Evidence map›Paper›PMID 12420141›Full record

ArticleCurrent genetics2002

Proteolysis of a nucleotide excision repair protein by the 26 S proteasome.

Lori Lommel, Tatiana Ortolan, Li Chen, Kiran Madura, Kevin S Sweder

Abstract read
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In one paragraph

Article in Current genetics, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Review
  3. Loss of RAD-23 Protects Against Models of Motor Neuron Disease by Enhancing Mutant Protein Clearance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Navigating the nucleotide excision repair threshold.Journal of cellular physiology · 2010
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
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  18. Article
  19. The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

5 authors at 2 institutions in 1 country.

Lori LommelSusan Lehman Cullman Laboratory for Cancer Research, Department of Chemical Biology, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, 164 Frelinghuysen Road, Piscataway 08854-8020, USA.
Tatiana Ortolan
Li Chen
Kiran Madura
Kevin S Sweder
Johnson University · USRutgers, The State University of New Jersey · US

Funding

FUNCTIONAL ANALYSIS OF RAD23 PROTEINR01CA083875 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI MADURA, KIRAN · 2000 to 2016
$4.4M
NCI NIH HHS 1R01 CA83875
6 · The paper itself

Abstract

The 26 S proteasome degrades a broad spectrum of proteins and interacts with several nucleotide excision repair (NER) proteins, including the complex of Rad4 and Rad23 that binds preferentially to UV-damaged DNA. The rate of NER is increased in yeast strains with mutations in genes encoding subunits of the 26 S proteasome, indicating that it could negatively regulate a repair process. The specific function of the 26 S proteasome in DNA repair is unclear. It might degrade DNA repair proteins after repair is completed or act as a molecular chaperone to promote the assembly or disassembly of the repair complex. In this study, we show that Rad4 is ubiquitylated and that Rad23 can control this process. We also find that ubiquitylated Rad4 is degraded by the 26 S proteasome. However, the interaction of Rad23 with Rad4 is not only to control degradation of Rad4, but also to assist in assembling the NER incision complex at UV-induced cyclobutane pyrimidine dimers. We speculate that, following the completion of DNA repair, specific repair proteins might be degraded by the proteasome to regulate repair.

Indexed as

Proteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsDNA LigasesDNA RepairFungal ProteinsMutationPeptide HydrolasesSaccharomyces cerevisiaeUbiquitinUltraviolet RaysATP dependent 26S proteaseDNA-Binding ProteinsDNA LigasesFungal ProteinsPeptide HydrolasesProteasome Endopeptidase ComplexRAD23 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin

Identifiers

PMID12420141
OpenAlexW2071639356

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.