Mammalian initiator apoptotic caspases

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Human initiator caspases trigger apoptotic and autophagic phenotypes in Saccharomyces cerevisiae.

Caspases are a family of proteases that participate in the progression and execution of the apoptotic program. However, regulation of the caspase activation and their substrates has not yet been fully elucidated. Here we explore the effect of the ectopic expression of the human initiator caspases-8 and -10 in Saccharomyces cerevisiae. Our results showed that the expression of human CASP10 and C...

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Caspases play a critical role in the execution of metazoan apoptosis and are thus attractive therapeutic targets for apoptosis-associated diseases. Here we report that baculovirus P49, a homolog of pancaspase inhibitor P35, prevents apoptosis in invertebrates by inhibiting an initiator caspase that is P35 insensitive. Consequently P49 blocked proteolytic activation of effector caspases at a uni...

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Interaction Between Mitochondria and Caspases: Apoptotic and Non-Apoptotic Roles

Mitochondria, play an important role in a variety of processes including energy production, apoptosis, autophagy and inflammation. Caspases, are proteases that play an essential role in mediating apoptotic process of programmed cell death. An association between mitochondria and caspases is very well defined during apoptosis. Besides apoptosis, emerging data is strongly suggesting a direct asso...

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Proapoptotic BAX and BAK control multiple initiator caspases.

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Apoptotic signaling pathways: caspases and stress-activated protein kinases.

Apoptotic cell death is an active process mediated by various signaling pathways, which include the caspase cascade and the stress-activated protein kinase pathways. The caspase cascade is activated by two distinct routes: one from cell surface and the other from mitochondria. Activation of the route from cell surface requires the cellular components that include membrane receptors, adaptor pro...

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ژورنال

عنوان ژورنال: FEBS Journal

سال: 2005

ISSN: 1742-464X,1742-4658

DOI: 10.1111/j.1742-4658.2005.04966.x