Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/115539
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dc.titleEmerging roles of caspase-3 in apoptosis
dc.contributor.authorPorter, A.G.
dc.contributor.authorJänicke, R.U.
dc.date.accessioned2014-12-12T07:16:48Z
dc.date.available2014-12-12T07:16:48Z
dc.date.issued1999
dc.identifier.citationPorter, A.G.,Jänicke, R.U. (1999). Emerging roles of caspase-3 in apoptosis. Cell Death and Differentiation 6 (2) : 99-104. ScholarBank@NUS Repository.
dc.identifier.issn13509047
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/115539
dc.description.abstractCaspases are crucial mediators of programmed cell death (apoptosis). Among them, caspase-3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins. However, the specific requirements of this (or any other) caspase in apoptosis have remained largely unknown until now. Pathways to caspase-3 activation have been identified that are either dependent on or independent of mitochondrial cytochrome c release and caspase-9 function. Caspase-9 is essential for normal brain development and is important or essential in other apoptotic scenarios in a remarkable tissue-, cell type- or death stimulus-specific manner. Caspase-3 is also required for some typical hallmarks of apoptosis, and is indispensable for apoptotic chromatin condensation and DNA fragmentation in all cell types examined. Thus, caspase-3 is essential for certain processes associated with the dismantling of the cell and the formation of apoptotic bodies, but it may also function before or at the stage when commitment to loss of cell viability is made.
dc.sourceScopus
dc.subjectApoptotic morphology
dc.subjectCaspase-3
dc.subjectCytochrome c
dc.subjectDNA fragmentation
dc.typeReview
dc.contributor.departmentINSTITUTE OF MOLECULAR & CELL BIOLOGY
dc.description.sourcetitleCell Death and Differentiation
dc.description.volume6
dc.description.issue2
dc.description.page99-104
dc.description.codenCDDIE
dc.identifier.isiutNOT_IN_WOS
Appears in Collections:Staff Publications

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