Evidence map›Paper›PMID 33296738›Full record

ReviewCurrent opinion in structural biology2021

Mechanisms of substrate recognition by the 26S proteasome.

Caroline Davis, Brian Logan Spaller, Andreas Matouschek

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
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  11. Antitumor effect of BC12-3 on multiple myeloma via proteasome inhibition.Medical oncology (Northwood, London, England) · 2025
    Article
  12. Review
  13. Ubiquitin-Independent Degradation: An Emerging PROTAC Approach?BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Review
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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.

Caroline DavisDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
Brian Logan SpallerDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
Andreas MatouschekDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: matouschek@austin.utexas.edu.
The University of Texas at Austin · US

Funding

Deciphering a second component to the proteasomal degradation codeR01GM124501 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MATOUSCHEK, ANDREAS · 2017 to 2020
$1.6M
Characterizing proteasome-substrate interactions by mass spectrometry proteomicsR01GM135264 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., MATOUSCHEK, ANDREAS · 2020 to 2024
$1.4M
NIGMS NIH HHS R01 GM124501NIGMS NIH HHS R01 GM135264
6 · The paper itself

Abstract

The majority of regulated protein degradation in eukaryotes is accomplished by the 26S proteasome, the large proteolytic complex responsible for removing regulatory proteins and damaged proteins. Proteins are targeted to the proteasome by ubiquitination, and degradation is initiated at a disordered region within the protein. The ability of the proteasome to precisely select which proteins to break down is necessary for cellular functioning. Recent studies reveal the subtle mechanisms of substrate recognition by the proteasome - diverse ubiquitin chains can act as potent proteasome targeting signals, ubiquitin receptors function uniquely and cooperatively, and modification of initiation regions modulate degradation. Here, we summarize recent findings illuminating the nature of substrate recognition by the proteasome.

Indexed as

Proteasome Endopeptidase ComplexUbiquitinProteolysisUbiquitinationATP dependent 26S proteaseProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID33296738
PMCPMC8096638
OpenAlexW3112304119

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.