Browsing Genetics (Scholarly Publications) by Author "CREAGH, EMMA"
Now showing items 1-6 of 6
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Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2
CREAGH, EMMA; MARTIN, SEAMUS JOSEPH (2001)Smac/DIABLO is a mitochondrial protein that potentiates some forms of apoptosis, possibly by neutralizing one or more members of the IAP family of apoptosis inhibitory proteins. Smac has been shown to exit mitochondria and ... -
Bicaudal is a conserved substrate for Drosophila and mammalian caspases and is essential for cell survival.
MARTIN, SEAMUS; CREAGH, EMMA (2009)Members of the caspase family of cysteine proteases coordinate cell death through restricted proteolysis of diverse protein substrates and play a conserved role in apoptosis from nematodes to man. However, while numerous ... -
CARDINAL, a novel caspase recruitment domain protein, is an inhibitor of multiple NF-kappa B activation pathways.
CREAGH, EMMA; MARTIN, SEAMUS (2001)Proteins possessing the caspase recruitment domain (CARD) motif have been implicated in pathways leading to activation of caspases or NF-kappaB in the context of apoptosis or inflammation, respectively. Here we report the ... -
Caspase-dependent inactivation of proteasome function during programmed cell death in Drosophila and man
MARTIN, SEAMUS JOSEPH; CREAGH, EMMA (The American Society for Biochemistry and Molecular Biology, 2004)The caspase family of cysteine proteases plays a conserved role in the coordinate demolition of cellular structures during programmed cell death from nematodes to man. Because cells undergoing programmed cell death in ... -
Interchain proteolysis, in the absence of a dimerization stimulus, can initiate apoptosis-associated caspase-8 activation
MARTIN, SEAMUS; CREAGH, EMMA (2004)Caspases coordinate the internal demolition of the cell that is seen during apoptosis. Proteolytic processing of caspases is observed during apoptosis, and this correlates with conversion of inactive caspase proenzymes ... -
Smac/Diablo antagonizes ubiquitin ligase activity of inhibitor of apoptosis proteins
MARTIN, SEAMUS; CREAGH, EMMA (2004)Inhibitor of apoptosis proteins (IAPs) can block apoptosis through binding to active caspases and antagonizing their function. IAP function can be neutralized by Smac/Diablo, an IAP-binding protein that is released from ...