ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control.
ADP-ribose (ADPR)
ADP-ribose hydrolase (ARH)
ADP-ribosyl transferase (ART)
macro-domain (MACRO)
poly ADP-ribose glycohydrolase (PARG)
poly ADP-ribose polymerase (PARP)
sirtuin (SIRT)
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
07 Oct 2021
07 Oct 2021
Historique:
received:
12
09
2021
revised:
02
10
2021
accepted:
05
10
2021
entrez:
13
10
2021
pubmed:
14
10
2021
medline:
26
10
2021
Statut:
epublish
Résumé
Among the post-translational modifications of proteins, ADP-ribosylation has been studied for over fifty years, and a large set of functions, including DNA repair, transcription, and cell signaling, have been assigned to this post-translational modification (PTM). This review presents an update on the function of a large set of enzyme writers, the readers that are recruited by the modified targets, and the erasers that reverse the modification to the original amino acid residue, removing the covalent bonds formed. In particular, the review provides details on the involvement of the enzymes performing monoADP-ribosylation/polyADP-ribosylation (MAR/PAR) cycling in cancers. Of note, there is potential for the application of the inhibitors developed for cancer also in the therapy of non-oncological diseases such as the protection against oxidative stress, the suppression of inflammatory responses, and the treatment of neurodegenerative diseases. This field of studies is not concluded, since novel enzymes are being discovered at a rapid pace.
Identifiants
pubmed: 34639169
pii: ijms221910829
doi: 10.3390/ijms221910829
pmc: PMC8509805
pii:
doi:
Substances chimiques
Poly(ADP-ribose) Polymerase Inhibitors
0
Poly Adenosine Diphosphate Ribose
26656-46-2
Poly (ADP-Ribose) Polymerase-1
EC 2.4.2.30
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
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