On the path to the heat shock response: destabilization and formation of partially folded protein intermediates, a consequence of protein thiol modification.

Freeman ML, Borrelli MJ, Meredith MJ, Lepock JR
Free Radic Biol Med. 1999 26 (5-6): 737-45

PMID: 10218664 · DOI:10.1016/s0891-5849(98)00258-5

This review discusses the initial events that occur during oxidative stress that induce the synthesis of heat shock proteins. The focus is on non-native oxidation or modification of protein thiols and the destablization that can result. Proteins that contain non-native modified thiols can become destablized such that they unfold into molten globule-like intermediates at or below 37 degrees C, relieving Hsf-1 negative regulation, and inducing Hsp transcription.

MeSH Terms (11)

Animals Heat-Shock Proteins Hot Temperature Humans Mammals Molecular Chaperones Oxidation-Reduction Oxidative Stress Protein Folding Proteins Sulfhydryl Compounds

Connections (1)

This publication is referenced by other Labnodes entities:

Links