Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol

Angew Chem Int Ed Engl. 2009;48(32):5853-5. doi: 10.1002/anie.200900929.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cell Cycle Proteins / antagonists & inhibitors
  • Cell Cycle Proteins / metabolism*
  • Chaperonins / antagonists & inhibitors
  • Chaperonins / metabolism*
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors
  • HSP90 Heat-Shock Proteins / metabolism*
  • Humans
  • Pentacyclic Triterpenes
  • Protein Folding
  • Triterpenes / chemistry*
  • Triterpenes / pharmacology

Substances

  • CDC37 protein, human
  • Cell Cycle Proteins
  • HSP90 Heat-Shock Proteins
  • Pentacyclic Triterpenes
  • Triterpenes
  • Chaperonins
  • celastrol