Evidence map›Paper›PMID 25681016›Full record

ReviewJournal of molecular biology2015

A first line of stress defense: small heat shock proteins and their function in protein homeostasis.

Martin Haslbeck, Elizabeth Vierling

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 303 papers.

0numbers the graph read from it
0cells of the map it votes in
303citing 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

303 citing papers in PubMed.

  1. Article
  2. The kinetic basis of photosynthetic heat tolerance.Nature ecology & evolution · 2026
    Article
  3. Article
  4. Article
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  6. Article
  7. Review
  8. Review
  9. Article
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  12. Review
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  14. Article
  15. Article
  16. Article
  17. Human Crystallin Variation and Cataract.Investigative ophthalmology & visual science · 2026
    Review
  18. Article
  19. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  20. Article

243 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

2 authors.

Martin HaslbeckDepartment Chemie, Technische Universität München, Lichtenbergstrasse 4, 85 748 Garching, Germany. Electronic address: martin.haslbeck@tum.de.
Elizabeth VierlingDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Life Science Laboratories, N329 240 Thatcher Road, Amherst, MA 01003-9364, USA. Electronic address: vierling@biochem.umass.edu.

Funding

Structure/Function of Small Heat Shock ProteinsR01GM042762 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI VIERLING, ELIZABETH · 1989 to 2014
$3.6M
NIGMS NIH HHS R01 GM042762NIGMS NIH HHS R01 GM42762
6 · The paper itself

Abstract

Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can prevent the irreversible aggregation of denaturing proteins. sHsps complex with a variety of non-native proteins in an ATP-independent manner and, in the context of the stress response, form a first line of defense against protein aggregation in order to maintain protein homeostasis. In vertebrates, they act to maintain the clarity of the eye lens, and in humans, sHsp mutations are linked to myopathies and neuropathies. Although found in all domains of life, sHsps are quite diverse and have evolved independently in metazoans, plants and fungi. sHsp monomers range in size from approximately 12 to 42kDa and are defined by a conserved β-sandwich α-crystallin domain, flanked by variable N- and C-terminal sequences. Most sHsps form large oligomeric ensembles with a broad distribution of different, sphere- or barrel-like oligomers, with the size and structure of the oligomers dictated by features of the N- and C-termini. The activity of sHsps is regulated by mechanisms that change the equilibrium distribution in tertiary features and/or quaternary structure of the sHsp ensembles. Cooperation and/or co-assembly between different sHsps in the same cellular compartment add an underexplored level of complexity to sHsp structure and function.

Indexed as

HomeostasisAnimalsEvolution, MolecularHeat-Shock Proteins, SmallHumansModels, MolecularMolecular ChaperonesProteinsProtein Structure, QuaternaryStress, PhysiologicalHeat-Shock Proteins, SmallMolecular ChaperonesProteinsmolecular chaperonesprotein aggregationprotein foldingstress responseα-crystallin

Identifiers

PMID25681016
PMCPMC4360138

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.