Abstract
Since Ritossa’s seminal discovery in 1962 that the puffing pattern changes of Drosophila salivary gland polytene chromosomes can be induced by heat shock and chemical treatment (Ritossa, 1962), the heat shock response (HSR) has served as an excellent model and paradigm of inducible gene expression. During the ensuing decades considerable evidence has accumulated, from diverse areas of biology, about the regulation of the stress response during development, homeostatic maintenance of organs and organisms, and pathophysiological conditions. From bacteria to man, environmental stress, cell growth, differentiation, and pathophysiological states are all known to induce the rapid and reversible synthesis of evolutionary conserved set of proteins commonly termed, heat shock proteins (HSPs). HSPs, acting as molecular chaperones, play essential roles in protein folding, trafficking, higher order assembly and degradation of proteins thereby ensuring survival under both stressful and extreme physiological conditions (Lindquist, 1986; Lindquist and Craig, 1988; Morimoto, 1998).
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Orosz, A., Benjamin, I.J. (2007). Genetic Models of HSF Function. In: Calderwood, S.K. (eds) Cell Stress Proteins. Protein Reviews, vol 7. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39717-7_5
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DOI: https://doi.org/10.1007/978-0-387-39717-7_5
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