ArticleJournal of structural biology: X2020
Structural analysis of missense mutations occurring in the DNA-binding domain of HSF4 associated with congenital cataracts.
Article in Journal of structural biology: X, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Heat shock transcription factors in development and disease.Disease models & mechanisms · 2026Review
- 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
- Targeting Heat Shock Transcription Factor 4 Enhances the Efficacy of Cabozantinib and Immune Checkpoint Inhibitors in Renal Cell Carcinoma.International journal of molecular sciences · 2025Article
- Article
- Aquaporin 5 maintains lens transparency by regulating the lysosomal pathway using circRNA.Journal of cellular and molecular medicine · 2023Article
- Structures of heat shock factor trimers bound to DNA.iScience · 2021Article
- More Than Meets the Eye: Revisiting the Roles of Heat Shock Factor 4 in Health and Diseases.Biomolecules · 2021Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Congenital cataract (CC) is the major cause of childish blindness, and nearly 50% of CCs are hereditary disorders. HSF4, a member of the heat shock transcription factor family, acts as a key regulator of cell growth and differentiation during the development of sensory organs. Missense mutations in the HSF4-encoding gene have been reported to cause CC formation; in particular, those occurring within the DNA-binding domain (DBD) are usually autosomal dominant mutations. To address how the identified mutations lead to HSF4 malfunction by placing adverse impacts on protein structure and DNA-binding specificity and affinity, we determined two high-resolution structures of the wild-type DBD and the K23N mutant of human HSF4, built DNA-binding models, conducted
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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.