Formation of a Major Histocompatibility Complex Class I Tapasin Disulfide Indicates a Change in Spatial Organization of the Peptide-loading Complex during Assembly

This publication has 26 references indexed in Scilit:

• Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin
  Nature Immunology, 2007
• ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
  The EMBO Journal, 2006
• Redox Regulation Facilitates Optimal Peptide Selection by MHC Class I during Antigen Processing
  Cell, 2006
• A Specific Interface between Integrin Transmembrane Helices and Affinity for Ligand
  PLoS Biology, 2004
• Disulfide Bond Isomerization and the Assembly of MHC Class I-Peptide Complexes
  Immunity, 2002
• ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain
  The FASEB Journal, 2001
• The Role of ERp57 in Disulfide Bond Formation during the Assembly of Major Histocompatibility Complex Class I in a Synchronized Semipermeabilized Cell Translation System
  Published by Elsevier ,2000
• β2-Microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins
  Molecular Immunology, 1997
• Interaction of the Thiol-Dependent Reductase ERp57 with Nascent Glycoproteins
  Science, 1997
• Characterization of class I MHC folding intermediates and their disparate interactions with peptide and β2-microglobulin
  Molecular Immunology, 1995