Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130 (Q28511752)

25 January 2017

title

Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130 (English)

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25 January 2017

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Spleen tyrosine kinase

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GOA release 2020-03-11

L. M. Keshvara

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25 January 2017

C. Isaacson

series ordinal

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25 January 2017

M. L. Harrison

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25 January 2017

R. L. Geahlen

series ordinal

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25 January 2017

language of work or name

English

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publication date

18 April 1997

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Journal of Biological Chemistry

25 January 2017

published in

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25 January 2017

volume

272

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25 January 2017

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25 January 2017

page(s)

10377–10381

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Regulation of antigen receptor signal transduction by protein tyrosine kinases

25 January 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Protein tyrosine kinases in the initiation of antigen receptor signaling

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Signal transduction by the B cell antigen receptor and its coreceptors

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Signal transduction by lymphocyte antigen receptors

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Signaling pathways activated by protein tyrosine phosphorylation in lymphocytes

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Syk tyrosine kinase required for mouse viability and B-cell development

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Antigen receptor tail clue.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates alpha-tubulin on tyrosine

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Identification of the major sites of autophosphorylation of the murine protein-tyrosine kinase Syk

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Distinct tyrosine phosphorylation sites in ZAP-70 mediate activation and negative regulation of antigen receptor function

21 January 2018

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Activating and Inhibitory Mutations in Adjacent Tyrosines in the Kinase Domain of ZAP-70

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

Identification of the site in the Syk protein tyrosine kinase that binds the SH2 domain of Lck

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.272.16.10377

21 January 2018

Identifiers

DOI

10.1074/JBC.272.16.10377

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