Evidence map›Paper›PMID 15545636›Full record

ArticleNucleic acids research2004

Roles of Rad23 protein in yeast nucleotide excision repair.

Zhongwen Xie, Shuqian Liu, Yanbin Zhang, Zhigang Wang

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

37 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Review
  3. Divergent roles of Rad4 and Rad23 homologs inApplied and environmental microbiology · 2023
    Article
  4. Article
  5. Comparative Roles of Rad4A and Rad4B in Photoprotection ofJournal of fungi (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Altitudinal Heterogeneity of UV Adaptation inJournal of fungi (Basel, Switzerland) · 2021
    Article
  10. New Insights inToxins · 2020
    Article
  11. Article
  12. Article
  13. Comparative Transcriptome Analyses ofFrontiers in microbiology · 2020
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Architecture of the human XPC DNA repair and stem cell coactivator complex.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. 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

4 authors at 1 institution in 1 country.

Zhongwen XieGraduate Center for Toxicology, University of Kentucky, Lexington, KY 40536, USA.
Shuqian Liu
Yanbin Zhang
Zhigang Wang
The Graduate Center, CUNY · US

Funding

MOLECULAR DISSECTION OF YEAST NUCLEOTIDE EXCISION REPAIRR01CA067978 · NCI · UNIVERSITY OF KENTUCKY · PI WANG, ZHIGANG · 1997 to 2006
$1.3M
MOLECULAR DISSECTION OF YEAST NUCLEOTIDE EXCISION REPAIRR55CA067978 · NCI · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI WANG, ZHIGANG · 1995 to 1995
–
NCI NIH HHS CA67978NCI NIH HHS R01 CA067978NCI NIH HHS R55 CA067978
6 · The paper itself

Abstract

Nucleotide excision repair (NER) removes many different types of DNA lesions. Most NER proteins are indispensable for repair. In contrast, the yeast Rad23 represents a class of accessory NER proteins, without which NER activity is reduced but not eliminated. In mammals, the complex of HR23B (Rad23 homolog) and XPC (yeast Rad4 homolog) has been suggested to function in the damage recognition step of NER. However, the precise function of Rad23 or HR23B in NER remains unknown. Recently, it was suggested that the primary function of RAD23 protein in NER is its stabilization of XPC protein. Here, we tested the significance of Rad23-mediated Rad4 stabilization in NER, and analyzed the repair and biochemical activities of purified yeast Rad23 protein. Cellular Rad4 was indeed stabilized by Rad23 in the absence of DNA damage. Persistent overexpression of Rad4 in rad23 mutant cells, however, largely failed to complement the ultraviolet sensitivity of the mutant. Consistently, deficient NER in rad23 mutant cell extracts could not be complemented by purified Rad4 protein in vitro. In contrast, partial complementation was observed with purified Rad23 protein. Specific complementation to the level of wild-type repair was achieved by adding purified Rad23 together with small amounts of Rad4 protein to rad23 mutant cell extracts. Purified Rad23 protein was unable to bind to DNA, but stimulated the binding activity of purified Rad4 protein to N-acetyl-2-aminofluorene-damaged DNA. These results support two roles of Rad23 protein in NER: (i) its direct participation in the repair biochemistry, possibly due to its stimulatory activity on Rad4-mediated damage binding/recognition; and (ii) its stabilization of cellular Rad4 protein.

Indexed as

DNA RepairDNA-Binding ProteinsFungal ProteinsMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUltraviolet RaysDNA-Binding ProteinsFungal ProteinsRad4 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID15545636
PMCPMC534619
OpenAlexW2108444625

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.