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- W2771043670 endingPage "1136" @default.
- W2771043670 startingPage "1092" @default.
- W2771043670 abstract "Posttranslational modifications (PTMs) regulate protein functions and interactions. ADP-ribosylation is a PTM, in which ADP-ribosyltransferases use nicotinamide adenine dinucleotide (NAD+) to modify target proteins with ADP-ribose. This modification can occur as mono- or poly-ADP-ribosylation. The latter involves the synthesis of long ADP-ribose chains that have specific properties due to the nature of the polymer. ADP-Ribosylation is reversed by hydrolases that cleave the glycosidic bonds either between ADP-ribose units or between the protein proximal ADP-ribose and a given amino acid side chain. Here we discuss the properties of the different enzymes associated with ADP-ribosylation and the consequences of this PTM on substrates. Furthermore, the different domains that interpret either mono- or poly-ADP-ribosylation and the implications for cellular processes are described." @default.
- W2771043670 created "2017-12-04" @default.
- W2771043670 creator A5007105384 @default.
- W2771043670 creator A5025243974 @default.
- W2771043670 creator A5041462448 @default.
- W2771043670 creator A5068273379 @default.
- W2771043670 creator A5077679932 @default.
- W2771043670 creator A5089487002 @default.
- W2771043670 date "2017-11-27" @default.
- W2771043670 modified "2023-10-17" @default.
- W2771043670 title "ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease" @default.
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