Human Diabetes Associated with a Mutation in the Tyrosine Kinase Domain of the Insulin Receptor

DOI Web Site 被引用文献12件
  • Masato Odawara
    Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Hongo, Tokyo, Japan 113.
  • Takashi Kadowaki
    Diabetes Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
  • Ritsuko Yamamoto
    Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Hongo, Tokyo, Japan 113.
  • Yoshikazu Shibasaki
    Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Hongo, Tokyo, Japan 113.
  • Kazuyuki Tobe
    Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Hongo, Tokyo, Japan 113.
  • Domenico Accili
    Diabetes Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
  • Charles Bevins
    Diabetes Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
  • Yuhei Mikami
    Department of Pediatrics, Hokkaido University School of Medicine, Sapporo, Japan 060.
  • Nobuo Matsuura
    Department of Pediatrics, Hokkaido University School of Medicine, Sapporo, Japan 060.
  • Yasuo Akanuma
    Institute for Diabetes Care and Research, Asahi Life Foundation, Marunouchi, Tokyo, Japan 100.
  • Fumimaro Takaku
    Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Hongo, Tokyo, Japan 113.
  • Simeon I. Taylor
    Diabetes Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
  • Masato Kasuga
    Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Hongo, Tokyo, Japan 113.

抄録

<jats:p> Insulin receptor complementary DNA has been cloned from an insulin-resistant individual whose receptors have impaired tyrosine protein kinase activity. One of this individual's alleles has a mutation in which valine is substituted for Gly <jats:sup>996</jats:sup> , the third glycine in the conserved Gly-X-Gly-X-X-Gly motif in the putative binding site for adenosine triphosphate. Expression of the mutant receptor by transfection into Chinese hamster ovary cells confirmed that the mutation impairs tyrosine kinase activity. </jats:p>

収録刊行物

  • Science

    Science 245 (4913), 66-68, 1989-07-07

    American Association for the Advancement of Science (AAAS)

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