Evidence map›Paper›PMID 17418826›Full record

ReviewFEBS letters2007

A proteasome for all occasions.

John Hanna, Daniel Finley

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 180 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Proteasomal subunit depletions differentially affect germline integrity inFrontiers in cell and developmental biology · 2022
    Article
  11. Biomolecules · 2021
    Article
  12. Article
  13. Review
  14. Chaperone-mediated reflux of secretory proteins to the cytosol during endoplasmic reticulum stress.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Review
  20. Article

20 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

2 authors at 1 institution in 1 country.

John HannaDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Daniel Finley
Harvard University · US

Funding

Regulation of Proteasome Activity by Ubp6 and Hul5R01GM065592 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 2003 to 2010
$3.5M
NIGMS NIH HHS R01 GM065592
6 · The paper itself

Abstract

In the ubiquitin-proteasome system, substrates fated for destruction first acquire covalent modification by ubiquitin, and are subsequently destroyed by the proteasome. Traditionally, 26S proteasomes have been seen as largely uniform in their composition and functional capacity. Accordingly, cells can control proteasome abundance via transcriptional pathways that mediate concerted regulation of all known proteasome genes. However, recent evidence suggests that the proteasome is also subject to subunit-specific modes of regulation, which serve to alter proteasome function and may generate ensembles of compositionally distinct proteasomes. These modes of proteasome regulation provide varied means to adapt protein degradation pathways to changing conditions in the cell.

Indexed as

AnimalsArsenitesDNA-Binding ProteinsEndopeptidasesHumansModels, BiologicalModels, MolecularMultiprotein ComplexesProteasome Endopeptidase ComplexRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional ActivationTranscription FactorsUbiquitinarseniteArsenitesDNA-Binding ProteinsEndopeptidasesMultiprotein ComplexesProteasome Endopeptidase ComplexRNA-Binding ProteinsRPN4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUBP6 protein, S cerevisiae

Identifiers

PMID17418826
PMCPMC1965587
OpenAlexW2084575237

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.