Death and survival signals determine active/inactive conformations of pro-apoptotic BAX, BAD, and BID molecules

Cold Spring Harb Symp Quant Biol. 1999;64:343-50. doi: 10.1101/sqb.1999.64.343.
No abstract available

Publication types

  • Review

MeSH terms

  • Animals
  • Antigens, CD / metabolism
  • Apoptosis / physiology*
  • BH3 Interacting Domain Death Agonist Protein
  • Biological Transport, Active
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Caspase 8
  • Caspase 9
  • Caspases / metabolism
  • Cell Death
  • Cell Survival
  • Dimerization
  • Humans
  • Mitochondria / metabolism
  • Models, Biological
  • Models, Molecular
  • Phosphorylation
  • Protein Conformation
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-bcl-2*
  • Receptors, Tumor Necrosis Factor / metabolism
  • Receptors, Tumor Necrosis Factor, Type I
  • Signal Transduction
  • bcl-2-Associated X Protein
  • bcl-Associated Death Protein
  • fas Receptor / metabolism

Substances

  • Antigens, CD
  • BAD protein, human
  • BAX protein, human
  • BH3 Interacting Domain Death Agonist Protein
  • BID protein, human
  • Carrier Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Receptors, Tumor Necrosis Factor
  • Receptors, Tumor Necrosis Factor, Type I
  • bcl-2-Associated X Protein
  • bcl-Associated Death Protein
  • fas Receptor
  • CASP8 protein, human
  • CASP9 protein, human
  • Caspase 8
  • Caspase 9
  • Caspases