Understanding of the Hsp90 molecular chaperone reaches new heights

Nat Struct Mol Biol. 2010 Dec;17(12):1400-4. doi: 10.1038/nsmb1210-1400.

Abstract

Heat shock protein 90 (Hsp90) was the focus of a recent meeting in the Swiss Alps, where the Hsp90 community met to discuss the operation and functions of this ubiquitous and essential molecular chaperone.

Publication types

  • Congress

MeSH terms

  • Anti-Infective Agents / chemistry
  • Antineoplastic Agents / chemistry
  • Biological Evolution
  • Caloric Restriction
  • Gene Expression Regulation
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / physiology*
  • Models, Molecular
  • Phosphorylation
  • Protein Folding
  • Protein Isoforms / physiology
  • Protein Structure, Tertiary

Substances

  • Anti-Infective Agents
  • Antineoplastic Agents
  • HSP90 Heat-Shock Proteins
  • Protein Isoforms