
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.
ADP Ribose Transferases, Niacinamide, Adenosine Diphosphate Ribose, Poly Adenosine Diphosphate Ribose, Molecular Structure, Poly (ADP-Ribose) Polymerase-1, Cell Biology, NAD, 10226 Department of Molecular Mechanisms of Disease, Biosynthetic Pathways, 1307 Cell Biology, Models, Chemical, 1312 Molecular Biology, 570 Life sciences; biology, Humans, Poly(ADP-ribose) Polymerases, Molecular Biology, Signal Transduction
ADP Ribose Transferases, Niacinamide, Adenosine Diphosphate Ribose, Poly Adenosine Diphosphate Ribose, Molecular Structure, Poly (ADP-Ribose) Polymerase-1, Cell Biology, NAD, 10226 Department of Molecular Mechanisms of Disease, Biosynthetic Pathways, 1307 Cell Biology, Models, Chemical, 1312 Molecular Biology, 570 Life sciences; biology, Humans, Poly(ADP-ribose) Polymerases, Molecular Biology, Signal Transduction
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