Evidence map›Paper›PMID 29351842›Full record

ReviewMolecular cell2018

Maintaining a Healthy Proteome during Oxidative Stress.

Dana Reichmann, Wilhelm Voth, Ursula Jakob

Abstract readReview
In one paragraph

Review in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
–field-weighted citation impact
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

103 citing papers in PubMed.

  1. Article
  2. Article
  3. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  4. Article
  5. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

43 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.

Dana ReichmannDepartment of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 91904, Israel. Electronic address: danare@mail.huji.ac.il.
Wilhelm VothDepartment of Molecular, Cellular, and Developmental Biology and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Ursula JakobDepartment of Molecular, Cellular, and Developmental Biology and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-1048, USA. Electronic address: ujakob@umich.edu.

Funding

Role of Molecular Chaperones in Stress Response and DiseaseR35GM122506 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ursula H. Jakob · 2017 to 2026
$6.8M
Mechanism of an Acid Activated ChaperoneR01GM102829 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BARDWELL, JAMES, JAKOB, URSULA H. · 2013 to 2016
$1.8M
BIOBEHAVIORAL STUDIES OF NARCOTICS ABUSE IN HUMANSK05DA000064 · NIDA · MC LEAN HOSPITAL (BELMONT, MA) · PI MENDELSON, JACK H · 1985 to 2007
$911k
NIDA NIH HHS K05 DA000064NIGMS NIH HHS R01 GM102829NIGMS NIH HHS R35 GM122506
6 · The paper itself

Abstract

Some of the most challenging stress conditions that organisms encounter during their lifetime involve the transient accumulation of reactive oxygen and chlorine species. Extremely reactive to amino acid side chains, these oxidants cause widespread protein unfolding and aggregation. It is therefore not surprising that cells draw on a variety of different strategies to counteract the damage and maintain a healthy proteome. Orchestrated largely by direct changes in the thiol oxidation status of key proteins, the response strategies involve all layers of protein protection. Reprogramming of basic biological functions helps decrease nascent protein synthesis and restore redox homeostasis. Mobilization of oxidative stress-activated chaperones and production of stress-resistant non-proteinaceous chaperones prevent irreversible protein aggregation. Finally, redox-controlled increase in proteasome activity removes any irreversibly damaged proteins. Together, these systems pave the way to restore protein homeostasis and enable organisms to survive stress conditions that are inevitable when living an aerobic lifestyle.

Indexed as

AnimalsHeat-Shock ProteinsHumansMolecular ChaperonesOxidantsOxidation-ReductionOxidative StressProtein UnfoldingProteomeProteostasisReactive Oxygen SpeciesSulfhydryl CompoundsHeat-Shock ProteinsMolecular ChaperonesOxidantsProteomeReactive Oxygen SpeciesSulfhydryl Compounds

Identifiers

PMID29351842
PMCPMC5777170

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.