The fibronectin-binding integrins alpha5beta1 and alphavbeta3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis.
Research output: Contribution to journal › Journal article › Research › peer-review
Original language | English |
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Journal | Journal of Cell Biology |
Volume | 159 |
Issue number | 6 |
Pages (from-to) | 1071-86 |
Number of pages | 15 |
ISSN | 0021-9525 |
DOIs | |
Publication status | Published - 2002 |
Bibliographical note
Keywords: Actins; Animals; Cell Adhesion; Cell Separation; DNA, Complementary; DNA-Binding Proteins; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fibrin; Fibronectins; Flow Cytometry; Focal Adhesion Kinase 1; Focal Adhesion Protein-Tyrosine Kinases; GTPase-Activating Proteins; Gene Expression Regulation; Guanine Nucleotide Exchange Factors; Guanosine Triphosphate; Humans; Integrin alpha5beta1; Integrin alphaVbeta3; Integrins; Mice; Microfilament Proteins; Microscopy, Fluorescence; Nuclear Proteins; Phenotype; Phosphoproteins; Phosphorylation; Protein Binding; Protein Structure, Tertiary; Protein-Tyrosine Kinases; Proteins; Repressor Proteins; Retinoblastoma-Like Protein p130; Time Factors; Transfection; Vinculin; rhoA GTP-Binding Protein
ID: 5141451