Molecular chaperones, evolution and medicine

Peter Csermely, Csaba Soti, Eva Kalmar, Eszter Papp, Balint Pato, Akos Vermes, Amere S. Sreedhar

Research output: Contribution to journalArticleScientificpeer-review

5 Citations (Scopus)


Protein folding has numerous steps, which need assistance in vivo. Molecular chaperones are required for many proteins to fold, or re-fold into native structures forming an ancient, primary system for 'intracellular self-defense'. Molecular chaperones participate in the organization of the cytoarchitecture, were necessary for the development of modern enzymes and - by stabilizing the genome - for the development of the first stable cells. They have a profound importance in medical practice. Chaperone induction provides cytoprotection in various pathological conditions, while chaperone inhibition can be an efficient tool to fight against cancer. Chaperones are inefficient enzymes and have low-affinity interactions, therefore their assays require unusual methods, which will be summarized in the concluding part of the paper.

Original languageEnglish
Pages (from-to)373-380
JournalJournal of Molecular Structure: THEOCHEM
Publication statusPublished - 2003
Externally publishedYes


  • Heat shock proteins
  • Low affinity
  • Molecular chaperones
  • Protein folding
  • Stress proteins


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