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  • Mutation  (3)
  • Crystallography, X-Ray
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Geophysical Union (AGU)
  • National Academy of Sciences
  • Nature Publishing Group (NPG)
  • Springer
  • 2000-2004  (4)
  • 2002  (4)
Sammlung
Schlagwörter
Verlag/Herausgeber
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Geophysical Union (AGU)
  • National Academy of Sciences
  • Nature Publishing Group (NPG)
  • Springer
Erscheinungszeitraum
  • 2000-2004  (4)
Jahr
  • 1
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    C-cadherin ectodomain structure and implications for cell adhesion mechanisms (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-04-20
    Beschreibung: 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〉
    Schlagwort(e): 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
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    Finding genes that underlie complex traits (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-12-21
    Beschreibung: Phenotypic variation among organisms is central to evolutionary adaptations underlying natural and artificial selection, and also determines individual susceptibility to common diseases. These types of complex traits pose special challenges for genetic analysis because of gene-gene and gene-environment interactions, genetic heterogeneity, low penetrance, and limited statistical power. Emerging genome resources and technologies are enabling systematic identification of genes underlying these complex traits. We propose standards for proof of gene discovery in complex traits and evaluate the nature of the genes identified to date. These proof-of-concept studies demonstrate the insights that can be expected from the accelerating pace of gene discovery in this field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glazier, Anne M -- Nadeau, Joseph H -- Aitman, Timothy J -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2345-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physiological Genomics and Medicine Group, MRC Clinical Sciences Centre, Hammersmith Hospital, Imperial College Faculty of Medicine, Ducane Road, London W12 0NN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493905" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alleles ; Animals ; Chromosome Mapping ; Genetic Linkage ; *Genetic Predisposition to Disease ; Genetic Variation ; Humans ; *Multifactorial Inheritance ; Mutation ; Phenotype ; Plants/genetics ; *Quantitative Trait Loci ; *Quantitative Trait, Heritable ; Saccharomyces cerevisiae/genetics ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
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    Sex matters in meiosis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-06-22
    Beschreibung: In mammals, fertilization typically involves the ovulation of one or a few eggs at one end of the female reproductive tract and the entry of millions of sperm at the other. Given this disparity in numbers, it might be expected that the more precious commodity-eggs-would be subject to more stringent quality-control mechanisms. However, information from engineered mutations of meiotic genes suggests just the opposite. Specifically, the available mutants demonstrate striking sexual dimorphism in response to meiotic disruption; for example, faced with adversity, male meiosis grinds to a halt, whereas female meiosis soldiers on. This female "robustness" comes with a cost, however, because aneuploidy appears to be increased in the resultant oocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunt, Patricia A -- Hassold, Terry J -- HD21341/HD/NICHD NIH HHS/ -- HD31866/HD/NICHD NIH HHS/ -- HD37502/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2181-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Case Western Reserve University, Cleveland, OH 44106-4955, USA. pah13@po.cwru.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077403" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Aneuploidy ; Animals ; Cell Cycle ; Female ; Humans ; Male ; *Meiosis ; Mice ; Mutation ; Oocytes/*physiology ; *Oogenesis ; Prophase ; Proteins/genetics/metabolism ; Sex Characteristics ; Spermatocytes/*physiology ; *Spermatogenesis
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
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    Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-09-14
    Beschreibung: The mechanism by which disruption of reading frame can influence pre-messenger RNA (pre-mRNA) processing is poorly understood. We assessed the role of factors essential for nonsense-mediated mRNA decay (NMD) in nonsense-mediated altered splicing (NAS) with the use of RNA interference (RNAi) in mammalian cells. Inhibition of rent1/hUpf1 expression abrogated both NMD and NAS of nonsense T cell receptor beta transcripts. In contrast, inhibition of rent2/hUpf2 expression did not disrupt NAS despite achieving comparable stabilization of nonsense transcripts. We also demonstrate that NAS and NMD are genetically separable functions of rent1/hUpf1. Additionally, rent1/hUpf1 enters the nucleus where it may directly influence early events in mRNA biogenesis. This provides compelling evidence that NAS relies on a component of the nonsense surveillance machinery but is not an indirect consequence of NMD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendell, Joshua T -- ap Rhys, Colette M J -- Dietz, Harry C -- GM55239/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):419-22. Epub 2002 Sep 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Genetic Medicine and Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 858 Ross Building, 720 Rutland Avenue, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228722" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Active Transport, Cell Nucleus ; *Alternative Splicing ; Amino Acid Substitution ; Blotting, Northern ; Cell Nucleus/metabolism ; *Codon, Nonsense ; Cytoplasm/metabolism ; Equilibrative-Nucleoside Transporter 2/genetics/metabolism ; Fatty Acids, Unsaturated/pharmacology ; Gene Silencing ; Genes, T-Cell Receptor beta ; HeLa Cells ; Humans ; Mutation ; RNA Helicases/genetics/*metabolism ; RNA, Messenger/genetics/*metabolism ; RNA, Small Interfering/metabolism ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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