{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T15:50:28Z","timestamp":1786981828805,"version":"build-2736575974"},"reference-count":134,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T00:00:00Z","timestamp":1771200000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T00:00:00Z","timestamp":1771200000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100012550","name":"Nemzeti Kutat\u00e1si, Fejleszt\u00e9si \u00e9s Innovaci\u00f3s Alap","doi-asserted-by":"publisher","award":["TKP2021-NKTA-47"],"award-info":[{"award-number":["TKP2021-NKTA-47"]}],"id":[{"id":"10.13039\/501100012550","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012550","name":"Nemzeti Kutat\u00e1si, Fejleszt\u00e9si \u00e9s Innovaci\u00f3s Alap","doi-asserted-by":"publisher","award":["National Cardiovascular Laboratory Program (RRF-2.3.1-21-2022-00003)"],"award-info":[{"award-number":["National Cardiovascular Laboratory Program (RRF-2.3.1-21-2022-00003)"]}],"id":[{"id":"10.13039\/501100012550","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002332","name":"Semmelweis University","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100002332","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["GeroScience"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Sirtuins (SIRT1\u2013SIRT7) are NAD\u207a-dependent regulators of mitochondrial metabolism, chromatin remodeling, and stress resilience pathways\u2014processes that are central to both aging biology and breast cancer (BC) heterogeneity. We systematically evaluated their prognostic and transcriptional patterns across molecular subtypes of BC. We constructed an integrated BC dataset comprising gene expression and survival data containing tumors from 55 datasets. Prognostic associations with recurrence-free survival (RFS,\n                    <jats:italic>n<\/jats:italic>\n                    \u2009=\u20094384) were evaluated by univariate Cox and Kaplan\u2013Meier analyses using best cutoffs with FDR control, first for individual sirtuins and then for multigene combinations. Differential expression across normal, tumor, and metastatic tissues, as well as pairwise coexpression (Spearman\u2019s\n                    <jats:italic>\u03c1<\/jats:italic>\n                    ), was assessed using the TNMplot platform. Among individual genes, SIRT3 showed the most consistent association with improved RFS across PAM50 subtypes. Multigene signatures outperformed individual sirtuins and displayed clear subtype specificity. A three-gene panel (SIRT3+SIRT5+SIRT6) stratified risk in Luminal A (\n                    <jats:italic>p<\/jats:italic>\n                    \u2009=\u20098.1e-7), Luminal B (\n                    <jats:italic>p<\/jats:italic>\n                    \u2009=\u20096.6e-6), HER2-enriched (\n                    <jats:italic>p<\/jats:italic>\n                    \u2009=\u20091.0e-4), and Basal-like BC (\n                    <jats:italic>p<\/jats:italic>\n                    \u2009=\u20093.8e-5). In Basal-like tumors, the combination of SIRT3, SIRT6, and SIRT7 achieved the best performance (\n                    <jats:italic>p<\/jats:italic>\n                    \u2009=\u20092.6e-7). Top-performing panels were not simple aggregates of individually significant genes, indicating synergistic, context-dependent effects. Expression analyses revealed concordant downregulation of SIRT3 and SIRT5 in tumors, accompanied by consistent upregulation of SIRT7. Coexpression analysis revealed disease-specific rewiring: tumors exhibited a reinforced axis linking SIRT3\/SIRT5\/SIRT6\/SIRT2, and attenuation of SIRT1 and SIRT4 coupling. Distinct integrated sirtuin scores thus capture subtype-specific metabolic\/epigenetic states and provide robust RFS stratification across BC subtypes. These findings highlight sirtuins as integrators of longevity pathways and tumor metabolism, suggesting therapeutically exploitable vulnerabilities along NAD\u207a-dependent regulatory axes.\n                  <\/jats:p>","DOI":"10.1007\/s11357-026-02143-9","type":"journal-article","created":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T01:26:05Z","timestamp":1771205165000},"page":"3315-3334","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Subtype-specific sirtuin expression signatures link mitochondrial\u2013epigenetic networks to breast cancer survival"],"prefix":"10.1007","volume":"48","author":[{"given":"Zoltan","family":"Ungvari","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ot\u00edlia","family":"Menyh\u00e1rt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alberto","family":"Ocana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4285-7518","authenticated-orcid":false,"given":"Andrea","family":"Lehoczki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monika","family":"Fekete","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giampaolo","family":"Bianchini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bal\u00e1zs","family":"Gy\u0151rffy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,2,16]]},"reference":[{"key":"2143_CR1","doi-asserted-by":"publisher","DOI":"10.1038\/s41591-025-03502-3","author":"J Kim","year":"2025","unstructured":"Kim J, Harper A, McCormack V, Sung H, Houssami N, Morgan E, et al. Global patterns and trends in breast cancer incidence and mortality across 185 countries. Nat Med. 2025. https:\/\/doi.org\/10.1038\/s41591-025-03502-3.","journal-title":"Nat Med"},{"key":"2143_CR2","doi-asserted-by":"publisher","first-page":"7","DOI":"10.3322\/caac.21708","volume":"72","author":"RL Siegel","year":"2022","unstructured":"Siegel RL, Miller KD, Fuchs HE, Jemal A. Cancer statistics, 2022. CA Cancer J Clin. 2022;72:7\u201333. https:\/\/doi.org\/10.3322\/caac.21708.","journal-title":"CA Cancer J Clin"},{"key":"2143_CR3","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/j.breast.2022.08.010","volume":"66","author":"M Arnold","year":"2022","unstructured":"Arnold M, Morgan E, Rumgay H, Mafra A, Singh D, Laversanne M, et al. Current and future burden of breast cancer: global statistics for 2020 and 2040. Breast. 2022;66:15\u201323. https:\/\/doi.org\/10.1016\/j.breast.2022.08.010.","journal-title":"Breast"},{"key":"2143_CR4","doi-asserted-by":"publisher","first-page":"1051","DOI":"10.1093\/jnci\/djz020","volume":"111","author":"JK Kresovich","year":"2019","unstructured":"Kresovich JK, Xu Z, O\u2019Brien KM, Weinberg CR, Sandler DP, Taylor JA. Methylation-based biological age and breast cancer risk. J Natl Cancer Inst. 2019;111:1051\u20138. https:\/\/doi.org\/10.1093\/jnci\/djz020.","journal-title":"J Natl Cancer Inst"},{"key":"2143_CR5","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/j.freeradbiomed.2018.03.012","volume":"120","author":"MDM Saez-Freire","year":"2018","unstructured":"Saez-Freire MDM, Blanco-Gomez A, Castillo-Lluva S, Gomez-Vecino A, Galvis-Jimenez JM, Martin-Seisdedos C, et al. The biological age linked to oxidative stress modifies breast cancer aggressiveness. Free Radic Biol Med. 2018;120:133\u201346. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2018.03.012.","journal-title":"Free Radic Biol Med"},{"key":"2143_CR6","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1016\/j.cmet.2022.11.001","volume":"35","author":"C Lopez-Otin","year":"2023","unstructured":"Lopez-Otin C, Pietrocola F, Roiz-Valle D, Galluzzi L, Kroemer G. Meta-hallmarks of aging and cancer. Cell Metab. 2023;35:12\u201335. https:\/\/doi.org\/10.1016\/j.cmet.2022.11.001.","journal-title":"Cell Metab"},{"key":"2143_CR7","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbadis.2025.167691","volume":"1871","author":"JS Tharayil","year":"2025","unstructured":"Tharayil JS, Kandettu A, Chakrabarty S. The curious case of mitochondrial sirtuin in rewiring breast cancer metabolism: mr hyde or Dr Jekyll? Biochim Biophys Acta Mol Basis Dis. 2025;1871:167691. https:\/\/doi.org\/10.1016\/j.bbadis.2025.167691.","journal-title":"Biochim Biophys Acta Mol Basis Dis"},{"key":"2143_CR8","doi-asserted-by":"publisher","DOI":"10.1016\/j.bcp.2025.116743","volume":"232","author":"D Sharma","year":"2025","unstructured":"Sharma D, Panchaksaram M, Muniyan R. Advancements in understanding the role and mechanism of sirtuin family (SIRT1-7) in breast cancer management. Biochem Pharmacol. 2025;232:116743. https:\/\/doi.org\/10.1016\/j.bcp.2025.116743.","journal-title":"Biochem Pharmacol"},{"key":"2143_CR9","doi-asserted-by":"publisher","first-page":"9825","DOI":"10.1080\/07391102.2023.2252898","volume":"42","author":"A Ullah","year":"2024","unstructured":"Ullah A, Waqas M, Halim SA, Daud M, Jan A, Khan A, et al. Sirtuin 1 inhibition: a promising avenue to suppress cancer progression through small inhibitors design. J Biomol Struct Dyn. 2024;42:9825\u201341. https:\/\/doi.org\/10.1080\/07391102.2023.2252898.","journal-title":"J Biomol Struct Dyn"},{"key":"2143_CR10","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1016\/j.molimm.2023.04.011","volume":"158","author":"F Xiao","year":"2023","unstructured":"Xiao F, Hu B, Si Z, Yang H, Xie J. Sirtuin 6 is a negative regulator of the anti-tumor function of natural killer cells in murine inflammatory colorectal cancer. Mol Immunol. 2023;158:68\u201378. https:\/\/doi.org\/10.1016\/j.molimm.2023.04.011.","journal-title":"Mol Immunol"},{"key":"2143_CR11","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1007\/978-3-031-07634-3_10","volume":"100","author":"S Raghu","year":"2022","unstructured":"Raghu S, Prabhashankar AB, Shivanaiah B, Tripathi E, Sundaresan NR. Sirtuin 6 is a critical epigenetic regulator of cancer. Subcell Biochem. 2022;100:337\u201360. https:\/\/doi.org\/10.1007\/978-3-031-07634-3_10.","journal-title":"Subcell Biochem"},{"key":"2143_CR12","doi-asserted-by":"publisher","DOI":"10.1155\/2022\/5498743","volume":"2022","author":"L Mao","year":"2022","unstructured":"Mao L, Hong X, Xu L, Wang X, Liu J, Wang H, et al. Sirtuin 4 inhibits prostate cancer progression and metastasis by modulating p21 nuclear translocation and glutamate dehydrogenase 1 ADP-ribosylation. J Oncol. 2022;2022:5498743. https:\/\/doi.org\/10.1155\/2022\/5498743.","journal-title":"J Oncol"},{"key":"2143_CR13","doi-asserted-by":"publisher","first-page":"C398","DOI":"10.1152\/ajpcell.00112.2019","volume":"317","author":"M Torrens-Mas","year":"2019","unstructured":"Torrens-Mas M, Hernandez-Lopez R, Pons DG, Roca P, Oliver J, Sastre-Serra J. Sirtuin 3 silencing impairs mitochondrial biogenesis and metabolism in colon cancer cells. Am J Physiol Cell Physiol. 2019;317:C398\u2013404. https:\/\/doi.org\/10.1152\/ajpcell.00112.2019.","journal-title":"Am J Physiol Cell Physiol"},{"key":"2143_CR14","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1016\/j.devcel.2019.03.011","volume":"49","author":"A Latifkar","year":"2019","unstructured":"Latifkar A, Ling L, Hingorani A, Johansen E, Clement A, Zhang X, et al. Loss of sirtuin 1 alters the secretome of breast cancer cells by impairing lysosomal integrity. Dev Cell. 2019;49:393-408 e397. https:\/\/doi.org\/10.1016\/j.devcel.2019.03.011.","journal-title":"Dev Cell"},{"key":"2143_CR15","doi-asserted-by":"publisher","DOI":"10.1038\/npjamd.2016.17","volume":"2","author":"SI Imai","year":"2016","unstructured":"Imai SI, Guarente L. It takes two to tango: NAD(+) and sirtuins in aging\/longevity control. NPJ Aging Mech Dis. 2016;2:16017. https:\/\/doi.org\/10.1038\/npjamd.2016.17.","journal-title":"NPJ Aging Mech Dis"},{"key":"2143_CR16","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1038\/nrm.2016.93","volume":"17","author":"MS Bonkowski","year":"2016","unstructured":"Bonkowski MS, Sinclair DA. Slowing ageing by design: the rise of NAD(+) and sirtuin-activating compounds. Nat Rev Mol Cell Biol. 2016;17:679\u201390. https:\/\/doi.org\/10.1038\/nrm.2016.93.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2143_CR17","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms5211","volume":"5","author":"A Satoh","year":"2014","unstructured":"Satoh A, Imai S. Systemic regulation of mammalian ageing and longevity by brain sirtuins. Nat Commun. 2014;5:4211. https:\/\/doi.org\/10.1038\/ncomms5211.","journal-title":"Nat Commun"},{"key":"2143_CR18","doi-asserted-by":"publisher","first-page":"464","DOI":"10.1016\/j.tcb.2014.04.002","volume":"24","author":"S Imai","year":"2014","unstructured":"Imai S, Guarente L. NAD+ and sirtuins in aging and disease. Trends Cell Biol. 2014;24:464\u201371. https:\/\/doi.org\/10.1016\/j.tcb.2014.04.002.","journal-title":"Trends Cell Biol"},{"key":"2143_CR19","doi-asserted-by":"publisher","first-page":"77","DOI":"10.7555\/JBR.36.20220078","volume":"37","author":"H Li","year":"2022","unstructured":"Li H, Cai Z. SIRT3 regulates mitochondrial biogenesis in aging-related diseases. J Biomed Res. 2022;37:77\u201388. https:\/\/doi.org\/10.7555\/JBR.36.20220078.","journal-title":"J Biomed Res"},{"key":"2143_CR20","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.mad.2016.02.003","volume":"155","author":"Y Yuan","year":"2016","unstructured":"Yuan Y, Cruzat VF, Newsholme P, Cheng J, Chen Y, Lu Y. Regulation of SIRT1 in aging: roles in mitochondrial function and biogenesis. Mech Ageing Dev. 2016;155:10\u201321. https:\/\/doi.org\/10.1016\/j.mad.2016.02.003.","journal-title":"Mech Ageing Dev"},{"key":"2143_CR21","doi-asserted-by":"publisher","first-page":"13628","DOI":"10.18632\/aging.205394","volume":"15","author":"ME Copp","year":"2023","unstructured":"Copp ME, Shine J, Brown HL, Nimmala KR, Hansen OB, Chubinskaya S, et al. Sirtuin 6 activation rescues the age-related decline in DNA damage repair in primary human chondrocytes. Aging Albany NY. 2023;15:13628\u201345. https:\/\/doi.org\/10.18632\/aging.205394.","journal-title":"Aging Albany NY"},{"key":"2143_CR22","doi-asserted-by":"publisher","first-page":"1438","DOI":"10.15252\/embj.201386907","volume":"33","author":"BJ North","year":"2014","unstructured":"North BJ, Rosenberg MA, Jeganathan KB, Hafner AV, Michan S, Dai J, et al. SIRT2 induces the checkpoint kinase BubR1 to increase lifespan. EMBO J. 2014;33:1438\u201353. https:\/\/doi.org\/10.15252\/embj.201386907.","journal-title":"EMBO J"},{"key":"2143_CR23","doi-asserted-by":"publisher","first-page":"164","DOI":"10.4093\/dmj.2022.0270","volume":"47","author":"EJ Bae","year":"2023","unstructured":"Bae EJ, Park BH. Multiple roles of sirtuin 6 in adipose tissue inflammation. Diabetes Metab J. 2023;47:164\u201372. https:\/\/doi.org\/10.4093\/dmj.2022.0270.","journal-title":"Diabetes Metab J"},{"key":"2143_CR24","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1016\/j.brainresbull.2022.04.012","volume":"185","author":"X Chen","year":"2022","unstructured":"Chen X, Wei G, Li D, Fan Y, Zeng Y, Qian Z, et al. Sirtuin 1 alleviates microglia-induced inflammation by modulating the PGC-1\u03b1\/Nrf2 pathway after traumatic brain injury in male rats. Brain Res Bull. 2022;185:28\u201338. https:\/\/doi.org\/10.1016\/j.brainresbull.2022.04.012.","journal-title":"Brain Res Bull"},{"key":"2143_CR25","doi-asserted-by":"publisher","DOI":"10.3390\/antiox11040706","author":"X Cao","year":"2022","unstructured":"Cao X, Wu Y, Hong H, Tian XY. Sirtuin 3 dependent and independent effects of NAD(+) to suppress vascular inflammation and improve endothelial function in mice. Antioxidants. 2022. https:\/\/doi.org\/10.3390\/antiox11040706.","journal-title":"Antioxidants"},{"key":"2143_CR26","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1053\/j.gastro.2017.05.022","volume":"153","author":"AS Wellman","year":"2017","unstructured":"Wellman AS, Metukuri MR, Kazgan N, Xu X, Xu Q, Ren NSX, et al. Intestinal epithelial Sirtuin 1 regulates intestinal inflammation during aging in mice by altering the intestinal microbiota. Gastroenterology. 2017;153:772\u201386. https:\/\/doi.org\/10.1053\/j.gastro.2017.05.022.","journal-title":"Gastroenterology"},{"key":"2143_CR27","doi-asserted-by":"publisher","first-page":"7266","DOI":"10.3168\/jds.2023-23366","volume":"106","author":"L Liu","year":"2023","unstructured":"Liu L, Lu O, Li D, Tian Y, Liu Z, Wen Y, et al. Sirtuin 3 mitigates oxidative-stress-induced apoptosis in bovine mammary epithelial cells. J Dairy Sci. 2023;106:7266\u201380. https:\/\/doi.org\/10.3168\/jds.2023-23366.","journal-title":"J Dairy Sci"},{"key":"2143_CR28","doi-asserted-by":"publisher","first-page":"807","DOI":"10.1523\/JNEUROSCI.2939-14.2015","volume":"35","author":"SH Cho","year":"2015","unstructured":"Cho SH, Chen JA, Sayed F, Ward ME, Gao F, Nguyen TA, et al. SIRT1 deficiency in microglia contributes to cognitive decline in aging and neurodegeneration via epigenetic regulation of IL-1\u03b2. J Neurosci. 2015;35:807\u201318. https:\/\/doi.org\/10.1523\/JNEUROSCI.2939-14.2015.","journal-title":"J Neurosci"},{"key":"2143_CR29","unstructured":"\/2\/807 [pii]"},{"key":"2143_CR30","doi-asserted-by":"publisher","first-page":"3169","DOI":"10.1038\/sj.emboj.7601758","volume":"26","author":"D Kim","year":"2007","unstructured":"Kim D, Nguyen MD, Dobbin MM, Fischer A, Sananbenesi F, Rodgers JT, et al. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer\u2019s disease and amyotrophic lateral sclerosis. EMBO J. 2007;26:3169\u201379.","journal-title":"EMBO J"},{"key":"2143_CR31","doi-asserted-by":"publisher","first-page":"746","DOI":"10.1038\/cr.2013.70","volume":"23","author":"AZ Herskovits","year":"2013","unstructured":"Herskovits AZ, Guarente L. Sirtuin deacetylases in neurodegenerative diseases of aging. Cell Res. 2013;23:746\u201358. https:\/\/doi.org\/10.1038\/cr.2013.70.","journal-title":"Cell Res"},{"key":"2143_CR32","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1016\/j.yjmcc.2007.08.008","volume":"43","author":"H Ota","year":"2007","unstructured":"Ota H, Akishita M, Eto M, Iijima K, Kaneki M, Ouchi Y. Sirt1 modulates premature senescence-like phenotype in human endothelial cells. J Mol Cell Cardiol. 2007;43:571\u20139. https:\/\/doi.org\/10.1016\/j.yjmcc.2007.08.008.","journal-title":"J Mol Cell Cardiol"},{"key":"2143_CR33","doi-asserted-by":"publisher","first-page":"711","DOI":"10.1089\/ars.2017.7178","volume":"28","author":"N D'Onofrio","year":"2018","unstructured":"D\u2019Onofrio N, Servillo L, Balestrieri ML. SIRT1 and SIRT6 signaling pathways in cardiovascular disease protection. Antioxid Redox Signal. 2018;28:711\u201332. https:\/\/doi.org\/10.1089\/ars.2017.7178.","journal-title":"Antioxid Redox Signal"},{"key":"2143_CR34","doi-asserted-by":"publisher","first-page":"1512","DOI":"10.1161\/01.RES.0000267723.65696.4a","volume":"100","author":"RR Alcendor","year":"2007","unstructured":"Alcendor RR, Gao S, Zhai P, Zablocki D, Holle E, Yu X, et al. Sirt1 regulates aging and resistance to oxidative stress in the heart. Circ Res. 2007;100:1512\u201321.","journal-title":"Circ Res"},{"key":"2143_CR35","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1007\/s12975-013-0277-y","volume":"4","author":"V Petegnief","year":"2013","unstructured":"Petegnief V, Planas AM. SIRT1 regulation modulates stroke outcome. Transl Stroke Res. 2013;4:663\u201371. https:\/\/doi.org\/10.1007\/s12975-013-0277-y.","journal-title":"Transl Stroke Res"},{"key":"2143_CR36","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1111\/acel.12538","volume":"16","author":"A Ansari","year":"2017","unstructured":"Ansari A, Rahman MS, Saha SK, Saikot FK, Deep A, Kim KH. Function of the SIRT3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease. Aging Cell. 2017;16:4\u201316. https:\/\/doi.org\/10.1111\/acel.12538.","journal-title":"Aging Cell"},{"key":"2143_CR37","doi-asserted-by":"publisher","first-page":"677","DOI":"10.1089\/ars.2017.7264","volume":"28","author":"LR Bringman-Rodenbarger","year":"2018","unstructured":"Bringman-Rodenbarger LR, Guo AH, Lyssiotis CA, Lombard DB. Emerging roles for SIRT5 in metabolism and cancer. Antioxid Redox Signal. 2018;28:677\u201390. https:\/\/doi.org\/10.1089\/ars.2017.7264.","journal-title":"Antioxid Redox Signal"},{"key":"2143_CR38","doi-asserted-by":"publisher","DOI":"10.3390\/nu8030145","volume":"8","author":"C Buhrmann","year":"2016","unstructured":"Buhrmann C, Shayan P, Popper B, Goel A, Shakibaei M. Sirt1 is required for resveratrol-mediated chemopreventive effects in colorectal cancer cells. Nutrients. 2016;8:145. https:\/\/doi.org\/10.3390\/nu8030145.","journal-title":"Nutrients"},{"key":"2143_CR39","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1007\/s00394-022-02989-7","volume":"62","author":"L Chen","year":"2023","unstructured":"Chen L, Li M, Zhou H, Liu Y, Pang W, Ma T, et al. Sirtuin1 (SIRT1) is involved in the anticancer effect of black raspberry anthocyanins in colorectal cancer. Eur J Nutr. 2023;62:395\u2013406. https:\/\/doi.org\/10.1007\/s00394-022-02989-7.","journal-title":"Eur J Nutr"},{"key":"2143_CR40","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0002020","volume":"3","author":"R Firestein","year":"2008","unstructured":"Firestein R, Blander G, Michan S, Oberdoerffer P, Ogino S, Campbell J, et al. The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS One. 2008;3:e2020.","journal-title":"PLoS One"},{"key":"2143_CR41","doi-asserted-by":"crossref","unstructured":"Mostoslavsky R. DNA repair, insulin signaling and sirtuins: at the crossroads between cancer and aging. Front Biosci. 2008;13:6966\u201390.3203[pii].","DOI":"10.2741\/3203"},{"key":"2143_CR42","doi-asserted-by":"publisher","first-page":"2061","DOI":"10.1159\/000366401","volume":"34","author":"S He","year":"2014","unstructured":"He S, He C, Yuan H, Xiong S, Xiao Z, Chen L. The SIRT 3 expression profile is associated with pathological and clinical outcomes in human breast cancer patients. Cell Physiol Biochem. 2014;34:2061\u20139. https:\/\/doi.org\/10.1159\/000366401.","journal-title":"Cell Physiol Biochem"},{"key":"2143_CR43","doi-asserted-by":"publisher","DOI":"10.3390\/cells9020427","author":"A Kaiser","year":"2020","unstructured":"Kaiser A, Kruger T, Eiselt G, Bechler J, Kniemeyer O, Huber O, et al. Identification of PARP-1, histone H1 and SIRT-1 as new regulators of breast cancer-related aromatase promoter I.3\/II. Cells. 2020. https:\/\/doi.org\/10.3390\/cells9020427.","journal-title":"Cells"},{"key":"2143_CR44","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1089\/jir.2023.0216","volume":"44","author":"M Khalil","year":"2024","unstructured":"Khalil M, Desouky EM, Khaliefa AK, Hozyen WG, Mohamed SS, Hasona NA. Insights into the crosstalk between miR-200a\/lncRNA H-19 and IL-6\/SIRT-1 axis in breast cancer. J Interferon Cytokine Res. 2024;44:191\u20137. https:\/\/doi.org\/10.1089\/jir.2023.0216.","journal-title":"J Interferon Cytokine Res"},{"key":"2143_CR45","doi-asserted-by":"publisher","first-page":"3784","DOI":"10.4161\/cc.8.22.10055","volume":"8","author":"JE Kim","year":"2009","unstructured":"Kim JE, Lou Z, Chen J. Interactions between DBC1 and SIRT 1 are deregulated in breast cancer cells. Cell Cycle. 2009;8:3784\u20135. https:\/\/doi.org\/10.4161\/cc.8.22.10055.","journal-title":"Cell Cycle"},{"key":"2143_CR46","doi-asserted-by":"publisher","first-page":"1486","DOI":"10.1080\/15384047.2015.1071731","volume":"16","author":"P Sarma","year":"2015","unstructured":"Sarma P, Bag I, Ramaiah MJ, Kamal A, Bhadra U, Pal Bhadra M. Bisindole-PBD regulates breast cancer cell proliferation via SIRT-p53 axis. Cancer Biol Ther. 2015;16:1486\u2013501. https:\/\/doi.org\/10.1080\/15384047.2015.1071731.","journal-title":"Cancer Biol Ther"},{"key":"2143_CR47","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1016\/j.tips.2023.12.005","volume":"45","author":"J Zhang","year":"2024","unstructured":"Zhang J, Ye J, Zhu S, Han B, Liu B. Context-dependent role of SIRT3 in cancer. Trends Pharmacol Sci. 2024;45:173\u201390. https:\/\/doi.org\/10.1016\/j.tips.2023.12.005.","journal-title":"Trends Pharmacol Sci"},{"key":"2143_CR48","doi-asserted-by":"publisher","first-page":"1025","DOI":"10.1038\/ncb1468","volume":"8","author":"C Wang","year":"2006","unstructured":"Wang C, Chen L, Hou X, Li Z, Kabra N, Ma Y, et al. Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat Cell Biol. 2006;8:1025\u201331.","journal-title":"Nat Cell Biol"},{"key":"2143_CR49","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1038\/emm.2007.2","volume":"39","author":"J Jeong","year":"2007","unstructured":"Jeong J, Juhn K, Lee H, Kim SH, Min BH, Lee KM, et al. SIRT1 promotes DNA repair activity and deacetylation of Ku70. Exp Mol Med. 2007;39:8\u201313. https:\/\/doi.org\/10.1038\/emm.2007.2.","journal-title":"Exp Mol Med"},{"key":"2143_CR50","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/j.molcel.2010.07.006","volume":"39","author":"W Fan","year":"2010","unstructured":"Fan W, Luo J. SIRT1 regulates UV-induced DNA repair through deacetylating XPA. Mol Cell. 2010;39:247\u201358. https:\/\/doi.org\/10.1016\/j.molcel.2010.07.006.","journal-title":"Mol Cell"},{"key":"2143_CR51","doi-asserted-by":"publisher","first-page":"2935","DOI":"10.3892\/or.2015.4287","volume":"34","author":"L Li","year":"2015","unstructured":"Li L, Ye S, Yang M, Yu W, Fan Z, Zhang H, et al. SIRT1 downregulation enhances chemosensitivity and survival of adult T-cell leukemia-lymphoma cells by reducing DNA double-strand repair. Oncol Rep. 2015;34:2935\u201342. https:\/\/doi.org\/10.3892\/or.2015.4287.","journal-title":"Oncol Rep"},{"key":"2143_CR52","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1042\/BJ20130670","volume":"456","author":"A Madabushi","year":"2013","unstructured":"Madabushi A, Hwang BJ, Jin J, Lu AL. Histone deacetylase SIRT1 modulates and deacetylates DNA base excision repair enzyme thymine DNA glycosylase. Biochem J. 2013;456:89\u201398. https:\/\/doi.org\/10.1042\/BJ20130670.","journal-title":"Biochem J"},{"key":"2143_CR53","doi-asserted-by":"publisher","first-page":"15428","DOI":"10.1021\/acs.jmedchem.4c01053","volume":"67","author":"S Jana","year":"2024","unstructured":"Jana S, Shang J, Hong JY, Fenwick MK, Puri R, Lu X, et al. A mitochondria-targeting SIRT3 inhibitor with activity against diffuse large B cell lymphoma. J Med Chem. 2024;67:15428\u201337. https:\/\/doi.org\/10.1021\/acs.jmedchem.4c01053.","journal-title":"J Med Chem"},{"key":"2143_CR54","doi-asserted-by":"publisher","DOI":"10.1111\/1440-1681.13856","volume":"51","author":"T Li","year":"2024","unstructured":"Li T, Fan L, Jia Y, Xu C, Guo W, Wang Y, et al. Colorectal cancer cells with stably expressed SIRT3 demonstrate proliferating retardation by Wnt\/beta-catenin cascade inactivation. Clin Exp Pharmacol Physiol. 2024;51:e13856. https:\/\/doi.org\/10.1111\/1440-1681.13856.","journal-title":"Clin Exp Pharmacol Physiol"},{"key":"2143_CR55","doi-asserted-by":"publisher","first-page":"137","DOI":"10.2147\/CMAR.S445248","volume":"16","author":"L Ning","year":"2024","unstructured":"Ning L, Xie N. SIRT3 expression predicts overall survival and neoadjuvant chemosensitivity in Triple-Negative Breast Cancer. Cancer Manag Res. 2024;16:137\u201350. https:\/\/doi.org\/10.2147\/CMAR.S445248.","journal-title":"Cancer Manag Res"},{"key":"2143_CR56","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1002\/aac2.12035","volume":"2","author":"EC Jenkins","year":"2021","unstructured":"Jenkins EC, Chattopadhyay M, Germain D. Are the estrogen receptor and SIRT3 axes of the mitochondrial UPR key regulators of breast cancer sub-type determination according to age? Aging Cancer. 2021;2:75\u201381. https:\/\/doi.org\/10.1002\/aac2.12035.","journal-title":"Aging Cancer"},{"key":"2143_CR57","doi-asserted-by":"publisher","first-page":"1433","DOI":"10.1007\/s13258-021-01145-5","volume":"43","author":"H Chen","year":"2021","unstructured":"Chen H, Zhang DM, Zhang ZP, Li MZ, Wu HF. SIRT3-mediated mitochondrial unfolded protein response weakens breast cancer sensitivity to cisplatin. Genes & Genomics. 2021;43:1433\u201344. https:\/\/doi.org\/10.1007\/s13258-021-01145-5.","journal-title":"Genes & Genomics"},{"key":"2143_CR58","doi-asserted-by":"publisher","DOI":"10.1016\/j.gene.2020.144629","volume":"745","author":"R Guo","year":"2020","unstructured":"Guo R, Li Y, Xue Y, Chen Y, Li J, Deng X, et al. SIRT3 increases cisplatin sensitivity of small-cell lung cancer through apoptosis. Gene. 2020;745:144629. https:\/\/doi.org\/10.1016\/j.gene.2020.144629.","journal-title":"Gene"},{"key":"2143_CR59","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1158\/0008-5472.CAN-20-1708","volume":"81","author":"A Sawant Dessai","year":"2021","unstructured":"Sawant Dessai A, Dominguez MP, Chen UI, Hasper J, Prechtl C, Yu C, et al. Transcriptional repression of SIRT3 potentiates mitochondrial aconitase activation to drive aggressive prostate cancer to the bone. Cancer Res. 2021;81:50\u201363. https:\/\/doi.org\/10.1158\/0008-5472.CAN-20-1708.","journal-title":"Cancer Res"},{"key":"2143_CR60","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2023.115326","volume":"166","author":"E Abbotto","year":"2023","unstructured":"Abbotto E, Miro C, Piacente F, Salis A, Murolo M, Nappi A, et al. SIRT6 pharmacological inhibition delays skin cancer progression in the squamous cell carcinoma. Biomed Pharmacother. 2023;166:115326. https:\/\/doi.org\/10.1016\/j.biopha.2023.115326.","journal-title":"Biomed Pharmacother"},{"key":"2143_CR61","doi-asserted-by":"publisher","first-page":"1657","DOI":"10.1002\/2211-5463.13452","volume":"12","author":"S Bandopadhyay","year":"2022","unstructured":"Bandopadhyay S, Prasad P, Ray U, Das Ghosh D, Roy SS. SIRT6 promotes mitochondrial fission and subsequent cellular invasion in ovarian cancer. FEBS Open Bio. 2022;12:1657\u201376. https:\/\/doi.org\/10.1002\/2211-5463.13452.","journal-title":"FEBS Open Bio"},{"key":"2143_CR62","doi-asserted-by":"publisher","DOI":"10.3389\/fonc.2022.861334","volume":"12","author":"Y Li","year":"2022","unstructured":"Li Y, Jin J, Wang Y. SIRT6 widely regulates aging, immunity, and cancer. Front Oncol. 2022;12:861334. https:\/\/doi.org\/10.3389\/fonc.2022.861334.","journal-title":"Front Oncol"},{"key":"2143_CR63","doi-asserted-by":"publisher","DOI":"10.1186\/s13578-024-01333-2","volume":"14","author":"X Wang","year":"2024","unstructured":"Wang X, Zhang P, Yan J, Huang J, Shen Y, He H, et al. SIRT6 deficiency impairs the deacetylation and ubiquitination of UHRF1 to strengthen glycolysis and lactate secretion in bladder cancer. Cell Biosci. 2024;14:153. https:\/\/doi.org\/10.1186\/s13578-024-01333-2.","journal-title":"Cell Biosci"},{"key":"2143_CR64","doi-asserted-by":"publisher","first-page":"883","DOI":"10.1007\/s10495-022-01751-y","volume":"27","author":"Q You","year":"2022","unstructured":"You Q, Wang J, Yu Y, Li F, Meng L, Chen M, et al. The histone deacetylase SIRT6 promotes glycolysis through the HIF-1\u03b1\/HK2 signaling axis and induces erlotinib resistance in non-small cell lung cancer. Apoptosis. 2022;27:883\u201398. https:\/\/doi.org\/10.1007\/s10495-022-01751-y.","journal-title":"Apoptosis"},{"key":"2143_CR65","doi-asserted-by":"publisher","DOI":"10.3390\/cancers13051156","author":"F Fiorentino","year":"2021","unstructured":"Fiorentino F, Carafa V, Favale G, Altucci L, Mai A, Rotili D. The two-faced role of SIRT6 in cancer. Cancers (Basel). 2021. https:\/\/doi.org\/10.3390\/cancers13051156.","journal-title":"Cancers (Basel)"},{"key":"2143_CR66","doi-asserted-by":"publisher","DOI":"10.1038\/s41419-024-07321-1","volume":"15","author":"Y Cao","year":"2024","unstructured":"Cao Y, Wang S, Ma J, Long M, Ma X, Yang X, et al. Mechanistic insights into SIRT7 and EZH2 regulation of cisplatin resistance in bladder cancer cells. Cell Death Dis. 2024;15:931. https:\/\/doi.org\/10.1038\/s41419-024-07321-1.","journal-title":"Cell Death Dis"},{"key":"2143_CR67","doi-asserted-by":"publisher","DOI":"10.1016\/j.canlet.2024.217109","volume":"598","author":"K Chen","year":"2024","unstructured":"Chen K, Li T, Diao H, Wang Q, Zhou X, Huang Z, et al. SIRT7 knockdown promotes gemcitabine sensitivity of pancreatic cancer cell via upregulation of GLUT3 expression. Cancer Lett. 2024;598:217109. https:\/\/doi.org\/10.1016\/j.canlet.2024.217109.","journal-title":"Cancer Lett"},{"key":"2143_CR68","first-page":"1938","volume":"8","author":"Q Geng","year":"2015","unstructured":"Geng Q, Peng H, Chen F, Luo R, Li R. High expression of Sirt7 served as a predictor of adverse outcome in breast cancer. Int J Clin Exp Pathol. 2015;8:1938\u201345.","journal-title":"Int J Clin Exp Pathol"},{"key":"2143_CR69","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-025-58317-0","volume":"16","author":"Z Hu","year":"2025","unstructured":"Hu Z, Tang M, Huang Y, Cai B, Sun X, Chen G, et al. SIRT7 facilitates endometrial cancer progression by regulating PTEN stability in an estrogen-dependent manner. Nat Commun. 2025;16:2989. https:\/\/doi.org\/10.1038\/s41467-025-58317-0.","journal-title":"Nat Commun"},{"key":"2143_CR70","doi-asserted-by":"publisher","first-page":"1528","DOI":"10.7150\/ijbs.75340","volume":"19","author":"Q Huo","year":"2023","unstructured":"Huo Q, Chen S, Zhuang J, Quan C, Wang Y, Xie N. SIRT7 downregulation promotes breast cancer metastasis via LAP2alpha-induced chromosomal instability. Int J Biol Sci. 2023;19:1528\u201342. https:\/\/doi.org\/10.7150\/ijbs.75340.","journal-title":"Int J Biol Sci"},{"key":"2143_CR71","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2409269121","volume":"121","author":"P Kumari","year":"2024","unstructured":"Kumari P, Tarighi S, Fuchshuber E, Li L, Fernandez-Duran I, Wang M, et al. SIRT7 promotes lung cancer progression by destabilizing the tumor suppressor ARF. Proc Natl Acad Sci U S A. 2024;121:e2409269121. https:\/\/doi.org\/10.1073\/pnas.2409269121.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2143_CR72","doi-asserted-by":"publisher","first-page":"1741","DOI":"10.1158\/1078-0432.CCR-13-1547","volume":"20","author":"S Paredes","year":"2014","unstructured":"Paredes S, Villanova L, Chua KF. Molecular pathways: emerging roles of mammalian sirtuin SIRT7 in cancer. Clin Cancer Res. 2014;20:1741\u20136. https:\/\/doi.org\/10.1158\/1078-0432.CCR-13-1547.","journal-title":"Clin Cancer Res"},{"key":"2143_CR73","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/j.amjms.2024.08.028","volume":"369","author":"X Shi","year":"2025","unstructured":"Shi X, Ji Y, Wu X, Du Y, Yan X, Wang Y, et al. Blocking of SIRT7\/FOXO3a axis by miR-152-3p enhances cisplatin sensitivity in breast cancer. Am J Med Sci. 2025;369:105\u201315. https:\/\/doi.org\/10.1016\/j.amjms.2024.08.028.","journal-title":"Am J Med Sci"},{"key":"2143_CR74","doi-asserted-by":"publisher","first-page":"1346","DOI":"10.7150\/thno.18804","volume":"7","author":"M Tang","year":"2017","unstructured":"Tang M, Lu X, Zhang C, Du C, Cao L, Hou T, et al. Downregulation of SIRT7 by 5-fluorouracil induces radiosensitivity in human colorectal cancer. Theranostics. 2017;7:1346\u201359. https:\/\/doi.org\/10.7150\/thno.18804.","journal-title":"Theranostics"},{"key":"2143_CR75","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-017-00396-9","volume":"8","author":"X Tang","year":"2017","unstructured":"Tang X, Shi L, Xie N, Liu Z, Qian M, Meng F, et al. SIRT7 antagonizes TGF-beta signaling and inhibits breast cancer metastasis. Nat Commun. 2017;8:318. https:\/\/doi.org\/10.1038\/s41467-017-00396-9.","journal-title":"Nat Commun"},{"key":"2143_CR76","doi-asserted-by":"publisher","DOI":"10.1080\/23723556.2024.2381287","volume":"11","author":"S Tarighi","year":"2024","unstructured":"Tarighi S, Kumari P, Vaquero A, Braun T, Ianni A. The SIRT7-nucleolus connection in cancer: ARF enters the fray. Mol Cell Oncol. 2024;11:2381287. https:\/\/doi.org\/10.1080\/23723556.2024.2381287.","journal-title":"Mol Cell Oncol"},{"key":"2143_CR77","doi-asserted-by":"publisher","DOI":"10.1016\/j.prp.2024.155233","volume":"256","author":"B Xu","year":"2024","unstructured":"Xu B, Cai X, Cai G, Huang G. SIRT7: a potential prognostic marker and therapeutic target in gallbladder cancer. Pathol Res Pract. 2024;256:155233. https:\/\/doi.org\/10.1016\/j.prp.2024.155233.","journal-title":"Pathol Res Pract"},{"key":"2143_CR78","doi-asserted-by":"publisher","first-page":"1405","DOI":"10.1007\/s13402-021-00649-2","volume":"44","author":"F Yang","year":"2021","unstructured":"Yang F, Hu Y, Shao L, Zhuang J, Huo Q, He S, et al. SIRT7 interacts with TEK (TIE2) to promote adriamycin induced metastasis in breast cancer. Cell Oncol (Dordr). 2021;44:1405\u201324. https:\/\/doi.org\/10.1007\/s13402-021-00649-2.","journal-title":"Cell Oncol (Dordr)"},{"key":"2143_CR79","doi-asserted-by":"publisher","first-page":"3434","DOI":"10.1158\/1078-0432.CCR-13-2952","volume":"20","author":"H Yu","year":"2014","unstructured":"Yu H, Ye W, Wu J, Meng X, Liu RY, Ying X, et al. Overexpression of sirt7 exhibits oncogenic property and serves as a prognostic factor in colorectal cancer. Clin Cancer Res. 2014;20:3434\u201345. https:\/\/doi.org\/10.1158\/1078-0432.CCR-13-2952.","journal-title":"Clin Cancer Res"},{"key":"2143_CR80","doi-asserted-by":"publisher","DOI":"10.1038\/srep09787","volume":"5","author":"S Zhang","year":"2015","unstructured":"Zhang S, Chen P, Huang Z, Hu X, Chen M, Hu S, et al. Sirt7 promotes gastric cancer growth and inhibits apoptosis by epigenetically inhibiting miR-34a. Sci Rep. 2015;5:9787. https:\/\/doi.org\/10.1038\/srep09787.","journal-title":"Sci Rep"},{"key":"2143_CR81","doi-asserted-by":"publisher","first-page":"2723","DOI":"10.1007\/s12253-020-00873-5","volume":"26","author":"B Uzelac","year":"2020","unstructured":"Uzelac B, Krivokuca A, Brankovic-Magic M, Magic Z, Susnjar S, Milovanovic Z, et al. Expression of SIRT1, SIRT3 and SIRT6 genes for predicting survival in triple-negative and hormone receptor-positive subtypes of breast cancer. Pathol Oncol Res. 2020;26:2723\u201331. https:\/\/doi.org\/10.1007\/s12253-020-00873-5.","journal-title":"Pathol Oncol Res"},{"key":"2143_CR82","doi-asserted-by":"publisher","first-page":"747","DOI":"10.1038\/35021093","volume":"406","author":"CM Perou","year":"2000","unstructured":"Perou CM, Sorlie T, Eisen MB, van de Rijn M, Jeffrey SS, Rees CA, et al. Molecular portraits of human breast tumours. Nature. 2000;406:747\u201352. https:\/\/doi.org\/10.1038\/35021093.","journal-title":"Nature"},{"key":"2143_CR83","doi-asserted-by":"publisher","first-page":"10869","DOI":"10.1073\/pnas.191367098","volume":"98","author":"T Sorlie","year":"2001","unstructured":"Sorlie T, Perou CM, Tibshirani R, Aas T, Geisler S, Johnsen H, et al. Gene expression patterns of breast carcinomas distinguish tumor subclasses with clinical implications. Proc Natl Acad Sci U S A. 2001;98:10869\u201374. https:\/\/doi.org\/10.1073\/pnas.191367098.","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2143_CR84","doi-asserted-by":"publisher","first-page":"1160","DOI":"10.1200\/JCO.2008.18.1370","volume":"27","author":"JS Parker","year":"2009","unstructured":"Parker JS, Mullins M, Cheang MC, Leung S, Voduc D, Vickery T, et al. Supervised risk predictor of breast cancer based on intrinsic subtypes. J Clin Oncol. 2009;27:1160\u20137. https:\/\/doi.org\/10.1200\/JCO.2008.18.1370.","journal-title":"J Clin Oncol"},{"key":"2143_CR85","doi-asserted-by":"publisher","first-page":"1889","DOI":"10.1007\/s11357-023-00742-4","volume":"45","author":"B Gyorffy","year":"2023","unstructured":"Gyorffy B. Discovery and ranking of the most robust prognostic biomarkers in serous ovarian cancer. Geroscience. 2023;45:1889\u201398. https:\/\/doi.org\/10.1007\/s11357-023-00742-4.","journal-title":"Geroscience"},{"key":"2143_CR86","doi-asserted-by":"publisher","first-page":"4101","DOI":"10.1016\/j.csbj.2021.07.014","volume":"19","author":"B Gyorffy","year":"2021","unstructured":"Gyorffy B. Survival analysis across the entire transcriptome identifies biomarkers with the highest prognostic power in breast cancer. Comput Struct Biotechnol J. 2021;19:4101\u20139. https:\/\/doi.org\/10.1016\/j.csbj.2021.07.014.","journal-title":"Comput Struct Biotechnol J"},{"key":"2143_CR87","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1111\/bph.16257","volume":"181","author":"B Gyorffy","year":"2024","unstructured":"Gyorffy B. Transcriptome-level discovery of survival-associated biomarkers and therapy targets in non-small-cell lung cancer. Br J Pharmacol. 2024;181:362\u201374. https:\/\/doi.org\/10.1111\/bph.16257.","journal-title":"Br J Pharmacol"},{"key":"2143_CR88","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1111\/j.2517-6161.1995.tb02031.x","volume":"57","author":"Y Benjamini","year":"1995","unstructured":"Benjamini Y, Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J Roy Stat Soc: Ser B (Methodol). 1995;57:289\u2013300.","journal-title":"J Roy Stat Soc: Ser B (Methodol)"},{"key":"2143_CR89","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0245824","volume":"16","author":"O Menyhart","year":"2021","unstructured":"Menyhart O, Weltz B, Gyorffy B. Multipletesting.com: a tool for life science researchers for multiple hypothesis testing correction. PLoS One. 2021;16:e0245824. https:\/\/doi.org\/10.1371\/journal.pone.0245824.","journal-title":"PLoS One"},{"key":"2143_CR90","doi-asserted-by":"publisher","unstructured":"Bartha A, Gyorffy B. TNMplot.com: a web tool for the comparison of gene expression in normal, tumor and metastatic tissues. Int J Mol Sci. 2021;22. https:\/\/doi.org\/10.3390\/ijms22052622","DOI":"10.3390\/ijms22052622"},{"key":"2143_CR91","doi-asserted-by":"publisher","first-page":"686","DOI":"10.1038\/nature02789","volume":"430","author":"JG Wood","year":"2004","unstructured":"Wood JG, Rogina B, Lavu S, Howitz K, Helfand SL, Tatar M, et al. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature. 2004;430:686\u20139.","journal-title":"Nature"},{"key":"2143_CR92","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1038\/nature01960","volume":"425","author":"KT Howitz","year":"2003","unstructured":"Howitz KT, Bitterman KJ, Cohen HY, Lamming DW, Lavu S, Wood JG, et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature. 2003;425:191\u20136.","journal-title":"Nature"},{"key":"2143_CR93","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1038\/nature01578","volume":"423","author":"RM Anderson","year":"2003","unstructured":"Anderson RM, Bitterman KJ, Wood JG, Medvedik O, Sinclair DA. Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature. 2003;423:181\u20135.","journal-title":"Nature"},{"key":"2143_CR94","first-page":"237","volume":"16","author":"Y Kobayashi","year":"2005","unstructured":"Kobayashi Y, Furukawa-Hibi Y, Chen C, Horio Y, Isobe K, Ikeda K, et al. SIRT1 is critical regulator of FOXO-mediated transcription in response to oxidative stress. Int J Mol Med. 2005;16:237\u201343.","journal-title":"Int J Mol Med"},{"key":"2143_CR95","doi-asserted-by":"publisher","first-page":"2011","DOI":"10.1126\/science.1094637","volume":"303","author":"A Brunet","year":"2004","unstructured":"Brunet A, Sweeney LB, Sturgill JF, Chua KF, Greer PL, Lin Y, et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science. 2004;303:2011\u20135.","journal-title":"Science"},{"key":"2143_CR96","doi-asserted-by":"crossref","unstructured":"Yang H, Yang T, Baur JA, Perez E, Matsui T, Carmona JJ, et al. Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival. Cell. 2007;130:1095\u2013107. S0092-8674(07)00973-7 [pii].","DOI":"10.1016\/j.cell.2007.07.035"},{"key":"2143_CR97","doi-asserted-by":"crossref","unstructured":"1016\/j.cell.2007.07.035","DOI":"10.1088\/1126-6708\/2007\/07\/035"},{"key":"2143_CR98","doi-asserted-by":"publisher","first-page":"937","DOI":"10.3892\/ol.2018.9698","volume":"17","author":"S Mao","year":"2019","unstructured":"Mao S, Ma J, Yu H. Sirtuin\u20117 knockdown inhibits the growth of endometrial cancer cells by inducing apoptosis via the NF\u2011\u03baB signaling pathway. Oncol Lett. 2019;17:937\u201343. https:\/\/doi.org\/10.3892\/ol.2018.9698.","journal-title":"Oncol Lett"},{"key":"2143_CR99","doi-asserted-by":"publisher","unstructured":"Curtis C, Shah SP, Chin SF, Turashvili G, Rueda OM, Dunning MJ, Speed D, Lynch AG, Samarajiwa S, Yuan Y, Graf S, Ha G, Haffari G, Bashashati A, Russell R, McKinney S, Group M, Langerod A, Green A, Provenzano E, Wishart G, Pinder S, Watson P, Markowetz F, Murphy L, Ellis I, Purushotham A, Borresen-Dale AL, Brenton JD, Tavare S, et al. The genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups. Nature. 2012;486:346\u2013352. https:\/\/doi.org\/10.1038\/nature10983","DOI":"10.1038\/nature10983"},{"key":"2143_CR100","doi-asserted-by":"publisher","DOI":"10.5808\/gi.23003","volume":"21","author":"ND Zulkifli","year":"2023","unstructured":"Zulkifli ND, Zulkifle N. Insight from sirtuins interactome: topological prominence and multifaceted roles of SIRT1 in modulating immunity, aging and cancer. Genomics Inform. 2023;21:e23. https:\/\/doi.org\/10.5808\/gi.23003.","journal-title":"Genomics Inform"},{"key":"2143_CR101","doi-asserted-by":"publisher","first-page":"5489","DOI":"10.1038\/sj.onc.1210616","volume":"26","author":"LR Saunders","year":"2007","unstructured":"Saunders LR, Verdin E. Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene. 2007;26:5489\u2013504. https:\/\/doi.org\/10.1038\/sj.onc.1210616.","journal-title":"Oncogene"},{"key":"2143_CR102","doi-asserted-by":"publisher","first-page":"905","DOI":"10.2217\/fon.10.57","volume":"6","author":"RM Rodriguez","year":"2010","unstructured":"Rodriguez RM, Fraga MF. Aging and cancer: are sirtuins the link? Future Oncol. 2010;6:905\u201315. https:\/\/doi.org\/10.2217\/fon.10.57.","journal-title":"Future Oncol"},{"key":"2143_CR103","doi-asserted-by":"publisher","first-page":"1208","DOI":"10.1111\/acel.12685","volume":"16","author":"C O'Callaghan","year":"2017","unstructured":"O\u2019Callaghan C, Vassilopoulos A. Sirtuins at the crossroads of stemness, aging, and cancer. Aging Cell. 2017;16:1208\u201318. https:\/\/doi.org\/10.1111\/acel.12685.","journal-title":"Aging Cell"},{"key":"2143_CR104","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1016\/j.cmet.2010.06.009","volume":"12","author":"HS Kim","year":"2010","unstructured":"Kim HS, Xiao C, Wang RH, Lahusen T, Xu X, Vassilopoulos A, et al. Hepatic-specific disruption of SIRT6 in mice results in fatty liver formation due to enhanced glycolysis and triglyceride synthesis. Cell Metab. 2010;12:224\u201336. https:\/\/doi.org\/10.1016\/j.cmet.2010.06.009.","journal-title":"Cell Metab"},{"key":"2143_CR105","doi-asserted-by":"publisher","first-page":"1401","DOI":"10.1016\/j.cell.2016.04.033","volume":"165","author":"S Kugel","year":"2016","unstructured":"Kugel S, Sebastian C, Fitamant J, Ross KN, Saha SK, Jain E, et al. SIRT6 suppresses pancreatic cancer through control of Lin28b. Cell. 2016;165:1401\u201315. https:\/\/doi.org\/10.1016\/j.cell.2016.04.033.","journal-title":"Cell"},{"key":"2143_CR106","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1038\/s12276-021-00578-y","volume":"53","author":"JJ Park","year":"2021","unstructured":"Park JJ, Hah YS, Ryu S, Cheon SY, Won SJ, Lee JS, et al. MDM2-dependent Sirt1 degradation is a prerequisite for Sirt6-mediated cell death in head and neck cancers. Exp Mol Med. 2021;53:422\u201331. https:\/\/doi.org\/10.1038\/s12276-021-00578-y.","journal-title":"Exp Mol Med"},{"key":"2143_CR107","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1016\/j.ccr.2008.09.001","volume":"14","author":"RH Wang","year":"2008","unstructured":"Wang RH, Sengupta K, Li C, Kim HS, Cao L, Xiao C, et al. Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice. Cancer Cell. 2008;14:312\u201323. https:\/\/doi.org\/10.1016\/j.ccr.2008.09.001.","journal-title":"Cancer Cell"},{"key":"2143_CR108","doi-asserted-by":"publisher","first-page":"22623","DOI":"10.1073\/pnas.1010377108","volume":"107","author":"M Ming","year":"2010","unstructured":"Ming M, Shea CR, Guo X, Li X, Soltani K, Han W, et al. Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C. Proc Natl Acad Sci U S A. 2010;107:22623\u20138. https:\/\/doi.org\/10.1073\/pnas.1010377108.","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"10","key":"2143_CR109","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1038\/nrc3985","volume":"15","author":"A Chalkiadaki","year":"2015","unstructured":"Chalkiadaki A, Guarente L. The multifaceted functions of sirtuins in cancer. Nat Rev Cancer. 2015;15(10):608\u201324. https:\/\/doi.org\/10.1038\/nrc3985.","journal-title":"Nat Rev Cancer"},{"key":"2143_CR110","doi-asserted-by":"publisher","DOI":"10.3390\/cancers11121949","author":"E Zhao","year":"2019","unstructured":"Zhao E, Hou J, Ke X, Abbas MN, Kausar S, Zhang L, et al. The roles of sirtuin family proteins in cancer progression. Cancers (Basel). 2019. https:\/\/doi.org\/10.3390\/cancers11121949.","journal-title":"Cancers (Basel)"},{"key":"2143_CR111","doi-asserted-by":"publisher","DOI":"10.3389\/fonc.2019.00754","volume":"9","author":"X Sun","year":"2019","unstructured":"Sun X, Wang S, Gai J, Guan J, Li J, Li Y, et al. SIRT5 promotes cisplatin resistance in ovarian cancer by suppressing DNA damage in a ROS-dependent manner via regulation of the Nrf2\/HO-1 pathway. Front Oncol. 2019;9:754. https:\/\/doi.org\/10.3389\/fonc.2019.00754.","journal-title":"Front Oncol"},{"key":"2143_CR112","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1021\/bi901627u","volume":"49","author":"H Cimen","year":"2010","unstructured":"Cimen H, Han MJ, Yang Y, Tong Q, Koc H, Koc EC. Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry. 2010;49:304\u201311. https:\/\/doi.org\/10.1021\/bi901627u.","journal-title":"Biochemistry"},{"key":"2143_CR113","doi-asserted-by":"publisher","first-page":"534","DOI":"10.1038\/embor.2011.65","volume":"12","author":"Y Chen","year":"2011","unstructured":"Chen Y, Zhang J, Lin Y, Lei Q, Guan KL, Zhao S, et al. Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep. 2011;12:534\u201341. https:\/\/doi.org\/10.1038\/embor.2011.65.","journal-title":"EMBO Rep"},{"key":"2143_CR114","doi-asserted-by":"publisher","DOI":"10.3390\/cancers9070090","author":"M Torrens-Mas","year":"2017","unstructured":"Torrens-Mas M, Oliver J, Roca P, Sastre-Serra J. SIRT3: oncogene and tumor suppressor in cancer. Cancers (Basel). 2017. https:\/\/doi.org\/10.3390\/cancers9070090.","journal-title":"Cancers (Basel)"},{"issue":"1","key":"2143_CR115","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-65423-0","volume":"10","author":"M Locatelli","year":"2020","unstructured":"Locatelli M, Zoja C, Zanchi C, Corna D, Villa S, Bolognini S, et al. Manipulating sirtuin 3 pathway ameliorates renal damage in experimental diabetes. Sci Rep. 2020;10(1):8418. https:\/\/doi.org\/10.1038\/s41598-020-65423-0.","journal-title":"Sci Rep"},{"key":"2143_CR116","doi-asserted-by":"publisher","first-page":"2986","DOI":"10.1038\/onc.2011.37","volume":"30","author":"EL Bell","year":"2011","unstructured":"Bell EL, Emerling BM, Ricoult SJ, Guarente L. SirT3 suppresses hypoxia inducible factor 1\u03b1 and tumor growth by inhibiting mitochondrial ROS production. Oncogene. 2011;30:2986\u201396. https:\/\/doi.org\/10.1038\/onc.2011.37.","journal-title":"Oncogene"},{"key":"2143_CR117","doi-asserted-by":"publisher","first-page":"416","DOI":"10.1016\/j.ccr.2011.02.014","volume":"19","author":"LW Finley","year":"2011","unstructured":"Finley LW, Carracedo A, Lee J, Souza A, Egia A, Zhang J, et al. SIRT3 opposes reprogramming of cancer cell metabolism through HIF1alpha destabilization. Cancer Cell. 2011;19:416\u201328. https:\/\/doi.org\/10.1016\/j.ccr.2011.02.014.","journal-title":"Cancer Cell"},{"key":"2143_CR118","doi-asserted-by":"publisher","first-page":"2380","DOI":"10.1002\/cam4.2089","volume":"8","author":"L Xu","year":"2019","unstructured":"Xu L, Li Y, Zhou L, Dorfman RG, Liu L, Cai R, et al. SIRT3 elicited an anti-Warburg effect through HIF1alpha\/PDK1\/PDHA1 to inhibit cholangiocarcinoma tumorigenesis. Cancer Med. 2019;8:2380\u201391. https:\/\/doi.org\/10.1002\/cam4.2089.","journal-title":"Cancer Med"},{"key":"2143_CR119","doi-asserted-by":"publisher","first-page":"3990","DOI":"10.1158\/0008-5472.CAN-16-2393","volume":"77","author":"X Zou","year":"2017","unstructured":"Zou X, Zhu Y, Park SH, Liu G, O\u2019Brien J, Jiang H, et al. SIRT3-mediated dimerization of IDH2 directs cancer cell metabolism and tumor growth. Cancer Res. 2017;77:3990\u20139. https:\/\/doi.org\/10.1158\/0008-5472.CAN-16-2393.","journal-title":"Cancer Res"},{"key":"2143_CR120","doi-asserted-by":"publisher","DOI":"10.1186\/2049-3002-2-15","volume":"2","author":"Y Zhu","year":"2014","unstructured":"Zhu Y, Yan Y, Principe DR, Zou X, Vassilopoulos A, Gius D. SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis. Cancer Metab. 2014;2:15. https:\/\/doi.org\/10.1186\/2049-3002-2-15.","journal-title":"Cancer Metab"},{"key":"2143_CR121","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1016\/j.celrep.2015.09.022","volume":"13","author":"S Kugel","year":"2015","unstructured":"Kugel S, Feldman JL, Klein MA, Silberman DM, Sebastian C, Mermel C, et al. Identification of and molecular basis for SIRT6 loss-of-function point mutations in cancer. Cell Rep. 2015;13:479\u201388. https:\/\/doi.org\/10.1016\/j.celrep.2015.09.022.","journal-title":"Cell Rep"},{"key":"2143_CR122","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1152\/physrev.00030.2018","volume":"100","author":"AR Chang","year":"2020","unstructured":"Chang AR, Ferrer CM, Mostoslavsky R. SIRT6, a mammalian deacylase with multitasking abilities. Physiol Rev. 2020;100:145\u201369. https:\/\/doi.org\/10.1152\/physrev.00030.2018.","journal-title":"Physiol Rev"},{"key":"2143_CR123","doi-asserted-by":"publisher","first-page":"2210","DOI":"10.1002\/jcb.25171","volume":"116","author":"M Choe","year":"2015","unstructured":"Choe M, Brusgard JL, Chumsri S, Bhandary L, Zhao XF, Lu S, et al. The RUNX2 transcription factor negatively regulates SIRT6 expression to alter glucose metabolism in breast cancer cells. J Cell Biochem. 2015;116:2210\u201326. https:\/\/doi.org\/10.1002\/jcb.25171.","journal-title":"J Cell Biochem"},{"key":"2143_CR124","doi-asserted-by":"publisher","first-page":"1185","DOI":"10.1016\/j.cell.2012.10.047","volume":"151","author":"C Sebastian","year":"2012","unstructured":"Sebastian C, Zwaans BM, Silberman DM, Gymrek M, Goren A, Zhong L, et al. The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism. Cell. 2012;151:1185\u201399. https:\/\/doi.org\/10.1016\/j.cell.2012.10.047.","journal-title":"Cell"},{"key":"2143_CR125","doi-asserted-by":"publisher","DOI":"10.3390\/biom13111593","author":"Y Lu","year":"2023","unstructured":"Lu Y, Wang S, Jiao Y. The effects of deregulated ribosomal biogenesis in cancer. Biomolecules. 2023. https:\/\/doi.org\/10.3390\/biom13111593.","journal-title":"Biomolecules"},{"key":"2143_CR126","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1038\/s41401-020-0442-2","volume":"42","author":"JL Shang","year":"2021","unstructured":"Shang JL, Ning SB, Chen YY, Chen TX, Zhang J. MDL-800, an allosteric activator of SIRT6, suppresses proliferation and enhances EGFR-TKIs therapy in non-small cell lung cancer. Acta Pharmacol Sin. 2021;42:120\u201331. https:\/\/doi.org\/10.1038\/s41401-020-0442-2.","journal-title":"Acta Pharmacol Sin"},{"key":"2143_CR127","doi-asserted-by":"publisher","first-page":"15395","DOI":"10.1002\/jcp.28186","volume":"234","author":"S Zhang","year":"2019","unstructured":"Zhang S, Yang Y, Huang S, Deng C, Zhou S, Yang J, et al. SIRT1 inhibits gastric cancer proliferation and metastasis via STAT3\/MMP-13 signaling. J Cell Physiol. 2019;234:15395\u2013406. https:\/\/doi.org\/10.1002\/jcp.28186.","journal-title":"J Cell Physiol"},{"key":"2143_CR128","doi-asserted-by":"publisher","first-page":"575","DOI":"10.3892\/mmr.2020.11113","volume":"22","author":"Z Eroglu","year":"2020","unstructured":"Eroglu Z, Erdem C, Oktem G, Bozok Cetintas V, Duzgun Z. Effect of SIRT1 activators and inhibitors on CD44+\/CD133+\u2011enriched non\u2011small cell lung cancer cells. Mol Med Rep. 2020;22:575\u201381. https:\/\/doi.org\/10.3892\/mmr.2020.11113.","journal-title":"Mol Med Rep"},{"key":"2143_CR129","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.adv0766","volume":"17","author":"Q Gao","year":"2025","unstructured":"Gao Q, Yang L, Ye S, Mai M, Liu Y, Jiang X, et al. Targeting SIRT2 induces MLH1 deficiency and boosts antitumor immunity in preclinical colorectal cancer models. Sci Transl Med. 2025;17:eadv0766. https:\/\/doi.org\/10.1126\/scitranslmed.adv0766.","journal-title":"Sci Transl Med"},{"key":"2143_CR130","doi-asserted-by":"publisher","first-page":"326","DOI":"10.1089\/ars.2016.6641","volume":"25","author":"X Zou","year":"2016","unstructured":"Zou X, Santa-Maria CA, O\u2019Brien J, Gius D, Zhu Y. Manganese superoxide dismutase acetylation and dysregulation, due to loss of SIRT3 activity, promote a luminal B-like breast carcinogenic-permissive phenotype. Antioxid Redox Signal. 2016;25:326\u201336. https:\/\/doi.org\/10.1089\/ars.2016.6641.","journal-title":"Antioxid Redox Signal"},{"key":"2143_CR131","doi-asserted-by":"publisher","first-page":"1060","DOI":"10.1089\/ars.2014.6213","volume":"22","author":"S Kumar","year":"2015","unstructured":"Kumar S, Lombard DB. Mitochondrial sirtuins and their relationships with metabolic disease and cancer. Antioxid Redox Signal. 2015;22:1060\u201377. https:\/\/doi.org\/10.1089\/ars.2014.6213.","journal-title":"Antioxid Redox Signal"},{"key":"2143_CR132","doi-asserted-by":"publisher","first-page":"2164","DOI":"10.1080\/15384101.2019.1634953","volume":"18","author":"LF Costa-Machado","year":"2019","unstructured":"Costa-Machado LF, Fernandez-Marcos PJ. The sirtuin family in cancer. Cell Cycle. 2019;18:2164\u201396. https:\/\/doi.org\/10.1080\/15384101.2019.1634953.","journal-title":"Cell Cycle"},{"key":"2143_CR133","doi-asserted-by":"publisher","DOI":"10.1080\/23723556.2014.1001199","volume":"2","author":"N Djouder","year":"2015","unstructured":"Djouder N. Boosting NAD(+) for the prevention and treatment of liver cancer. Mol Cell Oncol. 2015;2:e1001199. https:\/\/doi.org\/10.1080\/23723556.2014.1001199.","journal-title":"Mol Cell Oncol"},{"key":"2143_CR134","doi-asserted-by":"publisher","DOI":"10.1038\/s41392-020-00311-7","volume":"5","author":"N Xie","year":"2020","unstructured":"Xie N, Zhang L, Gao W, Huang C, Huber PE, Zhou X, et al. NAD(+) metabolism: pathophysiologic mechanisms and therapeutic potential. Signal Transduct Target Ther. 2020;5:227. https:\/\/doi.org\/10.1038\/s41392-020-00311-7.","journal-title":"Signal Transduct Target Ther"}],"container-title":["GeroScience"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11357-026-02143-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11357-026-02143-9","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11357-026-02143-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,11]],"date-time":"2026-07-11T10:09:03Z","timestamp":1783764543000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11357-026-02143-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,16]]},"references-count":134,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2026,6]]}},"alternative-id":["2143"],"URL":"https:\/\/doi.org\/10.1007\/s11357-026-02143-9","relation":{},"ISSN":["2509-2723"],"issn-type":[{"value":"2509-2723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,16]]},"assertion":[{"value":"29 October 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 January 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 February 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"NA.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"NA.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"Dr. Bal\u00e1zs Gy\u0151rffy serves as Associate Editor for\n                      GeroScience\n                      . Dr. Zoltan Ungvari serves as Editor-in-Chief for\n                      GeroScience\n                      .","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}