The Role of Tyrosine Phosphorylation of Cortactin in the Locomotion of Endothelial Cells (Q28283364)

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10 January 2025

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C. Huang

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J. Liu

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C. C. Haudenschild

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X. Zhan

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publication date

2 October 1998

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language of work or name

English

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work available at URL

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https://syndication.highwire.org/content/doi/10.1074/jbc.273.40.25770

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Journal of Biological Chemistry

10 January 2025

published in

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volume

273

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issue

40

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page(s)

25770-6

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cites work

Tyrosine phosphorylation of p130Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix

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Mechanical strain induces pp60src activation and translocation to cytoskeleton in fetal rat lung cells

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Identification and characterization of a novel cytoskeleton-associated pp60src substrate

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Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex

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Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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FGF-1-dependent proliferative and migratory responses are impaired in senescent human umbilical vein endothelial cells and correlate with the inability to signal tyrosine phosphorylation of fibroblast growth factor receptor-1 substrates

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Role of tyrosine phosphorylation of HS1 in B cell antigen receptor-mediated apoptosis

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Physical and functional association of cortactin with Syk in human leukemic cell line K562

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Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3.

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Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates

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