Evidence map›Paper›PMID 35625547›Full record

ReviewBiomolecules2022

Biology of the Extracellular Proteasome.

Gili Ben-Nissan, Naama Katzir, Maria Gabriella Füzesi-Levi, Michal Sharon

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. ACS chemical neuroscience · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. The AhR Is a Critical Regulator of the Pulmonary Response to Cannabis Smoke.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. The proteomic landscape ofFrontiers in cellular and infection microbiology · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

Gili Ben-NissanDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0003-1913-3703
Naama KatzirDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0001-8486-0208
Maria Gabriella Füzesi-LeviDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0001-5880-830X
Michal SharonDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0003-3933-0595
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteasomes are traditionally considered intracellular complexes that play a critical role in maintaining proteostasis by degrading short-lived regulatory proteins and removing damaged proteins. Remarkably, in addition to these well-studied intracellular roles, accumulating data indicate that proteasomes are also present in extracellular body fluids. Not much is known about the origin, biological role, mode(s) of regulation or mechanisms of extracellular transport of these complexes. Nevertheless, emerging evidence indicates that the presence of proteasomes in the extracellular milieu is not a random phenomenon, but rather a regulated, coordinated physiological process. In this review, we provide an overview of the current understanding of extracellular proteasomes. To this end, we examine 143 proteomic datasets, leading us to the realization that 20S proteasome subunits are present in at least 25 different body fluids. Our analysis also indicates that while 19S subunits exist in some of those fluids, the dominant proteasome activator in these compartments is the PA28α/β complex. We also elaborate on the positive correlations that have been identified in plasma and extracellular vesicles, between 20S proteasome and activity levels to disease severity and treatment efficacy, suggesting the involvement of this understudied complex in pathophysiology. In addition, we address the considerations and practical experimental methods that should be taken when investigating extracellular proteasomes. Overall, we hope this review will stimulate new opportunities for investigation and thoughtful discussions on this exciting topic that will contribute to the maturation of the field.

Indexed as

Extracellular VesiclesProteasome Endopeptidase ComplexCytoplasmProteinsProteomicsProteasome Endopeptidase ComplexProteinsbody fluidsextracellular vesiclepathophysiologyproteasomeprotein degradation

Identifiers

PMID35625547
PMCPMC9139032
OpenAlexW4224285838

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.