Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS. - Wikidata - wikimedia - TriplyDB

Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS.

Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS.

http://www.wikidata.org/entity/Q30424126

about

Roles of paxillin family members in adhesion and ECM degradation coupling at invadosomes MEKK2 regulates paxillin ubiquitylation and localization in MDA-MB 231 breast cancer cells.Interactions between E6, FAK, and GIT1 at paxillin LD4 are necessary for transformation by bovine papillomavirus 1 E6 Annexin A1, formyl peptide receptor, and NOX1 orchestrate epithelial repair.GIT1 promotes lung cancer cell metastasis through modulating Rac1/Cdc42 activity and is associated with poor prognosis.Cbl-b promotes cell detachment via ubiquitination of focal adhesion kinase mTORC2 regulates mechanically induced cytoskeletal reorganization and lineage selection in marrow-derived mesenchymal stem cells.Paxillin: a crossroad in pathological cell migration The adaptor protein and Arf GTPase-activating protein Cat-1/Git-1 is required for cellular transformation.Cool-associated Tyrosine-phosphorylated Protein 1 Is Required for the Anchorage-independent Growth of Cervical Carcinoma Cells by Binding Paxillin and Promoting AKT Activation.Association of papillomavirus E6 proteins with either MAML1 or E6AP clusters E6 proteins by structure, function, and evolutionary relatedness.

P2860

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P2860

Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS.

http://www.wikidata.org/entity/Q30424126

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Paxillin enables attachment-in ...... ase and transformation by RAS.

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Paxillin enables attachment-in ...... ase and transformation by RAS.

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type

label

Paxillin enables attachment-in ...... ase and transformation by RAS.

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Paxillin enables attachment-in ...... ase and transformation by RAS.

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prefLabel

Paxillin enables attachment-in ...... ase and transformation by RAS.

@ast

Paxillin enables attachment-in ...... ase and transformation by RAS.

@en

P1433

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P356

JBC.M111.294504

P1433

Journal of Biological Chemistry

P1476

Paxillin enables attachment-in ...... ase and transformation by RAS.

@en

P2093

Charles Lyons

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

Nicole Brimer

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

Ramon Wade

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

Scott Vande Pol

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

P2860

Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate

Smad7 is inactivated through a direct physical interaction with the LIM protein Hic-5/ARA55

Association of Bovine Papillomavirus Type 1 E6 oncoprotein with the focal adhesion protein paxillin through a conserved protein interaction motif

Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence

Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase

Paxillin comes of age

Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding.

Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling.

Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion

GIT1 Paxillin-binding Domain Is a Four-helix Bundle, and It Binds to Both Paxillin LD2 and LD4 Motifs

P304

37932-37944

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scholarly article

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10.1074/JBC.M111.294504

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44

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286

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2011-09-07T00:00:00Z

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P698

21900245

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P921

phosphorylation

P932

3207406

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