Modulation of the Catalytic Activity of the Src Family Tyrosine Kinase Hck by Autophosphorylation at a Novel Site in the Unique Domain
Open Access
- 1 October 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (43) , 33353-33364
- https://doi.org/10.1074/jbc.m002022200
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Common in Vitro Substrate Specificity and Differential Src Homology 2 Domain Accessibility Displayed by Two Members of the Src Family of Protein-tyrosine Kinases, c-Src and HckPublished by Elsevier ,1998
- The 2.35 å crystal structure of the inactivated form of chicken src: a dynamic molecule with multiple regulatory interactionsJournal of Molecular Biology, 1997
- CELLULAR FUNCTIONS REGULATED BY SRC FAMILY KINASESAnnual Review of Cell and Developmental Biology, 1997
- Common and differential recognition of structural features in synthetic peptides by the catalytic domain and the Src‐Homology 2 (SH2) domain of pp60c‐srcChemical Biology & Drug Design, 1997
- Crystal structure of the Src family tyrosine kinase HckNature, 1997
- Three-dimensional structure of the tyrosine kinase c-SrcNature, 1997
- SH2 domains recognize specific phosphopeptide sequencesPublished by Elsevier ,1993
- Immunological detection of phospholamban phosphorylation states facilitates the description of the mechanism of phosphorylation and dephosphorylationBiochemistry, 1990
- Mitosis-specific phosphorylation of p60c-src by p34cdc2-associated protein kinaseCell, 1989
- CSF-1 stimulates Na+K+-ATPase mediated 86Rb+ uptake in mouse bone marrow-derived macrophagesBiochemical and Biophysical Research Communications, 1985