Bovine Spleen Multicatalytic Proteinase Complex (Proteasome)

This publication has 50 references indexed in Scilit:

• On the size of the active site in proteases. I. Papain
  Published by Elsevier ,2005
• 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
• Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins
  Current Biology, 1994
• Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon‐γ for acquirement of the functional diversity responsible for antigen processing
  FEBS Letters, 1994
• Peptide selection by class I molecules of the major histocompatibility complex
  Current Biology, 1993
• Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy
  FEBS Letters, 1991
• The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria
  FEBS Letters, 1989
• A multicatalytical protease complex from pituitary that forms enkephalin and enkephalin containing peptides
  Biochemical and Biophysical Research Communications, 1981
• Sulfoxide-Carbodiimide Reactions. I. A Facile Oxidation of Alcohols
  Journal of the American Chemical Society, 1965