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• W1994843656 startingPage "33" @default.
• W1994843656 abstract "Oxidized pyrimidines in DNA are removed by a distinct base excision repair pathway initiated by the DNA glycosylase--AP lyase hNth1 in human cells. We have reconstituted this single-residue replacement pathway with recombinant proteins, including the AP endonuclease HAP1/APE, DNA polymerase beta, and DNA ligase III-XRCC1 heterodimer. With these proteins, the nucleotide excision repair enzyme XPG serves as a cofactor for the efficient function of hNth1. XPG protein promotes binding of hNth1 to damaged DNA. The stimulation of hNth1 activity is retained in XPG catalytic site mutants inactive in nucleotide excision repair. The data support the model that development of Cockayne syndrome in XP-G patients is related to inefficient excision of endogenous oxidative DNA damage." @default.
• W1994843656 created "2016-06-24" @default.
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• W1994843656 date "1999-01-01" @default.
• W1994843656 modified "2023-10-14" @default.
• W1994843656 title "Base Excision Repair of Oxidative DNA Damage Activated by XPG Protein" @default.
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• W1994843656 doi "https://doi.org/10.1016/s1097-2765(00)80172-0" @default.
• W1994843656 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10024877" @default.
• W1994843656 hasPublicationYear "1999" @default.
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