(Q42820023)

English

Insulin stimulates phosphorylation of the beta 2-adrenergic receptor by the insulin receptor, creating a potent feedback inhibitor of its tyrosine kinase

scientific article published on 8 January 2002

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Insulin stimulates phosphorylation of the beta 2-adrenergic receptor by the insulin receptor, creating a potent feedback inhibitor of its tyrosine kinase (English)

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

phosphorylation

1 reference

based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

author name string

Sergey Doronin

1

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Hsien-yu Wang Hy

2

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Craig C Malbon

3

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

language of work or name

0 references

publication date

8 January 2002

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

277

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

10698-10703

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Insulin-like growth factor receptor-1 stimulates phosphorylation of the beta2-adrenergic receptor in vivo on sites distinct from those phosphorylated in response to insulin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

Expression, characterization, and crystallization of the catalytic core of the human insulin receptor protein-tyrosine kinase domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

The full-length, cytoplasmic C-terminus of the beta 2-adrenergic receptor expressed in E. coli acts as a substrate for phosphorylation by protein kinase A, insulin receptor tyrosine kinase, GRK2, but not protein kinase C and suppresses desensitizati

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

Protein-protein interaction in insulin signaling and the molecular mechanisms of insulin resistance

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

The beta-adrenergic receptor is a substrate for the insulin receptor tyrosine kinase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

Phosphorylation of Tyrosyl Residues 350/354 of the β-Adrenergic Receptor Is Obligatory for Counterregulatory Effects of Insulin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

G-protein-linked receptors as substrates for tyrosine kinases: cross-talk in signaling.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

Insulin activation of mitogen-activated protein kinases Erk1,2 is amplified via beta-adrenergic receptor expression and requires the integrity of the Tyr350 of the receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109432200

21 January 2018

Identifiers

10.1074/JBC.M109432200

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

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