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- W2046007718 abstract "Discovery of the insulin receptor 25 years ago was followed by an era of expectation. How was the insulin signal passed into cells? Was there a second messenger analogous to cyclic AMP relaying the glucagon signal? No easy solution emerged from early work. The puzzle persisted despite the discovery in 1982 of kinase activity in the intracellular portion of the insulin receptor and hence a means of initiating the intracellular signalling process. 1 Kasuga M Karlsson FA Kahn CR Insulin stimulates the phosphorylation of the 95 95000-Dalton subunit of its own receptor. Science. 1982; 215: 185-187 Crossref PubMed Scopus (683) Google Scholar By the early 1990s increasing evidence pointed not to a single pathway of insulin action but to a network of pathways with multiple points of modulation by other hormones and signalling molecules. 2 Taylor R Insulin action 1991. Clin Endocrinol. 1991; 34: 159-171 Crossref PubMed Scopus (29) Google Scholar This network allowed explanation of insulin's remarkable ability to regulate more processes than any other hormone. In the past 5 years, at least three immediate substrates for the insulin receptor kinase have been confirmed and many of the intermediate signalling molecules have been identified. 3 Wolf G Trub T Ottinger E et al. PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities. J Biol Chemistry. 1995; 270: 27407-27410 Crossref PubMed Scopus (208) Google Scholar , 4 Patti ME Sun XJ Bruening JC et al. 4PS/insulin receptor substrate (IRS)-2 is the alternative substrate of the insulin receptor in IRS-1-deficient mice. J Biol Chemistry. 1995; 270: 24670-24673 Crossref PubMed Scopus (200) Google Scholar" @default.
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- W2046007718 title "Insulin resistance: circumventing nature's blocks" @default.
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- W2046007718 doi "https://doi.org/10.1016/s0140-6736(05)64410-8" @default.
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