Evidence map›Paper›PMID 32253742›Full record

ReviewCell stress & chaperones2020

Small heat-shock proteins and their role in mechanical stress.

Miranda P Collier, Justin L P Benesch

Abstract readReview
In one paragraph

Review in Cell stress & chaperones, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
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  3. Birth Season and Breed Effects on NewbornAnimals : an open access journal from MDPI · 2026
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  17. MicroRNAs as the Sentinels of Redox and Hypertrophic Signalling.International journal of molecular sciences · 2022
    Review
  18. Article
  19. Article
  20. Article
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.

Miranda P CollierDepartment of Biology, Stanford University, 318 Campus Drive, Stanford, CA, 94305, USA.
Justin L P BeneschDepartment of Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK. justin.benesch@chem.ox.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of cells to respond to stress is central to health. Stress can damage folded proteins, which are vulnerable to even minor changes in cellular conditions. To maintain proteostasis, cells have developed an intricate network in which molecular chaperones are key players. The small heat-shock proteins (sHSPs) are a widespread family of molecular chaperones, and some sHSPs are prominent in muscle, where cells and proteins must withstand high levels of applied force. sHSPs have long been thought to act as general interceptors of protein aggregation. However, evidence is accumulating that points to a more specific role for sHSPs in protecting proteins from mechanical stress. Here, we briefly introduce the sHSPs and outline the evidence for their role in responses to mechanical stress. We suggest that sHSPs interact with mechanosensitive proteins to regulate physiological extension and contraction cycles. It is likely that further study of these interactions - enabled by the development of experimental methodologies that allow protein contacts to be studied under the application of mechanical force - will expand our understanding of the activity and functions of sHSPs, and of the roles played by chaperones in general.

Indexed as

Heat-Shock Proteins, SmallProteostasisStress, MechanicalAnimalsHeat-Shock ProteinsHumansMiceMolecular ChaperonesProtein FoldingHeat-Shock ProteinsHeat-Shock Proteins, SmallHsbp1 protein, mouseMolecular ChaperonesCardiomyocytesFilamin CFLNCHspB8Mechanical stressMechanosensingMolecular chaperonesMonodispersityMusclePolydispersityProteostasissHSPsSmall heat-shock proteins

Identifiers

PMID32253742
PMCPMC7332611

What OpenQuestion holds

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LicenceCC BY
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.