Activation of CPP32 and Mch3 alpha in wild-type p53-induced apoptosis.

Ítems similars

• Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis.
  per: Takahashi, A, et al.
  Publicat: (1996)
• Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32.
  per: Slee, E A, et al.
  Publicat: (1996)
• In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.
  per: Fernandes-Alnemri, T, et al.
  Publicat: (1996)
• Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells.
  per: Faleiro, L, et al.
  Publicat: (1997)
• Cytokine suppression of protease activation in wild-type p53-dependent and p53-independent apoptosis
  per: Lotem, Joseph, et al.
  Publicat: (1997)