Evidence map›Paper›PMID 21767633›Full record

ArticleFree radical biology & medicine2011

HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress.

Tilman Grune, Betül Catalgol, Anke Licht, Gennady Ermak, Andrew M Pickering, Jenny K Ngo, Kelvin J A Davies

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed, 1 pooled it
5.7field-weighted citation impact, top 3% 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

110 citing papers in PubMed, 1 synthesis or guideline pooled it, 216 citations in OpenAlex.

  1. Pooled it
  2. Article
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  4. Review
  5. Article
  6. Review
  7. Article
  8. Mechanisms of Biological Aging with Special Reference to the Skeletal Muscle.Advances in experimental medicine and biology · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Discovery and Development of Cyclic Peptide Proteasome Stimulators.Chembiochem : a European journal of chemical biology · 2024
    Article
  14. Article
  15. Review
  16. Review
  17. Article
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  19. Article
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50 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

7 authors at 2 institutions in 2 countries.

Tilman GruneInstitute of Nutrition, Department of Nutritional Toxicology, Friedrich Schiller University, Jena, Germany. tilman.grune@uni-jena.de
Betül Catalgol
Anke Licht
Gennady Ermak
Andrew M Pickering
Jenny K Ngo
Kelvin J A Davies
University of Southern California · USFriedrich Schiller University Jena · DE

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

We report an entirely new role for the HSP70 chaperone in dissociating 26S proteasome complexes (into free 20S proteasomes and bound 19S regulators), preserving 19S regulators, and reconstituting 26S proteasomes in the first 1-3h after mild oxidative stress. These responses, coupled with direct 20S proteasome activation by poly(ADP ribose) polymerase in the nucleus and by PA28αβ in the cytoplasm, instantly provide cells with increased capacity to degrade oxidatively damaged proteins and to survive the initial effects of stress exposure. Subsequent adaptive (hormetic) processes (3-24h after stress exposure), mediated by several signal transduction pathways and involving increased transcription/translation of 20S proteasomes, immunoproteasomes, and PA28αβ, abrogate the need for 26S proteasome dissociation. During this adaptive period, HSP70 releases its bound 19S regulators, 26S proteasomes are reconstituted, and ATP-stimulated proteolysis is restored. The 26S proteasome-dependent, and ATP-stimulated, turnover of ubiquitinylated proteins is essential for normal cell metabolism, and its restoration is required for successful stress adaptation.

Indexed as

Adaptation, PhysiologicalCell NucleusCytoplasmHSP70 Heat-Shock ProteinsHumansImmunoprecipitationK562 CellsMuscle ProteinsOxidation-ReductionOxidative StressPoly(ADP-ribose) PolymerasesProteasome Endopeptidase ComplexProtein BindingProtein BiosynthesisProteolysisSignal Transduction26S proteasome non-ATPase regulatory subunit 13ATP dependent 26S proteaseHSP70 Heat-Shock ProteinsMuscle ProteinsPoly(ADP-ribose) PolymerasesProteasome Endopeptidase ComplexPSME1 protein, humanPSME2 protein, human

Identifiers

PMID21767633
PMCPMC3172204
OpenAlexW1990040633

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.