Coordinated Dual Cleavages Induced by the Proteasome Regulator PA28 Lead to Dominant MHC Ligands

This publication has 31 references indexed in Scilit:

• Kinetic Characterization of the Chymotryptic Activity of the 20S Proteasome
  Biochemistry, 1996
• Incorporation of major histocompatibility complex – encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon‐γ
  European Journal of Immunology, 1995
• Primary structures of two homologous subunits of PA28, a γ‐interferon‐inducible protein activator of the 20S proteasome
  FEBS Letters, 1995
• Analysis of the fine specificity of rat, mouse and human TAP peptide transporters
  European Journal of Immunology, 1995
• Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules
  Immunity, 1995
• Existence of a molecular ruler in proteasomes suggested by analysis of degradation products
  FEBS Letters, 1994
• PA28 Activator Protein Forms Regulatory Caps on Proteasome Stacked Rings
  Journal of Molecular Biology, 1994
• Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules
  Nature, 1992
• Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends on its neighboring residues in the protein
  Cell, 1991
• Degradation of oxidized insulin B chain by the multiproteinase complex macropain (proteasome)
  Biochemistry, 1991