Evidence map›Paper›PMID 16118187›Full record

ArticleGenetics2005

Saccharomyces cerevisiae Ub-conjugating enzyme Ubc4 binds the proteasome in the presence of translationally damaged proteins.

Show-Mei Chuang, Kiran Madura

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Genetics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Proteome Profiling ofMicroorganisms · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. microPublication biology · 2019
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Proteasome inhibitors and cardiac cell growth.Cardiovascular research · 2010
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. p62 serves as a shuttling factor for TrkA interaction with the proteasome.Biochemical and biophysical research communications · 2008
    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

2 authors at 1 institution in 1 country.

Show-Mei ChuangDepartment of Biochemistry, Rm. 383, SPH/Research Building, Robert Wood Johnson Medical School, 683 Hoes Lane, Piscataway, NJ 08854, USA.
Kiran Madura
Johnson University · 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 CA 38375NCI NIH HHS R01 CA083875
6 · The paper itself

Abstract

Surveillance mechanisms that monitor protein synthesis can promote rapid elimination of misfolded nascent proteins. We showed that the translation elongation factor eEF1A and the proteasome subunit Rpt1 play a central role in the translocation of nascent-damaged proteins to the proteasome. We show here that multiubiquitinated proteins, and the ubiquitin-conjugating (E2) enzyme Ubc4, are rapidly detected in the proteasome following translational damage. However, Ubc4 levels in the proteasome were reduced significantly in a strain that expressed a mutant Rpt1 subunit. Ubc4 and Ubc5 are functionally redundant E2 enzymes that represent ideal candidates for ubiquitinating damaged nascent proteins because they lack significant substrate specificity, are required for the degradation of bulk, damaged proteins, and contribute to cellular stress-tolerance mechanisms. In agreement with this hypothesis, we determined that ubc4Delta ubc5Delta is exceedingly sensitive to protein translation inhibitors. Collectively, these studies suggest a specific role for Ubc4 and Ubc5 in the degradation of cotranslationally damaged proteins that are targeted to the proteasome.

Indexed as

Protein BiosynthesisAdenosine TriphosphatasesDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelImmunoblottingMutationProteasome Endopeptidase ComplexProtein FoldingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Conjugating EnzymesAdenosine TriphosphatasesDNA-Binding ProteinsProteasome Endopeptidase ComplexRPT1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbc4 protein, S cerevisiaeUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID16118187
PMCPMC1456077
OpenAlexW2168219682

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.