Modification of the function of pertussis toxin substrate GTP-binding protein by cholera toxin-catalyzed ADP-ribosylation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
1. G protein involvement in receptor-effector coupling.
2. Islet-activating protein, pertussis toxin: a probe for functions of the inhibitory guanine nucleotide regulatory component of adenylate cyclase
3. The GTPase superfamily: a conserved switch for diverse cell functions
4. Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site.
5. Identification of sites for alkylation byN-ethylmaleimide and pertussis toxin-catalyzed ADP-ribosylation on GTP-binding proteins
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1. The Inhibitory G Protein Gi Identified as Pertussis Toxin-Catalyzed ADP-Ribosylation;Biological and Pharmaceutical Bulletin;2012
2. Human Gs mutant causes pseudohypoparathyroidism type Ia/neonatal diarrhea, a potential cell-specific role of the palmitoylation cycle;Proceedings of the National Academy of Sciences;2007-10-25
3. PTH-dependent adenylyl cyclase activation in SaOS-2 cells: Passage dependent effects on G protein interactions;Journal of Cellular Physiology;2002-08-15
4. Enhanced fMLP-stimulated chemotaxis in human neutrophils from individuals carrying the G protein β3 subunit 825 T-allele;FEBS Letters;1998-10-02
5. Conditional activation defect of a human Gs mutant;Proceedings of the National Academy of Sciences;1997-05-27
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