pHocal adhesion kinase regulation is on a FERM foundation. - Wikidata - wikimedia - TriplyDB

pHocal adhesion kinase regulation is on a FERM foundation.

pHocal adhesion kinase regulation is on a FERM foundation.

http://www.wikidata.org/entity/Q37180585

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pHocal adhesion kinase regulation is on a FERM foundation.

http://www.wikidata.org/entity/Q37180585

description

article científic

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article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

pHocal adhesion kinase regulation is on a FERM foundation.

@en

pHocal adhesion kinase regulation is on a FERM foundation.

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pHocal adhesion kinase regulation is on a FERM foundation.

@en

pHocal adhesion kinase regulation is on a FERM foundation.

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prefLabel

pHocal adhesion kinase regulation is on a FERM foundation.

@en

pHocal adhesion kinase regulation is on a FERM foundation.

@nl

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Journal of Cell Biology

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pHocal adhesion kinase regulation is on a FERM foundation.

@en

P2093

Christine Lawson

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

David D Schlaepfer

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

P2860

Phosphorylation of focal adhesion kinase on tyrosine 194 by Met leads to its activation through relief of autoinhibition

FAK promotes recruitment of talin to nascent adhesions to control cell motility

Structural basis for the autoinhibition of focal adhesion kinase

Cortactin as a target for FAK in the regulation of focal adhesion dynamics

Alternative splicing controls the mechanisms of FAK autophosphorylation

Direct binding of the Na--H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation

Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding

Focal adhesion kinase: the first ten years

Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration.

Considering protonation as a posttranslational modification regulating protein structure and function.

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833-836

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scholarly article

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10.1083/JCB.201308034

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6

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202

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2013-09-01T00:00:00Z

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256666112

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24043698

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3776349

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