Evidence map›Paper›PMID 24632559›Full record

ReviewCurrent opinion in structural biology2014

Paradigms of protein degradation by the proteasome.

Tomonao Inobe, Andreas Matouschek

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

67 citing papers in PubMed, 120 citations in OpenAlex.

  1. Trial
  2. Review
  3. Review
  4. Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025
    Review
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  6. Review
  7. Article
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  9. Article
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  11. Bimodular architecture of bacterial effector SAP05 that drives ubiquitin-independent targeted protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

7 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.

Tomonao InobeFrontier Research Core for Life Sciences, University of Toyama, Toyama 930-8555, Japan.
Andreas MatouschekDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: matouschek@austin.utexas.edu.
University of Toyama · JP

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI O'HALLORAN, THOMAS V · 2009 to 2013
$12.8M
Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
NCI NIH HHS U54 CA143869NCI NIH HHS U54CA143869NIGMS NIH HHS R01 GM063004NIGMS NIH HHS R01GM63004NIGMS NIH HHS U54 GM105816NIGMS NIH HHS U54GM105816
6 · The paper itself

Abstract

The proteasome is the main proteolytic machine in the cytosol and nucleus of eukaryotic cells where it degrades hundreds of regulatory proteins, removes damaged proteins, and produces peptides that are presented by MHC complexes. New structures of the proteasome particle show how its subunits are arranged and provide insights into how the proteasome is regulated. Proteins are targeted to the proteasome by tags composed of several ubiquitin moieties. The structure of the tags tunes the order in which proteins are degraded. The proteasome itself edits the ubiquitin tags and drugs that interfere in this process can enhance the clearance of toxic proteins from cells. Finally, the proteasome initiates degradation at unstructured regions within its substrates and this step contributes to substrate selection.

Indexed as

ProteolysisAnimalsHumansModels, MolecularProteasome Endopeptidase ComplexProteinsUbiquitinUbiquitinationProteasome Endopeptidase ComplexProteinsUbiquitin

Identifiers

PMID24632559
PMCPMC4010099
OpenAlexW2082211585

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.