Evidence map›Paper›PMID 25698115›Full record

ReviewJournal of molecular biology2015

Protein quality control under oxidative stress conditions.

Jan-Ulrik Dahl, Michael J Gray, Ursula Jakob

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
5.9field-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

116 citing papers in PubMed, 188 citations in OpenAlex.

  1. Article
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  9. Article
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  11. Review
  12. Factors governing the response ofFrontiers in cellular and infection microbiology · 2026
    Review
  13. Cell membrane asymmetries and cellular aging.The Biochemical journal · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Photoregulation of lipid metabolism inFrontiers in plant science · 2025
    Article
  20. Review

56 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

3 authors at 1 institution in 1 country.

Jan-Ulrik DahlDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Michael J GrayDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Ursula JakobDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA. Electronic address: ujakob@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Functional Analysis of the Intrinsically Disordered Chaperone Hsp33R01GM065318 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2003 to 2015
$3.9M
Mechanism of an Acid Activated ChaperoneR01GM102829 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BARDWELL, JAMES, JAKOB, URSULA H. · 2013 to 2016
$1.8M
Cellular stress response to the oxidizing effects of bleachF32GM096613 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GRAY, MICHAEL JEFFREY · 2011 to 2012
$101k
NIGMS NIH HHS F32 GM096613NIGMS NIH HHS F32GM096613NIGMS NIH HHS R01 GM065318NIGMS NIH HHS R01GM065318NIGMS NIH HHS R01 GM102829
6 · The paper itself

Abstract

Accumulation of reactive oxygen and chlorine species (RO/CS) is generally regarded to be a toxic and highly undesirable event, which serves as contributing factor in aging and many age-related diseases. However, it is also put to excellent use during host defense, when high levels of RO/CS are produced to kill invading microorganisms and regulate bacterial colonization. Biochemical and cell biological studies of how bacteria and other microorganisms deal with RO/CS have now provided important new insights into the physiological consequences of oxidative stress, the major targets that need protection, and the cellular strategies employed by organisms to mitigate the damage. This review examines the redox-regulated mechanisms by which cells maintain a functional proteome during oxidative stress. We will discuss the well-characterized redox-regulated chaperone Hsp33, and we will review recent discoveries demonstrating that oxidative stress-specific activation of chaperone function is a much more widespread phenomenon than previously anticipated. New members of this group include the cytosolic ATPase Get3 in yeast, the Escherichia coli protein RidA, and the mammalian protein α2-macroglobulin. We will conclude our review with recent evidence showing that inorganic polyphosphate (polyP), whose accumulation significantly increases bacterial oxidative stress resistance, works by a protein-like chaperone mechanism. Understanding the relationship between oxidative and proteotoxic stresses will improve our understanding of both host-microbe interactions and how mammalian cells combat the damaging side effects of uncontrolled RO/CS production, a hallmark of inflammation.

Indexed as

AnimalsAnti-Infective AgentsChlorine CompoundsHumansOxidation-ReductionOxidative StressProtein AggregatesProteinsProtein UnfoldingReactive Oxygen SpeciesAnti-Infective AgentsChlorine CompoundsProtein AggregatesProteinsReactive Oxygen Speciesdisulfide bond formationmolecular chaperoneN-chlorinationoxidative stressprotein aggregation

Identifiers

PMID25698115
PMCPMC4357566
OpenAlexW2086749432

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.