ADPribosylaa

ADPribosylaa is not a widely established term in the scientific literature. It appears to be a variant or misspelling related to ADP-ribosylation, a common post-translational modification in which ADP-ribose units are transferred from nicotinamide adenine dinucleotide (NAD+) to target molecules. The standard terminology uses “ADP-ribosylation” or “ADP-ribosyltransferase” to describe the enzymes that catalyze the reaction and the modification itself.

Mechanistically, ADP-ribosylation is carried out by ADP-ribosyltransferases, including the mono-ADP-ribosyltransferases (MARTs) and the poly(ADP-ribose) polymerases (PARPs). MARylation adds a single ADP-ribose unit to specific amino acid residues on target proteins, while PARylation builds long chains of ADP-ribose. In cells, PARP family members respond to DNA damage and other stresses by synthesizing poly(ADP-ribose) chains that help recruit repair factors. Bacterial toxins also exploit ADP-ribosylation to modify host proteins and disrupt signaling pathways.

Biological roles of ADP-ribosylation are diverse. It participates in DNA damage repair, chromatin remodeling, transcriptional regulation, and stress responses. Substrates include various amino acid residues on proteins (such as arginine, serine, and others) and, in some systems, nucleic acids. Reversal is accomplished by hydrolases and macrodomain-containing enzymes, restoring the original state after signaling or damage responses.

clinically, PARP inhibitors are used to treat certain cancers by interfering with PARP-mediated DNA repair. The terminology surrounding ADPribosylaa is not standard, and readers are advised to refer to ADP-ribosylation and related enzymes for precise definitions.