{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T16:18:44Z","timestamp":1785860324873,"version":"3.56.0"},"reference-count":89,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,9,1]],"date-time":"2019-09-01T00:00:00Z","timestamp":1567296000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,9,1]],"date-time":"2019-09-01T00:00:00Z","timestamp":1567296000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","jmmc-online.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular and Cellular Cardiology"],"published-print":{"date-parts":[[2019,9]]},"DOI":"10.1016\/j.yjmcc.2019.07.009","type":"journal-article","created":{"date-parts":[[2019,7,22]],"date-time":"2019-07-22T11:05:54Z","timestamp":1563793554000},"page":"154-164","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":40,"special_numbering":"C","title":["Roles and mechanisms of SUMOylation on key proteins in myocardial ischemia\/reperfusion injury"],"prefix":"10.1016","volume":"134","author":[{"given":"Jingwen","family":"Chen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuanyuan","family":"Luo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuai","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4875-0209","authenticated-orcid":false,"given":"Dongye","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.yjmcc.2019.07.009_bb0005","first-page":"2","article-title":"Heart disease and stroke statistics-2012 update: a report from the American heart association","volume":"125","author":"Roger","year":"2012","journal-title":"Circulation"},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0010","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1056\/NEJM198010163031601","article-title":"Prevalence of total coronary occlusion during the early hours of transmural myocardial infarction","volume":"303","author":"De Wood","year":"2010","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0015","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/S0008-6363(96)88531-2","article-title":"Ischaemia in intact rat heart: role of intracellular calcium","volume":"29","author":"Brooks","year":"1995","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0020","doi-asserted-by":"crossref","first-page":"4277","DOI":"10.4049\/jimmunol.157.10.4277","article-title":"Protection against Fas\/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin","volume":"157","author":"Okura","year":"1996","journal-title":"J. Immunol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0025","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcel.2005.03.012","article-title":"SUMO\u202f: a history of modification review","volume":"18","author":"Hay","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0030","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1038\/nrm2293","article-title":"Concepts in sumoylation: a decade on","volume":"8","author":"Geiss-friedlander","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0035","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1038\/ng1391","article-title":"A functional variant of SUMO4, a new I\u03baB\u03b1 modifier, is associated with type diabetes","volume":"36","author":"Guo","year":"2004","journal-title":"Nat. Genet."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0040","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1016\/j.bbadis.2017.01.018","article-title":"Sub-cellular localization specific SUMOylation in the heart","volume":"1863","author":"Le","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. basis Dis."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0045","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1016\/j.cell.2010.11.016","article-title":"Will the ubiquitin system furnish as many drug targets as protein kinases?","volume":"143","author":"Cohen","year":"2010","journal-title":"Cell."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0050","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1089\/ars.2008.2182","article-title":"SUMO proteases: redox regulation and biological consequences","volume":"11","author":"Xu","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0055","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1016\/j.tcb.2007.08.002","article-title":"SUMO-specific proteases: a twist in the tail","volume":"17","author":"Hay","year":"2007","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0060","doi-asserted-by":"crossref","first-page":"3355","DOI":"10.1074\/jbc.275.5.3355","article-title":"Differential regulation of sentrinized proteins by a novel sentrin-specific protease","volume":"275","author":"Gong","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0065","doi-asserted-by":"crossref","first-page":"15869","DOI":"10.1074\/jbc.M511658200","article-title":"Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3","volume":"281","author":"Gong","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0070","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1016\/j.ymthe.2016.12.021","article-title":"Manipulating PML SUMOylation via silencing UBC9 and RNF4 regulates cardiac fibrosis","volume":"25","author":"Liu","year":"2017","journal-title":"Mol. Ther."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0075","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.taap.2018.03.006","article-title":"Pharmacological inhibition of SUMO-1 with ginkgolic acid alleviates cardiac fibrosis induced by myocardial infarction in mice","volume":"345","author":"Qiu","year":"2018","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0080","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-018-05812-2","article-title":"SUMOylation of VEGFR2 regulates its intracellular trafficking and pathological angiogenesis","volume":"9","author":"Zhou","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0085","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1172\/jci.insight.125570","article-title":"MAGI1 as a link between endothelial activation and ER stress drives atherosclerosis","volume":"4","author":"Abe","year":"2019","journal-title":"JCI Insight."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0090","doi-asserted-by":"crossref","first-page":"H1660","DOI":"10.1152\/ajpheart.00677.2010","article-title":"cGMP-dependent protein kinase and the regulation of vascular smooth muscle cell gene expression: possible involvement of Elk-1 sumoylation","volume":"299","author":"Choi","year":"2010","journal-title":"Am. J. Physiol. Circ. Physiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0095","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.yjmcc.2013.10.008","article-title":"Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond","volume":"71","author":"Cui","year":"2014","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0100","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.biocel.2016.09.015","article-title":"Proteostasis and SUMO in the heart","volume":"79","author":"Da Silva-Ferrada","year":"2016","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0105","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1038\/nature10407","article-title":"SUMO1-dependent modulation of SERCA2a in heart failure","volume":"477","author":"Kho","year":"2011","journal-title":"Nature."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0110","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1016\/j.jacc.2007.12.014","article-title":"Reversal of cardiac dysfunction after long-term expression of SERCA2a by gene transfer in a pre-clinical model of heart failure","volume":"51","author":"Kawase","year":"2008","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0115","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1159\/000487283","article-title":"Luteolin modulates SERCA2a leading to attenuation of myocardial ischemia\/reperfusion injury via sumoylation at Lysin 585 in mice","volume":"45","author":"Du","year":"2018","journal-title":"Cell. Physiol. Biochem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0120","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1073\/pnas.97.2.793","article-title":"Adenoviral gene transfer of SERCA2a improves left-ventricular function in aortic-banded rats in transition to heart failure","volume":"97","author":"Miyamoto","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0125","doi-asserted-by":"crossref","first-page":"2308","DOI":"10.1161\/01.CIR.100.23.2308","article-title":"Restoration of contractile function in isolated cardiomyocytes from failing human hearts by gene transfer of SERCA2a","volume":"100","author":"Monte","year":"1999","journal-title":"Circulation"},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0130","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1093\/eurjhf\/hfq234","article-title":"Augmentation of left ventricular mechanics by recirculation-mediated AAV2\/1-SERCA2a gene delivery in experimental heart failure","volume":"13","author":"Mariani","year":"2011","journal-title":"Eur. J. Heart Fail."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0135","doi-asserted-by":"crossref","first-page":"1986","DOI":"10.1089\/ars.2014.5983","article-title":"The role of SUMO-1 in cardiac oxidative stress and hypertrophy","volume":"21","author":"Lee","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0140","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1016\/j.yjmcc.2007.01.003","article-title":"Restoration of mechanical and energetic function in failing aortic-banded rat hearts by gene transfer of calcium cycling proteins","volume":"42","author":"Sakata","year":"2007","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0145","doi-asserted-by":"crossref","first-page":"5622","DOI":"10.1073\/pnas.0305778101","article-title":"Abrogation of ventricular arrhythmias in a model of ischemia and reperfusion by targeting myocardial calcium cycling","volume":"101","author":"del Monte","year":"2004","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0150","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/ncomms8229","article-title":"Small-molecule activation of SERCA2a SUMOylation for the treatment of heart failure","volume":"6","author":"Kho","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0155","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1139\/y82-043","article-title":"Effect of myocardial ischemia on uridine incorporation and histone acetylation","volume":"60","author":"Taylor","year":"1982","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0160","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.taap.2010.03.022","article-title":"Molecular targets of epigenetic regulation and effectors of environmental in fluences","volume":"245","author":"Choudhuri","year":"2010","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0165","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1183\/09031936.05.00117504","article-title":"Histone acetylation and deacetylation: importance in inflammatory lung diseases","volume":"25","author":"Barnes","year":"2005","journal-title":"Eur. Respir. J."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0170","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1016\/j.bbadis.2016.08.011","article-title":"Mechanisms of transcription factor acetylation and consequences in hearts","volume":"1862","author":"Thiagarajan","year":"2016","journal-title":"BBA-Mol. Basis Dis."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0175","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1002\/(SICI)1521-1878(199808)20:8<615::AID-BIES4>3.0.CO;2-H","article-title":"Roles of histone acetyltransferases and deacetylases in gene regulation","volume":"20","author":"Kuo","year":"1998","journal-title":"BioEssays."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0180","doi-asserted-by":"crossref","first-page":"7816","DOI":"10.1128\/MCB.19.11.7816","article-title":"HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor","volume":"19","author":"Wang","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0185","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.yjmcc.2017.12.004","article-title":"HDAC1 localizes to the mitochondria of cardiac myocytes and contributes to early cardiac reperfusion injury","volume":"114","author":"Herr","year":"2018","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0190","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1124\/jpet.111.189910","article-title":"Inhibition of histone deacetylases preserves myocardial performance and prevents cardiac remodeling through stimulation of endogenous angiomyogenesis","volume":"341","author":"Zhang","year":"2012","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0195","doi-asserted-by":"crossref","first-page":"3246","DOI":"10.1002\/jcb.23251","article-title":"HDAC inhibition promotes cardiogenesis and the survival of embryonic stem cells through proteasome-dependent pathway","volume":"112","author":"Chen","year":"2011","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0200","doi-asserted-by":"crossref","first-page":"C358","DOI":"10.1152\/ajpcell.00187.2013","article-title":"Specific inhibition of HDAC4 in cardiac progenitor cells enhances myocardial repairs","volume":"307","author":"Zhang","year":"2014","journal-title":"AJP Cell Physiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0205","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/j.cardiores.2007.08.010","article-title":"Inhibition of histone deacetylases triggers pharmacologic preconditioning effects against myocardial ischemic injury","volume":"76","author":"Zhao","year":"2007","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0210","doi-asserted-by":"crossref","first-page":"3549","DOI":"10.1096\/fj.08-108548","article-title":"Histone deacetylase inhibition reduces myocardial ischemia-reperfusion injury in mice","volume":"22","author":"Granger","year":"2008","journal-title":"FASEB J."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0215","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1002\/jcp.24871","article-title":"HDAC4 degradation mediates HDAC inhibition-induced protective effects against hypoxia\/reoxygenation injury","volume":"230","author":"Du","year":"2015","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0220","doi-asserted-by":"crossref","first-page":"35368","DOI":"10.1074\/jbc.M104214200","article-title":"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1\/SAE2 and Ubc9","volume":"276","author":"Tatham","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0225","first-page":"1","article-title":"Irisin ameliorates hypoxia\/reoxygenation-induced injury through modulation of histone deacetylase 4","author":"Zhao","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0230","doi-asserted-by":"crossref","first-page":"6823","DOI":"10.1074\/jbc.M609554200","article-title":"Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1","volume":"282","author":"Tanno","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0235","doi-asserted-by":"crossref","first-page":"2170","DOI":"10.1161\/CIRCULATIONAHA.110.958033","article-title":"Silent information regulator 1 protects the heart from ischemia\/reperfusion","volume":"122","author":"Hsu","year":"2010","journal-title":"Circulation."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0240","doi-asserted-by":"crossref","first-page":"4332","DOI":"10.1096\/fj.12-216473","article-title":"Impaired SIRT1 nucleocytoplasmic shuttling in the senescent heart during ischemic stress","volume":"27","author":"Tong","year":"2013","journal-title":"FASEB J."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0245","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1006\/jmbi.1998.1839","article-title":"Structure determination of the small ubiquitin-related modifier SUMO-1","volume":"280","author":"Bayer","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0250","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.mad.2008.04.007","article-title":"Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart","volume":"129","author":"Li","year":"2008","journal-title":"Mech. Ageing Dev."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0255","doi-asserted-by":"crossref","first-page":"1522","DOI":"10.1089\/ars.2012.4803","article-title":"Regulation of SIRT1 by oxidative stress-responsive miRNAs and a systematic approach to identify its role in the endothelium","volume":"19","author":"Chen","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0260","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1093\/cvr\/cvq287","article-title":"Lysine deacetylation in ischaemic preconditioning: the role of SIRT1","volume":"89","author":"Nadtochiy","year":"2011","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0265","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1111\/1440-1681.12496","article-title":"HDAC4 stabilizes SIRT1 via sumoylation SIRT1 to delay cellular senescence","volume":"43","author":"Han","year":"2016","journal-title":"Clin. Exp. Pharmacol. Physiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0270","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1152\/physrev.00024.2007","article-title":"Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury","volume":"88","author":"Murphy","year":"2008","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0275","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1126\/science.1219855","article-title":"REVIEW mitochondrial fission, fusion, and stress","volume":"337","author":"Youle","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0280","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/B978-0-12-394309-5.00006-7","article-title":"Cell biology of ischemia\/reperfusion injury","volume":"298","author":"Kalogeris","year":"2012","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0285","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1146\/annurev.biochem.76.071905.090048","article-title":"The machines that divide and fuse Mitochondria","volume":"76","author":"Hoppins","year":"2007","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0290","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/S1097-2765(00)80391-3","article-title":"C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane","volume":"4","author":"Labrousse","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0295","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1016\/j.cub.2005.02.064","article-title":"Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission","volume":"15","author":"De Vos","year":"2005","journal-title":"Curr. Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0300","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1016\/j.biocel.2009.05.001","article-title":"Mitochondrial outer-membrane permeabilization and remodelling in apoptosis","volume":"41","author":"Jourdain","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0305","doi-asserted-by":"crossref","first-page":"5969","DOI":"10.1073\/pnas.1213294110","article-title":"Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation","volume":"110","author":"Din","year":"2013","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0310","doi-asserted-by":"crossref","first-page":"2012","DOI":"10.1161\/CIRCULATIONAHA.109.906610","article-title":"Inhibiting mitochondrial fission protects the heart against ischemia\/reperfusion injury","volume":"121","author":"Ong","year":"2010","journal-title":"Circulation."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0315","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1038\/sj.embor.7401077","article-title":"The phosphorylation state of Drp1 determines cell fate","volume":"8","author":"Jahani-Asl","year":"2007","journal-title":"EMBO Rep."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0320","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1083\/jcb.200610042","article-title":"Bax\/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death","volume":"177","author":"Wasiak","year":"2007","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0325","doi-asserted-by":"crossref","first-page":"3917","DOI":"10.1096\/fj.09-136630","article-title":"SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle","volume":"23","author":"Figueroa-Romero","year":"2009","journal-title":"FASEB J."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0330","doi-asserted-by":"crossref","first-page":"1514","DOI":"10.1038\/emboj.2013.65","article-title":"SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia","volume":"32","author":"Guo","year":"2013","journal-title":"EMBO J."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0335","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.yjmcc.2016.04.008","article-title":"DJ-1 protects the heart against ischemia-reperfusion injury by regulating mitochondrial fission","volume":"97","author":"Shimizu","year":"2016","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0340","first-page":"154","article-title":"SENP5, a SUMO isopeptidase, induces apoptosis and cardiomyopathy","volume":"78","author":"Young","year":"2014","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0345","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.jgg.2017.12.002","article-title":"The desumoylating enzyme sentrin-specific protease 3 contributes to myocardial ischemia reperfusion injury","volume":"45","author":"Gao","year":"2018","journal-title":"J. Genet. Genomics."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0350","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1042\/BJ20100504","article-title":"Distribution and paralogue specificity of mammalian deSUMOylating enzymes","volume":"430","author":"Kolli","year":"2010","journal-title":"Biochem. J."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0355","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1006\/scdb.2001.0287","article-title":"Oxygen sensors and angiogenesis","volume":"13","author":"Maxwell","year":"2002","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0360","doi-asserted-by":"crossref","first-page":"1230","DOI":"10.1074\/jbc.270.3.1230","article-title":"Purification and characterization of Hypoxia-inducible Factor 1","volume":"270","author":"Wang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0365","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1006\/bbrc.1997.6371","article-title":"cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix\/PAS protein (BMAL1) and identification of alternatively spliced variants with alternative translation initiation site usage 1","volume":"264","author":"Ikeda","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0370","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/embor.2010.170","article-title":"The hypoxia-inducible transcription factor pathway regulates oxygen sensing in the simplest animal, Trichoplax adhaerens","volume":"12","author":"Loenarz","year":"2011","journal-title":"EMBO Rep."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0375","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.febslet.2004.05.079","article-title":"Increase of SUMO-1 expression in response to hypoxia: direct interaction with HIF-1\u03b1 in adult mouse brain and heart in vivo","volume":"569","author":"Shao","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0380","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1093\/cvr\/cvu177","article-title":"SENP1 protects against myocardial ischaemia\/reperfusion injury via a HIF1\u03b1-dependent pathway","volume":"104","author":"Gu","year":"2014","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0385","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1016\/j.cell.2007.08.045","article-title":"SUMO-specific protease 1 is essential for stabilization of HIF1\u03b1 during hypoxia","volume":"131","author":"Cheng","year":"2007","journal-title":"Cell."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0390","doi-asserted-by":"crossref","first-page":"2748","DOI":"10.1038\/emboj.2009.210","article-title":"SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation","volume":"28","author":"Huang","year":"2009","journal-title":"EMBO J."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0395","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.ghir.2013.12.002","article-title":"Increased genome instability and oxidative DNA damage and their association with IGF-1 levels in patients with active acromegaly","volume":"24","author":"Bayram","year":"2014","journal-title":"Growth Hormon. IGF Res."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0400","doi-asserted-by":"crossref","first-page":"12666","DOI":"10.1074\/jbc.M113.546481","article-title":"C-terminal src kinase (CSK)-mediated phosphorylation of eukaryotic elongation factor 2 (EEF2) promotes proteolytic cleavage and nuclear translocation of EEF2","volume":"289","author":"Yao","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0405","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1016\/j.cell.2013.04.055","article-title":"The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation","volume":"153","author":"Leprivier","year":"2013","journal-title":"Cell."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0410","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1016\/j.jjcc.2016.05.020","article-title":"Phosphorylated eEF2 is SUMOylated and induces cardiomyocyte apoptosis during myocardial ischemia reperfusion","volume":"69","author":"Zhang","year":"2017","journal-title":"J. Cardiol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0415","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1007\/s10495-017-1355-5","article-title":"Heat shock protein 70 protects cardiomyocytes through suppressing SUMOylation and nucleus translocation of phosphorylated eukaryotic elongation factor 2 during myocardial ischemia and reperfusion","volume":"22","author":"Zhang","year":"2017","journal-title":"Apoptosis."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0420","doi-asserted-by":"crossref","first-page":"1390","DOI":"10.1128\/MCB.01307-14","article-title":"HSP105 recruits protein phosphatase 2A to dephosphorylate \u03b2-catenin","volume":"35","author":"Yu","year":"2015","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0425","first-page":"3","article-title":"Inhibitors targeting the SUMOylation pathway: a patent review 2012-2015 (review)","volume":"41","author":"Zhou","year":"2018","journal-title":"Int. J. Mol. Med."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0430","doi-asserted-by":"crossref","DOI":"10.1016\/j.heliyon.2018.e00601","article-title":"SENP1 and SENP2 regulate SUMOylation of amyloid precursor protein","volume":"4","author":"Maruyama","year":"2018","journal-title":"Heliyon."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0435","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.gep.2009.11.004","article-title":"Gene expression patterns sexually dimorphic gene expression of the Zimp7 and Zimp10 genes in embryonic gonads","volume":"10","author":"Rodr\u00edguez-magad\u00e1n","year":"2010","journal-title":"Gene Expr. Patterns"},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0440","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep15768","article-title":"5-Azacytidine modulates interferon regulatory factor 1 in macrophages to exert a cardioprotective effect","volume":"5","author":"Jeong","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.yjmcc.2019.07.009_bb0445","first-page":"1","article-title":"Luteolin improves cardiac dysfunction in heart failure rats by regulating sarcoplasmic reticulum","author":"Hu","year":"2017","journal-title":"Nat. Publ. Gr."}],"container-title":["Journal of Molecular and Cellular Cardiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022282819301518?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022282819301518?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T20:29:06Z","timestamp":1758313746000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022282819301518"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,9]]},"references-count":89,"alternative-id":["S0022282819301518"],"URL":"https:\/\/doi.org\/10.1016\/j.yjmcc.2019.07.009","relation":{},"ISSN":["0022-2828"],"issn-type":[{"value":"0022-2828","type":"print"}],"subject":[],"published":{"date-parts":[[2019,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Roles and mechanisms of SUMOylation on key proteins in myocardial ischemia\/reperfusion injury","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular and Cellular Cardiology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.yjmcc.2019.07.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}