ArticleBiomolecular NMR assignments2010
Chemical shift assignments for human apurinic/apyrimidinic endonuclease 1.
Article in Biomolecular NMR assignments, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Live-cell decoding of labile post-translational modifications in APE1 with a rationally engineered nano-catcher.Nucleic acids research · 2026Article
- Chemically induced partial unfolding of the multifunctional apurinic/apyrimidinic endonuclease 1.Protein science : a publication of the Protein Society · 2025Review
- Characterizing inhibitors of human AP endonuclease 1.PloS one · 2023Article
- Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues.Nucleic acids research · 2016Article
- Thymine DNA glycosylase exhibits negligible affinity for nucleobases that it removes from DNA.Nucleic acids research · 2015Article
- Structure of human apurinic/apyrimidinic endonuclease 1 with the essential Mg2+ cofactor.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Coordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions.DNA repair · 2013Article
- Article
- NMR studies reveal an unexpected binding site for a redox inhibitor of AP endonuclease 1.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Apurinic/apyrimidinic endonuclease 1 (APE1 or Ref-1) is the major enzyme in mammals for processing abasic sites in DNA. These cytotoxic and mutagenic lesions arise via spontaneous rupture of the base-sugar bond or the removal of damaged bases by a DNA glycosylase. APE1 cleaves the DNA backbone 5' to an abasic site, giving a 3'-OH primer for repair synthesis, and mediates other key repair activities. The DNA repair functions are essential for embryogenesis and cell viability. APE1-deficient cells are hypersensitive to DNA-damaging agents, and APE1 is considered an attractive target for inhibitors that could potentially enhance the efficacy of some anti-cancer agents. To enable an important new method for studying the structure, dynamics, catalytic mechanism, and inhibition of APE1, we assigned the chemical shifts (backbone and (13)C(beta)) of APE1 residues 39-318. We also report a protocol for refolding APE1, which was essential for achieving complete exchange of backbone amide sites for the perdeuterated protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.