Evidence map›Paper›PMID 8455593›Full record

ArticleMolecular and cellular biology1993

Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway.

A Nakai, R I Morimoto

Open 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. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

70 citing papers in PubMed, 265 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. Review
  3. Review
  4. Article
  5. Heat shock proteins with an emphasis on HSP 60.Molecular biology reports · 2021
    Review
  6. Article
  7. Review
  8. Review
  9. Regulation of gene expression in chickens by heat stress.Journal of animal science and biotechnology · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Tailoring of Proteostasis Networks with Heat Shock Factors.Cold Spring Harbor perspectives in biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

10 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 at 1 institution in 1 country.

A NakaiDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208.
R I Morimoto
Northwestern University · US

Funding

REGULATION AND EXPRESSION OF THE HSP70 GENE FAMILYR37GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2000 to 2009
$5.6M
REGULATION AND EXPRESSION OF THE HUMAN HSP70 GENE FAMILYR01GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 1987 to 2013
$2.2M
NIGMS NIH HHS GM38109
6 · The paper itself

Abstract

We have cloned three avian heat shock transcription factor (HSF) genes corresponding to a novel factor, HSF3, and the avian homologs of mammalian HSF1 and HSF2. The predicted amino acid sequence of HSF3 is approximately 40% related to the sequence of HSF1 and HSF2. The sequences for all three factors exhibit extensive identify in the DNA binding motifs and the heptad repeats of hydrophobic amino acids which are common to all eukaryotic HSFs. Despite these overall similarities, each avian HSF exhibits distinct DNA binding properties. HSF2 when expressed in vitro binds constitutively to the heat shock element promoter sequence, whereas neither HSF1 nor HSF3 expressed in vitro binds to DNA. HSF1 DNA binding is induced upon heat shock or treatment with nonionic detergents, whereas the DNA binding properties of HSF3 are not induced by these conditions in vitro. These results suggest that HSF3 activation may involve an induction pathway distinct from the traditional forms of heat shock gene induction. HSF3 DNA binding activity, however, is obtained when the carboxyl-terminal region including the distal heptad repeat is deleted, indicating the presence of negative cis-regulatory sequences. The HSF3 message, like HSF1 and HSF2 messages, is coexpressed during development and in most tissues, which suggests a general role for the regulatory pathway involving HSF3.

Indexed as

Gene Expression RegulationAge FactorsAmino Acid SequenceAnimalsBase SequenceChickensCloning, MolecularConsensus SequenceDNA-Binding ProteinsGenesHeat-Shock ProteinsHeat Shock Transcription FactorsIn Situ HybridizationMolecular Sequence DataOligodeoxyribonucleotidesRestriction MappingDNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsOligodeoxyribonucleotidesRNA, MessengerTranscription Factors

Identifiers

PMID8455593
PMCPMC359520
OpenAlexW1954249603

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.