Switching Nucleotide Specificity of Ha-Ras p21 by a Single Amino Acid Substitution at Aspartate 119
Open Access
- 1 April 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (17) , 10002-10007
- https://doi.org/10.1074/jbc.270.17.10002
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Mutagenesis of the H-ras p21 at glycine-60 residue disrupts GTP-induced conformational changeBiochemistry, 1995
- Elongation Factor Tu D138N, a Mutant with Modified Substrate Specificity, as a Tool To Study Energy Consumption in Protein BiosynthesisBiochemistry, 1994
- Phosphatidylinositol-3-OH kinase direct target of RasNature, 1994
- Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?Trends in Biochemical Sciences, 1994
- Proteins regulating Ras and its relativesNature, 1993
- Complexes of Ras⋅GTP with Raf-1 and Mitogen-Activated Protein Kinase KinaseScience, 1993
- Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDPJournal of Molecular Biology, 1991
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- Enhancement of the GDP-GTP Exchange of RAS Proteins by the Carboxyl-Terminal Domain of SCD25Science, 1990
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978