RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

Item

http://www.wikidata.org/entity/Q43687397

description

2001 nî lūn-bûn

@nan

2001年の論文

@ja

2001年学术文章

@wuu

2001年学术文章

@zh

2001年学术文章

@zh-cn

2001年学术文章

@zh-hans

2001年学术文章

@zh-my

2001年学术文章

@zh-sg

2001年學術文章

@yue

2001年學術文章

@zh-hant

name

RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

@en

RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

@nl

type

Item

label

RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

@en

RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

@nl

prefLabel

RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

@en

RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

@nl

P1476

RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase.

@en

P2093

E Kaczmarek

http://www.w3.org/2001/XMLSchema#string

H Avraham

http://www.w3.org/2001/XMLSchema#string

K Koziak

http://www.w3.org/2001/XMLSchema#string

S Avraham

http://www.w3.org/2001/XMLSchema#string

S Y Park

http://www.w3.org/2001/XMLSchema#string

Y Fu

http://www.w3.org/2001/XMLSchema#string

P2860

Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain

Thrombin receptors on human platelets. Initial localization and subsequent redistribution during platelet activation

RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

RAFTK/Pyk2 tyrosine kinase mediates the association of p190 RhoGAP with RasGAP and is involved in breast cancer cell invasion

PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway

Suppression of protein kinase C is associated with inhibition of PYK2 tyrosine phosphorylation and enhancement of PYK2 interaction with Src in thrombin-activated platelets.

Molecular basis for ADP-induced platelet activation. I. Evidence for three distinct ADP receptors on human platelets.

Platelet-collagen interactions.

Lipid products of phosphoinositide 3-kinase and phosphatidylinositol 4',5'-bisphosphate are both required for ADP-dependent platelet spreading.

P304

134-140

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P31

scholarly article

P356

10.1046/J.1365-2141.2001.02894.X

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

114

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P577

2001-07-01T00:00:00Z

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P5875

11870965

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P698

11472358

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