Evidence map›Paper›PMID 11410533›Full record

ArticleGenes & development2001

The 19S complex of the proteasome regulates nucleotide excision repair in yeast.

T G Gillette, W Huang, S J Russell, S H Reed, S A Johnston, E C Friedberg

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Yeast Rpn4 Links the Proteasome and DNA Repair viaInternational journal of molecular sciences · 2020
    Article
  5. Article
  6. AAA-ATPases in Protein Degradation.Frontiers in molecular biosciences · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. 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

6 authors at 3 institutions in 3 countries.

T G GilletteLaboratory of Molecular Pathology, Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9072, USA.
W Huang
S J Russell
S H Reed
S A Johnston
E C Friedberg
The University of Texas Southwestern Medical Center · USNational Cheng Kung University · TWSouthwestern Medical Center

Funding

NCI NIH HHS CA-12424
6 · The paper itself

Abstract

Previous studies suggest that the amino-terminal ubiquitin-like (ubl) domain of Rad23 protein can recruit the proteasome for a stimulatory role during nucleotide excision repair in the yeast Saccharomyces cerevisiae. In this report, we show that the 19S regulatory complex of the yeast proteasome can affect nucleotide excision repair independently of Rad23 protein. Strains with mutations in 19S regulatory subunits (but not 20S subunits) of the proteasome promote partial recovery of nucleotide excision repair in vivo in rad23 deletion mutants, but not in other nucleotide excision repair-defective strains tested. In addition, a strain that expresses a temperature-degradable ATPase subunit of the 19S regulatory complex manifests a dramatically increased rate of nucleotide excision repair in vivo. These data indicate that the 19S regulatory complex of the 26S proteasome can negatively regulate the rate of nucleotide excision repair in yeast and suggest that Rad23 protein not only recruits the 19S regulatory complex, but also can mediate functional interactions between the 19S regulatory complex and the nucleotide excision repair machinery. The 19S regulatory complex of the yeast proteasome functions in nucleotide excision repair independent of proteolysis.

Indexed as

DNA RepairSaccharomyces cerevisiae ProteinsCysteine EndopeptidasesDNA-Binding ProteinsDNA DamageDNA, FungalFungal ProteinsMultienzyme ComplexesMutagenesisProteasome Endopeptidase ComplexSaccharomyces cerevisiaeTemperatureUbiquitinsUltraviolet RaysCysteine EndopeptidasesDNA-Binding ProteinsDNA, FungalFungal ProteinsMultienzyme ComplexesProteasome Endopeptidase ComplexRAD23 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitins

Identifiers

PMID11410533
PMCPMC312714
OpenAlexW2100300146

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.