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  • Articles  (161)
  • Latest Papers from Table of Contents or Articles in Press  (161)
  • Protein Structure, Tertiary  (86)
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  • 2000-2004  (161)
  • 1995-1999
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  • 2002  (161)
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  • Articles  (161)
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  • Latest Papers from Table of Contents or Articles in Press  (161)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-23
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907122/" 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/PMC3907122/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falke, Joseph J -- R01 GM040731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1480-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biophysics Program and the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA. falke@colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859184" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry ; Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Nitrogen/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermodynamics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    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
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, Martin -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):92-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364779" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Genetically Modified ; *Anopheles/genetics/parasitology/physiology ; Behavior, Animal ; Biological Evolution ; *Culicidae/genetics/parasitology/physiology ; Ecology ; Genetics, Population ; Genome ; Humans ; *Insect Vectors/genetics/parasitology/physiology ; Malaria/prevention & control/transmission ; Molecular Biology ; Mosquito Control ; Plasmodium/physiology ; *Research ; Research Support as Topic ; Sequence Analysis, DNA ; Sexual Behavior, Animal
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  • 4
    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
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  • 5
    Publication Date: 2002-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1320-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434031" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; *Planets ; Research Personnel ; Research Support as Topic ; Solar System ; Space Flight/*economics/*organization & administration/trends ; Spacecraft ; United States ; United States National Aeronautics and Space ; Administration/*economics/*organization & administration/trends
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  • 6
    Publication Date: 2002-02-09
    Description: Double-stranded RNA-mediated gene interference (RNAi) in Caenorhabditis elegans systemically inhibits gene expression throughout the organism. To investigate how gene-specific silencing information is transmitted between cells, we constructed a strain that permits visualization of systemic RNAi. We used this strain to identify systemic RNA interference-deficient (sid) loci required to spread gene-silencing information between tissues but not to initiate or maintain an RNAi response. One of these loci, sid-1, encodes a conserved protein with predicted transmembrane domains. SID-1 is expressed in cells sensitive to RNAi, is localized to the cell periphery, and is required cell-autonomously for systemic RNAi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winston, William M -- Molodowitch, Christina -- Hunter, Craig P -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2456-9. Epub 2002 Feb 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834782" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/embryology/*genetics/metabolism ; Caenorhabditis elegans Proteins/chemistry/*genetics/*physiology ; Calmodulin-Binding Proteins/genetics ; Cytoplasm/metabolism ; Embryo, Nonmammalian/physiology ; *Gene Silencing ; Genes, Helminth ; Germ Cells/metabolism ; Green Fluorescent Proteins ; Intestines/metabolism ; Luminescent Proteins/genetics ; Membrane Proteins/chemistry/*genetics/*physiology ; Molecular Sequence Data ; Mosaicism ; Muscle Proteins/genetics ; Muscles/metabolism ; Mutation ; Protein Structure, Tertiary ; RNA, Double-Stranded/*genetics/metabolism ; RNA, Helminth/*genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Transgenes
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malakoff, David -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446877" target="_blank"〉PubMed〈/a〉
    Keywords: *Bioterrorism ; Financing, Government ; Government Agencies/economics/legislation & jurisprudence/*organization & ; administration ; National Institutes of Health (U.S.) ; Research/*organization & administration ; Research Support as Topic ; Security Measures/economics/legislation & jurisprudence/*organization & ; administration ; United States
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-04-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coombs, Rod -- Georghiou, Luke -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):471.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Manchester School of Management, University of Manchester Institute of Science and Technology (UMIST), and the Center for Research on Innovation and Competition, Manchester University and UMIST, Manchester M60 1QD, UK. rod.coombs@umist.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964461" target="_blank"〉PubMed〈/a〉
    Keywords: *Industry ; International Cooperation ; *Research ; Research Support as Topic ; *Technology ; Universities
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallo, Robert C -- Montagnier, Luc -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1730-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Virology and Department of Microbiology and Immunology, University of Maryland, Baltimore, MD 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459577" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/immunology/therapeutic use ; *Acquired Immunodeficiency Syndrome/drug therapy/prevention & ; control/transmission/virology ; Anti-HIV Agents/therapeutic use ; Biomedical Research ; Clinical Trials as Topic ; Developed Countries ; Developing Countries ; Drug Costs ; Female ; HIV/drug effects ; Health Services/economics ; Humans ; Infant, Newborn ; Infectious Disease Transmission, Vertical ; International Cooperation ; Pregnancy ; Pregnancy Complications, Infectious/drug therapy ; Research Support as Topic ; Technology Transfer ; United Nations
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  • 10
    Publication Date: 2002-02-02
    Description: In bacteria, promoter recognition depends on the RNA polymerase sigma subunit, which combines with the catalytically proficient RNA polymerase core to form the holoenzyme. The major class of bacterial promoters is defined by two conserved elements (the -10 and -35 elements, which are 10 and 35 nucleotides upstream of the initiation point, respectively) that are contacted by sigma in the holoenzyme. We show that recognition of promoters of this class depends on the "flexible flap" domain of the RNA polymerase beta subunit. The flap interacts with conserved region 4 of sigma and triggers a conformational change that moves region 4 into the correct position for interaction with the -35 element. Because the flexible flap is evolutionarily conserved, this domain may facilitate promoter recognition by specificity factors in eukaryotes as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuznedelov, Konstantin -- Minakhin, Leonid -- Niedziela-Majka, Anita -- Dove, Simon L -- Rogulja, Dragana -- Nickels, Bryce E -- Hochschild, Ann -- Heyduk, Tomasz -- Severinov, Konstantin -- GM44025/GM/NIGMS NIH HHS/ -- GM50514/GM/NIGMS NIH HHS/ -- R01 GM044025/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):855-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823642" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/*metabolism ; DNA, Bacterial/genetics/metabolism ; DNA-Directed RNA Polymerases/chemistry/genetics/*metabolism ; Energy Transfer ; Escherichia coli/*enzymology/genetics ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Sigma Factor/chemistry/genetics/*metabolism ; *Transcription, Genetic ; Two-Hybrid System Techniques
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huete-Perez, J A -- Orozco, D A -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2289-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11764811" target="_blank"〉PubMed〈/a〉
    Keywords: *Biotechnology/economics ; *Developing Countries ; Financing, Government ; Industry ; International Cooperation ; Research Support as Topic ; Technology Transfer ; Universities
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  • 12
    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
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  • 13
    Publication Date: 2002-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yimin, Ding -- Mervis, Jeffrey -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2317-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493892" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture ; Biotechnology ; China ; Commerce ; Crops, Agricultural/*genetics ; Financing, Government ; *Food, Genetically Modified ; International Cooperation ; Investments ; *Plants, Genetically Modified ; Research ; Research Support as Topic
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schnaitman, Carl A -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2329.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12498169" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/virology ; Bacteriophage P1/genetics/*physiology ; Bacteriophages/genetics/*physiology ; Biomedical Research ; Lipopolysaccharides/metabolism ; Receptors, Virus/genetics/physiology ; Research Support as Topic
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, Andrew -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1315-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434026" target="_blank"〉PubMed〈/a〉
    Keywords: Materials Testing ; Physical Phenomena ; *Physics ; Research Support as Topic ; Space Flight/*organization & administration ; *Spacecraft ; United States ; United States National Aeronautics and Space Administration/*organization & ; administration ; *Weightlessness
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  • 16
    Publication Date: 2002-10-05
    Description: Erythrocyte invasion by Plasmodium falciparum involves multiple ligand-receptor interactions and numerous apparent redundancies. The genome sequence of this parasite reveals new gene families encoding proteins that appear to mediate erythrocyte invasion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cowman, Alan F -- Crabb, Brendan S -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):126-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Walter and Eliza Hall Institute of Medical Research, PO Royal Melbourne Hospital, Melbourne, Victoria 3050, Australia. cowman@wehi.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364790" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Erythrocyte Membrane/parasitology/ultrastructure ; Erythrocytes/metabolism/*parasitology ; Evolution, Molecular ; Genes, Protozoan ; *Genome, Protozoan ; Humans ; Ligands ; Malaria Vaccines ; Merozoite Surface Protein 1/chemistry/metabolism ; Multigene Family ; Plasmodium/pathogenicity/physiology ; Plasmodium falciparum/*genetics/*pathogenicity/physiology/ultrastructure ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry/*metabolism ; Receptors, Cell Surface/*metabolism ; Tight Junctions/ultrastructure
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  • 17
    Publication Date: 2002-05-25
    Description: The sulfated peptide phytosulfokine (PSK) is an intercellular signal that plays a key role in cellular dedifferentiation and proliferation in plants. Using ligand-based affinity chromatography, we purified a 120-kilodalton membrane protein, specifically interacting with PSK, from carrot microsomal fractions. The corresponding complementary DNA encodes a 1021-amino acid receptor kinase that contains extracellular leucine-rich repeats, a single transmembrane domain, and a cytoplasmic kinase domain. Overexpression of this receptor kinase in carrot cells caused enhanced callus growth in response to PSK and a substantial increase in the number of tritium-labeled PSK binding sites, suggesting that PSK and this receptor kinase act as a ligand-receptor pair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsubayashi, Yoshikatsu -- Ogawa, Mari -- Morita, Akiko -- Sakagami, Youji -- New York, N.Y. -- Science. 2002 May 24;296(5572):1470-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Bio-Agricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan. matsu@agr.nagoya-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029134" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Cell Line ; Chromatography, Affinity ; DNA, Complementary ; Daucus carota/cytology/*enzymology/genetics/growth & development ; Genes, Plant ; Glycosylation ; Leucine ; Ligands ; Microsomes/enzymology ; Molecular Sequence Data ; Molecular Weight ; Peptide Hormones ; *Plant Growth Regulators ; Plant Proteins/*chemistry/genetics/isolation & purification/*metabolism ; Plants, Genetically Modified ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Receptors, Cell Surface/*chemistry/genetics/isolation & purification/*metabolism ; Repetitive Sequences, Amino Acid
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  • 18
    Publication Date: 2002-11-26
    Description: The reversible blockage of synthetic pores formed by rigid-rod beta barrels, either by substrates or products, was used to sense a variety of enzymatic reactions in high-throughput format with "naked-eye" fluorescent detection. Improvement of sensor sensitivity beyond three orders of magnitude by straightforward internal mutations underscores the functional plasticity of rigid-rod beta barrels. Such detectors of enzyme activity with the aforementioned characteristics are needed in areas as diverse as proteomics and environmentally benign organic synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Das, Gopal -- Talukdar, Pinaki -- Matile, Stefan -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1600-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organic Chemistry, University of Geneva, CH-1211 Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446904" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Alkaline Phosphatase/metabolism ; Apyrase/*metabolism ; Catalysis ; Enzymes/*metabolism ; *Fluorescent Dyes ; *Fluorometry ; Fructose-Bisphosphate Aldolase/metabolism ; Galactosyltransferases/metabolism ; Lipid Bilayers ; Peptides/chemistry ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Proteome ; Sensitivity and Specificity
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-05-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davidson, Amy L -- New York, N.Y. -- Science. 2002 May 10;296(5570):1038-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA. davidson@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004108" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Transport Systems, Basic/chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Carrier Proteins/chemistry/metabolism ; *DNA-Binding Proteins ; Dimerization ; Escherichia coli/*chemistry/metabolism ; Escherichia coli Proteins/*chemistry/metabolism ; Fungal Proteins/chemistry/metabolism ; Hydrolysis ; Models, Molecular ; *Periplasmic Binding Proteins ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; *Saccharomyces cerevisiae Proteins ; Vitamin B 12/metabolism
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  • 20
    Publication Date: 2002-03-09
    Description: Time courses of translocation of fluorescently conjugated proteins to the plasma membrane were simultaneously measured in thousands of individual rat basophilic leukemia cells. We found that the C2 domain---a calcium-sensing, lipid-binding protein module that is an essential regulator of protein kinase C and numerous other proteins---targeted proteins to the plasma membrane transiently if calcium was released from internal stores, and persistently in response to entry of extracellular calcium across the plasma membrane. The C2 domain translocation time courses of stimulated cells clustered into only two primary modes. Hence, the reversible recruitment of families of signaling proteins from one cellular compartment to another is a rapid bifurcation mechanism for inducing discrete states of cellular signaling networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teruel, Mary N -- Meyer, Tobias -- CA83229/CA/NCI NIH HHS/ -- GM062144/GM/NIGMS NIH HHS/ -- HG00057/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1910-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Stanford University Medical School, 269 Campus Drive, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884760" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Calcium/*metabolism ; *Calcium Signaling ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Fluorescence ; Fluorescent Dyes ; Isoenzymes/chemistry/*metabolism ; Kinetics ; Luminescent Proteins ; Platelet Activating Factor/pharmacology ; Protein Binding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Tertiary ; *Protein Transport ; Rats ; Receptors, Cell Surface/*metabolism ; Recombinant Fusion Proteins/metabolism ; Software ; Thapsigargin/pharmacology ; Transfection ; Tumor Cells, Cultured
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-06-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bostanci, Adam -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1778.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052923" target="_blank"〉PubMed〈/a〉
    Keywords: Disclosure ; *Ethics, Professional ; Germany ; Guidelines as Topic ; Research/*standards ; Research Support as Topic ; *Scientific Misconduct ; Universities/economics/*standards
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-06-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dayton, Leigh -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1779-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052925" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/economics ; Australia ; Bioethical Issues ; *Biotechnology/economics ; Cell Culture Techniques ; *Cell Line ; Embryo, Mammalian/*cytology ; Financing, Government ; Humans ; *Research/legislation & jurisprudence ; Research Support as Topic ; *Stem Cells ; Universities/economics
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-04-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dayton, Leigh -- New York, N.Y. -- Science. 2002 Apr 26;296(5568):641.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976422" target="_blank"〉PubMed〈/a〉
    Keywords: Authorship ; Humans ; Kidney Transplantation ; New South Wales ; Publishing/standards ; Research/*standards ; Research Support as Topic ; *Scientific Misconduct ; Universities
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  • 24
    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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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meisterernst, Michael -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):984-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Department, National Research Center for Environment and Health-GSF Institute of Molecular Immunology, Marchionini-Strasse 25, D-81377 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834806" target="_blank"〉PubMed〈/a〉
    Keywords: CCAAT-Enhancer-Binding Proteins/chemistry/metabolism ; Chromatin/metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Herpes Simplex Virus Protein Vmw65/chemistry/metabolism ; Macromolecular Substances ; Microscopy, Electron ; Molecular Weight ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits ; RNA Polymerase II/chemistry/metabolism ; Sterol Regulatory Element Binding Protein 1 ; Trans-Activators/*chemistry/isolation & purification/*metabolism ; *Transcription Factors ; *Transcription, Genetic
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  • 26
    Publication Date: 2002-09-28
    Description: Unc104/KIF1A belongs to a class of monomeric kinesin motors that have been thought to possess an unusual motility mechanism. Unlike the unidirectional motion driven by the coordinated actions of the two heads in conventional kinesins, single-headed KIF1A was reported to undergo biased diffusional motion along microtubules. Here, we show that Unc104/KIF1A can dimerize and move unidirectionally and processively with rapid velocities characteristic of transport in living cells. These results suggest that Unc104/KIF1A operates in vivo by a mechanism similar to conventional kinesin and that regulation of motor dimerization may be used to control transport by this class of kinesins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomishige, Michio -- Klopfenstein, Dieter R -- Vale, Ronald D -- AR42895/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2263-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Howard Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351789" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/chemistry/physiology ; Diffusion ; Dimerization ; Humans ; Kinesin/*chemistry/physiology ; Liposomes ; Microtubules/*physiology ; Molecular Motor Proteins/*chemistry/*physiology ; Molecular Sequence Data ; Movement ; Mutation ; Nerve Tissue Proteins/*chemistry/*physiology ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/chemistry
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):39.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364761" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cnidaria ; *Conservation of Natural Resources ; *Ecosystem ; Financing, Government ; *Marine Biology ; Research Support as Topic ; United States
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Chi -- Thompson, Craig B -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1346-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Abramson Family Cancer Research Institute, University of Pennsylvania, Philadelphia, PA 19104, USA. drt@mail.med.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434041" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/*pharmacology/therapeutic use ; *Apoptosis ; Asparagine/metabolism ; Aspartic Acid/metabolism ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins/metabolism ; *DNA Damage ; DNA, Neoplasm/drug effects ; Genes, Retinoblastoma ; Genes, p53 ; Humans ; Models, Biological ; Mutation ; Neoplasms/*drug therapy/metabolism/*pathology ; Protein Binding ; Protein Structure, Tertiary ; Proto-Oncogene Proteins c-bcl-2/*metabolism ; Retinoblastoma Protein/metabolism ; Tumor Suppressor Protein p53/metabolism ; bcl-X Protein
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):346-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12376680" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dinoflagellida/pathogenicity/physiology ; Fish Diseases/*parasitology ; Fishes/parasitology ; Humans ; Mid-Atlantic Region ; Nervous System Diseases/etiology ; Neurotoxicity Syndromes/etiology ; Pfiesteria piscicida/cytology/growth & development/*pathogenicity/physiology ; Protozoan Infections, Animal/*parasitology ; Research ; Research Support as Topic ; Southeastern United States ; *Toxins, Biological/isolation & purification/metabolism/toxicity ; Virulence ; Water/*parasitology
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  • 30
    Publication Date: 2002-08-17
    Description: The enediynes exemplify nature's ingenuity. We have cloned and characterized the biosynthetic locus coding for perhaps the most notorious member of the nonchromoprotein enediyne family, calicheamicin. This gene cluster contains an unusual polyketide synthase (PKS) that is demonstrated to be essential for enediyne biosynthesis. Comparison of the calicheamicin locus with the locus encoding the chromoprotein enediyne C-1027 reveals that the enediyne PKS is highly conserved among these distinct enediyne families. Contrary to previous hypotheses, this suggests that the chromoprotein and nonchromoprotein enediynes are generated by similar biosynthetic pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahlert, Joachim -- Shepard, Erica -- Lomovskaya, Natalia -- Zazopoulos, Emmanuel -- Staffa, Alfredo -- Bachmann, Brian O -- Huang, Kexue -- Fonstein, Leonid -- Czisny, Anne -- Whitwam, Ross E -- Farnet, Chris M -- Thorson, Jon S -- CA08748/CA/NCI NIH HHS/ -- CA84374/CA/NCI NIH HHS/ -- GM58196/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1173-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183629" target="_blank"〉PubMed〈/a〉
    Keywords: *Aminoglycosides ; Anti-Bacterial Agents/*biosynthesis ; Antibiotics, Antineoplastic/*biosynthesis ; Blotting, Southern ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; Conserved Sequence ; Enediynes ; *Genes, Bacterial ; Micromonospora/enzymology/*genetics/metabolism ; Multienzyme Complexes/*chemistry/*genetics/metabolism ; Multigene Family ; Mutation ; Open Reading Frames ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Sequence Analysis, DNA
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  • 31
    Publication Date: 2002-06-08
    Description: Nucleation of branched actin filaments by the Arp2/3 complex is a conserved process in eukaryotic cells, yet the source of unbranched actin filaments has remained obscure. In yeast, formins stimulate assembly of actin cables independently of Arp2/3. Here, the conserved core of formin homology domains 1 and 2 of Bni1p (Bni1pFH1FH2) was found to nucleate unbranched actin filaments in vitro. Bni1pFH2 provided the minimal region sufficient for nucleation. Unique among actin nucleators, Bni1pFH1FH2 remained associated with the growing barbed ends of filaments. This combination of properties suggests a direct role for formins in regulating nucleation and polarization of unbranched filamentous actin structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pruyne, David -- Evangelista, Marie -- Yang, Changsong -- Bi, Erfei -- Zigmond, Sally -- Bretscher, Anthony -- Boone, Charles -- AI19883/AI/NIAID NIH HHS/ -- GH39066/GH/CGH CDC HHS/ -- GM59216/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):612-5. Epub 2002 Jun 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052901" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actins/*metabolism ; Cytochalasin B/pharmacology ; Fungal Proteins/*chemistry/*metabolism ; *Microfilament Proteins ; Microscopy, Electron ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*metabolism/ultrastructure ; Saccharomyces cerevisiae Proteins/chemistry/metabolism
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  • 32
    Publication Date: 2002-10-12
    Description: Recent observations indicating that promoter identity influences alternative RNA-processing decisions have created interest in the regulatory interactions between RNA polymerase II transcription and precursor messenger RNA (pre-mRNA) processing. We examined the impact of steroid receptor-mediated transcription on RNA processing with reporter genes subject to alternative splicing driven by steroid-sensitive promoters. Steroid hormones affected the processing of pre-mRNA synthesized from steroid-sensitive promoters, but not from steroid-unresponsive promoters, in a steroid receptor-dependent and receptor-selective manner. Several nuclear receptor coregulators showed differential splicing effects, suggesting that steroid hormone receptors may simultaneously control gene transcription activity and exon content of the product mRNA by recruiting coregulators involved in both processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Auboeuf, Didier -- Honig, Arnd -- Berget, Susan M -- O'Malley, Bert W -- GM 38526/GM/NIGMS NIH HHS/ -- HD-08818/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):416-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12376702" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Animals ; Antigens, CD44/genetics ; COS Cells ; Calcitonin/genetics ; Calcitonin Gene-Related Peptide/genetics ; Carrier Proteins/*metabolism ; Dexamethasone/metabolism/pharmacology ; Estradiol/metabolism/pharmacology ; Estrogen Receptor alpha ; Estrogen Receptor beta ; Exons ; Genes, Reporter ; HeLa Cells ; Humans ; *Intracellular Signaling Peptides and Proteins ; Mutation ; Progesterone/metabolism/pharmacology ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; RNA Helicases/*metabolism ; RNA-Binding Protein FUS/*metabolism ; Receptors, Estrogen/genetics/metabolism ; Receptors, Glucocorticoid/metabolism ; Receptors, Progesterone/metabolism ; Response Elements ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-08-24
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2220017/" 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/PMC2220017/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henry, Michelle R -- Cho, Mildred K -- Weaver, Meredith A -- Merz, Jon F -- R01 HG002034/HG/NHGRI NIH HHS/ -- R01 HG002034-01A1/HG/NHGRI NIH HHS/ -- R01 HG002034-01A1S1/HG/NHGRI NIH HHS/ -- R01 HG002034-01A1S2/HG/NHGRI NIH HHS/ -- R01 HG002034-02/HG/NHGRI NIH HHS/ -- R01 HG002034-03/HG/NHGRI NIH HHS/ -- R01HG02034/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1279.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Bioethics, University of Pennsylvania, Philadelphia, PA, 19104-3308, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193770" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/legislation & jurisprudence ; Commerce/*legislation & jurisprudence ; *Dna ; Financing, Government ; *Genetics ; Interviews as Topic ; National Institutes of Health (U.S.) ; *Patents as Topic ; Research Support as Topic ; *Technology Transfer ; United States ; Universities/*legislation & jurisprudence
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  • 34
    Publication Date: 2002-08-17
    Description: C-1027 is a potent antitumor agent with a previously undescribed molecular architecture and mode of action. Cloning and characterization of the 85-kilobase C-1027 biosynthesis gene cluster from Streptomyces globisporus revealed (i) an iterative type I polyketide synthase that is distinct from any bacterial polyketide synthases known to date, (ii) a general polyketide pathway for the biosynthesis of both the 9- and 10-membered enediyne antibiotics, and (iii) a convergent biosynthetic strategy for the C-1027 chromophore from four building blocks. Manipulation of genes governing C-1027 biosynthesis allowed us to produce an enediyne compound in a predicted manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Wen -- Christenson, Steven D -- Standage, Scott -- Shen, Ben -- AI51689/AI/NIAID NIH HHS/ -- CA78747/CA/NCI NIH HHS/ -- T32 GM07377/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1170-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Pharmaceutical Sciences, University of Wisconsin, Madison, WI 53705, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183628" target="_blank"〉PubMed〈/a〉
    Keywords: *Aminoglycosides ; Anti-Bacterial Agents/*biosynthesis ; Antibiotics, Antineoplastic/*biosynthesis ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; Enediynes ; *Genes, Bacterial ; Multienzyme Complexes/chemistry/genetics/metabolism ; Multigene Family ; Mutation ; Open Reading Frames ; Protein Structure, Tertiary ; Streptomyces/enzymology/*genetics/*metabolism
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  • 35
    Publication Date: 2002-02-16
    Description: Animal SGT1 is a component of Skp1-Cullin-F-box protein (SCF) ubiquitin ligases that target regulatory proteins for degradation. Mutations in one (SGT1b) of two highly homologous Arabidopsis SGT1 genes disable early plant defenses conferred by multiple resistance (R) genes. Loss of SGT1b function in resistance is not compensated for by SGT1a. R genes differ in their requirements for SGT1b and a second resistance signaling gene, RAR1, that was previously implicated as an SGT1 interactor. Moreover, SGT1b and RAR1 contribute additively to RPP5-mediated pathogen recognition. These data imply both operationally distinct and cooperative functions of SGT1 and RAR1 in plant disease resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Austin, Mark J -- Muskett, Paul -- Kahn, Katherine -- Feys, Bart J -- Jones, Jonathan D G -- Parker, Jane E -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2077-80. Epub 2002 Feb 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/11847308" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/*genetics/metabolism/microbiology ; Arabidopsis Proteins/chemistry/*genetics/*metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Cycle Proteins/chemistry/*genetics/*metabolism ; Cell Death ; *Genes, Plant ; Immunity, Innate ; Molecular Sequence Data ; Mutation ; Oomycetes/pathogenicity/physiology ; *Plant Diseases ; Plant Leaves/microbiology ; Plant Proteins/*genetics/physiology ; Protein Structure, Tertiary ; Sequence Alignment ; Spores, Fungal/physiology
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  • 36
    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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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loomis, Dana -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1335-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12436979" target="_blank"〉PubMed〈/a〉
    Keywords: *Advisory Committees ; Federal Government ; Human Engineering ; *National Institute for Occupational Safety and Health (U.S.) ; Peer Review, Research ; *Politics ; Public Policy ; Research Support as Topic ; United States ; *United States Dept. of Health and Human Services
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  • 38
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    American Association for the Advancement of Science (AAAS)
    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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  • 39
    Publication Date: 2002-02-02
    Description: The hypoxia-inducible factors (HIFs) 1alpha and 2alpha are key mammalian transcription factors that exhibit dramatic increases in both protein stability and intrinsic transcriptional potency during low-oxygen stress. This increased stability is due to the absence of proline hydroxylation, which in normoxia promotes binding of HIF to the von Hippel-Lindau (VHL tumor suppressor) ubiquitin ligase. We now show that hypoxic induction of the COOH-terminal transactivation domain (CAD) of HIF occurs through abrogation of hydroxylation of a conserved asparagine in the CAD. Inhibitors of Fe(II)- and 2-oxoglutarate-dependent dioxygenases prevented hydroxylation of the Asn, thus allowing the CAD to interact with the p300 transcription coactivator. Replacement of the conserved Asn by Ala resulted in constitutive p300 interaction and strong transcriptional activity. Full induction of HIF-1alpha and -2alpha, therefore, relies on the abrogation of both Pro and Asn hydroxylation, which during normoxia occur at the degradation and COOH-terminal transactivation domains, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lando, David -- Peet, Daniel J -- Whelan, Dean A -- Gorman, Jeffrey J -- Whitelaw, Murray L -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):858-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biosciences (Biochemistry), Adelaide University, SA 5005, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823643" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Asparagine/*metabolism ; Basic Helix-Loop-Helix Transcription Factors ; Cell Hypoxia/*physiology ; Cell Line ; Humans ; Hydroxylation ; Hypoxia-Inducible Factor 1, alpha Subunit ; Mass Spectrometry ; Mice ; Mixed Function Oxygenases/metabolism ; Molecular Sequence Data ; Mutation ; Oxygen/*physiology ; Proline/metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcriptional Activation
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 May 24;296(5572):1391-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029111" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosome Mapping/economics ; Continental Population Groups/genetics ; Costs and Cost Analysis ; Databases, Nucleic Acid ; Financing, Government ; Genetic Predisposition to Disease ; *Genome, Human ; *Genomics ; Genotype ; *Haplotypes ; Humans ; Mutation ; National Institutes of Health (U.S.) ; Polymorphism, Single Nucleotide ; Research Support as Topic ; United States
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  • 41
    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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  • 42
    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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  • 43
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    American Association for the Advancement of Science (AAAS)
    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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  • 44
    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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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boehning, Darren -- Snyder, Solomon H -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2339-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493901" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Autonomic Nervous System/metabolism ; Basic Helix-Loop-Helix Transcription Factors ; Behavior, Animal ; Brain/metabolism ; CLOCK Proteins ; Carbon Monoxide/*metabolism/pharmacology ; *Circadian Rhythm/genetics ; DNA/metabolism ; Diffusion ; Dimerization ; Helix-Loop-Helix Motifs ; Heme/metabolism ; Heme Oxygenase (Decyclizing)/metabolism ; Mice ; Models, Genetic ; NAD/metabolism ; NADP/metabolism ; Nerve Tissue Proteins/*chemistry/*metabolism ; Neurons/*metabolism ; Neurotransmitter Agents/metabolism ; Oxidation-Reduction ; Protein Structure, Tertiary ; Synaptic Transmission ; Trans-Activators/metabolism ; Transcription Factors/*chemistry/*metabolism ; Transcription, Genetic
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  • 46
    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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  • 47
    Publication Date: 2002-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zerhouni, Elias -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2197-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351769" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Specimen Banks ; Bioterrorism ; Budgets ; Clinical Trials as Topic ; Financing, Government ; National Institutes of Health (U.S.)/economics/*organization & administration ; *Research ; Research Support as Topic ; Stem Cells ; United States
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-06-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2316.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089417" target="_blank"〉PubMed〈/a〉
    Keywords: Australia ; Financing, Government ; Foreign Professional Personnel/*legislation & jurisprudence ; *International Cooperation ; National Institutes of Health (U.S.)/*legislation & jurisprudence ; *Patents as Topic ; Public Policy ; Research Support as Topic ; United States
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, Andrew -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):435.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799222" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/economics/*organization & administration ; Aerospace Medicine/economics/*organization & administration ; *Astronauts ; Budgets ; History, 21st Century ; Humans ; Research ; Research Support as Topic ; *Space Flight ; United States ; United States National Aeronautics and Space Administration/economics
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-04-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):452-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964453" target="_blank"〉PubMed〈/a〉
    Keywords: Centers for Disease Control and Prevention (U.S.) ; Chronic Disease/*epidemiology ; Databases, Factual ; *Environmental Health ; Financing, Government ; Humans ; *Life Style ; *Population Surveillance ; *Registries ; Research Support as Topic ; United States/epidemiology
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  • 51
    Publication Date: 2002-03-30
    Description: The small guanosine triphosphatase Ran is loaded with guanosine triphosphate (GTP) by the chromatin-bound guanine nucleotide exchange factor RCC1 and releases import cargoes in the nucleus during interphase. In mitosis, Ran-GTP promotes spindle assembly around chromosomes by locally discharging cargoes that regulate microtubule dynamics and organization. We used fluorescence resonance energy transfer-based biosensors to visualize gradients of Ran-GTP and liberated cargoes around chromosomes in mitotic Xenopus egg extracts. Both gradients were required to assemble and maintain spindle structure. During interphase, Ran-GTP was highly enriched in the nucleoplasm, and a steep concentration difference between nuclear and cytoplasmic Ran-GTP was established, providing evidence for a Ran-GTP gradient surrounding chromosomes throughout the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalab, Petr -- Weis, Karsten -- Heald, Rebecca -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2452-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3200, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923538" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Bacterial Proteins/metabolism ; Biosensing Techniques ; Carrier Proteins/chemistry ; Cell Nucleus/*metabolism ; Chromosomes/metabolism ; Cytoplasm/*metabolism ; Energy Transfer ; Fluorescence ; Fluorescent Dyes ; Green Fluorescent Proteins ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/*metabolism ; *Interphase ; Luminescent Proteins/metabolism ; Male ; Microtubules/metabolism ; *Mitosis ; Ovum/metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Spectrometry, Fluorescence ; Spindle Apparatus/metabolism ; Xenopus ; alpha Karyopherins/chemistry/metabolism ; beta Karyopherins/chemistry/metabolism ; ran GTP-Binding Protein/*metabolism
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  • 52
    Publication Date: 2002-11-26
    Description: Neuronal PAS domain protein 2 (NPAS2) is a mammalian transcription factor that binds DNA as an obligate dimeric partner of BMAL1 and is implicated in the regulation of circadian rhythm. Here we show that both PAS domains of NPAS2 bind heme as a prosthetic group and that the heme status controls DNA binding in vitro. NPAS2-BMAL1 heterodimers, existing in either the apo (heme-free) or holo (heme-loaded) state, bound DNA avidly under favorably reducing ratios of the reduced and oxidized forms of nicotinamide adenine dinucleotide phosphate. Low micromolar concentrations of carbon monoxide inhibited the DNA binding activity of holo-NPAS2 but not that of apo-NPAS2. Upon exposure to carbon monoxide, inactive BMAL1 homodimers were formed at the expense of NPAS2-BMAL1 heterodimers. These results indicate that the heterodimerization of NPAS2, and presumably the expression of its target genes, are regulated by a gas through the heme-based sensor described here.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dioum, Elhadji M -- Rutter, Jared -- Tuckerman, Jason R -- Gonzalez, Gonzalo -- Gilles-Gonzalez, Marie-Alda -- McKnight, Steven L -- NIH5-T32-GM08-291-12/GM/NIGMS NIH HHS/ -- R01 HL640381/HL/NHLBI NIH HHS/ -- R01 MH5938805/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2385-7. Epub 2002 Nov 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Biochemistry and Plant Biology and Plant Biotechnology Center, The Ohio State University, 1060 Carmack Road, Columbus, OH 43210, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446832" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Carbon Monoxide/*metabolism/pharmacology ; Circadian Rhythm ; DNA/*metabolism ; Dimerization ; Helix-Loop-Helix Motifs ; Heme/chemistry/*metabolism ; Ligands ; Myoglobin/metabolism ; NADP/metabolism ; Nerve Tissue Proteins/*chemistry/*metabolism ; Oxidation-Reduction ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Spectrophotometry, Ultraviolet ; Transcription Factors/*chemistry/*metabolism
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perez-Iratxeta, Carolina -- Andrade, Miguel A -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):519.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12143877" target="_blank"〉PubMed〈/a〉
    Keywords: *Developed Countries ; *Developing Countries ; *Medline ; *Publishing/trends ; Research Support as Topic
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bruick, Richard K -- McKnight, Steven L -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):807-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard L3.124, Dallas, TX 75390-9152, USA. bruick@biochem.swmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823627" target="_blank"〉PubMed〈/a〉
    Keywords: Asparagine/*metabolism ; Cell Hypoxia/*physiology ; Cell Nucleus/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Humans ; Hydroxylation ; Hypoxia-Inducible Factor 1 ; Hypoxia-Inducible Factor 1, alpha Subunit ; Models, Biological ; Nuclear Proteins/chemistry/*metabolism ; Oxygen/*physiology ; Procollagen-Proline Dioxygenase/*metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein Subunits ; Response Elements ; Transcription Factors/chemistry/*metabolism ; *Transcriptional Activation
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-06-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):1957-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065816" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/economics/history/*organization & administration ; Biotechnology ; Budgets ; Computational Biology ; *Genomics/history ; History, 20th Century ; History, 21st Century ; Maryland ; Molecular Biology/history ; National Institutes of Health (U.S.) ; Research ; Research Personnel ; Research Support as Topic ; Sequence Analysis, DNA ; United States
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  • 56
    Publication Date: 2002-01-26
    Description: During development, neurons extend axons along defined routes to specific target cells. We show that additional mechanisms ensure that axons maintain their correct positioning in defined axonal tracts. After termination of axonal outgrowth and target recognition, axons in the ventral nerve cord (VNC) of Caenorhabditis elegans require the presence of a specific VNC neuron, PVT, to maintain their correct positioning in the left and right fascicles of the VNC. PVT may exert its stabilizing function by the temporally tightly controlled secretion of 2-immunoglobulin (Ig)-domain proteins encoded by the zig genes. Dedicated axon maintenance mechanisms may be widely used to ensure the preservation of functional neuronal circuitries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aurelio, Oscar -- Hall, David H -- Hobert, Oliver -- 5F32NS11107-02/NS/NINDS NIH HHS/ -- RR12596/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):686-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Center for Neurobiology and Behavior, 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/11809975" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Axons/*physiology ; *Body Patterning ; Caenorhabditis elegans/embryology/genetics/*growth & development/metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/*physiology ; Cues ; Genes, Helminth ; Genes, Reporter ; Immunoglobulins/chemistry ; Interneurons/metabolism/*physiology ; Larva/genetics/metabolism ; Movement ; Mutation ; Nervous System/cytology/growth & development ; Neural Pathways/growth & development ; Phenotype ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism
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  • 57
    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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  • 58
    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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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baird, Patricia -- Downie, Jocelyn -- Thompson, Jon -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2211.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics, University of British Columbia, Vancouver, BC, V6T 1Z3 Canada. pbaird@interchange.ubc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351773" target="_blank"〉PubMed〈/a〉
    Keywords: Canada ; Clinical Trials as Topic/legislation & jurisprudence/*standards ; *Confidentiality ; Conflict of Interest ; *Disclosure ; *Drug Industry/legislation & jurisprudence ; Ethics, Clinical ; Hospitals, Teaching ; Humans ; Multicenter Studies as Topic ; *Patient Rights ; Periodicals as Topic ; Publishing ; Research Support as Topic ; Risk ; United States ; Universities
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):941-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411675" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Asia ; *Chromosome Mapping ; Genetic Research ; *Genome, Human ; *Haplotypes ; Humans ; International Cooperation ; National Institutes of Health (U.S.) ; Research Support as Topic ; United States
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  • 61
    Publication Date: 2002-08-31
    Description: Synapses, the junctions between nerve cells through which they communicate, are formed by the coordinated assembly and tight attachment of pre- and postsynaptic specializations. We now show that SynCAM is a brain-specific, immunoglobulin domain-containing protein that binds to intracellular PDZ-domain proteins and functions as a homophilic cell adhesion molecule at the synapse. Expression of the isolated cytoplasmic tail of SynCAM in neurons inhibited synapse assembly. Conversely, expression of full-length SynCAM in nonneuronal cells induced synapse formation by cocultured hippocampal neurons with normal release properties. Glutamatergic synaptic transmission was reconstituted in these nonneuronal cells by coexpressing glutamate receptors with SynCAM, which suggests that a single type of adhesion molecule and glutamate receptor are sufficient for a functional postsynaptic response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biederer, Thomas -- Sara, Yildirim -- Mozhayeva, Marina -- Atasoy, Deniz -- Liu, Xinran -- Kavalali, Ege T -- Sudhof, Thomas C -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1525-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Basic Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Thomas.Biederer@UTSouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/cytology/*physiology ; Brain Chemistry ; Cell Adhesion Molecules/chemistry/isolation & purification/*physiology ; Cell Adhesion Molecules, Neuronal/chemistry/isolation & purification/*physiology ; Cell Line ; Coculture Techniques ; Exocytosis ; Humans ; Immunoglobulins ; Molecular Sequence Data ; Neurons/physiology ; Prosencephalon/chemistry/physiology ; Protein Structure, Tertiary ; Rats ; Receptors, AMPA/physiology ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid ; Synapses/chemistry/*physiology ; Synaptic Transmission/physiology ; Transfection ; Tumor Suppressor Proteins
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerstein, Mark -- Lan, Ning -- Jansen, Ronald -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):284-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. mark.gerstein@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786630" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; *Computational Biology ; Databases, Genetic ; Databases, Protein ; Gene Expression Profiling ; Genome ; Genome, Fungal ; *Genomics ; Humans ; Peptide Library ; Protein Structure, Tertiary ; Proteins/*chemistry/*metabolism ; *Proteome ; Saccharomyces cerevisiae/genetics/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; Two-Hybrid System Techniques
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-04-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mertl, Melissa -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):453.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964454" target="_blank"〉PubMed〈/a〉
    Keywords: Financing, Government ; Foundations/economics/history/*organization & administration ; Genomics ; Great Britain ; History, 21st Century ; Research ; Research Support as Topic
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  • 64
    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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  • 65
    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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  • 66
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hart, David M -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):439.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799997" target="_blank"〉PubMed〈/a〉
    Keywords: Intellectual Property ; *Private Sector ; Public Policy ; *Research ; Research Support as Topic ; Warfare
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  • 68
    Publication Date: 2002-08-17
    Description: In striated muscle, the plasma membrane forms tubular invaginations (transverse tubules or T-tubules) that function in depolarization-contraction coupling. Caveolin-3 and amphiphysin were implicated in their biogenesis. Amphiphysin isoforms have a putative role in membrane deformation at endocytic sites. An isoform of amphiphysin 2 concentrated at T-tubules induced tubular plasma membrane invaginations when expressed in nonmuscle cells. This property required exon 10, a phosphoinositide-binding module. In developing myotubes, amphiphysin 2 and caveolin-3 segregated in tubular and vesicular portions of the T-tubule system, respectively. These findings support a role of the bilayer-deforming properties of amphiphysin at T-tubules and, more generally, a physiological role of amphiphysin in membrane deformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Eunkyung -- Marcucci, Melissa -- Daniell, Laurie -- Pypaert, Marc -- Weisz, Ora A -- Ochoa, Gian-Carlo -- Farsad, Khashayar -- Wenk, Markus R -- De Camilli, Pietro -- CA46128/CA/NCI NIH HHS/ -- NS36251/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1193-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183633" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Caveolin 3 ; Caveolins/metabolism ; Cell Differentiation ; Cell Line ; Cell Membrane/metabolism ; Cell Membrane Structures/metabolism/*ultrastructure ; Cricetinae ; Dynamins ; Exons ; GTP Phosphohydrolases/metabolism ; Liposomes/metabolism ; Mice ; Microscopy, Electron ; Morphogenesis ; *Muscle Development ; Muscle, Skeletal/metabolism/*ultrastructure ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Protein Isoforms ; Protein Structure, Tertiary ; RNA, Small Interfering ; RNA, Untranslated/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vivier, Eric -- Biron, Christine A -- New York, N.Y. -- Science. 2002 May 17;296(5571):1248-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre d'Immunologie de Marseille-Luminy, INSERM-CNRS-Universite Mediterranee, Marseille, France. vivier@ciml.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016296" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Antigens, Ly/chemistry/genetics/*immunology/metabolism ; Evolution, Molecular ; Herpesviridae Infections/*immunology ; Humans ; Immunity, Innate ; Interferon-gamma/biosynthesis ; Killer Cells, Natural/*immunology ; Lectins, C-Type ; Ligands ; Lymphocyte Activation ; Membrane Glycoproteins/chemistry/genetics/*immunology/metabolism ; Mice ; Mice, Inbred Strains ; Muromegalovirus/*immunology ; Protein Structure, Tertiary ; Receptors, Immunologic/chemistry/genetics/*immunology/metabolism ; Receptors, NK Cell Lectin-Like ; Receptors, Natural Killer Cell ; Viral Proteins/*immunology/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alberts, Bruce -- May, Robert M -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1135.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424342" target="_blank"〉PubMed〈/a〉
    Keywords: Access to Information ; *Biological Science Disciplines ; Biological Warfare/*prevention & control ; Bioterrorism/*prevention & control ; International Cooperation ; Policy Making ; *Research ; Research Support as Topic ; Security Measures ; United States
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  • 71
    Publication Date: 2002-07-06
    Description: Drosophila host defense to fungal and Gram-positive bacterial infection is mediated by the Spaetzle/Toll/cactus gene cassette. It has been proposed that Toll does not function as a pattern recognition receptor per se but is activated through a cleaved form of the cytokine Spaetzle. The upstream events linking infection to the cleavage of Spaetzle have long remained elusive. Here we report the identification of a central component of the fungal activation of Toll. We show that ethylmethane sulfonate-induced mutations in the persephone gene, which encodes a previously unknown serine protease, block induction of the Toll pathway by fungi and resistance to this type of infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ligoxygakis, Petros -- Pelte, Nadege -- Hoffmann, Jules A -- Reichhart, Jean-Marc -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):114-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie Moleculaire et Cellulaire, UPR 9022 du CNRS, 15 rue R. Descartes, F67084 Strasbourg Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12098703" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Chromosome Mapping ; Drosophila/genetics/immunology/*metabolism/*microbiology ; Drosophila Proteins/*blood/chemistry/*genetics/*metabolism ; Escherichia coli/physiology ; Female ; Gene Expression Regulation ; Genes, Insect ; Gram-Positive Cocci/physiology ; Hemolymph/immunology/metabolism ; Hypocreales/*physiology ; Insect Proteins/genetics/metabolism ; Male ; Molecular Sequence Data ; Mutation ; Protein Sorting Signals ; Protein Structure, Tertiary ; Receptors, Cell Surface/genetics/*metabolism ; Serine Endopeptidases/*blood/chemistry/*genetics ; Toll-Like Receptors
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    American Association for the Advancement of Science (AAAS)
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-10-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):37-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364759" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Cloning, Organism/economics/legislation & jurisprudence ; Embryo, Mammalian/*cytology ; Ethics Committees, Research ; Great Britain ; History, 21st Century ; Humans ; Nuclear Transfer Techniques ; Patents as Topic ; Research ; Research Support as Topic ; *Stem Cells
    Print ISSN: 0036-8075
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-05
    Description: SpoIIIE mediates postseptational chromosome partitioning in Bacillus subtilis, but the mechanism controlling the direction of DNA transfer remains obscure. Here, we demonstrated that SpoIIIE acts as a DNA exporter: When SpoIIIE was synthesized in the larger of the two cells necessary for sporulation, the mother cell, DNA was translocated into the smaller forespore; however, when it was synthesized in the forespore, DNA was translocated into the mother cell. Furthermore, the DNA-tracking domain of SpoIIIE inhibited SpoIIIE complex assembly in the forespore. Thus, during sporulation, chromosome partitioning is controlled by the preferential assembly of SpoIIIE in one daughter cell.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885158/" 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/PMC2885158/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharp, Marc D -- Pogliano, Kit -- GM-57045/GM/NIGMS NIH HHS/ -- R01 GM057045/GM/NIGMS NIH HHS/ -- R01 GM057045-02/GM/NIGMS NIH HHS/ -- R01 GM057045-03/GM/NIGMS NIH HHS/ -- R01 GM057045-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):137-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, University of California, San Diego, La Jolla, CA 92093-0349, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778051" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/genetics/metabolism/*physiology ; Bacterial Proteins/chemistry/genetics/*metabolism ; Chromosomes, Bacterial/*metabolism ; DNA, Bacterial/*metabolism ; Green Fluorescent Proteins ; Luminescent Proteins ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; *Sigma Factor ; Spores, Bacterial/genetics/metabolism/*physiology ; *Transcription Factors
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1784.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228689" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Specimen Banks ; *Biomedical Research ; Budgets ; *Embryo, Mammalian/cytology ; *European Union ; Humans ; Research Support as Topic ; *Stem Cells
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, Joe -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):329-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Chemistry, Physical ; Collagen/chemistry ; Elasticity ; Elastin/chemistry ; *Fibroins ; Insect Proteins/chemistry ; Microfilament Proteins/chemistry ; Physicochemical Phenomena ; Polymers/*chemistry ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry ; Recombinant Proteins/chemistry ; Repetitive Sequences, Amino Acid ; Stress, Mechanical
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Fred -- Peter, Matthias -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):531-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA. fc99@columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142518" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actin-Related Protein 3 ; Actins/*metabolism ; Carrier Proteins/chemistry/*metabolism ; *Cytoskeletal Proteins ; Fungal Proteins/*chemistry/*metabolism ; *Heterotrimeric GTP-Binding Proteins ; *Microfilament Proteins ; Protein Binding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/*metabolism/ultrastructure ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; Schizosaccharomyces/metabolism ; *Vesicular Transport Proteins
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, Martin -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12098679" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Genetically Modified/parasitology/physiology ; Anopheles/*genetics/parasitology/physiology ; *Ecosystem ; Genes, Insect ; Genetics, Population ; Humans ; Insect Vectors/*genetics/parasitology/physiology ; Malaria, Falciparum/parasitology/transmission ; Pilot Projects ; Plasmodium falciparum/*physiology ; Research Support as Topic
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henry, Carol J -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481785" target="_blank"〉PubMed〈/a〉
    Keywords: *Chemical Industry ; *Environmental Health ; Humans ; *National Institutes of Health (U.S.) ; Peer Review, Research ; Private Sector ; Public Sector ; Research Support as Topic ; *Toxicology ; United States
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisner, Thomas -- Berenbaum, May -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):1973.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896239" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biochemical Phenomena ; *Biochemistry ; *Biological Factors/chemistry ; *Biology ; Chemical Phenomena ; Chemistry ; *Ecology ; Ecosystem ; *Molecular Biology ; Research Support as Topic ; United States
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  • 81
    Publication Date: 2002-07-06
    Description: Blue light regulates many physiological processes in fungi, but their photoreceptors are not known. In Neurospora crassa, all light responses depend on the Per-Arnt-Sim (PAS) domain-containing transcription factor white collar-1 (wc-1). By removing the WC-1 light, oxygen, or voltage domain, a specialized PAS domain that binds flavin mononucleotide in plant phototropins, we show that light responses are abolished, including light entrainment of the circadian clock. However, the WC-1-mediated dark activation of frq remains normal in this mutant, and the circadian clock can be entrained by temperature. Furthermore, we demonstrate that the purified Neurospora WC-1-WC-2 protein complex is associated with stoichiometric amounts of the chromophore flavin-adenine dinucleotide. Together, these observations suggest that WC-1 is the blue-light photoreceptor for the circadian clock and other light responses in Neurospora.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Qiyang -- Cheng, Ping -- Yang, Yuhong -- Wang, Lixing -- Gardner, Kevin H -- Liu, Yi -- New York, N.Y. -- Science. 2002 Aug 2;297(5582):840-3. Epub 2002 Jul 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, 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/12098705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Circadian Rhythm/radiation effects ; Color ; DNA, Fungal/genetics/metabolism ; DNA-Binding Proteins/chemistry/deficiency/genetics/*metabolism ; Darkness ; Dimerization ; Flavin Mononucleotide/metabolism ; Flavin-Adenine Dinucleotide/metabolism ; Fungal Proteins/chemistry/genetics/metabolism ; Gene Deletion ; Gene Expression Regulation, Fungal/radiation effects ; *Light ; Molecular Sequence Data ; Neurospora crassa/genetics/*metabolism/radiation effects ; Oxygen/metabolism ; Photoreceptors, Microbial/chemistry/genetics/*metabolism ; Promoter Regions, Genetic/genetics ; Protein Binding ; Protein Structure, Tertiary ; Response Elements/genetics ; Temperature ; Transcription Factors/chemistry/deficiency/genetics/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Radda, George -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):445-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council, London W1N 4AL, United Kingdom. george.radda.@headoffice.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799225" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; Europe ; *European Union ; *International Cooperation ; *Research ; Research Support as Topic
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  • 83
    Publication Date: 2002-12-14
    Description: Theory predicts the existence of barrierless protein folding. Without barriers, folding should be noncooperative and the degree of native structure should be coupled to overall protein stability. We investigated the thermal unfolding of the peripheral subunit binding domain from Escherichia coli's 2-oxoglutarate dehydrogenase multienzyme complex (termed BBL) with a combination of spectroscopic techniques and calorimetry. Each technique probed a different feature of protein structure. BBL has a defined three-dimensional structure at low temperatures. However, each technique showed a distinct unfolding transition. Global analysis with a statistical mechanical model identified BBL as a downhill-folding protein. Because of BBL's biological function, we propose that downhill folders may be molecular rheostats, in which effects could be modulated by altering the distribution of an ensemble of structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia-Mira, Maria M -- Sadqi, Mourad -- Fischer, Niels -- Sanchez-Ruiz, Jose M -- Munoz, Victor -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2191-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481137" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/*chemistry ; Calorimetry, Differential Scanning ; Circular Dichroism ; Escherichia coli/enzymology ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Hydrogen-Ion Concentration ; Ketoglutarate Dehydrogenase Complex/*chemistry ; Models, Chemical ; Models, Molecular ; Multienzyme Complexes/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Denaturation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Temperature ; Thermodynamics
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  • 84
    Publication Date: 2002-02-09
    Description: The human cofactor complexes ARC (activator-recruited cofactor) and CRSP (cofactor required for Sp1 activation) mediate activator-dependent transcription in vitro. Although these complexes share several common subunits, their structural and functional relationships remain unknown. Here, we report that affinity-purified ARC consists of two distinct multisubunit complexes: a larger complex, denoted ARC-L, and a smaller coactivator, CRSP. Reconstituted in vitro transcription with biochemically separated ARC-L and CRSP reveals differential cofactor functions. The ARC-L complex is transcriptionally inactive, whereas the CRSP complex is highly active. Structural determination by electron microscopy (EM) and three-dimensional reconstruction indicate substantial differences in size and shape between ARC-L and CRSP. Moreover, EM analysis of independently derived CRSP complexes reveals distinct conformations induced by different activators. These results suggest that CRSP may potentiate transcription via specific activator-induced conformational changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taatjes, Dylan J -- Naar, Anders M -- Andel, Frank 3rd -- Nogales, Eva -- Tjian, Robert -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1058-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and, Lawrence Berkeley National Laboratory, Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834832" target="_blank"〉PubMed〈/a〉
    Keywords: CCAAT-Enhancer-Binding Proteins/chemistry/metabolism ; Chromatin/metabolism ; DNA-Binding Proteins/chemistry/metabolism ; HeLa Cells ; Herpes Simplex Virus Protein Vmw65/metabolism ; Humans ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Macromolecular Substances ; Microscopy, Electron ; Models, Genetic ; Precipitin Tests ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits ; Recombinant Fusion Proteins/chemistry/metabolism ; Recombinant Proteins/metabolism ; Sterol Regulatory Element Binding Protein 1 ; Trans-Activators/*chemistry/isolation & purification/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic ; Transcriptional Activation
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-09-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, Andrew -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):1977-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242416" target="_blank"〉PubMed〈/a〉
    Keywords: International Cooperation ; *Research ; Research Support as Topic ; *Space Flight ; *Spacecraft ; United States ; *United States National Aeronautics and Space Administration
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  • 86
    Publication Date: 2002-10-05
    Description: Comparison of the genomes and proteomes of the two diptera Anopheles gambiae and Drosophila melanogaster, which diverged about 250 million years ago, reveals considerable similarities. However, numerous differences are also observed; some of these must reflect the selection and subsequent adaptation associated with different ecologies and life strategies. Almost half of the genes in both genomes are interpreted as orthologs and show an average sequence identity of about 56%, which is slightly lower than that observed between the orthologs of the pufferfish and human (diverged about 450 million years ago). This indicates that these two insects diverged considerably faster than vertebrates. Aligned sequences reveal that orthologous genes have retained only half of their intron/exon structure, indicating that intron gains or losses have occurred at a rate of about one per gene per 125 million years. Chromosomal arms exhibit significant remnants of homology between the two species, although only 34% of the genes colocalize in small "microsyntenic" clusters, and major interarm transfers as well as intra-arm shuffling of gene order are detected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zdobnov, Evgeny M -- von Mering, Christian -- Letunic, Ivica -- Torrents, David -- Suyama, Mikita -- Copley, Richard R -- Christophides, George K -- Thomasova, Dana -- Holt, Robert A -- Subramanian, G Mani -- Mueller, Hans-Michael -- Dimopoulos, George -- Law, John H -- Wells, Michael A -- Birney, Ewan -- Charlab, Rosane -- Halpern, Aaron L -- Kokoza, Elena -- Kraft, Cheryl L -- Lai, Zhongwu -- Lewis, Suzanna -- Louis, Christos -- Barillas-Mury, Carolina -- Nusskern, Deborah -- Rubin, Gerald M -- Salzberg, Steven L -- Sutton, Granger G -- Topalis, Pantelis -- Wides, Ron -- Wincker, Patrick -- Yandell, Mark -- Collins, Frank H -- Ribeiro, Jose -- Gelbart, William M -- Kafatos, Fotis C -- Bork, Peer -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):149-59.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364792" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles/chemistry/*genetics/physiology ; Biological Evolution ; Chromosome Inversion ; Chromosomes/genetics ; Cluster Analysis ; Dosage Compensation, Genetic ; Drosophila Proteins/chemistry/genetics/physiology ; Drosophila melanogaster/chemistry/*genetics/physiology ; Exons ; Gene Order ; Genes, Insect ; *Genome ; Insect Proteins/chemistry/genetics/physiology ; Introns ; Physical Chromosome Mapping ; Protein Structure, Tertiary ; *Proteome ; Pseudogenes ; Sequence Homology, Nucleic Acid ; Species Specificity ; Synteny
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  • 87
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, Gary -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2116-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481116" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Single-Stranded/genetics ; *Gene Conversion ; Gene Targeting/*methods ; Genetic Therapy/*methods ; Genetic Vectors ; Humans ; Oligonucleotides/*genetics ; Publishing ; RNA/genetics ; Recombination, Genetic ; Reproducibility of Results ; Research Support as Topic ; Transfection
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  • 88
    Publication Date: 2002-05-04
    Description: Extracts of the resin of the guggul tree (Commiphora mukul) lower LDL (low-density lipoprotein) cholesterol levels in humans. The plant sterol guggulsterone [4,17(20)-pregnadiene-3,16-dione] is the active agent in this extract. We show that guggulsterone is a highly efficacious antagonist of the farnesoid X receptor (FXR), a nuclear hormone receptor that is activated by bile acids. Guggulsterone treatment decreases hepatic cholesterol in wild-type mice fed a high-cholesterol diet but is not effective in FXR-null mice. Thus, we propose that inhibition of FXR activation is the basis for the cholesterol-lowering activity of guggulsterone. Other natural products with specific biologic effects may modulate the activity of FXR or other relatively promiscuous nuclear hormone receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Urizar, Nancy L -- Liverman, Amy B -- Dodds, D'Nette T -- Silva, Frank Valentin -- Ordentlich, Peter -- Yan, Yingzhuo -- Gonzalez, Frank J -- Heyman, Richard A -- Mangelsdorf, David J -- Moore, David D -- New York, N.Y. -- Science. 2002 May 31;296(5573):1703-6. Epub 2002 May 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Caco-2 Cells ; Carrier Proteins/genetics/metabolism ; Cells, Cultured ; Chenodeoxycholic Acid/pharmacology ; Cholesterol/*metabolism ; Cholesterol, Dietary/administration & dosage ; DNA/metabolism ; DNA-Binding Proteins/*antagonists & inhibitors/chemistry/genetics/*metabolism ; Hepatocytes/metabolism ; Histone Acetyltransferases ; Humans ; *Hydroxysteroid Dehydrogenases ; Hypolipidemic Agents/metabolism/*pharmacology ; Ligands ; Liver/metabolism ; *Membrane Glycoproteins ; Mice ; Nuclear Receptor Coactivator 1 ; Pregnenediones/metabolism/*pharmacology ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear/antagonists & inhibitors/genetics/metabolism ; Receptors, Steroid/antagonists & inhibitors/metabolism ; Transcription Factors/*antagonists & inhibitors/chemistry/genetics/*metabolism ; Transcriptional Activation/drug effects ; Transfection ; Tumor Cells, Cultured
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-05-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2002 May 3;296(5569):827.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988548" target="_blank"〉PubMed〈/a〉
    Keywords: Access to Information ; Databases, Protein ; Financing, Government ; International Cooperation ; National Institutes of Health (U.S.) ; *Organizations ; Private Sector ; Proteins/*chemistry/*physiology ; *Proteome ; Public Sector ; Research Support as Topic ; United States
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-04-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):24-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934992" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Biomedical Engineering ; Bioterrorism ; Budgets ; Diagnostic Imaging ; History, 20th Century ; History, 21st Century ; National Institutes of Health (U.S.)/economics/*organization & administration ; Neoplasms ; Research Support as Topic ; United States
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leshner, Alan I -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):929.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834784" target="_blank"〉PubMed〈/a〉
    Keywords: International Cooperation ; Research Support as Topic ; *Science/education ; *Societies, Scientific/organization & administration ; United States
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  • 92
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hampp, Norbert -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1561-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physical Chemistry, University of Marburg, 35032 Marburg, Germany. hampp@mailer.uni-marburg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446893" target="_blank"〉PubMed〈/a〉
    Keywords: Diffusion ; Enzymes/*metabolism ; *Fluorescent Dyes ; *Fluorometry ; Lipid Bilayers ; Peptides/chemistry ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Proteome
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  • 93
    Publication Date: 2002-06-29
    Description: Axonal regeneration in the adult central nervous system (CNS) is limited by two proteins in myelin, Nogo and myelin-associated glycoprotein (MAG). The receptor for Nogo (NgR) has been identified as an axonal glycosyl-phosphatidyl-inositol (GPI)-anchored protein, whereas the MAG receptor has remained elusive. Here, we show that MAG binds directly, with high affinity, to NgR. Cleavage of GPI-linked proteins from axons protects growth cones from MAG-induced collapse, and dominant-negative NgR eliminates MAG inhibition of neurite outgrowth. MAG-resistant embryonic neurons are rendered MAG-sensitive by expression of NgR. MAG and Nogo-66 activate NgR independently and serve as redundant NgR ligands that may limit axonal regeneration after CNS injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Betty P -- Fournier, Alyson -- GrandPre, Tadzia -- Strittmatter, Stephen M -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1190-3. Epub 2002 Jun 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Section of Neurobiology, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089450" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Binding Sites ; COS Cells ; Chick Embryo ; Cloning, Molecular ; GPI-Linked Proteins ; Ganglia, Spinal/cytology/embryology/metabolism ; Gene Library ; Ligands ; Mice ; Myelin Proteins/chemistry/metabolism/pharmacology ; Myelin-Associated Glycoprotein/chemistry/genetics/*metabolism ; Nerve Regeneration ; Neurites/*physiology ; Neurons/metabolism ; Peptide Fragments/metabolism/pharmacology ; Phosphatidylinositol Diacylglycerol-Lyase ; Protein Structure, Tertiary ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Sialic Acids/metabolism ; Transfection ; Type C Phospholipases/metabolism
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  • 94
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1616-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872804" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/*immunology ; Acquired Immunodeficiency Syndrome/immunology/prevention & control ; *Clinical Trials as Topic ; Cytotoxicity, Immunologic ; Financing, Government ; HIV/*immunology ; HIV Antibodies/biosynthesis ; Humans ; Killer Cells, Natural/immunology ; National Institutes of Health (U.S.) ; Research Support as Topic ; United States ; Vaccines, DNA/immunology ; Vaccines, Synthetic/immunology
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-26
    Description: A survey of China's plant biotechnologists shows that China is developing the largest plant biotechnology capacity outside of North America. The list of genetically modified plant technologies in trials, including rice, wheat, potatoes, and peanuts, is impressive and differs from those being worked on in other countries. Poor farmers in China are cultivating more area of genetically modified plants than are small farmers in any other developing country. A survey of agricultural producers in China demonstrates that Bacillus thuringiensis cotton adoption increases production efficiency and improves farmer health.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Jikun -- Rozelle, Scott -- Pray, Carl -- Wang, Qinfang -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):674-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Chinese Agricultural Policy, Institute of Geographical Sciences and Natural Resource Research, Chinese Academy of Sciences (CAS), Building 917, Datun Road, Beijing 100101, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809972" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; *Agriculture/economics ; *Biotechnology/economics/manpower ; China ; Costs and Cost Analysis ; *Crops, Agricultural ; Developing Countries ; Financing, Government ; Genetic Engineering ; Gossypium/genetics ; Pesticides/economics ; *Plants ; *Plants, Genetically Modified ; Public Policy ; Research ; Research Support as Topic
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  • 96
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-10-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Batt, Carl A -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2208-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12353522" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes ; Biotechnology/education ; Financing, Government ; *Government Agencies ; Research Support as Topic ; Science/*education ; United States
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  • 97
    Publication Date: 2002-04-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):36-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11935002" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes/economics/organization & administration ; Animals ; China ; *Computational Biology ; Computers ; Genome, Plant ; *Genomics ; Human Genome Project ; Oryza/*genetics ; Research Support as Topic ; *Sequence Analysis, DNA ; Software ; Swine/genetics
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  • 98
    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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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fava, G A -- Breno, E -- Guardabasso, V -- Stefanelli, M -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1715-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12462236" target="_blank"〉PubMed〈/a〉
    Keywords: Databases, Factual ; Europe ; Publishing/*standards ; Research Personnel/*standards ; Research Support as Topic ; Universities/*standards
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  • 100
    Publication Date: 2002-01-26
    Description: The intracellular pathogen Legionella pneumophila subverts vesicle traffic in eukaryotic host cells to create a vacuole that supports replication. The dot/icm genes encode a protein secretion apparatus that L. pneumophila require for biogenesis of this vacuole. Here we show that L. pneumophila produce a protein called RalF that functions as an exchange factor for the ADP ribosylation factor (ARF) family of guanosine triphosphatases (GTPases). The RalF protein is required for the localization of ARF on phagosomes containing L. pneumophila. Translocation of RalF protein through the phagosomal membrane is a dot/icm-dependent process. Thus, RalF is a substrate of the Dot/Icm secretion apparatus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nagai, Hiroki -- Kagan, Jonathan C -- Zhu, Xinjun -- Kahn, Richard A -- Roy, Craig R -- R01 AI44371/AI/NIAID NIH HHS/ -- R29 AI41699/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):679-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809974" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1/genetics/*metabolism ; ADP-Ribosylation Factors/metabolism ; Acanthamoeba/microbiology ; Amino Acid Sequence ; Animals ; Bacterial Proteins/genetics/metabolism ; Carrier Proteins/genetics/metabolism ; Cell Line ; Genes, Bacterial ; Guanine Nucleotide Exchange Factors/chemistry/genetics/*metabolism ; Humans ; Legionella/genetics ; Legionella pneumophila/genetics/growth & development/*metabolism ; Macrophages/microbiology ; Mice ; Mice, Inbred A ; Molecular Sequence Data ; Phagosomes/*metabolism/*microbiology ; Protein Structure, Tertiary ; Protein Transport ; RNA, Bacterial/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid
    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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