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Hiroshi Sakurai

Researcher at Kanazawa University

Publications -  50
Citations -  1671

Hiroshi Sakurai is an academic researcher from Kanazawa University. The author has contributed to research in topics: Heat shock factor & HSF1. The author has an hindex of 20, co-authored 48 publications receiving 1559 citations. Previous affiliations of Hiroshi Sakurai include RMIT University.

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A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II.

Henri Marc Bourbon, +47 more
- 04 Jun 2004 - 
TL;DR: A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II is proposed.
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Identification of a novel class of target genes and a novel type of binding sequence of heat shock transcription factor in Saccharomyces cerevisiae.

TL;DR: It is revealed that Hsf1 is necessary for heat-induced transcription of not only HSP but also genes encoding proteins involved in diverse cellular processes such as protein degradation, detoxification, energy generation, carbohydrate metabolism, and maintenance of cell wall integrity.
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Novel aspects of heat shock factors: DNA recognition, chromatin modulation and gene expression.

TL;DR: This minireview focuses on the molecular mechanisms of DNA recognition, chromatin modulation and gene expression by yeast and mammalian HSFs.
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Saccharomyces cerevisiae Heat Shock Transcription Factor Regulates Cell Wall Remodeling in Response to Heat Shock

TL;DR: The results suggest that Hsf1 in concert with Pkc1 regulates cell wall remodeling in response to heat shock, and several of the other suppressors were found to encode proteins functioning in cell wall organization.
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Phosphorylation of the yeast heat shock transcription factor is implicated in gene-specific activation dependent on the architecture of the heat shock element.

TL;DR: It is suggested that CTM alleviates repression by CE2, which allows HSF to be heat-inducibly phosphorylated and presume that phosphorylation is a prerequisite for the activator function of HSF when it binds to an atypical HSE.