A 22 kDaras-related G-protein is the substrate for an ADP-ribosyltransferase fromClostridium botulinum
- 26 September 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 238 (1) , 22-26
- https://doi.org/10.1016/0014-5793(88)80217-5
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum.Molecular and Cellular Biology, 1988
- Botulinum ADP-ribosyltransferase C3 but not botulinum neurotoxins C1 and D ADP-ribosylates low molecular mass GTP-binding proteinsFEBS Letters, 1987
- Myristoylated alpha subunits of guanine nucleotide-binding regulatory proteins.Proceedings of the National Academy of Sciences, 1987
- ras GENESAnnual Review of Biochemistry, 1987
- ADP-ribosylation of specific membrane proteins in pheochromocytoma and primary-cultured brain cells by botulinum neurotoxins type C and DFEBS Letters, 1987
- Expression of p21ras in normal and malignant human tissues: lack of association with proliferation and malignancy.Proceedings of the National Academy of Sciences, 1987
- Identification of effector residues and a neutralizing epitope of Ha-ras-encoded p21.Proceedings of the National Academy of Sciences, 1986
- Direct identification of palmitic acid as the lipid attached to p21ras.Molecular and Cellular Biology, 1986
- G proteins and dual control of adenylate cyclaseCell, 1984
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976