Reassembly of Active Caspase-3 Is Facilitated by the Propeptide

This publication has 39 references indexed in Scilit:

• pH effects on the stability and dimerization of procaspase‐3
  Protein Science, 2005
• Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3
  Biochemical Journal, 2004
• Mutations in the Procaspase-3 Dimer Interface Affect the Activity of the Zymogen
  Biochemistry, 2003
• An Uncleavable Procaspase-3 Mutant Has a Lower Catalytic Efficiency but an Active Site Similar to That of Mature Caspase-3
  Biochemistry, 2003
• Human Caspase-7 Activity and Regulation by Its N-terminal Peptide
  Journal of Biological Chemistry, 2003
• Removal of the Pro-Domain Does Not Affect the Conformation of the Procaspase-3 Dimer
  Biochemistry, 2001
• Dimeric Procaspase-3 Unfolds via a Four-State Equilibrium Process
  Biochemistry, 2001
• The short prodomain influences caspase-3 activation in HeLa cells
  Biochemical Journal, 2000
• Oncogene-dependent apoptosis in extracts from drug-resistant cells.
  Genes & Development, 1997
• Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants
  Protein Science, 1993