{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,28]],"date-time":"2026-05-28T04:02:13Z","timestamp":1779940933056,"version":"3.53.1"},"reference-count":52,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Cell Tissue Res"],"published-print":{"date-parts":[[2026,5]]},"DOI":"10.1007\/s00441-026-04069-2","type":"journal-article","created":{"date-parts":[[2026,5,17]],"date-time":"2026-05-17T23:21:02Z","timestamp":1779060062000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The subcellular distribution of methionine sulfoxide reductase A in mouse and human tissues"],"prefix":"10.1007","volume":"404","author":[{"given":"Hans","family":"Agricola","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Lesser","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Reinhard","family":"Wetzker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,5,18]]},"reference":[{"issue":"2","key":"4069_CR1","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1007\/s00441-024-03915","volume":"398","author":"H Agricola","year":"2024","unstructured":"Agricola H, Braeunig P (2024) The complex neurochemistry of the cockroach antennal heart. Cell Tissue Res 398(2):139\u2013160. https:\/\/doi.org\/10.1007\/s00441-024-03915","journal-title":"Cell Tissue Res"},{"key":"4069_CR2","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1111\/j.1474-9726.2010.00657.x","volume":"10","author":"JC Aledo","year":"2011","unstructured":"Aledo JC, Li Y, de Magalh\u00e3es JP, Ruiz\u2010Camacho M, P\u00e9rez\u2010Claros JA (2011) Mitochondrially encoded methionine is inversely related to longevity in mammals. Aging Cell 10:198\u2013207","journal-title":"Aging Cell"},{"issue":"4","key":"4069_CR3","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1016\/j.cell.2005.02.001","volume":"120","author":"RS Balaban","year":"2005","unstructured":"Balaban RS, Nemoto S, Finkel T (2005) Mitochondria, oxidants, and aging. Cell 120(4):483\u2013495. https:\/\/doi.org\/10.1016\/j.cell.2005.02.001","journal-title":"Cell"},{"issue":"2","key":"4069_CR4","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1016\/j.exer.2008.05.018","volume":"88","author":"LA Brennan","year":"2009","unstructured":"Brennan LA, Kantorow M (2009) Mitochondrial function and redox control in the aging eye: role of MsrA and other repair systems in cataract and macular degenerations. Exp Eye Res 88(2):195\u2013203. https:\/\/doi.org\/10.1016\/j.exer.2008.05.018","journal-title":"Exp Eye Res"},{"issue":"1-3","key":"4069_CR5","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1089\/ars.2023.0252","volume":"41","author":"C Chahla","year":"2024","unstructured":"Chahla C, Kovacic H, Ferhat L, Leloup L (2024) Pathological impact of redox post-translational modifications. Antioxid Redox Signal 41(1\u20133):152\u2013180. https:\/\/doi.org\/10.1089\/ars.2023.0252","journal-title":"Antioxid Redox Signal"},{"issue":"3","key":"4069_CR6","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1152\/physrev.1979.59.3.527","volume":"59","author":"B Chance","year":"1979","unstructured":"Chance B, Sies H, Boveris A (1979) Hydroperoxide metabolism in mammalian organs. Physiol Rev 59(3):527\u2013605. https:\/\/doi.org\/10.1152\/physrev.1979.59.3.527","journal-title":"Physiol Rev"},{"issue":"11","key":"4069_CR7","doi-asserted-by":"publisher","first-page":"1703","DOI":"10.1261\/rna.079643.123","volume":"29","author":"JR Child","year":"2023","unstructured":"Child JR, Hofler AC, Chen Q, Yang BH, Kristofich JC, Zheng T, Hannigan MM, Elles AL, Reid DW, Nicchitta CV (2023) Examining SRP pathway function in mRNA localization to the endoplasmic reticulum. RNA 29(11):1703\u20131724. https:\/\/doi.org\/10.1261\/rna.079643.123","journal-title":"RNA"},{"issue":"12","key":"4069_CR8","doi-asserted-by":"publisher","DOI":"10.3390\/antiox7120191","volume":"7","author":"S Louren\u00e7o Dos Santos","year":"2018","unstructured":"dos Santos LS, Petropoulos I, Friguet B (2018) The oxidized protein repair enzymes methionine sulfoxide reductases and their roles in protecting against oxidative stress, in ageing and in regulating protein function. Antioxidants (Basel) 7(12):191. https:\/\/doi.org\/10.3390\/antiox7120191","journal-title":"Antioxidants (Basel)"},{"key":"4069_CR9","doi-asserted-by":"publisher","unstructured":"Fairley JA, Gilmour K, Walsh K (2012) Making the most of pathological specimens: molecular diagnosis in formalin-fi xed, paraffi n embedded tissue. Curr Drug Targets 13(12):1475\u20131487.\u00a0https:\/\/doi.org\/10.2174\/138945012803530125","DOI":"10.2174\/138945012803530125"},{"issue":"10","key":"4069_CR10","doi-asserted-by":"publisher","first-page":"3307","DOI":"10.1083\/JCB.201901001","volume":"218","author":"YHH Fu","year":"2019","unstructured":"Fu YHH, Chandrasekar S, Lee JH, Shan SO (2019) A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting. J Cell Biol 218(10):3307\u20133319. https:\/\/doi.org\/10.1083\/JCB.201901001","journal-title":"J Cell Biol"},{"issue":"11-12","key":"4069_CR11","doi-asserted-by":"publisher","first-page":"978","DOI":"10.1080\/10715760802566541","volume":"42","author":"R Haenold","year":"2008","unstructured":"Haenold R, Wassef R, Brot N et al (2008) Protection of vascular smooth muscle cells by over-expressed methionine sulphoxide reductase A: role of intracellular localization and substrate availability. Free Radic Res 42(11\u201312):978\u2013988. https:\/\/doi.org\/10.1080\/10715760802566541","journal-title":"Free Radic Res"},{"issue":"2","key":"4069_CR12","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/j.bbapap.2004.09.010","volume":"1703","author":"A Hansel","year":"2005","unstructured":"Hansel A, Heinemann SH, Hoshi T (2005) Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation. Biochim Biophys Acta 1703(2):239\u2013247. https:\/\/doi.org\/10.1016\/j.bbapap.2004.09.010","journal-title":"Biochim Biophys Acta"},{"issue":"8","key":"4069_CR13","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1096\/fj.01-0737fje","volume":"16","author":"A Hansel","year":"2002","unstructured":"Hansel A, Kuschel L, Hehl S, Lemke C, Agricola HJ, Hoshi T, Heinemann SH (2002) Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. FASEB J 16(8):911\u2013913. https:\/\/doi.org\/10.1096\/fj.01-0737fje","journal-title":"FASEB J"},{"key":"4069_CR14","unstructured":"Harlow E, Lane D (1988) Antibodies, a laboratory manual. Cold Spring Harbor, Cold Spring Harbor Laboratory 1988"},{"issue":"10","key":"4069_CR15","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1016\/j.tcb.2011.06.008","volume":"21","author":"S Hekimi","year":"2011","unstructured":"Hekimi S, Lapointe J, Wen Y (2011) Taking a \u201cgood\u201d look at free radicals in the aging process. Trends Cell Biol 21(10):569\u2013576. https:\/\/doi.org\/10.1016\/j.tcb.2011.06.008","journal-title":"Trends Cell Biol"},{"key":"4069_CR16","doi-asserted-by":"publisher","unstructured":"Hoshi T, Heinemann S (2001) Regulation of cell function by methionine oxidation and reduction. J Physiol 531(Pt 1):1\u201311. https:\/\/doi.org\/10.1111\/j.1469-7793.2001.0001j.x","DOI":"10.1111\/j.1469-7793.2001.0001j.x"},{"key":"4069_CR17","unstructured":"Human Protein Atlas (n.d.) https:\/\/www.proteinatlas.org"},{"issue":"3","key":"4069_CR18","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1161\/01.res.87.3.179","volume":"87","author":"K Irani","year":"2000","unstructured":"Irani K (2000) Oxidant signaling in vascular cell growth, death, and survival\u202f: a review of the roles of reactive oxygen species in smooth muscle and endothelial cell mitogenic and apoptotic signaling. Circ Res 87(3):179\u2013183. https:\/\/doi.org\/10.1161\/01.res.87.3.179","journal-title":"Circ Res"},{"key":"4069_CR19","doi-asserted-by":"publisher","DOI":"10.1155\/2019\/2471312","volume":"2019","author":"A Jankovic","year":"2019","unstructured":"Jankovic A, Saso L, Korac A, Korac B (2019) Relation of redox and structural alterations of rat skin in the function of chronological aging. Oxid Med Cell Longev 2019:2471312. https:\/\/doi.org\/10.1155\/2019\/2471312","journal-title":"Oxid Med Cell Longev"},{"key":"4069_CR20","doi-asserted-by":"publisher","first-page":"1562","DOI":"10.1134\/S0006297914130082","volume":"79","author":"EV Kalinina","year":"2014","unstructured":"Kalinina EV, Chernov NN, Novichkova MD (2014) Role of glutathione, glutathione transferase, and glutaredoxin in regulation of redox-dependent processes. Biochemistry 79:1562\u20131583. https:\/\/doi.org\/10.1134\/S0006297914130082","journal-title":"Biochemistry"},{"key":"4069_CR21","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1016\/j.exer.2010.09.007","volume":"100","author":"M Kantorow","year":"2012","unstructured":"Kantorow M, Lee W, Chauss D (2012) Focus on molecules: methionine sulfoxide reductase A. Exp Eye Res 100:110\u2013111","journal-title":"Exp Eye Res"},{"issue":"1","key":"4069_CR22","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2199-7-11","volume":"7","author":"HY Kim","year":"2006","unstructured":"Kim HY, Gladyshev VN (2006) Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases. BMC Mol Biol 7(1):11. https:\/\/doi.org\/10.1186\/1471-2199-7-11","journal-title":"BMC Mol Biol"},{"issue":"3","key":"4069_CR23","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1042\/BJ20070929","volume":"407","author":"HY Kim","year":"2007","unstructured":"Kim HY, Gladyshev VN (2007) Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem J 407(3):321\u2013329. https:\/\/doi.org\/10.1042\/BJ20070929","journal-title":"Biochem J"},{"key":"4069_CR24","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1093\/abbs\/gmu011","volume":"46","author":"JY Kim","year":"2014","unstructured":"Kim JY, Kim Y, Kwak GH, Oh SY, Kim HY (2014) Over-expression of methionine sulfoxide reductase A in the endoplasmic reticulum increases resistance to oxidative and ER stresses. Acta Biochim Biophys Sin 46:415\u2013419. https:\/\/doi.org\/10.1093\/abbs\/gmu011","journal-title":"Acta Biochim Biophys Sin"},{"issue":"3-4","key":"4069_CR25","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1515\/BC.2002.047","volume":"383","author":"LO Klotz","year":"2002","unstructured":"Klotz LO (2002) Oxidant-induced signaling: effects of peroxynitrite and singlet oxygen. Biol Chem 383(3\u20134):443\u2013456. https:\/\/doi.org\/10.1515\/BC.2002.047","journal-title":"Biol Chem"},{"issue":"1","key":"4069_CR26","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/s0014-5793(99)00917-5","volume":"456","author":"L Kuschel","year":"1999","unstructured":"Kuschel L, Hansel A, Sch\u00f6nherr R et al (1999) Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett 456(1):17\u201321. https:\/\/doi.org\/10.1016\/s0014-5793(99)00917-5","journal-title":"FEBS Lett"},{"issue":"6","key":"4069_CR27","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0131523","volume":"10","author":"EH Lee","year":"2015","unstructured":"Lee EH, Lee K, Kwak GH, Park YS, Lee KJ, Hwang KY, Kim HY (2015) Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii. PLoS ONE 10(6):e0131523. https:\/\/doi.org\/10.1371\/journal.pone.0131523","journal-title":"PLoS ONE"},{"issue":"5","key":"4069_CR28","doi-asserted-by":"publisher","first-page":"816","DOI":"10.1016\/j.exer.2005.10.003","volume":"82","author":"JW Lee","year":"2006","unstructured":"Lee JW, Gordiyenko NV, Marchetti M et al (2006) Gene structure, localization and role in oxidative stress of methionine sulfoxide reductase A (MSRA) in the monkey retina. Exp Eye Res 82(5):816\u2013827. https:\/\/doi.org\/10.1016\/j.exer.2005.10.003","journal-title":"Exp Eye Res"},{"issue":"4","key":"4069_CR29","doi-asserted-by":"publisher","first-page":"256","DOI":"10.5483\/BMBRep.2011.44.4.256","volume":"44","author":"TH Lee","year":"2011","unstructured":"Lee TH, Choi SH, Kim HY (2011) The protein truncation caused by fusion of PEP-1 peptide and protective roles of transduced PEP-1-MsrA in skin cells. BMB Rep 44(4):256\u2013261. https:\/\/doi.org\/10.5483\/BMBRep.2011.44.4.256","journal-title":"BMB Rep"},{"issue":"4","key":"4069_CR30","doi-asserted-by":"publisher","DOI":"10.3390\/ijms26041495","volume":"26","author":"S Li","year":"2025","unstructured":"Li S, Wang X, Liu G, Li F (2025) Methionine modulates the growth and development of heat-stressed dermal papilla cells via the Wnt\/\u03b2-catenin signaling pathway. Int J Mol Sci 26(4):1495. https:\/\/doi.org\/10.3390\/ijms26041495","journal-title":"Int J Mol Sci"},{"key":"4069_CR31","doi-asserted-by":"publisher","unstructured":"Lim VJT, Tabassum NI, Orian JM, Arumugam TV, Weng EF (2025) Hormesis and brain diseases. Prog Brain Res 295:229\u2013258.\u00a0https:\/\/doi.org\/10.1016\/bs.pbr.2025.05.003","DOI":"10.1016\/bs.pbr.2025.05.003"},{"issue":"7","key":"4069_CR32","doi-asserted-by":"publisher","DOI":"10.3390\/antiox12071374","volume":"12","author":"P Lohana","year":"2023","unstructured":"Lohana P, Suryaprawira A, Woods EL et al (2023) Role of enzymic antioxidants in mediating oxidative stress and contrasting wound healing capabilities in oral mucosal\/skin fibroblasts and tissues. Antioxidants 12(7):1374. https:\/\/doi.org\/10.3390\/antiox12071374","journal-title":"Antioxidants"},{"key":"4069_CR33","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.freeradbiomed.2013.07.036","volume":"66","author":"J Lu","year":"2014","unstructured":"Lu J, Holmgren A (2014) The thioredoxin antioxidant system. Free Radic Biol Med 66:75\u201387. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2013.07.036","journal-title":"Free Radic Biol Med"},{"key":"4069_CR34","doi-asserted-by":"publisher","unstructured":"Moskovitz J, Weissbach H, Brot N ( 1996) Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc Natl Acad Sci 93(5):2095\u20139. https:\/\/doi.org\/10.1073\/pnas.93.5.2095","DOI":"10.1073\/pnas.93.5.2095"},{"issue":"23","key":"4069_CR35","doi-asserted-by":"publisher","first-page":"12920","DOI":"10.1073\/pnas.231472998","volume":"98","author":"J Moskovitz","year":"2001","unstructured":"Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER (2001) Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci U S A 98(23):12920\u201312925. https:\/\/doi.org\/10.1073\/pnas.231472998","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"4069_CR36","doi-asserted-by":"publisher","first-page":"1128","DOI":"10.1038\/sj.jid.5700116","volume":"126","author":"F Ogawa","year":"2006","unstructured":"Ogawa F, Sander CS, Hansel A et al (2006) The repair enzyme peptide methionine-S-sulfoxide reductase is expressed in human epidermis and upregulated by UVA radiation. J Invest Dermatol 126(5):1128\u20131134. https:\/\/doi.org\/10.1038\/sj.jid.5700116","journal-title":"J Invest Dermatol"},{"issue":"1","key":"4069_CR37","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.ygeno.2008.09.002","volume":"93","author":"I Pascual","year":"2009","unstructured":"Pascual I, Larrayoz IM, Rodriguez IR (2009) Retinoic acid regulates the human methionine sulfoxide reductase A (MSRA) gene via two distinct promoters. Genomics 93(1):62\u201371. https:\/\/doi.org\/10.1016\/j.ygeno.2008.09.002","journal-title":"Genomics"},{"issue":"3","key":"4069_CR38","doi-asserted-by":"publisher","first-page":"819","DOI":"10.1042\/bj3550819","volume":"355","author":"I Petropoulos","year":"2001","unstructured":"Petropoulos I, Mary J, Perichon M, Friguet B (2001) Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 355(3):819\u2013825. https:\/\/doi.org\/10.1042\/bj3550819","journal-title":"Biochem J"},{"issue":"9","key":"4069_CR39","doi-asserted-by":"publisher","first-page":"859","DOI":"10.1016\/j.exger.2007.02.006","volume":"42","author":"CR Picot","year":"2007","unstructured":"Picot CR, Moreau M, Juan M et al (2007) Impairment of methionine sulfoxide reductase during UV irradiation and photoaging. Exp Gerontol 42(9):859\u2013863. https:\/\/doi.org\/10.1016\/j.exger.2007.02.006","journal-title":"Exp Gerontol"},{"issue":"10","key":"4069_CR40","doi-asserted-by":"publisher","first-page":"1332","DOI":"10.1016\/j.freeradbiomed.2005.06.017","volume":"39","author":"CR Picot","year":"2005","unstructured":"Picot CR, Petropoulos I, Perichon M, Moreau M, Nizard C, Friguet B (2005) Overexpression of MsrA protects WI-38 SV40 human fibroblasts against H2O2-mediated oxidative stress. Free Radic Biol Med 39(10):1332\u20131341. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2005.06.017","journal-title":"Free Radic Biol Med"},{"issue":"5","key":"4069_CR41","doi-asserted-by":"publisher","first-page":"2748","DOI":"10.1073\/pnas.032671199","volume":"99","author":"H Ruan","year":"2002","unstructured":"Ruan H, Tang XD, Chen ML, Joiner ML, Sun G, Brot N, Weissbach H, Heinemann SH, Iverson L, Wu CF, Hoshi T (2002) High-quality life extension by the enzyme peptide methionine sulfoxide reductase. Proc Natl Acad Sci U S A 99(5):2748\u20132753. https:\/\/doi.org\/10.1073\/pnas.032671199","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1-3","key":"4069_CR42","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1080\/10409238.2025.2503746","volume":"60","author":"WN S\u00e1nchez","year":"2025","unstructured":"S\u00e1nchez WN, Driessen AJM, Wilson CAM (2025) Protein targeting to the ER membrane: multiple pathways and shared machinery. Crit Rev Biochem Mol Biol 60(1\u20133):33\u201379. https:\/\/doi.org\/10.1080\/10409238.2025.2503746","journal-title":"Crit Rev Biochem Mol Biol"},{"issue":"1","key":"4069_CR43","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1016\/j.bbrc.2006.01.124","volume":"342","author":"KU Schallreuter","year":"2006","unstructured":"Schallreuter KU, R\u00fcbsam K, Chavan B et al (2006) Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. Biochem Biophys Res Commun 342(1):145\u2013152. https:\/\/doi.org\/10.1016\/j.bbrc.2006.01.124","journal-title":"Biochem Biophys Res Commun"},{"key":"4069_CR44","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1038\/s41580-020-0230-3","volume":"21","author":"H Sies","year":"2020","unstructured":"Sies H, Jones DP (2020) Reactive oxygen species (ROS) as pleiotropic physiological signalling agents. Nat Rev Mol Cell Biol 21:363\u2013383. https:\/\/doi.org\/10.1038\/s41580-020-0230-3","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"5","key":"4069_CR45","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1097\/DAD.0b013e3181882c21","volume":"31","author":"WM Taungjaruwinai","year":"2009","unstructured":"Taungjaruwinai WM, Bhawan J, Keady M, Thiele JJ (2009) Differential expression of the antioxidant repair enzyme methionine sulfoxide reductase (MSRA and MSRB) in human skin. Am J Dermatopathol 31(5):427\u2013431. https:\/\/doi.org\/10.1097\/DAD.0b013e3181882c21","journal-title":"Am J Dermatopathol"},{"key":"4069_CR46","doi-asserted-by":"publisher","unstructured":"Thyne KM, Camones R, Salmon AB (2023) Sulfur amino acid restriction alters mitochondrial function depending on tissue, sex, and methionine sulfoxide reductase A (MsrA) status. Preprint.\u00a0Res Sq 2023;rs.3.rs-3755231. https:\/\/doi.org\/10.21203\/rs.3.rs-3755231\/v1","DOI":"10.21203\/rs.3.rs-3755231\/v1"},{"issue":"1","key":"4069_CR47","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1007\/BF00319134","volume":"282","author":"J Ude","year":"1995","unstructured":"Ude J, Agricola H (1995) FMRFamide-like and allatostatin-like immunoreactivity in the lateral heart nerve of Periplaneta americana: colocalization at the electron-microscopic level. Cell Tissue Res 282(1):69\u201380. https:\/\/doi.org\/10.1007\/BF00319134","journal-title":"Cell Tissue Res"},{"key":"4069_CR48","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1042\/bj20030443","volume":"373","author":"S Vougier","year":"2003","unstructured":"Vougier S, Mary J, Friguet B (2003) Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. Biochem J 373:531\u2013537","journal-title":"Biochem J"},{"issue":"3","key":"4069_CR49","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1002\/ajhb.21137","volume":"23","author":"Z Wang","year":"2011","unstructured":"Wang Z, Ying Z, Bosy-Westphal A et al (2011) Evaluation of specific metabolic rates of major organs and tissues: comparison between men and women. Am J Hum Biol 23(3):333\u2013338. https:\/\/doi.org\/10.1002\/ajhb.21137","journal-title":"Am J Hum Biol"},{"issue":"1","key":"4069_CR50","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1038\/s42003-025-07909-z","volume":"8","author":"Y Yao","year":"2025","unstructured":"Yao Y, Erkamp N, Sneideris T, Yang X, Scrutton R, Schneider MM, Fischer CM, Schoenmakers E, Schoenmakers N, Knowles TPJ (2025Mar 21) Extracellular phase separation mediates storage and release of thyroglobulin in the thyroid follicular lumen. Commun Biol 8(1):466. https:\/\/doi.org\/10.1038\/s42003-025-07909-z","journal-title":"Commun Biol"},{"issue":"3","key":"4069_CR51","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1111\/j.1469-185X.2008.00042.x","volume":"83","author":"XH Zhang","year":"2008","unstructured":"Zhang XH, Weissbach H (2008) Origin and evolution of the protein-repairing enzymes methionine sulphoxide reductases. Biol Rev Camb Philos Soc 83(3):249\u2013257. https:\/\/doi.org\/10.1111\/j.1469-185X.2008.00042.x","journal-title":"Biol Rev Camb Philos Soc"},{"issue":"3","key":"4069_CR52","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1111\/apha.12515","volume":"214","author":"L Zuo","year":"2015","unstructured":"Zuo L, Zhou T, Pannell BK, Ziegler AC, Best TM (2015) Biological and physiological role of reactive oxygen species\u2013the good, the bad and the ugly. Acta Physiol (Oxf) 214(3):329\u2013348. https:\/\/doi.org\/10.1111\/apha.12515","journal-title":"Acta Physiol (Oxf)"}],"container-title":["Cell and Tissue Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00441-026-04069-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00441-026-04069-2","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00441-026-04069-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,28]],"date-time":"2026-05-28T03:03:39Z","timestamp":1779937419000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00441-026-04069-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5]]},"references-count":52,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2026,5]]}},"alternative-id":["4069"],"URL":"https:\/\/doi.org\/10.1007\/s00441-026-04069-2","relation":{},"ISSN":["0302-766X","1432-0878"],"issn-type":[{"value":"0302-766X","type":"print"},{"value":"1432-0878","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5]]},"assertion":[{"value":"3 February 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"15 April 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 May 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":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}],"article-number":"12"}}