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

Free Radic Biol Med. 1999 Mar;26(5-6):737-45. 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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Heat-Shock Proteins / biosynthesis*
  • Heat-Shock Proteins / physiology
  • Hot Temperature*
  • Humans
  • Mammals
  • Molecular Chaperones / physiology
  • Oxidation-Reduction
  • Oxidative Stress*
  • Protein Folding*
  • Proteins / metabolism
  • Sulfhydryl Compounds


  • Heat-Shock Proteins
  • Molecular Chaperones
  • Proteins
  • Sulfhydryl Compounds