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The heat shock protein response pathway is a highly conserved cellular defense mechanism activated by various forms of stress, most notably elevated temperatures. Its primary function is to maintain proteostasis by increasing the expression of molecular chaperones—heat shock proteins (HSPs)—that assist in proper protein folding, prevent aggregation of misfolded proteins, and facilitate repair or degradation of damaged proteins. The pathway is regulated by Heat Shock Factor 1 (HSF1) which induces the expression of HSPs. The pathway operates with negative feedback: increased levels of newly synthesized chaperones re-bind to free regulatory factors like HSF1 once proteostasis is restored.
Modulation of chaperone activity, HSF1 inhibition
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