ADP-ribosylation by cholera toxin: functional analysis of a cellular system that stimulates the enzymic activity of cholera toxin fragment A1
- 1 October 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 26 (20), 6364-6371
- https://doi.org/10.1021/bi00394a009
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 12 references indexed in Scilit:
- A novel ras-related gene familyCell, 1985
- Regulation of protein synthesis in eukaryotes. Mode of action of eRF, an eIF-2-recycling factor from rabbit reticulocytes involved in GDP/GTP exchangeEuropean Journal of Biochemistry, 1984
- Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin.Journal of Biological Chemistry, 1984
- A second guanyl nucleotide-binding site associated with adenylate cyclase. Distinct nucleotides activate adenylate cyclase and permit ADP-ribosylation by cholera toxin.Journal of Biological Chemistry, 1983
- A GDP/GTP exchange factor essential for eukaryotic initiation factor 2 cycling in Ehrlich ascites tumor cells and its regulation by eukaryotic initiation factor 2 phosphorylation.Journal of Biological Chemistry, 1983
- Cholera toxin activation of adenylate cyclase. Roles of nucleoside triphosphates and a macromolecular factor in the ADP ribosylation of the GTP-dependent regulatory component.Journal of Biological Chemistry, 1980
- Guanine nucleotide-binding activity as an assay for src protein of rat-derived murine sarcoma virusesProceedings of the National Academy of Sciences, 1979
- Requirement for guanosine triphosphate in the activation of adenylate cyclase by cholera toxinJournal of Supramolecular Structure, 1979
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
- ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase.Proceedings of the National Academy of Sciences, 1978