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- W1447005185 abstract "The toxins alter the activity of the guanine nucleotide-binding proteins (G proteins) by catalyzing the transfer of the ADP-ribose moiety of NAD to a critical amino acid in the a subunit. This ADP-ribosylation reaction results in either activation (e.g., cholera toxin, E. coli heat-labile enterotoxin) or inactivation (e.g., pertussis toxin) of the G protein. The G proteins are heterotrimeric signal-transducing proteins responsible for coupling cell-surface receptors to their intracellular effectors. Cholera toxin and E. coli heat-labile enterotoxins catalyze the ADP-ribosylation of the α-subunit of Gs, the stimulatory G protein of the adenylylcyclase system that is also believed to regulate Ca2+ channels. ADP-ribosylation by pertussis toxin of the Gαi, Gαo, and Gαt proteins on a cysteine residue near the carboxy terminus interferes with their ability to interact functionally with cell-surface receptors, thereby interrupting transmembrane signalling. In addition to these proteins, there is a family of Gα subunits that appear not to be substrates for any of these bacterial toxins." @default.
- W1447005185 created "2016-06-24" @default.
- W1447005185 creator A5014520949 @default.
- W1447005185 creator A5048042168 @default.
- W1447005185 date "1993-01-01" @default.
- W1447005185 modified "2023-10-11" @default.
- W1447005185 title "ADP-ribosylation Factors Protein Activators of Cholera Toxin" @default.
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- W1447005185 doi "https://doi.org/10.1016/s0079-6603(08)60866-1" @default.
- W1447005185 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8341803" @default.
- W1447005185 hasPublicationYear "1993" @default.
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