Posttranslational Modification of Proteins by ADP-ribosylation
Description:
This work presents the development of a highly sensitive and selective chemical assay for mono(ADP-ribose) residues covalently bound to proteins in vivo. An extensive review of the literature is presented in the introduction of this work. The physiological.functions of mono(ADP-ribosyl)transferase activities associated with certain bacterial toxins (e.g., diphtheria, cholera and pertussis toxins) are well established. However, the roles of endogenous vertebrate transferases are unknown. The elu…
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Date:
December 1984
Creator:
Payne, David M. (David Michael)
Partner:
UNT Libraries