Evidence map›Paper›PMID 28890254›Full record

ReviewTrends in cell biology2017

Rethinking HSF1 in Stress, Development, and Organismal Health.

Jian Li, Johnathan Labbadia, Richard I Morimoto

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

175 citing papers in PubMed, 278 citations in OpenAlex.

  1. Article
  2. Ferroptosis in heatstroke: Mechanisms and therapeutic perspectives (Review).International journal of molecular medicine · 2026
    Review
  3. Article
  4. More than the 'master regulator of cytosolic proteostasis': new roles for HSF1 in promoting tissue health.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  5. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Article
  8. c-MYC is an aggregation-prone, amyloidogenic protein.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

115 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 3 institutions in 2 countries.

Jian LiDepartment of Molecular Biosciences, Rice Institute for Biomedical Research Northwestern University, Evanston, IL 60208, USA; Present address: Functional and Chemical Genomics Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA.
Johnathan LabbadiaDepartment of Molecular Biosciences, Rice Institute for Biomedical Research Northwestern University, Evanston, IL 60208, USA; Present address: Institute of Healthy Ageing, Genetics, Evolution and Environment, University College London, WC1E 6BT, UK.
Richard I MorimotoDepartment of Molecular Biosciences, Rice Institute for Biomedical Research Northwestern University, Evanston, IL 60208, USA. Electronic address: r-morimoto@northwestern.edu.
Northwestern University · USRice Institute · USUniversity College London · GB

Funding

Role of LUBAC and Na K-ATPase in Acute Lung InjuryP01HL071643 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SZNAJDER, JACOB I · 2003 to 2019
$30.8M
Tissue resident macrophages regulate proteostasis in the aging lungP01AG049665 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GR Scott Budinger · 2015 to 2026
$26.9M
C. elegans Model for Neurodegenerative Diseases of AgingR37AG026647 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2010 to 2019
$3.9M
Biotechnology and Biological Sciences Research CouncilNHLBI NIH HHS P01 HL071643NIA NIH HHS P01 AG049665NIA NIH HHS R37 AG026647
6 · The paper itself

Abstract

The heat shock response (HSR) was originally discovered as a transcriptional response to elevated temperature shock and led to the identification of heat shock proteins and heat shock factor 1 (HSF1). Since then HSF1 has been shown to be important for combating other forms of environmental perturbations as well as genetic variations that cause proteotoxic stress. The HSR has long been thought to be an absolute response to conditions of cell stress and the primary mechanism by which HSF1 promotes organismal health by preventing protein aggregation and subsequent proteome imbalance. Accumulating evidence now shows that HSF1, the central player in the HSR, is regulated according to specific cellular requirements through cell-autonomous and non-autonomous signals, and directs transcriptional programs distinct from the HSR during development and in carcinogenesis. We discuss here these 'non-canonical' roles of HSF1, its regulation in diverse conditions of development, reproduction, metabolism, and aging, and posit that HSF1 serves to integrate diverse biological and pathological responses.

Indexed as

Heat-Shock ResponseAnimalsCarcinogenesisHeat-Shock ProteinsHeat Shock Transcription FactorsHumansModels, BiologicalProtein Aggregation, PathologicalProteomeSignal TransductionHeat-Shock ProteinsHeat Shock Transcription FactorsHSF1 protein, humanProteomecell proliferationheat shock response (HSR)HSF1metabolismorganismal healthproteostasis

Identifiers

PMID28890254
PMCPMC5696061
OpenAlexW2751896753

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.