Evidence map›Paper›PMID 22564544›Full record

ArticleArchives of biochemistry and biophysics2012

Differential roles of proteasome and immunoproteasome regulators Pa28αβ, Pa28γ and Pa200 in the degradation of oxidized proteins.

Andrew M Pickering, Kelvin J A Davies

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
4.7field-weighted citation impact, top 4% 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

94 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

  1. Pooled it
  2. APOE4 disrupts the central dogma by arresting neuronal proteome dynamics.bioRxiv : the preprint server for biology · 2026
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  9. Tracking proteasome degradation: A cross-organ analysis via intact degradomics mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  17. Review
  18. Adaptation of the Tumor Antigen Presentation Machinery to Ionizing Radiation.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Article
  19. PSME4 determines mesenchymal stem cell fate towards cardiac commitment through YAP1 degradation.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2023
    Article
  20. Review

34 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, The University of Southern California, Los Angeles, CA 90089-0191, 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 3R01-ES 003598-22S2NIEHS NIH HHS R01 ES003598NIEHS NIH HHS R01-ES003598
6 · The paper itself

Abstract

The response and functions of proteasome regulators Pa28αβ (or 11S), Pa28γ and Pa200 in oxidative-stress adaptation (also called hormesis) was studied in murine embryonic fibroblasts (MEFs), using a well-characterized model of cellular adaptation to low concentrations (1.0-10.0 μM) of hydrogen peroxide (H(2)O(2)), which alter gene expression profiles, increasing resistance to higher levels of oxidative-stress. Pa28αβ bound to 20S proteasomes immediately upon H(2)O(2)-treatment, whereas 26S proteasomes were disassembled at the same time. Over the next 24h, the levels of Pa28αβ, Pa28γ and Pa200 proteasome regulators increased during H(2)O(2)-adaptation, whereas the 19S regulator was unchanged. Purified Pa28αβ, and to a lesser extent Pa28γ, significantly increased the ability of purified 20S proteasome to selectively degrade oxidized proteins; Pa28αβ also increased the capacity of purified immunoproteasome to selectively degrade oxidized proteins but Pa28γ did not. Pa200 regulator actually decreased 20S proteasome and immunoproteasome's ability to degrade oxidized proteins but Pa200 and poly-ADP ribose polymerase may cooperate in enabling initiation of DNA repair. Our results indicate that cytoplasmic Pa28αβ and nuclear Pa28γ may both be important regulators of proteasome's ability to degrade oxidatively-damaged proteins, and induced-expression of both 20S proteasome and immunoproteasome, and their Pa28αβ and Pa28γ regulators are important for oxidative-stress adaptation.

Indexed as

ProteolysisAnimalsAutoantigensCell LineHydrogen PeroxideMiceNuclear ProteinsOxidative StressProteasome Endopeptidase ComplexAutoantigensHydrogen PeroxideKi antigenNuclear ProteinsPa200 protein, mouseProteasome Endopeptidase ComplexPsme1 protein, mouse

Identifiers

PMID22564544
PMCPMC3384713
OpenAlexW2032194164

What OpenQuestion holds

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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.