Tyr(612) and Tyr(632) in human insulin receptor substrate-1 are important for full activation of insulin-stimulated phosphatidylinositol 3-kinase activity and translocation of GLUT4 in adipose cells (Q24291346)

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scientific article published in July 2001

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English	Tyr(612) and Tyr(632) in human insulin receptor substrate-1 are important for full activation of insulin-stimulated phosphatidylinositol 3-kinase activity and translocation of GLUT4 in adipose cells	scientific article published in July 2001

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11416002%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

Tyr(612) and Tyr(632) in human insulin receptor substrate-1 are important for full activation of insulin-stimulated phosphatidylinositol 3-kinase activity and translocation of GLUT4 in adipose cells (English)

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Europe PubMed Central

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8 November 2019

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Alessandro Cama

3

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11416002%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

Michael J. Quon

4

1 reference

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11416002%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

author name string

D L Esposito

1

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8 November 2019

Y Li

2

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8 November 2019

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publication date

1 July 2001

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8 November 2019

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11416002%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

142

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8 November 2019

7

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8 November 2019

2833-2840

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8 November 2019

Molecular scanning for mutations in the insulin receptor substrate-1 (IRS-1) gene in Mexican Americans with Type 2 diabetes mellitus

1 reference

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Transfection of DNA into isolated rat adipose cells by electroporation: evaluation of promoter activity in transfected adipose cells which are highly responsive to insulin after one day in culture

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Molecular scanning of the glycogen synthase and insulin receptor substrate-1 genes in Japanese subjects with non-insulin-dependent diabetes mellitus

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Insulin receptor substrate-1 gene mutations in NIDDM; implications for the study of polygenic disease

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Aminoacid polymorphisms of insulin receptor substrate-1 in non-insulin-dependent diabetes mellitus.

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Insulin receptor substrate (IRS-1) gene polymorphisms in French NIDDM families

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Insulin signalling: metabolic pathways and mechanisms for specificity

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Postbinding characterization of five naturally occurring mutations in the human insulin receptor gene: impaired insulin-stimulated c-jun expression and thymidine incorporation despite normal receptor autophosphorylation

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Potent Activation of Phosphatidylinositol 3'-Kinase by Simple Phosphotyrosine Peptides Derived from Insulin Receptor Substrate 1 Containing Two YMXM Motifs for binding SH2 Domains

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Disruption of IRS-2 causes type 2 diabetes in mice

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Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1.

1 reference

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Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene.

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Amino acid polymorphism Gly 972 Arg in IRS-1 is not associated to lower clamp-derived insulin sensitivity in young healthy first degree relatives of patients with type 2 diabetes.

1 reference

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Tyrosine kinase-deficient mutant human insulin receptors (Met1153-->Ile) overexpressed in transfected rat adipose cells fail to mediate translocation of epitope-tagged GLUT4.

1 reference

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Regulation of phosphatidylinositol 3'-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit

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Mutant of insulin receptor substrate-1 incapable of activating phosphatidylinositol 3-kinase did not mediate insulin-stimulated maturation of Xenopus laevis oocytes

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Protein-tyrosine phosphatases PTP1B and syp are modulators of insulin-stimulated translocation of GLUT4 in transfected rat adipose cells

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Role of insulin receptor substrate-1 and pp60 in the regulation of insulin-induced glucose transport and GLUT4 translocation in primary adipocytes

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7 January 2021

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Insulin receptor substrate-2 (IRS-2) can mediate the action of insulin to stimulate translocation of GLUT4 to the cell surface in rat adipose cells.

1 reference

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7 January 2021

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Tandem SH2 domains confer high specificity in tyrosine kinase signaling

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7 January 2021

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Modulation of insulin receptor substrate-1 tyrosine phosphorylation by an Akt/phosphatidylinositol 3-kinase pathway

1 reference

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7 January 2021

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Phosphorylation of insulin receptor substrate-1 (IRS-1) by protein kinase B positively regulates IRS-1 function

1 reference

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7 January 2021

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Essential role of insulin receptor substrate-2 in insulin stimulation of Glut4 translocation and glucose uptake in brown adipocytes

1 reference

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7 January 2021

based on heuristic

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Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin.

1 reference

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7 January 2021

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Roles of insulin receptor substrate-1, phosphatidylinositol 3-kinase, and release of intracellular Ca2+ stores in insulin-stimulated insulin secretion in beta -cells.

1 reference

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7 January 2021

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The common Arg972 polymorphism in insulin receptor substrate-1 causes apoptosis of human pancreatic islets

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A generic intron increases gene expression in transgenic mice

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

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Roles of 1-phosphatidylinositol 3-kinase and ras in regulating translocation of GLUT4 in transfected rat adipose cells

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Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation

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Insulin signalling and insulin actions in the muscles and livers of insulin-resistant, insulin receptor substrate 1-deficient mice

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

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Adenovirus-mediated overexpression of IRS-1 interacting domains abolishes insulin-stimulated mitogenesis without affecting glucose transport in 3T3-L1 adipocytes

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Insulin receptor substrate-1 variants in non-insulin-dependent diabetes

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based on heuristic

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A common amino acid polymorphism in insulin receptor substrate-1 causes impaired insulin signaling. Evidence from transfection studies

1 reference

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inferred from DOI database lookup

The Gly972-->Arg amino acid polymorphism in IRS-1 impairs insulin secretion in pancreatic beta cells

1 reference

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1 reference

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Action of insulin receptor substrate-3 (IRS-3) and IRS-4 to stimulate translocation of GLUT4 in rat adipose cells

1 reference

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inferred from DOI database lookup

Insulin receptor substrate polymorphisms and type 2 diabetes mellitus

1 reference

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based on heuristic

inferred from DOI database lookup

Molecular scanning of the insulin receptor substrate 1 gene in subjects with severe insulin resistance: detection and functional analysis of a naturally occurring mutation in a YMXM motif.

1 reference

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inferred from DOI database lookup

Identifiers

10.1210/EN.142.7.2833

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

10.1210/ENDO.142.7.8283

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11416002%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

release_xpl5w5ssajgplmusvg2c3v3pgy

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https://api.fatcat.wiki/v0/release/xpl5w5ssajgplmusvg2c3v3pgy

24 November 2022

based on heuristic

mapped directly with Wikidata item

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

2 references

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11416002%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

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