Evidence map›Paper›PMID 37734998›Full record

ReviewSeminars in cell & developmental biology2024

Proteotoxic stress and the ubiquitin proteasome system.

Rachel Kandel, Jasmine Jung, Sonya Neal

Open access · hybridAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
12.8field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Human iPSC models revealResearch square · 2026
    Article
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  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Male germ cell-specific deletion ofZoological research · 2026
    Article
  12. Review
  13. Article
  14. Article
  15. Ubiquitination-Driven Reprogramming of Proteostasis in Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

4 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

3 authors at 2 institutions in 1 country.

Rachel KandelSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093, United States.
Jasmine JungSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093, United States.
Sonya NealSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093, United States; Howard Hughes Medical Institute, Chevy Chase, MD, USA. Electronic address: seneal@ucsd.edu.
University of California San Diego · USHoward Hughes Medical Institute · US

Funding

Training In Cardiovascular Physiology & PharmacologyT32HL007444 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Ju Chen, Robert Scott Ross · 1985 to 2026
$11.1M
UCSD PRIDE Faculty Development Program in Cardiovascular SciencesR25HL145817 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Robert Scott Ross, Joann Trejo · 2019 to 2026
$3.3M
The Discovery of Molecules and Mechanisms of the Rhomboid SuperfamilyR35GM133565 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Sonya Elina Neal · 2019 to 2026
$2.9M
NHLBI NIH HHS R25 HL145817NHLBI NIH HHS T32 HL007444NIGMS NIH HHS R35 GM133565
6 · The paper itself

Abstract

The ubiquitin proteasome system maintains protein homeostasis by regulating the breakdown of misfolded proteins, thereby preventing misfolded protein aggregates. The efficient elimination is vital for preventing damage to the cell by misfolded proteins, known as proteotoxic stress. Proteotoxic stress can lead to the collapse of protein homeostasis and can alter the function of the ubiquitin proteasome system. Conversely, impairment of the ubiquitin proteasome system can also cause proteotoxic stress and disrupt protein homeostasis. This review examines two impacts of proteotoxic stress, 1) disruptions to ubiquitin homeostasis (ubiquitin stress) and 2) disruptions to proteasome homeostasis (proteasome stress). Here, we provide a mechanistic description of the relationship between proteotoxic stress and the ubiquitin proteasome system. This relationship is illustrated by findings from several protein misfolding diseases, mainly neurodegenerative diseases, as well as from basic biology discoveries from yeast to mammals. In addition, we explore the importance of the ubiquitin proteasome system in endoplasmic reticulum quality control, and how proteotoxic stress at this organelle is alleviated. Finally, we highlight how cells utilize the ubiquitin proteasome system to adapt to proteotoxic stress and how the ubiquitin proteasome system can be genetically and pharmacologically manipulated to maintain protein homeostasis.

Indexed as

Proteasome Endopeptidase ComplexUbiquitinAnimalsMammalsProteinsProteotoxic StressProteasome Endopeptidase ComplexProteinsUbiquitinAggregatesDeubiquitinaseNeurodegenerationNrf1ProteasomeProteasome stressProtein misfoldingProteotoxic stressUbiquitinUbiquitin proteasome systemUbiquitin stressUnfolded protein responseUsp14

Identifiers

PMID37734998
PMCPMC10807858
OpenAlexW4386865930

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.