Ontology highlight
ABSTRACT:
SUBMITTER: Lebedeva NA
PROVIDER: S-EPMC7833210 | biostudies-literature | 2020
REPOSITORIES: biostudies-literature
Lebedeva Natalia A NA Rechkunova Nadejda I NI Endutkin Anton V AV Lavrik Olga I OI
Frontiers in cell and developmental biology 20210111
Bifunctional 8-oxoguanine-DNA glycosylase (OGG1), a crucial DNA-repair enzyme, removes from DNA 8-oxo-7,8-dihydroguanine (8-oxoG) with following cleavage of the arising apurinic/apyrimidinic (AP) site. The major enzyme in eukaryotic cells that catalyzes the cleavage of AP sites is AP endonuclease 1 (APE1). Alternatively, AP sites can be cleaved by tyrosyl-DNA phosphodiesterase 1 (TDP1) to initiate APE1-independent repair, thus expanding the ability of the base excision repair (BER) process. Poly ...[more]