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.

Authors

S J Korsmeyer¹, A Gross, H Harada, J Zha, K Wang, X M Yin, M Wei, S Zinkel

Affiliation

¹ Departments of Pathology and Medicine, Harvard Medical School, and Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.

PMID: 11232306
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