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  • Articles  (131)
  • Latest Papers from Table of Contents or Articles in Press  (131)
  • Molecular Sequence Data  (93)
  • Protein Conformation
  • 2000-2004  (131)
  • 1980-1984
  • 1935-1939
  • 2002  (131)
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  • Articles  (131)
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  • Latest Papers from Table of Contents or Articles in Press  (131)
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  • 2000-2004  (131)
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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
    Publication Date: 2002-10-05
    Description: The detection of single-nucleotide polymorphisms in pathogenic microorganisms has normally been carried out by trial and error. Here we show that DNA hybridization with high-density oligonucleotide arrays provides rapid and convenient detection of single-nucleotide polymorphisms in Plasmodium falciparum, despite its exceptionally high adenine-thymine (AT) content (82%). A disproportionate number of polymorphisms are found in genes encoding proteins associated with the cell membrane. These genes are targets for only 22% of the oligonucleotide probes but account for 69% of the polymorphisms. Genetic variation is also enriched in subtelomeric regions, which account for 22% of the chromosome but 76% of the polymorphisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkman, Sarah K -- Hartl, Daniel L -- Wirth, Dyann F -- Nielsen, Kaare M -- Choi, Mehee -- Batalov, Serge -- Zhou, Yingyao -- Plouffe, David -- Le Roch, Karine G -- Abagyan, Ruben -- Winzeler, Elizabeth A -- GM61351/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):216-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364807" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosomes/genetics ; DNA, Protozoan/genetics ; *Genes, Protozoan ; Genetic Variation ; Genome, Protozoan ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Plasmodium falciparum/*genetics ; *Polymorphism, Single Nucleotide ; Protozoan Proteins/*genetics ; Sequence Analysis, DNA
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  • 3
    Publication Date: 2002-04-06
    Description: Higher order chromatin structure presents a barrier to the recognition and repair of DNA damage. Double-strand breaks (DSBs) induce histone H2AX phosphorylation, which is associated with the recruitment of repair factors to damaged DNA. To help clarify the physiological role of H2AX, we targeted H2AX in mice. Although H2AX is not essential for irradiation-induced cell-cycle checkpoints, H2AX-/- mice were radiation sensitive, growth retarded, and immune deficient, and mutant males were infertile. These pleiotropic phenotypes were associated with chromosomal instability, repair defects, and impaired recruitment of Nbs1, 53bp1, and Brca1, but not Rad51, to irradiation-induced foci. Thus, H2AX is critical for facilitating the assembly of specific DNA-repair complexes on damaged DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721576/" 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/PMC4721576/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celeste, Arkady -- Petersen, Simone -- Romanienko, Peter J -- Fernandez-Capetillo, Oscar -- Chen, Hua Tang -- Sedelnikova, Olga A -- Reina-San-Martin, Bernardo -- Coppola, Vincenzo -- Meffre, Eric -- Difilippantonio, Michael J -- Redon, Christophe -- Pilch, Duane R -- Olaru, Alexandru -- Eckhaus, Michael -- Camerini-Otero, R Daniel -- Tessarollo, Lino -- Livak, Ferenc -- Manova, Katia -- Bonner, William M -- Nussenzweig, Michel C -- Nussenzweig, Andre -- Z99 CA999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):922-7. Epub 2002 Apr 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, NIH, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934988" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology/physiology ; Base Sequence ; Cell Aging ; Cell Cycle ; Cells, Cultured ; *Chromosome Aberrations ; DNA Damage ; *DNA Repair ; Female ; Gene Targeting ; Histones/chemistry/*genetics/*physiology ; Immunoglobulin Class Switching ; Infertility, Male/genetics/physiopathology ; Lymphocyte Count ; Male ; Meiosis ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; Phosphorylation ; *Recombination, Genetic ; Spermatocytes/physiology ; T-Lymphocytes/immunology/physiology
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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: 2002-12-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Funes, Soledad -- Davidson, Edgar -- Reyes-Prieto, Adrian -- Magallon, Susana -- Herion, Pascal -- King, Michael P -- Gonzalez-Halphen, Diego -- HL59646/HL/NHLBI NIH HHS/ -- TW01176/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2155.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto de Fisiologia Celular, Universidad Nacional Autonoma de Mexico (UNAM), 04510 D.F., Mexico.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apicomplexa/enzymology/*genetics/ultrastructure ; *Biological Evolution ; Cell Nucleus/genetics ; Chlamydomonas reinhardtii/enzymology/genetics ; Chlorophyta/enzymology/*genetics ; Cloning, Molecular ; DNA, Mitochondrial/genetics ; Electron Transport Complex IV/chemistry/*genetics ; *Gene Transfer, Horizontal ; Genes ; Genes, Protozoan ; Molecular Sequence Data ; Phylogeny ; Plastids/*genetics ; Symbiosis ; Toxoplasma/enzymology/genetics
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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
    Publication Date: 2002-04-27
    Description: Little is known of how plant disease resistance (R) proteins recognize pathogens and activate plant defenses. Rcr3 is specifically required for the function of Cf-2, a Lycopersicon pimpinellifolium gene bred into cultivated tomato (Lycopersicon esculentum) for resistance to Cladosporium fulvum. Rcr3 encodes a secreted papain-like cysteine endoprotease. Genetic analysis shows Rcr3 is allelic to the L. pimpinellifolium Ne gene, which suppresses the Cf-2-dependent autonecrosis conditioned by its L. esculentum allele, ne (necrosis). Rcr3 alleles from these two species encode proteins that differ by only seven amino acids. Possible roles of Rcr3 in Cf-2-dependent defense and autonecrosis are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kruger, Julia -- Thomas, Colwyn M -- Golstein, Catherine -- Dixon, Mark S -- Smoker, Matthew -- Tang, Saijun -- Mulder, Lonneke -- Jones, Jonathan D G -- New York, N.Y. -- Science. 2002 Apr 26;296(5568):744-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976458" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Cladosporium/*physiology ; Cloning, Molecular ; Cysteine Endopeptidases/chemistry/*genetics/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Gene Expression Regulation, Plant ; *Genes, Plant ; Immunity, Innate ; Leucine/analogs & derivatives/pharmacology ; Lycopersicon esculentum/*enzymology/genetics/*microbiology/physiology ; Molecular Sequence Data ; Mutation ; Phenotype ; *Plant Diseases ; Plant Leaves/enzymology ; Plant Proteins/*metabolism ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/chemistry/metabolism ; Tobacco/genetics ; Transgenes
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  • 8
    Publication Date: 2002-04-06
    Description: The conserved Sir2 family of proteins has protein deacetylase activity that is dependent on NAD (the oxidized form of nicotinamide adenine dinucleotide). Although histones are one likely target for the enzymatic activity of eukaryotic Sir2 proteins, little is known about the substrates and roles of prokaryotic Sir2 homologs. We reveal that an archaeal Sir2 homolog interacts specifically with the major archaeal chromatin protein, Alba, and that Alba exists in acetylated and nonacetylated forms. Furthermore, we show that Sir2 can deacetylate Alba and mediate transcriptional repression in a reconstituted in vitro transcription system. These data provide a paradigm for how Sir2 family proteins influence transcription and suggest that modulation of chromatin structure by acetylation arose before the divergence of the archaeal and eukaryotic lineages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bell, Stephen D -- Botting, Catherine H -- Wardleworth, Benjamin N -- Jackson, Stephen P -- White, Malcolm F -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):148-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) Cancer Cell Unit, The Hutchison/MRC Research Centre, Hills Road, Cambridge, CB2 2QH, UK. sdb@mole.bio.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11935028" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Archaeal Proteins/*chemistry/*metabolism ; Chromatin/*metabolism ; DNA/metabolism ; Gene Expression Regulation, Archaeal ; Histone Deacetylases/chemistry/*metabolism ; Molecular Sequence Data ; Molecular Weight ; Protein Binding ; Recombinant Fusion Proteins/chemistry/metabolism ; *Silent Information Regulator Proteins, Saccharomyces cerevisiae ; Sirtuin 2 ; Sirtuins ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Sulfolobus/*chemistry/genetics/metabolism ; Templates, Genetic ; Trans-Activators/chemistry/*metabolism ; Transcription, Genetic
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  • 9
    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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  • 10
    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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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gewolb, Josh -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2205-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910091" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/genetics/metabolism ; Bacteria/enzymology/genetics ; Bacterial Proteins/biosynthesis ; Cyclosporine/metabolism ; Drug Design ; Fungi/enzymology/genetics ; Genetic Engineering ; Models, Molecular ; Penicillins/biosynthesis ; Peptide Synthases/chemistry/genetics/*metabolism ; *Protein Biosynthesis ; Protein Conformation ; Protein Engineering/*methods ; Protein Subunits ; Proteins/*chemistry ; Stereoisomerism ; Substrate Specificity
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  • 12
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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〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):28-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934996" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid beta-Peptides/chemistry ; Animals ; Humans ; Mice ; Protein Conformation ; *Protein Folding ; *Protein Structure, Quaternary ; Proteins/*chemistry ; Rats
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  • 13
    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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  • 14
    Publication Date: 2002-09-28
    Description: It has been known since 1986 that CD8 T lymphocytes from certain HIV-1-infected individuals who are immunologically stable secrete a soluble factor, termed CAF, that suppresses HIV-1 replication. However, the identity of CAF remained elusive despite an extensive search. By means of a protein-chip technology, we identified a cluster of proteins that were secreted when CD8 T cells from long-term nonprogressors with HIV-1 infection were stimulated. These proteins were identified as alpha-defensin 1, 2, and 3 on the basis of specific antibody recognition and amino acid sequencing. CAF activity was eliminated or neutralized by an antibody specific for human alpha-defensins. Synthetic and purified preparations of alpha-defensins also inhibited the replication of HIV-1 isolates in vitro. Taken together, our results indicate that alpha-defensin 1, 2, and 3 collectively account for much of the anti-HIV-1 activity of CAF that is not attributable to beta-chemokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Linqi -- Yu, Wenjie -- He, Tian -- Yu, Jian -- Caffrey, Rebecca E -- Dalmasso, Enrique A -- Fu, Siyu -- Pham, Thang -- Mei, Jianfeng -- Ho, Jaclyn J -- Zhang, Wenyong -- Lopez, Peter -- Ho, David D -- AI-42848/AI/NIAID NIH HHS/ -- M01-RR00102/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):995-1000. Epub 2002 Sep 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aaron Diamond AIDS Research Center, The Rockefeller University, 455 First Avenue, New York, NY 10016, USA. lzhang@adarc.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351674" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Antiviral Agents/chemistry/isolation & purification/*pharmacology ; CD8-Positive T-Lymphocytes/chemistry/*immunology ; Cells, Cultured ; Chemokines, CC/immunology/physiology ; HIV Infections/*immunology/virology ; HIV Long-Term Survivors ; HIV-1/drug effects/*physiology ; Humans ; Mass Spectrometry ; Molecular Sequence Data ; Neutrophils/chemistry/immunology ; Protein Array Analysis ; Virus Replication ; alpha-Defensins/chemistry/isolation & purification/pharmacology/*physiology
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-16
    Description: The corepressor CtBP (carboxyl-terminal binding protein) is involved in transcriptional pathways important for development, cell cycle regulation, and transformation. We demonstrate that CtBP binding to cellular and viral transcriptional repressors is regulated by the nicotinamide adenine dinucleotides NAD+ and NADH, with NADH being two to three orders of magnitude more effective. Levels of free nuclear nicotinamide adenine dinucleotides, determined using two-photon microscopy, correspond to the levels required for half-maximal CtBP binding and are considerably lower than those previously reported. Agents capable of increasing NADH levels stimulate CtBP binding to its partners in vivo and potentiate CtBP-mediated repression. We propose that this ability to detect changes in nuclear NAD+/NADH ratio allows CtBP to serve as a redox sensor for transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Qinghong -- Piston, David W -- Goodman, Richard H -- K01 CA096561/CA/NCI NIH HHS/ -- R01 CA115468/CA/NCI NIH HHS/ -- R01 CA115468-05/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1895-7. Epub 2002 Feb 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847309" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Alcohol Oxidoreductases ; Amino Acid Sequence ; Animals ; Binding Sites ; Cadherins/genetics ; Cell Nucleus/*metabolism ; Cytoplasm/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; *Gene Expression Regulation ; HeLa Cells ; Homeodomain Proteins/metabolism ; Humans ; Microscopy, Fluorescence ; Molecular Sequence Data ; Mutation ; NAD/*metabolism ; Oxidation-Reduction ; Phosphoproteins/chemistry/genetics/*metabolism ; Promoter Regions, Genetic ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/*metabolism ; *Transcription Factors ; Transcription, Genetic ; Transfection
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  • 16
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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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  • 17
    Publication Date: 2002-05-23
    Description: Mechanical and thermal cues stimulate a specialized group of sensory neurons that terminate in the skin. Three members of the transient receptor potential (TRP) family of channels are expressed in subsets of these neurons and are activated at distinct physiological temperatures. Here, we describe the cloning and characterization of a novel thermosensitive TRP channel. TRPV3 has a unique threshold: It is activated at innocuous (warm) temperatures and shows an increased response at noxious temperatures. TRPV3 is specifically expressed in keratinocytes; hence, skin cells are capable of detecting heat via molecules similar to those in heat-sensing neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peier, Andrea M -- Reeve, Alison J -- Andersson, David A -- Moqrich, Aziz -- Earley, Taryn J -- Hergarden, Anne C -- Story, Gina M -- Colley, Sian -- Hogenesch, John B -- McIntyre, Peter -- Bevan, Stuart -- Patapoutian, Ardem -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2046-9. Epub 2002 May 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016205" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Newborn ; Blotting, Northern ; CHO Cells ; Capsaicin/*analogs & derivatives/pharmacology ; *Cation Transport Proteins ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Cricetinae ; Epidermis/cytology/innervation/metabolism ; Ganglia, Spinal/metabolism ; *Hot Temperature ; Humans ; In Situ Hybridization ; Ion Channels/chemistry/genetics/*metabolism ; Keratinocytes/*metabolism ; Membrane Potentials ; Mice ; Molecular Sequence Data ; Nerve Endings/physiology ; Neurons/physiology ; Patch-Clamp Techniques ; RNA, Messenger/genetics/metabolism ; Ruthenium Red/pharmacology ; Signal Transduction ; Spinal Cord/metabolism ; TRPV Cation Channels ; Temperature
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  • 18
    Publication Date: 2002-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meegaskumbura, M -- Bossuyt, F -- Pethiyagoda, R -- Manamendra-Arachchi, K -- Bahir, M -- Milinkovitch, M C -- Schneider, C J -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):379.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Boston University, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12376694" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anura/anatomy & histology/*classification/genetics/physiology ; Base Sequence ; Biological Evolution ; DNA, Mitochondrial/genetics ; *Ecosystem ; Embryonic Development ; Female ; Male ; Molecular Sequence Data ; Oviposition ; Ovum/physiology ; *Phylogeny ; Sri Lanka ; Trees
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  • 19
    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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  • 20
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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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  • 21
    Publication Date: 2002-03-02
    Description: Type III secreted "effector" proteins of bacterial pathogens play central roles in virulence, yet are notoriously difficult to identify. We used an in vivo genetic screen to identify 13 effectors secreted by the type III apparatus (called Hrp, for "hypersensitive response and pathogenicity") of the plant pathogen Pseudomonas syringae. Although sharing little overall homology, the amino-terminal regions of these effectors had strikingly similar amino acid compositions. This feature facilitated the bioinformatic prediction of 38 P. syringae effectors, including 15 previously unknown proteins. The secretion of two of these putative effectors was shown to be type III--dependent. Effectors showed high interstrain variation, supporting a role for some effectors in adaptation to different hosts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guttman, David S -- Vinatzer, Boris A -- Sarkar, Sara F -- Ranall, Max V -- Kettler, Gregory -- Greenberg, Jean T -- GM020024/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1722-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, University of Toronto, 25 Willcocks Street, Toronto, ON M5S 3B2, Canada. guttman@botany.utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872842" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Arabidopsis/genetics/metabolism/*microbiology ; *Arabidopsis Proteins ; Bacterial Proteins/chemistry/*genetics/*metabolism ; Computational Biology ; DNA Transposable Elements ; *Genes, Bacterial ; Genomics ; Molecular Sequence Data ; Plant Proteins/metabolism ; Promoter Regions, Genetic ; Proteome ; Pseudomonas/*genetics/*metabolism/pathogenicity ; Recombinant Fusion Proteins/metabolism ; Virulence
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  • 22
    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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  • 23
    Publication Date: 2002-12-14
    Description: The first chordates appear in the fossil record at the time of the Cambrian explosion, nearly 550 million years ago. The modern ascidian tadpole represents a plausible approximation to these ancestral chordates. To illuminate the origins of chordate and vertebrates, we generated a draft of the protein-coding portion of the genome of the most studied ascidian, Ciona intestinalis. The Ciona genome contains approximately 16,000 protein-coding genes, similar to the number in other invertebrates, but only half that found in vertebrates. Vertebrate gene families are typically found in simplified form in Ciona, suggesting that ascidians contain the basic ancestral complement of genes involved in cell signaling and development. The ascidian genome has also acquired a number of lineage-specific innovations, including a group of genes engaged in cellulose metabolism that are related to those in bacteria and fungi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dehal, Paramvir -- Satou, Yutaka -- Campbell, Robert K -- Chapman, Jarrod -- Degnan, Bernard -- De Tomaso, Anthony -- Davidson, Brad -- Di Gregorio, Anna -- Gelpke, Maarten -- Goodstein, David M -- Harafuji, Naoe -- Hastings, Kenneth E M -- Ho, Isaac -- Hotta, Kohji -- Huang, Wayne -- Kawashima, Takeshi -- Lemaire, Patrick -- Martinez, Diego -- Meinertzhagen, Ian A -- Necula, Simona -- Nonaka, Masaru -- Putnam, Nik -- Rash, Sam -- Saiga, Hidetoshi -- Satake, Masanobu -- Terry, Astrid -- Yamada, Lixy -- Wang, Hong-Gang -- Awazu, Satoko -- Azumi, Kaoru -- Boore, Jeffrey -- Branno, Margherita -- Chin-Bow, Stephen -- DeSantis, Rosaria -- Doyle, Sharon -- Francino, Pilar -- Keys, David N -- Haga, Shinobu -- Hayashi, Hiroko -- Hino, Kyosuke -- Imai, Kaoru S -- Inaba, Kazuo -- Kano, Shungo -- Kobayashi, Kenji -- Kobayashi, Mari -- Lee, Byung-In -- Makabe, Kazuhiro W -- Manohar, Chitra -- Matassi, Giorgio -- Medina, Monica -- Mochizuki, Yasuaki -- Mount, Steve -- Morishita, Tomomi -- Miura, Sachiko -- Nakayama, Akie -- Nishizaka, Satoko -- Nomoto, Hisayo -- Ohta, Fumiko -- Oishi, Kazuko -- Rigoutsos, Isidore -- Sano, Masako -- Sasaki, Akane -- Sasakura, Yasunori -- Shoguchi, Eiichi -- Shin-i, Tadasu -- Spagnuolo, Antoinetta -- Stainier, Didier -- Suzuki, Miho M -- Tassy, Olivier -- Takatori, Naohito -- Tokuoka, Miki -- Yagi, Kasumi -- Yoshizaki, Fumiko -- Wada, Shuichi -- Zhang, Cindy -- Hyatt, P Douglas -- Larimer, Frank -- Detter, Chris -- Doggett, Norman -- Glavina, Tijana -- Hawkins, Trevor -- Richardson, Paul -- Lucas, Susan -- Kohara, Yuji -- Levine, Michael -- Satoh, Nori -- Rokhsar, Daniel S -- HD-37105/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2157-67.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481130" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Apoptosis ; Base Sequence ; Cellulose/metabolism ; Central Nervous System/physiology ; Ciona intestinalis/anatomy & histology/classification/*genetics/physiology ; Computational Biology ; Endocrine System/physiology ; Gene Dosage ; Gene Duplication ; Genes ; Genes, Homeobox ; *Genome ; Heart/embryology/physiology ; Immunity/genetics ; Molecular Sequence Data ; Multigene Family ; Muscle Proteins/genetics ; Organizers, Embryonic/physiology ; Phylogeny ; Polymorphism, Genetic ; Proteins/genetics/physiology ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Species Specificity ; Thyroid Gland/physiology ; Urochordata/genetics ; Vertebrates/anatomy & histology/classification/genetics/physiology
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-16
    Description: We describe an approach to detect the frequency of interaction between any two genomic loci. Generation of a matrix of interaction frequencies between sites on the same or different chromosomes reveals their relative spatial disposition and provides information about the physical properties of the chromatin fiber. This methodology can be applied to the spatial organization of entire genomes in organisms from bacteria to human. Using the yeast Saccharomyces cerevisiae, we could confirm known qualitative features of chromosome organization within the nucleus and dynamic changes in that organization during meiosis. We also analyzed yeast chromosome III at the G1 stage of the cell cycle. We found that chromatin is highly flexible throughout. Furthermore, functionally distinct AT- and GC-rich domains were found to exhibit different conformations, and a population-average 3D model of chromosome III could be determined. Chromosome III emerges as a contorted ring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dekker, Job -- Rippe, Karsten -- Dekker, Martijn -- Kleckner, Nancy -- GM25326/GM/NIGMS NIH HHS/ -- GM44794/GM/NIGMS NIH HHS/ -- R01 GM025326/GM/NIGMS NIH HHS/ -- R01 GM044794/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1306-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA. jdekker@fas.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847345" target="_blank"〉PubMed〈/a〉
    Keywords: AT Rich Sequence ; Cell Fractionation ; Cell Nucleus/ultrastructure ; Centromere/chemistry/ultrastructure ; Chromatin/*chemistry/metabolism ; Chromosomes, Fungal/*chemistry/genetics/metabolism/*ultrastructure ; Cross-Linking Reagents ; Deoxyribonuclease EcoRI/metabolism ; Formaldehyde ; *G1 Phase ; GC Rich Sequence ; Genome, Fungal ; Mathematics ; *Meiosis ; Mitosis ; Polymerase Chain Reaction ; Protein Conformation ; Saccharomyces cerevisiae/*genetics/physiology/ultrastructure ; Telomere/chemistry/ultrastructure
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  • 25
    Publication Date: 2002-01-19
    Description: Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of alpha-ketoacid dehydrogenase complexes that are central to intermediary metabolism. We find that Lpd and SucB support Mtb's antioxidant defense. The peroxiredoxin alkyl hydroperoxide reductase (AhpC) is linked to Lpd and SucB by an adaptor protein, AhpD. The 2.0 angstrom AhpD crystal structure reveals a thioredoxin-like active site that is responsive to lipoamide. We propose that Lpd, SucB (the only lipoyl protein detected in Mtb), AhpD, and AhpC together constitute a nicotinamide adenine dinucleotide (reduced)-dependent peroxidase and peroxynitrite reductase. AhpD thus represents a class of thioredoxin-like molecules that enables an antioxidant defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bryk, R -- Lima, C D -- Erdjument-Bromage, H -- Tempst, P -- Nathan, C -- HL61241/HL/NHLBI NIH HHS/ -- P30 CA08748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1073-7. Epub 2002 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799204" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/*metabolism ; Amino Acid Sequence ; Antioxidants ; Binding Sites ; Catalysis ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; Dihydrolipoamide Dehydrogenase/*metabolism ; Hydrogen Bonding ; Hydrogen Peroxide/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mycobacterium tuberculosis/*enzymology/genetics/metabolism ; NAD/metabolism ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Peroxidases/*chemistry/*metabolism ; Peroxiredoxins ; Peroxynitrous Acid/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Thioctic Acid/*analogs & derivatives/metabolism ; Thioredoxins/chemistry/metabolism
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  • 26
    Publication Date: 2002-01-19
    Description: Spider silks are protein-based "biopolymer" filaments or threads secreted by specialized epithelial cells as concentrated soluble precursors of highly repetitive primary sequences. Spider dragline silk is a flexible, lightweight fiber of extraordinary strength and toughness comparable to that of synthetic high-performance fibers. We sought to "biomimic" the process of spider silk production by expressing in mammalian cells the dragline silk genes (ADF-3/MaSpII and MaSpI) of two spider species. We produced soluble recombinant (rc)-dragline silk proteins with molecular masses of 60 to 140 kilodaltons. We demonstrated the wet spinning of silk monofilaments spun from a concentrated aqueous solution of soluble rc-spider silk protein (ADF-3; 60 kilodaltons) under modest shear and coagulation conditions. The spun fibers were water insoluble with a fine diameter (10 to 40 micrometers) and exhibited toughness and modulus values comparable to those of native dragline silks but with lower tenacity. Dope solutions with rc-silk protein concentrations 〉20% and postspinning draw were necessary to achieve improved mechanical properties of the spun fibers. Fiber properties correlated with finer fiber diameter and increased birefringence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lazaris, Anthoula -- Arcidiacono, Steven -- Huang, Yue -- Zhou, Jiang-Feng -- Duguay, Francois -- Chretien, Nathalie -- Welsh, Elizabeth A -- Soares, Jason W -- Karatzas, Costas N -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):472-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nexia Biotechnologies, Vaudreuil-Dorion, Quebec J7V 8P5, Canada. alazaris@nexiabiotech.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799236" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biopolymers ; Birefringence ; Cattle ; Cell Line ; Cloning, Molecular ; Cricetinae ; Culture Media, Conditioned ; DNA, Complementary ; Elasticity ; Epithelial Cells/metabolism ; *Fibroins ; Materials Testing ; Mechanics ; Molecular Sequence Data ; Molecular Weight ; *Protein Biosynthesis ; Protein Structure, Secondary ; Proteins/chemistry/*genetics/isolation & purification ; Recombinant Proteins/biosynthesis/chemistry/isolation & purification ; Solubility ; Spiders/*genetics/metabolism ; Stress, Mechanical ; Tensile Strength ; Water
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  • 27
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-23
    Description: Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenmesser, Elan Zohar -- Bosco, Daryl A -- Akke, Mikael -- Kern, Dorothee -- GM62117/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1520-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859194" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Isomerism ; Kinetics ; Mathematics ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation
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  • 28
    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
    Print ISSN: 0036-8075
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  • 29
    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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  • 30
    Publication Date: 2002-05-23
    Description: Genes involved in late specification of the mandibular arch, the source of the vertebrate jaw, are expressed with similar patterns in the oral regions of chick and lamprey embryos. However, morphological comparisons indicate that apparently orthologous homeobox genes were expressed in different subdivisions of the ectomesenchyme in the two species. Therefore, the homology and gene expression of the oral region are uncoupled during the transition from agnathan to gnathostome; we conclude that a heterotopic shift of tissue interaction was involved in the evolution of the jaw.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shigetani, Yasuyo -- Sugahara, Fumiaki -- Kawakami, Yayoi -- Murakami, Yasunori -- Hirano, Shigeki -- Kuratani, Shigeru -- New York, N.Y. -- Science. 2002 May 17;296(5571):1316-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Evolutionary Morphology, Center for Developmental Biology, RIKEN, Hyogo 650-0047, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016315" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Body Patterning ; Bone Morphogenetic Proteins/genetics/pharmacology/physiology ; Brain/embryology/metabolism ; Chick Embryo ; Epidermis/embryology/metabolism ; Epithelium/embryology/physiology ; Fibroblast Growth Factors/genetics/pharmacology/physiology ; Gene Expression Profiling ; *Gene Expression Regulation, Developmental ; Genes, Homeobox ; Homeodomain Proteins/genetics/metabolism ; Humans ; *Jaw/anatomy & histology/embryology ; Lampreys/*embryology/genetics ; Lip/embryology/metabolism ; Mandible/anatomy & histology/*embryology ; Mesoderm/metabolism/*physiology ; Molecular Sequence Data ; Mouth/embryology/metabolism ; Neural Crest/embryology/physiology ; Phylogeny ; Transcription Factors
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  • 31
    Publication Date: 2002-08-24
    Description: Polyketide synthases (PKSs) assemble the polyketide carbon backbone by sequential decarboxylative condensation of acyl coenzyme A (CoA) precursors, and the C-C bond-forming step in this process is catalyzed by the beta-ketoacyl synthase (KS) domain or subunit. Genetic and biochemical characterization of the nonactin biosynthesis gene cluster from Streptomyces griseus revealed two KSs, NonJ and NonK, that are highly homologous to known KSs but catalyze sequential condensation of the acyl CoA substrates by forming C-O rather than C-C bonds. This chemistry can be used in PKS engineering to increase the scope and diversity of polyketide biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kwon, Hyung-Jin -- Smith, Wyatt C -- Scharon, A Janelle -- Hwang, Sung Hee -- Kurth, Mark J -- Shen, Ben -- AI51689/AI/NIAID NIH HHS/ -- T32 GM08505/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1327-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Pharmaceutical Sciences and, Department of Chemistry, University of Wisconsin, Madison, WI 53705, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193782" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/*chemistry/*metabolism ; Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalysis ; Chromatography, High Pressure Liquid ; Genes, Bacterial ; Macrolides/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/*metabolism ; Multigene Family ; Mutation ; Protein Engineering ; Protein Subunits ; Sequence Alignment ; Spectrometry, Mass, Electrospray Ionization ; Streptomyces/genetics ; Streptomyces griseus/*enzymology/genetics ; Transformation, Bacterial
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  • 32
    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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  • 33
    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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  • 34
    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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  • 35
    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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  • 36
    Publication Date: 2002-06-29
    Description: Comparison of two fully sequenced genomes of Buchnera aphidicola, the obligate endosymbionts of aphids, reveals the most extreme genome stability to date: no chromosome rearrangements or gene acquisitions have occurred in the past 50 to 70 million years, despite substantial sequence evolution and the inactivation and loss of individual genes. In contrast, the genomes of their closest free-living relatives, Escherichia coli and Salmonella spp., are more than 2000-fold more labile in content and gene order. The genomic stasis of B. aphidicola, likely attributable to the loss of phages, repeated sequences, and recA, indicates that B. aphidicola is no longer a source of ecological innovation for its hosts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tamas, Ivica -- Klasson, Lisa -- Canback, Bjorn -- Naslund, A Kristina -- Eriksson, Ann-Sofie -- Wernegreen, Jennifer J -- Sandstrom, Jonas P -- Moran, Nancy A -- Andersson, Siv G E -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2376-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Evolution, Evolutionary Biology Center, University of Uppsala, Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089438" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aphids/*microbiology/physiology ; Bacterial Proteins/chemistry/genetics ; Biological Evolution ; Buchnera/*genetics/physiology ; DNA, Intergenic ; Diet ; Ecosystem ; Escherichia coli/genetics ; *Evolution, Molecular ; Genes, Bacterial ; Genetic Variation ; *Genome, Bacterial ; Molecular Sequence Data ; Mutation ; Operon ; Pseudogenes ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Salmonella typhimurium/genetics ; Species Specificity ; *Symbiosis
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  • 37
    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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  • 38
    Publication Date: 2002-09-28
    Description: Insecticide resistance is one of the most widespread genetic changes caused by human activity, but we still understand little about the origins and spread of resistant alleles in global populations of insects. Here, via microarray analysis of all P450s in Drosophila melanogaster, we show that DDT-R, a gene conferring resistance to DDT, is associated with overtranscription of a single cytochrome P450 gene, Cyp6g1. Transgenic analysis of Cyp6g1 shows that overtranscription of this gene alone is both necessary and sufficient for resistance. Resistance and up-regulation in Drosophila populations are associated with a single Cyp6g1 allele that has spread globally. This allele is characterized by the insertion of an Accord transposable element into the 5' end of the Cyp6g1 gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daborn, P J -- Yen, J L -- Bogwitz, M R -- Le Goff, G -- Feil, E -- Jeffers, S -- Tijet, N -- Perry, T -- Heckel, D -- Batterham, P -- Feyereisen, R -- Wilson, T G -- ffrench-Constant, R H -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2253-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351787" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Animals, Genetically Modified ; Base Sequence ; Chromosome Mapping ; Cytochrome P-450 Enzyme System/*genetics/metabolism ; *Ddt ; Drosophila Proteins/*genetics/metabolism ; Drosophila melanogaster/enzymology/*genetics ; Gene Expression Profiling ; Gene Expression Regulation, Enzymologic ; *Genes, Insect ; Insecticide Resistance/*genetics ; *Insecticides/metabolism ; Introns ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Phylogeny ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, DNA ; Substrate Specificity ; Transcription, Genetic ; Transgenes
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  • 39
    Publication Date: 2002-03-23
    Description: P/Q-type presynaptic calcium currents (IpCa) undergo activity-dependent facilitation during repetitive activation at the calyx of the Held synapse. We investigated whether neuronal calcium sensor 1 (NCS-1) may underlie this phenomenon. Direct loading of NCS-1 into the nerve terminal mimicked activity-dependent IpCa facilitation by accelerating the activation time of IpCa in a Ca2+-dependent manner. A presynaptically loaded carboxyl-terminal peptide of NCS-1 abolished IpCa facilitation. These results suggest that residual Ca2+ activates endogenous NCS-1, thereby facilitating IpCa. Because both P/Q-type Ca2+ channels and NCS-1 are widely expressed in mammalian nerve terminals, NCS-1 may contribute to the activity-dependent synaptic facilitation at many synapses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsujimoto, Tetsuhiro -- Jeromin, Andreas -- Saitoh, Naoto -- Roder, John C -- Takahashi, Tomoyuki -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2276-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, University of Tokyo Faculty of Medicine, Tokyo 113-0033, Japan. tujimoto-tky@umin.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910115" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Amino Acid Sequence ; Animals ; Brain Stem/cytology/drug effects/metabolism ; Calcium/*metabolism/pharmacology ; Calcium Channels/*metabolism ; Calcium-Binding Proteins/administration & ; dosage/chemistry/*metabolism/pharmacology ; Electric Conductivity ; In Vitro Techniques ; Ion Channel Gating/drug effects ; Molecular Sequence Data ; Neuronal Calcium-Sensor Proteins ; Neuropeptides/administration & dosage/chemistry/*metabolism/pharmacology ; Presynaptic Terminals/drug effects/*metabolism ; Rats ; Rats, Wistar
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  • 40
    Publication Date: 2002-05-11
    Description: The majority (〉99%) of microorganisms from the environment resist cultivation in the laboratory. Ribosomal RNA analysis suggests that uncultivated organisms are found in nearly every prokaryotic group, and several divisions have no known cultivable representatives. We designed a diffusion chamber that allowed the growth of previously uncultivated microorganisms in a simulated natural environment. Colonies of representative marine organisms were isolated in pure culture. These isolates did not grow on artificial media alone but formed colonies in the presence of other microorganisms. This observation may help explain the nature of microbial uncultivability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaeberlein, T -- Lewis, K -- Epstein, S S -- New York, N.Y. -- Science. 2002 May 10;296(5570):1127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Northeastern University, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004133" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/classification/cytology/*growth & development/*isolation & purification ; *Bacteriological Techniques ; Colony Count, Microbial ; Culture Media ; DNA, Bacterial/analysis/genetics ; DNA, Ribosomal/analysis/genetics ; Diffusion Chambers, Culture ; Geologic Sediments/*microbiology ; Molecular Sequence Data ; RNA, Ribosomal, 16S/genetics ; *Seawater ; Silicon Dioxide
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  • 41
    Publication Date: 2002-03-23
    Description: One role of messenger RNA (mRNA) degradation is to maintain the fidelity of gene expression by degrading aberrant transcripts. Recent results show that mRNAs without translation termination codons are unstable in eukaryotic cells. We used yeast mutants to demonstrate that these "nonstop" mRNAs are degraded by the exosome in a 3'-to-5' direction. The degradation of nonstop transcripts requires the exosome-associated protein Ski7p. Ski7p is closely related to the translation elongation factor EF1A and the translation termination factor eRF3. This suggests that the recognition of nonstop mRNAs involves the binding of Ski7p to an empty aminoacyl-(RNA-binding) site (A site) on the ribosome, thereby bringing the exosome to a mRNA with a ribosome stalled near the 3' end. This system efficiently degrades mRNAs that are prematurely polyadenylated within the coding region and prevents their expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Hoof, Ambro -- Frischmeyer, Pamela A -- Dietz, Harry C -- Parker, Roy -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2262-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, 4000 Jones Bridge Road, Chevy Chase, MD 20815, USA. : ambro@u.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910110" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Alleles ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Codon, Terminator/*genetics ; Fungal Proteins/chemistry/genetics/*metabolism ; *GTP-Binding Proteins ; Gene Expression Regulation, Fungal ; Genes, Fungal/genetics ; Half-Life ; Molecular Sequence Data ; Polyadenylation ; Protein Binding ; Protein Biosynthesis ; RNA 3' End Processing ; *RNA Processing, Post-Transcriptional ; RNA Stability ; RNA, Fungal/genetics/metabolism ; RNA, Messenger/*genetics/*metabolism ; Ribosomes/metabolism ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Sequence Alignment ; Sequence Deletion/*genetics
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  • 42
    Publication Date: 2002-07-13
    Description: Arabidopsis VRN genes mediate vernalization, the process by which a long period of cold induces a mitotically stable state that leads to accelerated flowering during later development. VRN1 encodes a protein that binds DNA in vitro in a non-sequence-specific manner and functions in stable repression of the major target of the vernalization pathway, the floral repressor FLC. Overexpression of VRN1 reveals a vernalization-independent function for VRN1, mediated predominantly through the floral pathway integrator FT, and demonstrates that VRN1 requires vernalization-specific factors to target FLC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, Yaron Y -- Mesnage, Stephane -- Mylne, Joshua S -- Gendall, Anthony R -- Dean, Caroline -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, 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/12114624" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/anatomy & histology/*genetics/growth & development/*physiology ; Arabidopsis Proteins/chemistry/*genetics/metabolism/*physiology ; Base Sequence ; Cloning, Molecular ; DNA, Plant/genetics/metabolism ; DNA-Binding Proteins/chemistry/*genetics/*physiology ; Down-Regulation ; Gene Expression Regulation, Plant ; Genes, Plant ; MADS Domain Proteins/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Photoperiod ; Plant Proteins/genetics/metabolism ; Plant Structures/anatomy & histology/physiology ; Plants, Genetically Modified ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; *Repressor Proteins ; Temperature
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  • 43
    Publication Date: 2002-04-16
    Description: Tomato plants harboring the ripening-inhibitor (rin) mutation yield fruits that fail to ripen. Additionally, rin plants display enlarged sepals and loss of inflorescence determinacy. Positional cloning of the rin locus revealed two tandem MADS-box genes (LeMADS-RIN and LeMADS-MC), whose expression patterns suggested roles in fruit ripening and sepal development, respectively. The rin mutation alters expression of both genes. Gene repression and mutant complementation demonstrate that LeMADS-RIN regulates ripening, whereas LeMADS-MC affects sepal development and inflorescence determinacy. LeMADS-RIN demonstrates an agriculturally important function of plant MADS-box genes and provides molecular insight into nonhormonal (developmental) regulation of ripening.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vrebalov, Julia -- Ruezinsky, Diane -- Padmanabhan, Veeraragavan -- White, Ruth -- Medrano, Diana -- Drake, Rachel -- Schuch, Wolfgang -- Giovannoni, Jim -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):343-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Agriculture-Agricultural Research Service (USDA-ARS) Plant, Soil and Nutrition Lab and Boyce Thompson Institute for Plant Research, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11951045" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; Chromosomes, Artificial, Yeast ; Cloning, Molecular ; DNA, Antisense ; DNA, Complementary ; Ethylenes/biosynthesis/pharmacology ; Fruit/physiology ; Gene Expression ; Gene Expression Regulation, Plant ; *Genes, Plant ; Genetic Complementation Test ; Lycopersicon esculentum/*genetics/*physiology ; MADS Domain Proteins/*genetics/physiology ; Molecular Sequence Data ; Mutation ; Phylogeny ; Plant Proteins/*genetics/physiology ; Plant Structures/genetics/physiology ; Plants, Genetically Modified
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  • 44
    Publication Date: 2002-09-07
    Description: A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Einsle, Oliver -- Tezcan, F Akif -- Andrade, Susana L A -- Schmid, Benedikt -- Yoshida, Mika -- Howard, James B -- Rees, Douglas C -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1696-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Division of Chemistry and Chemical Engineering, California Institute of Technology, Mail Code 147-75CH, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215645" target="_blank"〉PubMed〈/a〉
    Keywords: Azotobacter vinelandii/enzymology ; Coenzymes/*chemistry/metabolism ; Crystallography, X-Ray ; Ligands ; Models, Molecular ; Molybdoferredoxin/*chemistry/metabolism ; Nitrogen/chemistry ; Nitrogenase/*chemistry/metabolism ; Protein Conformation
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  • 45
    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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  • 46
    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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  • 47
    Publication Date: 2002-07-27
    Description: Helicobacter pylori adherence in the human gastric mucosa involves specific bacterial adhesins and cognate host receptors. Here, we identify sialyl-dimeric-Lewis x glycosphingolipid as a receptor for H. pylori and show that H. pylori infection induced formation of sialyl-Lewis x antigens in gastric epithelium in humans and in a Rhesus monkey. The corresponding sialic acid-binding adhesin (SabA) was isolated with the "retagging" method, and the underlying sabA gene (JHP662/HP0725) was identified. The ability of many H. pylori strains to adhere to sialylated glycoconjugates expressed during chronic inflammation might thus contribute to virulence and the extraordinary chronicity of H. pylori infection.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2570540/" 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/PMC2570540/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahdavi, Jafar -- Sonden, Berit -- Hurtig, Marina -- Olfat, Farzad O -- Forsberg, Lina -- Roche, Niamh -- Angstrom, Jonas -- Larsson, Thomas -- Teneberg, Susann -- Karlsson, Karl-Anders -- Altraja, Siiri -- Wadstrom, Torkel -- Kersulyte, Dangeruta -- Berg, Douglas E -- Dubois, Andre -- Petersson, Christoffer -- Magnusson, Karl-Eric -- Norberg, Thomas -- Lindh, Frank -- Lundskog, Bertil B -- Arnqvist, Anna -- Hammarstrom, Lennart -- Boren, Thomas -- P30 DK52574/DK/NIDDK NIH HHS/ -- R01 AI38166/AI/NIAID NIH HHS/ -- R01 CA082312/CA/NCI NIH HHS/ -- R01 CA082312-08/CA/NCI NIH HHS/ -- R01 DK53727/DK/NIDDK NIH HHS/ -- R03 AI49161/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):573-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Odontology/Oral Microbiology, Umea University, SE-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142529" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/isolation & purification/*metabolism ; Amino Acid Sequence ; Animals ; Antigens, CD15/*metabolism ; *Bacterial Adhesion ; Carbohydrate Sequence ; Carrier Proteins/genetics/metabolism ; Gastric Mucosa/immunology/metabolism/*microbiology ; Gastritis/immunology/metabolism/*microbiology ; Genes, Bacterial ; Glycoconjugates/metabolism ; Helicobacter Infections/immunology/metabolism/*microbiology ; Helicobacter pylori/genetics/isolation & purification/*physiology ; Humans ; Macaca mulatta ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Oligosaccharides/*metabolism ; Sialic Acids/metabolism
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  • 48
    Publication Date: 2002-05-23
    Description: The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (alpha2betabeta'omegasigmaA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel. All sequence-specific contacts with core promoter elements are mediated by the sigma subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the sigma subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced -10 and -35 elements and provides the basis for models of the closed and open promoter complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murakami, Katsuhiko S -- Masuda, Shoko -- Campbell, Elizabeth A -- Muzzin, Oriana -- Darst, Seth A -- GM20470/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- GM61898/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1285-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016307" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA, Bacterial/*chemistry/genetics/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Subunits ; Sigma Factor/*chemistry/metabolism ; Templates, Genetic ; Thermus/*enzymology ; *Transcription, Genetic
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  • 49
    Publication Date: 2002-06-01
    Description: The high degree of similarity between the mouse and human genomes is demonstrated through analysis of the sequence of mouse chromosome 16 (Mmu 16), which was obtained as part of a whole-genome shotgun assembly of the mouse genome. The mouse genome is about 10% smaller than the human genome, owing to a lower repetitive DNA content. Comparison of the structure and protein-coding potential of Mmu 16 with that of the homologous segments of the human genome identifies regions of conserved synteny with human chromosomes (Hsa) 3, 8, 12, 16, 21, and 22. Gene content and order are highly conserved between Mmu 16 and the syntenic blocks of the human genome. Of the 731 predicted genes on Mmu 16, 509 align with orthologs on the corresponding portions of the human genome, 44 are likely paralogous to these genes, and 164 genes have homologs elsewhere in the human genome; there are 14 genes for which we could find no human counterpart.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mural, Richard J -- Adams, Mark D -- Myers, Eugene W -- Smith, Hamilton O -- Miklos, George L Gabor -- Wides, Ron -- Halpern, Aaron -- Li, Peter W -- Sutton, Granger G -- Nadeau, Joe -- Salzberg, Steven L -- Holt, Robert A -- Kodira, Chinnappa D -- Lu, Fu -- Chen, Lin -- Deng, Zuoming -- Evangelista, Carlos C -- Gan, Weiniu -- Heiman, Thomas J -- Li, Jiayin -- Li, Zhenya -- Merkulov, Gennady V -- Milshina, Natalia V -- Naik, Ashwinikumar K -- Qi, Rong -- Shue, Bixiong Chris -- Wang, Aihui -- Wang, Jian -- Wang, Xin -- Yan, Xianghe -- Ye, Jane -- Yooseph, Shibu -- Zhao, Qi -- Zheng, Liansheng -- Zhu, Shiaoping C -- Biddick, Kendra -- Bolanos, Randall -- Delcher, Arthur L -- Dew, Ian M -- Fasulo, Daniel -- Flanigan, Michael J -- Huson, Daniel H -- Kravitz, Saul A -- Miller, Jason R -- Mobarry, Clark M -- Reinert, Knut -- Remington, Karin A -- Zhang, Qing -- Zheng, Xiangqun H -- Nusskern, Deborah R -- Lai, Zhongwu -- Lei, Yiding -- Zhong, Wenyan -- Yao, Alison -- Guan, Ping -- Ji, Rui-Ru -- Gu, Zhiping -- Wang, Zhen-Yuan -- Zhong, Fei -- Xiao, Chunlin -- Chiang, Chia-Chien -- Yandell, Mark -- Wortman, Jennifer R -- Amanatides, Peter G -- Hladun, Suzanne L -- Pratts, Eric C -- Johnson, Jeffery E -- Dodson, Kristina L -- Woodford, Kerry J -- Evans, Cheryl A -- Gropman, Barry -- Rusch, Douglas B -- Venter, Eli -- Wang, Mei -- Smith, Thomas J -- Houck, Jarrett T -- Tompkins, Donald E -- Haynes, Charles -- Jacob, Debbie -- Chin, Soo H -- Allen, David R -- Dahlke, Carl E -- Sanders, Robert -- Li, Kelvin -- Liu, Xiangjun -- Levitsky, Alexander A -- Majoros, William H -- Chen, Quan -- Xia, Ashley C -- Lopez, John R -- Donnelly, Michael T -- Newman, Matthew H -- Glodek, Anna -- Kraft, Cheryl L -- Nodell, Marc -- Ali, Feroze -- An, Hui-Jin -- Baldwin-Pitts, Danita -- Beeson, Karen Y -- Cai, Shuang -- Carnes, Mark -- Carver, Amy -- Caulk, Parris M -- Center, Angela -- Chen, Yen-Hui -- Cheng, Ming-Lai -- Coyne, My D -- Crowder, Michelle -- Danaher, Steven -- Davenport, Lionel B -- Desilets, Raymond -- Dietz, Susanne M -- Doup, Lisa -- Dullaghan, Patrick -- Ferriera, Steven -- Fosler, Carl R -- Gire, Harold C -- Gluecksmann, Andres -- Gocayne, Jeannine D -- Gray, Jonathan -- Hart, Brit -- Haynes, Jason -- Hoover, Jeffery -- Howland, Tim -- Ibegwam, Chinyere -- Jalali, Mena -- Johns, David -- Kline, Leslie -- Ma, Daniel S -- MacCawley, Steven -- Magoon, Anand -- Mann, Felecia -- May, David -- McIntosh, Tina C -- Mehta, Somil -- Moy, Linda -- Moy, Mee C -- Murphy, Brian J -- Murphy, Sean D -- Nelson, Keith A -- Nuri, Zubeda -- Parker, Kimberly A -- Prudhomme, Alexandre C -- Puri, Vinita N -- Qureshi, Hina -- Raley, John C -- Reardon, Matthew S -- Regier, Megan A -- Rogers, Yu-Hui C -- Romblad, Deanna L -- Schutz, Jakob -- Scott, John L -- Scott, Richard -- Sitter, Cynthia D -- Smallwood, Michella -- Sprague, Arlan C -- Stewart, Erin -- Strong, Renee V -- Suh, Ellen -- Sylvester, Karena -- Thomas, Reginald -- Tint, Ni Ni -- Tsonis, Christopher -- Wang, Gary -- Wang, George -- Williams, Monica S -- Williams, Sherita M -- Windsor, Sandra M -- Wolfe, Keriellen -- Wu, Mitchell M -- Zaveri, Jayshree -- Chaturvedi, Kabir -- Gabrielian, Andrei E -- Ke, Zhaoxi -- Sun, Jingtao -- Subramanian, Gangadharan -- Venter, J Craig -- Pfannkoch, Cynthia M -- Barnstead, Mary -- Stephenson, Lisa D -- New York, N.Y. -- Science. 2002 May 31;296(5573):1661-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Celera Genomics, 45 West Gude Drive, Rockville, MD 20850, USA. richard.mural@celera.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040188" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Chromosomes/*genetics ; Chromosomes, Human/genetics ; Computational Biology ; Conserved Sequence ; Databases, Nucleic Acid ; Evolution, Molecular ; Genes ; Genetic Markers ; *Genome ; *Genome, Human ; Genomics ; Humans ; Mice ; Mice, Inbred A/genetics ; Mice, Inbred DBA/genetics ; Mice, Inbred Strains/*genetics ; Molecular Sequence Data ; Physical Chromosome Mapping ; Proteins/chemistry/genetics ; Sequence Alignment ; *Sequence Analysis, DNA ; Species Specificity ; *Synteny
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  • 50
    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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  • 51
    Publication Date: 2002-06-22
    Description: The Arabidopsis gene DDM1 is required to maintain DNA methylation levels and is responsible for transposon and transgene silencing. However, rather than encoding a DNA methyltransferase, DDM1 has similarity to the SWI/SNF family of adenosine triphosphate-dependent chromatin remodeling genes, suggesting an indirect role in DNA methylation. Here we show that DDM1 is also required to maintain histone H3 methylation patterns. In wild-type heterochromatin, transposons and silent genes are associated with histone H3 methylated at lysine 9, whereas known genes are preferentially associated with methylated lysine 4. In ddm1 heterochromatin, DNA methylation is lost, and methylation of lysine 9 is largely replaced by methylation of lysine 4. Because DNA methylation has recently been shown to depend on histone H3 lysine 9 methylation, our results suggest that transposon methylation may be guided by histone H3 methylation in plant genomes. This would account for the epigenetic inheritance of hypomethylated DNA once histone H3 methylation patterns are altered.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gendrel, Anne-Valerie -- Lippman, Zachary -- Yordan, Cristy -- Colot, Vincent -- Martienssen, Robert A -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1871-3. Epub 2002 Jun 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077425" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arabidopsis/*genetics/metabolism ; Arabidopsis Proteins/chemistry/genetics/metabolism ; DNA Methylation ; DNA Transposable Elements ; DNA, Plant/metabolism ; DNA-Binding Proteins/*genetics/physiology ; Gene Expression ; Gene Expression Profiling ; Gene Silencing ; *Genes, Plant ; Heterochromatin/*metabolism ; Histones/chemistry/*metabolism ; Humans ; Lysine/metabolism ; Methylation ; Molecular Sequence Data ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Alignment ; Transcription Factors/*genetics/physiology
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-10-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, John W -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):552-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA. john.peters@chemistry.montana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386322" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acetyl Coenzyme A/metabolism ; Aldehyde Oxidoreductases/*chemistry/*metabolism ; Anaerobiosis ; Binding Sites ; Biomass ; Carbon Dioxide/*metabolism ; Carbon Monoxide/metabolism ; Clostridium/enzymology ; Copper/*chemistry ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Iron/*chemistry ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Nickel/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Quaternary
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  • 53
    Publication Date: 2002-03-30
    Description: Type I ubiquitin-like proteins constitute a family of protein modifiers. Here we report the identification of a posttranslational protein modifier from Saccharomyces cerevisiae, Hub1. Overexpression of Hub1 resulted in enhanced conjugate formation when its carboxyl-terminal residue was deleted, suggesting that mature Hub1 may be produced by proteolytic processing. In vivo targets of Hub1 conjugation included cell polarity factors Sph1 and Hbt1. In the hub1Delta mutant, the subcellular localization of both Hbt1 and Sph1 was disrupted, and cell polarization during the formation of mating projections was defective. Consistent with these polarization defects, the hub1Delta mutant was deficient in mating.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dittmar, Gunnar A G -- Wilkinson, Caroline R M -- Jedrzejewski, Paul T -- Finley, Daniel -- GM58223/GM/NIGMS NIH HHS/ -- GM62663/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2442-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923536" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Evolution ; *Cell Polarity ; Electrophoresis, Gel, Two-Dimensional ; Gene Deletion ; Genes, Fungal ; Humans ; Ligases/chemistry/genetics/*metabolism ; Mass Spectrometry ; *Microfilament Proteins ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Peptides/pharmacology ; Phenotype ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*physiology ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Schizosaccharomyces/genetics ; Sequence Alignment ; Subcellular Fractions/metabolism ; Ubiquitin/chemistry/metabolism
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  • 54
    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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  • 55
    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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  • 56
    Publication Date: 2002-05-25
    Description: The mating response of the budding yeast Saccharomyces cerevisiae is mediated by a prototypical heterotrimeric GTP-binding protein (G protein) and mitogen-activated protein kinase (MAPK) cascade. Although signal transmission by such pathways has been modeled in detail, postreceptor down-regulation is less well understood. The pheromone-responsive G protein alpha subunit (Galpha) of yeast down-regulates the mating signal, but its targets are unknown. We have found that Galpha binds directly to the mating-specific MAPK in yeast cells responding to pheromone. This interaction contributes both to modulation of the mating signal and to the chemotropic response, and it demonstrates direct communication between the top and bottom of a Galpha-MAPK pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Metodiev, Metodi V -- Matheos, Dina -- Rose, Mark D -- Stone, David E -- New York, N.Y. -- Science. 2002 May 24;296(5572):1483-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, 900 South Ashland Avenue (M/C 567), Chicago, IL 60607, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029138" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Down-Regulation ; *GTP-Binding Protein alpha Subunits ; GTP-Binding Protein alpha Subunits, Gq-G11 ; *GTP-Binding Protein beta Subunits ; Guanosine Diphosphate/metabolism ; Heterotrimeric GTP-Binding Proteins/chemistry/genetics/*metabolism ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/*metabolism ; Molecular Sequence Data ; Mutation ; Pheromones/pharmacology ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism/physiology ; Saccharomyces cerevisiae Proteins/*metabolism
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  • 57
    Publication Date: 2002-07-20
    Description: It has been more than 10 years since it was first proposed that the neurodegeneration in Alzheimer's disease (AD) may be caused by deposition of amyloid beta-peptide (Abeta) in plaques in brain tissue. According to the amyloid hypothesis, accumulation of Abeta in the brain is the primary influence driving AD pathogenesis. The rest of the disease process, including formation of neurofibrillary tangles containing tau protein, is proposed to result from an imbalance between Abeta production and Abeta clearance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardy, John -- Selkoe, Dennis J -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Neurogenetics, National Institute on Aging, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130773" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*drug therapy/*etiology/genetics/pathology ; Amino Acid Sequence ; Amyloid beta-Peptides/*metabolism ; Amyloid beta-Protein Precursor/chemistry/genetics/metabolism ; Animals ; Anti-Inflammatory Agents/therapeutic use ; Anticholesteremic Agents/therapeutic use ; Brain/*metabolism/pathology ; Clinical Trials as Topic ; Humans ; Molecular Sequence Data ; Nerve Degeneration ; Neurofibrillary Tangles/metabolism/pathology ; Neurons/pathology ; Plaque, Amyloid/pathology ; Protease Inhibitors/therapeutic use ; tau Proteins/metabolism
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-16
    Description: GSK3/SHAGGY is a highly conserved serine/threonine kinase implicated in many signaling pathways in eukaryotes. Although many GSK3/SHAGGY-like kinases have been identified in plants, little is known about their functions in plant growth and development. Here we show that the Arabidopsis BRASSINOSTEROID-INSENSITIVE 2 (BIN2) gene encodes a GSK3/SHAGGY-like kinase. Gain-of-function mutations within its coding sequence or its overexpression inhibit brassinosteroid (BR) signaling, resulting in plants that resemble BR-deficient and BR-response mutants. In contrast, reduced BIN2 expression via cosuppression partially rescues a weak BR-signaling mutation. Thus, BIN2 acts as a negative regulator to control steroid signaling in plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Jianming -- Nam, Kyoung Hee -- GM60519/GM/NIGMS NIH HHS/ -- R01 GM060519/GM/NIGMS NIH HHS/ -- R01 GM060519-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1299-301.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*enzymology/genetics/growth & development/metabolism ; Arabidopsis Proteins/chemistry/*genetics/*metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/chemistry ; Cloning, Molecular ; *Drosophila Proteins ; Genes, Plant ; Glycogen Synthase Kinase 3 ; Humans ; Molecular Sequence Data ; Mutation ; Phenotype ; Phosphorylation ; Plant Growth Regulators/*metabolism ; Plants, Genetically Modified ; Protein Kinases/chemistry/*genetics/*metabolism ; Protein-Serine-Threonine Kinases/chemistry ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction ; Steroids/*metabolism
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  • 59
    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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  • 60
    Publication Date: 2002-03-09
    Description: Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent protein misfolding and aggregation in the crowded environment of the cell. Nascent chain--binding chaperones, including trigger factor, Hsp70, and prefoldin, stabilize elongating chains on ribosomes in a nonaggregated state. Folding in the cytosol is achieved either on controlled chain release from these factors or after transfer of newly synthesized proteins to downstream chaperones, such as the chaperonins. These are large, cylindrical complexes that provide a central compartment for a single protein chain to fold unimpaired by aggregation. Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hartl, F Ulrich -- Hayer-Hartl, Manajit -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1852-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biochemistry, Max-Planck-Institut fur Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany. uhartl@biochem.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884745" target="_blank"〉PubMed〈/a〉
    Keywords: Chaperonins/chemistry/metabolism ; Cytosol/*chemistry ; Eukaryotic Cells/*chemistry/metabolism ; HSP70 Heat-Shock Proteins/chemistry/metabolism ; Macromolecular Substances ; Models, Molecular ; Molecular Chaperones/chemistry/*metabolism ; Prokaryotic Cells/*chemistry/metabolism ; Protein Binding ; Protein Biosynthesis ; Protein Conformation ; *Protein Folding ; Proteins/*chemistry/metabolism ; Ribosomes/metabolism
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Katzenellenbogen, Benita S -- Katzenellenbogen, John A -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2380-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Integrative Physiology, University of Illinois and College of Medicine at Urbana-Champaign, Urbana, IL 61801, USA. katzenel@life.uiuc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923515" target="_blank"〉PubMed〈/a〉
    Keywords: Breast/*drug effects/metabolism ; Breast Neoplasms/drug therapy/metabolism/prevention & control ; DNA/metabolism ; Drug Resistance, Neoplasm ; Estradiol/metabolism/pharmacology ; Estrogen Replacement Therapy ; Female ; Histone Acetyltransferases ; Humans ; Ligands ; Macromolecular Substances ; Nuclear Receptor Coactivator 1 ; Organ Specificity ; Protein Conformation ; Raloxifene Hydrochloride/pharmacology ; Receptors, Estrogen/chemistry/*metabolism ; Response Elements ; Selective Estrogen Receptor Modulators/*metabolism/*pharmacology ; Tamoxifen/chemistry/metabolism/pharmacology/therapeutic use ; Transcription Factors/metabolism ; Uterine Neoplasms/metabolism ; Uterus/*drug effects/metabolism
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  • 62
    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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  • 63
    Publication Date: 2002-09-28
    Description: Celiac Sprue, a widely prevalent autoimmune disease of the small intestine, is induced in genetically susceptible individuals by exposure to dietary gluten. A 33-mer peptide was identified that has several characteristics suggesting it is the primary initiator of the inflammatory response to gluten in Celiac Sprue patients. In vitro and in vivo studies in rats and humans demonstrated that it is stable toward breakdown by all gastric, pancreatic, and intestinal brush-border membrane proteases. The peptide reacted with tissue transglutaminase, the major autoantigen in Celiac Sprue, with substantially greater selectivity than known natural substrates of this extracellular enzyme. It was a potent inducer of gut-derived human T cell lines from 14 of 14 Celiac Sprue patients. Homologs of this peptide were found in all food grains that are toxic to Celiac Sprue patients but are absent from all nontoxic food grains. The peptide could be detoxified in in vitro and in vivo assays by exposure to a bacterial prolyl endopeptidase, suggesting a strategy for oral peptidase supplement therapy for Celiac Sprue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shan, Lu -- Molberg, Oyvind -- Parrot, Isabelle -- Hausch, Felix -- Filiz, Ferda -- Gray, Gary M -- Sollid, Ludvig M -- Khosla, Chaitan -- R01 DK100619/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2275-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351792" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Celiac Disease/*immunology/therapy ; Cell Line ; Edible Grain/chemistry ; Endopeptidases/metabolism ; Epitopes, T-Lymphocyte ; GTP-Binding Proteins/metabolism ; Gliadin/*chemistry/*immunology/metabolism ; HLA-DQ Antigens/immunology ; Humans ; Immunodominant Epitopes ; Intestinal Mucosa/enzymology/*immunology ; Intestine, Small/enzymology/*immunology ; Lymphocyte Activation ; Microvilli/enzymology ; Molecular Sequence Data ; Peptide Fragments/chemistry/immunology ; Rats ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology, Amino Acid ; Serine Endopeptidases/administration & dosage/metabolism/therapeutic use ; T-Lymphocytes/*immunology ; Transglutaminases/metabolism
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  • 64
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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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  • 65
    Publication Date: 2002-07-20
    Description: The mammalian protein MBD4 contains a methyl-CpG binding domain and can enzymatically remove thymine (T) or uracil (U) from a mismatched CpG site in vitro. These properties suggest that MBD4 might function in vivo to minimize the mutability of 5-methylcytosine by removing its deamination product from DNA. We tested this hypothesis by analyzing Mbd4-/- mice and found that the frequency of of C --〉 T transitions at CpG sites was increased by a factor of three. On a cancer-susceptible Apc(Min/+) background, Mbd4-/- mice showed accelerated tumor formation with CpG --〉 TpG mutations in the Apc gene. Thus MBD4 suppresses CpG mutability and tumorigenesis in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Millar, Catherine B -- Guy, Jacky -- Sansom, Owen J -- Selfridge, Jim -- MacDougall, Eilidh -- Hendrich, Brian -- Keightley, Peter D -- Bishop, Stefan M -- Clarke, Alan R -- Bird, Adrian -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):403-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Cell Biology, The King's Buildings, Edinburgh University, Edinburgh EH9 3JR, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130785" target="_blank"〉PubMed〈/a〉
    Keywords: 5-Methylcytosine ; Alleles ; Amino Acid Sequence ; Animals ; Base Pair Mismatch ; Cytosine/*analogs & derivatives/metabolism ; DNA Methylation ; DNA Repair ; Deamination ; Dinucleoside Phosphates/*genetics ; Endodeoxyribonucleases/*genetics/*physiology ; Female ; Gene Targeting ; Genes, APC ; Genetic Predisposition to Disease ; Intestinal Neoplasms/etiology/*genetics ; Intestine, Large ; Loss of Heterozygosity ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; *Point Mutation ; Suppression, Genetic
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  • 66
    Publication Date: 2002-02-09
    Description: The primary circadian pacemaker, in the suprachiasmatic nucleus (SCN) of the mammalian brain, is photoentrained by light signals from the eyes through the retinohypothalamic tract. Retinal rod and cone cells are not required for photoentrainment. Recent evidence suggests that the entraining photoreceptors are retinal ganglion cells (RGCs) that project to the SCN. The visual pigment for this photoreceptor may be melanopsin, an opsin-like protein whose coding messenger RNA is found in a subset of mammalian RGCs. By cloning rat melanopsin and generating specific antibodies, we show that melanopsin is present in cell bodies, dendrites, and proximal axonal segments of a subset of rat RGCs. In mice heterozygous for tau-lacZ targeted to the melanopsin gene locus, beta-galactosidase-positive RGC axons projected to the SCN and other brain nuclei involved in circadian photoentrainment or the pupillary light reflex. Rat RGCs that exhibited intrinsic photosensitivity invariably expressed melanopsin. Hence, melanopsin is most likely the visual pigment of phototransducing RGCs that set the circadian clock and initiate other non-image-forming visual functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885915/" 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/PMC2885915/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hattar, S -- Liao, H W -- Takao, M -- Berson, D M -- Yau, K W -- R37 EY006837/EY/NEI NIH HHS/ -- R37 EY006837-13/EY/NEI NIH HHS/ -- R37 EY006837-14/EY/NEI NIH HHS/ -- R37 EY006837-15/EY/NEI NIH HHS/ -- R37 EY006837-15S1/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1065-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834834" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/chemistry ; *Biological Clocks ; Brain/*cytology ; Cell Membrane/chemistry ; *Circadian Rhythm ; Cloning, Molecular ; Dendrites/chemistry ; Fluorescent Antibody Technique ; Lac Operon ; *Light ; Mice ; Microscopy, Confocal ; Molecular Sequence Data ; Optic Nerve/cytology ; Rats ; Retinal Ganglion Cells/*chemistry/physiology ; Rod Opsins/*analysis/chemistry/genetics/*physiology ; Suprachiasmatic Nucleus/cytology ; Visual Pathways/cytology ; beta-Galactosidase/analysis
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  • 67
    Publication Date: 2002-01-12
    Description: Members of a multigene family in the rodent malaria parasite Plasmodium yoelii yoelii code for 235-kilodalton proteins (Py235) that are located in the merozoite apical complex, are implicated in virulence, and may determine red blood cell specificity. We show that distinct subsets of py235 genes are expressed in sporozoites and hepatic and erythrocytic stages. Antibodies to Py235 inhibited sporozoite invasion of hepatocytes. The switch in expression profile occurred immediately after transition from one stage to another. The results suggest that this differential expression is driven by strong biological requirements and provide evidence that hepatic and erythrocytic merozoites differ.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preiser, P R -- Khan, S -- Costa, F T M -- Jarra, W -- Belnoue, E -- Ogun, S -- Holder, A A -- Voza, T -- Landau, I -- Snounou, G -- Renia, L -- MC_U117532067/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):342-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Parasitology, National Institute for Medical Research, The Ridgeway, London, NW7 1AA, UK. ppreise@nimr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786645" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anopheles/parasitology ; Cells, Cultured ; Erythrocytes/parasitology ; Fluorescent Antibody Technique ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; *Genes, Protozoan ; Hepatocytes/parasitology ; Life Cycle Stages ; Malaria/parasitology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; *Multigene Family ; Plasmodium yoelii/*genetics/*growth & development/metabolism ; Protozoan Proteins/chemistry/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Salivary Glands/parasitology ; *Transcription, Genetic
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  • 68
    Publication Date: 2002-10-05
    Description: In tropical Africa, Anopheles funestus is one of the three most important malaria vectors. We physically mapped 157 A. funestus complementary DNAs (cDNAs) to the polytene chromosomes of this species. Sequences of the cDNAs were mapped in silico to the A. gambiae genome as part of a comparative genomic study of synteny, gene order, and sequence conservation between A. funestus and A. gambiae. These species are in the same subgenus and diverged about as recently as humans and chimpanzees. Despite nearly perfect preservation of synteny, we found substantial shuffling of gene order along corresponding chromosome arms. Since the divergence of these species, at least 70 chromosomal inversions have been fixed, the highest rate of rearrangement of any eukaryote studied to date. The high incidence of paracentric inversions and limited colinearity suggests that locating genes in one anopheline species based on gene order in another may be limited to closely related taxa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharakhov, Igor V -- Serazin, Andrew C -- Grushko, Olga G -- Dana, Ali -- Lobo, Neil -- Hillenmeyer, Maureen E -- Westerman, Richard -- Romero-Severson, Jeanne -- Costantini, Carlo -- Sagnon, N'Fale -- Collins, Frank H -- Besansky, Nora J -- AI48842/AI/NIAID NIH HHS/ -- U01 AI48846/AI/NIAID NIH HHS/ -- U01 AI50687/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):182-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Tropical Disease Research and Training, University of Notre Dame, Notre Dame, IN 46556-0369, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles/classification/*genetics ; *Chromosome Inversion ; Chromosomes/genetics ; Conserved Sequence ; DNA, Complementary ; Evolution, Molecular ; Expressed Sequence Tags ; *Gene Order ; Gene Rearrangement ; *Genes, Insect ; Genetic Linkage ; In Situ Hybridization, Fluorescence ; Molecular Sequence Data ; Mutation ; Physical Chromosome Mapping ; Species Specificity ; Synteny
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  • 69
    Publication Date: 2002-10-19
    Description: Changes in prion protein (PrP) folding are associated with fatal neurodegenerative disorders, but the neurotoxic species is unknown. Like other proteins that traffic through the endoplasmic reticulum, misfolded PrP is retrograde transported to the cytosol for degradation by proteasomes. Accumulation of even small amounts of cytosolic PrP was strongly neurotoxic in cultured cells and transgenic mice. Mice developed normally but acquired severe ataxia, with cerebellar degeneration and gliosis. This establishes a mechanism for converting wild-type PrP to a highly neurotoxic species that is distinct from the self-propagating PrP(Sc) isoform and suggests a potential common framework for seemingly diverse PrP neurodegenerative disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ma, Jiyan -- Wollmann, Robert -- Lindquist, Susan -- GM25874/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1781-5. Epub 2002 Oct 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Pathology, University of Chicago, 5841 South Maryland Avenue, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386337" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Brain/metabolism/pathology ; Cell Survival ; Cysteine Endopeptidases ; Cysteine Proteinase Inhibitors/pharmacology ; Cytosol/*metabolism ; Glycosylation ; In Situ Nick-End Labeling ; Leupeptins/pharmacology ; Membrane Proteins/genetics/metabolism ; Mice ; Mice, Transgenic ; Multienzyme Complexes/antagonists & inhibitors ; *Nerve Degeneration ; Neurons/*physiology ; PrPSc Proteins/chemistry/metabolism ; Presenilin-1 ; Prion Diseases/*metabolism/pathology ; Prions/*chemistry/genetics/*metabolism ; Promoter Regions, Genetic ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Transport ; Transfection ; Tumor Cells, Cultured
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  • 70
    Publication Date: 2002-07-27
    Description: Bphs controls Bordetella pertussis toxin (PTX)-induced vasoactive amine sensitization elicited by histamine (VAASH) and has an established role in autoimmunity. We report that congenic mapping links Bphs to the histamine H1 receptor gene (Hrh1/H1R) and that H1R differs at three amino acid residues in VAASH-susceptible and -resistant mice. Hrh1-/- mice are protected from VAASH, which can be restored by genetic complementation with a susceptible Bphs/Hrh1 allele, and experimental allergic encephalomyelitis and autoimmune orchitis due to immune deviation. Thus, natural alleles of Hrh1 control both the autoimmune T cell and vascular responses regulated by histamine after PTX sensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ma, Runlin Z -- Gao, Jianfeng -- Meeker, Nathan D -- Fillmore, Parley D -- Tung, Kenneth S K -- Watanabe, Takeshi -- Zachary, James F -- Offner, Halina -- Blankenhorn, Elizabeth P -- Teuscher, Cory -- AI41236/AI/NIAID NIH HHS/ -- AI41747/AI/NIAID NIH HHS/ -- AI42376/AI/NIAID NIH HHS/ -- AI4515/AI/NIAID NIH HHS/ -- AR45222/AR/NIAMS NIH HHS/ -- NS23444/NS/NINDS NIH HHS/ -- NS36526/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):620-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory Animal Center, Institute of Genetics, Chinese Academy of Sciences, Beijing, China 100101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142541" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Autoimmune Diseases/etiology/*genetics/immunology ; Chromosome Mapping ; Cloning, Molecular ; Cytokines/biosynthesis ; Disease Susceptibility ; Encephalomyelitis, Autoimmune, Experimental/etiology/genetics/immunology ; Genetic Complementation Test ; Genetic Predisposition to Disease ; Histamine/pharmacology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Inbred Strains ; Molecular Sequence Data ; Pertussis Toxin ; Polymorphism, Single Nucleotide ; Receptors, Histamine H1/chemistry/*genetics ; Second Messenger Systems ; T-Lymphocytes/immunology ; Virulence Factors, Bordetella/toxicity
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-09-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Barry E -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1654-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉John Innes Centre, Colney, Norwich NR4 7UH, UK. barry.smith@bbsrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215632" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Molybdoferredoxin/chemistry ; Nitrogen/chemistry ; Nitrogen Fixation ; Nitrogenase/biosynthesis/*chemistry/metabolism ; Protein Conformation
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  • 72
    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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  • 73
    Publication Date: 2002-10-05
    Description: We used bioinformatic approaches to identify a total of 276 G protein-coupled receptors (GPCRs) from the Anopheles gambiae genome. These include GPCRs that are likely to play roles in pathways affecting almost every aspect of the mosquito's life cycle. Seventy-nine candidate odorant receptors were characterized for tissue expression and, along with 76 putative gustatory receptors, for their molecular evolution relative to Drosophila melanogaster. Examples of lineage-specific gene expansions were observed as well as a single instance of unusually high sequence conservation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, Catherine A -- Fox, A Nicole -- Pitts, R Jason -- Kent, Lauren B -- Tan, Perciliz L -- Chrystal, Mathew A -- Cravchik, Anibal -- Collins, Frank H -- Robertson, Hugh M -- Zwiebel, Laurence J -- F31 DC05265-01A1/DC/NIDCD NIH HHS/ -- R01 DC004692/DC/NIDCD NIH HHS/ -- R01 DC04692-01/DC/NIDCD NIH HHS/ -- U01AI48846/AI/NIAID NIH HHS/ -- U01AI50687/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):176-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Notre Dame, Notre Dame, IN 46556, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364795" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Anopheles/chemistry/*genetics/metabolism ; Computational Biology ; Conserved Sequence ; Drosophila Proteins/chemistry/genetics/metabolism ; Drosophila melanogaster/chemistry/genetics/metabolism ; Evolution, Molecular ; GTP-Binding Proteins/*metabolism ; Gene Amplification ; Gene Expression ; *Genes, Insect ; Genome ; Insect Proteins/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Multigene Family ; Phylogeny ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; Receptors, Odorant/chemistry/*genetics/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction
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  • 74
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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〉Bezanilla, Francisco -- Perozo, Eduardo -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1562-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, Los Angeles, CA 90095, USA. fbezanil@ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446894" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/physiology ; Cell Membrane/chemistry/physiology ; Crystallization ; Crystallography, X-Ray ; Electric Conductivity ; Escherichia coli/*chemistry/physiology ; Escherichia coli Proteins/*chemistry/*physiology ; Ion Channel Gating ; Ion Channels/*chemistry/*physiology ; *Mechanotransduction, Cellular ; Membrane Potentials ; Models, Molecular ; Osmolar Concentration ; Potassium Channels/chemistry/physiology ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary
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  • 75
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Jean -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2348-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923504" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Aging ; *Cell Division ; DNA/chemistry/metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/physiology ; Humans ; Models, Molecular ; Neoplasms/etiology ; Protein Conformation ; Telomerase/chemistry/genetics/*metabolism ; Telomere/chemistry/*physiology ; Tetrahymena/physiology/ultrastructure
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  • 76
    Publication Date: 2002-06-18
    Description: Activation-induced cytidine deaminase (AID), a putative RNA-editing enzyme, is indispensable for somatic hypermutation (SHM), class switch recombination, and gene conversion of immunoglobulin genes, which indicates a common molecular mechanism for these phenomena. Here we show that ectopic expression of AID alone can induce hypermutation in an artificial GFP substrate in NIH 3T3 murine fibroblast cells. The frequency of mutations was closely correlated with the level of transcription of the target gene, and the distribution of mutations in NIH 3T3 cells was similar to those of SHM in B lymphocytes. These results indicate that AID is sufficient for the generation of SHM in an actively transcribed gene in fibroblasts, as well as B cells, and that any of the required cofactors must be present in these fibroblasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshikawa, Kiyotsugu -- Okazaki, Il-Mi -- Eto, Tomonori -- Kinoshita, Kazuo -- Muramatsu, Masamichi -- Nagaoka, Hitoshi -- Honjo, Tasuku -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2033-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Chemistry and Molecular Biology, Graduate School of Medicine, Kyoto University, Yoshida Konoe-cho, Sakyo-ku, Kyoto, 606-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065838" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; B-Lymphocytes/physiology ; Base Sequence ; Cytidine Deaminase/genetics/*metabolism ; DNA/chemistry/genetics ; Genes, Reporter ; Green Fluorescent Proteins ; Luminescent Proteins/genetics/metabolism ; Mice ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Conformation ; Point Mutation ; Recombinant Proteins/metabolism ; Somatic Hypermutation, Immunoglobulin ; Transcription, Genetic ; Transfection
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  • 77
    Publication Date: 2002-04-06
    Description: We have produced a draft sequence of the rice genome for the most widely cultivated subspecies in China, Oryza sativa L. ssp. indica, by whole-genome shotgun sequencing. The genome was 466 megabases in size, with an estimated 46,022 to 55,615 genes. Functional coverage in the assembled sequences was 92.0%. About 42.2% of the genome was in exact 20-nucleotide oligomer repeats, and most of the transposons were in the intergenic regions between genes. Although 80.6% of predicted Arabidopsis thaliana genes had a homolog in rice, only 49.4% of predicted rice genes had a homolog in A. thaliana. The large proportion of rice genes with no recognizable homologs is due to a gradient in the GC content of rice coding sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Jun -- Hu, Songnian -- Wang, Jun -- Wong, Gane Ka-Shu -- Li, Songgang -- Liu, Bin -- Deng, Yajun -- Dai, Li -- Zhou, Yan -- Zhang, Xiuqing -- Cao, Mengliang -- Liu, Jing -- Sun, Jiandong -- Tang, Jiabin -- Chen, Yanjiong -- Huang, Xiaobing -- Lin, Wei -- Ye, Chen -- Tong, Wei -- Cong, Lijuan -- Geng, Jianing -- Han, Yujun -- Li, Lin -- Li, Wei -- Hu, Guangqiang -- Huang, Xiangang -- Li, Wenjie -- Li, Jian -- Liu, Zhanwei -- Li, Long -- Liu, Jianping -- Qi, Qiuhui -- Liu, Jinsong -- Li, Li -- Li, Tao -- Wang, Xuegang -- Lu, Hong -- Wu, Tingting -- Zhu, Miao -- Ni, Peixiang -- Han, Hua -- Dong, Wei -- Ren, Xiaoyu -- Feng, Xiaoli -- Cui, Peng -- Li, Xianran -- Wang, Hao -- Xu, Xin -- Zhai, Wenxue -- Xu, Zhao -- Zhang, Jinsong -- He, Sijie -- Zhang, Jianguo -- Xu, Jichen -- Zhang, Kunlin -- Zheng, Xianwu -- Dong, Jianhai -- Zeng, Wanyong -- Tao, Lin -- Ye, Jia -- Tan, Jun -- Ren, Xide -- Chen, Xuewei -- He, Jun -- Liu, Daofeng -- Tian, Wei -- Tian, Chaoguang -- Xia, Hongai -- Bao, Qiyu -- Li, Gang -- Gao, Hui -- Cao, Ting -- Wang, Juan -- Zhao, Wenming -- Li, Ping -- Chen, Wei -- Wang, Xudong -- Zhang, Yong -- Hu, Jianfei -- Wang, Jing -- Liu, Song -- Yang, Jian -- Zhang, Guangyu -- Xiong, Yuqing -- Li, Zhijie -- Mao, Long -- Zhou, Chengshu -- Zhu, Zhen -- Chen, Runsheng -- Hao, Bailin -- Zheng, Weimou -- Chen, Shouyi -- Guo, Wei -- Li, Guojie -- Liu, Siqi -- Tao, Ming -- Wang, Jian -- Zhu, Lihuang -- Yuan, Longping -- Yang, Huanming -- 1 RO1 ES09909/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):79-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beijing Genomics Institute/Center of Genomics and Bioinformatics, Chinese Academy of Sciences, Beijing 101300, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11935017" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics ; Base Composition ; Computational Biology ; Contig Mapping ; DNA Transposable Elements ; DNA, Intergenic ; DNA, Plant/chemistry/genetics ; Databases, Nucleic Acid ; Exons ; Gene Duplication ; Genes, Plant ; *Genome, Plant ; Genomics ; Introns ; Molecular Sequence Data ; Oryza/*genetics ; Plant Proteins/chemistry/genetics ; Polymorphism, Genetic ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Software ; Species Specificity ; Synteny
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  • 78
    Publication Date: 2002-04-20
    Description: Aquaporins are transmembrane channels found in cell membranes of all life forms. We examine their apparently paradoxical property, facilitation of efficient permeation of water while excluding protons, which is of critical importance to preserving the electrochemical potential across the cell membrane. We have determined the structure of the Escherichia coli aquaglyceroporin GlpF with bound water, in native (2.7 angstroms) and in W48F/F200T mutant (2.1 angstroms) forms, and carried out 12-nanosecond molecular dynamics simulations that define the spatial and temporal probability distribution and orientation of a single file of seven to nine water molecules inside the channel. Two conserved asparagines force a central water molecule to serve strictly as a hydrogen bond donor to its neighboring water molecules. Assisted by the electrostatic potential generated by two half-membrane spanning loops, this dictates opposite orientations of water molecules in the two halves of the channel, and thus prevents the formation of a "proton wire," while permitting rapid water diffusion. Both simulations and observations revealed a more regular distribution of channel water and an increased water permeability for the W48F/F200T mutant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tajkhorshid, Emad -- Nollert, Peter -- Jensen, Morten O -- Miercke, Larry J W -- O'Connell, Joseph -- Stroud, Robert M -- Schulten, Klaus -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):525-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theoretical Biophysics Group, Beckman Institute, University of Illinois at Urbana-Champaign, 405 North Mathews, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964478" target="_blank"〉PubMed〈/a〉
    Keywords: Aquaporins/*chemistry/genetics/metabolism ; Asparagine/chemistry ; Chemistry, Physical ; Computer Simulation ; Crystallography, X-Ray ; Diffusion ; Electrochemistry ; Escherichia coli ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Glycerol/metabolism ; Hydrogen Bonding ; Models, Molecular ; Mutation ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Secondary ; Protons ; Static Electricity ; Water/chemistry/*metabolism
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  • 79
    Publication Date: 2002-08-17
    Description: The 26S proteasome mediates degradation of ubiquitin-conjugated proteins. Although ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at the proteasome and its relation to substrate degradation remain unknown. The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated metalloisopeptidase (JAMM) motif-EX(n)HXHX(10)D. Mutation of the predicted active-site histidines to alanine (rpn11AXA) was lethal and stabilized ubiquitin pathway substrates in yeast. Rpn11(AXA) mutant proteasomes assembled normally but failed to either deubiquitinate or degrade ubiquitinated Sic1 in vitro. Our findings reveal an unexpected coupling between substrate deubiquitination and degradation and suggest a unifying rationale for the presence of the lid in eukaryotic proteasomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, Rati -- Aravind, L -- Oania, Robert -- McDonald, W Hayes -- Yates, John R 3rd -- Koonin, Eugene V -- Deshaies, Raymond J -- RR11823-05-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):611-5. Epub 2002 Aug 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and 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/12183636" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Carbon-Nitrogen Lyases/chemistry/*metabolism ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cysteine Endopeptidases/metabolism ; DNA-Binding Proteins/chemistry ; Endopeptidases/chemistry/*metabolism ; Fungal Proteins/*metabolism ; Metalloendopeptidases/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/metabolism ; Mutation ; Oligopeptides/pharmacology ; Peptide Hydrolases/*metabolism ; Proteasome Endopeptidase Complex ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Transcription Factors/chemistry ; Ubiquitins/*metabolism ; Yeasts/metabolism ; Zinc/metabolism
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  • 80
    Publication Date: 2002-12-10
    Description: The Frizzled-2 receptor (Rfz2) from rat binds Wnt proteins and can signal by activating calcium release from intracellular stores. We show that wild-type Rfz2 and a chimeric receptor consisting of the extracellular and transmembrane portions of the beta2-adrenergic receptor with cytoplasmic domains of Rfz2 also signaled through modulation of cyclic guanosine 3',5'-monophosphate (cGMP). Activation of either receptor led to a decline in the intracellular concentration of cGMP, a process that was inhibited in cells treated with pertussis toxin, reduced by suppression of the expression of the heterotrimeric GTP-binding protein (G protein) transducin, and suppressed through inhibition of cGMP-specific phosphodiesterase (PDE) activity. Moreover, PDE inhibitors blocked Rfz2-induced calcium transients in zebrafish embryos. Thus, Frizzled-2 appears to couple to PDEs and calcium transients through G proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahumada, Adriana -- Slusarski, Diane C -- Liu, Xunxian -- Moon, Randall T -- Malbon, Craig C -- Wang, Hsien-yu -- T32-DK07521/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):2006-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Diabetes and Metabolic Diseases Research Center, University Medical Center, SUNY-Stony Brook, Stony Brook, NY 11794-8651, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471263" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Calcium/metabolism ; Cricetinae ; Culture Media, Conditioned ; Cyclic GMP/*metabolism ; Embryo, Nonmammalian/metabolism ; Frizzled Receptors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Molecular Sequence Data ; Pertussis Toxin/pharmacology ; Phosphodiesterase Inhibitors/pharmacology ; Phosphoric Diester Hydrolases/*metabolism ; Rats ; Receptors, Adrenergic, beta-2/chemistry/metabolism ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; *Signal Transduction ; Transducin/genetics/metabolism ; Transfection ; Tumor Cells, Cultured ; Zebrafish
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  • 81
    Publication Date: 2002-08-24
    Description: The dendritic morphology of neurons determines the number and type of inputs they receive. In the Drosophila peripheral nervous system (PNS), the external sensory (ES) neurons have a single nonbranched dendrite, whereas the lineally related multidendritic (MD) neurons have extensively branched dendritic arbors. We report that hamlet is a binary genetic switch between these contrasting morphological types. In hamlet mutants, ES neurons are converted to an MD fate, whereas ectopic hamlet expression in MD precursors results in transformation of MD neurons into ES neurons. Moreover, hamlet expression induced in MD neurons undergoing dendrite outgrowth drastically reduces arbor branching.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, Adrian W -- Jan, Lily Yeh -- Jan, Yuh Nung -- R01NS40929/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Physiology, 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/12193790" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Differentiation ; Cell Lineage ; Clone Cells ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/*genetics/*physiology ; Dendrites/*ultrastructure ; Drosophila/*embryology/genetics/physiology ; Drosophila Proteins/chemistry/*genetics/*physiology ; Gene Expression ; Genetic Complementation Test ; Mitosis ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Neurons/physiology/*ultrastructure ; Neurons, Afferent/*ultrastructure ; Nuclear Proteins/chemistry/*genetics/*physiology ; Peripheral Nervous System/cytology/embryology ; RNA, Double-Stranded/genetics ; Sense Organs/embryology ; Transcription Factors/chemistry/*genetics/*physiology
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  • 82
    Publication Date: 2002-12-21
    Description: ACT is a LIM-only protein expressed exclusively in round spermatids, where it cooperates with transcriptional activator CREM in regulating various postmeiotic genes. Targeted inactivation of CREM leads to a complete block of mouse spermiogenesis. We sought to identify the regulatory steps controlling the functional interplay between CREM and ACT. We found that ACT selectively associates with KIF17b, a kinesin highly expressed in male germ cells. The ACT-KIF17b interaction is restricted to specific stages of spermatogenesis and directly determines the intracellular localization of ACT. Sensitivity to leptomycin B indicates that KIF17b can be actively exported from the nucleus through the Crm1 receptor. Thus, a kinesin directly controls the activity of a transcriptional coactivator by a tight regulation of its intracellular localization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macho, Betina -- Brancorsini, Stefano -- Fimia, Gian Maria -- Setou, Mitsutoshi -- Hirokawa, Nobutaka -- Sassone-Corsi, Paolo -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2388-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire, B. P. 10142, 67404 Illkirch, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493914" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; COS Cells ; Cell Nucleus/metabolism ; Cyclic AMP Response Element Modulator ; Cytoplasm/metabolism ; DNA-Binding Proteins/metabolism ; Fatty Acids, Unsaturated/pharmacology ; Gene Expression Regulation, Developmental ; Karyopherins/metabolism ; Kinesin/chemistry/genetics/*metabolism ; LIM Domain Proteins ; Male ; Mice ; Molecular Motor Proteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Promoter Regions, Genetic ; Protein Isoforms/chemistry/genetics/metabolism ; *Receptors, Cytoplasmic and Nuclear ; *Repressor Proteins ; Spermatids/*metabolism ; *Spermatogenesis ; Testis/metabolism ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Transfection
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  • 83
    Publication Date: 2002-05-11
    Description: Comparison of the whole-genome sequence of Bacillus anthracis isolated from a victim of a recent bioterrorist anthrax attack with a reference reveals 60 new markers that include single nucleotide polymorphisms (SNPs), inserted or deleted sequences, and tandem repeats. Genome comparison detected four high-quality SNPs between the two sequenced B. anthracis chromosomes and seven differences among different preparations of the reference genome. These markers have been tested on a collection of anthrax isolates and were found to divide these samples into distinct families. These results demonstrate that genome-based analysis of microbial pathogens will provide a powerful new tool for investigation of infectious disease outbreaks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Read, Timothy D -- Salzberg, Steven L -- Pop, Mihai -- Shumway, Martin -- Umayam, Lowell -- Jiang, Lingxia -- Holtzapple, Erik -- Busch, Joseph D -- Smith, Kimothy L -- Schupp, James M -- Solomon, Daniel -- Keim, Paul -- Fraser, Claire M -- R01-LM06845/LM/NLM NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2028-33. Epub 2002 May 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Institute for Genomic Research, 9712 Medical Center Drive, Rockville, MD 20850, USA., Department of Biological Sciences, Northern Arizona University, Flagstaff, AZ 86011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004073" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthrax/microbiology ; Bacillus anthracis/classification/*genetics/isolation & ; purification/pathogenicity ; Bacterial Typing Techniques ; Base Sequence ; Bioterrorism ; Chromosome Inversion ; Computational Biology ; Disease Outbreaks ; Genetic Markers ; *Genetic Variation ; *Genome, Bacterial ; Genomics ; Humans ; Minisatellite Repeats ; Molecular Sequence Data ; Mutation ; Phenotype ; Phylogeny ; Plasmids ; *Polymorphism, Single Nucleotide ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA ; Sequence Deletion ; Species Specificity ; Transposases/genetics ; Virulence/genetics
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  • 84
    Publication Date: 2002-01-05
    Description: Tumstatin is a 28-kilodalton fragment of type IV collagen that displays both anti-angiogenic and proapoptotic activity. Here we show that tumstatin functions as an endothelial cell-specific inhibitor of protein synthesis. Through a requisite interaction with alphaVbeta3 integrin, tumstatin inhibits activation of focal adhesion kinase (FAK), phosphatidylinositol 3-kinase (PI3-kinase), protein kinase B (PKB/Akt), and mammalian target of rapamycin (mTOR), and it prevents the dissociation of eukaryotic initiation factor 4E protein (eIF4E) from 4E-binding protein 1. These results establish a role for integrins in mediating cell-specific inhibition of cap-dependent protein synthesis and suggest a potential mechanism for tumstatin's selective effects on endothelial cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maeshima, Yohei -- Sudhakar, Akulapalli -- Lively, Julie C -- Ueki, Kohjiro -- Kharbanda, Surender -- Kahn, C Ronald -- Sonenberg, Nahum -- Hynes, Richard O -- Kalluri, Raghu -- DK-51711/DK/NIDDK NIH HHS/ -- DK-55001/DK/NIDDK NIH HHS/ -- P01-HL66105/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Matrix Biology, Department of Medicine and the Cancer Center, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778052" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Autoantigens/chemistry/metabolism/*pharmacology ; Carrier Proteins/metabolism ; Cattle ; Cells, Cultured ; Collagen Type IV/chemistry/metabolism/*pharmacology ; Endothelium, Vascular/*cytology/drug effects/*metabolism ; Enzyme Activation/drug effects ; Eukaryotic Initiation Factor-4E ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Humans ; Mice ; Molecular Sequence Data ; Peptide Fragments/pharmacology ; Peptide Initiation Factors/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; *Protein Biosynthesis/drug effects ; Protein Kinase Inhibitors ; Protein Kinases/metabolism ; Protein Synthesis Inhibitors/*pharmacology ; *Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; RNA Caps/metabolism ; RNA, Messenger/genetics/metabolism ; Receptors, Vitronectin/metabolism ; Signal Transduction ; TOR Serine-Threonine Kinases ; Tumor Cells, Cultured
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  • 85
    Publication Date: 2002-11-26
    Description: Apoptosis-inducing factor (AIF), a mitochondrial oxidoreductase, is released into the cytoplasm to induce cell death in response to apoptotic signals. However, the mechanisms underlying this process have not been resolved. We report that inactivation of the Caenorhabditis elegans AIF homolog wah-1 by RNA interference delayed the normal progression of apoptosis and caused a defect in apoptotic DNA degradation. WAH-1 localized in C. elegans mitochondria and was released into the cytosol and nucleus by the BH3-domain protein EGL-1 in a caspase (CED-3)-dependent manner. In addition, WAH-1 associated and cooperated with the mitochondrial endonuclease CPS-6/endonuclease G (EndoG) to promote DNA degradation and apoptosis. Thus, AIF and EndoG define a single, mitochondria-initiated apoptotic DNA degradation pathway that is conserved between C. elegans and mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Xiaochen -- Yang, Chonglin -- Chai, Jijie -- Shi, Yigong -- Xue, Ding -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1587-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446902" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; Apoptosis Inducing Factor ; Caenorhabditis elegans/cytology/embryology/genetics/*physiology ; Caenorhabditis elegans Proteins/chemistry/genetics/*physiology ; Caspases/metabolism ; Cell Nucleus/metabolism ; Cell Survival ; Cloning, Molecular ; Cytosol/metabolism ; *DNA Fragmentation ; DNA, Helminth/*metabolism ; Endodeoxyribonucleases/metabolism ; Flavoproteins/physiology ; Humans ; In Situ Nick-End Labeling ; Membrane Proteins/physiology ; Mitochondria/metabolism ; Mitochondrial Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Mutation ; Phenotype ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/metabolism ; Sequence Alignment
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  • 86
    Publication Date: 2002-09-21
    Description: Somatically mutated high-affinity autoantibodies are a hallmark of some autoimmune diseases, including systemic lupus erythematosus. It has long been presumed that germinal centers (GCs) are critical in autoantibody production, because they are the only sites currently believed to sustain a high rate of somatic hypermutation. Contrary to this idea, we found that splenic autoreactive B cells in autoimmune MRL.Fas(lpr) mice proliferated and underwent active somatic hypermutation at the T zone-red pulp border rather than in GCs. Our results implicate this region as an important site for hypermutation and the loss of B cell self-tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉William, Jacqueline -- Euler, Chad -- Christensen, Sean -- Shlomchik, Mark J -- P01-A36529/PHS HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2066-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Laboratory Medicine, Section of Immunobiology, Yale University School of Medicine, Box 208035, New Haven, CT 06520-8035, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242446" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Anti-Idiotypic/immunology ; Autoantibodies/*biosynthesis ; Autoimmune Diseases/immunology ; *Autoimmunity ; B-Lymphocytes/*immunology ; Base Sequence ; Dendritic Cells, Follicular/immunology ; Genes, Immunoglobulin ; Germinal Center/*immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mice, Inbred MRL lpr ; Mice, Transgenic ; Molecular Sequence Data ; Rheumatoid Factor/*biosynthesis ; Self Tolerance ; *Somatic Hypermutation, Immunoglobulin ; Spleen/*immunology ; T-Lymphocytes/immunology
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  • 87
    Publication Date: 2002-05-11
    Description: Light-powered molecular machines are conjectured to be essential constituents of future nanoscale devices. As a model for such systems, we have synthesized a polymer of bistable photosensitive azobenzenes. Individual polymers were investigated by single-molecule force spectroscopy in combination with optical excitation in total internal reflection. We were able to optically lengthen and contract individual polymers by switching the azo groups between their trans and cis configurations. The polymer was found to contract against an external force acting along the polymer backbone, thus delivering mechanical work. As a proof of principle, the polymer was operated in a periodic mode, demonstrating for the first time optomechanical energy conversion in a single-molecule device.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hugel, Thorsten -- Holland, Nolan B -- Cattani, Anna -- Moroder, Luis -- Seitz, Markus -- Gaub, Hermann E -- New York, N.Y. -- Science. 2002 May 10;296(5570):1103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl fur Angewandte Physik & Center for Nanoscience, Ludwig-Maximilians Universitat, Amalienstrasse 54, 80799 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004125" target="_blank"〉PubMed〈/a〉
    Keywords: Azo Compounds/*chemistry ; Chemistry, Physical ; Dimethyl Sulfoxide ; *Light ; Mechanics ; Microscopy, Atomic Force ; Molecular Conformation ; Nanotechnology ; Optics and Photonics ; Peptides/*chemistry ; Photochemistry ; Physicochemical Phenomena ; Polymers ; Protein Conformation ; Software ; Spectrum Analysis ; Temperature
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  • 88
    Publication Date: 2002-09-21
    Description: The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunt, John F -- Weinkauf, Sevil -- Henry, Lisa -- Fak, John J -- McNicholas, Paul -- Oliver, Donald B -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2018-26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, 702A Fairchild Center, MC2434, Columbia University, New York, NY 10027, USA. hunt@sid.bio.columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242434" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/chemistry/*metabolism ; Adenosine Triphosphatases/*chemistry/*metabolism ; Adenosine Triphosphate/chemistry/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacillus subtilis/*enzymology ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Helicases/chemistry ; DNA, Bacterial/chemistry/metabolism ; DNA, Single-Stranded/chemistry/metabolism ; Dimerization ; Escherichia coli ; Escherichia coli Proteins/*chemistry/*metabolism ; Eukaryotic Initiation Factor-4A ; Fluorescence Polarization ; Fourier Analysis ; Hydrogen Bonding ; Ligands ; Membrane Transport Proteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptide Initiation Factors/chemistry ; Peptides/chemistry ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Precursors/metabolism ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Temperature
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  • 89
    Publication Date: 2002-05-25
    Description: Pyrrolysine is a lysine derivative encoded by the UAG codon in methylamine methyltransferase genes of Methanosarcina barkeri. Near a methyltransferase gene cluster is the pylT gene, which encodes an unusual transfer RNA (tRNA) with a CUA anticodon. The adjacent pylS gene encodes a class II aminoacyl-tRNA synthetase that charges the pylT-derived tRNA with lysine but is not closely related to known lysyl-tRNA synthetases. Homologs of pylS and pylT are found in a Gram-positive bacterium. Charging a tRNA(CUA) with lysine is a likely first step in translating UAG amber codons as pyrrolysine in certain methanogens. Our results indicate that pyrrolysine is the 22nd genetically encoded natural amino acid.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srinivasan, Gayathri -- James, Carey M -- Krzycki, Joseph A -- New York, N.Y. -- Science. 2002 May 24;296(5572):1459-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Ohio State University, Columbus, OH 43210, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029131" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/chemistry/*genetics/metabolism ; Anticodon ; Archaeal Proteins ; Base Sequence ; Catalytic Domain ; *Codon ; Codon, Terminator ; Kinetics ; Lysine/analogs & derivatives/chemistry/*genetics/metabolism ; Methanosarcina barkeri/chemistry/enzymology/*genetics ; Methyltransferases/genetics/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Biosynthesis ; RNA, Archaeal/chemistry/genetics/metabolism ; RNA, Transfer/chemistry/*genetics/metabolism ; Recombinant Proteins/metabolism ; Sequence Alignment
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  • 90
    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
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  • 91
    Publication Date: 2002-06-29
    Description: Phototaxis and photophobic responses of green algae are mediated by rhodopsins with microbial-type chromophores. We report a complementary DNA sequence in the green alga Chlamydomonas reinhardtii that encodes a microbial opsin-related protein, which we term Channelopsin-1. The hydrophobic core region of the protein shows homology to the light-activated proton pump bacteriorhodopsin. Expression of Channelopsin-1, or only the hydrophobic core, in Xenopus laevis oocytes in the presence of all-trans retinal produces a light-gated conductance that shows characteristics of a channel selectively permeable for protons. We suggest that Channelrhodopsins are involved in phototaxis of green algae.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nagel, Georg -- Ollig, Doris -- Fuhrmann, Markus -- Kateriya, Suneel -- Musti, Anna Maria -- Bamberg, Ernst -- Hegemann, Peter -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2395-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biophysik, Kennedyallee 70, 60596 Frankfurt am Main, Germany. nagel@mpibp-frankfurt.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089443" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriorhodopsins/chemistry/metabolism ; Butyric Acid/pharmacology ; Chlamydomonas reinhardtii/chemistry/genetics/*metabolism ; Electric Conductivity ; Hydrogen-Ion Concentration ; Ion Channel Gating ; Ion Channels/*chemistry/genetics/*metabolism ; Ion Transport ; *Light ; Membrane Potentials ; Molecular Sequence Data ; Oocytes ; Patch-Clamp Techniques ; *Protons ; RNA, Complementary ; Recombinant Proteins/metabolism ; Retinaldehyde/pharmacology ; Sequence Alignment ; Temperature ; Xenopus laevis
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  • 92
    Publication Date: 2002-12-14
    Description: The proteasome plays a central role in the degradation of regulatory and misfolded proteins. Current models suggest that substrates access the internal catalytic sites by processively threading their termini through the gated substrate channel. Here, we found that latent (closed) and activated (open) proteasomes degraded two natively disordered substrates at internal peptide bonds even when they lacked accessible termini, suggesting that these substrates themselves promoted gating of the proteasome. This endoproteolysis provides a molecular mechanism for regulated release of transcription factors from inactive precursors as well as a means of accessing internal folding defects of misfolded multidomain proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3516294/" 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/PMC3516294/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Chang-Wei -- Corboy, Michael J -- DeMartino, George N -- Thomas, Philip J -- DK46818/DK/NIDDK NIH HHS/ -- DK49835/DK/NIDDK NIH HHS/ -- R01 DK049835/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 17;299(5605):408-11. Epub 2002 Dec 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481023" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins/chemistry/*metabolism ; Cyclization ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Green Fluorescent Proteins ; Leupeptins/pharmacology ; Luminescent Proteins/chemistry/metabolism ; Multienzyme Complexes/*metabolism ; Nerve Tissue Proteins/chemistry/*metabolism ; Peptide Hydrolases/*metabolism ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Splicing ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Synucleins
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  • 93
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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〉Murzin, Alexey G -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):61-2. Epub 2002 May 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, UK. agm@mrc-lmb.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029066" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/enzymology ; Binding Sites ; Crystallography, X-Ray ; Deoxyuracil Nucleotides/metabolism ; Drug Design ; Enzyme Inhibitors ; Evolution, Molecular ; Flavin-Adenine Dinucleotide/metabolism ; Helicobacter pylori/*enzymology ; Humans ; Methyltransferases/chemistry/metabolism ; Models, Molecular ; Phylogeny ; Protein Conformation ; Protein Structure, Tertiary ; Protozoan Proteins/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Tetrahydrofolates/metabolism ; Thermotoga maritima/*enzymology ; Thymidine Monophosphate/*biosynthesis ; Thymidylate Synthase/antagonists & inhibitors/*chemistry/genetics/*metabolism
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  • 94
    Publication Date: 2002-03-16
    Description: An outbreak of paralytic poliomyelitis occurred in the Dominican Republic (13 confirmed cases) and Haiti (8 confirmed cases, including 2 fatal cases) during 2000-2001. All but one of the patients were either unvaccinated or incompletely vaccinated children, and cases occurred in communities with very low (7 to 40%) rates of coverage with oral poliovirus vaccine (OPV). The outbreak was associated with the circulation of a derivative of the type 1 OPV strain, probably originating from a single OPV dose given in 1998-1999. The vaccine-derived poliovirus associated with the outbreak had biological properties indistinguishable from those of wild poliovirus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kew, Olen -- Morris-Glasgow, Victoria -- Landaverde, Mauricio -- Burns, Cara -- Shaw, Jing -- Garib, Zacarias -- Andre, Jean -- Blackman, Elizabeth -- Freeman, C Jason -- Jorba, Jaume -- Sutter, Roland -- Tambini, Gina -- Venczel, Linda -- Pedreira, Cristina -- Laender, Fernando -- Shimizu, Hiroyuki -- Yoneyama, Tetsuo -- Miyamura, Tatsuo -- van Der Avoort, Harrie -- Oberste, M Steven -- Kilpatrick, David -- Cochi, Stephen -- Pallansch, Mark -- de Quadros, Ciro -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):356-9. Epub 2002 Mar 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention (CDC), 1600 Clifton Road, Atlanta, GA 30333, USA. okew@cdc.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896235" target="_blank"〉PubMed〈/a〉
    Keywords: 5' Untranslated Regions ; Adolescent ; Animals ; Capsid/genetics ; Capsid Proteins ; Child ; Child, Preschool ; *Disease Outbreaks ; Dominican Republic/epidemiology ; Female ; Genes, Viral ; Haiti/epidemiology ; Humans ; Immunization Programs ; Infant ; Male ; Mice ; Molecular Sequence Data ; Point Mutation ; Poliomyelitis/*epidemiology/prevention & control/transmission/*virology ; Poliovirus/classification/*genetics/isolation & purification/*pathogenicity ; Poliovirus Vaccine, Oral/*adverse effects ; Population Surveillance ; Recombination, Genetic ; Vaccination ; Virulence
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  • 95
    Publication Date: 2002-08-31
    Description: The Escherichia coli catabolite activator protein (CAP) activates transcription at P(lac), P(gal), and other promoters through interactions with the RNA polymerase alpha subunit carboxyl-terminal domain (alphaCTD). We determined the crystal structure of the CAP-alphaCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alphaCTD, and alphaCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and alphaCTD, and the interface between CAP and alphaCTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benoff, Brian -- Yang, Huanwang -- Lawson, Catherine L -- Parkinson, Gary -- Liu, Jinsong -- Blatter, Erich -- Ebright, Yon W -- Berman, Helen M -- Ebright, Richard H -- GM21589/GM/NIGMS NIH HHS/ -- GM41376/GM/NIGMS NIH HHS/ -- GM64375/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1562-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute and Department of Chemistry, Howard Hughes Medical Institute, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202833" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Cyclic AMP Receptor Protein/*chemistry/metabolism/physiology ; DNA/*chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism/physiology ; Macromolecular Substances ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; *Transcription, Genetic ; Transcriptional Activation
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  • 96
    Publication Date: 2002-08-24
    Description: Every year, approximately 450,000 individuals in the United States die suddenly of cardiac arrhythmia. We identified a variant of the cardiac sodium channel gene SCN5A that is associated with arrhythmia in African Americans (P = 0.000028) and linked with arrhythmia risk in an African-American family (P = 0.005). In transfected cells, the variant allele (Y1102) accelerated channel activation, increasing the likelihood of abnormal cardiac repolarization and arrhythmia. About 13.2% of African Americans carry the Y1102 allele. Because Y1102 has a subtle effect on risk, most carriers will never have an arrhythmia. However, Y1102 may be a useful molecular marker for the prediction of arrhythmia susceptibility in the context of additional acquired risk factors such as the use of certain medications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Splawski, Igor -- Timothy, Katherine W -- Tateyama, Michihiro -- Clancy, Colleen E -- Malhotra, Alka -- Beggs, Alan H -- Cappuccio, Francesco P -- Sagnella, Giuseppe A -- Kass, Robert S -- Keating, Mark T -- HL53773/HL/NHLBI NIH HHS/ -- P01 HL 67849/HL/NHLBI NIH HHS/ -- R01 HL 56810/HL/NHLBI NIH HHS/ -- R01 HL48074/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1333-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Harvard Medical School and Howard Hughes Medical Institute, Boston, MA 02115, USA. igor@enders.tch.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193783" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; African Continental Ancestry Group/*genetics ; Aged ; Alleles ; Amino Acid Sequence ; Arrhythmias, Cardiac/etiology/*genetics ; Case-Control Studies ; Cell Line ; Child ; Electrocardiography ; Female ; *Genetic Predisposition to Disease ; *Genetic Variation ; Humans ; Ion Channel Gating ; Long QT Syndrome/genetics ; Male ; Middle Aged ; Molecular Sequence Data ; NAV1.5 Voltage-Gated Sodium Channel ; Patch-Clamp Techniques ; Pedigree ; *Point Mutation ; Polymorphism, Single-Stranded Conformational ; Probability ; Risk Factors ; Sodium Channels/chemistry/*genetics/metabolism ; Syncope ; Transfection
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  • 97
    Publication Date: 2002-11-26
    Description: The origin of the domestic dog from wolves has been established, but the number of founding events, as well as where and when these occurred, is not known. To address these questions, we examined the mitochondrial DNA (mtDNA) sequence variation among 654 domestic dogs representing all major dog populations worldwide. Although our data indicate several maternal origins from wolf, 〉95% of all sequences belonged to three phylogenetic groups universally represented at similar frequencies, suggesting a common origin from a single gene pool for all dog populations. A larger genetic variation in East Asia than in other regions and the pattern of phylogeographic variation suggest an East Asian origin for the domestic dog, approximately 15,000 years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Savolainen, Peter -- Zhang, Ya-ping -- Luo, Jing -- Lundeberg, Joakim -- Leitner, Thomas -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1610-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology, Royal Institute of Technology (KTH), 10691 Stockholm, Sweden. savo@biotech.kth.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446907" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Domestic/anatomy & histology/classification/*genetics ; Archaeology ; Asia ; DNA, Mitochondrial/*genetics ; Dogs/anatomy & histology/classification/*genetics ; Female ; Gene Pool ; Genes ; *Genetic Variation ; Haplotypes ; Molecular Sequence Data ; Phylogeny ; Time ; Wolves/genetics
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  • 98
    Publication Date: 2002-11-26
    Description: The DJ-1 gene encodes a ubiquitous, highly conserved protein. Here, we show that DJ-1 mutations are associated with PARK7, a monogenic form of human parkinsonism. The function of the DJ-1 protein remains unknown, but evidence suggests its involvement in the oxidative stress response. Our findings indicate that loss of DJ-1 function leads to neurodegeneration. Elucidating the physiological role of DJ-1 protein may promote understanding of the mechanisms of brain neuronal maintenance and pathogenesis of Parkinson's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonifati, Vincenzo -- Rizzu, Patrizia -- van Baren, Marijke J -- Schaap, Onno -- Breedveld, Guido J -- Krieger, Elmar -- Dekker, Marieke C J -- Squitieri, Ferdinando -- Ibanez, Pablo -- Joosse, Marijke -- van Dongen, Jeroen W -- Vanacore, Nicola -- van Swieten, John C -- Brice, Alexis -- Meco, Giuseppe -- van Duijn, Cornelia M -- Oostra, Ben A -- Heutink, Peter -- New York, N.Y. -- Science. 2003 Jan 10;299(5604):256-9. Epub 2002 Nov 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetic-Epidemiologic Unit, Department of Clinical Genetics, Department of Epidemiology and Biostatistics, Erasmus Medical Center Rotterdam, Post Office Box 1738, 3000 DR Rotterdam, Netherlands. bonifati@kgen.fgg.eur.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446870" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Base Sequence ; Brain/metabolism ; COS Cells ; Cell Nucleus/metabolism ; Chromosomes, Human, Pair 1 ; Cloning, Molecular ; Cytoplasm/metabolism ; DNA, Complementary ; Exons ; Genes, Recessive ; Humans ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; *Mutation ; Oncogene Proteins/chemistry/*genetics/metabolism ; Oxidative Stress ; PC12 Cells ; Parkinsonian Disorders/*genetics/metabolism ; Pedigree ; Physical Chromosome Mapping ; Point Mutation ; Protein Structure, Secondary ; Rats ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Deletion ; Transfection
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  • 99
    Publication Date: 2002-11-02
    Description: Proliferation of legume nodule primordia is controlled by shoot-root signaling known as autoregulation of nodulation (AON). Mutants defective in AON show supernodulation and increased numbers of lateral roots. Here, we demonstrate that AON in soybean is controlled by the receptor-like protein kinase GmNARK (Glycine max nodule autoregulation receptor kinase), similar to Arabidopsis CLAVATA1 (CLV1). Whereas CLV1 functions in a protein complex controlling stem cell proliferation by short-distance signaling in shoot apices, GmNARK expression in the leaf has a major role in long-distance communication with nodule and lateral root primordia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Searle, Iain R -- Men, Artem E -- Laniya, Titeki S -- Buzas, Diana M -- Iturbe-Ormaetxe, Inaki -- Carroll, Bernard J -- Gresshoff, Peter M -- New York, N.Y. -- Science. 2003 Jan 3;299(5603):109-12. Epub 2002 Oct 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry and Molecular Biology, School of Molecular and Microbial Sciences, School of Land and Food Sciences, Botany, School of Life Sciences, The University of Queensland, Brisbane, St. Lucia, QLD 4072, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/enzymology/genetics ; Arabidopsis Proteins/chemistry/genetics/metabolism ; Biological Evolution ; Chromosomes, Artificial, Bacterial ; Chromosomes, Plant/genetics ; Cloning, Molecular ; Gene Duplication ; *Genes, Plant ; Meristem/cytology/enzymology ; Molecular Sequence Data ; Mutation ; Phenotype ; Phylogeny ; Physical Chromosome Mapping ; Plant Leaves/enzymology ; Plant Roots/enzymology/metabolism ; Plant Shoots/enzymology/metabolism ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Protein Kinases/chemistry/*genetics/*metabolism ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/metabolism ; *Signal Transduction ; Soybeans/*enzymology/*genetics/physiology ; Synteny
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 2002-10-05
    Description: The African malaria mosquito, Anopheles gambiae, is specialized for rapid completion of development and reproduction. A vertebrate blood meal is required for egg production, and multiple feedings subsequently allow transmission of malaria parasites, Plasmodium spp. Regulatory peptides from 35 genes annotated from the A. gambiae genome likely coordinate these and other physiological processes. Plasmodium parasites may affect actions of newly identified insulin-like peptides, which coordinate growth and reproduction of its vector, A. gambiae, as in Drosophila melanogaster, Caenorhabditis elegans, and mammals. This genomic information provides a basis to expand understanding of hematophagy and pathogen transmission in this mosquito.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riehle, Michael A -- Garczynski, Stephen F -- Crim, Joe W -- Hill, Catherine A -- Brown, Mark R -- AI33108/AI/NIAID NIH HHS/ -- R01 AI033108/AI/NIAID NIH HHS/ -- U01 AI48846/AI/NIAID NIH HHS/ -- U01 AI50687/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):172-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of Georgia, Athens, GA 30602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364794" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anopheles/chemistry/genetics/parasitology/*physiology ; Blood ; Computational Biology ; Cues ; Ecdysteroids/secretion ; Feeding Behavior ; Female ; Genes, Insect ; Homeostasis ; Insect Hormones/chemistry/genetics/*metabolism ; Insect Proteins/chemistry/genetics/*metabolism ; Insulin/metabolism ; Molecular Sequence Data ; Molting ; Neuropeptides/chemistry/genetics/*metabolism ; Peptides/chemistry/genetics/*metabolism ; Plasmodium/physiology ; Signal Transduction ; Water-Electrolyte Balance
    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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