Extracellular domain dependence of PTPalpha transforming activity

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http://www.wikidata.org/entity/Q36926645

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

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2010年論文

@zh-tw

2010年论文

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2010年论文

@zh

2010年论文

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name

Extracellular domain dependence of PTPalpha transforming activity

@en

type

Item

label

Extracellular domain dependence of PTPalpha transforming activity

@en

prefLabel

Extracellular domain dependence of PTPalpha transforming activity

@en

P1476

Extracellular domain dependence of PTPalpha transforming activity

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P2093

Barbara Tremper-Wells

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David Shalloway

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Leslie J Holsinger

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Ross J Resnick

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Xinmin Zheng

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P2860

Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn

A phosphotyrosine displacement mechanism for activation of Src by PTPalpha

Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation

Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase

Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo

Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain

Structural diversity and evolution of human receptor-like protein tyrosine phosphatases

Cloning and expression of a widely expressed receptor tyrosine phosphatase

Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains

Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase

P304

711-724

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P31

scholarly article

P356

10.1111/J.1365-2443.2010.01410.X

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P433

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P478

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P577

2010-06-07T00:00:00Z

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P5875

44671013

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P698

20545765

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P932

4876864

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