Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/130916
Citations
Scopus Web of Science® Altmetric
?
?
Full metadata record
DC FieldValueLanguage
dc.contributor.authorLim, Y.en
dc.contributor.authorDorstyn, L.en
dc.contributor.authorKumar, S.en
dc.date.issued2021en
dc.identifier.citationExperimental and Molecular Medicine, 2021; 53(4):517-527en
dc.identifier.issn0378-8512en
dc.identifier.issn2092-6413en
dc.identifier.urihttp://hdl.handle.net/2440/130916-
dc.description.abstractCaspase-2 was discovered almost three decades ago. It was one of the first two mammalian homologs of CED-3, the other being interleukin 1β-converting enzyme (ICE/caspase-1). Despite high similarity with CED-3 and its fly and mammalian counterparts (DRONC and caspase-9, respectively), the function of caspase-2 in apoptosis has remained enigmatic. A number of recent studies suggest that caspase-2 plays an important role in the regulation of p53 in response to cellular stress and DNA damage to prevent the proliferation and accumulation of damaged or aberrant cells. Here, we review these recent observations and their implications in caspase-2-mediated cellular death, senescence, and tumor suppression.en
dc.description.statementofresponsibilityYoon Lim, Loretta Dorstyn and Sharad Kumaren
dc.language.isoenen
dc.publisherKorean Society of Medical Biochemistry and Molecular Biologyen
dc.rights© The Author(s) 2021. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any mediumor format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changesweremade. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.en
dc.titleThe p53-caspase-2 axis in the cell cycle and DNA damage responseen
dc.typeJournal articleen
dc.identifier.doi10.1038/s12276-021-00590-2en
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1103006en
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1156601en
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1144500en
pubs.publication-statusPublisheden
dc.identifier.orcidKumar, S. [0000-0001-7126-9814]en
Appears in Collections:Molecular and Biomedical Science publications

Files in This Item:
File Description SizeFormat 
hdl_130916.pdf1.37 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.