The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling (Q28284128)

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5 December 2019

title

The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling (English)

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5 December 2019

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5 December 2019

author name string

M G Myers

1

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5 December 2019

P Shi

3

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5 December 2019

J H Pierce

4

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5 December 2019

R Rhoads

5

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5 December 2019

M F White

6

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5 December 2019

publication date

1 October 1998

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Journal of Biological Chemistry

5 December 2019

language of work or name

English

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published in

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5 December 2019

volume

273

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5 December 2019

issue

41

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5 December 2019

page(s)

26908-26914

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Insulin signal transduction and the IRS proteins

5 December 2019

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Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein

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Role of IRS-2 in insulin and cytokine signalling

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A Novel 160-kDa Phosphotyrosine Protein in Insulin-treated Embryonic Kidney Cells Is a New Member of the Insulin Receptor Substrate Family

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The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family

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The pleckstrin homology domain is the principal link between the insulin receptor and IRS-1.

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Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew

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corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso

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The nonreceptor protein tyrosine phosphatase corkscrew functions in multiple receptor tyrosine kinase pathways in Drosophila

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Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1

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Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

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Crystal Structure of the Tyrosine Phosphatase SHP-2

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Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation

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Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling.

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The structure and function of p55PIK reveal a new regulatory subunit for phosphatidylinositol 3-kinase

21 January 2018

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IRS-1: essential for insulin- and IL-4-stimulated mitogenesis in hematopoietic cells

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7 Preparation and use of anti-phosphotyrosine antibodies to study structure and function of insulin receptor

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YMXM motifs and signaling by an insulin receptor substrate 1 molecule without tyrosine phosphorylation sites

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The pleckstrin homology domain in insulin receptor substrate-1 sensitizes insulin signaling

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Activation of phosphatidylinositol 3-kinase by insulin

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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Role of IRS-1-GRB-2 complexes in insulin signaling

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Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases

21 January 2018

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Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate 1 and phosphatidylinositol 3-kinase

21 January 2018

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Requirement of Protein Kinase Cζ for Stimulation of Protein Synthesis by Insulin

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Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction

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Coordinate regulation of STAT signaling and c-fos expression by the tyrosine phosphatase SHP-2.

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The protein tyrosine phosphatase SHP-2 negatively regulates ciliary neurotrophic factor induction of gene expression

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Protein tyrosine phosphatase 2 (SHP-2) moderates signaling by gp130 but is not required for the induction of acute-phase plasma protein genes in hepatic cells

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Interleukin-3 Induces Association of the Protein-tyrosine Phosphatase SHP2 and Phosphatidylinositol 3-Kinase with a 100-kDa Tyrosine-phosphorylated Protein in Hemopoietic Cells

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.41.26908

2 references

Consolidated OpenCitations Corpus – April 2017

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5 December 2019

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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