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Elizabeth A. Slee
Researcher at Maynooth University
Publications - 13
Citations - 3993
Elizabeth A. Slee is an academic researcher from Maynooth University. The author has contributed to research in topics: Caspase & Apoptosis. The author has an hindex of 7, co-authored 8 publications receiving 3793 citations. Previous affiliations of Elizabeth A. Slee include National University of Ireland & Trinity College, Dublin.
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Journal ArticleDOI
Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner.
Elizabeth A. Slee,Mary T. Harte,Ruth M. Kluck,Beni B. Wolf,Carlos A. Casiano,Donald D. Newmeyer,Hong Gang Wang,John C. Reed,Donald W. Nicholson,Emad S. Alnemri,Douglas R. Green,Seamus J. Martin +11 more
TL;DR: Six additional caspases (caspases-2, -3, -6, -7, -8, and -10) are processed in cell-free extracts in response to cytochrome c, and that three others failed to be activated under the same conditions.
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Executioner Caspase-3, -6, and -7 Perform Distinct, Non-redundant Roles during the Demolition Phase of Apoptosis *
TL;DR: It is shown that caspase-3 is the primary executioner caspases in this system, necessary for cytochromec/dATP-inducible cleavage of fodrin, gelsolin, U1 small nuclear ribonucleoprotein, DNA fragmentation factor 45, and topoisomerase I, vimentin, Rb, and lamin B.
Journal ArticleDOI
Serial killers: ordering caspase activation events in apoptosis
TL;DR: The apoptosis-associated caspases cascade and the hierarchy of caspase activation events within it are discussed and caspasing-3 may perform an important role in propagating the caspased cascade, in addition to its role as an effector casp enzyme within the death programme.
Journal ArticleDOI
Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: a potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release.
TL;DR: It is shown that BID is cleaved in response to multiple death-inducing stimuli, but BID cleavage in these contexts was blocked by Bcl-2, suggesting that proteolysis of BID occurred distal to cytochrome c release.
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Regulation of Apoptotic Protease Activating Factor-1 Oligomerization and Apoptosis by the WD-40 Repeat Region
TL;DR: It is shown that Apaf-1 can dimerize via the CED-4 homologous and linker domains of the molecule providing a means by which Apaf -1 can promote the clustering of caspase-9 and facilitate its activation.