An Endoplasmic Reticulum Protein Implicated in Chaperoning Peptides to Major Histocompatibility of Class I Is an Aminopeptidase

This publication has 31 references indexed in Scilit:

• Detection of enzymes active on various β‐1, 3‐glucans after denaturing polyacrylamide gel electrophoresis
  Electrophoresis, 1998
• Promiscuous liberation of MHC-class I-binding peptides from the C termini of membrane and soluble proteins in the secretory pathway
  European Journal of Immunology, 1998
• Purification of Heat Shock Protein–Peptide Complexes for Use in Vaccination against Cancers and Intracellular Pathogens
  Methods, 1997
• The Rat cim Effect: TAP Allele-Dependent Changes in a Class I MHC Anchor Motif and Evidence Against C-Terminal Trimming of Peptides in the ER
  Immunity, 1996
• Molecular chaperones and the biosynthesis of antigen receptors
  Immunology Today, 1995
• A Mechanism for the Specific Immunogenicity of Heat Shock Protein-Chaperoned Peptides
  Science, 1995
• Trimming of antigenic peptides in an early secretory compartment.
  The Journal of Experimental Medicine, 1994
• Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling.
  The Journal of Experimental Medicine, 1994
• Mapping of the genes for human endoplasmic reticular heat shock protein gp96/grp94
  Somatic Cell and Molecular Genetics, 1993
• A highly specific aminotripeptidase of rat brain cytosol
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982