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• W2017452092 abstract "Apoptosis is a major form of cell death, characterized by a series of morphological changes induced by cleaving cytoplasmic and nuclear proteins via active caspases. The data presented here show, by fluorescence microscopic and immunoblotting analyses, that a prodomain of caspase-7 inhibits its nuclear translocation and apoptosis-inducing activity. This nuclear localization is dependent on the presence of a basic tetrapeptide that is conserved in mammalian and Xenopus caspase-7 and that is located downstream of a cleavage site between a prodomain and a catalytic protease domain. Furthermore, an attachment of the caspase-7 prodomain (31 amino acids) represses the nuclear transport of a fusion protein of a heterologous protein and the caspase-7 nuclear localization signal (19 amino acids), suggesting that the inhibition of nuclear localization by the prodomain is mediated by the interaction of these short peptides." @default.
• W2017452092 created "2016-06-24" @default.
• W2017452092 creator A5041188920 @default.
• W2017452092 date "2002-02-01" @default.
• W2017452092 modified "2023-10-15" @default.
• W2017452092 title "Inhibition of Nuclear Transport of Caspase-7 by Its Prodomain" @default.
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• W2017452092 doi "https://doi.org/10.1006/bbrc.2002.6408" @default.
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