Abstract
Intracellular protein ADP-ribosylation is catalyzed by diphteria toxin-like ADP-ribosyltransferases (ARTDs, formerly PARPs) ("writers"), which use NAD(+) for the modification of different amino acids. While some ARTD members catalyze protein poly-ADP-ribosylation, most of them are mono-ADP-ribosyltransferases. ADP-ribosylation is recognized by protein domains ("readers") and reversed by different enzymes ("erasers"). ADP-ribosylation signaling regulates several key cellular processes during health and disease.
Copyright © 2015 Elsevier Inc. All rights reserved.
MeSH terms
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ADP Ribose Transferases / metabolism
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Adenosine Diphosphate Ribose / chemistry
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Adenosine Diphosphate Ribose / metabolism*
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Biosynthetic Pathways
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Humans
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Models, Chemical
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Molecular Structure
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NAD / metabolism
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Niacinamide / metabolism
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Poly (ADP-Ribose) Polymerase-1
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Poly Adenosine Diphosphate Ribose / chemistry
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Poly Adenosine Diphosphate Ribose / metabolism*
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Poly(ADP-ribose) Polymerases / metabolism*
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Signal Transduction*
Substances
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NAD
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Adenosine Diphosphate Ribose
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Niacinamide
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Poly Adenosine Diphosphate Ribose
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ADP Ribose Transferases
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PARP1 protein, human
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Poly (ADP-Ribose) Polymerase-1
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Poly(ADP-ribose) Polymerases