Evidence map›Paper›PMID 23028185›Full record

ReviewGenetics2012

The ubiquitin-proteasome system of Saccharomyces cerevisiae.

Daniel Finley, Helle D Ulrich, Thomas Sommer, Peter Kaiser

Abstract readReview
In one paragraph

Review in Genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 268 papers.

0numbers the graph read from it
0cells of the map it votes in
268citing 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

268 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Transient acceleration ofFrontiers in microbiology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Evolution of cross-tolerance to metals in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Review
  20. Review

208 more citing papers are in PubMed but not listed here.

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

4 authors.

Daniel FinleyDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Helle D Ulrich
Thomas Sommer
Peter Kaiser

Funding

Ubiquitin SignalingR01GM066164 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER · 2002 to 2022
$7.4M
Functional Analysis of the Proteasome BaseR37GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 2004 to 2013
$5.9M
UBIQUITIN-PROTEIN CONJUGATES AND FUSIONSR01GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 1990 to 2020
$4.3M
A Functional Census of p53 Cancer and Suppressor MutantsR01CA112560 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER, LATHROP, RICHARD H · 2005 to 2013
$3.2M
Ubiquitin chain editing by the mammalian proteasomeR01GM095526 · NIGMS · HARVARD MEDICAL SCHOOL · PI FINLEY, DANIEL J · 2011 to 2014
$1.8M
Regulation by Proteolysis-Independent UbiquitinationR56GM066164 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER · 2007 to 2007
$265k
Cancer Research UKNCI NIH HHS CA112560NCI NIH HHS R01 CA112560NIGMS NIH HHS GM095526NIGMS NIH HHS GM43601NIGMS NIH HHS GM66164NIGMS NIH HHS R01 GM043601NIGMS NIH HHS R01 GM066164NIGMS NIH HHS R01 GM095526NIGMS NIH HHS R37 GM043601NIGMS NIH HHS R56 GM066164
6 · The paper itself

Abstract

Protein modifications provide cells with exquisite temporal and spatial control of protein function. Ubiquitin is among the most important modifiers, serving both to target hundreds of proteins for rapid degradation by the proteasome, and as a dynamic signaling agent that regulates the function of covalently bound proteins. The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins. The resulting ubiquitin code is interpreted by an extensive family of ubiquitin receptors. Here we review the components of this regulatory network and its effects throughout the cell.

Indexed as

Protein TransportSaccharomyces cerevisiaeUbiquitinAdenosine TriphosphatasesCell Cycle ProteinsMembrane ProteinsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalProteolysisSaccharomyces cerevisiae ProteinsSubstrate SpecificityUbiquitinationValosin Containing ProteinAdenosine TriphosphatasesCDC48 protein, S cerevisiaeCell Cycle ProteinsMembrane ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitinValosin Containing Protein

Identifiers

PMID23028185
PMCPMC3454868

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.