ArticleNature structural & molecular biology2016
Structure of human heat-shock transcription factor 1 in complex with DNA.
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 75 papers.
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.
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.
Who cites it
75 citing papers in PubMed, 124 citations in OpenAlex.
- 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 · 2026Review
- DNA-Induced Entropic Gain Triggers an Allosteric Switch for Biomolecular Condensation of Heat Shock Transcription Factor 1.Angewandte Chemie (International ed. in English) · 2026Article
- Evolution of Hsp90 targeting: From stress biology to clinical translation.Cell stress & chaperones · 2026Review
- Functional interplay between heat shock protein 90 (HSP90) and heat shock factors (HSFs).Cell stress & chaperones · 2026Review
- Heat shock transcription factors in development and disease.Disease models & mechanisms · 2026Review
- Article
- Article
- Promoter and domain swap analysis delineates heat stress memory-specific determinants of heat shock factor HSFA2.Plant physiology · 2025Article
- Article
- A guide to heat shock factors as multifunctional transcriptional regulators.The FEBS journal · 2025Review
- The Structural Deciphering of the α3 Helix Within ZmHsfA2'S DNA-Binding Domain for the Recognition of Heat Shock Elements in Maize.Plants (Basel, Switzerland) · 2025Article
- Identifying Genes Associated with the Anticancer Activity of a Fluorinated Chalcone in Triple-Negative Breast Cancer Cells Using Bioinformatics Tools.International journal of molecular sciences · 2025Article
- HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025Review
- Review
- Single-cell multi-modal integrative analyses highlight functional dynamic gene regulatory networks directing human cardiac development.Cell genomics · 2024Article
- Discovery of a CK2α'-Biased ATP-Competitive Inhibitor from a High-Throughput Screen of an Allosteric-Inhibitor-Like Compound Library.ACS chemical neuroscience · 2024Article
- Article
- Alternative Splicing Reveals Acute Stress Response of Litopenaeus vannamei at High Alkalinity.Marine biotechnology (New York, N.Y.) · 2024Article
- Stress biology: Complexity and multifariousness in health and disease.Cell stress & chaperones · 2024Article
- Identification of CK2α' selective inhibitors by the screening of an allosteric-kinase-inhibitor-like compound library.bioRxiv : the preprint server for biology · 2024Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock transcription factor 1 (HSF1) has a central role in mediating the protective response to protein conformational stresses in eukaryotes. HSF1 consists of an N-terminal DNA-binding domain (DBD), a coiled-coil oligomerization domain, a regulatory domain and a transactivation domain. Upon stress, HSF1 trimerizes via its coiled-coil domain and binds to the promoters of heat shock protein-encoding genes. Here, we present cocrystal structures of the human HSF1 DBD in complex with cognate DNA. A comparative analysis of the HSF1 paralog Skn7 from Chaetomium thermophilum showed that single amino acid changes in the DBD can switch DNA binding specificity, thus revealing the structural basis for the interaction of HSF1 with cognate DNA. We used a crystal structure of the coiled-coil domain of C. thermophilum Skn7 to develop a model of the active human HSF1 trimer in which HSF1 embraces the heat-shock-element DNA.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.