Peptide mapping of fat cell membrane substrates for cholera toxin-catalyzed ADP-ribosylation
- 25 February 1982
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - General Subjects
- Vol. 714 (3), 429-434
- https://doi.org/10.1016/0304-4165(82)90150-7
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Genetic evidence that cholera toxin substrates are regulatory components of adenylate cyclase.Journal of Biological Chemistry, 1978
- Mechanism of adenylate cyclase activation through the beta-adrenergic receptor: catecholamine-induced displacement of bound GDP by GTP.Proceedings of the National Academy of Sciences, 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
- Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase systemProceedings of the National Academy of Sciences, 1978
- GTP stimulates and inhibits adenylate cyclase in fat cell membranes through distinct regulatory processes.Journal of Biological Chemistry, 1977
- GTP-binding proteins in membranes and the control of adenylate cyclase activity.Journal of Biological Chemistry, 1977
- Reconstitution of catecholamine-sensitive adenylate cyclase activity: interactions of solubilized components with receptor-replete membranes.Proceedings of the National Academy of Sciences, 1977
- Influence of cholera toxin on the regulation of adenylate cyclase by GTPBiochemical and Biophysical Research Communications, 1977
- METABOLISM OF ISOLATED FAT CELLS .I. EFFECTS OF HORMONES ON GLUCOSE METABOLISM + LIPOLYSIS1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951