ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Divergent evolution of opposite base specificity and single-stranded DNA activity in animal and plant AP endonucleases.Nucleic acids research · 2025Article
- Abasic site-peptide cross-links are blocking lesions repaired by AP endonucleases.Nucleic acids research · 2023Article
- Structural and Functional Characterization of a Unique AP Endonuclease FromFrontiers in microbiology · 2020Article
- Specificity and Efficiency of the Uracil DNA Glycosylase-Mediated Strand Cleavage Surveyed on Large Sequence Libraries.Scientific reports · 2019Article
- Structural basis for recognition and repair of the 3'-phosphate by NExo, a base excision DNA repair nuclease from Neisseria meningitidis.Nucleic acids research · 2018Article
- Correlation of bistranded clustered abasic DNA lesion processing with structural and dynamic DNA helix distortion.Nucleic acids research · 2016Article
- Capturing snapshots of APE1 processing DNA damage.Nature structural & molecular biology · 2015Article
- Recognition and repair of chemically heterogeneous structures at DNA ends.Environmental and molecular mutagenesis · 2015Review
- fH-dependent complement evasion by disease-causing meningococcal strains with absent fHbp genes or frameshift mutations.Vaccine · 2013Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Base excision repair (BER) is a highly conserved DNA repair pathway throughout all kingdoms from bacteria to humans. Whereas several enzymes are required to complete the multistep repair process of damaged bases, apurinic-apyrimidic (AP) endonucleases play an essential role in enabling the repair process by recognizing intermediary abasic sites cleaving the phosphodiester backbone 5' to the abasic site. Despite extensive study, there is no structure of a bacterial AP endonuclease bound to substrate DNA. Furthermore, the structural mechanism for AP-site cleavage is incomplete. Here we report a detailed structural and biochemical study of the AP endonuclease from Neisseria meningitidis that has allowed us to capture structural intermediates providing more complete snapshots of the catalytic mechanism. Our data reveal subtle differences in AP-site recognition and kinetics between the human and bacterial enzymes that may reflect different evolutionary pressures.
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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.