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- W367054555 abstract "In eukaryotes, DNA strand breaks introduced either directly by ionizing radiations or indirectly following enzymatic incision of a DNA-base lesion trigger immediately the synthesis of poly(ADP-ribose) by the enzyme poly(ADP-ribose) polymerase (PARP; EC 2.4.2.30). At a site of breakage, PARP catalyzes the transfer of the ADP-ribose moiety from its substrate, NAD+, to a limited number of protein acceptors (heteromodification) involved in chromatin architecture (histones H1, H2B, lamin B) or in DNA metabolism (topoisomerases, DNA replication factors) including PARP itself (automodification) (for reviews see Althaus and Richter 1987; Lautier et al. 1993; Oei et al. 1997). These modified proteins, mainly DNA-binding proteins, carrying chains of negatively charged ADP-ribose polymers, lose their affinity for DNA and consequently are inactivated. The short half-life of the polymer is attributed to the high activity of poly(ADP-ribose) glycohydrolase (PARG) which cleaves the ribose-ribose bond (Alvarez-Gonzalez and Althaus 1989; Lin et al. 1997). Poly(ADP-ribosylation) is therefore an immediate and transient posttranslational modification of nuclear proteins induced by DNA strand breaks (Fig. 1A)." @default.
- W367054555 created "2016-06-24" @default.
- W367054555 creator A5034169747 @default.
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- W367054555 creator A5087610351 @default.
- W367054555 date "1998-01-01" @default.
- W367054555 modified "2023-09-25" @default.
- W367054555 title "Poly(ADP-Ribose) Polymerase Is Required for Maintenance of Genomic Integrity During Base Excision Repair" @default.
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