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Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
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Smac/DIABLO selectively reduces the levels of cIAP1 and cIAP2 but not that of XIAP and livin in HeLa cells
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Nuclear import of proinflammatory transcription factors is required for massive liver apoptosis induced by bacterial lipopolysaccharide
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Optimization of mouse model of fulminant hepatic failure by factorial experiment
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Lipopolysaccharide and D-galactosamine-induced hepatsic injury is mediated by TNF-alpha and not by Fas ligand
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Fibroblast growth factor 2-mediated translational control of IAPs blocks mitochondrial release of Smac /DIABLO and apoptosis in small cell lung cancer cells
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Smac/Diablo antagonizes ubiquitin ligase activity of inhibitor of apoptosis proteins
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The inhibitor of apoptosis protein 2 binding domain of Smac is not essential for its proapoptotic activity
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Mature DIABLO /Smac is produced by the IMP protease complex on the mitochondrial inner membrane
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