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Article

Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases

1 Jun 1998

Abstract excerpt

Sites of base loss in DNA arise spontaneously, are induced by damaging agents or are generated by DNA glycosylases. Repair of these potentially mutagenic or lethal lesions is carried out by apurinic/apyrimidinic (AP) endonucleases. To test current models of AP site recognition, we examined the effects of site-specific DNA structural modifications and an F266A mutation on incision and protein-DNA complex formation...

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PMID: 9592167
DOI: 10.1093/nar/26.11.2771

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleasesPMID 9592167Read ↗

Mutations in the alpha8 loop of human APE1 alter binding and cleavage of DNA containing an abasic site.Semantic proximity Read ↗

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Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III.Semantic proximity Read ↗

Structural comparison of AP endonucleases from the exonuclease III family reveals new amino acid residues in human AP endonuclease 1 that are involved in incision of damaged DNA.Semantic proximity Read ↗

Pre-steady-state kinetic and mutational insights into mechanisms of endo- and exonuclease DNA processing by mutant forms of human AP endonuclease.Semantic proximity Read ↗

Lys98 substitution in human AP endonuclease 1 affects the kinetic mechanism of enzyme action in base excision and nucleotide incision repair pathways.Semantic proximity Read ↗

Uracil in duplex DNA is a substrate for the nucleotide incision repair pathway in human cellsSemantic proximity Read ↗

Modulation of the Apurinic/Apyrimidinic Endonuclease Activity of Human APE1 and of Its Natural Polymorphic Variants by Base Excision Repair Proteins.Semantic proximity Read ↗

DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected].Semantic proximity Read ↗

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