Molecular chaperones: small heat shock proteins in the limelight

Curr Biol. 1999 Feb 11;9(3):R103-5. doi: 10.1016/s0960-9822(99)80061-x.

Abstract

Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / physiology
  • Cataract / genetics
  • Crystallins / chemistry
  • Crystallins / genetics
  • Evolution, Molecular
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / physiology*
  • Humans
  • Intermediate Filament Proteins / chemistry
  • Intermediate Filament Proteins / physiology
  • Macromolecular Substances
  • Mice
  • Mice, Knockout
  • Multigene Family
  • Protein Folding*

Substances

  • Bacterial Proteins
  • Crystallins
  • Heat-Shock Proteins
  • Intermediate Filament Proteins
  • Macromolecular Substances