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Understanding of BRCA1/2 interaction with the base excision repair (BER) pathway could improve therapy based on ‘synthetic lethality’, whose effectiveness is based on homologous recombination ...
Escherichia coli endonuclease VIII and endonuclease III are oxidative base excision repair DNA glycosylases that remove oxidized pyrimidines from DNA. The genes encoding these proteins, nei and nth ...
and potential lethality. A major DNA N-glycosylase responsible for the excision of modified pyrimidine bases is the base excision repair (BER) glycosylase endonuclease III , for which functional homologs have been ...
gene encodes the AtRAD2/XPG gene product. In humans, the homologous XPG protein is also involved in removal of oxygen‐damaged nucleotides by base excision repair. We discuss the possibility ...
, Ward CJ , Cheadle JP , Sampson JR , Lindahl T , Harris PC , Hickson ID . Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III , Proc. Natl. Acad. Sci. U.S.A ...
are removed by an ensemble of nine DNA glycosylases (7). Deinococcus radiodurans contains three homologs of endonuclease III (DR0928, DR2438 and DR0289), two of which possess both DNA glycosylase and AP lyase ...
(NHEJ) and oxidative damage to DNA is primarily coped with base excision repair (BER), a contribution of these two pathways towards survival, DSB induction, mutation frequency and types of mutations ...
Abstract Escherichia coli endonuclease VIII and endonuclease III are oxidative base excision repair DNA glycosylases that remove oxidized pyrimidines from DNA. The genes encoding these proteins, nei ...
to oxidants or ionizing radiation (1–4). An ionizing radiation-induced DNA damage, thymine glycol, is mainly repaired by the base excision repair pathway initiated by endonuclease III (Nth) in Escherichia coli ...
Abstract The Escherichia coli endonuclease III (Nth-Eco) protein is involved in the removal of damaged pyrimidine residues from DNA by base excision repair. It is an iron-sulphur enzyme possessing ...
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