Phosphorylation of p125FAK and paxillin focal adhesion proteins in src-transformed cells with different metastatic capacity. - Wikidata - wikimedia - TriplyDB

Phosphorylation of p125FAK and paxillin focal adhesion proteins in src-transformed cells with different metastatic capacity.

Phosphorylation of p125FAK and paxillin focal adhesion proteins in src-transformed cells with different metastatic capacity.

http://www.wikidata.org/entity/Q40938673

about

Macrophage motility requires distinct α5β1/FAK and α4β1/paxillin signaling events Distinct roles for paxillin and Hic-5 in regulating breast cancer cell morphology, invasion, and metastasis.Knockdown of WAVE3 impairs HGF induced migration and invasion of prostate cancer cells Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility.Neural Wiskott-Aldrich syndrome protein (nWASP) is implicated in human lung cancer invasion Diverse roles for the paxillin family of proteins in cancer.Elevated c-Src is linked to altered cell-matrix adhesion rather than proliferation in KM12C human colorectal cancer cells.Src kinase contributes to the metastatic spread of carcinoma cells.c-Src and HSP72 interact in ATP-depleted renal epithelial cells.Focal adhesion kinase functions as an akt downstream target in migration of colorectal cancer cells.v-Src rescues actin-based cytoskeletal architecture and cell motility and induces enhanced anchorage independence during oncogenic transformation of focal adhesion kinase-null fibroblasts.Epithelial cell spreading induced by hepatocyte growth factor influences paxillin protein synthesis and posttranslational modification.

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P2860

Phosphorylation of p125FAK and paxillin focal adhesion proteins in src-transformed cells with different metastatic capacity.

http://www.wikidata.org/entity/Q40938673

description

1999 nî lūn-bûn

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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1999年论文

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1999年论文

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name

Phosphorylation of p125FAK and ...... different metastatic capacity.

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type

label

Phosphorylation of p125FAK and ...... different metastatic capacity.

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prefLabel

Phosphorylation of p125FAK and ...... different metastatic capacity.

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Phosphorylation of p125FAK and ...... different metastatic capacity.

@en

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Kreuser ED

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Musatkina E

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Rodina A

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Schramm K

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

Tatosyan A

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Tavitian A

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

P2860

Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases

Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases

Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases.

pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

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.

Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice

Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.

Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK.

Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin

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145-148

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10.1016/S0014-5793(99)00794-2

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1-2

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12870236

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10428489

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phosphorylation