Evidence map›Paper›PMID 30065390›Full record

ReviewNature reviews. Molecular cell biology2018

Regulation of proteasome assembly and activity in health and disease.

Adrien Rousseau, Anne Bertolotti

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 311 papers.

0numbers the graph read from it
0cells of the map it votes in
311citing papers in PubMed
16.2field-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

311 citing papers in PubMed, 511 citations in OpenAlex.

  1. Article
  2. More than the 'master regulator of cytosolic proteostasis': new roles for HSF1 in promoting tissue health.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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  15. BAG2 Condensates Couple Proteostasis to CD8bioRxiv : the preprint server for biology · 2026
    Article
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  19. Article
  20. Article

251 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 2 institutions in 1 country.

Adrien RousseauMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dow Street, Dundee, UK.
Anne BertolottiMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK. aberto@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0002-9185-0558
MRC Laboratory of Molecular Biology · GBUniversity of Dundee · GB

Funding

Medical Research Council MC_U105185860
6 · The paper itself

Abstract

The proteasome degrades most cellular proteins in a controlled and tightly regulated manner and thereby controls many processes, including cell cycle, transcription, signalling, trafficking and protein quality control. Proteasomal degradation is vital in all cells and organisms, and dysfunction or failure of proteasomal degradation is associated with diverse human diseases, including cancer and neurodegeneration. Target selection is an important and well-established way to control protein degradation. In addition, mounting evidence indicates that cells adjust proteasome-mediated degradation to their needs by regulating proteasome abundance through the coordinated expression of proteasome subunits and assembly chaperones. Central to the regulation of proteasome assembly is TOR complex 1 (TORC1), which is the master regulator of cell growth and stress. This Review discusses how proteasome assembly and the regulation of proteasomal degradation are integrated with cellular physiology, including the interplay between the proteasome and autophagy pathways. Understanding these mechanisms has potential implications for disease therapy, as the misregulation of proteasome function contributes to human diseases such as cancer and neurodegeneration.

Indexed as

AnimalsAutophagyCell ProliferationHumansMolecular ChaperonesNeoplasmsNeurodegenerative DiseasesProteasome Endopeptidase ComplexProteolysisSignal TransductionMolecular ChaperonesProteasome Endopeptidase Complex

Identifiers

PMID30065390
OpenAlexW2885938058

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.