Evidence map›Paper›PMID 22727423›Full record

ReviewProgress in molecular biology and translational science2012

Degradation of damaged proteins: the main function of the 20S proteasome.

Andrew M Pickering, Kelvin J A Davies

Open access · greenAbstract readReview
In one paragraph

Review in Progress in molecular biology and translational science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
19.4field-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

109 citing papers in PubMed, 181 citations in OpenAlex.

  1. Article
  2. Protein oxidation in crowded environments.The Biochemical journal · 2026
    Review
  3. Review
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  9. Article
  10. Article
  11. The Role of the Ubiquitin System in Eye Diseases.Life (Basel, Switzerland) · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Discovery and Development of Cyclic Peptide Proteasome Stimulators.Chembiochem : a European journal of chemical biology · 2024
    Article
  20. Review

49 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.

Andrew M PickeringEthel Percy Andrus Gerontology Center of the Davis School of Gerontology and Division of Molecular & Computational Biology, Department of Biological Sciences, Dornsife College of Letters, Arts & Sciences: The University of Southern California, Los Angeles, California, USA.
Kelvin J A Davies
University of Southern California · US

Funding

OXYGEN RADICAL TOXICITY AND RED CELL PROTEIN DEGRADATIONR01ES003598 · NIEHS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI DAVIES, KELVIN J. A. · 1988 to 2017
$5.7M
NIEHS NIH HHS R01 ES003598
6 · The paper itself

Abstract

Cellular proteins are exposed to oxidative modification and other forms of damage through oxidative stress and disease, and as a consequence of aging. This oxidative damage results in loss and/or modification of protein function, which in turn compromises cell function and may even cause cell death. Therefore, the removal of damaged proteins is extremely important for the maintenance of normal cell function. The 20S proteasome functions primarily as a system for removal of such damaged proteins. Unlike the 26S proteasome, the 20S proteasome exhibits a high degree of selectivity in degrading the oxidized, or otherwise damaged, forms of cell proteins. The 20S proteasome is broadly distributed throughout the cell and has a range of specific functions in different organelles, which are controlled through a number of proteasome regulators. It is also activated, and its synthesis is induced, under conditions of enhanced oxidative stress, thus permitting greater removal of damaged proteins.

Indexed as

ProteolysisAgingAnimalsFree RadicalsHumansOxidation-ReductionProteasome Endopeptidase ComplexProteinsFree RadicalsProteasome Endopeptidase ComplexProteins

Identifiers

PMID22727423
PMCPMC3710712
OpenAlexW34570582

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.