The Mechanism of GTP Hydrolysis by Ras Probed by Fourier Transform Infrared Spectroscopy
Open Access
- 1 March 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (12) , 8492-8500
- https://doi.org/10.1074/jbc.275.12.8492
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras MutantsScience, 1997
- Ras-catalyzed hydrolysis of GTP: a new perspective from model studies.Proceedings of the National Academy of Sciences, 1996
- Mechanistic Analysis of the Observed Linear Free Energy Relationships in p21ras and Related SystemsBiochemistry, 1996
- Ras target proteins in eukaryotic cellsThe FASEB Journal, 1995
- Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteinsNature Structural & Molecular Biology, 1995
- Simulation of the solution structure of the H-ras p21-GTP complexBiochemistry, 1992
- X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.Proceedings of the National Academy of Sciences, 1992
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- The GTPase superfamily: a conserved switch for diverse cell functionsNature, 1990
- Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.Proceedings of the National Academy of Sciences, 1990