Two naturally occurring mutant insulin receptors phosphorylate insulin receptor substrate-1 (IRS-1) but fail to mediate the biological effects of insulin: Evidence that IRS-1 phosphorylation is not sufficient for normal insulin action

Journal of Biological Chemistry

Volumn 271, Issue 12, 1996, Pages 7134-7140

  Krook, Anna ^a   Moller, David E ^b,c   Dib, Karim ^a,d   O'Rahilly, Stephen ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

^c MERCK RESEARCH LABORATORIES   (United States)

^d European Union   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR ANTIBODY; INSULIN RECEPTOR KINASE; MUTANT PROTEIN;

ANIMAL CELL; ARTICLE; CHO CELL; CONGENITAL DISORDER; CONTROLLED STUDY; ENZYME ACTIVITY; GLYCOGEN SYNTHESIS; HORMONE RECEPTOR INTERACTION; HUMAN; INSULIN RESISTANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION;

ADOLESCENT; ANIMALS; BASE SEQUENCE; CHO CELLS; CLONING, MOLECULAR; CRICETINAE; DNA PRIMERS; ENZYME ACTIVATION; FEMALE; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHOPROTEINS; PHOSPHORYLATION; POINT MUTATION; PROTEIN KINASES; RECEPTOR, INSULIN; TYROSINE;

EID: 0029927839     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.12.7134     Document Type: Article

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