Evidence map›Paper›PMID 28893460›Full record

ReviewTrends in biochemical sciences2017

Stress-Activated Chaperones: A First Line of Defense.

Wilhelm Voth, Ursula Jakob

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

58 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. A J-domain protein enhances memory by promoting physiological amyloid formation inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Article
  10. Proteomic Analysis of the Differential Response ofAntibiotics (Basel, Switzerland) · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Transcriptional Regulation Mechanisms in Adaptively EvolvedJournal of fungi (Basel, Switzerland) · 2025
    Article
  19. A microaerobically induced small heat shock protein contributes toApplied and environmental microbiology · 2025
    Article
  20. Review
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 2 institutions in 2 countries.

Wilhelm VothDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA; Department of Molecular Biology, Universitätsmedizin Göttingen, 37073 Göttingen, Germany.
Ursula JakobDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: ujakob@umich.edu.
Universitätsmedizin Göttingen · DEUniversity of Michigan–Ann Arbor · US

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
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
Polyphosphate - A Novel Member of the Proteostasis NetworkR01GM116582 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2015 to 2016
$913k
Characterization of bleach-specific transcriptional regulators in bacteriaR21AI097893 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2012 to 2013
$417k
NIAID NIH HHS R21 AI097893NIGMS NIH HHS R01 GM065318NIGMS NIH HHS R01 GM102829NIGMS NIH HHS R01 GM116582NIGMS NIH HHS R35 GM122506
6 · The paper itself

Abstract

Proteins are constantly challenged by environmental stress conditions that threaten their structure and function. Especially problematic are oxidative, acid, and severe heat stress which induce very rapid and widespread protein unfolding and generate conditions that make canonical chaperones and/or transcriptional responses inadequate to protect the proteome. We review here recent advances in identifying and characterizing stress-activated chaperones which are inactive under non-stress conditions but become potent chaperones under specific protein-unfolding stress conditions. We discuss the post-translational mechanisms by which these chaperones sense stress, and consider the role that intrinsic disorder plays in their regulation and function. We examine their physiological roles under both non-stress and stress conditions, their integration into the cellular proteostasis network, and their potential as novel therapeutic targets.

Indexed as

AnimalsHumansMolecular ChaperonesOxidative StressProtein Processing, Post-TranslationalProtein UnfoldingProteomeMolecular ChaperonesProteomemolecular chaperoneoxidative stressprotein aggregationprotein unfoldingproteostasis

Identifiers

PMID28893460
PMCPMC5659914
OpenAlexW2751048227

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.