Evidence map›Paper›PMID 32331382›Full record

ReviewCells2020

HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity.

Thomas L Prince, Benjamin J Lang, Martin E Guerrero-Gimenez, Juan Manuel Fernandez-Muñoz, Andrew Ackerman, Stuart K Calderwood

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. HSPBiomedicines · 2025
    Article
  7. Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  8. Review
  9. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
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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

6 authors at 3 institutions in 2 countries.

Thomas L PrinceDepartment of Molecular Functional Genomics, Geisinger Clinic, Danville, PA 17821, USA.ORCID 0000-0003-3333-9599
Benjamin J LangDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-2205-8591
Martin E Guerrero-GimenezLaboratory of Oncology, Institute of Medicine and Experimental Biology of Cuyo (IMBECU), National Scientific and Technical Research Council (CONICET), Buenos Aires B1657, Argentina.ORCID 0000-0002-5306-5065
Juan Manuel Fernandez-MuñozLaboratory of Oncology, Institute of Medicine and Experimental Biology of Cuyo (IMBECU), National Scientific and Technical Research Council (CONICET), Buenos Aires B1657, Argentina.ORCID 0000-0003-1827-4926
Andrew AckermanDepartment of Molecular Functional Genomics, Geisinger Clinic, Danville, PA 17821, USA.ORCID 0000-0002-9218-3224
Stuart K CalderwoodDepartment of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0001-9966-3354
Beth Israel Deaconess Medical Center · USConsejo Nacional de Investigaciones Científicas y Técnicas · ARGeisinger Medical Center · US

Funding

Complex Role of HSF1 in Breast CancerR01CA176326 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CALDERWOOD, STUART KEITH, SHERMAN, MICHAEL Y · 2014 to 2018
$1.8M
NCI NIH HHS R01 CA176326
6 · The paper itself

Abstract

Heat shock factor 1 (HSF1) is the primary component for initiation of the powerful heat shock response (HSR) in eukaryotes. The HSR is an evolutionarily conserved mechanism for responding to proteotoxic stress and involves the rapid expression of heat shock protein (HSP) molecular chaperones that promote cell viability by facilitating proteostasis. HSF1 activity is amplified in many tumor contexts in a manner that resembles a chronic state of stress, characterized by high levels of

Indexed as

AnimalsCell Transformation, NeoplasticHeat Shock Transcription FactorsHumansMolecular ChaperonesMolecular Targeted TherapyMorbidityNeoplasmsHeat Shock Transcription FactorsMolecular Chaperonescancercancer therapyheat shock factor 1heat shock proteinsheat shock responseHSF1HSF1 expression in cancerHSF1 in cancerHSPsHSRmetastasismolecular chaperonestumorigenesis

Identifiers

PMID32331382
PMCPMC7226471
OpenAlexW3018281064

What OpenQuestion holds

Textmetadata
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.