Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli

This publication has 53 references indexed in Scilit:

• Degradation versus Aggregation of Misfolded Maltose-binding Protein in the Periplasm of Escherichia coli
  Journal of Biological Chemistry, 1998
• The Proteasome: Paradigm of a Self-Compartmentalizing Protease
  Cell, 1998
• Crystal structure of heat shock locus V (HslV) from Escherichia coli
  Proceedings of the National Academy of Sciences, 1997
• Building bridges: disulphide bond formation in the cell
  Molecular Microbiology, 1994
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
  Nature, 1994
• Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
  Gene, 1993
• Mammalian heat shock protein families. Expression and functions
  Cellular and Molecular Life Sciences, 1992
• Refined structure of baboon α-lactalbumin at 1.7 Å resolution
  Journal of Molecular Biology, 1989
• Electron microscopy and image analysis of the multicatalytic proteinase
  FEBS Letters, 1988
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976