{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T11:24:43Z","timestamp":1770290683143,"version":"3.49.0"},"reference-count":64,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2019,7,22]],"date-time":"2019-07-22T00:00:00Z","timestamp":1563753600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0219782","type":"journal-article","created":{"date-parts":[[2019,7,22]],"date-time":"2019-07-22T17:32:23Z","timestamp":1563816743000},"page":"e0219782","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":8,"title":["Cullin-4B E3 ubiquitin ligase mediates Apaf-1 ubiquitination to regulate caspase-9 activity"],"prefix":"10.1371","volume":"14","author":[{"given":"Eri","family":"Ohta","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masanori","family":"Itoh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masashi","family":"Ueda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoko","family":"Hida","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miao-xing","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miki","family":"Hayakawa-Ogura","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shimo","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emika","family":"Nishida","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kazunori","family":"Ohta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"family":"Tana","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Saiful","family":"Islam","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kiyomi","family":"Nakagawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomomi","family":"Sunayama","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Huayue","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"So","family":"Hirata","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masashi","family":"Endo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6777-4252","authenticated-orcid":true,"given":"Yoya","family":"Ohno","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8415-4119","authenticated-orcid":true,"given":"Toshiyuki","family":"Nakagawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2019,7,22]]},"reference":[{"issue":"4","key":"ref1","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/bjc.1972.33","article-title":"Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics","volume":"26","author":"JF Kerr","year":"1972","journal-title":"Br J Cancer"},{"issue":"1","key":"ref2","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1038\/cdd.2009.168","article-title":"Regulation of death receptor signaling by the ubiquitin system","volume":"17","author":"IE Wertz","year":"2010","journal-title":"Cell Death Differ"},{"issue":"3","key":"ref3","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/S0092-8674(00)80501-2","article-title":"Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3","volume":"90","author":"H Zou","year":"1997","journal-title":"Cell"},{"issue":"3","key":"ref4","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1016\/j.cell.2010.03.017","article-title":"Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4","volume":"141","author":"S Qi","year":"2010","journal-title":"Cell"},{"issue":"2","key":"ref5","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1242\/dev.116.2.309","article-title":"The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death","volume":"116","author":"J Yuan","year":"1992","journal-title":"Development"},{"issue":"5","key":"ref6","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/12984","article-title":"Dark is a Drosophila homologue of Apaf-1\/CED-4 and functions in an evolutionarily conserved death pathway","volume":"1","author":"A Rodriguez","year":"1999","journal-title":"Nat Cell Biol"},{"issue":"5","key":"ref7","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":"H Kanuka","year":"1999","journal-title":"Mol Cell"},{"issue":"5","key":"ref8","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":"L Zhou","year":"1999","journal-title":"Mol Cell"},{"issue":"1","key":"ref9","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0092-8674(00)80085-9","article-title":"Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c","volume":"86","author":"X Liu","year":"1996","journal-title":"Cell"},{"issue":"36","key":"ref10","doi-asserted-by":"crossref","first-page":"24400","DOI":"10.1074\/jbc.M804664200","article-title":"Parcs is a dual regulator of cell proliferation and apaf-1 function","volume":"283","author":"R Sanchez-Olea","year":"2008","journal-title":"J Biol Chem"},{"issue":"12","key":"ref11","doi-asserted-by":"crossref","first-page":"9239","DOI":"10.1074\/jbc.M006309200","article-title":"A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis","volume":"276","author":"ZL Chu","year":"2001","journal-title":"J Biol Chem"},{"issue":"38","key":"ref12","doi-asserted-by":"crossref","first-page":"39942","DOI":"10.1074\/jbc.M405747200","article-title":"Induced inhibition of ischemic\/hypoxic injury by APIP, a novel Apaf-1-interacting protein","volume":"279","author":"DH Cho","year":"2004","journal-title":"J Biol Chem"},{"issue":"1","key":"ref13","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S1097-2765(05)00021-3","article-title":"Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1","volume":"6","author":"BN Chau","year":"2000","journal-title":"Mol Cell"},{"issue":"8","key":"ref14","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1038\/35019501","article-title":"Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome","volume":"2","author":"HM Beere","year":"2000","journal-title":"Nat Cell Biol"},{"issue":"8","key":"ref15","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1038\/35019510","article-title":"Negative regulation of the Apaf-1 apoptosome by Hsp70","volume":"2","author":"A Saleh","year":"2000","journal-title":"Nat Cell Biol"},{"issue":"16","key":"ref16","doi-asserted-by":"crossref","first-page":"4310","DOI":"10.1093\/emboj\/19.16.4310","article-title":"Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90","volume":"19","author":"P Pandey","year":"2000","journal-title":"Embo J"},{"issue":"36","key":"ref17","doi-asserted-by":"crossref","first-page":"13397","DOI":"10.1073\/pnas.0604224103","article-title":"Matefin\/SUN-1 is a nuclear envelope receptor for CED-4 during Caenorhabditis elegans apoptosis","volume":"103","author":"YB Tzur","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"ref18","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.bbrc.2015.12.102","article-title":"CED-4 is an mRNA-binding protein that delivers ced-3 mRNA to ribosomes","volume":"470","author":"MX Wang","year":"2016","journal-title":"Biochem Biophys Res Commun"},{"issue":"5457","key":"ref19","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1126\/science.287.5457.1485","article-title":"Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death","volume":"287","author":"F Chen","year":"2000","journal-title":"Science"},{"issue":"3","key":"ref20","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/sj.cdd.4402288","article-title":"A biochemical analysis of the activation of the Drosophila caspase DRONC","volume":"15","author":"L Dorstyn","year":"2008","journal-title":"Cell Death Differ"},{"issue":"3","key":"ref21","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.molcel.2009.01.014","article-title":"Nonproteolytic functions of ubiquitin in cell signaling","volume":"33","author":"ZJ Chen","year":"2009","journal-title":"Mol Cell"},{"issue":"3","key":"ref22","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.tcb.2009.01.004","article-title":"Ubiquitin-mediated regulation of apoptosis","volume":"19","author":"M Broemer","year":"2009","journal-title":"Trends Cell Biol"},{"issue":"11","key":"ref23","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1038\/nsb989","article-title":"Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination","volume":"10","author":"J Chai","year":"2003","journal-title":"Nat Struct Biol"},{"issue":"6","key":"ref24","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1038\/ncb799","article-title":"The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis","volume":"4","author":"R Wilson","year":"2002","journal-title":"Nat Cell Biol"},{"issue":"4","key":"ref25","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.molcel.2008.09.025","article-title":"Inactivation of effector caspases through nondegradative polyubiquitylation","volume":"32","author":"M Ditzel","year":"2008","journal-title":"Mol Cell"},{"issue":"3","key":"ref26","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":"CT Kuo","year":"2006","journal-title":"Neuron"},{"issue":"6","key":"ref27","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1038\/ncb793","article-title":"Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms","volume":"4","author":"SJ Yoo","year":"2002","journal-title":"Nat Cell Biol"},{"issue":"10","key":"ref28","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1242\/dev.050088","article-title":"A novel F-box protein is required for caspase activation during cellular remodeling in Drosophila","volume":"137","author":"M Bader","year":"2010","journal-title":"Development"},{"issue":"3","key":"ref29","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.cell.2011.03.021","article-title":"A conserved f box regulatory complex controls proteasome activity in Drosophila","volume":"145","author":"M Bader","year":"2011","journal-title":"Cell"},{"issue":"15","key":"ref30","doi-asserted-by":"crossref","first-page":"8662","DOI":"10.1073\/pnas.161506698","article-title":"Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death","volume":"98","author":"Y Suzuki","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"19","key":"ref31","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":"YE Choi","year":"2009","journal-title":"J Biol Chem"},{"issue":"35","key":"ref32","doi-asserted-by":"crossref","first-page":"26661","DOI":"10.1016\/S0021-9258(19)61427-4","article-title":"The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7","volume":"275","author":"H Huang","year":"2000","journal-title":"J Biol Chem"},{"issue":"4","key":"ref33","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/j.cell.2009.03.015","article-title":"Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling","volume":"137","author":"Z Jin","year":"2009","journal-title":"Cell"},{"issue":"6","key":"ref34","doi-asserted-by":"crossref","first-page":"888","DOI":"10.1016\/j.molcel.2012.09.031","article-title":"TRAF2 Sets a Threshold for Extrinsic Apoptosis by Tagging Caspase-8 with a Ubiquitin Shutoff Timer","volume":"48","author":"F Gonzalvez","year":"2012","journal-title":"Mol Cell"},{"issue":"2","key":"ref35","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1093\/jb\/mvi029","article-title":"X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac\/DIABLO","volume":"137","author":"Y Morizane","year":"2005","journal-title":"J Biochem"},{"issue":"26","key":"ref36","doi-asserted-by":"crossref","first-page":"10510","DOI":"10.1073\/pnas.1200094109","article-title":"Patched dependence receptor triggers apoptosis through ubiquitination of caspase-9","volume":"109","author":"J Fombonne","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"4","key":"ref37","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1083\/jcb.200711066","article-title":"E2-25K\/Hip-2 regulates caspase-12 in ER stress-mediated Abeta neurotoxicity","volume":"182","author":"S Song","year":"2008","journal-title":"J Cell Biol"},{"issue":"10","key":"ref38","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1038\/ncb1001-939","article-title":"Proteins containing the UBA domain are able to bind to multi-ubiquitin chains","volume":"3","author":"CR Wilkinson","year":"2001","journal-title":"Nat Cell Biol"},{"issue":"18","key":"ref39","doi-asserted-by":"crossref","first-page":"8055","DOI":"10.1128\/MCB.24.18.8055-8068.2004","article-title":"Sequestosome 1\/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation","volume":"24","author":"ML Seibenhener","year":"2004","journal-title":"Mol Cell Biol"},{"issue":"52","key":"ref40","doi-asserted-by":"crossref","first-page":"20820","DOI":"10.1073\/pnas.0709101105","article-title":"Differential Apaf-1 levels allow cytochrome c to induce apoptosis in brain tumors but not in normal neural tissues","volume":"104","author":"CE Johnson","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"ref41","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1093\/hmg\/ddi032","article-title":"Inactivation of Drosophila Apaf-1 related killer suppresses formation of polyglutamine aggregates and blocks polyglutamine pathogenesis","volume":"14","author":"TK Sang","year":"2005","journal-title":"Hum Mol Genet"},{"issue":"7154","key":"ref42","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1038\/nature06022","article-title":"Global changes to the ubiquitin system in Huntington's disease","volume":"448","author":"EJ Bennett","year":"2007","journal-title":"Nature"},{"issue":"2","key":"ref43","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.molcel.2011.08.025","article-title":"Systematic and quantitative assessment of the ubiquitin-modified proteome","volume":"44","author":"W Kim","year":"2011","journal-title":"Mol Cell"},{"issue":"7185","key":"ref44","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1038\/nature06780","article-title":"SCFbeta-TRCP controls oncogenic transformation and neural differentiation through REST degradation","volume":"452","author":"TF Westbrook","year":"2008","journal-title":"Nature"},{"issue":"3","key":"ref45","first-page":"62079","article-title":"Signaling, Polyubiquitination, Trafficking, and Inclusions: Sequestosome 1\/p62's Role in Neurodegenerative Disease","volume":"2006","author":"MW Wooten","year":"2006","journal-title":"J Biomed Biotechnol"},{"issue":"6","key":"ref46","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/j.cell.2007.10.035","article-title":"Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice","volume":"131","author":"M Komatsu","year":"2007","journal-title":"Cell"},{"issue":"8","key":"ref47","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/ncb2082","article-title":"Autophagy negatively regulates Wnt signalling by promoting Dishevelled degradation","volume":"12","author":"C Gao","year":"2010","journal-title":"Nat Cell Biol"},{"issue":"7","key":"ref48","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1038\/s41418-017-0025-z","article-title":"New insights into apoptosome structure and function","volume":"25","author":"L Dorstyn","year":"2018","journal-title":"Cell Death Differ"},{"issue":"2","key":"ref49","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.cell.2016.02.026","article-title":"BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation","volume":"165","author":"F Llambi","year":"2016","journal-title":"Cell"},{"issue":"4","key":"ref50","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1359\/JBMR.041205","article-title":"Loss of ubiquitin-binding associated with Paget's disease of bone p62 (SQSTM1) mutations","volume":"20","author":"JR Cavey","year":"2005","journal-title":"J Bone Miner Res"},{"issue":"3","key":"ref51","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.molcel.2011.05.033","article-title":"X-linked mental retardation gene CUL4B targets ubiquitylation of H3K4 methyltransferase component WDR5 and regulates neuronal gene expression","volume":"43","author":"T Nakagawa","year":"2011","journal-title":"Mol Cell"},{"issue":"11","key":"ref52","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.tibs.2009.07.002","article-title":"CRL4s: the CUL4-RING E3 ubiquitin ligases","volume":"34","author":"S Jackson","year":"2009","journal-title":"Trends Biochem Sci"},{"issue":"5","key":"ref53","doi-asserted-by":"crossref","first-page":"e37070","DOI":"10.1371\/journal.pone.0037070","article-title":"Lack of cul4b, an e3 ubiquitin ligase component, leads to embryonic lethality and abnormal placental development","volume":"7","author":"B Jiang","year":"2012","journal-title":"PLoS ONE"},{"issue":"8","key":"ref54","doi-asserted-by":"crossref","first-page":"1258","DOI":"10.1038\/cr.2012.48","article-title":"Essential role of the CUL4B ubiquitin ligase in extra-embryonic tissue development during mouse embryogenesis","volume":"22","author":"L Liu","year":"2012","journal-title":"Cell Res"},{"issue":"2","key":"ref55","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1086\/511134","article-title":"Mutations in CUL4B, which encodes a ubiquitin E3 ligase subunit, cause an X-linked mental retardation syndrome associated with aggressive outbursts, seizures, relative macrocephaly, central obesity, hypogonadism, pes cavus, and tremor","volume":"80","author":"PS Tarpey","year":"2007","journal-title":"Am J Hum Genet"},{"issue":"2","key":"ref56","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S0092-8674(00)80092-6","article-title":"An alternatively spliced C. elegans ced-4 RNA encodes a novel cell death inhibitor","volume":"86","author":"S Shaham","year":"1996","journal-title":"Cell"},{"issue":"5","key":"ref57","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.3892\/or.2014.3465","article-title":"CUL4B promotes proliferation and inhibits apoptosis of human osteosarcoma cells","volume":"32","author":"Z Chen","year":"2014","journal-title":"Oncol Rep"},{"issue":"8","key":"ref58","doi-asserted-by":"crossref","first-page":"3850","DOI":"10.1073\/pnas.070047997","article-title":"Bax degradation by the ubiquitin\/proteasome-dependent pathway: involvement in tumor survival and progression","volume":"97","author":"B Li","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"22","key":"ref59","doi-asserted-by":"crossref","first-page":"2889","DOI":"10.1038\/sj.onc.1202221","article-title":"Prostate carcinoma cell death resulting from inhibition of proteasome activity is independent of functional Bcl-2 and p53","volume":"17","author":"JL Herrmann","year":"1998","journal-title":"Oncogene"},{"issue":"9","key":"ref60","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1038\/sj.cdd.4401729","article-title":"Caspase activation and apoptosis in response to proteasome inhibitors","volume":"12","author":"CJ Henderson","year":"2005","journal-title":"Cell Death Differ"},{"issue":"12","key":"ref61","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1038\/sj.cdd.4400436","article-title":"Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts","volume":"5","author":"B An","year":"1998","journal-title":"Cell Death Differ"},{"issue":"2","key":"ref62","doi-asserted-by":"crossref","first-page":"845","DOI":"10.3892\/or.2016.4839","article-title":"Proteasome inhibitor MG132 potentiates TRAIL-induced apoptosis in gallbladder carcinoma GBC-SD cells via DR5-dependent pathway","volume":"36","author":"W Zhu","year":"2016","journal-title":"Oncol Rep"},{"issue":"49","key":"ref63","doi-asserted-by":"crossref","first-page":"32608","DOI":"10.1074\/jbc.273.49.32608","article-title":"Inhibition of human caspases by peptide-based and macromolecular inhibitors","volume":"273","author":"M Garcia-Calvo","year":"1998","journal-title":"J Biol Chem"},{"issue":"9","key":"ref64","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1038\/sj.leu.2402201","article-title":"Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an approximately 700 kDa Apaf-1 containing apoptosome complex","volume":"15","author":"JB Almond","year":"2001","journal-title":"Leukemia"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0219782","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,9,24]],"date-time":"2022-09-24T10:29:16Z","timestamp":1664015356000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0219782"}},"subtitle":[],"editor":[{"given":"Yi-Hsien","family":"Hsieh","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2019,7,22]]},"references-count":64,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2019,7,22]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0219782","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,7,22]]}}}