{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T09:55:50Z","timestamp":1793267750362,"version":"4.5.0"},"reference-count":77,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2021,8,4]],"date-time":"2021-08-04T00:00:00Z","timestamp":1628035200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2021,8,4]],"date-time":"2021-08-04T00:00:00Z","timestamp":1628035200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["425914\/2016-0"],"award-info":[{"award-number":["425914\/2016-0"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004263","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado do Rio Grande do Sul","doi-asserted-by":"publisher","award":["2266-2551\/14-2"],"award-info":[{"award-number":["2266-2551\/14-2"]}],"id":[{"id":"10.13039\/501100004263","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Financiadora de Estudos e Projetos\/Rede Instituto Brasileiro de Neuroci\u00eancia","award":["01.06.0842-00"],"award-info":[{"award-number":["01.06.0842-00"]}]},{"name":"Instituto Nacional de Ci\u00eancia e Tecnologia em Excitotoxicidade e Neuroprote\u00e7\u00e3o","award":["573677\/2008-5"],"award-info":[{"award-number":["573677\/2008-5"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Bioenerg Biomembr"],"published-print":{"date-parts":[[2021,10]]},"DOI":"10.1007\/s10863-021-09914-3","type":"journal-article","created":{"date-parts":[[2021,8,4]],"date-time":"2021-08-04T04:04:08Z","timestamp":1628049848000},"page":"525-539","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["S-adenosylmethionine induces mitochondrial dysfunction, permeability transition pore opening and redox imbalance in subcellular preparations of rat liver"],"prefix":"10.1007","volume":"53","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9803-7746","authenticated-orcid":false,"given":"Bianca","family":"Seminotti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3405-3739","authenticated-orcid":false,"given":"Ana Cristina","family":"Roginski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c2ngela","family":"Zanatta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6512-0714","authenticated-orcid":false,"given":"Alexandre Umpierrez","family":"Amaral","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thabata","family":"Fernandes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaleb Pinto","family":"Spannenberger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucas Henrique Rodrigues","family":"da Silva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5814-6369","authenticated-orcid":false,"given":"Rafael Teixeira","family":"Ribeiro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7964-8923","authenticated-orcid":false,"given":"Guilhian","family":"Leipnitz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6372-1807","authenticated-orcid":false,"given":"Moacir","family":"Wajner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,8,4]]},"reference":[{"key":"9914_CR1","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1016\/0014-5793(76)80434-6","volume":"68","author":"KE Akerman","year":"1976","unstructured":"Akerman KE, Wikstrom MK (1976) Safranine as a probe of the mitochondrial membrane potential. FEBS Lett 68:191\u2013197. https:\/\/doi.org\/10.1016\/0014-5793(76)80434-6","journal-title":"FEBS Lett"},{"key":"9914_CR2","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1016\/s0304-3940(01)01636-6","volume":"302","author":"MY Aksenov","year":"2001","unstructured":"Aksenov MY, Markesbery WR (2001) Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer\u2019s disease. Neurosci Lett 302:141\u2013145. https:\/\/doi.org\/10.1016\/s0304-3940(01)01636-6","journal-title":"Neurosci Lett"},{"key":"9914_CR3","doi-asserted-by":"publisher","first-page":"274","DOI":"10.1053\/jhep.2002.30419","volume":"35","author":"E Ansorena","year":"2002","unstructured":"Ansorena E, Garc\u00eda-Trevijano ER, Mart\u00ednez-Chantar ML, Huang ZZ, Chen L, Mato JM, Iraburu M, Lu SC, Avila MA (2002) S-adenosylmethionine and methylthioadenosine are antiapoptotic in cultured rat hepatocytes but proapoptotic in human hepatoma cells. Hepatology 35:274\u2013280. https:\/\/doi.org\/10.1053\/jhep.2002.30419","journal-title":"Hepatology"},{"key":"9914_CR4","doi-asserted-by":"publisher","first-page":"1655","DOI":"10.1002\/hep.22231","volume":"47","author":"AI Ara","year":"2008","unstructured":"Ara AI, Xia M, Ramani K, Mato JM, Lu SC (2008) S-adenosylmethionine inhibits lipopolysaccharide-induced gene expression via modulation of histone methylation. Hepatology 47:1655\u20131666. https:\/\/doi.org\/10.1002\/hep.22231","journal-title":"Hepatology"},{"key":"9914_CR5","doi-asserted-by":"publisher","first-page":"745","DOI":"10.1023\/B:BOLI.0000009978.17777.33","volume":"26","author":"P Augoustides-Savvopoulou","year":"2003","unstructured":"Augoustides-Savvopoulou P, Luka Z, Karyda S, Stabler SP, Allen RH, Patsiaoura K, Wagner C, Mudd SH (2003) Glycine N-methyltransferase deficiency: a new patient with a novel mutation. J Inherit Metab Dis 26:745\u2013759. https:\/\/doi.org\/10.1023\/B:BOLI.0000009978.17777.33","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR6","doi-asserted-by":"publisher","first-page":"4234","DOI":"10.1073\/pnas.0400658101","volume":"101","author":"I Bari\u0107","year":"2004","unstructured":"Bari\u0107 I, Fumic K, Glenn B, Cuk M, Schulze A, Finkelstein JD, James SJ, Mejaski-Bosnjak V, Pazanin L, Pogribny IP, Rados M, Sarnavka V, Scukanec-Spoljar M, Allen RH, Stabler S, Uzelac L, Vugrek O, Wagner C, Zeisel S, Mudd SH (2004) S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. Proc Natl Acad Sci USA 101:4234\u20134239. https:\/\/doi.org\/10.1073\/pnas.0400658101","journal-title":"Proc Natl Acad Sci USA"},{"key":"9914_CR7","doi-asserted-by":"publisher","first-page":"885","DOI":"10.1007\/s10545-005-0192-9","volume":"28","author":"I Bari\u0107","year":"2005","unstructured":"Bari\u0107 I, \u0106uk M, Fumi\u0107 K, Vugrek O, Allen RH, Glenn B, Maradin M, Pazanin L, Pogribny I, Rados M, Sarnavka V, Schulze A, Stabler S, Wagner C, Zeisel SH, Mudd SH (2005) S-adenosylhomocysteine hydrolase deficiency: a second patient, the younger brother of the index patient, and outcomes during therapy. J Inherit Metab Dis 28:885\u2013902. https:\/\/doi.org\/10.1007\/s10545-005-0192-9","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR8","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1007\/s10545-016-9972-7","volume":"40","author":"I Bari\u0107","year":"2017","unstructured":"Bari\u0107 I, Staufner C, Augoustides-Savvopoulou P, Chien YH, Dobbelaere D, Gr\u00fcnert SC, Opladen T, Petkovi\u0107 Ramad\u017ea D, Raki\u0107 B, Wedell A, Blom HJ (2017a) Consensus recommendations for the diagnosis, treatment and follow-up of inherited methylation disorders. J Inherit Metab Dis 40:5\u201320. https:\/\/doi.org\/10.1007\/s10545-016-9972-7","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR9","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1007\/8904_2016_543","volume":"31","author":"I Bari\u0107","year":"2017","unstructured":"Bari\u0107 I, Erdol S, Saglam H, Lovri\u0107 M, Belu\u017ei\u0107 R, Vugrek O, Blom HJ, Fumi\u0107 K (2017b) Glycine N-methyltransferase deficiency: A member of dysmethylating liver disorders? JIMD Rep 31:101\u2013106. https:\/\/doi.org\/10.1007\/8904_2016_543","journal-title":"JIMD Rep"},{"key":"9914_CR10","doi-asserted-by":"publisher","first-page":"740","DOI":"10.1002\/ajmg.a.61489","volume":"182","author":"H Bas","year":"2020","unstructured":"Bas H, Cilingir O, Tekin N, Saylisoy S, Durak Aras B, Uzay E, Erzurumluoglu Gokalp E, Artan S (2020) Turkish patient with novel AHCY variants and presumed diagnosis of S-adenosylhomocysteine hydrolase deficiency. Am J Med Genet A 182:740\u2013745. https:\/\/doi.org\/10.1002\/ajmg.a.61489","journal-title":"Am J Med Genet A"},{"key":"9914_CR11","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1016\/j.ajhg.2011.09.004","volume":"89","author":"MK Bjursell","year":"2011","unstructured":"Bjursell MK, Blom HJ, Cayuela JA, Engvall ML, Lesko N, Balasubramaniam S, Brandberg G, Halldin M, Falkenberg M, Jakobs C, Smith D, Struys E, von D\u00f6beln U, Gustafsson CM, Lundeberg J, Wedell A (2011) Adenosine kinase deficiency disrupts the methionine cycle and causes hypermethioninemia, encephalopathy, and abnormal liver function. Am J Hum Genet 89:507\u2013515. https:\/\/doi.org\/10.1016\/j.ajhg.2011.09.004","journal-title":"Am J Hum Genet"},{"key":"9914_CR12","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1385\/0-89603-472-0:347","volume":"108","author":"RW Browne","year":"1998","unstructured":"Browne RW, Armstrong D (1998) Reduced glutathione and glutathione disulfide. Methods Mol Biol 108:347\u2013352. https:\/\/doi.org\/10.1385\/0-89603-472-0:347","journal-title":"Methods Mol Biol"},{"key":"9914_CR13","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1007\/s10545-006-0240-0","volume":"29","author":"NR Buist","year":"2006","unstructured":"Buist NR, Glenn B, Vugrek O, Wagner C, Stabler S, Allen RH, Pogribny I, Schulze A, Zeisel SH, Bari\u0107 I, Mudd SH (2006) S-adenosylhomocysteine hydrolase deficiency in a 26-year-old man. J Inherit Metab Dis 29:538\u2013545. https:\/\/doi.org\/10.1007\/s10545-006-0240-0","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR14","doi-asserted-by":"publisher","first-page":"2942","DOI":"10.1021\/ja01131a519","volume":"74","author":"GL Cantoni","year":"1952","unstructured":"Cantoni GL (1952) The nature of the active methyl donor formed enzymatically from L-methionine and adenosinetriphosphate. J Am Chem Soc 74:2942\u20132943. https:\/\/doi.org\/10.1021\/ja01131a519","journal-title":"J Am Chem Soc"},{"key":"9914_CR15","doi-asserted-by":"publisher","first-page":"184","DOI":"10.1016\/j.jnutbio.2006.12.006","volume":"18","author":"M Cave","year":"2007","unstructured":"Cave M, Deaciuc I, Mendez C, Song Z, Joshi-Barve S, Barve S, McClain C (2007) Nonalcoholic fatty liver disease: predisposing factors and the role of nutrition. J Nutr Biochem 18:184\u2013195. https:\/\/doi.org\/10.1016\/j.jnutbio.2006.12.006","journal-title":"J Nutr Biochem"},{"key":"9914_CR16","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.mito.2019.09.008","volume":"50","author":"C Cecatto","year":"2020","unstructured":"Cecatto C, Amaral AU, Wajner A, Wajner SM, Castilho RF, Wajner M (2020) Disturbance of mitochondrial functions associated with permeability transition pore opening induced by cis-5-tetradecenoic and myristic acids in liver of adolescent rats. Mitochondrion 50:1\u201313. https:\/\/doi.org\/10.1016\/j.mito.2019.09.008","journal-title":"Mitochondrion"},{"key":"9914_CR17","doi-asserted-by":"publisher","first-page":"1366","DOI":"10.3748\/wjg.v16.i11.1366","volume":"16","author":"AI Cederbaum","year":"2010","unstructured":"Cederbaum AI (2010) Hepatoprotective effects of S-adenosyl-L-methionine against alcohol- and cytochrome P450 2E1-induced liver injury. World J Gastroenterol 16:1366\u20131376. https:\/\/doi.org\/10.3748\/wjg.v16.i11.1366","journal-title":"World J Gastroenterol"},{"key":"9914_CR18","doi-asserted-by":"publisher","first-page":"6746","DOI":"10.1074\/jbc.271.12.6746","volume":"271","author":"P Costantini","year":"1996","unstructured":"Costantini P, Chernyak BV, Petronilli V, Bernardi P (1996) Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J Biol Chem 271:6746\u20136751. https:\/\/doi.org\/10.1074\/jbc.271.12.6746","journal-title":"J Biol Chem"},{"key":"9914_CR19","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/s0009-8981(03)00003-2","volume":"329","author":"I Dalle-Donne","year":"2003","unstructured":"Dalle-Donne I, Rossi R, Giustarini D, Milzani A, Colombo R (2003) Protein carbonyl groups as biomarkers of oxidative stress. Clin Chim Acta 329:23\u201338. https:\/\/doi.org\/10.1016\/s0009-8981(03)00003-2","journal-title":"Clin Chim Acta"},{"key":"9914_CR20","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1016\/0076-6879(90)86134-H","volume":"186","author":"H Esterbauer","year":"1990","unstructured":"Esterbauer H, Cheeseman KH (1990) Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal. Methods Enzymol 186:407\u2013421. https:\/\/doi.org\/10.1016\/0076-6879(90)86134-H","journal-title":"Methods Enzymol"},{"key":"9914_CR21","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1006\/abbi.2001.2292","volume":"388","author":"P Evelson","year":"2001","unstructured":"Evelson P, Travacio M, Repetto M, Escobar J, Llesuy S, Lissi EA (2001) Evaluation of total reactive antioxidant potential (TRAP) of tissue homogenates and their cytosols. Arch Biochem Biophys 388:261\u2013266. https:\/\/doi.org\/10.1006\/abbi.2001.2292","journal-title":"Arch Biochem Biophys"},{"key":"9914_CR22","doi-asserted-by":"publisher","first-page":"19955","DOI":"10.1016\/S0021-9258(17)45467-6","volume":"265","author":"MM Fagian","year":"1990","unstructured":"Fagian MM, Pereira-da-Silva L, Martins IS, Vercesi AE (1990) Membrane protein thiol cross-linking associated with the permeabilization of the inner mitochondrial membrane by Ca2+ plus prooxidants. J Biol Chem 265:19955\u201319960","journal-title":"J Biol Chem"},{"key":"9914_CR23","doi-asserted-by":"publisher","first-page":"S15","DOI":"10.1016\/j.freeradbiomed.2014.10.589","volume":"75","author":"M Fedorova","year":"2014","unstructured":"Fedorova M, Griesser E, Vemula V, Weber D, Ni Z, Hoffmann R (2014) Protein and lipid carbonylation in cellular model of nitrosative stress: mass spectrometry, biochemistry and microscopy study. Free Radic Biol Med 75:S15. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2014.10.589","journal-title":"Free Radic Biol Med"},{"key":"9914_CR24","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1016\/0955-2863(90)90070-2","volume":"1","author":"JD Finkelstein","year":"1990","unstructured":"Finkelstein JD (1990) Methionine metabolism in mammals. J Nutr Biochem 1:228\u2013237. https:\/\/doi.org\/10.1016\/0955-2863(90)90070-2","journal-title":"J Nutr Biochem"},{"key":"9914_CR25","doi-asserted-by":"publisher","first-page":"84","DOI":"10.1016\/S0003-9861(71)80044-9","volume":"146","author":"JD Finkelstein","year":"1971","unstructured":"Finkelstein JD, Kyle W, Harris BJ (1971) Methionine metabolism in mammals. Regulation of homocysteine methyltransferases in rat tissue. Arch Biochem Biophys 146:84\u201392. https:\/\/doi.org\/10.1016\/S0003-9861(71)80044-9","journal-title":"Arch Biochem Biophys"},{"key":"9914_CR26","doi-asserted-by":"publisher","first-page":"e12514","DOI":"10.1111\/jpi.12514","volume":"65","author":"A Galano","year":"2018","unstructured":"Galano A, Reiter RJ (2018) Melatonin and its metabolites vs oxidative stress: from individual actions to collective protection. J Pineal Res 65:e12514. https:\/\/doi.org\/10.1111\/jpi.12514","journal-title":"J Pineal Res"},{"key":"9914_CR27","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1093\/acprof:oso\/9780198717478.003.0005","volume-title":"Free radicals in biology and medicine","author":"B Halliwell","year":"2015","unstructured":"Halliwell B, Gutteridge JMC (2015) Cellular responses to oxidative stress: adaptation, damage, repair, senescence and death. In: Halliwell B, Gutteridge JMC (eds) Free radicals in biology and medicine, 5th edn. Oxford University Press Inc., Oxford, pp 199\u2013283","edition":"5"},{"key":"9914_CR28","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2011.09.030","volume":"52","author":"B Kalyanaraman","year":"2012","unstructured":"Kalyanaraman B, Darley-Usmar V, Davies KJ, Dennery PA, Forman HJ, Grisham MB, Mann GE, Moore K, Roberts LJ 2nd, Ischiropoulos H (2012) Measuring reactive oxygen and nitrogen species with fluorescent probes: challenges and limitations. Free Radic Biol Med 52:1\u20136. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2011.09.030","journal-title":"Free Radic Biol Med"},{"key":"9914_CR29","doi-asserted-by":"publisher","first-page":"1121","DOI":"10.1038\/labinvest.2008.69","volume":"88","author":"K Ko","year":"2008","unstructured":"Ko K, Yang HP, Noureddin M, Iglesia-Ara A, Xia M, Wagner C, Luka Z, Mato JM, Lu SC (2008) Changes in S-adenosylmethionine and glutathione homeostasis during endotoxemia in mice. Lab Investig 88:1121\u20131129. https:\/\/doi.org\/10.1038\/labinvest.2008.69","journal-title":"Lab Investig"},{"key":"9914_CR30","doi-asserted-by":"publisher","first-page":"1248","DOI":"10.1096\/fj.00-0556fjev1","volume":"15","author":"MU Latasa","year":"2001","unstructured":"Latasa MU, Boukaba A, Garc\u00eda-Trevijano ER, Torres L, Rodr\u00edguez JL, Caballer\u00eda J, Lu SC, L\u00f3pez-Rodas G, Franco L, Mato JM, Avila MA (2001) Hepatocyte growth factor induces MAT2A expression and histone acetylation in rat hepatocytes: role in liver regeneration. FASEB J 15:1248\u20131250. https:\/\/doi.org\/10.1096\/fj.00-0556fjev1","journal-title":"FASEB J"},{"key":"9914_CR31","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1021\/tx00026a012","volume":"5","author":"CP LeBel","year":"1992","unstructured":"LeBel CP, Ischiropoulos H, Bondy SC (1992) Evaluation of the probe 2\u2032,7\u2032-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress. Chem Res Toxicol 5:227\u2013231. https:\/\/doi.org\/10.1021\/tx00026a012","journal-title":"Chem Res Toxicol"},{"key":"9914_CR32","doi-asserted-by":"publisher","first-page":"1021","DOI":"10.1007\/s10545-015-9863-3","volume":"38","author":"G Leipnitz","year":"2015","unstructured":"Leipnitz G, Vargas CR, Wajner M (2015) Disturbance of redox homeostasis as a contributing underlying pathomechanism of brain and liver alterations in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency. J Inherit Metab Dis 38:1021\u20131028. https:\/\/doi.org\/10.1007\/s10545-015-9863-3","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR33","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1007\/BF00785817","volume":"23","author":"E Lenartowicz","year":"1991","unstructured":"Lenartowicz E, Bernardi P, Azzone GF (1991) Phenylarsine oxide induces the cyclosporin A-sensitive membrane permeability transition in rat liver mitochondria. J Bioenerg Biomembr 23:679\u2013688. https:\/\/doi.org\/10.1007\/BF00785817","journal-title":"J Bioenerg Biomembr"},{"key":"9914_CR34","doi-asserted-by":"publisher","first-page":"1017","DOI":"10.1016\/j.bbrc.2003.08.105","volume":"309","author":"SS Leonard","year":"2003","unstructured":"Leonard SS, Xia C, Jiang BH, Stinefelt B, Klandorf H, Harris GK, Shi X (2003) Resveratrol scavenges reactive oxygen species and effects radical-induced cellular responses. Biochem Biophys Res Commun 309:1017\u20131026. https:\/\/doi.org\/10.1016\/j.bbrc.2003.08.105","journal-title":"Biochem Biophys Res Commun"},{"key":"9914_CR35","doi-asserted-by":"publisher","first-page":"192","DOI":"10.1124\/mol.108.054411","volume":"76","author":"TWH Li","year":"2009","unstructured":"Li TWH, Zhang Q, Oh P, Xia M, Chen H, Bemanian S, Lastra N, Circ M, Moyer MP, Mato JM, Aw TY, Lu SC (2009) S-adenosylmethionine and methylthioadenosine inhibit cellular FLICE inhibitory protein expression and induce apoptosis in colon cancer cells. Mol Pharmacol 76:192\u2013200. https:\/\/doi.org\/10.1124\/mol.108.054411","journal-title":"Mol Pharmacol"},{"key":"9914_CR36","doi-asserted-by":"publisher","first-page":"1068","DOI":"10.1016\/j.nbd.2011.12.025","volume":"45","author":"LP Liang","year":"2012","unstructured":"Liang LP, Waldbaum S, Rowley S, Huang TT, Day BJ, Patel M (2012) Mitochondrial oxidative stress and epilepsy in SOD2 deficient mice: attenuation by a lipophilic metalloporphyrin. Neurobiol Dis 45:1068\u20131076. https:\/\/doi.org\/10.1016\/j.nbd.2011.12.025","journal-title":"Neurobiol Dis"},{"key":"9914_CR37","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1042\/BST20060330","volume":"34","author":"WA Loenen","year":"2006","unstructured":"Loenen WA (2006) S-adenosylmethionine: Jack of all trades and master of everything? Biochem Soc Trans 34:330\u2013333. https:\/\/doi.org\/10.1042\/BST20060330","journal-title":"Biochem Soc Trans"},{"key":"9914_CR38","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","volume":"193","author":"OH Lowry","year":"1951","unstructured":"Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265\u2013275","journal-title":"J Biol Chem"},{"key":"9914_CR39","doi-asserted-by":"publisher","first-page":"1515","DOI":"10.1152\/physrev.00047.2011","volume":"92","author":"SC Lu","year":"2012","unstructured":"Lu SC, Mato JM (2012) S-adenosylmethionine in liver health, injury, and cancer. Physiol Rev 92:1515\u20131542. https:\/\/doi.org\/10.1152\/physrev.00047.2011","journal-title":"Physiol Rev"},{"key":"9914_CR40","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1179\/1351000213Y.0000000073","volume":"19","author":"OV Lushchak","year":"2014","unstructured":"Lushchak OV, Piroddi M, Galli F, Lushchak VI (2014) Aconitase post-translational modification as a key in linkage between Krebs cycle, iron homeostasis, redox signaling, and metabolism of reactive oxygen species. Redox Rep 19:8\u201315. https:\/\/doi.org\/10.1179\/1351000213Y.0000000073","journal-title":"Redox Rep"},{"key":"9914_CR41","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1016\/j.freeradbiomed.2017.06.013","volume":"110","author":"SL Menezes-Filho","year":"2017","unstructured":"Menezes-Filho SL, Amigo I, Prado FM, Ferreira NC, Koike MK, Pinto IFD, Miyamoto S, Montero EFS, Medeiros MHG, Kowaltowski AJ (2017) Caloric restriction protects livers from ischemia\/reperfusion damage by preventing Ca2+-induced mitochondrial permeability transition. Free Radic Biol Med 110:219\u2013227. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2017.06.013","journal-title":"Free Radic Biol Med"},{"key":"9914_CR42","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1007\/s10545-007-0798-1","volume":"31","author":"SR Mirandola","year":"2008","unstructured":"Mirandola SR, Melo DR, Schuck PF, Ferreira GC, Wajner M, Castilho RF (2008) Methylmalonate inhibits succinate-supported oxygen consumption by interfering with mitochondrial succinate uptake. J Inherit Metab Dis 31:44\u201354. https:\/\/doi.org\/10.1007\/s10545-007-0798-1","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR43","doi-asserted-by":"publisher","first-page":"298","DOI":"10.1016\/0006-291X(71)90102-1","volume":"42","author":"CL Moore","year":"1971","unstructured":"Moore CL (1971) Specific inhibition of mitochondrial Ca++ transport by ruthenium red. Biochem Biophys Res Commun 42:298\u2013305. https:\/\/doi.org\/10.1016\/0006-291X(71)90102-1","journal-title":"Biochem Biophys Res Commun"},{"key":"9914_CR44","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1042\/bj0580685","volume":"58","author":"JF Morrison","year":"1954","unstructured":"Morrison JF (1954) The activation of aconitase by ferrous ions and reducing agents. Biochem J 58:685\u2013692. https:\/\/doi.org\/10.1042\/bj0580685","journal-title":"Biochem J"},{"key":"9914_CR45","doi-asserted-by":"publisher","first-page":"448","DOI":"10.1023\/a:1010577512912","volume":"24","author":"SH Mudd","year":"2001","unstructured":"Mudd SH, Cerone R, Schiaffino MC, Fantasia AR, Minniti G, Caruso U, Lorini R, Watkins D, Matiaszuk N, Rosenblatt DS, Schwahn B, Rozen R, LeGros L, Kotb M, Capdevila A, Luka Z, Finkelstein JD, Tangerman A, Stabler SP, Allen RH, Wagner C (2001) Glycine N-methyltransferase deficiency: a novel inborn error causing persistent isolated hypermethioninemia. J Inherit Metab Dis 24:448\u2013464. https:\/\/doi.org\/10.1023\/a:1010577512912","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR46","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1093\/ajcn\/85.1.19","volume":"85","author":"SH Mudd","year":"2007","unstructured":"Mudd SH, Brosnan JT, Brosnan ME, Jacobs RL, Stabler SP, Allen RH, Vance DE, Wagner C (2007) Methyl balance and transmethylation fluxes in humans. Am J Clin Nutr 85:19\u201325. https:\/\/doi.org\/10.1093\/ajcn\/85.1.19","journal-title":"Am J Clin Nutr"},{"key":"9914_CR47","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1016\/j.ymgme.2011.11.006","volume":"105","author":"SH Mudd","year":"2012","unstructured":"Mudd SH, Wagner C, Luka Z, Stabler SP, Allen RH, Schroer R, Wood T, Wang J, Wong LJ (2012) Two patients with hepatic mtDNA depletion syndromes and marked elevations of S-adenosylmethionine and methionine. Mol Genet Metab 105:228\u2013236. https:\/\/doi.org\/10.1016\/j.ymgme.2011.11.006","journal-title":"Mol Genet Metab"},{"key":"9914_CR48","doi-asserted-by":"publisher","first-page":"1575","DOI":"10.1016\/S0006-2952(03)00083-2","volume":"65","author":"O Myhre","year":"2003","unstructured":"Myhre O, Andersen JM, Aarnes H, Fonnum F (2003) Evaluation of the probes 2\u2019,7\u2019-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation. Biochem Pharmacol 65:1575\u20131582. https:\/\/doi.org\/10.1016\/S0006-2952(03)00083-2","journal-title":"Biochem Pharmacol"},{"key":"9914_CR49","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1093\/clinchem\/44.3.679","volume":"44","author":"JA Navarro-Gonz\u00e1lvez","year":"1998","unstructured":"Navarro-Gonz\u00e1lvez JA, Garcia-Benayas C, Arenas J (1998) Semiautomated measurement of nitrate in biological fluids. Clin Chem 44:679\u2013681","journal-title":"Clin Chem"},{"key":"9914_CR50","doi-asserted-by":"publisher","first-page":"46","DOI":"10.4254\/wjh.v12.i2.46","volume":"12","author":"M Noureddin","year":"2020","unstructured":"Noureddin M, Sander-Struckmeier S, Mato JM (2020) Early treatment efficacy of S-adenosylmethionine in patients with intrahepatic cholestasis: a systematic review. World J Hepatol 12:46\u201363. https:\/\/doi.org\/10.4254\/wjh.v12.i2.46","journal-title":"World J Hepatol"},{"key":"9914_CR51","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1016\/j.jchromb.2005.04.025","volume":"827","author":"M Orioli","year":"2005","unstructured":"Orioli M, Aldini G, Beretta G, Facino RM, Carini M (2005) LC-ESI-MS\/MS determination of 4-hydroxy-trans-2-nonenal Michael adducts with cysteine and histidine-containing peptides as early markers of oxidative stress in excitable tissues. J Chromatogr B Analyt Technol Biomed Life Sci 827:109\u2013118. https:\/\/doi.org\/10.1016\/j.jchromb.2005.04.025","journal-title":"J Chromatogr B Analyt Technol Biomed Life Sci"},{"key":"9914_CR52","doi-asserted-by":"publisher","first-page":"1464","DOI":"10.1038\/ncb2868","volume":"15","author":"X Pan","year":"2013","unstructured":"Pan X, Liu J, Nguyen T, Liu C, Sun J, Teng Y, Fergusson MM, Rovira II, Allen M, Springer DA, Aponte AM, Gucek M, Balaban RS, Murphy E, Finkel T (2013) The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter. Nat Cell Biol 15:1464\u20131472. https:\/\/doi.org\/10.1038\/ncb2868","journal-title":"Nat Cell Biol"},{"key":"9914_CR53","doi-asserted-by":"publisher","first-page":"1951","DOI":"10.1016\/j.freeradbiomed.2004.08.021","volume":"37","author":"M Patel","year":"2004","unstructured":"Patel M (2004) Mitochondrial dysfunction and oxidative stress: cause and consequence of epileptic seizures. Free Radic Biol Med 37:1951\u20131962. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2004.08.021","journal-title":"Free Radic Biol Med"},{"key":"9914_CR54","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/j.ceca.2014.02.008","volume":"55","author":"D Pendin","year":"2014","unstructured":"Pendin D, Greotti E, Pozzan T (2014) The elusive importance of being a mitochondrial Ca(2+) uniporter. Cell Calcium 55:139\u2013145. https:\/\/doi.org\/10.1016\/j.ceca.2014.02.008","journal-title":"Cell Calcium"},{"key":"9914_CR55","unstructured":"Rakic B, Sinclair G, Stockler S, Vallance H (2015) Is glycine N-methyltransferase (GNMT) deficiency underdiagnosed? In: Garrod symposium \u201cmetabolic medicine in motion. book of abstracts, Vancouver, p 114"},{"key":"9914_CR56","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1016\/j.ceca.2011.04.007","volume":"50","author":"A Rasola","year":"2011","unstructured":"Rasola A, Bernardi P (2011) Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis. Cell Calcium 50:222\u2013233. https:\/\/doi.org\/10.1016\/j.ceca.2011.04.007","journal-title":"Cell Calcium"},{"key":"9914_CR57","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1016\/s0076-6879(94)33041-7","volume":"233","author":"AZ Reznick","year":"1994","unstructured":"Reznick AZ, Packer L (1994) Oxidative damage to proteins: spectrophotometric method for carbonyl assay. Methods Enzymol 233:357\u2013363. https:\/\/doi.org\/10.1016\/s0076-6879(94)33041-7","journal-title":"Methods Enzymol"},{"key":"9914_CR58","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbadis.2020.165682","volume":"1866","author":"AC Roginski","year":"2020","unstructured":"Roginski AC, Wajner A, Cecatto C, Wajner SM, Castilho RF, Wajner M, Amaral AU (2020) Disturbance of bioenergetics and calcium homeostasis provoked by metabolites accumulating in propionic acidemia in heart mitochondria of developing rats. Biochim Biophys Acta Mol Basis Dis 1866:165682. https:\/\/doi.org\/10.1016\/j.bbadis.2020.165682","journal-title":"Biochim Biophys Acta Mol Basis Dis"},{"key":"9914_CR59","doi-asserted-by":"publisher","first-page":"1667","DOI":"10.1007\/s11064-010-0228-x","volume":"35","author":"A Saito","year":"2010","unstructured":"Saito A, Castilho RF (2010) Inhibitory effects of adenine nucleotides on brain mitochondrial permeability transition. Neurochem Res 35:1667\u20131674. https:\/\/doi.org\/10.1007\/s11064-010-0228-x","journal-title":"Neurochem Res"},{"key":"9914_CR60","doi-asserted-by":"publisher","first-page":"2479","DOI":"10.1007\/s00726-016-2302-4","volume":"48","author":"BM Schweinberger","year":"2016","unstructured":"Schweinberger BM, Wyse AT (2016) Mechanistic basis of hypermethioninemia. Amino Acids 48:2479\u20132489. https:\/\/doi.org\/10.1007\/s00726-016-2302-4","journal-title":"Amino Acids"},{"key":"9914_CR61","doi-asserted-by":"publisher","first-page":"2760","DOI":"10.1007\/s12035-018-1275-6","volume":"56","author":"B Seminotti","year":"2019","unstructured":"Seminotti B, Zanatta \u00c2, Ribeiro RT, da Rosa MS, Wyse ATS, Leipnitz G, Wajner M (2019) Disruption of brain redox homeostasis, microglia activation and neuronal damage induced by intracerebroventricular administration of S-adenosylmethionine to developing rats. Mol Neurobiol 56:2760\u20132773. https:\/\/doi.org\/10.1007\/s12035-018-1275-6","journal-title":"Mol Neurobiol"},{"key":"9914_CR62","doi-asserted-by":"publisher","first-page":"1233","DOI":"10.1007\/s12035-019-01825-0","volume":"57","author":"B Seminotti","year":"2020","unstructured":"Seminotti B, da Silva JC, Ribeiro RT, Leipnitz G, Wajner M (2020) Free radical scavengers prevent argininosuccinic acid-induced oxidative stress in the brain of developing rats: A new adjuvant therapy for argininosuccinate lyase deficiency? Mol Neurobiol 57:1233\u20131244. https:\/\/doi.org\/10.1007\/s12035-019-01825-0","journal-title":"Mol Neurobiol"},{"key":"9914_CR63","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1016\/j.mcn.2012.07.005","volume":"55","author":"AA Starkov","year":"2013","unstructured":"Starkov AA (2013) An update on the role of mitochondrial \u03b1-ketoglutarate dehydrogenase in oxidative stress. Mol Cell Neurosci 55:13\u201316. https:\/\/doi.org\/10.1016\/j.mcn.2012.07.005","journal-title":"Mol Cell Neurosci"},{"key":"9914_CR64","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1007\/s10545-015-9904-y","volume":"39","author":"C Staufner","year":"2016","unstructured":"Staufner C, Lindner M, Dionisi-Vici C, Freisinger P, Dobbelaere D, Douillard C, Makhseed N, Straub BK, Kahrizi K, Ballhausen D, la Marca G, K\u00f6lker S, Haas D, Hoffmann GF, Gr\u00fcnert SC, Blom HJ (2016) Adenosine kinase deficiency: expanding the clinical spectrum and evaluating therapeutic options. J Inherit Metab Dis 39:273\u2013283. https:\/\/doi.org\/10.1007\/s10545-015-9904-y","journal-title":"J Inherit Metab Dis"},{"key":"9914_CR65","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1016\/j.ymgme.2015.10.009","volume":"116","author":"S Stender","year":"2015","unstructured":"Stender S, Chakrabarti RS, Xing C, Gotway G, Cohen JC, Hobbs HH (2015) Adult-onset liver disease and hepatocellular carcinoma in S-adenosylhomocysteine hydrolase deficiency. Mol Genet Metab 116:269\u2013274. https:\/\/doi.org\/10.1016\/j.ymgme.2015.10.009","journal-title":"Mol Genet Metab"},{"key":"9914_CR66","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1016\/j.ymgme.2015.06.005","volume":"116","author":"KA Strauss","year":"2015","unstructured":"Strauss KA, Ferreira C, Bottiglieri T, Zhao X, Arning E, Zhang S, Zeisel SH, Escolar ML, Presnick N, Puffenberger EG, Vugrek O, Kovacevic L, Wagner C, Mazariegos GV, Mudd SH, Soltys K (2015) Liver transplantation for treatment of severe S-adenosylhomocysteine hydrolase deficiency. Mol Genet Metab 116:44\u201352. https:\/\/doi.org\/10.1016\/j.ymgme.2015.06.005","journal-title":"Mol Genet Metab"},{"key":"9914_CR67","doi-asserted-by":"publisher","first-page":"166","DOI":"10.1111\/j.1432-1033.1996.0166q.x","volume":"238","author":"A Tanveer","year":"1996","unstructured":"Tanveer A, Virji S, Andreeva L, Totty NF, Hsuan JJ, Ward JM, Crompton M (1996) Involvement of cyclophilin D in the activation of a mitochondrial pore by Ca2+ and oxidant stress. Eur J Biochem 238:166\u2013172. https:\/\/doi.org\/10.1111\/j.1432-1033.1996.0166q.x","journal-title":"Eur J Biochem"},{"key":"9914_CR68","doi-asserted-by":"publisher","first-page":"8972","DOI":"10.1523\/JNEUROSCI.20-24-08972.2000","volume":"20","author":"L Tretter","year":"2000","unstructured":"Tretter L, Adam-Vizi V (2000) Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J Neurosci 20:8972\u20138979. https:\/\/doi.org\/10.1523\/JNEUROSCI.20-24-08972.2000","journal-title":"J Neurosci"},{"key":"9914_CR69","doi-asserted-by":"publisher","first-page":"7771","DOI":"10.1523\/JNEUROSCI.1842-04.2004","volume":"24","author":"L Tretter","year":"2004","unstructured":"Tretter L, Adam-Vizi V (2004) Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase. J Neurosci 24:7771\u20137778. https:\/\/doi.org\/10.1523\/JNEUROSCI.1842-04.2004","journal-title":"J Neurosci"},{"key":"9914_CR70","doi-asserted-by":"publisher","first-page":"2335","DOI":"10.1098\/rstb.2005.1764","volume":"360","author":"L Tretter","year":"2005","unstructured":"Tretter L, Adam-Vizi V (2005) Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress. Philos Trans R Soc Lond B Biol Sci 360:2335\u20132345. https:\/\/doi.org\/10.1098\/rstb.2005.1764","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"9914_CR71","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1006\/abbi.1993.1551","volume":"307","author":"VG Valle","year":"1993","unstructured":"Valle VG, Fagian MM, Parentoni LS, Meinicke AR, Vercesi AE (1993) The participation of reactive oxygen species and protein thiols in the mechanism of mitochondrial inner membrane permeabilization by calcium plus prooxidants. Arch Biochem Biophys 307:1\u20137. https:\/\/doi.org\/10.1006\/abbi.1993.1551","journal-title":"Arch Biochem Biophys"},{"key":"9914_CR72","doi-asserted-by":"publisher","first-page":"14064","DOI":"10.1074\/jbc.275.19.14064","volume":"275","author":"J Vasquez-Vivar","year":"2000","unstructured":"Vasquez-Vivar J, Kalyanaraman B, Kennedy MC (2000) Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation. J Biol Chem 275:14064\u201314069. https:\/\/doi.org\/10.1074\/jbc.275.19.14064","journal-title":"J Biol Chem"},{"key":"9914_CR73","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2018.08.034","volume":"29","author":"AE Vercesi","year":"2018","unstructured":"Vercesi AE, Castilho RF, Kowaltowski AJ, de Oliveira HCF, de Souza-Pinto NC, Figueira TR, Busanello ENB (2018) Mitochondrial calcium transport and the redox nature of the calcium-induced membrane permeability transition. Free Radic Biol Med 29:1\u201324. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2018.08.034","journal-title":"Free Radic Biol Med"},{"key":"9914_CR74","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1042\/bj3420021","volume":"342","author":"WH Watson","year":"1999","unstructured":"Watson WH, Zhao Y, Chawla RK (1999) S-adenosylmethionine attenuates the lipopolysaccharide-induced expression of the gene for tumour necrosis factor alpha. Biochem J 342:21\u201325","journal-title":"Biochem J"},{"key":"9914_CR75","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1002\/hep.20274","volume":"40","author":"H Yang","year":"2004","unstructured":"Yang H, Sadda MR, Li M, Zeng Y, Chen L, Bae W, Ou X, Runnegar MT, Mato JM, Lu SC (2004) S-adenosylmethionine and its metabolite induce apoptosis in HepG2 cells: Role of protein phosphatase 1 and Bcl-x(S). Hepatology 40:221\u2013231. https:\/\/doi.org\/10.1002\/hep.20274","journal-title":"Hepatology"},{"key":"9914_CR76","doi-asserted-by":"publisher","first-page":"1982","DOI":"10.1002\/hep.22908","volume":"49","author":"HP Yang","year":"2009","unstructured":"Yang HP, Ramani K, Xia M, Ko KS, Li TWH, Oh P, Li J, Lu SC (2009) Dysregulation of glutathione synthesis during cholestasis in mice: molecular mechanisms and therapeutic implications. Hepatology 49:1982\u20131991. https:\/\/doi.org\/10.1002\/hep.22908","journal-title":"Hepatology"},{"key":"9914_CR77","doi-asserted-by":"publisher","first-page":"5868","DOI":"10.1007\/s12035-017-0804-z","volume":"55","author":"\u00c2 Zanatta","year":"2018","unstructured":"Zanatta \u00c2, Cecatto C, Ribeiro RT, Amaral AU, Wyse AT, Leipnitz G, Wajner M (2018) S-adenosylmethionine promotes oxidative stress and decreases Na+, K+-ATPase activity in cerebral cortex supernatants of adolescent rats: implications for the pathogenesis of S-adenosylhomocysteine hydrolase deficiency. Mol Neurobiol 55:5868\u20135878. https:\/\/doi.org\/10.1007\/s12035-017-0804-z","journal-title":"Mol Neurobiol"}],"container-title":["Journal of Bioenergetics and Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10863-021-09914-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s10863-021-09914-3\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10863-021-09914-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,13]],"date-time":"2021-09-13T21:30:15Z","timestamp":1631568615000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s10863-021-09914-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8,4]]},"references-count":77,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2021,10]]}},"alternative-id":["9914"],"URL":"https:\/\/doi.org\/10.1007\/s10863-021-09914-3","relation":{},"ISSN":["0145-479X","1573-6881"],"issn-type":[{"value":"0145-479X","type":"print"},{"value":"1573-6881","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,8,4]]},"assertion":[{"value":"19 February 2021","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 July 2021","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 August 2021","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 they have no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"The experimental protocol followed the national animal rights regulation (Law 11.794\/2008) and the \u201cGuide for the Care and Use of Laboratory Animals\u201d (National Institutes of Health, 8th edition, revised 2011) and Directive 2010\/63\/EU. All efforts were made to minimize the number of animals and their suffering.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to participate"}},{"value":"Not applicable.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}}]}}