Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain (Q28280523)

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English	Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain	scientific article

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instance of

scholarly article

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title

Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain (English)

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main subject

phosphorylation

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based on heuristic

inferred from title

author name string

D R Stover

series ordinal

1

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P Furet

series ordinal

2

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N B Lydon

series ordinal

3

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language of work or name

English

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publication date

24 May 1996

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published in

Journal of Biological Chemistry

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volume

271

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issue

21

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page(s)

12481-7

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cites work

Transforming gene product of Rous sarcoma virus phosphorylates tyrosine

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https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

The cell cycle and c-Src

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21 January 2018

Tyr527 is phosphorylated in pp60c-src: implications for regulation

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reference URL

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21 January 2018

Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

SH2 domains recognize specific phosphopeptide sequences

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Involvement of pp60c-src with two major signaling pathways in human breast cancer

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Src phosphorylation of the epidermal growth factor receptor at novel sites mediates receptor interaction with Src and P85 alpha

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Association between the PDGF receptor and members of the src family of tyrosine kinases

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity.

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Augmented mitogenic responsiveness to epidermal growth factor in murine fibroblasts that overexpress pp60c-src

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reference URL

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21 January 2018

Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Purification and biochemical characterization of non-myristoylated recombinant pp60c-src kinase

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

RETRACTED: Selective inhibition of the platelet-derived growth factor signal transduction pathway by a protein-tyrosine kinase inhibitor of the 2-phenylaminopyrimidine class

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

The product of the protooncogene c-src is modified during the cellular response to platelet-derived growth factor

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Regulation of the Src protein tyrosine kinase

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stated in

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

retrieved

21 January 2018

Activation of p56lck by p72syk through physical association and N-terminal tyrosine phosphorylation

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.21.12481

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.21.12481

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PubMed publication ID

8647855

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