The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway
Open accessAbstract
Mutagenic abasic (AP) sites are generated directly by DNA-damaging agents or by DNA glycosylases acting in base excision repair. AP sites are corrected via incision by AP endonucleases, removal of deoxyribose 5-phosphate, repair synthesis, and ligation. Mammalian DNA polymerase β (Polβ) carries out most base excision repair synthesis and also can excise deoxyribose 5-phosphate after AP endonuclease incision. Yeast two-hybrid analysis now indicates protein–protein contact between Polβ and human AP endonuclease (Ape protein). In vitro , binding of Ape protein to uncleaved AP sites loads Polβ into a ternary complex with Ape and the AP-DNA. After incision by Ape, only Polβ exhibits stable DNA binding. Kinetic experiments indicated that Ape accelerates the excision of 5′-terminal deoxyribose 5-phosphate by Polβ. Thus, the two central players of the base excision repair pathway are coordinated in sequential reactions.
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Cites
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Cited by
DNA repair mechanisms in dividing and non-dividing cells
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Self-citationRepair of Endogenous DNA Damage
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Metadata
- Authors
- Bennett, R. A. O., Wilson, D. M., Wong, D., & Demple, B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-07-08
- Volume
- 94
- Issue
- 14
- Pages
- 7166-7169
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2064538331
- Cited by
- 349
- References
- 34
- FWCI
- 8.21
- Type
- journal article
- Language
- en
- Open access
- green
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- Bennett, R. A. O., Wilson, D. M., Wong, D., & Demple, B. (1997). Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.14.7166
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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