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  • Female  (29)
  • Binding Sites  (24)
  • American Association for the Advancement of Science (AAAS)  (53)
  • Nature Publishing Group
  • Oxford University Press
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  • 1
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    GWAS of 126,559 individuals identifies genetic variants associated with educational attainment (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-06-01
    Description: A genome-wide association study (GWAS) of educational attainment was conducted in a discovery sample of 101,069 individuals and a replication sample of 25,490. Three independent single-nucleotide polymorphisms (SNPs) are genome-wide significant (rs9320913, rs11584700, rs4851266), and all three replicate. Estimated effects sizes are small (coefficient of determination R(2) approximately 0.02%), approximately 1 month of schooling per allele. A linear polygenic score from all measured SNPs accounts for approximately 2% of the variance in both educational attainment and cognitive function. Genes in the region of the loci have previously been associated with health, cognitive, and central nervous system phenotypes, and bioinformatics analyses suggest the involvement of the anterior caudate nucleus. These findings provide promising candidate SNPs for follow-up work, and our effect size estimates can anchor power analyses in social-science genetics.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3751588/" 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/PMC3751588/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rietveld, Cornelius A -- Medland, Sarah E -- Derringer, Jaime -- Yang, Jian -- Esko, Tonu -- Martin, Nicolas W -- Westra, Harm-Jan -- Shakhbazov, Konstantin -- Abdellaoui, Abdel -- Agrawal, Arpana -- Albrecht, Eva -- Alizadeh, Behrooz Z -- Amin, Najaf -- Barnard, John -- Baumeister, Sebastian E -- Benke, Kelly S -- Bielak, Lawrence F -- Boatman, Jeffrey A -- Boyle, Patricia A -- Davies, Gail -- de Leeuw, Christiaan -- Eklund, Niina -- Evans, Daniel S -- Ferhmann, Rudolf -- Fischer, Krista -- Gieger, Christian -- Gjessing, Hakon K -- Hagg, Sara -- Harris, Jennifer R -- Hayward, Caroline -- Holzapfel, Christina -- Ibrahim-Verbaas, Carla A -- Ingelsson, Erik -- Jacobsson, Bo -- Joshi, Peter K -- Jugessur, Astanand -- Kaakinen, Marika -- Kanoni, Stavroula -- Karjalainen, Juha -- Kolcic, Ivana -- Kristiansson, Kati -- Kutalik, Zoltan -- Lahti, Jari -- Lee, Sang H -- Lin, Peng -- Lind, Penelope A -- Liu, Yongmei -- Lohman, Kurt -- Loitfelder, Marisa -- McMahon, George -- Vidal, Pedro Marques -- Meirelles, Osorio -- Milani, Lili -- Myhre, Ronny -- Nuotio, Marja-Liisa -- Oldmeadow, Christopher J -- Petrovic, Katja E -- Peyrot, Wouter J -- Polasek, Ozren -- Quaye, Lydia -- Reinmaa, Eva -- Rice, John P -- Rizzi, Thais S -- Schmidt, Helena -- Schmidt, Reinhold -- Smith, Albert V -- Smith, Jennifer A -- Tanaka, Toshiko -- Terracciano, Antonio -- van der Loos, Matthijs J H M -- Vitart, Veronique -- Volzke, Henry -- Wellmann, Jurgen -- Yu, Lei -- Zhao, Wei -- Allik, Juri -- Attia, John R -- Bandinelli, Stefania -- Bastardot, Francois -- Beauchamp, Jonathan -- Bennett, David A -- Berger, Klaus -- Bierut, Laura J -- Boomsma, Dorret I -- Bultmann, Ute -- Campbell, Harry -- Chabris, Christopher F -- Cherkas, Lynn -- Chung, Mina K -- Cucca, Francesco -- de Andrade, Mariza -- De Jager, Philip L -- De Neve, Jan-Emmanuel -- Deary, Ian J -- Dedoussis, George V -- Deloukas, Panos -- Dimitriou, Maria -- Eiriksdottir, Guethny -- Elderson, Martin F -- Eriksson, Johan G -- Evans, David M -- Faul, Jessica D -- Ferrucci, Luigi -- Garcia, Melissa E -- Gronberg, Henrik -- Guethnason, Vilmundur -- Hall, Per -- Harris, Juliette M -- Harris, Tamara B -- Hastie, Nicholas D -- Heath, Andrew C -- Hernandez, Dena G -- Hoffmann, Wolfgang -- Hofman, Adriaan -- Holle, Rolf -- Holliday, Elizabeth G -- Hottenga, Jouke-Jan -- Iacono, William G -- Illig, Thomas -- Jarvelin, Marjo-Riitta -- Kahonen, Mika -- Kaprio, Jaakko -- Kirkpatrick, Robert M -- Kowgier, Matthew -- Latvala, Antti -- Launer, Lenore J -- Lawlor, Debbie A -- Lehtimaki, Terho -- Li, Jingmei -- Lichtenstein, Paul -- Lichtner, Peter -- Liewald, David C -- Madden, Pamela A -- Magnusson, Patrik K E -- Makinen, Tomi E -- Masala, Marco -- McGue, Matt -- Metspalu, Andres -- Mielck, Andreas -- Miller, Michael B -- Montgomery, Grant W -- Mukherjee, Sutapa -- Nyholt, Dale R -- Oostra, Ben A -- Palmer, Lyle J -- Palotie, Aarno -- Penninx, Brenda W J H -- Perola, Markus -- Peyser, Patricia A -- Preisig, Martin -- Raikkonen, Katri -- Raitakari, Olli T -- Realo, Anu -- Ring, Susan M -- Ripatti, Samuli -- Rivadeneira, Fernando -- Rudan, Igor -- Rustichini, Aldo -- Salomaa, Veikko -- Sarin, Antti-Pekka -- Schlessinger, David -- Scott, Rodney J -- Snieder, Harold -- St Pourcain, Beate -- Starr, John M -- Sul, Jae Hoon -- Surakka, Ida -- Svento, Rauli -- Teumer, Alexander -- LifeLines Cohort Study -- Tiemeier, Henning -- van Rooij, Frank J A -- Van Wagoner, David R -- Vartiainen, Erkki -- Viikari, Jorma -- Vollenweider, Peter -- Vonk, Judith M -- Waeber, Gerard -- Weir, David R -- Wichmann, H-Erich -- Widen, Elisabeth -- Willemsen, Gonneke -- Wilson, James F -- Wright, Alan F -- Conley, Dalton -- Davey-Smith, George -- Franke, Lude -- Groenen, Patrick J F -- Hofman, Albert -- Johannesson, Magnus -- Kardia, Sharon L R -- Krueger, Robert F -- Laibson, David -- Martin, Nicholas G -- Meyer, Michelle N -- Posthuma, Danielle -- Thurik, A Roy -- Timpson, Nicholas J -- Uitterlinden, Andre G -- van Duijn, Cornelia M -- Visscher, Peter M -- Benjamin, Daniel J -- Cesarini, David -- Koellinger, Philipp D -- AA09367/AA/NIAAA NIH HHS/ -- AA11886/AA/NIAAA NIH HHS/ -- BB/F019394/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- CZB/4/710/Chief Scientist Office/United Kingdom -- DA024417/DA/NIDA NIH HHS/ -- DA029377/DA/NIDA NIH HHS/ -- DA05147/DA/NIDA NIH HHS/ -- DA13240/DA/NIDA NIH HHS/ -- ETM/55/Chief Scientist Office/United Kingdom -- F31 DA029377/DA/NIDA NIH HHS/ -- G0600705/Medical Research Council/United Kingdom -- G0700704/Medical Research Council/United Kingdom -- G9815508/Medical Research Council/United Kingdom -- K05 AA017688/AA/NIAAA NIH HHS/ -- MC_PC_U127561128/Medical Research Council/United Kingdom -- MC_UU_12013/1/Medical Research Council/United Kingdom -- MC_UU_12013/3/Medical Research Council/United Kingdom -- MC_UU_12013/5/Medical Research Council/United Kingdom -- MH016880/MH/NIMH NIH HHS/ -- MH066140/MH/NIMH NIH HHS/ -- MR/K026992/1/Medical Research Council/United Kingdom -- P01 AG005842/AG/NIA NIH HHS/ -- P01 CA089392/CA/NCI NIH HHS/ -- P01 GM099568/GM/NIGMS NIH HHS/ -- P01-AG005842/AG/NIA NIH HHS/ -- P01-AG005842-20S2/AG/NIA NIH HHS/ -- P30 AG012810/AG/NIA NIH HHS/ -- P30-AG012810/AG/NIA NIH HHS/ -- R01 AA009367/AA/NIAAA NIH HHS/ -- R01 AA011886/AA/NIAAA NIH HHS/ -- R01 DA013240/DA/NIDA NIH HHS/ -- R01 HL090620/HL/NHLBI NIH HHS/ -- R01 HL105756/HL/NHLBI NIH HHS/ -- R01 HL111314/HL/NHLBI NIH HHS/ -- R01 MH066140/MH/NIMH NIH HHS/ -- R37 DA005147/DA/NIDA NIH HHS/ -- T32 AG000186/AG/NIA NIH HHS/ -- T32 MH016880/MH/NIMH NIH HHS/ -- T32-AG000186-23/AG/NIA NIH HHS/ -- U01 AG009740/AG/NIA NIH HHS/ -- U01 DA024417/DA/NIDA NIH HHS/ -- Z01 AG001050-01/Intramural NIH HHS/ -- ZIA AG000196-03/Intramural NIH HHS/ -- ZIA AG000196-04/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2013 Jun 21;340(6139):1467-71. doi: 10.1126/science.1235488. Epub 2013 May 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Economics, Erasmus School of Economics, Erasmus University Rotterdam, Rotterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23722424" target="_blank"〉PubMed〈/a〉
    Keywords: Cognition ; *Educational Status ; Endophenotypes ; Female ; Genetic Loci ; *Genome-Wide Association Study ; Humans ; Male ; Multifactorial Inheritance ; *Polymorphism, Single Nucleotide
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    A model for the mechanism of human topoisomerase I (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The three-dimensional structure of a 70-kilodalton amino terminally truncated form of human topoisomerase I in complex with a 22-base pair duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact DNA. The linker region that connects the central core of the enzyme to the carboxyl-terminal domain assumes a coiled-coil configuration and protrudes away from the remainder of the enzyme. The positively charged DNA-proximal surface of the linker makes only a few contacts with the DNA downstream of the cleavage site. In combination with the crystal structures of the reconstituted human topoisomerase I before and after DNA cleavage, this information suggests which amino acid residues are involved in catalyzing phosphodiester bond breakage and religation. The structures also lead to the proposal that the topoisomerization step occurs by a mechanism termed "controlled rotation."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stewart, L -- Redinbo, M R -- Qiu, X -- Hol, W G -- Champoux, J J -- CA65656/CA/NCI NIH HHS/ -- GM16713/GM/NIGMS NIH HHS/ -- GM49156/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1534-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomolecular Structure Center and Department of Biological Structure, School of Medicine, University of Washington, Seattle, WA 98195-7742, USA. emerald_biostructures@rocketmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9488652" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/chemistry/metabolism ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Topoisomerases, Type I/*chemistry/*metabolism ; Humans ; Hydrogen Bonding ; *Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Tyrosine/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-16
    Description: Mutation of the VHL tumor suppressor is associated with the inherited von Hippel-Lindau (VHL) cancer syndrome and the majority of kidney cancers. VHL binds the ElonginC-ElonginB complex and regulates levels of hypoxia-inducible proteins. The structure of the ternary complex at 2.7 angstrom resolution shows two interfaces, one between VHL and ElonginC and another between ElonginC and ElonginB. Tumorigenic mutations frequently occur in a 35-residue domain of VHL responsible for ElonginC binding. A mutational patch on a separate domain of VHL indicates a second macromolecular binding site. The structure extends the similarities to the SCF (Skp1-Cul1-F-box protein) complex that targets proteins for degradation, supporting the hypothesis that VHL may function in an analogous pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stebbins, C E -- Kaelin, W G Jr -- Pavletich, N P -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):455-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Structural Biology, 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/10205047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Cycle Proteins/chemistry/metabolism ; Cloning, Molecular ; Crystallography, X-Ray ; *Genes, Tumor Suppressor ; Humans ; Hydrogen Bonding ; *Ligases ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Mutation, Missense ; Neoplasms/genetics ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/*chemistry/genetics/metabolism ; S-Phase Kinase-Associated Proteins ; Surface Properties ; Transcription Factors/*chemistry/metabolism ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    The glucocorticoid receptor: rapid exchange with regulatory sites in living cells (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-26
    Description: Steroid receptors bind to site-specific response elements in chromatin and modulate gene expression in a hormone-dependent fashion. With the use of a tandem array of mouse mammary tumor virus reporter elements and a form of glucocorticoid receptor labeled with green fluorescent protein, targeting of the receptor to response elements in live mouse cells was observed. Photobleaching experiments provide direct evidence that the hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment. Thus, the interaction of regulatory proteins with target sites in chromatin is a more dynamic process than previously believed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McNally, J G -- Muller, W G -- Walker, D -- Wolford, R -- Hager, G L -- New York, N.Y. -- Science. 2000 Feb 18;287(5456):1262-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Receptor Biology and Gene Expression, Building 41, Room B602, National Cancer Institute, Bethesda, MD 20892-5055, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10678832" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Line, Transformed ; Cell Nucleus/metabolism ; Chromatin/*metabolism ; Dexamethasone/metabolism/*pharmacology ; Green Fluorescent Proteins ; In Situ Hybridization, Fluorescence ; Ligands ; Luminescent Proteins ; Mammary Tumor Virus, Mouse/genetics ; Mice ; Microscopy, Confocal ; Microscopy, Fluorescence ; Nucleosomes/metabolism ; Receptors, Glucocorticoid/*metabolism ; *Response Elements ; *Terminal Repeat Sequences
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Location of a major susceptibility locus for familial schizophrenia on chromosome 1q21-q22 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-28
    Description: Schizophrenia is a complex disorder, and there is substantial evidence supporting a genetic etiology. Despite this, prior attempts to localize susceptibility loci have produced predominantly suggestive findings. A genome-wide scan for schizophrenia susceptibility loci in 22 extended families with high rates of schizophrenia provided highly significant evidence of linkage to chromosome 1 (1q21-q22), with a maximum heterogeneity logarithm of the likelihood of linkage (lod) score of 6.50. This linkage result should provide sufficient power to allow the positional cloning of the underlying susceptibility gene.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3787922/" 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/PMC3787922/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brzustowicz, L M -- Hodgkinson, K A -- Chow, E W -- Honer, W G -- Bassett, A S -- 53216/Canadian Institutes of Health Research/Canada -- K08 MH01392/MH/NIMH NIH HHS/ -- N01-HG-65403/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 28;288(5466):678-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular and Behavioral Neuroscience, Rutgers University, Newark, NJ 07102, USA. brzustowicz@axon.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10784452" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; Chromosomes, Human, Pair 1/*genetics ; Computer Simulation ; Female ; Genes, Dominant ; Genes, Recessive ; Genetic Heterogeneity ; Genetic Linkage ; Genetic Markers ; *Genetic Predisposition to Disease ; Humans ; Likelihood Functions ; Lod Score ; Male ; Models, Genetic ; Pedigree ; Schizophrenia/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Inhibition of the hammerhead ribozyme cleavage reaction by site-specific binding of Tb (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: Terbium(III) [Tb(III)] was shown to inhibit the hammerhead ribozyme by competing with a single magnesium(II) ion. X-ray crystallography revealed that the Tb(III) ion binds to a site adjacent to an essential guanosine in the catalytic core of the ribozyme, approximately 10 angstroms from the cleavage site. Synthetic modifications near this binding site yielded an RNA substrate that was resistant to Tb(III) binding and capable of being cleaved, even in the presence of up to 20 micromolar Tb(III). It is suggested that the magnesium(II) ion thought to bind at this site may act as a switch, affecting the conformational changes required to achieve the transition state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feig, A L -- Scott, W G -- Uhlenbeck, O C -- GM-36944/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):81-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417029" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Binding, Competitive ; Catalysis ; Crystallography, X-Ray ; Magnesium/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; RNA, Catalytic/*antagonists & inhibitors/chemistry/*metabolism ; Terbium/*metabolism/pharmacology
    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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  • 7
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    Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: Topoisomerases I promote the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. The crystal structures at 2.1 and 2.5 angstrom resolution of reconstituted human topoisomerase I comprising the core and carboxyl-terminal domains in covalent and noncovalent complexes with 22-base pair DNA duplexes reveal an enzyme that "clamps" around essentially B-form DNA. The core domain and the first eight residues of the carboxyl-terminal domain of the enzyme, including the active-site nucleophile tyrosine-723, share significant structural similarity with the bacteriophage family of DNA integrases. A binding mode for the anticancer drug camptothecin is proposed on the basis of chemical and biochemical information combined with these three-dimensional structures of topoisomerase I-DNA complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Redinbo, M R -- Stewart, L -- Kuhn, P -- Champoux, J J -- Hol, W G -- CA65656/CA/NCI NIH HHS/ -- GM49156/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1504-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomolecular Structure Center and Department of Biological Structure, Box 357742, School of Medicine, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9488644" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents, Phytogenic/metabolism/pharmacology ; Binding Sites ; Camptothecin/analogs & derivatives/metabolism/pharmacology ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Topoisomerases, Type I/*chemistry/genetics/metabolism ; *DNA-Binding Proteins ; Homeodomain Proteins/chemistry ; Host Cell Factor C1 ; Humans ; Hydrogen Bonding ; Integrases/chemistry ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Octamer Transcription Factor-1 ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Transcription Factors/chemistry ; Tyrosine/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-09
    Description: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milburn, M V -- Prive, G G -- Milligan, D L -- Scott, W G -- Yeh, J -- Jancarik, J -- Koshland, D E Jr -- Kim, S H -- AI 30725/AI/NIAID NIH HHS/ -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1342-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1660187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; Disulfides/analysis ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry/metabolism ; Salmonella typhimurium/metabolism ; X-Ray Diffraction
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  • 9
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    A regulatory SNP causes a human genetic disease by creating a new transcriptional promoter (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-05-27
    Description: We describe a pathogenetic mechanism underlying a variant form of the inherited blood disorder alpha thalassemia. Association studies of affected individuals from Melanesia localized the disease trait to the telomeric region of human chromosome 16, which includes the alpha-globin gene cluster, but no molecular defects were detected by conventional approaches. After resequencing and using a combination of chromatin immunoprecipitation and expression analysis on a tiled oligonucleotide array, we identified a gain-of-function regulatory single-nucleotide polymorphism (rSNP) in a nongenic region between the alpha-globin genes and their upstream regulatory elements. The rSNP creates a new promoterlike element that interferes with normal activation of all downstream alpha-like globin genes. Thus, our work illustrates a strategy for distinguishing between neutral and functionally important rSNPs, and it also identifies a pathogenetic mechanism that could potentially underlie other genetic diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Gobbi, Marco -- Viprakasit, Vip -- Hughes, Jim R -- Fisher, Chris -- Buckle, Veronica J -- Ayyub, Helena -- Gibbons, Richard J -- Vernimmen, Douglas -- Yoshinaga, Yuko -- de Jong, Pieter -- Cheng, Jan-Fang -- Rubin, Edward M -- Wood, William G -- Bowden, Don -- Higgs, Douglas R -- MC_U137961143/Medical Research Council/United Kingdom -- MC_U137961145/Medical Research Council/United Kingdom -- MC_U137961147/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 May 26;312(5777):1215-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, OX3 9DS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728641" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cells, Cultured ; Chromatin Immunoprecipitation ; Chromosomes, Human, Pair 16/*genetics ; Erythroblasts ; GATA1 Transcription Factor/metabolism ; Gene Expression ; Gene Expression Profiling ; Globins/*genetics ; Haplotypes ; Humans ; Melanesia ; Minisatellite Repeats ; Multigene Family ; Oligonucleotide Array Sequence Analysis ; *Polymorphism, Single Nucleotide ; *Promoter Regions, Genetic ; Regulatory Elements, Transcriptional ; Transcription, Genetic ; alpha-Thalassemia/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 10
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    Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: Structural changes in the extracellular matrix are necessary for cell migration during tissue remodeling and tumor invasion. Specific cleavage of laminin-5 (Ln-5) by matrix metalloprotease-2 (MMP2) was shown to induce migration of breast epithelial cells. MMP2 cleaved the Ln-5 gamma2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giannelli, G -- Falk-Marzillier, J -- Schiraldi, O -- Stetler-Stevenson, W G -- Quaranta, V -- CA47858/CA/NCI NIH HHS/ -- DE10063/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):225-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast/*cytology/metabolism ; Cell Adhesion ; Cell Adhesion Molecules/*metabolism ; Cell Division ; Cell Line ; *Cell Movement ; Cell Size ; Collagenases/metabolism ; Epithelial Cells ; Epithelium/metabolism ; Extracellular Matrix/*metabolism ; Female ; Fibrinolysin/metabolism ; Gelatinases/antagonists & inhibitors/*metabolism ; Humans ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Metalloendopeptidases/antagonists & inhibitors/*metabolism ; Mice ; Phenylalanine/analogs & derivatives/pharmacology ; Protease Inhibitors/pharmacology ; Rats ; Recombinant Fusion Proteins/metabolism ; Skin Neoplasms/metabolism/pathology ; Thiophenes/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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