Title : Identification of Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor in intact cells.

Pub. Date : 2001 Mar 30

PMID : 11401470






11 Functional Relationships(s)
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1 Identification of Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor in intact cells. Serine insulin receptor Homo sapiens
2 Identification of Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor in intact cells. Serine insulin receptor Homo sapiens
3 In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro. Serine insulin receptor Homo sapiens
4 In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro. Serine insulin receptor Homo sapiens
5 In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro. Serine insulin receptor Homo sapiens
6 In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro. Serine insulin receptor Homo sapiens
7 In this study, we determined the intrinsic activity of the IR to phosphorylate both serine residues in intact cells. Serine insulin receptor Homo sapiens
8 The IR was isolated by immunoprecipitation and SDS-PAGE and subsequently analysed for serine phosphorylation by phosphopeptide mapping of HPLC-purified tryptic phosphopeptides. Serine insulin receptor Homo sapiens
9 Activation of the IR in the intact cell appeared to result in phosphate incorporation into Ser(1275) and Ser(1309), providing strong evidence that both serine residues are phosphorylation sites of the activated receptor in intact cells. Serine insulin receptor Homo sapiens
10 Activation of the IR in the intact cell appeared to result in phosphate incorporation into Ser(1275) and Ser(1309), providing strong evidence that both serine residues are phosphorylation sites of the activated receptor in intact cells. Serine insulin receptor Homo sapiens
11 Activation of the IR in the intact cell appeared to result in phosphate incorporation into Ser(1275) and Ser(1309), providing strong evidence that both serine residues are phosphorylation sites of the activated receptor in intact cells. Serine insulin receptor Homo sapiens