Structural Basis for Relief of Autoinhibition of the Dbl Homology Domain of Proto-Oncogene Vav by Tyrosine Phosphorylation
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Open Access
- 1 September 2000
- Vol. 102 (5), 625-633
- https://doi.org/10.1016/s0092-8674(00)00085-4
Abstract
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This publication has 55 references indexed in Scilit:
- Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptorCurrent Biology, 1998
- Significantly Improved Resolution for NOE Correlations from Valine and Isoleucine (Cγ2) Methyl Groups in 15N,13C- and 15N,13C,2H-Labeled ProteinsJournal of the American Chemical Society, 1998
- Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin 1 1Edited by P. E. WrightJournal of Molecular Biology, 1997
- AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMRJournal of Biomolecular NMR, 1996
- Investigation of the GTP-Binding/GTPase Cycle of Cdc42Hs Using Extrinsic Reporter Group FluorescenceBiochemistry, 1996
- The VAV Family of Signal Transduction MoleculesCritical Reviews™ in Oncogenesis, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Site specificity of p72syk protein tyrosine kinase: efficient phosphorylation of motifs recognized by Src homology 2 domains of the Src familyFEBS Letters, 1995
- SH2 domains recognize specific phosphopeptide sequencesCell, 1993
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991