{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T15:53:13Z","timestamp":1787068393190,"version":"build-2736575974"},"reference-count":157,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2018,10,31]],"date-time":"2018-10-31T00:00:00Z","timestamp":1540944000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>A pivotal hallmark of some cancer cells is the evasion of apoptotic cell death. Importantly, the initiation of apoptosis often results in the activation of caspases, which, in turn, culminates in the generation of proteolytically-activated protein fragments with potentially new or altered roles. Recent investigations have revealed that the activity of a significant number of the protease-generated, activated, pro-apoptotic protein fragments can be curbed via their selective degradation by the N-end rule degradation pathways. Of note, previous work revealed that several proteolytically-generated, pro-apoptotic fragments are unstable in cells, as their destabilizing N-termini target them for proteasomal degradation via the N-end rule degradation pathways. Remarkably, previous studies also showed that the proteolytically-generated anti-apoptotic Lyn kinase protein fragment is targeted for degradation by the UBR1\/UBR2 E3 ubiquitin ligases of the N-end rule pathway in chronic myeloid leukemia cells. Crucially, the degradation of cleaved fragment of Lyn by the N-end rule counters imatinib resistance in these cells, implicating a possible linkage between the N-end rule degradation pathway and imatinib resistance. Herein, we highlight recent studies on the role of the N-end rule proteolytic pathways in regulating apoptosis in mammalian cells, and also discuss some possible future directions with respect to apoptotic proteolysis signaling.<\/jats:p>","DOI":"10.3390\/ijms19113414","type":"journal-article","created":{"date-parts":[[2018,10,31]],"date-time":"2018-10-31T11:55:41Z","timestamp":1540986941000},"page":"3414","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":37,"title":["Regulating Apoptosis by Degradation: The N-End Rule-Mediated Regulation of Apoptotic Proteolytic Fragments in Mammalian Cells"],"prefix":"10.3390","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9671-9340","authenticated-orcid":false,"given":"Mohamed A.","family":"Eldeeb","sequence":"first","affiliation":[{"name":"Department of Chemistry (Biochemistry Division), Faculty of Science, Cairo University, Giza 12613, Egypt"},{"name":"Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC H3A 2B4, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard P.","family":"Fahlman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada"},{"name":"Department of Oncology, University of Alberta, Edmonton, AB T6G 2H7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mansoore","family":"Esmaili","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed A.","family":"Ragheb","sequence":"additional","affiliation":[{"name":"Department of Chemistry (Biochemistry Division), Faculty of Science, Cairo University, Giza 12613, Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,10,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1126\/science.7878464","article-title":"Apoptosis in the pathogenesis and treatment of disease","volume":"267","author":"Thompson","year":"1995","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1146\/annurev.biochem.73.011303.073706","article-title":"Cytochrome c-mediated apoptosis","volume":"73","author":"Jiang","year":"2004","journal-title":"Annu. Rev. Biochem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/nrc776","article-title":"Death and anti-death: Tumour resistance to apoptosis","volume":"2","author":"Igney","year":"2002","journal-title":"Nat. Rev. Cancer"},{"key":"ref_4","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 Boil."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1146\/annurev.neuro.23.1.73","article-title":"Apoptosis in neural development and disease","volume":"23","author":"Nijhawan","year":"2000","journal-title":"Annu. Rev. Neurosci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1038\/sj.cdd.4400696","article-title":"Life and death decisions: Regulation of apoptosis by proteolysis of signaling molecules","volume":"7","author":"Utz","year":"2000","journal-title":"Cell Death Differ."},{"key":"ref_7","first-page":"a008672","article-title":"Cellular mechanisms controlling caspase activation and function","volume":"5","author":"Parrish","year":"2013","journal-title":"Cold Spring Harb. Perspect. Boil."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"12432","DOI":"10.1073\/pnas.1208616109","article-title":"Quantitative profiling of caspase-cleaved substrates reveals different drug-induced and cell-type patterns in apoptosis","volume":"109","author":"Shimbo","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1074\/mcp.O112.024372","article-title":"The degrabase: A database of proteolysis in healthy and apoptotic human cells","volume":"12","author":"Crawford","year":"2013","journal-title":"Mol. Cell. Proteom."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"E1839","DOI":"10.1073\/pnas.1207786109","article-title":"The n-end rule pathway counteracts cell death by destroying proapoptotic protein fragments","volume":"109","author":"Piatkov","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1007\/s10495-007-0167-4","article-title":"Caspase-dependent brca1 cleavage facilitates chemotherapy-induced apoptosis","volume":"13","author":"Dizin","year":"2008","journal-title":"Apoptosis"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1073\/pnas.0308050100","article-title":"Caspase cleavage of bimel triggers a positive feedback amplification of apoptotic signaling","volume":"101","author":"Chen","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/S0092-8674(00)81590-1","article-title":"Cleavage of bid by caspase 8 mediates the mitochondrial damage in the fas pathway of apoptosis","volume":"94","author":"Li","year":"1998","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2605","DOI":"10.1182\/blood-2003-01-0211","article-title":"Cleavage of bax to p18 bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 bax","volume":"102","author":"Cao","year":"2003","journal-title":"Blood"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1500","DOI":"10.1038\/leu.2009.60","article-title":"Inhibition of imatinib-mediated apoptosis by the caspase-cleaved form of the tyrosine kinase lyn in chronic myelogenous leukemia cells","volume":"23","author":"Gamas","year":"2009","journal-title":"Leukemia"},{"key":"ref_16","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. Boil. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"4839","DOI":"10.1038\/sj.onc.1202860","article-title":"Caspase-induced proteolysis of the cyclin-dependent kinase inhibitor p27kip1 mediates its anti-apoptotic activity","volume":"18","author":"Eymin","year":"1999","journal-title":"Oncogene"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"10425","DOI":"10.1128\/MCB.24.23.10425-10436.2004","article-title":"Partial cleavage of rasgap by caspases is required for cell survival in mild stress conditions","volume":"24","author":"Yang","year":"2004","journal-title":"Mol. Cell. Boil."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1038\/nrg2808","article-title":"Mutational effects and the evolution of new protein functions","volume":"11","author":"Soskine","year":"2010","journal-title":"Nat. Rev. Genet."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1002\/pro.666","article-title":"The n-end rule pathway and regulation by proteolysis","volume":"20","author":"Varshavsky","year":"2011","journal-title":"Protein Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1126\/science.3018930","article-title":"In vivo half-life of a protein is a function of its amino-terminal residue","volume":"234","author":"Bachmair","year":"1986","journal-title":"Science"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"a006080","DOI":"10.1101\/cshperspect.a006080","article-title":"Cell death signaling","volume":"7","author":"Green","year":"2015","journal-title":"Cold Spring Harb. Perspect. Boil."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1038\/sj.cdd.4402148","article-title":"Cell death modalities: Classification and pathophysiological implications","volume":"14","author":"Galluzzi","year":"2007","journal-title":"Cell Death Differ."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Fulda, S., Gorman, A.M., Hori, O., and Samali, A. (2010). Cellular stress responses: Cell survival and cell death. Int. J. Cell Biol., 214074.","DOI":"10.1155\/2010\/214074"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1570","DOI":"10.1056\/NEJMra0901217","article-title":"Cell death","volume":"361","author":"Hotchkiss","year":"2009","journal-title":"N. Engl. J. Med."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/bjc.1972.33","article-title":"Apoptosis: A basic biological phenomenon with wideranging implications in tissue kinetics","volume":"26","author":"Kerr","year":"1972","journal-title":"Br. J. Cancer"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1080\/01926230701320337","article-title":"Apoptosis: A review of programmed cell death","volume":"35","author":"Elmore","year":"2007","journal-title":"Toxicol. Pathol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1159\/000129697","article-title":"Senescence, apoptosis or autophagy?","volume":"54","author":"Vicencio","year":"2008","journal-title":"Gerontology"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1096\/fj.08-111005","article-title":"Life and death by death receptors","volume":"23","author":"Guicciardi","year":"2009","journal-title":"Faseb J."},{"key":"ref_30","first-page":"a008656","article-title":"Caspase functions in cell death and disease","volume":"5","author":"McIlwain","year":"2013","journal-title":"Cold Spring Harb. Perspect. Boil."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4197","DOI":"10.1073\/pnas.072544399","article-title":"Oligomerization and activation of caspase-9, induced by apaf-1 card","volume":"99","author":"Shiozaki","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/S1097-2765(02)00442-2","article-title":"Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation","volume":"9","author":"Acehan","year":"2002","journal-title":"Mol. Cell"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S0300-9084(02)01376-7","article-title":"The apaf-1 apoptosome: A large caspase-activating complex","volume":"84","author":"Cain","year":"2002","journal-title":"Biochimie"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/S1074-7613(00)80214-9","article-title":"Requirement for casper (c-flip) in regulation of death receptor\u2013induced apoptosis and embryonic development","volume":"12","author":"Yeh","year":"2000","journal-title":"Immunity"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.cell.2005.03.016","article-title":"Specific ablation of the apoptotic functions of cytochrome c reveals a differential requirement for cytochrome c and apaf-1 in apoptosis","volume":"121","author":"Hao","year":"2005","journal-title":"Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/0092-8674(95)90422-0","article-title":"Protease activation during apoptosis: Death by a thousand cuts?","volume":"82","author":"Martin","year":"1995","journal-title":"Cell"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/S1074-7613(03)00032-3","article-title":"Granzyme b-induced apoptosis requires both direct caspase activation and relief of caspase inhibition","volume":"18","author":"Goping","year":"2003","journal-title":"Immunity"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1016\/j.molmed.2012.09.009","article-title":"Granzyme b in injury, inflammation, and repair","volume":"18","author":"Hiebert","year":"2012","journal-title":"Trends Mol. Med."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"23549","DOI":"10.1074\/jbc.M412001200","article-title":"Extracellular matrix remodeling by human granzyme b via cleavage of vitronectin, fibronectin and laminin","volume":"280","author":"Buzza","year":"2005","journal-title":"J. Boil. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1038\/nature01991","article-title":"Molecular identification of a danger signal that alerts the immune system to dying cells","volume":"425","author":"Shi","year":"2003","journal-title":"Nature"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1038\/15200","article-title":"Natural adjuvants: Endogenous activators of dendritic cells","volume":"5","author":"Gallucci","year":"1999","journal-title":"Nat. Med."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1038\/nm1603","article-title":"Identification of a key pathway required for the sterile inflammatory response triggered by dying cells","volume":"13","author":"Chen","year":"2007","journal-title":"Nat. Med."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/nri2038","article-title":"Cooperation of toll-like receptor signals in innate immune defence","volume":"7","author":"Trinchieri","year":"2007","journal-title":"Nat. Rev. Immunol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1126\/science.1071059","article-title":"The danger model: A renewed sense of self","volume":"296","author":"Matzinger","year":"2002","journal-title":"Science"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/35037722","article-title":"Corpse clearance defines the meaning of cell death","volume":"407","author":"Savill","year":"2000","journal-title":"Nature"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1038\/nature00858","article-title":"Release of chromatin protein hmgb1 by necrotic cells triggers inflammation","volume":"418","author":"Scaffidi","year":"2002","journal-title":"Nature"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/0092-8674(93)90485-9","article-title":"The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1\u03b2-converting enzyme","volume":"75","author":"Yuan","year":"1993","journal-title":"Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/0092-8674(93)90486-A","article-title":"Induction of apoptosis in fibroblasts by il-1\u03b2-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3","volume":"75","author":"Miura","year":"1993","journal-title":"Cell"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1084\/jem.178.5.1693","article-title":"Protease inhibitors selectively block t cell receptor-triggered programmed cell death in a murine t cell hybridoma and activated peripheral t cells","volume":"178","author":"Sarin","year":"1993","journal-title":"J. Exp. Med."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/S0092-8674(94)90422-7","article-title":"Ich-1, an ice\/ced-3-related gene, encodes both positive and negative regulators of programmed cell death","volume":"78","author":"Wang","year":"1994","journal-title":"Cell"},{"key":"ref_51","first-page":"3976","article-title":"Specific proteolytic cleavage of poly (adp-ribose) polymerase: An early marker of chemotherapy-induced apoptosis","volume":"53","author":"Kaufmann","year":"1993","journal-title":"Cancer Res."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"3788","DOI":"10.4049\/jimmunol.154.8.3788","article-title":"Degradation of lamin b1 precedes oligonucleosomal DNA fragmentation in apoptotic thymocytes and isolated thymocyte nuclei","volume":"154","author":"Neamati","year":"1995","journal-title":"J. Immunol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.4049\/jimmunol.154.4.1707","article-title":"Activation of intracellular proteases is an early event in tnf-induced apoptosis","volume":"154","author":"Entingh","year":"1995","journal-title":"J. Immunol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"21777","DOI":"10.1074\/jbc.R800084200","article-title":"Human caspases: Activation, specificity, and regulation","volume":"284","author":"Pop","year":"2009","journal-title":"J. Boil. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1038\/sj.leu.2401879","article-title":"Noncaspase proteases in apoptosis","volume":"14","author":"Johnson","year":"2000","journal-title":"Leukemia"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0092-8674(00)81334-3","article-title":"Human ice\/ced-3 protease nomenclature","volume":"87","author":"Alnemri","year":"1996","journal-title":"Cell"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1038\/sj.cdd.4402034","article-title":"Caspase inhibitors: Viral, cellular and chemical","volume":"14","author":"Callus","year":"2007","journal-title":"Cell Death Differ."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/S1074-7613(00)80609-3","article-title":"Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the tnf receptors, fas\/apo1, and dr3 and is lethal prenatally","volume":"9","author":"Varfolomeev","year":"1998","journal-title":"Immunity"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1042\/BJ20041142","article-title":"The protein structures that shape caspase activity, specificity, activation and inhibition","volume":"384","author":"Salvesen","year":"2004","journal-title":"Biochem. J."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/nrm2153","article-title":"The apoptosome: Signalling platform of cell death","volume":"8","author":"Riedl","year":"2007","journal-title":"Nat. Rev. Mol. Cell Boil."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/S0092-8674(01)00544-X","article-title":"Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding","volume":"107","author":"Chai","year":"2001","journal-title":"Cell"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"14790","DOI":"10.1073\/pnas.221580098","article-title":"Structural basis for the activation of human procaspase-7","volume":"98","author":"Riedl","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"4398","DOI":"10.1021\/bi602623b","article-title":"Role of proteolysis in caspase-8 activation and stabilization","volume":"46","author":"Pop","year":"2007","journal-title":"Biochemistry"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2522","DOI":"10.4049\/jimmunol.181.4.2522","article-title":"Mutation of a self-processing site in caspase-8 compromises its apoptotic but not its nonapoptotic functions in bacterial artificial chromosome-transgenic mice","volume":"181","author":"Kang","year":"2008","journal-title":"J. Immunol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"17907","DOI":"10.1074\/jbc.272.29.17907","article-title":"A combinatorial approach defines specificities of members of the caspase family and granzyme b functional relationships established for key mediators of apoptosis","volume":"272","author":"Thornberry","year":"1997","journal-title":"J. Boil. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1038\/sj.cdd.4402059","article-title":"Caspase substrates","volume":"14","author":"Timmer","year":"2007","journal-title":"Cell Death Differ."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1042\/bj3500563","article-title":"Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8","volume":"350","author":"Stennicke","year":"2000","journal-title":"Biochem. J."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/S0968-0004(01)02045-X","article-title":"Reprieval from execution: The molecular basis of caspase inhibition","volume":"27","author":"Stennicke","year":"2002","journal-title":"Trends Biochem. Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1042\/BJ20081885","article-title":"Ubiquitin binding modulates iap antagonist-stimulated proteasomal degradation of c-iap1 and c-iap2","volume":"417","author":"Blankenship","year":"2009","journal-title":"Biochem. J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1038\/ncb1789","article-title":"Iaps contain an evolutionarily conserved ubiquitin-binding domain that regulates nf-\u03bab as well as cell survival and oncogenesis","volume":"10","author":"Darding","year":"2008","journal-title":"Nat. Cell Boil."},{"key":"ref_71","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":"ref_72","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1038\/sj.embor.7400795","article-title":"Human inhibitor of apoptosis proteins: Why xiap is the black sheep of the family","volume":"7","author":"Eckelman","year":"2006","journal-title":"Embo Rep."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/sj.cdd.4401360","article-title":"Catalytic activity of caspase-3 is required for its degradation: Stabilization of the active complex by synthetic inhibitors","volume":"11","author":"Tawa","year":"2004","journal-title":"Cell Death Differ."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0092-8674(00)80197-X","article-title":"Dff, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis","volume":"89","author":"Liu","year":"1997","journal-title":"Cell"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2240","DOI":"10.1091\/mbc.e11-11-0926","article-title":"Cell survival, DNA damage, and oncogenic transformation after a transient and reversible apoptotic response","volume":"23","author":"Tang","year":"2012","journal-title":"Mol. Boil. Cell"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/sj.bjc.6604802","article-title":"Reversibility of apoptosis in cancer cells","volume":"100","author":"Tang","year":"2009","journal-title":"Br. J. Cancer"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"9015","DOI":"10.1038\/srep09015","article-title":"In vivo caspasetracker biosensor system for detecting anastasis and non-apoptotic caspase activity","volume":"5","author":"Tang","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"13590","DOI":"10.1073\/pnas.0401372101","article-title":"Proapoptotic n-truncated bcl-xl protein activates endogenous mitochondrial channels in living synaptic terminals","volume":"101","author":"Jonas","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_79","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":"ref_80","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":"ref_81","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/nrc2889","article-title":"Iaps: From caspase inhibitors to modulators of nf-\u03bab, inflammation and cancer","volume":"10","author":"Meier","year":"2010","journal-title":"Nat. Rev. Cancer"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1111\/nph.14619","article-title":"Life and death of proteins after protease cleavage: protein degradation by the N-end rule pathway","volume":"218","author":"Dissmeyer","year":"2018","journal-title":"New Phytol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1093\/nar\/27.1.325","article-title":"Merops: The peptidase database","volume":"27","author":"Rawlings","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"16700","DOI":"10.1016\/S0021-9258(19)84762-2","article-title":"Universality and structure of the n-end rule","volume":"264","author":"Gonda","year":"1989","journal-title":"J. Boil. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1146\/annurev-biochem-051910-094049","article-title":"The ubiquitin system, an immense realm","volume":"81","author":"Varshavsky","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1097\/01.LAB.0000022226.23741.37","article-title":"Role and function of the 26s proteasome in proliferation and apoptosis","volume":"82","author":"Naujokat","year":"2002","journal-title":"Lab. Investig."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1126\/science.7624798","article-title":"Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27","volume":"269","author":"Pagano","year":"1995","journal-title":"Science"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.stem.2012.09.011","article-title":"Regulation of pluripotency and cellular reprogramming by the ubiquitin-proteasome system","volume":"11","author":"Buckley","year":"2012","journal-title":"Cell Stem Cell"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1038\/sj.cdd.4401692","article-title":"Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin\u2013proteasome system and onto human diseases and drug targeting","volume":"12","author":"Ciechanover","year":"2005","journal-title":"Cell Death Differ."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1126\/science.2876518","article-title":"Amino acid sequences common to rapidly degraded proteins: The pest hypothesis","volume":"234","author":"Rogers","year":"1986","journal-title":"Science"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/S0968-0004(96)10031-1","article-title":"Pest sequences and regulation by proteolysis","volume":"21","author":"Rechsteiner","year":"1996","journal-title":"Trends Biochem. Sci."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1073\/pnas.94.6.2221","article-title":"Regulation of e2f through ubiquitin\u2013proteasome-dependent degradation: Stabilization by the prb tumor suppressor protein","volume":"94","author":"Campanero","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1126\/science.8122109","article-title":"Heat-inducible degron: A method for constructing temperature-sensitive mutants","volume":"263","author":"Dohmen","year":"1994","journal-title":"Science"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1128\/MCB.15.2.731","article-title":"P34cdc28-mediated control of cln3 cyclin degradation","volume":"15","author":"Yaglom","year":"1995","journal-title":"Mol. Cell. Boil."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1093\/emboj\/18.6.1571","article-title":"The p21cip1 and p27kip1 cdk \u2018inhibitors\u2019 are essential activators of cyclin d-dependent kinases in murine fibroblasts","volume":"18","author":"Cheng","year":"1999","journal-title":"Embo J."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/18230","article-title":"Degradation of the cyclin-dependent-kinase inhibitor p27kip1 is instigated by jab1","volume":"398","author":"Tomoda","year":"1999","journal-title":"Nature"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"7288","DOI":"10.1128\/MCB.18.12.7288","article-title":"Nuclear export is required for degradation of endogenous p53 by mdm2 and human papillomavirus e6","volume":"18","author":"Freedman","year":"1998","journal-title":"Mol. Cell. Boil."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1126\/science.1962196","article-title":"The n-end rule in bacteria","volume":"254","author":"Tobias","year":"1991","journal-title":"Science"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/nature10534","article-title":"Homeostatic response to hypoxia is regulated by the n-end rule pathway in plants","volume":"479","author":"Gibbs","year":"2011","journal-title":"Nature"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.molcel.2013.03.018","article-title":"Control of protein quality and stoichiometries by n-terminal acetylation and the n-end rule pathway","volume":"50","author":"Shemorry","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1038\/35073627","article-title":"Degradation of a cohesin subunit by the n-end rule pathway is essential for chromosome stability","volume":"410","author":"Rao","year":"2001","journal-title":"Nature"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1016\/j.molcel.2012.10.012","article-title":"The auto-generated fragment of the usp1 deubiquitylase is a physiological substrate of the n-end rule pathway","volume":"48","author":"Piatkov","year":"2012","journal-title":"Mol. Cell"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/ncb984","article-title":"Degradation of diap1 by the n-end rule pathway is essential for regulating apoptosis","volume":"5","author":"Ditzel","year":"2003","journal-title":"Nat. Cell Boil."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1126\/science.1069531","article-title":"An essential role of n-terminal arginylation in cardiovascular development","volume":"297","author":"Kwon","year":"2002","journal-title":"Science"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/35014629","article-title":"Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway","volume":"405","author":"Turner","year":"2000","journal-title":"Nature"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"eaal3655","DOI":"10.1126\/science.aal3655","article-title":"An n-end rule pathway that recognizes proline and destroys gluconeogenic enzymes","volume":"355","author":"Chen","year":"2017","journal-title":"Science"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1126\/science.1183147","article-title":"N-terminal acetylation of cellular proteins creates specific degradation signals","volume":"327","author":"Hwang","year":"2010","journal-title":"Science"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"7120","DOI":"10.1128\/MCB.25.16.7120-7136.2005","article-title":"A family of mammalian e3 ubiquitin ligases that contain the ubr box motif and recognize n-degrons","volume":"25","author":"Tasaki","year":"2005","journal-title":"Mol. Cell. Boil."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"343","DOI":"10.2174\/0929866523666160108115809","article-title":"The-N-end rule: The beginning determines the end","volume":"23","author":"Eldeeb","year":"2016","journal-title":"Protein Pept. Lett."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1074\/jbc.M803641200","article-title":"The substrate recognition domains of the n-end rule pathway","volume":"284","author":"Tasaki","year":"2009","journal-title":"J. Boil. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"24011","DOI":"10.1074\/jbc.M802583200","article-title":"Substrate-sinding sites of ubr1, the ubiquitin ligase of the n-end rule pathway","volume":"283","author":"Xia","year":"2008","journal-title":"J. Boil. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1038\/nature04412","article-title":"Clps is an essential component of the n-end rule pathway in Escherichia coli","volume":"439","author":"Erbse","year":"2006","journal-title":"Nature"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1038\/embor.2009.62","article-title":"Structural basis of n-end rule substrate recognition in escherichia coli by the clpap adaptor protein clps","volume":"10","author":"Schuenemann","year":"2009","journal-title":"Embo Rep."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"8888","DOI":"10.1073\/pnas.0903614106","article-title":"Molecular basis of substrate selection by the n-end rule adaptor protein clps","volume":"106","author":"Grant","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1038\/nsmb.1907","article-title":"Structural basis for the recognition of n-end rule substrates by the ubr box of ubiquitin ligases","volume":"17","author":"Choi","year":"2010","journal-title":"Nat. Struct. Mol. Boil."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1182","DOI":"10.1038\/nsmb.1894","article-title":"Structural basis of substrate recognition and specificity in the n-end rule pathway","volume":"17","author":"Kozlov","year":"2010","journal-title":"Nat. Struct. Mol. Boil."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1038\/nsmb1010-1164","article-title":"The molecular principles of n-end rule recognition","volume":"17","author":"Sriram","year":"2010","journal-title":"Nat. Struct. Mol. Boil."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/0092-8674(89)90635-1","article-title":"The degradation signal in a short-lived protein","volume":"56","author":"Bachmair","year":"1989","journal-title":"Cell"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.cell.2013.11.031","article-title":"The N-terminal methionine of cellular proteins as a degradation signal","volume":"156","author":"Kim","year":"2014","journal-title":"Cell"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"22757","DOI":"10.1074\/jbc.M116.737387","article-title":"Phosphorylation impacts n-end rule degradation of the proteolytically activated form of bmx kinase","volume":"291","author":"Eldeeb","year":"2016","journal-title":"J. Boil. Chem."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"2714","DOI":"10.18632\/oncotarget.1931","article-title":"The anti-apoptotic form of tyrosine kinase lyn that is generated by proteolysis is degraded by the N-end rule pathway","volume":"5","author":"Eldeeb","year":"2014","journal-title":"Oncotarget"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"H2253","DOI":"10.1152\/ajpheart.00274.2009","article-title":"Caspase-mediated protein kinase c-\u03b4 cleavage is necessary for apoptosis of vascular smooth muscle cells","volume":"297","author":"Kato","year":"2009","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"2514","DOI":"10.1101\/gad.13.19.2514","article-title":"Cleavage of the death domain kinase rip by caspase-8 prompts tnf-induced apoptosis","volume":"13","author":"Lin","year":"1999","journal-title":"Genes Dev."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"20317","DOI":"10.1074\/jbc.272.33.20317","article-title":"Caspase-3-mediated cleavage of protein kinase c \u03b8 in induction of apoptosis","volume":"272","author":"Datta","year":"1997","journal-title":"J. Boil. Chem."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1111\/j.1462-5822.2008.01131.x","article-title":"Killing of macrophages by anthrax lethal toxin: Involvement of the n-end rule pathway","volume":"10","author":"Wickliffe","year":"2008","journal-title":"Cell. Microbiol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"e2378","DOI":"10.1038\/cddis.2016.284","article-title":"Posttranslational arginylation enzyme ate1 affects DNA mutagenesis by regulating stress response","volume":"7","author":"Kumar","year":"2016","journal-title":"Cell Death Dis."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"690","DOI":"10.4161\/cbt.11.7.15060","article-title":"Tyrosine kinase etk\/bmx protects nasopharyngeal carcinoma cells from apoptosis induced by radiation","volume":"11","author":"Zhang","year":"2011","journal-title":"Cancer Boil. Ther."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"17672","DOI":"10.1074\/jbc.M010964200","article-title":"Proteolytic activation of etk\/bmx tyrosine kinase by caspases","volume":"276","author":"Wu","year":"2001","journal-title":"J. Boil. Chem."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"6061","DOI":"10.1093\/emboj\/cdf626","article-title":"Dissection of c-mos degron","volume":"21","author":"Sheng","year":"2002","journal-title":"Embo J."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"7495","DOI":"10.1074\/jbc.M111.301002","article-title":"The c-terminal proteolytic fragment of the breast cancer susceptibility type 1 protein (brca1) is degraded by the n-end rule pathway","volume":"287","author":"Xu","year":"2012","journal-title":"J. Boil. Chem."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1172\/JCI26321","article-title":"Pharmacological manipulation of cell death: Clinical applications in sight?","volume":"115","author":"Green","year":"2005","journal-title":"J. Clin. Investig."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1016\/S0006-2952(03)00497-0","article-title":"Non-apoptotic functions of caspases in cellular proliferation and differentiation","volume":"66","author":"Schwerk","year":"2003","journal-title":"Biochem. Pharmacol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1002\/ijc.31374","article-title":"Caspase-3 regulates the migration, invasion and metastasis of colon cancer cells","volume":"143","author":"Zhou","year":"2018","journal-title":"Int. J. Cancer"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.tcb.2007.01.001","article-title":"Nonapoptotic functions of caspases: Caspases as regulatory molecules for immunity and cell-fate determination","volume":"17","author":"Kuranaga","year":"2007","journal-title":"Trends Cell Boil."},{"key":"ref_135","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":"ref_136","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1159\/000055530","article-title":"Lens fibre cell differentiation\u2014A link with apoptosis?","volume":"31","author":"Dahm","year":"1999","journal-title":"Ophthalmic Res."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.stem.2010.09.003","article-title":"Apoptotic caspases regulate induction of ipscs from human fibroblasts","volume":"7","author":"Li","year":"2010","journal-title":"Cell Stem Cell"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"4446","DOI":"10.1182\/blood-2002-06-1778","article-title":"Specific involvement of caspases in the differentiation of monocytes into macrophages","volume":"100","author":"Sordet","year":"2002","journal-title":"Blood"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1038\/nn1774","article-title":"Local caspase activity directs engulfment of dendrites during pruning","volume":"9","author":"Williams","year":"2006","journal-title":"Nat. Neurosci."},{"key":"ref_140","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":"ref_141","doi-asserted-by":"crossref","first-page":"4273","DOI":"10.1158\/0008-5472.CAN-05-4183","article-title":"Caspase-8 promotes cell motility and calpain activity under nonapoptotic conditions","volume":"66","author":"Helfer","year":"2006","journal-title":"Cancer Res."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1016\/j.cub.2006.06.032","article-title":"Ikk\u03b5 regulates f actin assembly and interacts with drosophila iap1 in cellular morphogenesis","volume":"16","author":"Oshima","year":"2006","journal-title":"Curr. Boil."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s10555-018-9736-y","article-title":"Novel roles of apoptotic caspases in tumor repopulation, epigenetic reprogramming, carcinogenesis, and beyond","volume":"37","author":"Zhao","year":"2018","journal-title":"Cancer Metastasis Rev."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"3355","DOI":"10.1083\/jcb.201706134","article-title":"A molecular signature for anastasis, recovery from the brink of apoptotic cell death","volume":"216","author":"Sun","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.neo.2018.01.005","article-title":"Apoptosis Reversal Promotes Cancer Stem Cell-Like Cell Formation","volume":"20","author":"Xu","year":"2018","journal-title":"Neoplasia"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"4058","DOI":"10.1038\/onc.2015.473","article-title":"Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers","volume":"35","author":"Rai","year":"2016","journal-title":"Oncogene"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.1038\/cdd.2017.44","article-title":"Caspases and their substrates","volume":"24","author":"Julien","year":"2017","journal-title":"Cell Death Differ."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1038\/sj.emboj.7600544","article-title":"Xiap inhibits caspase-3 and-7 using two binding sites: Evolutionarily conserved mechanism of iaps","volume":"24","author":"Scott","year":"2005","journal-title":"Embo J."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.cell.2010.07.014","article-title":"Activation of specific apoptotic caspases with an engineered small-molecule-activated protease","volume":"142","author":"Gray","year":"2010","journal-title":"Cell"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S1097-2765(04)00156-X","article-title":"Caspase activation inhibits proteasome function during apoptosis","volume":"14","author":"Sun","year":"2004","journal-title":"Mol. Cell"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/j.devcel.2017.05.013","article-title":"Coupled Caspase and N-End Rule Ligase Activities Allow Recognition and Degradation of Pluripotency Factor LIN-28 during Non-Apoptotic Development","volume":"41","author":"Weaver","year":"2017","journal-title":"Dev. Cell"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1038\/cdd.2017.36","article-title":"Caspase-dependent non-apoptotic processes in development","volume":"24","author":"Nakajima","year":"2017","journal-title":"Cell Death Differ."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1139\/bcb-2017-0274","article-title":"Emerging branches of the n-end rule pathways are revealing the sequence complexities of n-termini dependent protein degradation","volume":"96","author":"Eldeeb","year":"2017","journal-title":"Biochem. Cell Boil."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.2174\/1389203719666180809113122","article-title":"Post-translational N-terminal arginylation of protein fragments: A pivotal portal to proteolysis","volume":"19","author":"Eldeeb","year":"2018","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1038\/sj.cdd.4401235","article-title":"The regulatory domain of protein kinase c\u03b8 localises to the golgi complex and induces apoptosis in neuroblastoma and jurkat cells","volume":"10","author":"Schultz","year":"2003","journal-title":"Cell Death Differ."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Sun, H., and Wang, X. (2017). Beyond deubiquitylation: Usp30-mediated regulation of mitochondrial homeostasis. Mitochondrial DNA and Diseases, Springer.","DOI":"10.1007\/978-981-10-6674-0"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"e30590","DOI":"10.7554\/eLife.30590","article-title":"A picorna-like virus suppresses the N-end rule pathway to inhibit apoptosis","volume":"6","author":"Wang","year":"2017","journal-title":"eLife"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/19\/11\/3414\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T15:27:08Z","timestamp":1760196428000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/19\/11\/3414"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,10,31]]},"references-count":157,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2018,11]]}},"alternative-id":["ijms19113414"],"URL":"https:\/\/doi.org\/10.3390\/ijms19113414","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,10,31]]}}}