Evidence map›Paper›PMID 8441385›Full record

ArticleMolecular and cellular biology1993

Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress.

K D Sarge, S P Murphy, R I Morimoto

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 312 papers.

0numbers the graph read from it
0cells of the map it votes in
312citing papers in PubMed
17.6field-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

312 citing papers in PubMed, 876 citations in OpenAlex.

  1. Adaptation to heat stress by diversification of the vertebrate heat shock transcription factor family.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Identification of novel small molecule chaperone activators for neurodegenerative disease treatment.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. International journal of molecular sciences · 2024
    Article
  15. Article
  16. Thermal Stress and Nuclear Transport.Advances in experimental medicine and biology · 2024
    Review
  17. Review
  18. HSP90β prevents aging-related cataract formation through regulation of the charged multivesicular body protein (CHMP4B) and p53.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article

252 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

K D SargeDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208.
S P Murphy
R I Morimoto
Northwestern University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The existence of multiple heat shock factor (HSF) genes in higher eukaryotes has promoted questions regarding the functions of these HSF family members, especially with respect to the stress response. To address these questions, we have used polyclonal antisera raised against mouse HSF1 and HSF2 to examine the biochemical, physical, and functional properties of these two factors in unstressed and heat-shocked mouse and human cells. We have identified HSF1 as the mediator of stress-induced heat shock gene transcription. HSF1 displays stress-induced DNA-binding activity, oligomerization, and nuclear localization, while HSF2 does not. Also, HSF1 undergoes phosphorylation in cells exposed to heat or cadmium sulfate but not in cells treated with the amino acid analog L-azetidine-2-carboxylic acid, indicating that phosphorylation of HSF1 is not essential for its activation. Interestingly, HSF1 and HSF2 overexpressed in transfected 3T3 cells both display constitutive DNA-binding activity, oligomerization, and transcriptional activity. These results demonstrate that HSF1 can be activated in the absence of physiological stress and also provide support for a model of regulation of HSF1 and HSF2 activity by a titratable negative regulatory factor.

Indexed as

Transcription, Genetic3T3 CellsAnimalsAntibody SpecificityBase SequenceCell NucleusCytoplasmDNA-Binding ProteinsEscherichia coliFluorescent Antibody TechniqueGene Expression RegulationHeat-Shock ProteinsHeat Shock Transcription FactorsHot TemperatureHumansMiceDNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHSF1 protein, humanHSF2 protein, humanTranscription Factors

Identifiers

PMID8441385
PMCPMC359449
OpenAlexW2119624960

What OpenQuestion holds

Textmetadata
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.