Evidence map›Paper›PMID 16675952›Full record

ArticleThe EMBO journal2006

Distinct functions of the ubiquitin-proteasome pathway influence nucleotide excision repair.

Thomas G Gillette, Shirong Yu, Zheng Zhou, Raymond Waters, Stephen Albert Johnston, Simon H Reed

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 88 citations in OpenAlex.

  1. Photoreactivation Activities of Rad5, Rad16A and Rad16B HelpJournal of fungi (Basel, Switzerland) · 2024
    Article
  2. Article
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  4. Epigenetic Regulation of Nucleotide Excision Repair.Frontiers in cell and developmental biology · 2022
    Review
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  6. Article
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  9. Crystal structure of the ATPase-C domain of the chromatin remodeller Fun30 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
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  11. Review
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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 2 institutions in 2 countries.

Thomas G GilletteThe Center for Biomedical Inventions, Medicine and Microbiology, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Shirong Yu
Zheng Zhou
Raymond Waters
Stephen Albert Johnston
Simon H Reed
Cardiff University · GBThe University of Texas Southwestern Medical Center · US

Funding

Medical Research Council G0400113Medical Research Council G9900118
6 · The paper itself

Abstract

The Rad23/Rad4 nucleotide excision repair (NER) protein complex functions at an early stage of the NER reaction, possibly promoting the recognition of damaged DNA. Here we show that Rad4 protein is ubiquitinated and degraded in response to ultraviolet (UV) radiation, and identify a novel cullin-based E3 ubiquitin ligase required for this process. We also show that this novel ubiquitin ligase is required for optimal NER. Our results demonstrate that optimal NER correlates with the ubiquitination of Rad4 following UV radiation, but not its subsequent degradation. Furthermore, we show that the ubiquitin-proteasome pathway (UPP) regulates NER via two distinct mechanisms. The first occurs independently of de novo protein synthesis, and requires Rad23 and a nonproteolytic function of the 19S regulatory complex of the 26S proteasome. The second requires de novo protein synthesis, and relies on the activity of the newly identified E3 ubiquitin ligase. These studies reveal that, following UV radiation, NER is mediated by nonproteolytic activities of the UPP, via the ubiquitin-like domain of Rad23 and UV radiation-induced ubiquitination of Rad4.

Indexed as

DNA-Binding ProteinsDNA RepairProteasome Endopeptidase ComplexProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuppressor of Cytokine Signaling ProteinsUbiquitinUbiquitin-Protein LigasesUltraviolet RaysDNA-Binding ProteinsProteasome Endopeptidase ComplexProtein SubunitsRAD23 protein, S cerevisiaeRad4 protein, S cerevisiaeRAD7 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSuppressor of Cytokine Signaling ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID16675952
PMCPMC1478203
OpenAlexW2005618651

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.