Evidence map›Paper›PMID 9034344›Full record

ArticleThe EMBO journal1997

Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein.

E Evans, J Fellows, A Coffer, R D Wood

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
6.9field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 1 synthesis or guideline pooled it, 236 citations in OpenAlex.

  1. Pooled it
  2. Plant tolerance mechanisms to DNA-damaging UV stress.Journal of experimental botany · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. XPG: a multitasking genome caretaker.Cellular and molecular life sciences : CMLS · 2022
    Review
  10. CSB-independent, XPC-dependent transcription-coupled repair inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Specific Human ATR and ATM Inhibitors Modulate Single Strand DNA Formation inFrontiers in cellular and infection microbiology · 2021
    Article
  17. Review
  18. Article
  19. Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Review

34 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

E EvansImperial Cancer Research Fund, Clare Hall Laboratories, London, UK.
J Fellows
A Coffer
R D Wood
University of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human XPG nuclease makes the 3' incision during nucleotide excision repair of DNA. The enzyme cleaves model DNA bubble structures specifically near the junction of unpaired DNA with a duplex region. It is not yet known, however, whether an unpaired structure is an intermediate during actual DNA repair. We find here that XPG requires opening of >5 bp for efficient cleavage. To seek direct evidence for formation of an open structure around a lesion in DNA during a nucleotide excision repair reaction in vitro, KMnO4 footprinting experiments were performed on a damaged DNA molecule bearing a uniquely placed cisplatin adduct. An unwound open complex spanning approximately 25 nucleotides was observed that extended to the positions of 5' and 3' incision sites and was dependent on XPA protein and on ATP. Opening during repair occurred prior to strand incision by XPG.

Indexed as

Adenosine TriphosphateAntineoplastic AgentsBase SequenceCisplatinDNA-Binding ProteinsDNA DamageDNA Excision Repair Protein ERCC-5DNA FootprintingDNA RepairDNA, Single-StrandedElectrophoresis, Polyacrylamide GelEndonucleasesHumansIntercalating AgentsMolecular Sequence DataNuclear ProteinsAdenosine TriphosphateAntineoplastic AgentsCisplatinDNA-Binding ProteinsDNA Excision Repair Protein ERCC-5DNA, Single-StrandedEndonucleasesIntercalating AgentsNuclear ProteinsOligodeoxyribonucleotidesProliferating Cell Nuclear AntigenRecombinant ProteinsSingle-Strand Specific DNA and RNA EndonucleasesTranscription FactorsXeroderma Pigmentosum Group A ProteinXPA protein, human

Identifiers

PMID9034344
PMCPMC1169665
OpenAlexW2098711782

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.