Abstract
Caspase recruitment and oligomerization mediated by adaptor proteins constitute a basic mechanism of caspase activation. The complex phenotypes of the caspase knockout mice indicate that multiple mechanisms of caspase activation operate in parallel and that death signal transduction pathways are both cell-type and stimulus specific. The BH3-domain- containing pro-apototic members of Bcl-2 family may be one of the critical links between the initial death signals and the central machinery of apoptosis.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Apoptosis / physiology*
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Apoptotic Protease-Activating Factor 1
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Arabidopsis Proteins*
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Caspases / deficiency
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Caspases / genetics
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Caspases / physiology*
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Cell Survival / physiology*
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Enzyme Activation / physiology
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Enzyme Precursors / physiology
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Fatty Acid Desaturases / deficiency
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Fatty Acid Desaturases / genetics
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Fatty Acid Desaturases / physiology
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Mice
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Mice, Knockout
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Mitochondria / physiology
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Models, Biological
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Proteins / genetics
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Proteins / physiology
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Proto-Oncogene Proteins c-bcl-2 / classification
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Proto-Oncogene Proteins c-bcl-2 / physiology
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Signal Transduction / physiology*
Substances
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Apaf1 protein, mouse
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Apoptotic Protease-Activating Factor 1
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Arabidopsis Proteins
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Enzyme Precursors
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Proteins
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Proto-Oncogene Proteins c-bcl-2
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Fatty Acid Desaturases
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Fad7 protein, Arabidopsis
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Caspases