Evidence map›Paper›PMID 28525752›Full record

ReviewCell2017

The Logic of the 26S Proteasome.

Galen Andrew Collins, Alfred L Goldberg

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 578 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
578citing papers in PubMed, 1 pooled it
35.7field-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

578 citing papers in PubMed, 1 synthesis or guideline pooled it, 917 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Adaptation to heat stress by diversification of the vertebrate heat shock transcription factor family.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. PKA-Mediated Proteasome Activation Protects Against Cardiac Remodeling and Heart Failure During Systolic Overload.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. High-throughput screening identifies a critical role of the SPOP-PABPC1 axis in lung adenocarcinoma progression.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  20. Review

518 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.

Galen Andrew CollinsDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Alfred L GoldbergDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Electronic address: alfred_goldberg@hms.harvard.edu.
Harvard University · US

Funding

MOLECULAR CHAPERONES AND PROTEIN DEGRADATIONR01GM051923 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLDBERG, ALFRED L · 1995 to 2020
$10.1M
NIGMS NIH HHS R01 GM051923
6 · The paper itself

Abstract

The ubiquitin proteasome pathway is responsible for most of the protein degradation in mammalian cells. Rates of degradation by this pathway have generally been assumed to be determined by rates of ubiquitylation. However, recent studies indicate that proteasome function is also tightly regulated and determines whether a ubiquitylated protein is destroyed or deubiquitylated and survives longer. This article reviews recent advances in our understanding of the proteasome's multistep ATP-dependent mechanism, its biochemical and structural features that ensure efficient proteolysis and ubiquitin recycling while preventing nonselective proteolysis, and the regulation of proteasome activity by interacting proteins and subunit modifications, especially phosphorylation.

Indexed as

Adenosine TriphosphatasesAllosteric RegulationAnimalsEukaryotaHumansPhosphorylationProteasome Endopeptidase ComplexProteolysisUbiquitinationAdenosine TriphosphatasesATP dependent 26S proteaseProteasome Endopeptidase Complexproteasome phosphorylationprotein degradationprotein turnoverubiquitin proteasome system

Identifiers

PMID28525752
PMCPMC5609836
OpenAlexW2615829409

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.