{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T08:17:57Z","timestamp":1793089077769,"version":"4.5.0"},"reference-count":140,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2025,11,19]],"date-time":"2025-11-19T00:00:00Z","timestamp":1763510400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2025,11,19]],"date-time":"2025-11-19T00:00:00Z","timestamp":1763510400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100006345","name":"Uniwersytet Mikolaja Kopernika w Toruniu","doi-asserted-by":"publisher","award":["IDUB 2025"],"award-info":[{"award-number":["IDUB 2025"]}],"id":[{"id":"10.13039\/501100006345","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["GeroScience"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>As the world\u2019s population ages, strategies to promote healthy longevity are critical. SIRT5, belonging to the sirtuin family, plays a key role in regulating cellular metabolism and mitochondrial homeostasis by removing post-translational modifications such as succinylation, malonylation, and glutarylisation from lysine residues of proteins. Herein, we discuss the multifunctionality of SIRT5, its impact on heart function, and its involvement as a target in geroscience for the pathogenesis of cardiovascular diseases, including heart failure, diabetic cardiomyopathy, cardiac hypertrophy, and ischemia-reperfusion injury. Research indicates that SIRT5 modulates metabolic pathways, oxidative stress response, and apoptosis, making it a potential therapeutic target for extending the health span and lifespan. However, its role is complex and context-dependent, exhibiting protective and harmful effects in various pathological conditions.<\/jats:p>","DOI":"10.1007\/s11357-025-02021-w","type":"journal-article","created":{"date-parts":[[2025,11,19]],"date-time":"2025-11-19T01:09:52Z","timestamp":1763514592000},"page":"2101-2121","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Unveiling the importance of SIRT5 for cardiac health and disease in an era of increasing longevity"],"prefix":"10.1007","volume":"48","author":[{"given":"Arkadiusz","family":"Grzeczka","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Szymon","family":"Graczyk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3344-5060","authenticated-orcid":false,"given":"Pawel","family":"Kordowitzki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,11,19]]},"reference":[{"key":"2021_CR1","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1097\/CRD.0b013e318274956d","volume":"21","author":"PS Azevedo","year":"2013","unstructured":"Azevedo PS, Minicucci MF, Santos PP, Paiva SAR, Zornoff LAM. Energy metabolism in cardiac remodeling and heart failure. Cardiol Rev. 2013;21:135. https:\/\/doi.org\/10.1097\/CRD.0b013e318274956d.","journal-title":"Cardiol Rev"},{"key":"2021_CR2","doi-asserted-by":"publisher","first-page":"132","DOI":"10.1111\/j.1527-5299.2002.00717.x","volume":"8","author":"D Sorescu","year":"2002","unstructured":"Sorescu D, Griendling KK. Reactive oxygen species, mitochondria, and NAD(P)H oxidases in the development and progression of heart failure. Congest Heart Fail. 2002;8:132\u201340. https:\/\/doi.org\/10.1111\/j.1527-5299.2002.00717.x.","journal-title":"Congest Heart Fail"},{"key":"2021_CR3","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1023\/A:1015332726303","volume":"7","author":"JJ Lehman","year":"2002","unstructured":"Lehman JJ, Kelly DP. Gene regulatory mechanisms governing energy metabolism during cardiac hypertrophic growth. Heart Fail Rev. 2002;7:175\u201385. https:\/\/doi.org\/10.1023\/A:1015332726303.","journal-title":"Heart Fail Rev"},{"key":"2021_CR4","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41420-023-01560-5","volume":"9","author":"X Cheng","year":"2023","unstructured":"Cheng X, Wang K, Zhao Y, Wang K. Research progress on post-translational modification of proteins and cardiovascular diseases. Cell Death Discov. 2023;9:1\u201312. https:\/\/doi.org\/10.1038\/s41420-023-01560-5.","journal-title":"Cell Death Discov"},{"key":"2021_CR5","doi-asserted-by":"publisher","first-page":"193","DOI":"10.31662\/jmaj.2020-0036","volume":"3","author":"Y Morita","year":"2020","unstructured":"Morita Y, Tohyama S. Metabolic regulation of cardiac differentiation and maturation in pluripotent stem cells: a lesson from heart development. JMA J. 2020;3:193\u2013200. https:\/\/doi.org\/10.31662\/jmaj.2020-0036.","journal-title":"JMA J"},{"key":"2021_CR6","doi-asserted-by":"publisher","first-page":"1487","DOI":"10.1161\/CIRCRESAHA.121.318241","volume":"128","author":"GD Lopaschuk","year":"2021","unstructured":"Lopaschuk GD, Karwi QG, Tian R, Wende AR, Abel ED. Cardiac energy metabolism in heart failure. Circ Res. 2021;128:1487\u2013513. https:\/\/doi.org\/10.1161\/CIRCRESAHA.121.318241.","journal-title":"Circ Res"},{"key":"2021_CR7","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41392-022-01257-8","volume":"7","author":"Q-J Wu","year":"2022","unstructured":"Wu Q-J, Zhang T-N, Chen H-H, Yu X-F, Lv J-L, Liu Y-Y, et al. The sirtuin family in health and disease. Signal Transduct Target Ther. 2022;7:1\u201374. https:\/\/doi.org\/10.1038\/s41392-022-01257-8.","journal-title":"Signal Transduct Target Ther"},{"key":"2021_CR8","doi-asserted-by":"publisher","DOI":"10.1038\/s41514-025-00256-7","volume":"11","author":"A Grzeczka","year":"2025","unstructured":"Grzeczka A, Skowronska A, Sepe S, Skowronski MT, Kordowitzki P. Sirtuins and their role in ovarian aging-related fibrosis predisposing to ovarian cancer. NPJ Aging. 2025;11:65. https:\/\/doi.org\/10.1038\/s41514-025-00256-7.","journal-title":"NPJ Aging"},{"key":"2021_CR9","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejmech.2022.114363","volume":"236","author":"Y Wang","year":"2022","unstructured":"Wang Y, Chen H, Zha X. Overview of SIRT5 as a potential therapeutic target: structure, function and inhibitors. Eur J Med Chem. 2022;236:114363. https:\/\/doi.org\/10.1016\/j.ejmech.2022.114363.","journal-title":"Eur J Med Chem"},{"key":"2021_CR10","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1016\/j.ijcard.2018.11.019","volume":"284","author":"K Satoh","year":"2019","unstructured":"Satoh K, Shimokawa H. Sirtuin 5 promotes ischemia\/reperfusion-induced blood-brain barrier damage after stroke. Int J Cardiol. 2019;284:77\u20138. https:\/\/doi.org\/10.1016\/j.ijcard.2018.11.019.","journal-title":"Int J Cardiol"},{"key":"2021_CR11","doi-asserted-by":"publisher","first-page":"19767","DOI":"10.1074\/jbc.M117.809897","volume":"292","author":"KA Hershberger","year":"2017","unstructured":"Hershberger KA, Abraham DM, Martin AS, Mao L, Liu J, Gu H, et al. Sirtuin 5 is required for mouse survival in response to cardiac pressure overload. J Biol Chem. 2017;292:19767\u201381.","journal-title":"J Biol Chem"},{"key":"2021_CR12","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1016\/j.gene.2018.07.010","volume":"675","author":"L Chen","year":"2018","unstructured":"Chen L, Wang H, Gao F, Zhang J, Zhang Y, Ma R, et al. Functional genetic variants in the SIRT5 gene promoter in acute myocardial infarction. Gene. 2018;675:233\u20139. https:\/\/doi.org\/10.1016\/j.gene.2018.07.010.","journal-title":"Gene"},{"key":"2021_CR13","doi-asserted-by":"publisher","first-page":"912","DOI":"10.1007\/s11427-015-4902-8","volume":"58","author":"X Yang","year":"2015","unstructured":"Yang X, Liu B, Zhu W, Luo J. SIRT5, functions in cellular metabolism with a multiple enzymatic activities. Sci China Life Sci. 2015;58:912\u20134. https:\/\/doi.org\/10.1007\/s11427-015-4902-8.","journal-title":"Sci China Life Sci"},{"key":"2021_CR14","doi-asserted-by":"publisher","first-page":"560","DOI":"10.1016\/j.cell.2009.02.026","volume":"137","author":"T Nakagawa","year":"2009","unstructured":"Nakagawa T, Lomb DJ, Haigis MC, Guarente L. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell. 2009;137:560\u201370. https:\/\/doi.org\/10.1016\/j.cell.2009.02.026.","journal-title":"Cell"},{"key":"2021_CR15","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1016\/j.cmet.2014.03.014","volume":"19","author":"M Tan","year":"2014","unstructured":"Tan M, Peng C, Anderson KA, Chhoy P, Xie Z, Dai L, et al. Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell Metab. 2014;19:605\u201317. https:\/\/doi.org\/10.1016\/j.cmet.2014.03.014.","journal-title":"Cell Metab"},{"key":"2021_CR16","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1080\/15548627.2015.1009778","volume":"11","author":"L Polletta","year":"2015","unstructured":"Polletta L, Vernucci E, Carnevale I, Arcangeli T, Rotili D, Palmerio S, et al. SIRT5 regulation of ammonia-induced autophagy and mitophagy. Autophagy. 2015;11:253\u201370. https:\/\/doi.org\/10.1080\/15548627.2015.1009778.","journal-title":"Autophagy"},{"key":"2021_CR17","doi-asserted-by":"publisher","DOI":"10.1016\/j.cellsig.2024.111570","volume":"127","author":"H Yang","year":"2025","unstructured":"Yang H, Gao S, Lu G, He J, Dong J, Zhang X, et al. SIRT5-mediated GLS and GDH desuccinylation attenuates the autophagy of bovine mammary epithelial cells induced by ammonia. Cell Signal. 2025;127:111570. https:\/\/doi.org\/10.1016\/j.cellsig.2024.111570.","journal-title":"Cell Signal"},{"key":"2021_CR18","doi-asserted-by":"publisher","first-page":"4076","DOI":"10.1016\/j.febslet.2012.10.009","volume":"586","author":"Y Nakamura","year":"2012","unstructured":"Nakamura Y, Ogura M, Ogura K, Tanaka D, Inagaki N. SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice. FEBS Lett. 2012;586:4076\u201381. https:\/\/doi.org\/10.1016\/j.febslet.2012.10.009.","journal-title":"FEBS Lett"},{"key":"2021_CR19","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1016\/j.molcel.2015.05.022","volume":"59","author":"Y Nishida","year":"2015","unstructured":"Nishida Y, Rardin MJ, Carrico C, He W, Sahu AK, Gut P, et al. SIRT5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target. Mol Cell. 2015;59:321\u201332. https:\/\/doi.org\/10.1016\/j.molcel.2015.05.022.","journal-title":"Mol Cell"},{"key":"2021_CR20","doi-asserted-by":"publisher","first-page":"2331","DOI":"10.1016\/j.celrep.2017.05.065","volume":"19","author":"F Wang","year":"2017","unstructured":"Wang F, Wang K, Xu W, Zhao S, Ye D, Wang Y, et al. SIRT5 desuccinylates and activates pyruvate kinase M2 to block macrophage IL-1\u03b2 production and to prevent DSS-induced colitis in mice. Cell Rep. 2017;19:2331\u201344. https:\/\/doi.org\/10.1016\/j.celrep.2017.05.065.","journal-title":"Cell Rep"},{"key":"2021_CR21","doi-asserted-by":"publisher","first-page":"39517","DOI":"10.1038\/srep39517","volume":"6","author":"YS Xu","year":"2016","unstructured":"Xu YS, Liang JJ, Wang Y, Zhao XJ, Xu L, Xu Y, et al. STAT3 undergoes acetylation-dependent mitochondrial translocation to regulate pyruvate metabolism. Sci Rep. 2016;6:39517. https:\/\/doi.org\/10.1038\/srep39517.","journal-title":"Sci Rep"},{"key":"2021_CR22","doi-asserted-by":"publisher","first-page":"919","DOI":"10.1016\/j.molcel.2013.06.001","volume":"50","author":"J Park","year":"2013","unstructured":"Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, et al. SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol Cell. 2013;50:919\u201330. https:\/\/doi.org\/10.1016\/j.molcel.2013.06.001.","journal-title":"Mol Cell"},{"key":"2021_CR23","doi-asserted-by":"publisher","first-page":"124","DOI":"10.1038\/s41392-024-01839-8","volume":"9","author":"Y Zong","year":"2024","unstructured":"Zong Y, Li H, Liao P, Chen L, Pan Y, Zheng Y, et al. Mitochondrial dysfunction: mechanisms and advances in therapy. Signal Transduct Target Ther. 2024;9:124. https:\/\/doi.org\/10.1038\/s41392-024-01839-8.","journal-title":"Signal Transduct Target Ther"},{"key":"2021_CR24","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1038\/s41418-023-01240-y","volume":"31","author":"P Teng","year":"2024","unstructured":"Teng P, Cui K, Yao S, Fei B, Ling F, Li C, et al. SIRT5-mediated ME2 desuccinylation promotes cancer growth by enhancing mitochondrial respiration. Cell Death Differ. 2024;31:65\u201377.","journal-title":"Cell Death Differ"},{"key":"2021_CR25","doi-asserted-by":"publisher","first-page":"10239","DOI":"10.1074\/jbc.M117.785022","volume":"292","author":"Y Zhang","year":"2017","unstructured":"Zhang Y, Bharathi SS, Rardin MJ, Lu J, Maringer KV, Sims-Lucas S, et al. Lysine desuccinylase SIRT5 binds to cardiolipin and regulates the electron transport chain. J Biol Chem. 2017;292:10239\u201349. https:\/\/doi.org\/10.1074\/jbc.M117.785022.","journal-title":"J Biol Chem"},{"key":"2021_CR26","doi-asserted-by":"publisher","first-page":"920","DOI":"10.1016\/j.cmet.2013.11.013","volume":"18","author":"MJ Rardin","year":"2013","unstructured":"Rardin MJ, He W, Nishida Y, Newman JC, Carrico C, Danielson SR, et al. SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. Cell Metab. 2013;18:920\u201333. https:\/\/doi.org\/10.1016\/j.cmet.2013.11.013.","journal-title":"Cell Metab"},{"key":"2021_CR27","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1016\/j.bbrc.2013.10.033","volume":"441","author":"Z-F Lin","year":"2013","unstructured":"Lin Z-F, Xu H-B, Wang J-Y, Lin Q, Ruan Z, Liu F-B, et al. SIRT5 desuccinylates and activates SOD1 to eliminate ROS. Biochem Biophys Res Commun. 2013;441:191\u20135. https:\/\/doi.org\/10.1016\/j.bbrc.2013.10.033.","journal-title":"Biochem Biophys Res Commun"},{"key":"2021_CR28","doi-asserted-by":"publisher","first-page":"7235","DOI":"10.7150\/thno.52934","volume":"11","author":"X He","year":"2021","unstructured":"He X, Li T, Qin K, Luo S, Li Z, Ji Q, et al. Demalonylation of DDX3 by sirtuin 5 promotes antiviral innate immune responses. Theranostics. 2021;11:7235\u201346. https:\/\/doi.org\/10.7150\/thno.52934.","journal-title":"Theranostics"},{"key":"2021_CR29","doi-asserted-by":"publisher","first-page":"722","DOI":"10.1038\/s41418-021-00886-w","volume":"29","author":"X Liu","year":"2022","unstructured":"Liu X, Rong F, Tang J, Zhu C, Chen X, Jia S, et al. Repression of P53 function by SIRT5-mediated desuccinylation at lysine 120 in response to DNA damage. Cell Death Differ. 2022;29:722\u201336. https:\/\/doi.org\/10.1038\/s41418-021-00886-w.","journal-title":"Cell Death Differ"},{"key":"2021_CR30","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2022.101723","volume":"298","author":"DP Bhatt","year":"2022","unstructured":"Bhatt DP, Mills CA, Anderson KA, Henriques BJ, Lucas TG, Francisco S, et al. Deglutarylation of glutaryl-CoA dehydrogenase by deacylating enzyme SIRT5 promotes lysine oxidation in mice. J Biol Chem. 2022;298:101723.","journal-title":"J Biol Chem"},{"key":"2021_CR31","doi-asserted-by":"publisher","first-page":"1459","DOI":"10.1093\/gerona\/glx247","volume":"73","author":"TA Donlon","year":"2018","unstructured":"Donlon TA, Morris BJ, Chen R, Masaki KH, Allsopp RC, Willcox DC, et al. Analysis of polymorphisms in 59 potential candidate genes for association with human longevity. J Gerontol A Biol Sci Med Sci. 2018;73:1459\u201364. https:\/\/doi.org\/10.1093\/gerona\/glx247.","journal-title":"J Gerontol A Biol Sci Med Sci"},{"key":"2021_CR32","doi-asserted-by":"publisher","DOI":"10.3390\/antiox10121939","volume":"10","author":"N Rotllan","year":"2021","unstructured":"Rotllan N, Camacho M, Tondo M, Diarte-A\u00f1azco EMG, Canyelles M, M\u00e9ndez-Lara KA, et al. Therapeutic potential of emerging NAD+-increasing strategies for cardiovascular diseases. Antioxidants. 2021;10:1939. https:\/\/doi.org\/10.3390\/antiox10121939.","journal-title":"Antioxidants"},{"key":"2021_CR33","doi-asserted-by":"publisher","DOI":"10.1172\/JCI158447","author":"S Miwa","year":"2022","unstructured":"Miwa S, Kashyap S, Chini E, Zglinicki T. Mitochondrial dysfunction in cell senescence and aging. J Clin Invest. 2022. https:\/\/doi.org\/10.1172\/JCI158447.","journal-title":"J Clin Invest"},{"key":"2021_CR34","doi-asserted-by":"publisher","unstructured":"Rodr\u00edguez-D\u00edaz A, Mar\u00edn-Conde E, G\u00f3mez-Tatay L. Personalist bioethics as a guide to assessing emerging anti-aging therapies. Linacre Q 2025; 00243639251361196.\u00a0https:\/\/doi.org\/10.1177\/00243639251361196.","DOI":"10.1177\/00243639251361196"},{"key":"2021_CR35","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1038\/s41586-019-1365-2","volume":"571","author":"J Campisi","year":"2019","unstructured":"Campisi J, Kapahi P, Lithgow GJ, Melov S, Newman JC, Verdin E. From discoveries in ageing research to therapeutics for healthy ageing. Nature. 2019;571:183\u201392.","journal-title":"Nature"},{"key":"2021_CR36","doi-asserted-by":"publisher","first-page":"543","DOI":"10.1038\/s41569-018-0059-z","volume":"15","author":"A Picca","year":"2018","unstructured":"Picca A, Mankowski RT, Burman JL, Donisi L, Kim J-S, Marzetti E, et al. Mitochondrial quality control mechanisms as molecular targets in cardiac ageing. Nat Rev Cardiol. 2018;15:543\u201354. https:\/\/doi.org\/10.1038\/s41569-018-0059-z.","journal-title":"Nat Rev Cardiol"},{"key":"2021_CR37","doi-asserted-by":"publisher","first-page":"15510","DOI":"10.1038\/s41598-021-94185-6","volume":"11","author":"TN Haschler","year":"2021","unstructured":"Haschler TN, Horsley H, Balys M, Anderson G, Taanman J-W, Unwin RJ, et al. Sirtuin 5 depletion impairs mitochondrial function in human proximal tubular epithelial cells. Sci Rep. 2021;11:15510. https:\/\/doi.org\/10.1038\/s41598-021-94185-6.","journal-title":"Sci Rep"},{"key":"2021_CR38","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1016\/j.cophys.2018.03.011","volume":"3","author":"MA Walker","year":"2018","unstructured":"Walker MA, Tian R. NAD(H) in mitochondrial energy transduction: implications for health and disease. Curr Opin Physiol. 2018;3:101\u20139. https:\/\/doi.org\/10.1016\/j.cophys.2018.03.011.","journal-title":"Curr Opin Physiol"},{"key":"2021_CR39","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1016\/j.yjmcc.2019.11.159","volume":"138","author":"HR Ali","year":"2020","unstructured":"Ali HR, Michel CR, Lin YH, McKinsey TA, Jeong MY, Ambardekar AV, et al. Defining decreased protein succinylation of failing human cardiac myofibrils in ischemic cardiomyopathy. J Mol Cell Cardiol. 2020;138:304\u201317. https:\/\/doi.org\/10.1016\/j.yjmcc.2019.11.159.","journal-title":"J Mol Cell Cardiol"},{"key":"2021_CR40","doi-asserted-by":"publisher","DOI":"10.3389\/ftox.2023.1267667","author":"D Scieszka","year":"2023","unstructured":"Scieszka D, Bolt AM, McCormick MA, Brigman JL, Campen MJ. Aging, longevity, and the role of environmental stressors: a focus on wildfire smoke and air quality. Front Toxicol. 2023. https:\/\/doi.org\/10.3389\/ftox.2023.1267667.","journal-title":"Front Toxicol"},{"key":"2021_CR41","doi-asserted-by":"publisher","DOI":"10.3389\/fcvm.2021.774619","author":"Y Xin","year":"2021","unstructured":"Xin Y, Zhang X, Li J, Gao H, Li J, Li J, et al. New insights into the role of mitochondria quality control in ischemic heart disease. Front Cardiovasc Med. 2021. https:\/\/doi.org\/10.3389\/fcvm.2021.774619.","journal-title":"Front Cardiovasc Med"},{"key":"2021_CR42","doi-asserted-by":"publisher","DOI":"10.1016\/j.arr.2019.100982","volume":"57","author":"J Luo","year":"2020","unstructured":"Luo J, Mills K, le Cessie S, Noordam R, van Heemst D. Ageing, age-related diseases and oxidative stress: what to do next? Ageing Res Rev. 2020;57:100982. https:\/\/doi.org\/10.1016\/j.arr.2019.100982.","journal-title":"Ageing Res Rev"},{"key":"2021_CR43","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1177\/1098612X13516478","volume":"16","author":"DJ Hall","year":"2014","unstructured":"Hall DJ, Freeman LM, Rush JE, Cunningham SM. Comparison of serum fatty acid concentrations in cats with hypertrophic cardiomyopathy and healthy controls. J Feline Med Surg. 2014;16:631\u20136. https:\/\/doi.org\/10.1177\/1098612X13516478.","journal-title":"J Feline Med Surg"},{"key":"2021_CR44","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1146\/annurev.pathol.4.110807.092250","volume":"5","author":"MC Haigis","year":"2010","unstructured":"Haigis MC, Sinclair DA. Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol Mech Dis. 2010;5:253\u201395. https:\/\/doi.org\/10.1146\/annurev.pathol.4.110807.092250.","journal-title":"Annu Rev Pathol Mech Dis"},{"key":"2021_CR45","doi-asserted-by":"publisher","first-page":"5927","DOI":"10.1038\/s41467-020-19743-4","volume":"11","author":"P Gut","year":"2020","unstructured":"Gut P, Matilainen S, Meyer JG, P\u00e4llijeff P, Richard J, Carroll CJ, et al. SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease. Nat Commun. 2020;11:5927. https:\/\/doi.org\/10.1038\/s41467-020-19743-4.","journal-title":"Nat Commun"},{"key":"2021_CR46","doi-asserted-by":"publisher","DOI":"10.3389\/fphys.2021.763417","author":"KS Kalous","year":"2021","unstructured":"Kalous KS, Wynia-Smith SL, Smith BC. Sirtuin oxidative post-translational modifications. Front Physiol. 2021. https:\/\/doi.org\/10.3389\/fphys.2021.763417.","journal-title":"Front Physiol"},{"key":"2021_CR47","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2024.1407505","author":"X Hou","year":"2024","unstructured":"Hou X, Zhu L, Xu H, Shi J, Ji S. Dysregulation of protein succinylation and disease development. Front Mol Biosci. 2024. https:\/\/doi.org\/10.3389\/fmolb.2024.1407505.","journal-title":"Front Mol Biosci"},{"key":"2021_CR48","doi-asserted-by":"publisher","DOI":"10.1093\/eurheartj\/ehae666.3899","volume":"45","author":"K Yang","year":"2024","unstructured":"Yang K, Akhmedov A, Kraler S, Schmiady M, Puspitasari Y, Camici G, et al. Sirt5 as a mediator of endothelial and vascular dysfunction: potential therapeutic target in aging-related vascular diseases. Eur Heart J. 2024;45:ehae666.3899. https:\/\/doi.org\/10.1093\/eurheartj\/ehae666.3899.","journal-title":"Eur Heart J"},{"key":"2021_CR49","doi-asserted-by":"publisher","DOI":"10.1155\/2021\/5876841","volume":"2021","author":"X Chang","year":"2021","unstructured":"Chang X, Zhang T, Wang J, Liu Y, Yan P, Meng Q, 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. Oxid Med Cell Longev. 2021;2021:5876841. https:\/\/doi.org\/10.1155\/2021\/5876841.","journal-title":"Oxid Med Cell Longev"},{"key":"2021_CR50","doi-asserted-by":"publisher","DOI":"10.1155\/2022\/4155565","volume":"2022","author":"Z Zeng","year":"2022","unstructured":"Zeng Z, Xu P, He Y, Yi Y, Liu Z, Cai J, et al. Acetylation of Atp5f1c mediates cardiomyocyte senescence via metabolic dysfunction in radiation-induced heart damage. Oxid Med Cell Longev. 2022;2022:4155565. https:\/\/doi.org\/10.1155\/2022\/4155565.","journal-title":"Oxid Med Cell Longev"},{"key":"2021_CR51","doi-asserted-by":"publisher","first-page":"1064","DOI":"10.1007\/s00044-024-03249-5","volume":"33","author":"P-T Chen","year":"2024","unstructured":"Chen P-T, Yeong KY. New sirtuin modulators: their uncovering, pharmacophore, and implications in drug discovery. Med Chem Res. 2024;33:1064\u201378. https:\/\/doi.org\/10.1007\/s00044-024-03249-5.","journal-title":"Med Chem Res"},{"key":"2021_CR52","doi-asserted-by":"publisher","DOI":"10.1172\/JCI138926","author":"W Giblin","year":"2021","unstructured":"Giblin W, Bringman-Rodenbarger L, Guo AH, Kumar S, Monovich AC, Mostafa AM, et al. The deacylase SIRT5 supports melanoma viability by influencing chromatin dynamics. J Clin Invest. 2021. https:\/\/doi.org\/10.1172\/JCI138926.","journal-title":"J Clin Invest"},{"key":"2021_CR53","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/j.jbior.2018.09.002","volume":"71","author":"CE Bowman","year":"2019","unstructured":"Bowman CE, Wolfgang MJ. Role of the malonyl-CoA synthetase ACSF3 in mitochondrial metabolism. Adv Biol Regul. 2019;71:34\u201340.","journal-title":"Adv Biol Regul"},{"key":"2021_CR54","doi-asserted-by":"publisher","first-page":"842","DOI":"10.1016\/j.celrep.2013.07.024","volume":"4","author":"BT Weinert","year":"2013","unstructured":"Weinert BT, Sch\u00f6lz C, Wagner SA, Iesmantavicius V, Su D, Daniel JA, et al. Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep. 2013;4:842\u201351.","journal-title":"Cell Rep"},{"key":"2021_CR55","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0045098","volume":"7","author":"F Fischer","year":"2012","unstructured":"Fischer F, Gertz M, Suenkel B, Lakshminarasimhan M, Schutkowski M, Steegborn C. Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition. PLoS One. 2012;7:e45098. https:\/\/doi.org\/10.1371\/journal.pone.0045098.","journal-title":"PLoS One"},{"key":"2021_CR56","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1042\/BCJ20180745","volume":"476","author":"T Hang","year":"2019","unstructured":"Hang T, Chen W, Wu M, Zhan L, Wang C, Jia N, et al. Structural insights into the molecular mechanism underlying Sirt5-catalyzed desuccinylation of histone peptides. Biochem J. 2019;476:211\u201323.","journal-title":"Biochem J"},{"key":"2021_CR57","doi-asserted-by":"publisher","first-page":"2759","DOI":"10.1007\/s10815-024-03223-5","volume":"41","author":"J Ruan","year":"2024","unstructured":"Ruan J, Zheng J, Zhang X, Chen Z, Sun Y, Jia X. SIRT5 suppresses the trophoblast cell proliferation, invasion, and migration to promote preeclampsia via desuccinylating HOXB3. J Assist Reprod Genet. 2024;41:2759\u201370. https:\/\/doi.org\/10.1007\/s10815-024-03223-5.","journal-title":"J Assist Reprod Genet"},{"key":"2021_CR58","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1186\/s12974-024-03284-4","volume":"21","author":"X Zhao","year":"2024","unstructured":"Zhao X, Yang X, Du C, Hao H, Liu S, Liu G, et al. Up-regulated succinylation modifications induce a senescence phenotype in microglia by altering mitochondrial energy metabolism. J Neuroinflammation. 2024;21:296. https:\/\/doi.org\/10.1186\/s12974-024-03284-4.","journal-title":"J Neuroinflammation"},{"key":"2021_CR59","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2024.115060","author":"X Zhang","year":"2024","unstructured":"Zhang X, Ling C, Xiong Z, Gong T, Luo S, Liu X, et al. Desuccinylation of TBK1 by SIRT5 regulates inflammatory response of macrophages in sepsis. Cell Rep. 2024. https:\/\/doi.org\/10.1016\/j.celrep.2024.115060.","journal-title":"Cell Rep"},{"key":"2021_CR60","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1111\/jnc.13096","volume":"134","author":"GE Gibson","year":"2015","unstructured":"Gibson GE, Xu H, Chen H-L, Chen W, Denton TT, Zhang S. Alpha-ketoglutarate dehydrogenase complex-dependent succinylation of proteins in neurons and neuronal cell lines. J Neurochem. 2015;134:86\u201396. https:\/\/doi.org\/10.1111\/jnc.13096.","journal-title":"J Neurochem"},{"key":"2021_CR61","doi-asserted-by":"publisher","first-page":"844","DOI":"10.1016\/j.molcel.2019.03.021","volume":"74","author":"G Wang","year":"2019","unstructured":"Wang G, Meyer JG, Cai W, Softic S, Li ME, Verdin E, et al. Regulation of UCP1 and mitochondrial metabolism in brown adipose tissue by reversible succinylation. Mol Cell. 2019;74:844-857.e7. https:\/\/doi.org\/10.1016\/j.molcel.2019.03.021.","journal-title":"Mol Cell"},{"key":"2021_CR62","doi-asserted-by":"publisher","first-page":"1365","DOI":"10.1016\/j.celrep.2018.01.030","volume":"22","author":"K Kurmi","year":"2018","unstructured":"Kurmi K, Hitosugi S, Wiese EK, Boakye-Agyeman F, Gonsalves WI, Lou Z, et al. Carnitine palmitoyltransferase 1A has a lysine succinyltransferase activity. Cell Rep. 2018;22:1365\u201373. https:\/\/doi.org\/10.1016\/j.celrep.2018.01.030.","journal-title":"Cell Rep"},{"key":"2021_CR63","doi-asserted-by":"publisher","DOI":"10.3390\/ijms22083804","volume":"22","author":"L Siculella","year":"2021","unstructured":"Siculella L, Giannotti L, Di Chiara Stanca B, Calcagnile M, Rochira A, Stanca E, et al. Evidence for a negative correlation between human reactive enamine-imine intermediate deaminase A (RIDA) activity and cell proliferation rate: role of lysine succinylation of RIDA. Int J Mol Sci. 2021;22:3804. https:\/\/doi.org\/10.3390\/ijms22083804.","journal-title":"Int J Mol Sci"},{"key":"2021_CR64","doi-asserted-by":"publisher","DOI":"10.14336\/AD.2022.0711","volume":"14","author":"L Zou","year":"2023","unstructured":"Zou L, Yang Y, Wang Z, Fu X, He X, Song J, et al. Lysine malonylation and its links to metabolism and diseases. Aging Dis. 2023;14:84.","journal-title":"Aging Dis"},{"key":"2021_CR65","doi-asserted-by":"publisher","first-page":"806","DOI":"10.1126\/science.1207861","volume":"334","author":"J Du","year":"2011","unstructured":"Du J, Zhou Y, Su X, Yu JJ, Khan S, Jiang H, et al. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science. 2011;334:806\u20139. https:\/\/doi.org\/10.1126\/science.1207861.","journal-title":"Science"},{"key":"2021_CR66","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.M111.012658","author":"C Peng","year":"2011","unstructured":"Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, et al. The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics. 2011. https:\/\/doi.org\/10.1074\/mcp.M111.012658.","journal-title":"Mol Cell Proteomics"},{"key":"2021_CR67","doi-asserted-by":"publisher","DOI":"10.1016\/j.lfs.2023.121572","volume":"320","author":"J Nah\u00e1lkov\u00e1","year":"2023","unstructured":"Nah\u00e1lkov\u00e1 J. A new view on functions of the lysine demalonylase activity of SIRT5. Life Sci. 2023;320:121572. https:\/\/doi.org\/10.1016\/j.lfs.2023.121572.","journal-title":"Life Sci"},{"key":"2021_CR68","doi-asserted-by":"publisher","first-page":"2308","DOI":"10.1074\/mcp.R114.046664","volume":"14","author":"MD Hirschey","year":"2015","unstructured":"Hirschey MD, Zhao Y. Metabolic regulation by lysine malonylation, succinylation, and glutarylation. Molecular & Cellular Proteomics. 2015;14:2308\u201315. https:\/\/doi.org\/10.1074\/mcp.R114.046664.","journal-title":"Molecular & Cellular Proteomics"},{"key":"2021_CR69","doi-asserted-by":"publisher","DOI":"10.1016\/j.isci.2023.106193","author":"R Zhang","year":"2023","unstructured":"Zhang R, Bons J, Scheidemantle G, Liu X, Bielska O, Carrico C, et al. Histone malonylation is regulated by SIRT5 and KAT2A. iScience. 2023. https:\/\/doi.org\/10.1016\/j.isci.2023.106193.","journal-title":"iScience"},{"key":"2021_CR70","doi-asserted-by":"publisher","first-page":"6121","DOI":"10.1038\/s41467-022-33903-8","volume":"13","author":"H-L Wang","year":"2022","unstructured":"Wang H-L, Chen Y, Wang Y-Q, Tao E-W, Tan J, Liu Q-Q, et al. Sirtuin5 protects colorectal cancer from DNA damage by keeping nucleotide availability. Nat Commun. 2022;13:6121. https:\/\/doi.org\/10.1038\/s41467-022-33903-8.","journal-title":"Nat Commun"},{"key":"2021_CR71","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2024.116481","volume":"174","author":"M Chen","year":"2024","unstructured":"Chen M, Tan J, Jin Z, Jiang T, Wu J, Yu X. Research progress on sirtuins (SIRTs) family modulators. Biomed Pharmacother. 2024;174:116481.","journal-title":"Biomed Pharmacother"},{"key":"2021_CR72","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1007\/s11418-024-01871-6","volume":"79","author":"Y Xie","year":"2025","unstructured":"Xie Y, Cai N, Liu X, He L, Ma Y, Yan C, et al. SIRT5: a potential target for discovering bioactive natural products. J Nat Med. 2025;79:441\u201364. https:\/\/doi.org\/10.1007\/s11418-024-01871-6.","journal-title":"J Nat Med"},{"key":"2021_CR73","doi-asserted-by":"publisher","first-page":"e1340","DOI":"10.1038\/cddis.2014.185","volume":"5","author":"D Guan","year":"2014","unstructured":"Guan D, Lim JH, Peng L, Liu Y, Lam M, Seto E, et al. Deacetylation of the tumor suppressor protein PML regulates hydrogen peroxide-induced cell death. Cell Death Dis. 2014;5:e1340\u2013e1340. https:\/\/doi.org\/10.1038\/cddis.2014.185.","journal-title":"Cell Death Dis"},{"key":"2021_CR74","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1097\/FJC.0b013e3181e74a14","volume":"56","author":"GD Lopaschuk","year":"2010","unstructured":"Lopaschuk GD, Jaswal JS. Energy metabolic phenotype of the cardiomyocyte during development, differentiation, and postnatal maturation. J Cardiovasc Pharmacol. 2010;56:130. https:\/\/doi.org\/10.1097\/FJC.0b013e3181e74a14.","journal-title":"J Cardiovasc Pharmacol"},{"key":"2021_CR75","doi-asserted-by":"publisher","DOI":"10.3389\/fphys.2018.00959","author":"J Piquereau","year":"2018","unstructured":"Piquereau J, Ventura-Clapier R. Maturation of cardiac energy metabolism during perinatal development. Front Physiol. 2018. https:\/\/doi.org\/10.3389\/fphys.2018.00959.","journal-title":"Front Physiol"},{"key":"2021_CR76","doi-asserted-by":"publisher","first-page":"H347","DOI":"10.1152\/ajpheart.00900.2015","volume":"311","author":"A Fukushima","year":"2016","unstructured":"Fukushima A, Alrob OA, Zhang L, Wagg CS, Altamimi T, Rawat S, et al. Acetylation and succinylation contribute to maturational alterations in energy metabolism in the newborn heart. Am J Physiol Heart Circ Physiol. 2016;311:H347\u201363. https:\/\/doi.org\/10.1152\/ajpheart.00900.2015.","journal-title":"Am J Physiol Heart Circ Physiol"},{"key":"2021_CR77","doi-asserted-by":"publisher","first-page":"4320","DOI":"10.1073\/pnas.1519858113","volume":"113","author":"S Sadhukhan","year":"2016","unstructured":"Sadhukhan S, Liu X, Ryu D, Nelson OD, Stupinski JA, Li Z, et al. Metabolomics-assisted proteomics identifies succinylation and SIRT5 as important regulators of cardiac function. Proc Natl Acad Sci U S A. 2016;113:4320\u20135. https:\/\/doi.org\/10.1073\/pnas.1519858113.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2021_CR78","doi-asserted-by":"publisher","DOI":"10.1016\/j.ecoenv.2025.118416","volume":"299","author":"L Tian","year":"2025","unstructured":"Tian L, Sun Q, Lv J, Liu S, Zhang K, Li Y, et al. Multi-omics analysis of gestational PM2.5 exposure induces abnormal cardiac metabolism and development in offspring. Ecotoxicol Environ Saf. 2025;299:118416. https:\/\/doi.org\/10.1016\/j.ecoenv.2025.118416.","journal-title":"Ecotoxicol Environ Saf"},{"key":"2021_CR79","doi-asserted-by":"publisher","first-page":"1050","DOI":"10.1159\/000354505","volume":"32","author":"B Liu","year":"2013","unstructured":"Liu B, Che W, Zheng C, Liu W, Wen J, Fu H, et al. SIRT5: a safeguard against oxidative stress-induced apoptosis in cardiomyocytes. Cell Physiol Biochem. 2013;32:1050\u20139. https:\/\/doi.org\/10.1159\/000354505.","journal-title":"Cell Physiol Biochem"},{"key":"2021_CR80","doi-asserted-by":"publisher","first-page":"811","DOI":"10.15252\/embr.201541643","volume":"17","author":"L Zhou","year":"2016","unstructured":"Zhou L, Wang F, Sun R, Chen X, Zhang M, Xu Q, et al. SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense. EMBO Rep. 2016;17:811\u201322. https:\/\/doi.org\/10.15252\/embr.201541643.","journal-title":"EMBO Rep"},{"key":"2021_CR81","doi-asserted-by":"publisher","first-page":"1037","DOI":"10.1007\/s00421-011-2050-9","volume":"112","author":"W-Z Zhu","year":"2012","unstructured":"Zhu W-Z, Wu X-F, Zhang Y, Zhou Z-N. Proteomic analysis of mitochondrial proteins in cardiomyocytes from rats subjected to intermittent hypoxia. Eur J Appl Physiol. 2012;112:1037\u201346. https:\/\/doi.org\/10.1007\/s00421-011-2050-9.","journal-title":"Eur J Appl Physiol"},{"key":"2021_CR82","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0211796","volume":"14","author":"M Zhang","year":"2019","unstructured":"Zhang M, Wu J, Sun R, Tao X, Wang X, Kang Q, et al. SIRT5 deficiency suppresses mitochondrial ATP production and promotes AMPK activation in response to energy stress. PLoS One. 2019;14:e0211796. https:\/\/doi.org\/10.1371\/journal.pone.0211796.","journal-title":"PLoS One"},{"key":"2021_CR83","doi-asserted-by":"publisher","first-page":"1557","DOI":"10.1016\/j.celrep.2019.01.057","volume":"85","author":"KH Fisher-Wellman","year":"2019","unstructured":"Fisher-Wellman KH, Draper JA, Davidson MT, Williams AS, Narowski TM, Slentz DH, et al. Respiratory phenomics across multiple models of protein hyperacylation in cardiac mitochondria reveals a marginal impact on bioenergetics. Cell Rep. 2019;85:1557-1572.e8. https:\/\/doi.org\/10.1016\/j.celrep.2019.01.057.","journal-title":"Cell Rep"},{"key":"2021_CR84","doi-asserted-by":"publisher","first-page":"C519","DOI":"10.1152\/ajpcell.00156.2021","volume":"86","author":"JN Peoples","year":"2021","unstructured":"Peoples JN, Ghazal N, Duong DM, Hardin KR, Manning JR, Seyfried NT, et al. Loss of the mitochondrial phosphate carrier SLC25A3 induces remodeling of the cardiac mitochondrial protein acylome. Am J Physiol Cell Physiol. 2021;86:C519\u201334. https:\/\/doi.org\/10.1152\/ajpcell.00156.2021.","journal-title":"Am J Physiol Cell Physiol"},{"key":"2021_CR85","doi-asserted-by":"publisher","DOI":"10.3389\/fphys.2013.00347","author":"J Qian","year":"2013","unstructured":"Qian J, Fulton D. Post-translational regulation of endothelial nitric oxide synthase in vascular endothelium. Front Physiol. 2013. https:\/\/doi.org\/10.3389\/fphys.2013.00347.","journal-title":"Front Physiol"},{"key":"2021_CR86","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1016\/j.ebiom.2019.03.031","volume":"42","author":"B-B Yu","year":"2019","unstructured":"Yu B-B, Zhi H, Zhang X-Y, Liang J-W, He J, Su C, et al. Mitochondrial dysfunction-mediated decline in angiogenic capacity of endothelial progenitor cells is associated with capillary rarefaction in patients with hypertension via downregulation of CXCR4\/JAK2\/SIRT5 signaling. EBioMedicine. 2019;42:64\u201375. https:\/\/doi.org\/10.1016\/j.ebiom.2019.03.031.","journal-title":"EBioMedicine"},{"key":"2021_CR87","doi-asserted-by":"publisher","DOI":"10.3390\/ijms26072908","volume":"89","author":"Y Pan","year":"2025","unstructured":"Pan Y, Zhang Q, Li C, Li X, Li S, Wang Y, et al. SIRT5 alleviates apoptosis of vascular endothelial cells under simulated microgravity via desuccinylation of ERO1A. Int J Mol Sci. 2025;89:2908. https:\/\/doi.org\/10.3390\/ijms26072908.","journal-title":"Int J Mol Sci"},{"key":"2021_CR88","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2023.104889","volume":"90","author":"H Zhang","year":"2023","unstructured":"Zhang H, Zhang Y, Wang H, Yang P, Lu C, Liu Y, et al. Global proteomic analysis reveals lysine succinylation contributes to the pathogenesis of aortic aneurysm and dissection. J Proteomics. 2023;90:104889. https:\/\/doi.org\/10.1016\/j.jprot.2023.104889.","journal-title":"J Proteomics"},{"key":"2021_CR89","doi-asserted-by":"publisher","DOI":"10.7717\/peerj.15258","volume":"11","author":"Y Zhang","year":"2023","unstructured":"Zhang Y, Zhang H, Wang H, Wang C, Yang P, Lu C, et al. Tandem mass tag-based quantitative proteomic analysis identification of succinylation related proteins in pathogenesis of thoracic aortic aneurysm and aortic dissection. PeerJ. 2023;11:e15258. https:\/\/doi.org\/10.7717\/peerj.15258.","journal-title":"PeerJ"},{"key":"2021_CR90","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1038\/nature13909","volume":"515","author":"ET Chouchani","year":"2014","unstructured":"Chouchani ET, Pell VR, Gaude E, Aksentijevi\u0107 D, Sundier SY, Robb EL, et al. Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS. Nature. 2014;515:431\u20135. https:\/\/doi.org\/10.1038\/nature13909.","journal-title":"Nature"},{"key":"2021_CR91","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejphar.2019.172520","volume":"858","author":"L Liu","year":"2019","unstructured":"Liu L, Wang Q, Zhao B, Wu Q, Wang P. Exogenous nicotinamide adenine dinucleotide administration alleviates ischemia\/reperfusion-induced oxidative injury in isolated rat hearts via Sirt5-SDH-succinate pathway. Eur J Pharmacol. 2019;858:172520. https:\/\/doi.org\/10.1016\/j.ejphar.2019.172520.","journal-title":"Eur J Pharmacol"},{"key":"2021_CR92","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.yjmcc.2015.09.005","volume":"88","author":"JA Boylston","year":"2015","unstructured":"Boylston JA, Sun J, Chen Y, Gucek M, Sack MN, Murphy E. Characterization of the cardiac succinylome and its role in ischemia\u2013reperfusion injury. J Mol Cell Cardiol. 2015;88:73\u201381. https:\/\/doi.org\/10.1016\/j.yjmcc.2015.09.005.","journal-title":"J Mol Cell Cardiol"},{"key":"2021_CR93","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1016\/j.yjmcc.2019.11.159","volume":"138","author":"HR Ali","year":"2020","unstructured":"Ali HR, Michel CR, Lin YH, McKinsey TA, Jeong MY, Ambardekar AV, et al. Defining decreased protein succinylation of failing human cardiac myofibrils in ischemic cardiomyopathy. J Mol Cell Cardiol. 2020;138:304\u201317.","journal-title":"J Mol Cell Cardiol"},{"key":"2021_CR94","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2021.687559","volume":"9","author":"B Zhou","year":"2021","unstructured":"Zhou B, Xiao M, Hu H, Pei X, Xue Y, Miao G, et al. Cardioprotective role of SIRT5 in response to acute ischemia through a novel liver-cardiac crosstalk mechanism. Front Cell Dev Biol. 2021;9:687559.","journal-title":"Front Cell Dev Biol"},{"issue":"5","key":"2021_CR95","doi-asserted-by":"publisher","DOI":"10.1002\/ctm2.172","volume":"10","author":"T Ou","year":"2020","unstructured":"Ou T, Yang W, Li W, Lu Y, Dong Z, Zhu H, et al. <article-title update=\"added\">SIRT5 deficiency enhances the proliferative and therapeutic capacities of adipose\u2010derived mesenchymal stem cells via metabolic switching. Clin Transl Med. 2020;10(5):e172. https:\/\/doi.org\/10.1002\/ctm2.172.","journal-title":"Clin Transl Med"},{"key":"2021_CR96","doi-asserted-by":"publisher","unstructured":"Li S, Shen S, Hong Y, Ding K, Chen S, Chen J, Wang C, Wen Y, Mo G, Yu L, et al. Sirt5 preserves cardiac function in ischemia-reperfusion injury by inhibiting ANT2 lactylation 2024. https:\/\/doi.org\/10.1101\/2024.11.25.6215148.","DOI":"10.1101\/2024.11.25.6215148"},{"issue":"5","key":"2021_CR97","doi-asserted-by":"publisher","first-page":"2496","DOI":"10.1002\/ptr.8177","volume":"38","author":"X Chang","year":"2024","unstructured":"Chang X, Zhang Q, Huang Y, Liu J, Wang Y, Guan X, et al. <article-title update=\"added\"> Quercetin inhibits necroptosis in cardiomyocytes after ischemia\u2013reperfusion via <scp>DNA\u2010PKcs\u2010SIRT5<\/scp> \u2010orchestrated mitochondrial quality control. Phytother Res. 2024;38(5):2496\u2013517. https:\/\/doi.org\/10.1002\/ptr.8177.","journal-title":"Phytother Res"},{"key":"2021_CR98","doi-asserted-by":"publisher","DOI":"10.1080\/10641963.2023.2271196","volume":"45","author":"Y Wang","year":"2023","unstructured":"Wang Y, Zhou H, Wu J, Ye S. MG53 alleviates hypoxia\/reoxygenation-induced cardiomyocyte injury by succinylation and ubiquitination modification. Clin Exp Hypertens. 2023;45:2271196. https:\/\/doi.org\/10.1080\/10641963.2023.2271196.","journal-title":"Clin Exp Hypertens"},{"key":"2021_CR99","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1093\/cvr\/cvw007","volume":"109","author":"D Opacic","year":"2016","unstructured":"Opacic D, van Bragt KA, Nasrallah HM, Schotten U, Verheule S. Atrial metabolism and tissue perfusion as determinants of electrical and structural remodelling in atrial fibrillation. Cardiovasc Res. 2016;109:527\u201341.","journal-title":"Cardiovasc Res"},{"key":"2021_CR100","doi-asserted-by":"publisher","first-page":"993","DOI":"10.1253\/circj.CJ-13-1365","volume":"78","author":"T Tu","year":"2014","unstructured":"Tu T, Zhou S, Liu Z, Li X, Liu Q. Quantitative proteomics of changes in energy metabolism-related proteins in atrial tissue from valvular disease patients with permanent atrial fibrillation. Circ J. 2014;78:993\u20131001. https:\/\/doi.org\/10.1253\/circj.CJ-13-1365.","journal-title":"Circ J"},{"key":"2021_CR101","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1016\/j.cardfail.2019.08.005","volume":"25","author":"C Ozcan","year":"2019","unstructured":"Ozcan C, Li Z, Kim G, Jeevanandam V, Uriel N. Molecular mechanism of the association between atrial fibrillation and heart failure includes energy metabolic dysregulation due to mitochondrial dysfunction. J Card Fail. 2019;25:911\u201320. https:\/\/doi.org\/10.1016\/j.cardfail.2019.08.005.","journal-title":"J Card Fail"},{"key":"2021_CR102","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1016\/j.cca.2019.05.002","volume":"495","author":"F Bai","year":"2019","unstructured":"Bai F, Tu T, Qin F, Ma Y, Liu N, Liu Y, et al. Quantitative proteomics of changes in succinylated proteins expression profiling in left appendages tissue from valvular heart disease patients with atrial fibrillation. Clin Chim Acta. 2019;495:345\u201354. https:\/\/doi.org\/10.1016\/j.cca.2019.05.002.","journal-title":"Clin Chim Acta"},{"key":"2021_CR103","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2025.103576","volume":"81","author":"Y Zhang","year":"2025","unstructured":"Zhang Y, Gong H, Jin L, Liu P, Fan J, Qin X, et al. Succinate predisposes mice to atrial fibrillation by impairing mitochondrial function via SUCNR1\/AMPK axis. Redox Biol. 2025;81:103576. https:\/\/doi.org\/10.1016\/j.redox.2025.103576.","journal-title":"Redox Biol"},{"issue":"8","key":"2021_CR104","doi-asserted-by":"publisher","first-page":"e802","DOI":"10.1212\/WNL.0000000000006957","volume":"92","author":"SE Nelson","year":"2019","unstructured":"Nelson SE, Ament Z, Wolcott Z, Gerszten RE, Kimberly WT. Succinate links atrial dysfunction and cardioembolic stroke. Neurology. 2019;92(8):e802\u201310. https:\/\/doi.org\/10.1212\/WNL.0000000000006957.","journal-title":"Neurology"},{"issue":"7","key":"2021_CR105","doi-asserted-by":"publisher","first-page":"2891","DOI":"10.7150\/ijbs.107965","volume":"21","author":"C-K Hu","year":"2025","unstructured":"Hu C-K, Huang W-Z, He L, Chang C, Ren Y-L, Dai R-X, et al. De-succinylation-induced accumulation of TRMT10C in the nucleus plays a detrimental role in coronary microembolization via its m1A modification function. Int J Biol Sci. 2025;21(7):2891\u2013920. https:\/\/doi.org\/10.7150\/ijbs.107965.","journal-title":"Int J Biol Sci"},{"issue":"10","key":"2021_CR106","doi-asserted-by":"publisher","first-page":"2275","DOI":"10.1093\/cvr\/cvaa268","volume":"117","author":"L Liberale","year":"2021","unstructured":"Liberale L, Akhmedov A, Vlachogiannis NI, Bonetti NR, Nageswaran V, Miranda MX, et al. Sirtuin 5 promotes arterial thrombosis by blunting the fibrinolytic system. Cardiovasc Res. 2021;117(10):2275\u201388. https:\/\/doi.org\/10.1093\/cvr\/cvaa268.","journal-title":"Cardiovasc Res"},{"key":"2021_CR107","doi-asserted-by":"publisher","DOI":"10.1016\/j.brainres.2025.149613","volume":"1857","author":"L Zhang","year":"2025","unstructured":"Zhang L, Lv T, Hou P, Jin Y, Jia F. Sirt5-mediated polarization and metabolic reprogramming of macrophage sustain brain function following ischemic stroke. Brain Res. 2025;1857:149613. https:\/\/doi.org\/10.1016\/j.brainres.2025.149613.","journal-title":"Brain Res"},{"key":"2021_CR108","doi-asserted-by":"publisher","first-page":"4043","DOI":"10.1161\/STROKEAHA.121.034850","volume":"52","author":"Z-P Xiao","year":"2021","unstructured":"Xiao Z-P, Lv T, Hou P-P, Manaenko A, Liu Y, Jin Y, et al. Sirtuin 5-mediated lysine desuccinylation protects mitochondrial metabolism following subarachnoid hemorrhage in mice. Stroke. 2021;52:4043\u201353. https:\/\/doi.org\/10.1161\/STROKEAHA.121.034850.","journal-title":"Stroke"},{"key":"2021_CR109","doi-asserted-by":"publisher","DOI":"10.1002\/mco2.436","volume":"4","author":"Q Xia","year":"2023","unstructured":"Xia Q, Zhang X, Zhan G, Zheng L, Mao M, Zhao Y, et al. A cell-penetrating peptide exerts therapeutic effects against ischemic stroke by mediating the lysosomal degradation of sirtuin 5. MedComm. 2023;4:e436. https:\/\/doi.org\/10.1002\/mco2.436.","journal-title":"MedComm"},{"issue":"1","key":"2021_CR110","doi-asserted-by":"publisher","DOI":"10.1007\/s11481-024-10117-x","volume":"19","author":"Q Xia","year":"2024","unstructured":"Xia Q, Yu Y, Zhan G, Zhang X, Gao S, Han T, et al. The sirtuin 5 inhibitor MC3482 ameliorates microglia\u2011induced neuroinflammation following ischaemic stroke by upregulating the succinylation level of annexin-A1. J Neuroimmune Pharmacol. 2024;19(1):17. https:\/\/doi.org\/10.1007\/s11481-024-10117-x.","journal-title":"J Neuroimmune Pharmacol"},{"key":"2021_CR111","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1186\/s12974-022-02665-x","volume":"19","author":"Q Xia","year":"2022","unstructured":"Xia Q, Gao S, Han T, Mao M, Zhan G, Wang Y, et al. Sirtuin 5 aggravates microglia-induced neuroinflammation following ischaemic stroke by modulating the desuccinylation of annexin-A1. J Neuroinflammation. 2022;19:301. https:\/\/doi.org\/10.1186\/s12974-022-02665-x.","journal-title":"J Neuroinflammation"},{"key":"2021_CR112","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1016\/j.ijcard.2017.12.060","volume":"260","author":"C Diaz-Ca\u00f1estro","year":"2018","unstructured":"Diaz-Ca\u00f1estro C, Merlini M, Bonetti NR, Liberale L, W\u00fcst P, Briand-Schumacher S, et al. Sirtuin 5 as a novel target to blunt blood\u2013brain barrier damage induced by cerebral ischemia\/reperfusion injury. Int J Cardiol. 2018;260:148\u201355. https:\/\/doi.org\/10.1016\/j.ijcard.2017.12.060.","journal-title":"Int J Cardiol"},{"key":"2021_CR113","doi-asserted-by":"publisher","first-page":"998","DOI":"10.1007\/s11064-023-04095-4","volume":"49","author":"J Li","year":"2024","unstructured":"Li J, Wei G, Song Z, Chen Z, Gu J, Zhang L, et al. SIRT5 regulates ferroptosis through the Nrf2\/HO-1 signaling axis to participate in ischemia-reperfusion injury in ischemic stroke. Neurochem Res. 2024;49:998\u20131007. https:\/\/doi.org\/10.1007\/s11064-023-04095-4.","journal-title":"Neurochem Res"},{"key":"2021_CR114","doi-asserted-by":"publisher","first-page":"165","DOI":"10.31083\/j.rcm2305165","volume":"23","author":"A Caturano","year":"2022","unstructured":"Caturano A, Vetrano E, Galiero R, Salvatore T, Docimo G, Epifani R, et al. Cardiac hypertrophy: from pathophysiological mechanisms to heart failure development. Rev Cardiovasc Med. 2022;23:165.","journal-title":"Rev Cardiovasc Med"},{"key":"2021_CR115","doi-asserted-by":"publisher","unstructured":"Sunagawa Y, Funamoto M, Hamabe-Horiike T, Hieda K, Yabuki S, Tomino M, Ikai Y, Suzuki A, Ogawahara S, Yabuta A, et al. Nobiletin, a polymethoxyflavonoid, activates the desuccinylase activity of SIRT5 and prevents the development of heart failure 2024. https:\/\/doi.org\/10.1101\/2024.01.16.575602.","DOI":"10.1101\/2024.01.16.575602"},{"key":"2021_CR116","doi-asserted-by":"publisher","DOI":"10.1111\/jcmm.18276","volume":"28","author":"N Zhang","year":"2024","unstructured":"Zhang N, Zhou Z-Y, Meng Y-Y, Liao H-H, Mou S-Q, Lin Z, et al. <article-title update=\"added\"><scp>HINT2<\/scp> protects against pressure overload\u2010induced cardiac remodelling through mitochondrial pathways. J Cell Mol Med. 2024;28:e18276. https:\/\/doi.org\/10.1111\/jcmm.18276.","journal-title":"J Cell Mol Med"},{"key":"2021_CR117","doi-asserted-by":"publisher","DOI":"10.22038\/ijbms.2024.80343.17390","author":"L Liang","year":"2024","unstructured":"Liang L, Huang Y, Wang Q, Hong Y, Zhen H, Chen Y. SIRT5 prevents mitochondrial dysfunction and cardiac hypertrophy induced by RIP140. Iran J Basic Med Sci. 2024. https:\/\/doi.org\/10.22038\/ijbms.2024.80343.17390.","journal-title":"Iran J Basic Med Sci"},{"key":"2021_CR118","doi-asserted-by":"publisher","first-page":"10630","DOI":"10.1074\/jbc.RA118.002187","volume":"293","author":"KA Hershberger","year":"2018","unstructured":"Hershberger KA, Abraham DM, Liu J, Locasale JW, Grimsrud PA, Hirschey MD. Ablation of sirtuin5 in the postnatal mouse heart results in protein succinylation and normal survival in response to chronic pressure overload. J Biol Chem. 2018;293:10630\u201345.","journal-title":"J Biol Chem"},{"key":"2021_CR119","doi-asserted-by":"publisher","first-page":"12258","DOI":"10.1038\/s41598-022-16506-7","volume":"12","author":"AH Guo","year":"2022","unstructured":"Guo AH, Baliira R, Skinner ME, Kumar S, Andren A, Zhang L, et al. Sirtuin 5 levels are limiting in preserving cardiac function and suppressing fibrosis in response to pressure overload. Sci Rep. 2022;12:12258. https:\/\/doi.org\/10.1038\/s41598-022-16506-7.","journal-title":"Sci Rep"},{"key":"2021_CR120","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2022.104667","volume":"266","author":"L-F Wu","year":"2022","unstructured":"Wu L-F, Wang D-P, Shen J, Gao L-J, Zhou Y, Liu Q-H, et al. Global profiling of protein lysine malonylation in mouse cardiac hypertrophy. J Proteomics. 2022;266:104667. https:\/\/doi.org\/10.1016\/j.jprot.2022.104667.","journal-title":"J Proteomics"},{"key":"2021_CR121","doi-asserted-by":"publisher","first-page":"812","DOI":"10.1038\/s41569-023-00887-x","volume":"20","author":"J Ritterhoff","year":"2023","unstructured":"Ritterhoff J, Tian R. Metabolic mechanisms in physiological and pathological cardiac hypertrophy: new paradigms and challenges. Nat Rev Cardiol. 2023;20:812\u201329.","journal-title":"Nat Rev Cardiol"},{"key":"2021_CR122","doi-asserted-by":"publisher","first-page":"1598","DOI":"10.1161\/CIRCULATIONAHA.123.065880","volume":"149","author":"X Chen","year":"2024","unstructured":"Chen X, Wu H, Liu Y, Liu L, Houser SR, Wang WE. Metabolic reprogramming: a byproduct or a driver of cardiomyocyte proliferation? Circulation. 2024;149:1598\u2013610. https:\/\/doi.org\/10.1161\/CIRCULATIONAHA.123.065880.","journal-title":"Circulation"},{"issue":"Suppl_1","key":"2021_CR123","doi-asserted-by":"publisher","first-page":"A9328","DOI":"10.1161\/circ.146.suppl_1.9328","volume":"146","author":"M Wu","year":"2022","unstructured":"Wu M, Zhang H, Yuan W, Tan J, Huang Z, Chen Z, et al. Abstract 9328: Sirt5 deficiency promotes metabolic reprogramming to aggravate cardiac fibrosis. Circulation. 2022;146(Suppl_1):A9328\u2013A9328. https:\/\/doi.org\/10.1161\/circ.146.suppl_1.9328.","journal-title":"Circulation"},{"key":"2021_CR124","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1016\/j.gene.2018.07.010","volume":"675","author":"L Chen","year":"2018","unstructured":"Chen L, Wang H, Gao F, Zhang J, Zhang Y, Ma R, et al. Functional genetic variants in the SIRT5 gene promoter in acute myocardial infarction. Gene. 2018;675:233\u20139.","journal-title":"Gene"},{"key":"2021_CR125","doi-asserted-by":"publisher","DOI":"10.1002\/prca.201900103","volume":"14","author":"B Zhou","year":"2020","unstructured":"Zhou B, Du Y, Xue Y, Miao G, Wei T, Zhang P. Identification of malonylation, succinylation, and glutarylation in serum proteins of acute myocardial infarction patients. Proteomics Clin Appl. 2020;14:1900103. https:\/\/doi.org\/10.1002\/prca.201900103.","journal-title":"Proteomics Clin Appl"},{"key":"2021_CR126","doi-asserted-by":"publisher","first-page":"464","DOI":"10.1186\/s12872-024-04120-6","volume":"24","author":"Z Li","year":"2024","unstructured":"Li Z, Zheng Z, Dai X. SIRT5 induces autophagy and alleviates myocardial infarction via desuccinylation of TOM1. BMC Cardiovasc Disord. 2024;24:464. https:\/\/doi.org\/10.1186\/s12872-024-04120-6.","journal-title":"BMC Cardiovasc Disord"},{"key":"2021_CR127","doi-asserted-by":"publisher","first-page":"29240","DOI":"10.1038\/s41598-024-80505-z","volume":"14","author":"Z Zheng","year":"2024","unstructured":"Zheng Z, Liu Y, Chen D, Yang J, Ren L, Jin Z, et al. Catalpol improved energy metabolism and inflammation through the SIRT5-mediated signaling pathway to ameliorate myocardial injury. Sci Rep. 2024;14:29240.","journal-title":"Sci Rep"},{"issue":"3","key":"2021_CR128","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1016\/S1875-5364(25)60838-7","volume":"23","author":"X Chang","year":"2025","unstructured":"Chang X, Zhou S, Huang Y, Liu J, Wang Y, Guan X, et al. Zishen huoxue decoction (ZSHX) alleviates ischemic myocardial injury (MI) via Sirt5-\u03b2-tubulin mediated synergistic mechanism of \u201cmitophagy-unfolded protein response\u201d and mitophagy. Chin J Nat Med. 2025;23(3):311\u201321. https:\/\/doi.org\/10.1016\/S1875-5364(25)60838-7.","journal-title":"Chin J Nat Med"},{"key":"2021_CR129","doi-asserted-by":"publisher","first-page":"5489","DOI":"10.2147\/DDDT.S509337","volume":"19","author":"C Castiello","year":"2025","unstructured":"Castiello C, Efentakis P, Nikolaou P-E, Symeonidi L, Chania C, Barla I, et al. Cardioprotection through pharmacological activation of sirtuin 5 in a murine model of acute myocardial infarction. Drug Des Devel Ther. 2025;19:5489\u2013505. https:\/\/doi.org\/10.2147\/DDDT.S509337.","journal-title":"Drug Des Devel Ther"},{"key":"2021_CR130","doi-asserted-by":"publisher","unstructured":"Sacks D, Baxter B, Campbell BCV, Carpenter JS, Cognard C, Dippel D, Eesa M, Fischer U, Hausegger K, et al.; From the American Association of Neurological Surgeons (AANS), American Society of Neuroradiology (ASNR), Cardiovascular and Interventional Radiology Society of Europe (CIRSE), Canadian Interventional Radiology Association (CIRA), Congress of Neurological Surgeons (CNS), European Society of Minimally Invasive Neurological Therapy (ESMINT), European Society of Neuroradiology (ESNR), European Stroke Organization (ESO), Society for Cardiovascular Angiography and Interventions (SCAI), Society of Interventional Radiology (SIR), Society of NeuroInterventional Surgery (SNIS), and World Stroke Organization (WSO).\u00a0 Multisociety consensus quality improvement revised consensus statement for endovascular therapy of acute ischemic stroke. Int J Stroke. 2018;13:612\u2013632.\u00a0https:\/\/doi.org\/10.1177\/1747493018778713.","DOI":"10.1177\/1747493018778713"},{"key":"2021_CR131","doi-asserted-by":"publisher","first-page":"7768","DOI":"10.1038\/s41598-025-92716-z","volume":"15","author":"L Tang","year":"2025","unstructured":"Tang L, Sun Q, Luo J, Peng S. Metformin hydrochloride improves hepatic glucolipid metabolism in diabetes progression through SIRT5-mediated ECHA desuccinylation. Sci Rep. 2025;15:7768. https:\/\/doi.org\/10.1038\/s41598-025-92716-z.","journal-title":"Sci Rep"},{"key":"2021_CR132","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/j.bbrc.2015.10.126","volume":"468","author":"PK Bagul","year":"2015","unstructured":"Bagul PK, Dinda AK, Banerjee SK. Effect of resveratrol on sirtuins expression and cardiac complications in diabetes. Biochem Biophys Res Commun. 2015;468:221\u20137. https:\/\/doi.org\/10.1016\/j.bbrc.2015.10.126.","journal-title":"Biochem Biophys Res Commun"},{"key":"2021_CR133","doi-asserted-by":"publisher","first-page":"585","DOI":"10.7150\/ijbs.83306","volume":"20","author":"C Wei","year":"2024","unstructured":"Wei C, Shi M, Dong S, Li Z, Zhao B, Liu D, et al. SIRT5-related lysine demalonylation of GSTP1 contributes to cardiomyocyte pyroptosis suppression in diabetic cardiomyopathy. Int J Biol Sci. 2024;20:585\u2013605. https:\/\/doi.org\/10.7150\/ijbs.83306.","journal-title":"Int J Biol Sci"},{"key":"2021_CR134","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2024.103184","volume":"73","author":"M Wu","year":"2024","unstructured":"Wu M, Tan J, Cao Z, Cai Y, Huang Z, Chen Z, et al. Sirt5 improves cardiomyocytes fatty acid metabolism and ameliorates cardiac lipotoxicity in diabetic cardiomyopathy via CPT2 de-succinylation. Redox Biol. 2024;73:103184.","journal-title":"Redox Biol"},{"key":"2021_CR135","doi-asserted-by":"publisher","first-page":"607","DOI":"10.1007\/s10741-012-9340-0","volume":"18","author":"MG Rosca","year":"2013","unstructured":"Rosca MG, Hoppel CL. Mitochondrial dysfunction in heart failure. Heart Fail Rev. 2013;18:607\u201322.","journal-title":"Heart Fail Rev"},{"key":"2021_CR136","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1093\/cvr\/cvq240","volume":"88","author":"MG Rosca","year":"2010","unstructured":"Rosca MG, Hoppel CL. Mitochondria in heart failure. Cardiovasc Res. 2010;88:40\u201350.","journal-title":"Cardiovasc Res"},{"key":"2021_CR137","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1007\/s10741-012-9330-2","volume":"18","author":"J Mar\u00edn-Garc\u00eda","year":"2013","unstructured":"Mar\u00edn-Garc\u00eda J, Akhmedov AT, Moe GW. Mitochondria in heart failure: the emerging role of mitochondrial dynamics. Heart Fail Rev. 2013;18:439\u201356.","journal-title":"Heart Fail Rev"},{"key":"2021_CR138","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2203628119","volume":"119","author":"S Takada","year":"2022","unstructured":"Takada S, Maekawa S, Furihata T, Kakutani N, Setoyama D, Ueda K, et al. Succinyl-CoA-based energy metabolism dysfunction in chronic heart failure. Proc Natl Acad Sci U S A. 2022;119:e2203628119. https:\/\/doi.org\/10.1073\/pnas.2203628119.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2021_CR139","unstructured":"Jeremy Jenkins, PhD | BioRender Available online: https:\/\/app.biorender.com\/profile\/template\/details\/t-67f53c29e8ca693ea663656d-target-identification-in-ai-drug-discovery\/?source=profile&username=jeremyjenkins&tab=templates\u00a0Accessed 19 Oct 2025."},{"key":"2021_CR140","doi-asserted-by":"publisher","DOI":"10.1016\/j.xcrm.2025.102264","author":"L Spray","year":"2025","unstructured":"Spray L, Richardson G, Haendeler J, Altschmied J, Rumampouw V, Wallis SB, et al. Cardiovascular inflammaging: mechanisms, consequences, and therapeutic perspectives. Cell Rep Med. 2025. https:\/\/doi.org\/10.1016\/j.xcrm.2025.102264.","journal-title":"Cell Rep Med"}],"container-title":["GeroScience"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11357-025-02021-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11357-025-02021-w","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11357-025-02021-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T09:39:19Z","timestamp":1773049159000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11357-025-02021-w"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11,19]]},"references-count":140,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2026,4]]}},"alternative-id":["2021"],"URL":"https:\/\/doi.org\/10.1007\/s11357-025-02021-w","relation":{},"ISSN":["2509-2723"],"issn-type":[{"value":"2509-2723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,11,19]]},"assertion":[{"value":"1 August 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 November 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 November 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}