Evidence map›Paper›PMID 31074920›Full record

ReviewProtein science : a publication of the Protein Society2019

Substrate selection by the proteasome through initiation regions.

Takuya Tomita, Andreas Matouschek

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Proteasomal surveillance of exposed cysteines.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Oligomerization of PER2 as a dynamic mode of regulation of the mammalian circadian clock.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. The AAA+ protein Msp1 recognizes substrates by a hydrophobic mismatch.bioRxiv : the preprint server for biology · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
  12. Review
  13. Design principles that protect the proteasome from self-destruction.Protein science : a publication of the Protein Society · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021
    Review
  18. Mechanistic basis for ubiquitin modulation of a protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. 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

2 authors at 1 institution in 1 country.

Takuya TomitaDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, 78712.
Andreas MatouschekDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, 78712.ORCID 0000-0001-6016-2341
The University of Texas at Austin · US

Funding

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
Deciphering a second component to the proteasomal degradation codeR01GM124501 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MATOUSCHEK, ANDREAS · 2017 to 2020
$1.6M
Development of proteasome adaptors to catalytically deplete specific proteins from cellsR21CA196456 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI MATOUSCHEK, ANDREAS · 2016 to 2018
$597k
NCI NIH HHS R21 CA196456NCI NIH HHS R21CA196456NIGMS NIH HHS R01 GM124501NIGMS NIH HHS R01GM124501NIGMS NIH HHS U54 GM105816
6 · The paper itself

Abstract

Proteins in the cell have to be eliminated once their function is no longer desired or they become damaged. Most regulated protein degradation is achieved by a large enzymatic complex called the proteasome. Many proteasome substrates are targeted for degradation by the covalent attachment of ubiquitin molecules. Ubiquitinated proteins can be bound by the proteasome, but for proteolysis to occur the proteasome needs to find a disordered tail somewhere in the target at which it initiates degradation. The initiation step contributes to the specificity of proteasomal degradation. Here, we review how the proteasome selects initiation sites within its substrates and discuss how the initiation step affects physiological processes.

Indexed as

AnimalsHumansProteasome Endopeptidase ComplexSubstrate SpecificityUbiquitinProteasome Endopeptidase ComplexUbiquitininitiation regionproteasomeprotein degradationprotein unfoldingubiquitin

Identifiers

PMID31074920
PMCPMC6566540
OpenAlexW2943921273

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.