Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes. - Wikidata - awgldk - TriplyDB

Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes.

Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes.

http://www.wikidata.org/entity/Q41083153

about

SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates Analysis of a Shc family adaptor protein, ShcD/Shc4, that associates with muscle-specific kinase The src homology domain 2-containing inositol phosphatase SHIP forms a ternary complex with Shc and Grb2 in antigen receptor-stimulated B lymphocytes A key role for the phosphorylation of Ser440 by the cyclic AMP-dependent protein kinase in regulating the activity of the Src homology 2 domain-containing Inositol 5'-phosphatase (SHIP1).FcγRIIB-Independent Mechanisms Controlling Membrane Localization of the Inhibitory Phosphatase SHIP in Human B Cells.Regulation of immune cell signaling by SHIP1: A phosphatase, scaffold protein, and potential therapeutic target.Negative regulation of chemokine receptor signaling and B-cell chemotaxis by p66Shc.Distribution of the src-homology-2-domain-containing inositol 5-phosphatase SHIP-2 in both non-haemopoietic and haemopoietic cells and possible involvement of SHIP-2 in negative signalling of B-cells.

P2860

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P2860

Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes.

http://www.wikidata.org/entity/Q41083153

description

1997 nî lūn-bûn

@nan

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

1997年论文

@zh

1997年论文

@zh-cn

name

Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes.

@en

type

label

Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes.

@en

prefLabel

Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes.

@en

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P356

(SICI)1097-4644(19971001)67:1%3C32::AID-JCB4%3E3.0.CO;2-X

P1433

Journal of Cellular Biochemistry

P1476

Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes.

@en

P2093

K M Coggeshall

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M Pradhan

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P2860

The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions

p21ras activation via hemopoietin receptors and c-kit requires tyrosine kinase activity but not tyrosine phosphorylation of p21ras GTPase-activating protein

The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase

SH2 domains recognize specific phosphopeptide sequences

Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals

p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity

Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4

Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2

Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP

Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4

P304

32-42

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P31

scholarly article

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10.1002/(SICI)1097-4644(19971001)67:1<32::AID-JCB4>3.0.CO;2-X

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1

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67

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1997-10-01T00:00:00Z

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9328837

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