ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2026
Adaptation to heat stress by diversification of the vertebrate heat shock transcription factor family.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Cells survive and reproduce by coping with acute or chronic exposure to a fixed elevated temperature or fluctuating temperatures. These properties are one of the main evolutionary forces and involve the heat shock response. This response is characterized by the induction of heat-shock proteins (HSPs) and is mainly regulated by heat-shock transcription factors (HSFs) in vertebrates. A single HSF is present in yeast and invertebrates, such as Caenorhabditis elegans and Drosophila, whereas vertebrates have evolved multiple HSFs. The potential of HSFs to induce HSP expression is linked to the amino acid conservation of their domains and regions that are responsible for transcriptional activation and appears to be associated with the homeothermic capacity of vertebrate animals in a thermally fluctuating environment. HSFs protect cells and organisms from heat stress by regulating not only their expression of HSPs that assist in protein folding and suppress protein misfolding and aggregation, but also the expression of genes related to protein clearance, metabolism, the cell cycle, DNA damage response, apoptosis, senescence, the cytoskeleton, extracellular matrix and inflammation. The diversification of HSF genes may expand the cellular capacity to adapt to thermal changes in vertebrate animals. This article is part of the Theo Murphy meeting issue 'ProteostaSys: a systems view of proteostasis'.
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Identifiers
What Socratic 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 Socratic graph.