| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In the present study , beta 3 cytoplasmic domain deletion and substitution mutants were constructed to identify amino acids within the integrin beta 3 cytoplasmic domain that regulate its ability to trigger FAK phosphorylation . ^^^ |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| OBJECTIVE : To observe the effects of transforming growth factors beta 1 ( TGF beta 1 ) on the expression of integrin beta 3 and the activity of focal adhesion kinase ( FAK ) . ^^^ CONCLUSION : The expression of integrin beta 3 and the activity of FAK on EC were regulated by TGF beta 1 , and this regulation may be important in cell adherence , angiogenesis , and in the pathophysiology of atherosclerosis . . ^^^ |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| A comparison of gene expression profiles of primary tumors and lung metastatic focus between salvicine treated and untreated groups using the CLOTECH Atlas human Cancer 1 . 2 cDNA microarray revealed that genes involved in tumor metastasis , particularly those closely related to cell adhesion and motility , were obviously down regulated , including fibronectin , integrin alpha 3 , integrin beta 3 , integrin beta 5 , FAK , paxillin , and RhoC . ^^^ |
|
| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In turn , phosphorylation of Ser 732 would change the conformation of FAK , making it accessible to Pyk 2 activated in response to its association with integrin beta 3 . ^^^ |
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| Interacting proteins: P05106 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In the present study , we investigated if these results were related to changes in the mobilization of intracellular calcium , activation of phospholipase D ( PLD ) or amounts of GPIIIa and the intracellular tyrosine kinases Fak , Syk , Grb 2 , Shc and rhoA . ^^^ |
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