Evidence map›Paper›PMID 12815074›Full record

ArticleGenes & development2003

A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein.

Jessica M Y Ng, Wim Vermeulen, Gijsbertus T J van der Horst, Steven Bergink, Kaoru Sugasawa, Harry Vrieling, Jan H J Hoeijmakers

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
–field-weighted citation impact
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

114 citing papers in PubMed, 253 citations in OpenAlex.

  1. Review
  2. Ubiquitin Proteasome System Components, RAD23A and USP13, Modulate TDP-43 Solubility and Neuronal Toxicity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Role of Nucleotide Excision Repair in Cisplatin Resistance.International journal of molecular sciences · 2020
    Review
  15. Review
  16. Article
  17. Ubiquitin-Modulated Phase Separation of Shuttle Proteins: Does Condensate Formation Promote Protein Degradation?BioEssays : news and reviews in molecular, cellular and developmental biology · 2020
    Review
  18. Ubiquitination in the ERAD Process.International journal of molecular sciences · 2020
    Review
  19. Article
  20. DNA Oxidation and Excision Repair Pathways.International journal of molecular sciences · 2019
    Review

54 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

7 authors at 2 institutions in 1 country.

Jessica M Y NgMGC-Department of Cell Biology & Genetics, Centre for Biomedical Genetics, Erasmus Medical Center, Rotterdam, The Netherlands.
Wim Vermeulen
Gijsbertus T J van der Horst
Steven Bergink
Kaoru Sugasawa
Harry Vrieling
Jan H J Hoeijmakers
Science and Technology Corporation (Netherlands) · NLLeiden University Medical Center · NL

Funding

THE IMPACT OF CELLULAR DEFENSE ON THE ROLE OF Ku80 IN GENOME MAINTENANCE AND LONGP01AG017242 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI VIJG, JAN · 1999 to 2023
$46.1M
NIA NIH HHS P01 AG017242
6 · The paper itself

Abstract

Primary DNA damage sensing in mammalian global genome nucleotide excision repair (GG-NER) is performed by the xeroderma pigmentosum group C (XPC)/HR23B protein complex. HR23B and HR23A are human homologs of the yeast ubiquitin-domain repair factor RAD23, the function of which is unknown. Knockout mice revealed that mHR23A and mHR23B have a fully redundant role in NER, and a partially redundant function in embryonic development. Inactivation of both genes causes embryonic lethality, but appeared still compatible with cellular viability. Analysis of mHR23A/B double-mutant cells showed that HR23 proteins function in NER by governing XPC stability via partial protection against proteasomal degradation. Interestingly, NER-type DNA damage further stabilizes XPC and thereby enhances repair. These findings resolve the primary function of RAD23 in repair and reveal a novel DNA-damage-dependent regulation mechanism of DNA repair in eukaryotes, which may be part of a more global damage-response circuitry.

Indexed as

DNA DamageDNA RepairAcetoxyacetylaminofluoreneAnimalsCell LineCysteine EndopeptidasesDNA-Binding ProteinsDNA Repair EnzymesFemaleGene TargetingHot TemperatureHumansMaleMiceMice, Inbred C57BLMice, KnockoutAcetoxyacetylaminofluoreneCysteine EndopeptidasesDNA-Binding ProteinsDNA Repair EnzymesMultienzyme ComplexesProteasome Endopeptidase ComplexRAD23A protein, humanRad23a protein, mouseRAD23B protein, humanRad23b protein, mouseRecombinant Fusion ProteinsUbiquitinXPC protein, humanXpc protein, mouse

Identifiers

PMID12815074
PMCPMC196135
OpenAlexW2123456626

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.