Evidence map›Paper›PMID 9618470›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Assembly, subunit composition, and footprint of human DNA repair excision nuclease.

M Wakasugi, A Sancar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

77 citing papers in PubMed, 169 citations in OpenAlex.

  1. Article
  2. Mechanisms of DNA repair and mutagenesis induced by acetaldehyde, acrolein, aristolochic acids, and vinyl chloride.Journal of environmental science and health. Part C, Toxicology and carcinogenesis · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Nucleotide excision repair: a versatile and smart toolkit.Acta biochimica et biophysica Sinica · 2022
    Review
  11. XPG: a multitasking genome caretaker.Cellular and molecular life sciences : CMLS · 2022
    Review
  12. Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

17 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

2 authors at 1 institution in 1 country.

M WakasugiDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
A Sancar
University of North Carolina at Chapel Hill · US

Funding

STRUCTURE AND FUNCTION OF UVRABC EXCISION NUCLEASER01GM032833 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SANCAR, AZIZ · 1985 to 2015
$8.9M
NIGMS NIH HHS GM32833NIGMS NIH HHS R01 GM032833
6 · The paper itself

Abstract

The assembly and composition of human excision nuclease were investigated by electrophoretic mobility shift assay and DNase I footprinting. Individual repair factors or any combination of up to four repair factors failed to form DNA-protein complexes of high specificity and stability. A stable complex of high specificity can be detected only when XPA/RPA, transcription factor IIH, XPC.HHR23B, and XPG and ATP are present in the reaction mixture. The XPF.ERCC1 heterodimer changes the electrophoretic mobility of the DNA-protein complex formed with the other five repair factors, but it does not confer additional specificity. By using proteins with peptide tags or antibodies to the repair factors in electrophoretic mobility shift assays, it was found that XPA, replication protein A, transcription factor IIH, XPG, and XPF.excision repair cross-complementing 1 but not XPC.HHR23B were present in the penultimate and ultimate dual incision complexes. Thus, it appears that XPC.HHR23B is a molecular matchmaker that participates in the assembly of the excision nuclease but is not present in the ultimate dual incision complex. The excision nuclease makes an assymmetric DNase I footprint of approximately 30 bp around the damage and increases the DNase I sensitivity of the DNA on both sides of the footprint.

Indexed as

DNA RepairTranscription Factors, TFIIBase SequenceDNA-Binding ProteinsDNA Excision Repair Protein ERCC-5EndodeoxyribonucleasesEndonucleasesHumansMolecular Sequence DataNuclear ProteinsReplication Protein ATranscription FactorsTranscription Factor TFIIHXeroderma Pigmentosum Group A ProteinDNA-Binding ProteinsDNA Excision Repair Protein ERCC-5EndodeoxyribonucleasesEndonucleasesNuclear ProteinsReplication Protein ARPA1 protein, humanTranscription FactorsTranscription Factors, TFIITranscription Factor TFIIHXeroderma Pigmentosum Group A ProteinXPA protein, human

Identifiers

PMID9618470
PMCPMC22593
OpenAlexW1975365355

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.