Evidence map›Paper›PMID 20427185›Full record

ReviewTrends in cell biology2010

Assembly, structure, and function of the 26S proteasome.

Lynn Bedford, Simon Paine, Paul W Sheppard, R John Mayer, Jeroen Roelofs

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed
8.9field-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

133 citing papers in PubMed, 251 citations in OpenAlex.

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  11. Strengthening the Role ofInternational journal of molecular sciences · 2025
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  15. Long noncoding RNAs in ubiquitination, protein degradation, and human diseases.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
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  20. Article

73 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

5 authors at 2 institutions in 2 countries.

Lynn BedfordSchool of Biomedical Sciences, University of Nottingham Medical School, Nottingham, UK.
Simon Paine
Paul W Sheppard
R John Mayer
Jeroen Roelofs
University of Nottingham · GBKansas State University · US

Funding

UNDERSTANDING THE ROLE OF SMALL RNAS IN ARABIDOPSIS POLLEN DEVELOPMENTP20RR016475 · NCRR · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ACKLEY, BRIAN DOUGLAS · 2001 to 2011
$38.1M
NCRR NIH HHS P20 RR016475Parkinson's UK F-0702Parkinson's UK G-4055
6 · The paper itself

Abstract

The 26S proteasome is a large multiprotein complex involved in the regulated degradation of ubiquitinated proteins in the cell. The 26S proteasome has been shown to control an increasing number of essential biochemical mechanisms of the cellular lifecycle including DNA synthesis, repair, transcription, translation, and cell signal transduction. Concurrently, it is increasingly seen that malfunction of the ubiquitin proteasome system contributes to the pathogenesis of disease. The recent identification of four molecular chaperones, in addition to five previously identified chaperones, have provided mechanistic insight into how this cellular megastructure is assembled in the cell. These data, together with new insights into the structure and function of the proteasome, provide a much better understanding of this complex protease.

Indexed as

AnimalsCell Physiological PhenomenaHumansMolecular ChaperonesProteasome Endopeptidase ComplexUbiquitinated ProteinsATP dependent 26S proteaseMolecular ChaperonesProteasome Endopeptidase ComplexUbiquitinated Proteins

Identifiers

PMID20427185
PMCPMC2902798
OpenAlexW2079123938

What OpenQuestion holds

Textmetadata
LicenceTDM
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.