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    Human diabetes associated with a deletion of the tyrosine kinase domain of the insulin receptor (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-07-07
    Description: The insulin receptor has an intrinsic tyrosine kinase activity that is essential for signal transduction. A mutant insulin receptor gene lacking almost the entire kinase domain has been identified in an individual with type A insulin resistance and acanthosis nigricans. Insulin binding to the erythrocytes or cultured fibroblasts from this individual was normal. However receptor autophosphorylation and tyrosine kinase activity toward an exogenous substrate were reduced in partially purified insulin receptors from the proband's lymphocytes that had been transformed by Epstein-Barr virus. The insulin resistance associated with this mutated gene was inherited by the proband from her mother as an apparently autosomal dominant trait. Thus a deletion in one allele of the insulin receptor gene may be at least partly responsible for some instances of insulin-resistant diabetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taira, M -- Hashimoto, N -- Shimada, F -- Suzuki, Y -- Kanatsuka, A -- Nakamura, F -- Ebina, Y -- Tatibana, M -- Makino, H -- New York, N.Y. -- Science. 1989 Jul 7;245(4913):63-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Second Department of Internal Medicine, Chiba University School of Medicine, Inohana, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2544997" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Alleles ; Amino Acid Sequence ; Base Sequence ; *Chromosome Deletion ; Diabetes Mellitus, Type 1/enzymology/*genetics ; Female ; *Genes ; Humans ; Insulin Resistance ; Male ; Molecular Sequence Data ; Mutation ; Pedigree ; Protein-Tyrosine Kinases/*genetics ; Receptor, Insulin/*genetics ; Restriction Mapping
    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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  • 2
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    Mouse interferons: amino terminal amino acid sequences of various species (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-01
    Description: Mouse interferons of three size classes (A, 35,000 to 40,000 daltons; B, 26,000 to 33,000 daltons; and C, 20,000 daltons) were purified from Ehrlich ascites tumor cells infected with Newcastle disease virus. The sequences of the first 24 amino acids (No. 17 has not been identified) of interferons A and B are identical. The sequence of the first 20 amino acids of interferon C differs from that of A and B in 18 positions. There is partial homology in amino terminal sequence between mouse interferons A (or B) and a human fibroblast interferon and between mouse interferon C and a human lymphoblastoid interferon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taira, H -- Broeze, R J -- Jayaram, B M -- Lengyel, P -- Hunkapiller, M W -- Hood, L E -- New York, N.Y. -- Science. 1980 Feb 1;207(4430):528-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Evolution ; Carcinoma, Ehrlich Tumor/analysis ; Cells, Cultured ; Glycoproteins/analysis ; *Interferons/genetics ; Mice ; Molecular Weight
    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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