Evidence map›Paper›PMID 8197175›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Formation of a ternary complex by human XPA, ERCC1, and ERCC4(XPF) excision repair proteins.

C H Park, A Sancar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
7.8field-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

61 citing papers in PubMed, 187 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Nucleotide excision repair: a versatile and smart toolkit.Acta biochimica et biophysica Sinica · 2022
    Review
  7. Article
  8. Review
  9. ERCC1-XPF targeting to psoralen-DNA crosslinks depends on XPA and FANCD2.Cellular and molecular life sciences : CMLS · 2020
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. OncoTargets and therapy · 2016
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

1 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.

C H ParkDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill 27599.
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 GM32833
6 · The paper itself

Abstract

The xeroderma pigmentosum complementation group A (XP-A) protein, XPA, has recently been expressed in Escherichia coli in a soluble and fully functional form. An affinity column was prepared by linking the XPA protein to a solid support. When HeLa cell-free extract capable of excision repair was applied to the column, > 99.9% of the proteins were in the flow-through. However, the flow-through fraction lacked excision activity. The activity was restored by adding the high salt (1 M KCl) eluate of the column to the flow-through fraction. The XPA protein-bound fraction was tested for specific proteins by an in vitro complementation assay with a panel of cell-free extracts from DNA repair-deficient human and rodent cell lines. The XPA-bound fraction complemented cell-free extracts of excision repair cross-complementing 1 (ERCC-1), ERCC-4 (XP-F), and XP-A mutants. We conclude that the XPA damage recognition protein makes a ternary complex with the ERCC1/ERCC4(XPF) heterodimer with a potential nuclease function.

Indexed as

DNA RepairEndonucleasesAnimalsCell-Free SystemChromatography, AffinityCloning, MolecularDNA-Binding ProteinsDNA DamageEscherichia coliExonucleasesGenetic Complementation TestHeLa CellsHumansProtein BindingProteinsXeroderma Pigmentosum Group A ProteinDNA-Binding ProteinsEndonucleasesERCC1 protein, humanExonucleasesProteinsXeroderma Pigmentosum Group A Proteinxeroderma pigmentosum group F proteinXPA protein, human

Identifiers

PMID8197175
PMCPMC43921
OpenAlexW2091370689

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.