Evidence map›Paper›PMID 23290100›Full record

ReviewTrends in biochemical sciences2013

Functions of the 19S complex in proteasomal degradation.

Chang-Wei Liu, Andrew D Jacobson

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.6field-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

41 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Role of Proteasomes in Inflammation.Journal of clinical medicine · 2021
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Exploring long-range cooperativity in the 20S proteasome core particle fromProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Review
  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.

Chang-Wei LiuDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, 12801 E. 17th Ave, Aurora, CO 80045, USA. changwei.liu@ucdenver.edu
Andrew D Jacobson
University of Colorado Denver · US

Funding

Cellular regulation by protein ubiquitination/deubiquitinationR01NS072397 · NINDS · UNIVERSITY OF COLORADO DENVER · PI LIU, CHANGWEI · 2010 to 2014
$1.6M
NINDS NIH HHS 5R01NS72397NINDS NIH HHS R01 NS072397
6 · The paper itself

Abstract

The 26S proteasome degrades ubiquitylated proteins. It consists of the 20S proteasome and the PA700/19S complex. PA700 plays essential roles in processing ubiquitylated substrates; it can bind, deubiquitylate, and unfold ubiquitylated proteins, which then translocate into the proteolytic chamber of the 20S proteasome for degradation. Here, we summarize the current knowledge of PA700-mediated substrate binding and deubiquitylation, and provide models to explain how substrate binding and deubiquitylation could regulate proteasomal degradation. We also discuss the features and potential therapeutic uses of the two recently identified small molecule inhibitors of the proteasome-residing deubiquitylating enzymes.

Indexed as

Protein Structure, TertiaryAnimalsHumansModels, MolecularProteasome Endopeptidase ComplexProtein BindingProteolysisSubstrate SpecificityUbiquitinUbiquitination26S proteasome non-ATPase regulatory subunit 13Proteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID23290100
PMCPMC3557657
OpenAlexW2009896610

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.