Structural and stereochemical requirements of time-dependent inactivators of the interleukin-1β converting enzyme

This publication has 11 references indexed in Scilit:

• Aspartyl .alpha.-((1-Phenyl-3-(trifluoromethyl)- pyrazol-5-yl)oxy)methyl Ketones as Interleukin-1.beta. Converting Enzyme Inhibitors. Significance of the P1 and P3 Amido Nitrogens for Enzyme-Peptide Inhibitor Binding
  Journal of Medicinal Chemistry, 1994
• Preparation and evaluation of peptidic aspartyl hemiacetals as reversible inhibitors of interleukin‐l β converting enzyme (ICE)
  International Journal of Peptide and Protein Research, 1994
• Crystal structure of the cysteine protease interleukin-1β-converting enzyme: A (p20/p10)2 homodimer
  Cell, 1994
• Structure and mechanism of interleukin-lβ converting enzyme
  Nature, 1994
• Inactivation of Interleukin-1.beta. Converting Enzyme by Peptide (Acyloxy)methyl Ketones
  Biochemistry, 1994
• P1 Aspartate-Based Peptide .alpha.-((2,6-Dichlorobenzoyl)oxy)methyl Ketones as Potent Time-Dependent Inhibitors of Interleukin-1.beta.-Converting Enzyme
  Journal of Medicinal Chemistry, 1994
• The Role of Interleukin-1 in Disease
  New England Journal of Medicine, 1993
• A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
  Nature, 1992
• Peptidyl (acyloxy)methyl ketones and the quiescent affinity label concept: the departing group as a variable structural element in the design of inactivators of cysteine proteinases
  Biochemistry, 1991
• Alkylation of Amino Acids without Loss of Optical Activity: α‐ and β‐Alkylation of an Aspartic Acid Derivative
  Angewandte Chemie International Edition in English, 1981