[1]	Roth GA, Mensah GA, Johnson CO, et al. Global burden of cardiovascular diseases and risk factors,1990-2019:update from the GBD 2019 study[J]. J Am Coll Cardiol, 2020, 76(25):2982-3021.DOI:10.1016/j.jacc.2020.11.010. Cited in this article [1]

[2]	Balakumar P, Maung UK, Jagadeesh G. Prevalence and prevention of cardiovascular disease and diabetes mellitus[J]. Pharmacol Res, 2016, 113(Pt A):600-609.DOI:10.1016/j.phrs.2016.09.040. Cited in this article [1]

[3]	van den Boogert MAW, Larsen LE, Ali L, et al. N-glycosylation defects in humans lower low-density lipoprotein cholesterol through increased low-density lipoprotein receptor expression[J]. Circulation, 2019, 140(4):280-292.DOI:10.1161/CIRCULATIONAHA.118.036484. Cited in this article [1]

[4]	Jagavelu K, Tietge UJ, Gaestel M, et al. Systemic deficiency of the map kinase-activated protein kinase 2 reduces atherosclerosis in hypercholesterolemic mice[J]. Circ Res, 2007, 101(11):1104-1112.DOI:10.1161/CIRCRESAHA.107.156075. Cited in this article [1]

[5]	Hermann J, Schurgers L, Jankowski V. Identification and characterization of post-translational modifications:Clinical implications[J]. Mol Aspects Med, 2022, 86:101066.DOI:10.1016/j.mam.2022.101066. Cited in this article [1]

[6]	Gao J, Shao K, Chen X, et al. The involvement of post-translational modifications in cardiovascular pathologies:focus on sumoylation,neddylation,succinylation,and prenylation[J]. J Mol Cell Cardiol, 2020, 138:49-58.DOI:10.1016/j.yjmcc.2019.11.146. Cited in this article [1]

[7]	Ramazi S, Zahiri J. Posttranslational modifications in proteins:resources,tools and prediction methods[J]. Database (Oxford), 2021, 2021:baab012.DOI:10.1093/database/baab012. Cited in this article [1]

[8]	Stastna M, Van Eyk JE. Posttranslational modifications of lysine and evolving role in heart pathologies-recent developments[J]. Proteomics, 2015, 15(5-6):1164-1180.DOI:10.1002/pmic.201400312. Cited in this article [1]

[9]	Striebel F, Imkamp F, Ozcelik D, et al. Pupylation as a signal for proteasomal degradation in bacteria[J]. Biochim Biophys Acta, 2014, 1843(1):103-113.DOI:10.1016/j.bbamcr.2013.03.022. Cited in this article [1]

[10]	王志鹏, 程农壹, 梁妍钰, 等. 蛋白质中新型赖氨酸翻译后修饰的结构简介[J]. 大学化学, 2017, 32(12):41-47.DOI:10.3866/PKU.DXHX201708002. Cited in this article [1]

[11]	Zhang Z, Tan M, Xie Z, et al. Identification of lysine succinylation as a new post-translational modification[J]. Nat Chem Biol, 2011, 7(1):58-63.DOI:10.1038/nchembio.495. Cited in this article [1]

[12]	Xie Z, Dai J, Dai L, et al. Lysine succinylation and lysine malonylation in histones[J]. Mol Cell Proteomics, 2012, 11(5):100-107.DOI:10.1074/mcp.M111.015875. Cited in this article [1]

[13]	Sreedhar A, Wiese EK, Hitosugi T. Enzymatic and metabolic regulation of lysine succinylation[J]. Genes Dis, 2020, 7(2):166-171.DOI:10.1016/j.gendis.2019.09.011. Cited in this article [1]

[14]	Sabari BR, Zhang D, Allis CD, Zhao Y. Metabolic regulation of gene expression through histone acylations[J]. Nat Rev Mol Cell Biol, 2017, 18(2):90-101.DOI:10.1038/nrm.2016.140. Cited in this article [1]

[15]	Wagner GR, Payne RM. Widespread and enzyme-independent nepsilon-acetylation and nepsilon-succinylation of proteins in the chemical conditions of the mitochondrial matrix[J]. J Biol Chem, 2013, 288(40):29036-29045.DOI:10.1074/jbc.M113.486753. Cited in this article [1]

[16]	Wagner GR, Bhatt DP, O’Connell TM, et al. A class of reactive acyl-coa species reveals the non-enzymatic origins of protein acylation[J]. Cell Metab, 2017, 25(4):823-837.e8.DOI:10.1016/j.cmet.2017.03.006. Cited in this article [1]

[17]	Kurmi K, Hitosugi S, Wiese EK, et al. Carnitine palmitoyltransferase 1a has a lysine succinyltransferase activity[J]. Cell Rep, 2018, 22(6):1365-1373.DOI:10.1016/j.celrep.2018.01.030. Cited in this article [1]

[18]	Gibson GE, Xu H, Chen HL, et al. Alpha-ketoglutarate dehydrogenase complex-dependent succinylation of proteins in neurons and neuronal cell lines[J]. J Neurochem, 2015, 134(1):86-96.DOI:10.1111/jnc.13096. Cited in this article [2]

[19]	Hansen GE, Gibson GE. The alpha-ketoglutarate dehydrogenase complex as a hub of plasticity in neurodegeneration and regeneration[J]. Int J Mol Sci, 2022, 23(20).DOI:10.3390/ijms232012403. Cited in this article [1]

[20]	Wang Y, Guo YR, Liu K, et al. Kat2a coupled with the alpha-kgdh complex acts as a histone h3 succinyltransferase[J]. Nature, 2017, 552(7684):273-277.DOI:10.1038/nature25003. Cited in this article [1]

[21]	Yang G, Yuan Y, Yuan H, et al. Histone acetyltransferase 1 is a succinyltransferase for histones and non-histones and promotes tumorigenesis[J]. EMBO Rep, 2021, 22(2):e50967.DOI:10.15252/embr.202050967. Cited in this article [1]

[22]	Sun L, Yao Z, Guo Z, et al. Comprehensive analysis of the lysine acetylome in aeromonas hydrophila reveals cross-talk between lysine acetylation and succinylation in luxs[J]. Emerg Microbes Infect, 2019, 8(1):1229-1239.DOI:10.1080/22221751.2019.1656549. Cited in this article [1]

[23]	Colak G, Xie Z, Zhu AY, et al. Identification of lysine succinylation substrates and the succinylation regulatory enzyme cobb in escherichia coli[J]. Mol Cell Proteomics, 2013, 12(12):3509-3520.DOI:10.1074/mcp.M113.031567. Cited in this article [1]

[24]	Du J, Zhou Y, Su X, et al. Sirt5 is a nad-dependent protein lysine demalonylase and desuccinylase[J]. Science, 2011, 334(6057):806-809.DOI:10.1126/science.1207861. Cited in this article [1]

[25]	Rardin MJ, He W, Nishida Y, et al. Sirt5 regulates the mitochondrial lysine succinylome and metabolic networks[J]. Cell Metab, 2013, 18(6):920-933.DOI:10.1016/j.cmet.2013.11.013. Cited in this article [3]

[26]	Park J, Chen Y, Tishkoff DX, et al. Sirt5-mediated lysine desuccinylation impacts diverse metabolic pathways[J]. Mol Cell, 2013, 50(6):919-930.DOI:10.1016/j.molcel.2013.06.001. Cited in this article [2]

[27]	Li L, Shi L, Yang S, et al. Sirt7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability[J]. Nat Commun, 2016, 7:12235.DOI:10.1038/ncomms12235. Cited in this article [1]

[28]	Li J, Lu L, Liu L, et al. Hdac1/2/3 are major histone desuccinylases critical for promoter desuccinylation[J]. Cell Discov, 2023, 9(1):85.DOI:10.1038/s41421-023-00573-9. Cited in this article [2]

[29]	Dong YN, Mesaros C, Xu P, et al. Frataxin controls ketone body metabolism through regulation of oxct1[J]. PNAS Nexus, 2022, 1(3):pgac142.DOI:10.1093/pnasnexus/pgac142. Cited in this article [1]

[30]	Chen XF, Chen X, Tang X. Short-chain fatty acid,acylation and cardiovascular diseases[J]. Clin Sci (Lond), 2020, 134(6):657-676.DOI:10.1042/CS20200128. Cited in this article [1]

[31]	Chinopoulos C. The mystery of extramitochondrial proteins lysine succinylation[J]. Int J Mol Sci, 2021, 22(11):6085.DOI:10.3390/ijms22116085. Cited in this article [1]

[32]	Burch JS, Marcero JR, Maschek JA, et al. Glutamine via alpha-ketoglutarate dehydrogenase provides succinyl-coa for heme synthesis during erythropoiesis[J]. Blood, 2018, 132(10):987-998.DOI:10.1182/blood-2018-01-829036. Cited in this article [1]

[33]	Sadhukhan S, Liu X, Ryu D, et al. Metabolomics-assisted proteomics identifies succinylation and sirt5 as important regulators of cardiac function[J]. Proc Natl Acad Sci USA, 2016, 113(16):4320-4325.DOI:10.1073/pnas.1519858113. Cited in this article [2]

[34]	Zhou L, Wang F, Sun R, et al. Sirt5 promotes idh2 desuccinylation and g6pd deglutarylation to enhance cellular antioxidant defense[J]. EMBO Rep, 2016, 17(6):811-822.DOI:10.15252/embr.201541643. Cited in this article [1]

[35]	Chen H, Xu H, Potash S, et al. Mild metabolic perturbations alter succinylation of mitochondrial proteins[J]. J Neurosci Res, 2017, 95(11):2244-2252.DOI:10.1002/jnr.24103. Cited in this article [1]

[36]	Chen XF, Tian MX, Sun RQ, et al. Sirt5 inhibits peroxisomal acox1 to prevent oxidative damage and is downregulated in liver cancer[J]. EMBO Rep, 2018, 19(5):e45124.DOI:10.15252/embr.201745124. Cited in this article [1]

[37]	Fukushima A, Alrob OA, Zhang L, et al. Acetylation and succinylation contribute to maturational alterations in energy metabolism in the newborn heart[J]. Am J Physiol Heart Circ Physiol, 2016, 311(2):H347-H363.DOI:10.1152/ajpheart.00900.2015. Cited in this article [1]

[38]	Torres-Perez JV, Irfan J, Febrianto MR, et al. Histone post-translational modifications as potential therapeutic targets for pain management[J]. Trends Pharmacol Sci, 2021, 42(11):897-911.DOI:10.1016/j.tips.2021.08.002. Cited in this article [1]

[39]	Pineiro M, Hernandez F, Palacian E. Succinylation of histone amino groups facilitates transcription of nucleosomal cores[J]. Biochim Biophys Acta, 1992, 1129(2):183-187.DOI:10.1016/0167-4781(92)90485-i. Cited in this article [1]

[40]	Smestad J, Erber L, Chen Y, et al. Chromatin succinylation correlates with active gene expression and is perturbed by defective tca cycle metabolism[J]. iScience, 2018, 2:63-75.DOI:10.1016/j.isci.2018.03.012. Cited in this article [1]

[41]	Liu J, Shangguan Y, Tang D, et al. Histone succinylation and its function on the nucleosome[J]. J Cell Mol Med, 2021, 25(15):7101-7109.DOI:10.1111/jcmm.16676. Cited in this article [1]

[42]	Xu HD, Wang LN, Wen PP, et al. Site-specific systematic analysis of lysine modification crosstalk[J]. Proteomics, 2018, 18(9):e1700292.DOI:10.1002/pmic.201700292. Cited in this article [1]

[43]	Ali HR, Assiri MA, Harris PS, et al. Quantifying competition among mitochondrial protein acylation events induced by ethanol metabolism[J]. J Proteome Res, 2019, 18(4):1513-1531.DOI:10.1021/acs.jproteome.8b00800. Cited in this article [1]

[44]	Nishida Y, Rardin MJ, Carrico C, et al. Sirt5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target[J]. Mol Cell, 2015, 59(2):321-332.DOI:10.1016/j.molcel.2015.05.022. Cited in this article [1]

[45]	Zhou B, Xiao M, Hu H, et al. Cardioprotective role of sirt5 in response to acute ischemia through a novel liver-cardiac crosstalk mechanism[J]. Front Cell Dev Biol, 2021, 9:687559.DOI:10.3389/fcell.2021.687559. Cited in this article [1]

[46]	Takada S, Maekawa S, Furihata T, et al. Succinyl-coa-based energy metabolism dysfunction in chronic heart failure[J]. Proc Natl Acad Sci USA, 2022, 119(41):e2203628119.DOI:10.1073/pnas.2203628119. Cited in this article [1]

[47]	Wang Y, Zhou H, Wu J, et al. Mg53 alleviates hypoxia/reoxygenation-induced cardiomyocyte injury by succinylation and ubiquitination modification[J]. Clin Exp Hypertens, 2023, 45(1):2271196.DOI:10.1080/10641963.2023.2271196. Cited in this article [1]

[48]	Boylston JA, Sun J, Chen Y, et al. Characterization of the cardiac succinylome and its role in ischemia-reperfusion injury[J]. J Mol Cell Cardiol, 2015, 88:73-81.DOI:10.1016/j.yjmcc.2015.09.005. Cited in this article [1]

[49]	Ali HR, Michel CR, Lin YH, et al. Defining decreased protein succinylation of failing human cardiac myofibrils in ischemic cardiomyopathy[J]. J Mol Cell Cardiol, 2020, 138:304-317.DOI:10.1016/j.yjmcc.2019.11.159. Cited in this article [1]

[50]	Hershberger KA, Abraham DM, Martin AS, et al. Sirtuin 5 is required for mouse survival in response to cardiac pressure overload[J]. J Biol Chem, 2017, 292(48):19767-19781.DOI:10.1074/jbc.M117.809897. Cited in this article [1]

[51]	Cheng X, Wang K, Zhao Y, et al. Research progress on post-translational modification of proteins and cardiovascular diseases[J]. Cell Death Discov, 2023, 9(1):275.DOI:10.1038/s41420-023-01560-5. Cited in this article [1]

[52]	Hershberger KA, Abraham DM, Liu J, et al. Ablation of sirtuin5 in the postnatal mouse heart results in protein succinylation and normal survival in response to chronic pressure overload[J]. J Biol Chem, 2018, 293(27):10630-10645.DOI:10.1074/jbc.RA118.002187. Cited in this article [1]

[53]	Bai F, Ma Y, Liu Q. Succinylation as a novel mode of energy metabolism regulation during atrial fibrillation[J]. Med Hypotheses, 2018, 121:54-55.DOI:10.1016/j.mehy.2018.09.018. Cited in this article [1]

[54]	Bai F, Tu T, Qin F, et al. Quantitative proteomics of changes in succinylated proteins expression profiling in left appendages tissue from valvular heart disease patients with atrial fibrillation[J]. Clin Chim Acta, 2019, 495:345-354.DOI:10.1016/j.cca.2019.05.002. Cited in this article [1]

[55]	Gyongyosi M, Winkler J, Ramos I, et al. Myocardial fibrosis:biomedical research from bench to bedside[J]. Eur J Heart Fail, 2017, 19(2):177-191.DOI:10.1002/ejhf.696. Cited in this article [1]

[56]

Chang X, Zhang T, Wang J, et al. Sirt5-related desuccinylation modification contributes to quercetin-induced protection against heart failure and high-glucose-prompted cardiomyocytes injured through regulation of mitochondrial quality surveillance[J]. Oxid Med Cell Longev, 2021, 2021:5876841.DOI:10.1155/2021/5876841. Cited in this article [1]

[57]	Chakraborty A, Li Y, Zhang C, et al. Programmed cell death in aortic aneurysm and dissection:a potential therapeutic target[J]. J Mol Cell Cardiol, 2022, 163:67-80.DOI:10.1016/j.yjmcc.2021.09.010. Cited in this article [1]

[58]	Nienaber CA, Clough RE, Sakalihasan N, et al. Aortic dissection[J]. Nat Rev Dis Primers, 2016, 2:16053.DOI:10.1038/nrdp.2016.53. Cited in this article [1]

[59]	Zhang H, Zhang Y, Wang H, et al. Global proteomic analysis reveals lysine succinylation contributes to the pathogenesis of aortic aneurysm and dissection[J]. J Proteomics, 2023, 280:104889.DOI:10.1016/j.jprot.2023.104889. Cited in this article [1]

[60]	Zhang Y, Zhang H, Wang H, et al. Tandem mass tag-based quantitative proteomic analysis identification of succinylation related proteins in pathogenesis of thoracic aortic aneurysm and aortic dissection[J]. Peer J, 2023, 11:e15258.DOI:10.7717/peerj.15258. Cited in this article [1]