Evidence map›Paper›PMID 39362999›Full record

ReviewNature reviews. Molecular cell biology2025

Mechanisms and regulation of substrate degradation by the 26S proteasome.

Connor Arkinson, Ken C Dong, Christine L Gee, Andreas Martin

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Hsp90: A means to an end.Cell stress & chaperones · 2026
    Review
  16. Article
  17. Review
  18. Article
  19. 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

4 authors.

Connor ArkinsonCalifornia Institute for Quantitative Biosciences, University of California at Berkeley, Berkeley, CA, USA.
Ken C DongHoward Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA.
Christine L GeeCalifornia Institute for Quantitative Biosciences, University of California at Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-2632-6418
Andreas MartinCalifornia Institute for Quantitative Biosciences, University of California at Berkeley, Berkeley, CA, USA. a.martin@berkeley.edu.ORCID http://orcid.org/0000-0003-0923-3284

Funding

ATP-Dependent Protein Unfolding and Translocation by the Eukaryotic ProteasomeR01GM094497 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARTIN, ANDREAS · 2011 to 2024
$3.7M
NIGMS NIH HHS R01 GM094497
6 · The paper itself

Abstract

The 26S proteasome is involved in degrading and regulating the majority of proteins in eukaryotic cells, which requires a sophisticated balance of specificity and promiscuity. In this Review, we discuss the principles that underly substrate recognition and ATP-dependent degradation by the proteasome. We focus on recent insights into the mechanisms of conventional ubiquitin-dependent and ubiquitin-independent protein turnover, and discuss the plethora of modulators for proteasome function, including substrate-delivering cofactors, ubiquitin ligases and deubiquitinases that enable the targeting of a highly diverse substrate pool. Furthermore, we summarize recent progress in our understanding of substrate processing upstream of the 26S proteasome by the p97 protein unfoldase. The advances in our knowledge of proteasome structure, function and regulation also inform new strategies for specific inhibition or harnessing the degradation capabilities of the proteasome for the treatment of human diseases, for instance, by using proteolysis targeting chimera molecules or molecular glues.

Indexed as

Proteasome Endopeptidase ComplexProteolysisAnimalsHumansSubstrate SpecificityUbiquitinUbiquitin-Protein LigasesATP dependent 26S proteaseProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID39362999
PMCPMC11772106

What OpenQuestion holds

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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.