Titlebook: Endogenous ADP-Ribosylation; Friedrich Koch-Nolte Book 2015 The Editor(s) (if applicable) and The Author(s), under exclusive license to Sp

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https://doi.org/10.1007/978-3-319-01053-3e human enzymes that catalyze the reaction have been rounded up. Moreover, substrate proteins and specific functions for mono-ADP-ribosyltransferases are beginning to be defined. Reader domains that specifically recognize mono-ADP-ribosylated target proteins and erasers that remove the mono-ADP-ribo

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Mathematical Modelling of Granular Materials While many studies have addressed the function of poly-ADP-ribosylation, for example, in DNA repair, signaling, and gene transcription, little is known about the role of mono-ADP-ribosylation. Recent work describing the mono-ADP-ribosyltransferase ARTD10/PARP10 suggests that this enzyme affects apo

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https://doi.org/10.1007/978-3-030-40045-3f its nicotinamide moiety. This is accompanied by the transfer of a single (mono-) or several (poly-) ADP-ribose molecules from NAD . to a specific amino-acid residue of the protein. Recent reports have shed new light on the correlation between NAD . -dependent ADP-ribosylation reactions

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Regulation of Nitrogenase by Reversible Mono-ADP-Ribosylation,ibosylation was first described as a mechanism of action of bacterial toxins. Since these pioneering studies, the number of pathways regulated by ADP-ribosylation in organisms from all domains of life expanded significantly. However, in only a few cases the full regulatory ADP-ribosylation circuit i