How do the GTPases really work?
- 1 January 1995
- journal article
- editorial
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 2 (1) , 3-6
- https://doi.org/10.1038/nsb0195-3
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteinsNature Structural & Molecular Biology, 1995
- Probing the Structure and Mechanism of Ras Protein with an Expanded Genetic CodeScience, 1993
- 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
- Refined structure of elongation factor EF-Tu from Escherichia coliJournal of Molecular Biology, 1992
- Substitution of histidine-84 and the GTPase mechanism of elongation factor TuBiochemistry, 1991
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- The GTPase superfamily: a conserved switch for diverse cell functionsNature, 1990
- Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch moleculesCell, 1990
- The Mechanism of Guanosine Nucleotide Hydrolysis by p21 c-Ha-rasJournal of Biological Chemistry, 1989
- Biological and biochemical properties of human rasH genes mutated at codon 61Cell, 1986