@inbook{2abe133fe51549f89f182ffbddd41230,
title = "Monitoring of the heat shock response with a real-time luciferase reporter",
abstract = "The heat shock response (HSR) is a cellular mechanism for counteracting acute proteotoxic stress. In eukaryotes, transcriptional activation of the HSR is regulated by heat shock factor 1 (HSF1). Activation of HSF1 induces the expression of heat shock proteins (HSPs) that function as molecular chaperones to fold and maintain the three-dimensional structure of misfolded proteins. The regulation of the degree and duration of the HSR is controlled by multiple biochemical mechanisms that include posttranslational modification of HSF1 and numerous protein-protein interactions. In this chapter, we describe a method to evaluate the activation and deactivation of the HSR at the transcriptional level using a short half-life luciferase reporter assay. This assay can be used to further characterize the HSR or as a screen for small-molecule inducers, amplifiers, or repressors.",
keywords = "Drug screen, Heat shock factor 1 (HSF1), Heat shock protein 90 (HSP90), Heat shock response, Luciferase assay, Real-time",
author = "Toshiki Kijima and Takanori Eguchi and Len Neckers and Prince, {Thomas L.}",
note = "Publisher Copyright: {\textcopyright} 2018, Springer Science+Business Media, LLC.",
year = "2018",
doi = "10.1007/978-1-4939-7477-1_3",
language = "English",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "35--45",
booktitle = "Methods in Molecular Biology",
}