Evidence map›Paper›PMID 26727490›Full record

ArticleNature structural & molecular biology2016

Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors.

Alex M Jaeger, Charles W Pemble, Lea Sistonen, Dennis J Thiele

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 78 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
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  4. Article
  5. Review
  6. Article
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  8. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  9. Review
  10. International journal of molecular sciences · 2024
    Article
  11. Review
  12. Article
  13. Review
  14. HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023
    Review
  15. The function and regulation of heat shock transcription factor inFrontiers in cellular and infection microbiology · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Evolution and co-evolution: insights into the divergence of plant heat shock factor genes.Physiology and molecular biology of plants : an international journal of functional plant biology · 2022
    Article
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

4 authors at 2 institutions in 2 countries.

Alex M JaegerDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, North Carolina, USA.
Charles W PembleDuke University Human Vaccine Institute Macromolecular Crystallography Center, Duke University School of Medicine, Durham, North Carolina, USA.
Lea SistonenDepartment of Biosciences, Åbo Akademi University, Turku, Finland.ORCID http://orcid.org/0000-0003-1341-2867
Dennis J ThieleDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, North Carolina, USA.
Duke University · USÅbo Akademi University · FI

Funding

Pharmacological Sciences Training ProgramT32GM007105 · NIGMS · DUKE UNIVERSITY · PI KUHN, CYNTHIA M · 1985 to 2019
$9.0M
HSF1 as a therapeutic target in neurodegenerative diseaseR01NS065890 · NINDS · DUKE UNIVERSITY · PI THIELE, DENNIS J · 2010 to 2013
$1.3M
NIGMS NIH HHS T32 GM007105NINDS NIH HHS R01 NS065890
6 · The paper itself

Abstract

Heat-shock transcription factor (HSF) family members function in stress protection and in human diseases including proteopathies, neurodegeneration and cancer. The mechanisms that drive distinct post-translational modifications, cofactor recruitment and target-gene activation for specific HSF paralogs are unknown. We present crystal structures of the human HSF2 DNA-binding domain (DBD) bound to DNA, revealing an unprecedented view of HSFs that provides insights into their unique biology. The HSF2 DBD structures resolve a new C-terminal helix that directs wrapping of the coiled-coil domain around DNA, thereby exposing paralog-specific sequences of the DBD surface for differential post-translational modifications and cofactor interactions. We further demonstrate a direct interaction between HSF1 and HSF2 through their coiled-coil domains. Together, these features provide a new model for HSF structure as the basis for differential and combinatorial regulation, which influences the transcriptional response to cellular stress.

Indexed as

Amino Acid SequenceBase SequenceCrystallography, X-RayDNADNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHumansModels, MolecularMolecular Sequence DataProtein ConformationProtein Interaction Domains and MotifsSumoylationTranscription FactorsDNADNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHSF1 protein, humanHSF2 protein, humanTranscription Factors

Identifiers

PMID26727490
PMCPMC4973471
OpenAlexW2229818272

What OpenQuestion holds

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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.