregation ; Receptors, Antigen, T-Cell/*immunology ; Signal Transduction ; T-Lymphocytes/*immunology ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: N-methyl-D-aspartate receptors (NMDARs) mediate ischemic brain damage but also mediate essential neuronal excitation. To treat stroke without blocking NMDARs, we transduced neurons with peptides that disrupted the interaction of NMDARs with the postsynaptic density protein PSD-95. This procedure dissociated NMDARs from downstream neurotoxic signaling without blocking synaptic activity or calcium influx. The peptides, when applied either before or 1 hour after an insult, protected cultured neurons from excitotoxicity, reduced focal ischemic brain damage in rats, and improved their neurological function. This approach circumvents the negative consequences associated with blocking NMDARs and may constitute a practical stroke therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aarts, Michelle -- Liu, Yitao -- Liu, Lidong -- Besshoh, Shintaro -- Arundine, Mark -- Gurd, James W -- Wang, Yu-Tian -- Salter, Michael W -- Tymianski, Michael -- NS 39060/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):846-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Toronto Western Hospital Research Institute, 11-416 MC-PAV, 399 Bathurst Street, Toronto, Ontario M5T 2S8, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399596" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*drug effects/metabolism ; Brain Ischemia/*drug therapy/metabolism ; Calcium/metabolism ; Cells, Cultured ; Cerebral Infarction/*drug therapy/metabolism ; Cyclic GMP/metabolism ; Guanylate Kinase ; In Vitro Techniques ; Intracellular Signaling Peptides and Proteins ; Male ; Membrane Proteins ; Mice ; Mice, Inbred C57BL ; N-Methylaspartate/pharmacology ; Nerve Tissue Proteins/chemistry/*metabolism ; Neurons/drug effects/physiology ; Patch-Clamp Techniques ; Peptides/administration & dosage/*pharmacology/therapeutic use ; Protein Binding ; Rats ; Rats, Sprague-Dawley ; Rats, Wistar ; Receptors, N-Methyl-D-Aspartate/*chemistry/*metabolism ; Recombinant Fusion Proteins/administration & dosage/pharmacology/therapeutic use ; Signal Transduction ; Synaptic Transmission/drug effects
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    Enzymology. A trio of transition metals in anaerobic CO2 fixation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, John W -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):552-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA. john.peters@chemistry.montana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386322" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acetyl Coenzyme A/metabolism ; Aldehyde Oxidoreductases/*chemistry/*metabolism ; Anaerobiosis ; Binding Sites ; Biomass ; Carbon Dioxide/*metabolism ; Carbon Monoxide/metabolism ; Clostridium/enzymology ; Copper/*chemistry ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Iron/*chemistry ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Nickel/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Quaternary
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    Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-03
    Description: Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bracey, Michael H -- Hanson, Michael A -- Masuda, Kim R -- Stevens, Raymond C -- Cravatt, Benjamin F -- R01 DA013173/DA/NIDA NIH HHS/ -- R01 DA013173-02/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1793-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Skaggs Institute for Chemical Biology, 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/12459591" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/antagonists & inhibitors/*chemistry/metabolism ; Animals ; Arachidonic Acids/metabolism ; *Bacterial Proteins ; Binding Sites ; Cannabinoid Receptor Modulators ; Catalysis ; Catalytic Domain ; Cell Membrane/*enzymology ; Crystallography, X-Ray ; Dimerization ; Endocannabinoids ; Helix-Turn-Helix Motifs ; Lipid Bilayers ; Models, Molecular ; Organophosphonates/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Recombinant Proteins/chemistry/metabolism ; Signal Transduction ; Solubility
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    A new UAG-encoded residue in the structure of a methanogen methyltransferase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-25
    Description: Genes encoding methanogenic methylamine methyltransferases all contain an in-frame amber (UAG) codon that is read through during translation. We have identified the UAG-encoded residue in a 1.55 angstrom resolution structure of the Methanosarcina barkeri monomethylamine methyltransferase (MtmB). This structure reveals a homohexamer comprised of individual subunits with a TIM barrel fold. The electron density for the UAG-encoded residue is distinct from any of the 21 natural amino acids. Instead it appears consistent with a lysine in amide-linkage to (4R,5R)-4-substituted-pyrroline-5-carboxylate. We suggest that this amino acid be named l-pyrrolysine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hao, Bing -- Gong, Weimin -- Ferguson, Tsuneo K -- James, Carey M -- Krzycki, Joseph A -- Chan, Michael K -- GM43268/GM/NIGMS NIH HHS/ -- RR07707/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 May 24;296(5572):1462-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029132" target="_blank"〉PubMed〈/a〉
    Keywords: Archaeal Proteins/chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; *Codon ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Genes, Archaeal ; Hydrogen Bonding ; Lysine/analogs & derivatives/chemistry/*genetics ; Methanosarcina barkeri/*enzymology/genetics ; Methylamines/metabolism ; Methyltransferases/*chemistry/*genetics/metabolism ; Models, Molecular ; Molecular Weight ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Spectrometry, Mass, Electrospray Ionization
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    A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-19
    Description: A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doukov, Tzanko I -- Iverson, Tina M -- Seravalli, Javier -- Ragsdale, Stephen W -- Drennan, Catherine L -- R01-GM39451/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):567-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386327" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acetyl Coenzyme A/metabolism ; Aldehyde Oxidoreductases/*chemistry/*metabolism ; Anaerobiosis ; Binding Sites ; Carbon Dioxide/metabolism ; Carbon Monoxide/metabolism ; Catalysis ; Clostridium/*enzymology ; Copper/*chemistry ; Crystallography, X-Ray ; Dimerization ; Electron Spin Resonance Spectroscopy ; Hydrophobic and Hydrophilic Interactions ; Iron/*chemistry ; Ligands ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Nickel/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Zinc/chemistry
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    Development. Doublesex in the middle (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burtis, Kenneth C -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1135-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA. kcburtis@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183618" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; DNA-Binding Proteins/*genetics/*physiology ; Drosophila/*embryology/genetics/growth & development ; Drosophila Proteins/*genetics/*physiology ; Female ; Fibroblast Growth Factors/genetics/metabolism ; *Gene Expression Regulation, Developmental ; Genes, Homeobox ; Genes, Insect ; Genitalia, Female/cytology/embryology ; Genitalia, Male/cytology/embryology ; Male ; *Sex Characteristics ; Sex Determination Processes ; *Sex Differentiation ; Signal Transduction
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    The Anopheles genome and comparative insect genomics (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-10-05
    Description: The Anopheles gambiae genome sequence, coupled with the Drosophila melanogaster genome sequence, provides a better understanding of the insects, a group that contains our friends, foes, and competitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaufman, Thomas C -- Severson, David W -- Robinson, Gene E -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):97-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington, IN 47405, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364783" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/anatomy & histology/genetics/growth & development/physiology ; Animals ; Anopheles/anatomy & histology/*genetics/growth & development/physiology ; Bees/anatomy & histology/genetics/growth & development/physiology ; Beetles/genetics ; Behavior, Animal ; Biological Evolution ; Drosophila/genetics/physiology ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Genes, Insect ; *Genome ; *Genomics ; Insect Vectors/anatomy & histology/genetics/growth & development/physiology ; Insects/anatomy & histology/*genetics/growth & development/physiology ; Lepidoptera/genetics ; Sequence Analysis, DNA ; Signal Transduction
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    Shaping the vertebrate body plan by polarized embryonic cell movements (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: Polarized cell movements shape the major features of the vertebrate body plan during development. The head-to-tail body axis of vertebrates is elongated in embryonic stages by "convergent extension" tissue movements. During these movements cells intercalate between one another transverse to the elongating body axis to form a narrower, longer array. Recent discoveries show that these polarized cell movements are controlled by homologs of genes that control the polarity of epithelial cells in the developing wing and eye of the fruit fly, Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keller, Ray -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1950-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Virginia, Charlottesville, VA 22904, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471247" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; *Cell Movement ; *Cell Polarity ; Cell Size ; Drosophila/cytology/genetics/growth & development ; Embryo, Mammalian/*cytology/physiology ; Embryo, Nonmammalian/*cytology/physiology ; Embryonic Development ; Embryonic and Fetal Development ; Gene Expression Regulation, Developmental ; Genes ; Morphogenesis ; Proteins/metabolism ; Signal Transduction ; Vertebrates/*embryology/genetics
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    Close before opening (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-03-02
    Description: As bacteria need iron from the environment to survive, they have evolved active iron transporter proteins in their outer membranes. In her Perspective, Postle discusses new insights into iron transport revealed by the crystal structure of the iron transporter FecA in E. coli (Ferguson et al.).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Postle, K -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1658-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Molecular Biosciences, Washington State University, Pullman, WA 99164, USA. postle@mail.wsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872826" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/chemistry/metabolism ; Bacterial Proteins/metabolism ; Binding Sites ; Biological Transport, Active ; Carrier Proteins/*chemistry/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli/*metabolism ; Escherichia coli Proteins/chemistry/metabolism ; Ferric Compounds/*metabolism ; Ion Channel Gating ; Ligands ; Membrane Proteins/metabolism ; Models, Biological ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; *Receptors, Cell Surface ; Siderophores/metabolism
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    Generating and exploiting polarity in bacteria (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: Bacteria are often highly polarized, exhibiting specialized structures at or near the ends of the cell. Among such structures are actin-organizing centers, which mediate the movement of certain pathogenic bacteria within the cytoplasm of an animal host cell; organized arrays of membrane receptors, which govern chemosensory behavior in swimming bacteria; and asymmetrically positioned septa, which generate specialized progeny in differentiating bacteria. This polarization is orchestrated by complex and dynamic changes in the subcellular localization of signal transduction and cytoskeleton proteins as well as of specific regions of the chromosome. Recent work has provided information on how dynamic subcellular localization occurs and how it is exploited by the bacterial cell. The main task of a bacterial cell is to survive and duplicate itself. The bacterium must replicate its genetic material and divide at the correct site in the cell and at the correct time in the cell cycle with high precision. Each kind of bacterium also executes its own strategy to find nutrients in its habitat and to cope with conditions of stress from its environment. This involves moving toward food, adapting to environmental extremes, and, in many cases, entering and exploiting a eukaryotic host. These activities often involve processes that take place at or near the poles of the cell. Here we explore some of the schemes bacteria use to orchestrate dynamic changes at their poles and how these polar events execute cellular functions. In spite of their small size, bacteria have a remarkably complex internal organization and external architecture. Bacterial cells are inherently asymmetric, some more obviously so than others. The most easily recognized asymmetries involve surface structures, e.g., flagella, pili, and stalks that are preferentially assembled at one pole by many bacteria. "New" poles generated at the cell division plane differ from old poles from the previous round of cell division. Even in Escherichia coli, which is generally thought to be symmetrical, old poles are more static than new poles with respect to cell wall assembly (1), and they differ in the deposition of phospholipid domains (2). There are many instances of differential polar functions; among these is the preferential use of old poles when attaching to host cells as in the interaction of Bradyrhizobium with plant root hairs (3) or the polar pili-mediated attachment of the Pseudomonas aeruginosa pathogen to tracheal epithelia (4). An unusual polar organelle that mediates directed motility on solid surfaces is found in the nonpathogenic bacterium Myxococcus xanthus. The gliding motility of this bacterium is propelled by a nozzle-like structure that squirts a polysaccharide-containing slime from the pole of the cell (5). Interestingly, M. xanthus, which has nozzles at both poles, can reverse direction by closing one nozzle and opening the other in response to end-to-end interactions between cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shapiro, Lucy -- McAdams, Harley H -- Losick, Richard -- GM18568/GM/NIGMS NIH HHS/ -- GM32506/GM/NIGMS NIH HHS/ -- GM51426/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1942-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Stanford University School of Medicine, B300 Beckman Center, Stanford, CA 94305, USA. shapiro@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471245" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/cytology/physiology ; Bacteria/cytology/metabolism/pathogenicity ; *Bacterial Physiological Phenomena ; Bacterial Proteins/*physiology ; Cell Division ; *Cell Polarity ; Chemotaxis ; Chromosomes, Bacterial/metabolism ; Cytoskeleton/metabolism ; Diffusion ; Replication Origin ; Signal Transduction ; Spores, Bacterial/physiology
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    Endocrinology. Divorcing estrogen's bright and dark sides (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):723-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Density/*drug effects ; Breast Neoplasms/pathology ; Cell Division/drug effects ; Cell Nucleus/metabolism ; Cells, Cultured ; Estrenes/*pharmacology ; Estrogens/metabolism/pharmacology ; Female ; Gene Expression Regulation/drug effects ; Humans ; Mice ; Osteoblasts/*drug effects/physiology ; Osteoclasts/*drug effects/physiology ; Ovariectomy ; Receptors, Estrogen/metabolism ; Signal Transduction ; Uterus/drug effects
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    Viral IL-6-induced cell proliferation and immune evasion of interferon activity (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: Lymphoma cells infected with Kaposi's sarcoma-associated herpesvirus are autocrine dependent on virus-derived interleukin-6 (IL-6), but not on cellular IL-6. During viral infection, host cells induce the antiviral factor interferon (IFN) to up-regulate p21, initiate cell cycle arrest, and inhibit virus replication. Viral IL-6, however, blocks IFN signaling. A viral transcriptional program exists in which only the viral IL-6 gene is directly activated by IFN-alpha, allowing the virus to modify its cellular environment by sensing and responding to levels of intracellular IFN signaling. The human cytokine cannot mimic this effect because IFN-alpha down-regulates the IL-6 receptor, gp80. Viral IL-6 bypasses the gp80 regulatory checkpoint by binding directly to the gp130 transducer molecule, resulting in tumor cell autocrine dependence on the viral cytokine for proliferation and survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chatterjee, Malini -- Osborne, Julie -- Bestetti, Giovanna -- Chang, Yuan -- Moore, Patrick S -- CA76586/CA/NCI NIH HHS/ -- CA87661/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1432-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Columbia University, College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434062" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/genetics/metabolism ; Autocrine Communication ; *Cell Division ; Cytokine Receptor gp130 ; Down-Regulation ; Feedback, Physiological ; Genes, Viral ; Herpesvirus 8, Human/genetics/immunology/*physiology ; Humans ; Interferon-alpha/pharmacology/*physiology ; Interleukin-6/genetics/*physiology ; Membrane Glycoproteins/genetics/metabolism ; Mutation ; Promoter Regions, Genetic ; Receptors, Interleukin-6/genetics/metabolism ; Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription, Genetic ; Tumor Cells, Cultured ; Up-Regulation
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    G protein-coupled receptors in Anopheles gambiae (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-10-05
    Description: We used bioinformatic approaches to identify a total of 276 G protein-coupled receptors (GPCRs) from the Anopheles gambiae genome. These include GPCRs that are likely to play roles in pathways affecting almost every aspect of the mosquito's life cycle. Seventy-nine candidate odorant receptors were characterized for tissue expression and, along with 76 putative gustatory receptors, for their molecular evolution relative to Drosophila melanogaster. Examples of lineage-specific gene expansions were observed as well as a single instance of unusually high sequence conservation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, Catherine A -- Fox, A Nicole -- Pitts, R Jason -- Kent, Lauren B -- Tan, Perciliz L -- Chrystal, Mathew A -- Cravchik, Anibal -- Collins, Frank H -- Robertson, Hugh M -- Zwiebel, Laurence J -- F31 DC05265-01A1/DC/NIDCD NIH HHS/ -- R01 DC004692/DC/NIDCD NIH HHS/ -- R01 DC04692-01/DC/NIDCD NIH HHS/ -- U01AI48846/AI/NIAID NIH HHS/ -- U01AI50687/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):176-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364795" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Anopheles/chemistry/*genetics/metabolism ; Computational Biology ; Conserved Sequence ; Drosophila Proteins/chemistry/genetics/metabolism ; Drosophila melanogaster/chemistry/genetics/metabolism ; Evolution, Molecular ; GTP-Binding Proteins/*metabolism ; Gene Amplification ; Gene Expression ; *Genes, Insect ; Genome ; Insect Proteins/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Phylogeny ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; Receptors, Odorant/chemistry/*genetics/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction
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    Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-20
    Description: Class IA phosphoinositide 3-kinases (PI3Ks) are a family of p85/p110 heterodimeric lipid kinases that generate second messenger signals downstream of tyrosine kinases, thereby controlling cell metabolism, growth, proliferation, differentiation, motility, and survival. Mammals express three class IA catalytic subunits: p110alpha, p110beta, and p110delta. It is unclear to what extent these p110 isoforms have overlapping or distinct biological roles. Mice expressing a catalytically inactive form of p110delta (p110delta(D910A)) were generated by gene targeting. Antigen receptor signaling in B and T cells was impaired and immune responses in vivo were attenuated in p110delta mutant mice. They also developed inflammatory bowel disease. These results reveal a selective role for p110delta in immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Okkenhaug, Klaus -- Bilancio, Antonio -- Farjot, Geraldine -- Priddle, Helen -- Sancho, Sara -- Peskett, Emma -- Pearce, Wayne -- Meek, Stephen E -- Salpekar, Ashreena -- Waterfield, Michael D -- Smith, Andrew J H -- Vanhaesebroeck, Bart -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):1031-4. Epub 2002 Jul 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, 91 Riding House Street, London W1W 7BS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130661" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/immunology ; B-Lymphocytes/enzymology/*immunology ; Bone Marrow Cells/cytology ; Catalytic Domain ; Cell Differentiation ; Cell Division ; Female ; Gene Targeting ; Hematopoietic Stem Cells/cytology ; Immunoglobulins/blood ; Inflammatory Bowel Diseases/immunology/pathology ; Interleukin-2/biosynthesis ; Intestinal Mucosa/pathology ; Lymph Nodes/cytology/pathology ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred C57BL ; Phosphatidylinositol 3-Kinases/genetics/*metabolism ; Point Mutation ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Receptors, Antigen, B-Cell/*metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Signal Transduction ; Spleen/cytology/pathology ; T-Lymphocytes/enzymology/*immunology ; Thymus Gland/cytology
    Print ISSN: 0036-8075
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    Structural biology. Force and voltage sensors in one structure (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bezanilla, Francisco -- Perozo, Eduardo -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1562-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, Los Angeles, CA 90095, USA. fbezanil@ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446894" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/physiology ; Cell Membrane/chemistry/physiology ; Crystallization ; Crystallography, X-Ray ; Electric Conductivity ; Escherichia coli/*chemistry/physiology ; Escherichia coli Proteins/*chemistry/*physiology ; Ion Channel Gating ; Ion Channels/*chemistry/*physiology ; *Mechanotransduction, Cellular ; Membrane Potentials ; Models, Molecular ; Osmolar Concentration ; Potassium Channels/chemistry/physiology ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary
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    A critical role for IL-21 in regulating immunoglobulin production (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-26
    Description: The cytokine interleukin-21 (IL-21) is closely related to IL-2 and IL-15, and their receptors all share the common cytokine receptor gamma chain, gammac, which is mutated in humans with X-linked severe combined immunodeficiency disease (XSCID). We demonstrate that, although mice deficient in the receptor for IL-21 (IL-21R) have normal lymphoid development, after immunization, these animals have higher production of the immunoglobulin IgE, but lower IgG1, than wild-type animals. Mice lacking both IL-4 and IL-21R exhibited a significantly more pronounced phenotype, with dysgammaglobulinemia, characterized primarily by a severely impaired IgG response. Thus, IL-21 has a significant influence on the regulation of B cell function in vivo and cooperates with IL-4. This suggests that these gammac-dependent cytokines may be those whose inactivation is primarily responsible for the B cell defect in humans with XSCID.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ozaki, Katsutoshi -- Spolski, Rosanne -- Feng, Carl G -- Qi, Chen-Feng -- Cheng, Jun -- Sher, Alan -- Morse, Herbert C 3rd -- Liu, Chengyu -- Schwartzberg, Pamela L -- Leonard, Warren J -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1630-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-1674, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446913" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody-Producing Cells/immunology ; B-Lymphocytes/*immunology ; CD4-Positive T-Lymphocytes/immunology ; Cells, Cultured ; Gene Targeting ; Genetic Diseases, X-Linked/immunology ; Humans ; Immunization ; Immunoglobulin E/*biosynthesis ; Immunoglobulin G/*biosynthesis ; Immunoglobulins/biosynthesis ; Immunologic Memory ; Interferon-gamma/biosynthesis ; Interleukin-21 Receptor alpha Subunit ; Interleukin-4/biosynthesis/physiology ; Interleukins/*physiology ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Receptors, Interleukin/genetics/metabolism ; Receptors, Interleukin-21 ; Severe Combined Immunodeficiency/immunology ; Signal Transduction ; T-Lymphocytes/immunology ; Toxoplasmosis, Animal/immunology
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    Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-01-19
    Description: Sympathetic nervous system (SNS) regulation of cardiac action potential duration (APD) is mediated by beta adrenergic receptor (betaAR) activation, which increases the slow outward potassium ion current (IKS). Mutations in two human I(KS) channel subunits, hKCNQ1 and hKCNE1, prolong APD and cause inherited cardiac arrhythmias known as LQTS (long QT syndrome). We show that betaAR modulation of I(KS) requires targeting of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA) and protein phosphatase 1 (PP1) to hKCNQ1 through the targeting protein yotiao. Yotiao binds to hKCNQ1 by a leucine zipper motif, which is disrupted by an LQTS mutation (hKCNQ1-G589D). Identification of the hKCNQ1 macromolecular complex provides a mechanism for SNS modulation of cardiac APD through IKS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Steven O -- Kurokawa, Junko -- Reiken, Steven -- Motoike, Howard -- D'Armiento, Jeanine -- Marks, Andrew R -- Kass, Robert S -- P01HL67849-01/HL/NHLBI NIH HHS/ -- R01-AI39794/AI/NIAID NIH HHS/ -- R01-HL44365-07/HL/NHLBI NIH HHS/ -- R01-HL56180/HL/NHLBI NIH HHS/ -- R01-HL56810-05/HL/NHLBI NIH HHS/ -- R01-HL61503/HL/NHLBI NIH HHS/ -- R01-HL68093/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):496-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Center for Molecular Cardiology, Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799244" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; A Kinase Anchor Proteins ; Action Potentials ; *Adaptor Proteins, Signal Transducing ; Amino Acid Substitution ; Animals ; CHO Cells ; Carrier Proteins/*metabolism ; Cricetinae ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/*metabolism ; Cytoskeletal Proteins/*metabolism ; Humans ; KCNQ Potassium Channels ; KCNQ1 Potassium Channel ; Leucine Zippers ; Macromolecular Substances ; Mice ; Mice, Transgenic ; Mutation ; Myocardium/cytology/*metabolism ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Potassium/metabolism ; Potassium Channels/chemistry/genetics/*metabolism ; *Potassium Channels, Voltage-Gated ; Protein Phosphatase 1 ; Receptors, Adrenergic, beta/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Transduction
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    Connecting chromosomes, crisis, and cancer (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-07-27
    Description: Cancer is a disease of impaired genome stability. The molecular forces that maintain genome integrity and sense altered chromosome structure are invariably subverted in cancer cells. Here, we explore the contrasting contributions of telomeres in the initiation and suppression of cancer and review the evidence supporting a role for telomere dysfunction as a mechanism driving the radical chromosomal aberrations that typify cancer genomes. Recent work suggests that passage of cells through crisis in the setting of deactivated DNA damage checkpoints provides a mutational mechanism that can generate the diverse genetic alterations required for cancer initiation. A greater understanding of telomere-induced crisis and the cell's crisis management mechanisms should guide the rational development of new therapeutics for cancer and other disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maser, Richard S -- DePinho, Ronald A -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):565-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, M413, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142527" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle ; Cell Division ; *Cell Transformation, Neoplastic ; Cells, Cultured ; DNA Damage ; DNA Repair ; Disease Progression ; Genetic Therapy ; Humans ; Neoplasms/*genetics/pathology/*physiopathology ; Signal Transduction ; Telomerase/antagonists & inhibitors/*metabolism ; Telomere/*physiology/ultrastructure
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    Control of the selectivity of the aquaporin water channel family by global orientational tuning (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-04-20
    Description: Aquaporins are transmembrane channels found in cell membranes of all life forms. We examine their apparently paradoxical property, facilitation of efficient permeation of water while excluding protons, which is of critical importance to preserving the electrochemical potential across the cell membrane. We have determined the structure of the Escherichia coli aquaglyceroporin GlpF with bound water, in native (2.7 angstroms) and in W48F/F200T mutant (2.1 angstroms) forms, and carried out 12-nanosecond molecular dynamics simulations that define the spatial and temporal probability distribution and orientation of a single file of seven to nine water molecules inside the channel. Two conserved asparagines force a central water molecule to serve strictly as a hydrogen bond donor to its neighboring water molecules. Assisted by the electrostatic potential generated by two half-membrane spanning loops, this dictates opposite orientations of water molecules in the two halves of the channel, and thus prevents the formation of a "proton wire," while permitting rapid water diffusion. Both simulations and observations revealed a more regular distribution of channel water and an increased water permeability for the W48F/F200T mutant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tajkhorshid, Emad -- Nollert, Peter -- Jensen, Morten O -- Miercke, Larry J W -- O'Connell, Joseph -- Stroud, Robert M -- Schulten, Klaus -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):525-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theoretical Biophysics Group, Beckman Institute, University of Illinois at Urbana-Champaign, 405 North Mathews, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964478" target="_blank"〉PubMed〈/a〉
    Keywords: Aquaporins/*chemistry/genetics/metabolism ; Asparagine/chemistry ; Chemistry, Physical ; Computer Simulation ; Crystallography, X-Ray ; Diffusion ; Electrochemistry ; Escherichia coli ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Glycerol/metabolism ; Hydrogen Bonding ; Models, Molecular ; Mutation ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Secondary ; Protons ; Static Electricity ; Water/chemistry/*metabolism
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    Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-01-19
    Description: Protein-protein interactions and calcium entry through the N-methyl-d-aspartate (NMDA)-type glutamate receptor regulate synaptic development and plasticity in the central nervous system. The EphB receptor tyrosine kinases are localized at excitatory synapses where they cluster and associate with NMDA receptors. We identified a mechanism whereby EphBs modulate NMDA receptor function. EphrinB2 activation of EphB in primary cortical neurons potentiates NMDA receptor-dependent influx of calcium. Treatment of cells with ephrinB2 led to NMDA receptor tyrosine phosphorylation through activation of the Src family of tyrosine kinases. These ephrinB2-dependent events result in enhanced NMDA receptor-dependent gene expression. Our findings indicate that ephrinB2 stimulation of EphB modulates the functional consequences of NMDA receptor activation and suggest a mechanism whereby activity-independent and activity-dependent signals converge to regulate the development and remodeling of synaptic connections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takasu, Mari A -- Dalva, Matthew B -- Zigmond, Richard E -- Greenberg, Michael E -- CA43855/CA/NCI NIH HHS/ -- HD18655/HD/NICHD NIH HHS/ -- NS12651/NS/NINDS NIH HHS/ -- NS17512/NS/NINDS NIH HHS/ -- R01 NS045500/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):491-5. Epub 2001 Dec 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, and the Department of Neurobiology, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/pharmacology ; Calcium/*metabolism ; Cell Line ; Cells, Cultured ; Cerebral Cortex/cytology/embryology ; Cyclic AMP Response Element-Binding Protein/metabolism ; Ephrin-B2 ; *Gene Expression Regulation ; Genes, Reporter ; Glutamic Acid/metabolism ; Humans ; Immunoglobulin Fc Fragments ; Membrane Proteins/*metabolism/pharmacology ; Models, Neurological ; Mutation ; Neurons/*metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fyn ; Rats ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptor, EphB4 ; Receptors, Eph Family ; Receptors, N-Methyl-D-Aspartate/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism/pharmacology ; Signal Transduction ; Synapses/metabolism ; Transcription, Genetic ; src-Family Kinases/metabolism
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    Dynamics of thymocyte-stromal cell interactions visualized by two-photon microscopy (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: Thymocytes are selected to mature according to their ability to interact with self major histocompatibility complex (MHC)-peptide complexes displayed on the thymic stroma. Using two-photon microscopy, we performed real-time analysis of the cellular contacts made by developing thymocytes undergoing positive selection in a three-dimensional thymic organ culture. A large fraction of thymocytes within these cultures were highly motile. MHC recognition was found to increase the duration of thymocyte-stromal cell interactions and occurred as both long-lived cellular associations displaying stable cell-cell contacts and as shorter, highly dynamic contacts. Our results identify the diversity and dynamics of thymocyte interactions during positive selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bousso, Philippe -- Bhakta, Nirav R -- Lewis, Richard S -- Robey, Ellen -- AI32985/AI/NIAID NIH HHS/ -- AI42033/AI/NIAID NIH HHS/ -- GM45374/GM/NIGMS NIH HHS/ -- R01 GM045374/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1876-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052962" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen Presentation ; Benzopyrans ; CD8-Positive T-Lymphocytes/immunology ; Cell Aggregation ; *Cell Communication ; Cell Movement ; Cell Size ; Coculture Techniques ; Fluoresceins ; Fluorescent Dyes ; Histocompatibility Antigens Class I/*immunology ; Lasers ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Microscopy/methods ; Naphthols ; Organ Culture Techniques ; Photons ; Receptors, Antigen, T-Cell/*immunology ; Rhodamines ; Signal Transduction ; Stromal Cells/immunology/*physiology ; Succinimides ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/cytology/immunology/*physiology ; Thymus Gland/cytology/*immunology ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular mechanisms of axon guidance (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: Axons are guided along specific pathways by attractive and repulsive cues in the extracellular environment. Genetic and biochemical studies have led to the identification of highly conserved families of guidance molecules, including netrins, Slits, semaphorins, and ephrins. Guidance cues steer axons by regulating cytoskeletal dynamics in the growth cone through signaling pathways that are still only poorly understood. Elaborate regulatory mechanisms ensure that a given cue elicits the right response from the right axons at the right time but is otherwise ignored. With such regulatory mechanisms in place, a relatively small number of guidance factors can be used to generate intricate patterns of neuronal wiring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickson, Barry J -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1959-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology, Dr. Bohr-gasse 7, A-1030 Vienna, Austria. dickson@nt.imp.univie.ac.at〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471249" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology/ultrastructure ; Cues ; Cytoskeleton/physiology ; Ephrins/physiology ; Growth Cones/*physiology/ultrastructure ; Intercellular Signaling Peptides and Proteins/*physiology ; Morphogenesis ; Nerve Growth Factors/physiology ; Nerve Tissue Proteins/physiology ; Nucleotides, Cyclic/metabolism ; Protein Biosynthesis ; Receptors, Cell Surface/physiology ; Semaphorins/physiology ; Signal Transduction
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    Cell biology. The different hues of lipid rafts (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Meer, Gerrit -- New York, N.Y. -- Science. 2002 May 3;296(5569):855-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Membrane Enzymology, CBLE, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands. g.vanmeer@chem.uu.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988557" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Caveolae/metabolism ; Cholesterol/analysis ; Energy Transfer ; Fluorescence ; Glycosylphosphatidylinositols/analysis ; Green Fluorescent Proteins ; Lipid Metabolism ; Luminescent Proteins/*metabolism ; Membrane Microdomains/chemistry/*metabolism/physiology ; Models, Biological ; Protein Prenylation ; Proteins/*metabolism ; Signal Transduction ; Spectrometry, Fluorescence ; Sphingolipids/analysis ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structural genomics. Tapping DNA for structures produces a trickle (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):948-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411682" target="_blank"〉PubMed〈/a〉
    Keywords: Automation ; Bacterial Proteins/chemistry ; Computational Biology ; Crystallization ; Crystallography, X-Ray ; *Genomics ; Humans ; International Cooperation ; Nuclear Magnetic Resonance, Biomolecular ; *Protein Conformation ; Protein Folding ; Proteins/*chemistry ; *Proteomics ; Robotics ; Sequence Analysis, Protein ; Software ; Solubility
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Regulation of cerebral cortical size by control of cell cycle exit in neural precursors (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-20
    Description: Transgenic mice expressing a stabilized beta-catenin in neural precursors develop enlarged brains with increased cerebral cortical surface area and folds resembling sulci and gyri of higher mammals. Brains from transgenic animals have enlarged lateral ventricles lined with neuroepithelial precursor cells, reflecting an expansion of the precursor population. Compared with wild-type precursors, a greater proportion of transgenic precursors reenter the cell cycle after mitosis. These results show that beta-catenin can function in the decision of precursors to proliferate or differentiate during mammalian neuronal development and suggest that beta-catenin can regulate cerebral cortical size by controlling the generation of neural precursor cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chenn, Anjen -- Walsh, Christopher A -- R01NS32457/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):365-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130776" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Apoptosis ; Basic Helix-Loop-Helix Transcription Factors ; Brain/anatomy & histology/embryology ; Cell Adhesion Molecules, Neuronal/genetics/metabolism ; Cell Count ; *Cell Cycle ; Cell Differentiation ; Cell Division ; Cerebral Cortex/anatomy & histology/*embryology/metabolism ; Cytoskeletal Proteins/genetics/*metabolism ; DNA-Binding Proteins/genetics/metabolism ; Epithelium/embryology ; Extracellular Matrix Proteins/genetics/metabolism ; Fungal Proteins/genetics/metabolism ; In Situ Hybridization ; Ki-67 Antigen/genetics/metabolism ; Mice ; Mice, Transgenic ; Mitosis ; Nerve Tissue Proteins ; Neurons/cytology/metabolism/*physiology ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Serine Endopeptidases ; Signal Transduction ; Stem Cells/cytology/metabolism/*physiology ; *Trans-Activators ; beta Catenin
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    53BP1, a mediator of the DNA damage checkpoint (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-05
    Description: 53BP1 binds to the tumor suppressor protein p53 and has a potential role in DNA damage responses. We used small interfering RNA (siRNA) directed against 53BP1 in mammalian cells to demonstrate that 53BP1 is a key transducer of the DNA damage checkpoint signal. 53BP1 was required for p53 accumulation, G2-M checkpoint arrest, and the intra-S-phase checkpoint in response to ionizing radiation. 53BP1 played a partially redundant role in phosphorylation of the downstream checkpoint effector proteins Brca1 and Chk2 but was required for the formation of Brca1 foci in a hierarchical branched pathway for the recruitment of repair and signaling proteins to sites of DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Bin -- Matsuoka, Shuhei -- Carpenter, Phillip B -- Elledge, Stephen J -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1435-8. Epub 2002 Oct 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Mars McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364621" target="_blank"〉PubMed〈/a〉
    Keywords: BRCA1 Protein/metabolism ; Carrier Proteins/genetics/*metabolism ; Cell Cycle Proteins/metabolism ; Checkpoint Kinase 2 ; DNA/biosynthesis ; *DNA Damage ; *G2 Phase ; Histones/metabolism ; Humans ; *Intracellular Signaling Peptides and Proteins ; *Mitosis ; Nuclear Proteins/metabolism ; *Phosphoproteins ; Phosphorylation ; Protein Kinases/metabolism ; *Protein-Serine-Threonine Kinases ; RNA, Small Interfering ; Radiation, Ionizing ; *S Phase ; Signal Transduction ; Tumor Suppressor Protein p53/metabolism
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    Cell biology. PARP-1--a perpetrator of apoptotic cell death? (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiarugi, Alberto -- Moskowitz, Michael A -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):200-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Preclinical and Clinical Pharmacology, University of Florence, 50139 Florence, Italy. alberto.chiarugi@umassmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114611" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; *Apoptosis ; Apoptosis Inducing Factor ; Caspases/metabolism ; Cell Compartmentation ; Cell Nucleus/enzymology/metabolism ; Cytochrome c Group/metabolism ; Enzyme Activation ; Flavoproteins/*metabolism ; Humans ; Membrane Proteins/*metabolism ; Mitochondria/*metabolism ; NAD/metabolism ; Poly Adenosine Diphosphate Ribose/metabolism ; Poly(ADP-ribose) Polymerases/genetics/*metabolism ; Signal Transduction
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    Tumstatin, an endothelial cell-specific inhibitor of protein synthesis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: Tumstatin is a 28-kilodalton fragment of type IV collagen that displays both anti-angiogenic and proapoptotic activity. Here we show that tumstatin functions as an endothelial cell-specific inhibitor of protein synthesis. Through a requisite interaction with alphaVbeta3 integrin, tumstatin inhibits activation of focal adhesion kinase (FAK), phosphatidylinositol 3-kinase (PI3-kinase), protein kinase B (PKB/Akt), and mammalian target of rapamycin (mTOR), and it prevents the dissociation of eukaryotic initiation factor 4E protein (eIF4E) from 4E-binding protein 1. These results establish a role for integrins in mediating cell-specific inhibition of cap-dependent protein synthesis and suggest a potential mechanism for tumstatin's selective effects on endothelial cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maeshima, Yohei -- Sudhakar, Akulapalli -- Lively, Julie C -- Ueki, Kohjiro -- Kharbanda, Surender -- Kahn, C Ronald -- Sonenberg, Nahum -- Hynes, Richard O -- Kalluri, Raghu -- DK-51711/DK/NIDDK NIH HHS/ -- DK-55001/DK/NIDDK NIH HHS/ -- P01-HL66105/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Matrix Biology, Department of Medicine and the Cancer Center, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778052" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Autoantigens/chemistry/metabolism/*pharmacology ; Carrier Proteins/metabolism ; Cattle ; Cells, Cultured ; Collagen Type IV/chemistry/metabolism/*pharmacology ; Endothelium, Vascular/*cytology/drug effects/*metabolism ; Enzyme Activation/drug effects ; Eukaryotic Initiation Factor-4E ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Humans ; Mice ; Molecular Sequence Data ; Peptide Fragments/pharmacology ; Peptide Initiation Factors/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; *Protein Biosynthesis/drug effects ; Protein Kinase Inhibitors ; Protein Kinases/metabolism ; Protein Synthesis Inhibitors/*pharmacology ; *Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; RNA Caps/metabolism ; RNA, Messenger/genetics/metabolism ; Receptors, Vitronectin/metabolism ; Signal Transduction ; TOR Serine-Threonine Kinases ; Tumor Cells, Cultured
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    Influence of SHIP on the NK repertoire and allogeneic bone marrow transplantation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-16
    Description: Natural killer cell (NK) receptors for major histocompatibility complex (MHC) class I influence engraftment and graft-versus-tumor effects after allogeneic bone marrow transplantation. We find that SH2-containing inositol phosphatase (SHIP) influences the repertoire of NK receptors. In adult SHIP-/- mice, the NK compartment is dominated by cells that express two inhibitory receptors capable of binding either self or allogeneic MHC ligands. This promiscuous repertoire has significant functional consequences, because SHIP-/- mice fail to reject fully mismatched allogeneic marrow grafts and show enhanced survival after such transplants. Thus, SHIP plays an important role in two processes that limit the success of allogeneic marrow transplantation: graft rejection and graft-versus-host disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Jia-Wang -- Howson, Julie M -- Ghansah, Tomar -- Desponts, Caroline -- Ninos, John M -- May, Sarah L -- Nguyen, Kim H T -- Toyama-Sorimachi, Noriko -- Kerr, William G -- P01 NS27405/NS/NINDS NIH HHS/ -- R01 DK54767/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2094-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunology Program, H. Lee Moffitt Comprehensive Cancer Center and Research Institute, University of South Florida, Tampa, FL 33612, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896280" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; *Antigens, Ly ; Bone Marrow Transplantation/*immunology ; Cell Survival ; Graft Rejection/*immunology ; Graft Survival ; Graft vs Host Disease/*immunology ; H-2 Antigens/immunology/metabolism ; Haplotypes ; Histocompatibility Antigens Class I/immunology/metabolism ; Killer Cells, Natural/enzymology/*immunology/metabolism ; *Lectins, C-Type ; Ligands ; Lymphocyte Count ; Lymphocyte Subsets/immunology/metabolism ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Inbred A ; Mice, Inbred BALB C ; NK Cell Lectin-Like Receptor Subfamily D ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphoric Monoester Hydrolases/chemistry/genetics/*metabolism ; Phosphorylation ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Receptors, Immunologic/metabolism ; Receptors, NK Cell Lectin-Like ; Signal Transduction ; Transplantation, Homologous ; src Homology Domains
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    The protein kinase complement of the human genome (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-12-10
    Description: We have catalogued the protein kinase complement of the human genome (the "kinome") using public and proprietary genomic, complementary DNA, and expressed sequence tag (EST) sequences. This provides a starting point for comprehensive analysis of protein phosphorylation in normal and disease states, as well as a detailed view of the current state of human genome analysis through a focus on one large gene family. We identify 518 putative protein kinase genes, of which 71 have not previously been reported or described as kinases, and we extend or correct the protein sequences of 56 more kinases. New genes include members of well-studied families as well as previously unidentified families, some of which are conserved in model organisms. Classification and comparison with model organism kinomes identified orthologous groups and highlighted expansions specific to human and other lineages. We also identified 106 protein kinase pseudogenes. Chromosomal mapping revealed several small clusters of kinase genes and revealed that 244 kinases map to disease loci or cancer amplicons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manning, G -- Whyte, D B -- Martinez, R -- Hunter, T -- Sudarsanam, S -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1912-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉SUGEN Inc., 230 East Grand Avenue, South San Francisco, CA 94080, USA. gerard-manning@sugen.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalysis ; Chromosome Mapping ; Computational Biology ; Databases, Genetic ; Genes ; *Genome, Human ; Humans ; Neoplasms/genetics ; Phylogeny ; Protein Kinases/chemistry/classification/*genetics/*metabolism ; Protein Structure, Tertiary ; Pseudogenes ; Sequence Analysis, DNA ; Signal Transduction
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    Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-21
    Description: The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunt, John F -- Weinkauf, Sevil -- Henry, Lisa -- Fak, John J -- McNicholas, Paul -- Oliver, Donald B -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2018-26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, 702A Fairchild Center, MC2434, Columbia University, New York, NY 10027, USA. hunt@sid.bio.columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242434" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/chemistry/*metabolism ; Adenosine Triphosphatases/*chemistry/*metabolism ; Adenosine Triphosphate/chemistry/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacillus subtilis/*enzymology ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Helicases/chemistry ; DNA, Bacterial/chemistry/metabolism ; DNA, Single-Stranded/chemistry/metabolism ; Dimerization ; Escherichia coli ; Escherichia coli Proteins/*chemistry/*metabolism ; Eukaryotic Initiation Factor-4A ; Fluorescence Polarization ; Fourier Analysis ; Hydrogen Bonding ; Ligands ; Membrane Transport Proteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptide Initiation Factors/chemistry ; Peptides/chemistry ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Precursors/metabolism ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Temperature
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    Structural biology. LDL receptor's beta-propeller displaces LDL (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Innerarity, Thomas L -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2337-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Cardiovascular Disease, San Francisco, CA 94110, USA. tinnerarity@gladstone.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493900" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein B-100 ; Apolipoproteins B/metabolism ; Apolipoproteins E/metabolism ; Chemistry, Physical ; Crystallization ; Crystallography, X-Ray ; Endosomes/*metabolism ; Epidermal Growth Factor/chemistry ; Humans ; Hydrogen-Ion Concentration ; Ligands ; Lipoproteins, LDL/*metabolism ; Lysosomes/metabolism ; Models, Biological ; Physicochemical Phenomena ; Protein Binding ; Protein Precursors/chemistry ; Protein Structure, Tertiary ; Receptors, LDL/*chemistry/*metabolism ; Repetitive Sequences, Amino Acid
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    Biochemistry. DNA building block reinvented (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murzin, Alexey G -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):61-2. Epub 2002 May 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, UK. agm@mrc-lmb.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029066" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/enzymology ; Binding Sites ; Crystallography, X-Ray ; Deoxyuracil Nucleotides/metabolism ; Drug Design ; Enzyme Inhibitors ; Evolution, Molecular ; Flavin-Adenine Dinucleotide/metabolism ; Helicobacter pylori/*enzymology ; Humans ; Methyltransferases/chemistry/metabolism ; Models, Molecular ; Phylogeny ; Protein Conformation ; Protein Structure, Tertiary ; Protozoan Proteins/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Tetrahydrofolates/metabolism ; Thermotoga maritima/*enzymology ; Thymidine Monophosphate/*biosynthesis ; Thymidylate Synthase/antagonists & inhibitors/*chemistry/genetics/*metabolism
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    Structural basis of transcription activation: the CAP-alpha CTD-DNA complex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: The Escherichia coli catabolite activator protein (CAP) activates transcription at P(lac), P(gal), and other promoters through interactions with the RNA polymerase alpha subunit carboxyl-terminal domain (alphaCTD). We determined the crystal structure of the CAP-alphaCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alphaCTD, and alphaCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and alphaCTD, and the interface between CAP and alphaCTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benoff, Brian -- Yang, Huanwang -- Lawson, Catherine L -- Parkinson, Gary -- Liu, Jinsong -- Blatter, Erich -- Ebright, Yon W -- Berman, Helen M -- Ebright, Richard H -- GM21589/GM/NIGMS NIH HHS/ -- GM41376/GM/NIGMS NIH HHS/ -- GM64375/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1562-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute and Department of Chemistry, Howard Hughes Medical Institute, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202833" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Cyclic AMP Receptor Protein/*chemistry/metabolism/physiology ; DNA/*chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism/physiology ; Macromolecular Substances ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; *Transcription, Genetic ; Transcriptional Activation
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  • 85
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    Apoptosis. A cinderella caspase takes center stage (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumar, Sharad -- Vaux, David L -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1290-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hanson Institute, Frome Road, Adelaide 5000, Australia. sharad.kumar@imvs.sa.gov.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193776" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptotic Protease-Activating Factor 1 ; Caspase 2 ; Caspase 3 ; Caspase 9 ; Caspases/genetics/*metabolism ; Cell Line, Transformed ; Cytochrome c Group/metabolism ; Enzyme Activation ; Humans ; Mice ; Mice, Knockout ; Mitochondria/metabolism/*physiology ; Models, Biological ; Permeability ; Protein Transport ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-bcl-2/metabolism ; RNA, Small Interfering ; RNA, Untranslated ; Signal Transduction ; Tumor Cells, Cultured ; bcl-2-Associated X Protein
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  • 86
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    The neurotrophin receptor p75NTR as a positive modulator of myelination (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: Schwann cells in developing and regenerating peripheral nerves express elevated levels of the neurotrophin receptor p75NTR. Neurotrophins are key mediators of peripheral nervous system myelination. Our results show that myelin formation is inhibited in the absence of functional p75NTR and enhanced by blocking TrkC activity. Moreover, the enhancement of myelin formation by endogenous brain-derived neurotrophic factor is mediated by the p75NTR receptor, whereas TrkC receptors are responsible for neurotrophin-3 inhibition. Thus p75NTR and TrkC receptors have opposite effects on myelination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cosgaya, Jose M -- Chan, Jonah R -- Shooter, Eric M -- NS04270/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, 299 Campus Drive, Fairchild Building, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424382" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/immunology ; Axons/physiology ; Brain-Derived Neurotrophic Factor/pharmacology/physiology ; Coculture Techniques ; Ganglia, Spinal/cytology ; Immunohistochemistry ; Mice ; Models, Neurological ; Myelin P0 Protein/metabolism ; Myelin Sheath/*physiology ; Myelin-Associated Glycoprotein/metabolism ; Neurotrophin 3/pharmacology/physiology ; Rats ; Rats, Sprague-Dawley ; Receptor, Nerve Growth Factor ; Receptor, trkB/metabolism ; Receptor, trkC/metabolism ; Receptors, Nerve Growth Factor/immunology/*physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Schwann Cells/*physiology ; Sciatic Nerve/cytology/metabolism ; Signal Transduction
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  • 87
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    Neuroscience. It takes more than two to Nogo (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woolf, Clifford J -- Bloechlinger, Stefan -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1132-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neural Plasticity Research Group, Department of Anesthesia, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA. woolf.clifford@mgh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183616" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/metabolism ; Axons/*physiology ; Binding Sites ; Binding, Competitive ; Central Nervous System/physiology ; GPI-Linked Proteins ; Gangliosides/metabolism ; Growth Cones/physiology ; Models, Neurological ; Myelin Proteins/chemistry/*metabolism/pharmacology ; Myelin-Associated Glycoprotein/chemistry/genetics/*metabolism/pharmacology ; Myelin-Oligodendrocyte Glycoprotein ; Nerve Regeneration ; Neurons/*physiology ; Oligodendroglia/metabolism ; Peptide Fragments/metabolism/pharmacology ; Protein Structure, Tertiary ; Receptor, Nerve Growth Factor ; Receptors, Cell Surface/*metabolism ; Receptors, Nerve Growth Factor/metabolism ; Signal Transduction ; Spinal Cord Injuries/physiopathology ; rho GTP-Binding Proteins/metabolism
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  • 88
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    Neuropeptides and peptide hormones in Anopheles gambiae (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-10-05
    Description: The African malaria mosquito, Anopheles gambiae, is specialized for rapid completion of development and reproduction. A vertebrate blood meal is required for egg production, and multiple feedings subsequently allow transmission of malaria parasites, Plasmodium spp. Regulatory peptides from 35 genes annotated from the A. gambiae genome likely coordinate these and other physiological processes. Plasmodium parasites may affect actions of newly identified insulin-like peptides, which coordinate growth and reproduction of its vector, A. gambiae, as in Drosophila melanogaster, Caenorhabditis elegans, and mammals. This genomic information provides a basis to expand understanding of hematophagy and pathogen transmission in this mosquito.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riehle, Michael A -- Garczynski, Stephen F -- Crim, Joe W -- Hill, Catherine A -- Brown, Mark R -- AI33108/AI/NIAID NIH HHS/ -- R01 AI033108/AI/NIAID NIH HHS/ -- U01 AI48846/AI/NIAID NIH HHS/ -- U01 AI50687/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):172-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of Georgia, Athens, GA 30602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364794" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anopheles/chemistry/genetics/parasitology/*physiology ; Blood ; Computational Biology ; Cues ; Ecdysteroids/secretion ; Feeding Behavior ; Female ; Genes, Insect ; Homeostasis ; Insect Hormones/chemistry/genetics/*metabolism ; Insect Proteins/chemistry/genetics/*metabolism ; Insulin/metabolism ; Molecular Sequence Data ; Molting ; Neuropeptides/chemistry/genetics/*metabolism ; Peptides/chemistry/genetics/*metabolism ; Plasmodium/physiology ; Signal Transduction ; Water-Electrolyte Balance
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  • 89
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    Structure of the extracellular region of HER3 reveals an interdomain tether (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-08-03
    Description: We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family. The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor. The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling. These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Hyun-Soo -- Leahy, Daniel J -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1330-3. Epub 2002 Aug 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12154198" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; CHO Cells ; Cricetinae ; Crystallography, X-Ray ; Dimerization ; Epidermal Growth Factor/chemistry/metabolism ; Humans ; Hydrogen Bonding ; Ligands ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptor, Epidermal Growth Factor/chemistry/metabolism ; Receptor, ErbB-3/*chemistry/metabolism ; Recombinant Proteins/chemistry ; Signal Transduction
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  • 90
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    Activation of endothelial cell protease activated receptor 1 by the protein C pathway (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-06-08
    Description: The coagulant and inflammatory exacerbation in sepsis is counterbalanced by the protective protein C (PC) pathway. Activated PC (APC) was shown to use the endothelial cell PC receptor (EPCR) as a coreceptor for cleavage of protease activated receptor 1 (PAR1) on endothelial cells. Gene profiling demonstrated that PAR1 signaling could account for all APC-induced protective genes, including the immunomodulatory monocyte chemoattractant protein-1 (MCP-1), which was selectively induced by activation of PAR1, but not PAR2. Thus, the prototypical thrombin receptor is the target for EPCR-dependent APC signaling, suggesting a role for this receptor cascade in protection from sepsis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riewald, Matthias -- Petrovan, Ramona J -- Donner, Aaron -- Mueller, Barbara M -- Ruf, Wolfram -- P01-HL16411/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1880-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, C204, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052963" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Blood Coagulation Factors ; Cell Line ; Cells, Cultured ; Chemokine CCL2/genetics ; DNA-Binding Proteins/genetics ; Endothelium, Vascular/cytology/*metabolism ; Enzyme Activation ; Gene Expression Profiling ; Gene Expression Regulation ; Humans ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligonucleotide Array Sequence Analysis ; Phosphorylation ; Protein C/*metabolism ; Receptor, PAR-1 ; Receptor, PAR-2 ; Receptors, Cell Surface/metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Receptors, Thrombin/agonists/*metabolism ; Signal Transduction ; Thrombin/metabolism ; Transcription Factors/genetics
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  • 91
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    Generation of self-incompatible Arabidopsis thaliana by transfer of two S locus genes from A. lyrata (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-07-13
    Description: Transitions from cross-fertilizing to self-fertilizing mating systems have occurred frequently in natural and domesticated plant populations, but the underlying genetic causes are unknown. We show that gene transfer of the stigma receptor kinase SRK and its pollen-borne ligand SCR from one S-locus haplotype of the self-incompatible and cross-fertilizing Arabidopsis lyrata is sufficient to impart self-incompatibility phenotype in self-fertile Arabidopsis thaliana, which lacks functional orthologs of these genes. This successful complementation demonstrates that the signaling cascade leading to inhibition of self-related pollen was maintained in A. thaliana. Analysis of self-incompatibility will be facilitated by the tools available in this species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nasrallah, Mikhail E -- Liu, Pei -- Nasrallah, June B -- GM57527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):247-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Cornell University, Ithaca, NY 14853, USA. men4@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114625" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/*physiology ; Arabidopsis Proteins/*genetics/metabolism ; Crosses, Genetic ; *Genes, Plant ; Genetic Complementation Test ; Haplotypes ; Mutation ; Phenotype ; Plant Proteins ; Plants, Genetically Modified ; Pollen/physiology ; Protein Kinases/*genetics/metabolism ; Reproduction ; Signal Transduction ; Species Specificity ; Transformation, Genetic ; Transgenes
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  • 92
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    Immunity-related genes and gene families in Anopheles gambiae (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-10-05
    Description: We have identified 242 Anopheles gambiae genes from 18 gene families implicated in innate immunity and have detected marked diversification relative to Drosophila melanogaster. Immune-related gene families involved in recognition, signal modulation, and effector systems show a marked deficit of orthologs and excessive gene expansions, possibly reflecting selection pressures from different pathogens encountered in these insects' very different life-styles. In contrast, the multifunctional Toll signal transduction pathway is substantially conserved, presumably because of counterselection for developmental stability. Representative expression profiles confirm that sequence diversification is accompanied by specific responses to different immune challenges. Alternative RNA splicing may also contribute to expansion of the immune repertoire.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christophides, George K -- Zdobnov, Evgeny -- Barillas-Mury, Carolina -- Birney, Ewan -- Blandin, Stephanie -- Blass, Claudia -- Brey, Paul T -- Collins, Frank H -- Danielli, Alberto -- Dimopoulos, George -- Hetru, Charles -- Hoa, Ngo T -- Hoffmann, Jules A -- Kanzok, Stefan M -- Letunic, Ivica -- Levashina, Elena A -- Loukeris, Thanasis G -- Lycett, Gareth -- Meister, Stephan -- Michel, Kristin -- Moita, Luis F -- Muller, Hans-Michael -- Osta, Mike A -- Paskewitz, Susan M -- Reichhart, Jean-Marc -- Rzhetsky, Andrey -- Troxler, Laurent -- Vernick, Kenneth D -- Vlachou, Dina -- Volz, Jennifer -- von Mering, Christian -- Xu, Jiannong -- Zheng, Liangbiao -- Bork, Peer -- Kafatos, Fotis C -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):159-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364793" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Animals ; Anopheles/*genetics/*immunology/metabolism/microbiology/parasitology ; Apoptosis ; Bacteria/immunology ; Catechol Oxidase/metabolism ; Computational Biology ; Drosophila Proteins/chemistry/genetics/metabolism ; Drosophila melanogaster/genetics/immunology/metabolism ; Enzyme Precursors/metabolism ; Gene Expression Regulation ; *Genes, Insect ; Genome ; Immunity, Innate ; Insect Proteins/chemistry/genetics/metabolism ; Multigene Family ; Peptides/metabolism ; Phylogeny ; Plasmodium/immunology/physiology ; Protein Structure, Tertiary ; Selection, Genetic ; Serine Endopeptidases/metabolism ; Serpins/metabolism ; Signal Transduction
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    Immunology. Catalytic antibody bridges innate and adaptive immunity (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nathan, Carl -- AI46382/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2143-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology and Graduate Programs in Immunology and Molecular Biology, Weill Medical College of Cornell University, New York, NY 10021, USA. cnathan@med.cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481124" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/immunology/*metabolism ; Antigen-Antibody Complex ; Arthritis, Rheumatoid/immunology/metabolism ; Autoimmunity ; Catalysis ; Crohn Disease/immunology/metabolism ; Humans ; Hydrogen Peroxide/*metabolism ; Hydroxyl Radical/metabolism ; Immune Complex Diseases/immunology/metabolism ; Immunity, Active ; *Immunity, Innate ; Immunoglobulin E/immunology/metabolism ; NADH, NADPH Oxidoreductases/metabolism ; Neutrophils/immunology/*metabolism ; Ozone/*metabolism ; Reactive Oxygen Species/metabolism ; Second Messenger Systems ; Signal Transduction ; Singlet Oxygen/*metabolism
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    Structural basis of gating by the outer membrane transporter FecA (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, Andrew D -- Chakraborty, Ranjan -- Smith, Barbara S -- Esser, Lothar -- van der Helm, Dick -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1715-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872840" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Bacterial Outer Membrane Proteins/chemistry/metabolism ; Bacterial Proteins/metabolism ; Binding Sites ; Biological Transport, Active ; Carrier Proteins/*chemistry/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli Proteins/chemistry/metabolism ; Ferric Compounds/*metabolism ; Hydrogen Bonding ; *Ion Channel Gating ; Ligands ; Membrane Proteins/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Receptors, Cell Surface ; Siderophores/*metabolism ; Static Electricity
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    Critical role for STAT4 activation by type 1 interferons in the interferon-gamma response to viral infection (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-09-21
    Description: Interferons (IFNs) are essential for host defense. Although the antiviral effects of the type 1 IFNs IFN-alpha and IFN-beta (IFN-alpha/beta) have been established, their immunoregulatory functions, especially their ability to regulate IFN-gamma production, are poorly understood. Here we show that IFN-alpha/beta activate STAT4 directly (STAT, signal transducers and activators of transcription) and that this is required for IFN-gamma production during viral infections of mice, in concert with T cell receptor-derived signals. In contrast, STAT1 appears to negatively regulate IFN-alpha/beta induction of IFN-gamma. Thus, type 1 IFNs, in addition to interleukin-12, provide pathways for innate regulation of adaptive immunity, and their immunoregulatory functions are controlled by modulating the activity of individual STATs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nguyen, Khuong B -- Watford, Wendy T -- Salomon, Rachelle -- Hofmann, Sigrun R -- Pien, Gary C -- Morinobu, Akio -- Gadina, Massimo -- O'Shea, John J -- Biron, Christine A -- F31-GM20760-02/GM/NIGMS NIH HHS/ -- R01-CA41268/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2063-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Immunology, Division of Biology and Medicine, Brown University, Providence, RI 02912, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242445" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arenaviridae Infections/*immunology ; CD8-Positive T-Lymphocytes/*immunology/metabolism ; Cells, Cultured ; DNA-Binding Proteins/*metabolism ; Female ; Gene Expression Regulation ; Interferon Type I/*immunology/pharmacology ; Interferon-gamma/*biosynthesis/genetics ; Interleukin-12/physiology ; *Lymphocytic choriomeningitis virus ; Male ; Mice ; Mice, Inbred C57BL ; Phosphorylation ; Promoter Regions, Genetic ; Receptors, Antigen, T-Cell/immunology/metabolism ; Recombinant Proteins ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; Signal Transduction ; Th1 Cells/immunology/metabolism ; Trans-Activators/*metabolism
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    New insights into neuron-glia communication (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-19
    Description: Two-way communication between neurons and nonneural cells called glia is essential for axonal conduction, synaptic transmission, and information processing and thus is required for normal functioning of the nervous system during development and throughout adult life. The signals between neurons and glia include ion fluxes, neurotransmitters, cell adhesion molecules, and specialized signaling molecules released from synaptic and nonsynaptic regions of the neuron. In contrast to the serial flow of information along chains of neurons, glia communicate with other glial cells through intracellular waves of calcium and via intercellular diffusion of chemical messengers. By releasing neurotransmitters and other extracellular signaling molecules, glia can affect neuronal excitability and synaptic transmission and perhaps coordinate activity across networks of neurons.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1226318/" 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/PMC1226318/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fields, R Douglas -- Stevens-Graham, Beth -- Z01 HD000713-11/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):556-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurocytology and Physiology Section, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA. fields@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386325" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/cytology/physiology ; Brain/cytology/physiology ; *Cell Communication ; Humans ; Microglia/cytology/physiology ; Myelin Sheath/physiology ; Nerve Regeneration ; Nervous System Diseases/pathology/physiopathology ; Neuroglia/*physiology ; Neurons/*physiology ; Neurotransmitter Agents/metabolism ; Oligodendroglia/cytology/physiology ; Schwann Cells/cytology/physiology ; Signal Transduction ; Stem Cells/cytology/physiology ; Synapses/physiology ; Synaptic Transmission
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 97
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    Cell biology. Slick recruitment to the Golgi (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bankaitis, Vytas A -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):290-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. vytas_bankaitis@med.unc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786634" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/metabolism ; Catalytic Domain ; Cell Membrane/*metabolism ; Ceramides/metabolism ; Diglycerides/*metabolism ; Golgi Apparatus/drug effects/enzymology/metabolism ; Humans ; *Membrane Proteins ; Phosphatidate Phosphatase/antagonists & inhibitors/metabolism ; Phosphatidic Acids/metabolism ; Phosphatidylcholines/metabolism ; Phospholipid Transfer Proteins ; Protein Kinase C/*metabolism ; Protein Structure, Tertiary ; *Protein Transport ; *Saccharomyces cerevisiae Proteins ; Secretory Vesicles/metabolism ; Signal Transduction ; Sphingomyelins/metabolism ; Transferases (Other Substituted Phosphate Groups)/metabolism ; Yeasts/metabolism ; trans-Golgi Network/drug effects/*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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  • 98
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    On the origin of interictal activity in human temporal lobe epilepsy in vitro (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: The origin and mechanisms of human interictal epileptic discharges remain unclear. Here, we describe a spontaneous, rhythmic activity initiated in the subiculum of slices from patients with temporal lobe epilepsy. Synchronous events were similar to interictal discharges of patient electroencephalograms. They were suppressed by antagonists of either glutamatergic or gamma-aminobutyric acid (GABA)-ergic signaling. The network of neurons discharging during population events comprises both subicular interneurons and a subgroup of pyramidal cells. In these pyramidal cells, GABAergic synaptic events reversed at depolarized potentials. Depolarizing GABAergic responses in neurons downstream to the sclerotic CA1 region contribute to human interictal activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Ivan -- Navarro, Vincent -- Clemenceau, Stephane -- Baulac, Michel -- Miles, Richard -- MH54671/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1418-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉EMI 0224, CHU Pitie-Salpetriere, Universite Paris VI, 75013 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434059" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Adult ; Electroencephalography ; Epilepsy, Temporal Lobe/*physiopathology ; Excitatory Amino Acid Antagonists/pharmacology ; Glutamic Acid/metabolism ; Hippocampus/*physiopathology ; Humans ; In Vitro Techniques ; Interneurons/*physiology ; Membrane Potentials ; Microelectrodes ; Middle Aged ; Nerve Fibers/physiology ; Neurons, Afferent/physiology ; Pyramidal Cells/*physiology ; Signal Transduction ; Synaptic Transmission ; Temporal Lobe/*physiopathology ; gamma-Aminobutyric Acid/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Controlled elimination of clathrin heavy-chain expression in DT40 lymphocytes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: We exploited the high rate of homologous recombination shown by the chicken B cell line DT40 to inactivate the endogenous alleles for clathrin heavy chain and replace them with human clathrin complementary DNA under the control of a tetracycline-regulatable promoter. Clathrin repression perturbed the activities of Akt-mediated and mitogen-activated protein kinase-mediated signaling pathways and induced apoptosis; this finding suggests that in DT40 cells clathrin helps to maintain the integrity of antiapoptotic survival pathways. We also describe a variant cell line in which these signaling pathways were unaffected by clathrin down-regulation. This variant cell line did not undergo apoptosis in the absence of clathrin and was used to examine the effects of clathrin depletion on membrane-trafficking pathways. Receptor-mediated and fluid-phase endocytosis were both substantially inhibited, and transferrin-receptor recycling was modestly inhibited. Surprisingly, clathrin removal did not affect the morphology or biochemical composition of lysosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wettey, Frank R -- Hawkins, Steve F C -- Stewart, Abigail -- Luzio, J Paul -- Howard, Jonathan C -- Jackson, Antony P -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1521-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, Building O, Downing Site, Tennis Court Road, Cambridge CB2 1QW, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202821" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; B-Lymphocytes/*metabolism/ultrastructure ; Cell Line ; Chickens ; Clathrin/biosynthesis/*genetics/physiology ; Clathrin Heavy Chains ; Down-Regulation ; Doxycycline/pharmacology ; Endocytosis/physiology ; *Gene Expression Regulation/drug effects ; Lysosomes/physiology ; Membrane Proteins/physiology ; Molecular Sequence Data ; Signal Transduction
    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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    Signal transduction. MAP kinase signaling specificity (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weston, Claire R -- Lambright, David G -- Davis, Roger J -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2345-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Program in Molecular Medicine, 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/12089430" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/*metabolism ; MAP Kinase Kinase 3 ; *MAP Kinase Signaling System ; MEF2 Transcription Factors ; Mitogen-Activated Protein Kinase Kinases/chemistry/*metabolism ; Mitogen-Activated Protein Kinases/*chemistry/*metabolism ; Models, Molecular ; Myogenic Regulatory Factors ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/chemistry/*metabolism ; Transcription Factors/chemistry/*metabolism ; p38 Mitogen-Activated Protein Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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