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Melikishvili et al (2017) Transcriptome-wide identification of the RNA-binding landscape of the chromatin-associated protein PARP1 reveals functions in RNA biogenesis. Cell Discov. 3 17043 PMID: 29387452
De Vos et al (2014) Poly(ADP-ribose) Polymerase 1 (PARP1) Associates with E3 Ubiquitin-Protein Ligase UHRF1 and Modulates UHRF1 Biological Functions. J. Biol. Chem. 289(23) 16223 PMID: 24782312
Amino acids 487-496 of Poly(ADP-ribose) polymerase 1 (PARP1). PARP1 is a nuclear DNA repair enzyme that binds to DNA when damage is detected. PARP1 coordinates double and single strand break repair by first cleaving NAD+ into nicotinamide and ADP-ribose, and then synthesising poly-(ADP-ribose) (PAR) chains from ADP-ribose on target proteins (PARylation). PARylation of histone proteins mediates relaxation of the chromatin and recruitment of DNA-break repair enzymes.
PARP1 can also act as a transcriptional co-activator, modulating the expression of itself and many other genes by direct binding to or PARylation of enhancers and promoters. PARP1 is also involved in maintaining mtDNA.
PARP1 belongs to the PARP family which has 7 known and 10 putative members. PARP1 accounts for >85% of the PARP activity in cellular systems
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