Paxillin null embryonic stem cells are impaired in cell spreading and tyrosine phosphorylation of focal adhesion kinase (Q38292943)

1 September 2017

title

Paxillin null embryonic stem cells are impaired in cell spreading and tyrosine phosphorylation of focal adhesion kinase (English)

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1 September 2017

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Ramon Wade

1

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1 September 2017

Joanna Bohl

series ordinal

2

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1 September 2017

Scott Vande Pol

series ordinal

3

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1 September 2017

language of work or name

English

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publication date

1 January 2002

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1 September 2017

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1 September 2017

volume

21

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1 September 2017

issue

1

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1 September 2017

page(s)

96-107

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Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts

1 September 2017

cites work

1 reference

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Paxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeleton

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Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions

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Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase

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Integrins regulate the association and phosphorylation of paxillin by c-Abl

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Leupaxin is a novel LIM domain protein that forms a complex with PYK2

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Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses

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'Green mice' as a source of ubiquitous green cells.

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Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells

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inferred from DOI database lookup

7 January 2021

based on heuristic

The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase

1 reference

https://api.crossref.org/works/10.1038/SJ.ONC.1205013

inferred from DOI database lookup

7 January 2021

based on heuristic

54 Embryonic stem cell differentiation in vitro

1 reference

https://api.crossref.org/works/10.1038/SJ.ONC.1205013

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/SJ.ONC.1205013

1 reference

Dimensions Publication ID

1 September 2017

1031233256

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1 reference