{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T04:29:08Z","timestamp":1790310548788,"version":"4.1.0"},"reference-count":113,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2012,11,1]],"date-time":"2012-11-01T00:00:00Z","timestamp":1351728000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Trends in Neurosciences"],"published-print":{"date-parts":[[2012,11]]},"DOI":"10.1016\/j.tins.2012.06.004","type":"journal-article","created":{"date-parts":[[2012,7,14]],"date-time":"2012-07-14T04:03:31Z","timestamp":1342238611000},"page":"700-709","source":"Crossref","is-referenced-by-count":221,"title":["Caspase-3 in the central nervous system: beyond apoptosis"],"prefix":"10.1016","volume":"35","author":[{"given":"Marcello","family":"D\u2019Amelio","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Morgan","family":"Sheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesco","family":"Cecconi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.tins.2012.06.004_bib0005","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1038\/35037739","article-title":"Apoptosis in the nervous system","volume":"407","author":"Yuan","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.tins.2012.06.004_bib0010","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1093\/cercor\/9.6.621","article-title":"The role of cell death in regulating the size and shape of the mammalian forebrain","volume":"9","author":"Haydar","year":"1999","journal-title":"Cereb. Cortex"},{"key":"10.1016\/j.tins.2012.06.004_bib0015","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1038\/384368a0","article-title":"Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice","volume":"384","author":"Kuida","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.tins.2012.06.004_bib0020","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1038\/nsb0796-619","article-title":"The three-dimensional structure of apopain\/CPP32, a key mediator of apoptosis","volume":"3","author":"Rotonda","year":"1996","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.tins.2012.06.004_bib0025","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1016\/j.yexcr.2012.01.027","article-title":"Non-apoptotic roles for death-related molecules: When mitochondria chose cell fate","volume":"318","author":"Strappazzon","year":"2012","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.tins.2012.06.004_bib0030","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1046\/j.1432-1327.1998.2540439.x","article-title":"Apoptosis signaling by death receptors","volume":"254","author":"Schulze-Osthoff","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.tins.2012.06.004_bib0035","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1126\/science.1099320","article-title":"The pathophysiology of mitochondrial cell death","volume":"305","author":"Green","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.tins.2012.06.004_bib0040","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1016\/j.bbabio.2006.05.032","article-title":"Mitochondria as the target of the pro-apoptotic protein Bax","volume":"1757","author":"Er","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.tins.2012.06.004_bib0045","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1152\/physrev.00013.2006","article-title":"Mitochondrial membrane permeabilization in cell death","volume":"87","author":"Kroemer","year":"2007","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.tins.2012.06.004_bib0050","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1038\/sj.cdd.4401940","article-title":"BH3-only proteins in cell death initiation, malignant disease and anticancer therapy","volume":"13","author":"Labi","year":"2006","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.tins.2012.06.004_bib0055","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0968-0004(97)01043-8","article-title":"The CARD domain: a new apoptotic signalling motif","volume":"22","author":"Hofmann","year":"1997","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.tins.2012.06.004_bib0060","doi-asserted-by":"crossref","first-page":"6067","DOI":"10.1074\/jbc.275.9.6067","article-title":"Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes","volume":"275","author":"Cain","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0065","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1038\/nrm2312","article-title":"Apoptosis: controlled demolition at the cellular level","volume":"9","author":"Taylor","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.tins.2012.06.004_bib0070","doi-asserted-by":"crossref","first-page":"14507","DOI":"10.1074\/jbc.M414425200","article-title":"c-FLIPR, a new regulator of death receptor-induced apoptosis","volume":"280","author":"Golks","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0075","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/386517a0","article-title":"Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors","volume":"386","author":"Thome","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.tins.2012.06.004_bib0080","doi-asserted-by":"crossref","first-page":"14162","DOI":"10.1074\/jbc.M212255200","article-title":"Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis","volume":"278","author":"Neumar","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0085","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1016\/S0092-8674(01)00274-4","article-title":"Structural basis for the inhibition of caspase-3 by XIAP","volume":"104","author":"Riedl","year":"2001","journal-title":"Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0090","doi-asserted-by":"crossref","first-page":"12772","DOI":"10.1074\/jbc.M807550200","article-title":"The E3 ubiquitin ligase cIAP1 binds and ubiquitinates caspase-3 and -7 via unique mechanisms at distinct steps in their processing","volume":"284","author":"Choi","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0095","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1083\/jcb.200108085","article-title":"The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites","volume":"157","author":"Silke","year":"2002","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.tins.2012.06.004_bib0100","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1101\/gad.1663108","article-title":"Regulation of apoptosis by XIAP ubiquitin-ligase activity","volume":"22","author":"Schile","year":"2008","journal-title":"Genes Dev."},{"key":"10.1016\/j.tins.2012.06.004_bib0105","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1136\/fn.77.3.F165","article-title":"Apoptosis in neural development and disease","volume":"77","author":"Mazarakis","year":"1997","journal-title":"Arch. Dis. Child."},{"key":"10.1016\/j.tins.2012.06.004_bib0110","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/S0092-8674(00)81873-5","article-title":"Programmed cell death in animal development","volume":"88","author":"Jacobson","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0115","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12035-008-8021-4","article-title":"Cell death in brain development and degeneration: control of caspase expression may be key!","volume":"37","author":"Madden","year":"2008","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.tins.2012.06.004_bib0120","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.neuro.29.051605.112800","article-title":"Adaptive roles of programmed cell death during nervous system development","volume":"29","author":"Buss","year":"2006","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0125","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1242\/dev.122.4.1165","article-title":"Widespread programmed cell death in proliferative and postmitotic regions of the fetal cerebral cortex","volume":"122","author":"Blaschke","year":"1996","journal-title":"Development"},{"key":"10.1016\/j.tins.2012.06.004_bib0130","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/j.devcel.2004.09.018","article-title":"Drosophila caspase DRONC is required for specific developmental cell death pathways and stress induced apoptosis","volume":"7","author":"Daish","year":"2004","journal-title":"Dev. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0135","doi-asserted-by":"crossref","first-page":"2125","DOI":"10.1242\/dev.01790","article-title":"The CARD-carrying caspase Dronc is essential for most, but not all, developmental cell death in Drosophila","volume":"132","author":"Xu","year":"2005","journal-title":"Development"},{"key":"10.1016\/j.tins.2012.06.004_bib0140","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1016\/j.mod.2005.04.003","article-title":"The Drosophila caspase DRONC is required for metamorphosis and cell death in response to irradiation and developmental signals","volume":"122","author":"Waldhuber","year":"2005","journal-title":"Mech. Dev."},{"key":"10.1016\/j.tins.2012.06.004_bib0145","doi-asserted-by":"crossref","first-page":"5591","DOI":"10.1242\/dev.01432","article-title":"Caspase inhibition during apoptosis causes abnormal signalling and developmental aberrations in Drosophila","volume":"131","author":"Perez-Garijo","year":"2004","journal-title":"Development"},{"key":"10.1016\/j.tins.2012.06.004_bib0150","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/S1097-2765(00)80385-8","article-title":"HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis","volume":"4","author":"Zhou","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0155","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/S1097-2765(00)80386-X","article-title":"Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1\/CED-4-related caspase activator","volume":"4","author":"Kanuka","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0160","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1093\/jnen\/61.8.673","article-title":"Strain-dependent neurodevelopmental abnormalities in caspase-3-deficient mice","volume":"61","author":"Leonard","year":"2002","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.tins.2012.06.004_bib0165","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/S0092-8674(00)81476-2","article-title":"Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9","volume":"94","author":"Kuida","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0170","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/S0092-8674(00)81732-8","article-title":"Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development","volume":"94","author":"Cecconi","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0175","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.ydbio.2004.07.026","article-title":"Early neural cell death: dying to become neurons","volume":"274","author":"Yeo","year":"2004","journal-title":"Dev. Biol."},{"key":"10.1016\/j.tins.2012.06.004_bib0180","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/s12311-009-0093-9","article-title":"Physiological Purkinje cell death is spatiotemporally organized in the developing mouse cerebellum","volume":"8","author":"Jankowski","year":"2009","journal-title":"Cerebellum"},{"key":"10.1016\/j.tins.2012.06.004_bib0185","doi-asserted-by":"crossref","first-page":"4752","DOI":"10.1523\/JNEUROSCI.21-13-04752.2001","article-title":"Programmed cell death of developing mammalian neurons after genetic deletion of caspases","volume":"21","author":"Oppenheim","year":"2001","journal-title":"J. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0190","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.1523\/JNEUROSCI.18-04-01428.1998","article-title":"Widespread elimination of naturally occurring neuronal death in Bax-deficient mice","volume":"18","author":"White","year":"1998","journal-title":"J. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0195","doi-asserted-by":"crossref","first-page":"2941","DOI":"10.1523\/JNEUROSCI.3897-07.2008","article-title":"Misplacement of Purkinje cells during postnatal development in Bax knock-out mice: a novel role for programmed cell death in the nervous system?","volume":"28","author":"Jung","year":"2008","journal-title":"J. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0200","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1096\/fj.04-2981fje","article-title":"Neural stem cell differentiation is dependent upon endogenous caspase 3 activity","volume":"19","author":"Fernando","year":"2005","journal-title":"FASEB J."},{"key":"10.1016\/j.tins.2012.06.004_bib0205","doi-asserted-by":"crossref","first-page":"11025","DOI":"10.1073\/pnas.162172899","article-title":"Caspase-3 activity is required for skeletal muscle differentiation","volume":"99","author":"Fernando","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tins.2012.06.004_bib0210","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/S1534-5807(04)00098-X","article-title":"High commitment of embryonic keratinocytes to terminal differentiation through a Notch1\u2013caspase-3 regulatory mechanism","volume":"6","author":"Okuyama","year":"2004","journal-title":"Dev. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0215","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/S0896-6273(03)00158-2","article-title":"Apoptotic pathway and MAPKs differentially regulate chemotropic responses of retinal growth cones","volume":"37","author":"Campbell","year":"2003","journal-title":"Neuron"},{"key":"10.1016\/j.tins.2012.06.004_bib0220","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/j.stem.2008.04.001","article-title":"Caspase activity mediates the differentiation of embryonic stem cells","volume":"2","author":"Fujita","year":"2008","journal-title":"Cell Stem Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0225","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1016\/j.gde.2010.08.001","article-title":"Control of embryonic stem cell identity by nucleosome remodeling enzymes","volume":"20","author":"Fazzio","year":"2010","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/j.tins.2012.06.004_bib0230","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1016\/j.neuron.2006.10.033","article-title":"Dynamic role of postsynaptic caspase-3 and BIRC4 in zebra finch song-response habituation","volume":"52","author":"Huesmann","year":"2006","journal-title":"Neuron"},{"key":"10.1016\/j.tins.2012.06.004_bib0235","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.devcel.2010.06.009","article-title":"Gradients of a ubiquitin E3 ligase inhibitor and a caspase inhibitor determine differentiation or death in spermatids","volume":"19","author":"Kaplan","year":"2010","journal-title":"Dev. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0240","doi-asserted-by":"crossref","first-page":"13366","DOI":"10.1073\/pnas.0910488107","article-title":"Maturation of the olfactory sensory neurons by Apaf-1\/caspase-9-mediated caspase activity","volume":"107","author":"Ohsawa","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tins.2012.06.004_bib0245","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1038\/nature01790","article-title":"Semaphorin 7A promotes axon outgrowth through integrins and MAPKs","volume":"424","author":"Pasterkamp","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.tins.2012.06.004_bib0250","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1146\/annurev.cellbio.23.090506.123516","article-title":"The cell biology of synaptic plasticity: AMPA receptor trafficking","volume":"23","author":"Shepherd","year":"2007","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.tins.2012.06.004_bib0255","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/j.neuron.2004.11.011","article-title":"Shrinkage of dendritic spines associated with long-term depression of hippocampal synapses","volume":"44","author":"Zhou","year":"2004","journal-title":"Neuron"},{"key":"10.1016\/j.tins.2012.06.004_bib0260","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/j.cell.2010.03.053","article-title":"Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization","volume":"141","author":"Li","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0265","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/j.neuron.2011.04.004","article-title":"Nonapoptotic function of BAD and BAX in long-term depression of synaptic transmission","volume":"70","author":"Jiao","year":"2011","journal-title":"Neuron"},{"key":"10.1016\/j.tins.2012.06.004_bib0270","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1385\/NMM:2:2:197","article-title":"Do apoptotic mechanisms regulate synaptic plasticity and growth-cone motility?","volume":"2","author":"Gilman","year":"2002","journal-title":"Neuromol. Med."},{"key":"10.1016\/j.tins.2012.06.004_bib0275","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.neuron.2006.07.014","article-title":"Identification of E2\/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning","volume":"51","author":"Kuo","year":"2006","journal-title":"Neuron"},{"key":"10.1016\/j.tins.2012.06.004_bib0280","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.neuroscience.2005.08.010","article-title":"Central administration of a caspase inhibitor impairs shuttle-box performance in rats","volume":"136","author":"Stepanichev","year":"2005","journal-title":"Neuroscience"},{"issue":"Suppl. 2","key":"10.1016\/j.tins.2012.06.004_bib0285","doi-asserted-by":"crossref","first-page":"S453","DOI":"10.3233\/JAD-2010-100321","article-title":"Oxidative stress: emerging mitochondrial and cellular themes and variations in neuronal injury","volume":"20","author":"Higgins","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.tins.2012.06.004_bib0290","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1038\/nrn2665","article-title":"Mitochondrial membrane permeabilization in neuronal injury","volume":"10","author":"Galluzzi","year":"2009","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0295","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1007\/s00702-009-0309-7","article-title":"Mitochondria in neurodegenerative disorders: regulation of the redox state and death signaling leading to neuronal death and survival","volume":"116","author":"Naoi","year":"2009","journal-title":"J. Neural Transm."},{"key":"10.1016\/j.tins.2012.06.004_bib0300","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/nrn1868","article-title":"Expanding insights of mitochondrial dysfunction in Parkinson's disease","volume":"7","author":"Abou-Sleiman","year":"2006","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0305","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1242\/jcs.03443","article-title":"A cell biological perspective on mitochondrial dysfunction in Parkinson disease and other neurodegenerative diseases","volume":"120","author":"Mandemakers","year":"2007","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.tins.2012.06.004_bib0310","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.tins.2010.08.002","article-title":"Early synaptic pathophysiology in neurodegeneration: insights from Huntington's disease","volume":"33","author":"Milnerwood","year":"2010","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0315","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/B978-0-12-385504-6.00007-5","article-title":"Regulation of caspases in the nervous system: implications for functions in health and disease","volume":"299","author":"Troy","year":"2011","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"10.1016\/j.tins.2012.06.004_bib0320","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1042\/BJ20081118","article-title":"Mechanisms of neuronal death in disease: defining the models and the players","volume":"415","author":"Ribe","year":"2008","journal-title":"Biochem. J."},{"key":"10.1016\/j.tins.2012.06.004_bib0325","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.2741\/1357","article-title":"Apoptosis in acute and chronic neurological disorders","volume":"9","author":"Ekshyyan","year":"2004","journal-title":"Front. Biosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0330","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1056\/NEJMra022366","article-title":"Apoptosis and caspases in neurodegenerative diseases","volume":"348","author":"Friedlander","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.tins.2012.06.004_bib0335","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1006\/exnr.1995.1025","article-title":"Evidence for apoptotic cell death in Alzheimer's disease","volume":"133","author":"Smale","year":"1995","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.tins.2012.06.004_bib0340","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1097\/00001756-199505090-00026","article-title":"In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes","volume":"6","author":"Dragunow","year":"1995","journal-title":"Neuroreport"},{"key":"10.1016\/j.tins.2012.06.004_bib0345","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1006\/exnr.1995.1029","article-title":"DNA end labeling (TUNEL) in Huntington's disease and other neuropathological conditions","volume":"133","author":"Thomas","year":"1995","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.tins.2012.06.004_bib0350","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1016\/S0024-3205(03)00512-5","article-title":"Quantitative assessment of DNA fragmentation and beta-amyloid deposition in insular cortex and midfrontal gyrus from patients with Alzheimer's disease","volume":"73","author":"Colurso","year":"2003","journal-title":"Life Sci."},{"key":"10.1016\/j.tins.2012.06.004_bib0355","doi-asserted-by":"crossref","first-page":"215","DOI":"10.2174\/138161211795049705","article-title":"Matter of life and death: the pharmacological approaches targeting apoptosis in brain diseases","volume":"17","author":"Cavallucci","year":"2011","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.tins.2012.06.004_bib0360","doi-asserted-by":"crossref","first-page":"230","DOI":"10.2174\/138161211795049732","article-title":"Antiapoptotic drugs: a therapeutic strategy for the prevention of neurodegenerative diseases","volume":"17","author":"Sureda","year":"2011","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.tins.2012.06.004_bib0365","doi-asserted-by":"crossref","first-page":"679","DOI":"10.2174\/187152710793237511","article-title":"Organelle stress sensors and cell death mechanisms in neurodegenerative diseases","volume":"9","author":"Viana","year":"2010","journal-title":"CNS Neurol. Disord. Drug Targets"},{"key":"10.1016\/j.tins.2012.06.004_bib0370","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1016\/j.cell.2011.10.033","article-title":"Programmed cell death in animal development and disease","volume":"147","author":"Fuchs","year":"2011","journal-title":"Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0375","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.neures.2011.05.008","article-title":"Protein aggregate spreading in neurodegenerative diseases: problems and perspectives","volume":"70","author":"Lee","year":"2011","journal-title":"Neurosci. Res."},{"key":"10.1016\/j.tins.2012.06.004_bib0380","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1038\/ng0896-442","article-title":"Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract","volume":"13","author":"Goldberg","year":"1996","journal-title":"Nat. Genet."},{"key":"10.1016\/j.tins.2012.06.004_bib0385","doi-asserted-by":"crossref","first-page":"9158","DOI":"10.1074\/jbc.273.15.9158","article-title":"Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract","volume":"273","author":"Wellington","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0390","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1097\/00019052-199708000-00003","article-title":"Of molecular interactions, mice and mechanisms: new insights into Huntington's disease","volume":"10","author":"Wellington","year":"1997","journal-title":"Curr. Opin. Neurol."},{"key":"10.1016\/j.tins.2012.06.004_bib0395","doi-asserted-by":"crossref","first-page":"19831","DOI":"10.1074\/jbc.M001475200","article-title":"Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells","volume":"275","author":"Wellington","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0400","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1146\/annurev-neuro-061010-113613","article-title":"Amyloid precursor protein processing and Alzheimer's disease","volume":"34","author":"O\u2019Brien","year":"2011","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0405","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/S0092-8674(00)80748-5","article-title":"Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-\u03b2 precursor protein and amyloidogenic A\u03b2 peptide formation","volume":"97","author":"Gervais","year":"1999","journal-title":"Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0410","doi-asserted-by":"crossref","first-page":"14761","DOI":"10.1074\/jbc.273.24.14761","article-title":"The X11a protein slows cellular amyloid precursor protein processing and reduces A\u03b240 and A\u03b242 secretion","volume":"273","author":"Borg","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0415","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1046\/j.1471-4159.2001.00513.x","article-title":"The caspase-derived C-terminal fragment of betaAPP induces caspase-independent toxicity and triggers selective increase of Abeta42 in mammalian cells","volume":"8","author":"Dumanchin-Njock","year":"2001","journal-title":"J. Neurochem."},{"key":"10.1016\/j.tins.2012.06.004_bib0420","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1126\/science.277.5324.373","article-title":"Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease","volume":"277","author":"Kim","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.tins.2012.06.004_bib0425","doi-asserted-by":"crossref","first-page":"20655","DOI":"10.1074\/jbc.272.33.20655","article-title":"Presenilins are processed by caspase-type proteases","volume":"272","author":"Loetscher","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0430","doi-asserted-by":"crossref","first-page":"16649","DOI":"10.1074\/jbc.M512026200","article-title":"The presenilin-2 loop peptide perturbs intracellular Ca2+ homeostasis and accelerates apoptosis","volume":"281","author":"Cai","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0435","doi-asserted-by":"crossref","first-page":"12064","DOI":"10.1074\/jbc.M212379200","article-title":"The C-terminal fragment of presenilin 2 triggers p53-mediated staurosporine-induced apoptosis, a function independent of the presenilinase-derived N-terminal counterpart","volume":"278","author":"Alves da Costa","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0440","doi-asserted-by":"crossref","first-page":"28315","DOI":"10.1074\/jbc.272.45.28315","article-title":"Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis, and caspase-3 cleavage","volume":"272","author":"Vito","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0445","doi-asserted-by":"crossref","first-page":"31025","DOI":"10.1074\/jbc.271.49.31025","article-title":"Requirement of the familial Alzheimer's disease PS2 for apoptosis: opposing effect of ALG-3","volume":"271","author":"Vito","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0450","doi-asserted-by":"crossref","first-page":"5961","DOI":"10.1021\/bi971763a","article-title":"Proteolytic fragments of the Alzheimer's disease associated presenilins-1 and -2 are phosphorylated in TiTo by distinct cellular mechanisms","volume":"37","author":"Walter","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.tins.2012.06.004_bib0455","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1073\/pnas.96.4.1391","article-title":"Phosphorylation of presenilin-2 regulates its cleavage by caspases and retard progression of apoptosis","volume":"96","author":"Walter","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.tins.2012.06.004_bib0460","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/j.neuron.2007.05.012","article-title":"Depletion of GGA3 stabilizes BACE and enhances beta-secretase activity","volume":"54","author":"Tesco","year":"2007","journal-title":"Neuron"},{"key":"10.1016\/j.tins.2012.06.004_bib0465","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.brainres.2008.06.094","article-title":"Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer's disease","volume":"1228","author":"Rohn","year":"2009","journal-title":"Brain Res."},{"key":"10.1016\/j.tins.2012.06.004_bib0470","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1038\/nature08890","article-title":"Caspase activation precedes and leads to tangles","volume":"464","author":"de Calignon","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.tins.2012.06.004_bib0475","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1212\/01.wnl.0000260698.46517.8f","article-title":"Synaptic alterations in CA1 in mild Alzheimer's disease and mild cognitive impairment","volume":"68","author":"Scheff","year":"2007","journal-title":"Neurology"},{"key":"10.1016\/j.tins.2012.06.004_bib0480","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/nn.2709","article-title":"Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer's disease","volume":"14","author":"D\u2019Amelio","year":"2011","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0485","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1038\/nn.2785","article-title":"A\u03b21\u201342 inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3\u03b2","volume":"14","author":"Jo","year":"2011","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0490","doi-asserted-by":"crossref","first-page":"13","DOI":"10.3389\/fnmol.2012.00013","article-title":"A pivotal role of GSK-3 in synaptic plasticity","volume":"5","author":"Bradley","year":"2012","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.tins.2012.06.004_bib0495","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/j.expneurol.2009.09.011","article-title":"GSK3: a possible link between beta amyloid peptide and tau protein","volume":"223","author":"Hern\u00e1ndez","year":"2010","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.tins.2012.06.004_bib0500","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.2353\/ajpath.2008.080434","article-title":"Caspase-3 is enriched in postsynaptic densities and increased in Alzheimer's disease","volume":"173","author":"Louneva","year":"2008","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.tins.2012.06.004_bib0505","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1002\/jnr.22227","volume":"88","author":"Sultana","year":"2010","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.tins.2012.06.004_bib0510","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/0022-510X(95)00336-Z","article-title":"Histochemical detection of apoptosis in Parkinson's disease","volume":"137","author":"Mochizuki","year":"1996","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.tins.2012.06.004_bib0515","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/j.cellsig.2010.10.020","article-title":"Apoptosis in Parkinson's disease: is p53 the missing link between genetic and sporadic Parkinsonism?","volume":"23","author":"Alves da Costa","year":"2011","journal-title":"Cell. Signal."},{"key":"10.1016\/j.tins.2012.06.004_bib0520","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/S0072-9752(07)83029-6","article-title":"Programmed cell death in Parkinson's disease","volume":"83","author":"Burke","year":"2007","journal-title":"Handb. Clin. Neurol."},{"key":"10.1016\/j.tins.2012.06.004_bib0525","doi-asserted-by":"crossref","first-page":"11515","DOI":"10.1074\/jbc.M508619200","article-title":"Caspase-3-derived C-terminal product of synphilin-1 displays antiapoptotic function via modulation of the p53-dependent cell death pathway","volume":"281","author":"Giaime","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tins.2012.06.004_bib0530","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1038\/8820","article-title":"Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions","volume":"22","author":"Engelender","year":"1999","journal-title":"Nat. Genet."},{"key":"10.1016\/j.tins.2012.06.004_bib0535","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nature09788","article-title":"Caspase signalling controls microglia activation and neurotoxicity","volume":"472","author":"Burguillos","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.tins.2012.06.004_bib0540","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.ceb.2004.09.008","article-title":"Life's smile, death's grin: vital functions of apoptosis-executing proteins","volume":"16","author":"Garrido","year":"2004","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.tins.2012.06.004_bib0545","doi-asserted-by":"crossref","first-page":"2453","DOI":"10.1091\/mbc.E09-12-1031","article-title":"Lens fiber cell differentiation and denucleation are disrupted through expression of the N-terminal nuclear receptor box of NCOA6 and result in p53-dependent and p53-independent apoptosis","volume":"21","author":"Wang","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0550","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1038\/cdd.2010.140","article-title":"Caspase-activated ROCK-1 allows erythroblast terminal maturation independently of cytokine-induced Rho signaling","volume":"18","author":"Gabet","year":"2011","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.tins.2012.06.004_bib0555","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/S1534-5807(03)00120-5","article-title":"Caspase activity and a specific cytochrome c are required for sperm differentiation in Drosophila","volume":"4","author":"Arama","year":"2003","journal-title":"Dev. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0560","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1016\/j.molcel.2007.09.030","article-title":"Nonapoptotic role for Apaf-1 in the DNA damage checkpoint","volume":"28","author":"Zermati","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1016\/j.tins.2012.06.004_bib0565","doi-asserted-by":"crossref","first-page":"3450","DOI":"10.1242\/jcs.086298","article-title":"Apaf1 plays a pro-survival role by regulating centrosome morphology and function","volume":"124","author":"Ferraro","year":"2011","journal-title":"J. Cell Sci."}],"container-title":["Trends in Neurosciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0166223612001154?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0166223612001154?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,4,26]],"date-time":"2024-04-26T17:06:40Z","timestamp":1714151200000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0166223612001154"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,11]]},"references-count":113,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2012,11]]}},"alternative-id":["S0166223612001154"],"URL":"https:\/\/doi.org\/10.1016\/j.tins.2012.06.004","relation":{},"ISSN":["0166-2236"],"issn-type":[{"value":"0166-2236","type":"print"}],"subject":[],"published":{"date-parts":[[2012,11]]}}}