Electrostatic control of GTP and GDP binding in the oncoprotein p21ras
- 30 April 1996
- journal article
- Published by Elsevier BV in Structure
- Vol. 4 (4), 475-489
- https://doi.org/10.1016/s0969-2126(96)00052-4
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteinsNature Structural & Molecular Biology, 1995
- Signal transduction pathways involving RASCellular Signalling, 1994
- Proteins regulating Ras and its relativesNature, 1993
- FUNCTION AND REGULATION OF RASAnnual Review of Biochemistry, 1993
- On the mechanism of guanosine triphosphate hydrolysis in ras p21 proteinsBiochemistry, 1992
- Identification of murine homologues of the Drosophila son of sevenless gene: potential activators of ras.Proceedings of the National Academy of Sciences of the United States of America, 1992
- The GTPase superfamily: a conserved switch for diverse cell functionsNature, 1990
- A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic MutantsScience, 1987
- ras GENESAnnual Review of Biochemistry, 1987
- The S. cerevisiae CDC25 gene product regulates the RAS/adenylate cyclase pathwayCell, 1987