Sequence-Specific Repression of Cotranslational Translocation of the Hepatitis B Virus Envelope Proteins Coincides with Binding of Heat Shock Protein Hsc70

This publication has 16 references indexed in Scilit:

• The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation.
  The Journal of cell biology, 1996
• The Hepatitis B Virus Large Surface Protein (LHBs) Is a Transcriptional Activator
  Virology, 1996
• Post-translational protein translocation: not all hsc70s are created equal
  Trends in Biochemical Sciences, 1996
• A C-Terminal PRES1 Sequence Is Sufficient to Retain Hepatitis B Virus L Protein in 293 Cells
  Virology, 1995
• Selection of peptide inhibitors of interactions involved in complex protein assemblies: association of the core and surface antigens of hepatitis B virus.
  Proceedings of the National Academy of Sciences, 1995
• MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS
  Annual Review of Biochemistry, 1993
• Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment.
  The Journal of cell biology, 1992
• The role of envelope proteins in hepatitis B virus assembly.
  Proceedings of the National Academy of Sciences, 1991
• A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
  Nature, 1988
• Multiple topogenic sequences determine the transmembrane orientation of the hepatitis B surface antigen.
  Molecular and Cellular Biology, 1987