Evidence map›Paper›PMID 31783300›Full record

ReviewCurrent opinion in structural biology2020

Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspective.

Eric R Greene, Ken C Dong, Andreas Martin

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Antitumor effect of BC12-3 on multiple myeloma via proteasome inhibition.Medical oncology (Northwood, London, England) · 2025
    Article
  7. Article
  8. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  9. Review
  10. Article
  11. Bortezomib Inhibits Open Configurations of the 20S Proteasome.Journal of the American Society for Mass Spectrometry · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. High-Throughput Assay for Characterizing Rpn11 Deubiquitinase Activity.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  20. Review
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

3 authors at 1 institution in 1 country.

Eric R GreeneDepartment of Molecular Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, CA 94720, USA.
Ken C DongDepartment of Molecular Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California Berkeley, Berkeley, CA 94720, USA.
Andreas MartinDepartment of Molecular Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California Berkeley, Berkeley, CA 94720, USA. Electronic address: a.martin@berkeley.edu.
QB3 · US

Funding

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

Abstract

The 26S proteasome is the essential compartmental protease in eukaryotic cells required for the ubiquitin-dependent clearance of damaged polypeptides and obsolete regulatory proteins. Recently, a combination of high-resolution structural, biochemical, and biophysical studies has provided crucial new insights into the mechanisms of this fascinating molecular machine. A multitude of new cryo-electron microscopy structures provided snapshots of the proteasome during ATP-hydrolysis-driven substrate translocation, and detailed biochemical studies revealed the timing of individual degradation steps, elucidating the mechanisms for substrate selection and the commitment to degradation through conformational transitions. It was uncovered how ubiquitin removal from substrates is mechanically coupled to degradation, and cryo-electron tomography studies gave a glimpse of active proteasomes inside the cell, their subcellular localization, and interactions with protein aggregates. Here, we summarize these advances in our mechanistic understanding of the proteasome, with a particular focus on how its structural features and conformational transitions enable the multi-step degradation process.

Indexed as

Molecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationChemical PhenomenaCryoelectron MicroscopyHumansModels, MolecularProteasome Endopeptidase ComplexProtein BindingProtein ConformationProteolysisStructure-Activity RelationshipSubstrate SpecificityUbiquitinationATP dependent 26S proteaseProteasome Endopeptidase Complex

Identifiers

PMID31783300
PMCPMC7156321
OpenAlexW2991562942

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.