Evidence map›Paper›PMID 33450252›Full record

ArticleJournal of molecular biology2021

Dynamic Processing of a Common Oxidative DNA Lesion by the First Two Enzymes of the Base Excision Repair Pathway.

Austin T Raper, Brian A Maxwell, Zucai Suo

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Interlocking activities of DNA polymerase β in the base excision repair pathway.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Austin T RaperThe Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.
Brian A MaxwellThe Ohio State Biophysics Ph.D. Program, The Ohio State University, Columbus, OH 43210, USA.
Zucai SuoThe Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA; The Ohio State Biophysics Ph.D. Program, The Ohio State University, Columbus, OH 43210, USA; Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, FL 32306, USA. Electronic address: zucai.suo@med.fsu.edu.
The Ohio State University · USFlorida State University · US

Funding

Investigation of human DNA polymerase epsilon variantsR01ES028271 · NIEHS · TULANE UNIVERSITY OF LOUISIANA · PI Zachary F Pursell · 2017 to 2026
$3.6M
Investigation of DNA base excision repairR01GM122093 · NIGMS · FLORIDA STATE UNIVERSITY · PI SUO, ZUCAI · 2018 to 2021
$1.2M
NIEHS NIH HHS R01 ES028271NIGMS NIH HHS R01 GM122093
6 · The paper itself

Abstract

Base excision repair (BER) is the primary pathway by which eukaryotic cells resolve single base damage. One common example of single base damage is 8-oxo-7,8-dihydro-2'-deoxoguanine (8-oxoG). High incidence and mutagenic potential of 8-oxoG necessitate rapid and efficient DNA repair. How BER enzymes coordinate their activities to resolve 8-oxoG damage while limiting cytotoxic BER intermediates from propagating genomic instability remains unclear. Here we use single-molecule Förster resonance energy transfer (smFRET) and ensemble-level techniques to characterize the activities and interactions of consecutive BER enzymes important for repair of 8-oxoG. In addition to characterizing the damage searching and processing mechanisms of human 8-oxoguanine glycosylase 1 (hOGG1), our data support the existence of a ternary complex between hOGG1, the damaged DNA substrate, and human AP endonuclease 1 (APE1). Our results indicate that hOGG1 is actively displaced from its abasic site containing product by protein-protein interactions with APE1 to ensure timely repair of damaged DNA.

Indexed as

DNA Repair8-Hydroxy-2'-DeoxyguanosineBinding SitesDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageDNA GlycosylasesFluorescence Resonance Energy TransferGene ExpressionGenome, HumanGenomic InstabilityHumansKineticsModels, MolecularMutationNucleic Acid Conformation8-Hydroxy-2'-Deoxyguanosine8-oxo-7,8-dihydrodeoxyguanineAPEX1 protein, humanDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA Glycosylasesoxoguanine glycosylase 1, humanBase excision repairHuman 8-oxoguanine glycosylaseHuman AP endonucleaseSingle-molecule Förster resonance energy transferStopped-flow

Identifiers

PMID33450252
PMCPMC8225441
OpenAlexW3118432150

What OpenQuestion holds

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Registered trials

None linked

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.