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REF 1 |
SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase. Biochem J. 1998 Oct 1;335 ( Pt 1):103-9.
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REF 2 |
Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain. Mamm Genome. 1999 Dec;10(12):1160-7.
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REF 3 |
The association between the SH2-containing inositol polyphosphate 5-Phosphatase 2 (SHIP2) and the adaptor protein APS has an impact on biochemical properties of both partners. J Cell Physiol. 2008 Jan;214(1):260-72.
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REF 4 |
Primary and essential role of the adaptor protein APS for recruitment of both c-Cbl and its associated protein CAP in insulin signaling. J Biol Chem. 2004 May 14;279(20):21526-32.
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REF 5 |
Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction. J Biol Chem. 1995 Dec 8;270(49):29189-93.
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REF 6 |
Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro. Biochem Biophys Res Commun. 1994 Mar 15;199(2):780-5.
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REF 7 |
Fatty acylated caveolin-2 is a substrate of insulin receptor tyrosine kinase for insulin receptor substrate-1-directed signaling activation. Biochim Biophys Acta. 2015 May;1853(5):1022-34.
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REF 8 |
The Protein-tyrosine-phosphatase SHP2 is phosphorylated on serine residues 576 and 591 by protein kinase C isoforms alpha, beta 1, beta 2, and eta. Biochemistry. 2002 Jan 15;41(2):603-8.
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REF 9 |
PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities. J Biol Chem. 1995 Nov 17;270(46):27407-10.
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REF 10 |
Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action. J Biol Chem. 2002 Jan 11;277(2):1531-7.
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REF 11 |
Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786. J Biol Chem. 1996 Mar 15;271(11):5980-3.
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