T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G (Q28264262)

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English	T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G	scientific article

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scholarly article

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T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G (English)

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phosphorylation

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author name string

Y Ohashi

1

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K Tachibana

2

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K Kamiguchi

3

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H Fujita

4

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C Morimoto

5

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language of work or name

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publication date

13 March 1998

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Journal of Biological Chemistry

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273

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11

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6446-51

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Signal transduction by lymphocyte antigen receptors

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Complex complexes: signaling at the TCR.

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

SH2 domains recognize specific phosphopeptide sequences

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Ligation of VLA-4 on T cells stimulates tyrosine phosphorylation of a 105-kD protein

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Signaling through focal adhesion kinase

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Ligation of the T cell antigen receptor induces tyrosine phosphorylation of p105CasL, a member of the p130Cas-related docking protein family, and its subsequent binding to the Src homology 2 domain of c-Crk

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Interactions of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Nerve growth factor stimulates the tyrosine phosphorylation of endogenous Crk-II and augments its association with p130Cas in PC-12 cells

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Melanoma Growth Stimulatory Activity Signaling through the Class II Interleukin-8 Receptor Enhances the Tyrosine Phosphorylation of Crk-Associated Substrate, p130, and a 70-Kilodalton Protein

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin.

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

A ras-related gene with transformation suppressor activity

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Coassociation of Rap1A and Ha-Ras with Raf-1 N-terminal region interferes with ras-dependent activation of Raf-1

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Downstream of Crk adaptor signaling pathway: activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G.

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

JNK is involved in signal integration during costimulation of T lymphocytes.

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

T cell receptor- and beta 1 integrin-mediated signals synergize to induce tyrosine phosphorylation of focal adhesion kinase (pp125FAK) in human T cells

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Lymphocyte antigen receptor activation of a focal adhesion kinase-related tyrosine kinase substrate

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https://api.crossref.org/works/10.1074%2FJBC.273.11.6446

21 January 2018

Identifiers

10.1074/JBC.273.11.6446

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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