Modulation of the SH2 Binding Specificity and Kinase Activity of Src by Tyrosine Phosphorylation within Its SH2 Domain
Work
Year: 1996
Type: article
Abstract: The Src family of kinases are held in an inactive state by interaction of their SH2 domain with a C-terminal phosphotyrosine. Dephosphorylation of this site can reactivate Src; however, recent evidenc... more
Source: Journal of Biological Chemistry
Institution Novartis (Switzerland)
Cites: 33
Cited by: 92
Related to: 10
FWCI: 1.029
Citation percentile (by year/subfield): 92.99
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
APC paid (est): $2,500