Evidence map›Paper›PMID 15226437›Full record

ArticleMolecular and cellular biology2004

The NEF4 complex regulates Rad4 levels and utilizes Snf2/Swi2-related ATPase activity for nucleotide excision repair.

Kerrington L Ramsey, Joshua J Smith, Arindam Dasgupta, Nazif Maqani, Patrick Grant, David T Auble

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. 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
2.3field-weighted citation impact, top 12% 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, 65 citations in OpenAlex.

  1. Review
  2. Photoreactivation Activities of Rad5, Rad16A and Rad16B HelpJournal of fungi (Basel, Switzerland) · 2024
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  17. Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation.Proceedings of the National Academy of Sciences of the United States of America · 2009
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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 1 institution in 1 country.

Kerrington L RamseyDepartment of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908-0733, USA.
Joshua J Smith
Arindam Dasgupta
Nazif Maqani
Patrick Grant
David T Auble
University of Virginia Health System · US

Funding

MOLECULAR ANALYSIS OF A YEAST TRANSCRIPTIONAL REGULATORR01GM055763 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI AUBLE, DAVID T. · 1997 to 2021
$6.4M
NIGMS NIH HHS GM55763NIGMS NIH HHS R01 GM055763
6 · The paper itself

Abstract

Nucleotide excision repair factor 4 (NEF4) is required for repair of nontranscribed DNA in Saccharomyces cerevisiae. Rad7 and the Snf2/Swi2-related ATPase Rad16 are NEF4 subunits. We report previously unrecognized similarity between Rad7 and F-box proteins. Rad16 contains a RING domain embedded within its ATPase domain, and the presence of these motifs in NEF4 suggested that NEF4 functions as both an ATPase and an E3 ubiquitin ligase. Mutational analysis provides strong support for this model. The Rad16 ATPase is important for NEF4 function in vivo, and genetic analysis uncovered new interactions between NEF4 and Rad23, a repair factor that links repair to proteasome function. Elc1 is the yeast homologue of a mammalian E3 subunit, and it is a novel component of NEF4. Moreover, the E2s Ubc9 and Ubc13 were linked to the NEF4 repair pathway by genetic criteria. Mutations in NEF4 or Ubc13 result in elevated levels of the DNA damage recognition protein Rad4 and an increase in ubiquitylated species of Rad23. As Rad23 also controls Rad4 levels, these results suggest a complex system for globally regulating repair activity in vivo by controlling turnover of Rad4.

Indexed as

DNA RepairAdenosine TriphosphatasesAmino Acid SequenceDNA-Binding ProteinsDNA DamageFungal ProteinsMacromolecular SubstancesMolecular Sequence DataPhenotypeProtein Structure, TertiaryProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUltraviolet RaysAdenosine TriphosphatasesDNA-Binding ProteinsFungal ProteinsMacromolecular SubstancesProtein SubunitsRAD16 protein, S cerevisiaeRAD23 protein, S cerevisiaeRAD7 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID15226437
PMCPMC434245
OpenAlexW2116719682

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.