RACK1: a novel substrate for the Src protein-tyrosine kinase (Q42808892)

7 November 2017

RACK1: a novel substrate for the Src protein-tyrosine kinase (English)

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7 November 2017

Betty Y Chang

1

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7 November 2017

Rachel A Harte

series ordinal

2

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7 November 2017

Christine A Cartwright

series ordinal

3

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7 November 2017

language of work or name

English

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publication date

1 October 2002

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7 November 2017

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7 November 2017

21

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50

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7619-7629

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https://scigraph.springernature.com/pub.10.1038/sj.onc.1206002

7 November 2017

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cites work

Src family tyrosine kinases and growth factor signaling

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Selected glimpses into the activation and function of Src kinase

21 January 2018

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Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain

21 January 2018

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Structural and functional modification of pp60c-src associated with polyoma middle tumor antigen from infected or transformed cells

21 January 2018

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Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen

21 January 2018

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Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis

21 January 2018

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The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1

21 January 2018

1 reference

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RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells

21 January 2018

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A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor

21 January 2018

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Monoclonal antibodies to phosphotyrosine

21 January 2018

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Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation

21 January 2018

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Identification of GIYWHHY as a novel peptide substrate for human p60c-src protein tyrosine kinase

21 January 2018

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21 January 2018

The hunting of the Src

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Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases

21 January 2018

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Localization of protein kinases by anchoring proteins: a theme in signal transduction

21 January 2018

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The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts

21 January 2018

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The sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-src

21 January 2018

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G protein heterodimers: new structures propel new questions

21 January 2018

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The ancient regulatory-protein family of WD-repeat proteins

21 January 2018

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Src activity increases and Yes activity decreases during mitosis of human colon carcinoma cells

21 January 2018

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Enhanced phosphorylation of Src family kinase substrates containing SH2 domain binding sites.

21 January 2018

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Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src

21 January 2018

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Adaptor proteins in protein kinase C-mediated signal transduction

21 January 2018

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Catalytic specificity of phosphotyrosine kinases Blk, Lyn, c-Src and Syk as assessed by phage display

21 January 2018

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A mutation at the ATP-binding site of pp60v-src abolishes kinase activity, transformation, and tumorigenicity

21 January 2018

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Cellular functions regulated by Src family kinases

21 January 2018

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Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

21 January 2018

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Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1206002

inferred from DOI database lookup

7 January 2021

based on heuristic

Modulating protein kinase C signal transduction.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1206002

inferred from DOI database lookup

7 January 2021

based on heuristic

Activation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxy terminus.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1206002

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/SJ.ONC.1206002

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Dimensions Publication ID

7 November 2017

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