Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/45413
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dc.contributor.authorKumar, S.-
dc.date.issued2007-
dc.identifier.citationCell Death and Differentiation, 2007; 14(1):32-43-
dc.identifier.issn1350-9047-
dc.identifier.issn1476-5403-
dc.identifier.urihttp://hdl.handle.net/2440/45413-
dc.descriptionCopyright © 2007 Nature Publishing Group. All rights reserved.-
dc.description.abstractThe first proapoptotic caspase, CED-3, was cloned from Caenorhabditis elegans in 1993 and shown to be essential for the developmental death of all somatic cells. Following the discovery of CED-3, caspases have been cloned from several vertebrate and invertebrate species. As reviewed in other articles in this issue of Cell Death and Differentiation, many caspases function in nonapoptotic pathways. However, as is clear from the worm studies, the evolutionarily conserved role of caspases is to execute programmed cell death. In this article, I will specifically focus on caspases that function primarily in cell death execution. In particular, the physiological function of caspases in apoptosis is discussed using examples from the worm, fly and mammals.-
dc.description.statementofresponsibilityS Kumar-
dc.language.isoen-
dc.publisherNature Publishing Group-
dc.source.urihttp://www.nature.com/cdd/journal/v14/n1/pdf/4402060a.pdf-
dc.subjectAnimals-
dc.subjectHumans-
dc.subjectCaspases-
dc.subjectApoptosis-
dc.subjectBiological Evolution-
dc.titleCaspase function in programmed cell death-
dc.typeJournal article-
dc.identifier.doi10.1038/sj.cdd.4402060-
pubs.publication-statusPublished-
dc.identifier.orcidKumar, S. [0000-0001-7126-9814]-
Appears in Collections:Aurora harvest 6
Medicine publications

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