{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T01:02:16Z","timestamp":1780448536451,"version":"3.54.1"},"reference-count":99,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,4,4]],"date-time":"2026-04-04T00:00:00Z","timestamp":1775260800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T00:00:00Z","timestamp":1780444800000},"content-version":"vor","delay-in-days":60,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100002915","name":"Fondation pour la Recherche M\u00e9dicale","doi-asserted-by":"publisher","award":["Prix MARIE_PAULE BURRUS 2024 \u2013 PRS202407019918"],"award-info":[{"award-number":["Prix MARIE_PAULE BURRUS 2024 \u2013 PRS202407019918"]}],"id":[{"id":"10.13039\/501100002915","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Fondation Cl\u00e9ment Fayat"},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-21-CE18-0025-01 NOVEL"],"award-info":[{"award-number":["ANR-21-CE18-0025-01 NOVEL"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014865","name":"Fondation Maladies Rares","doi-asserted-by":"publisher","award":["Project Grant No. 10877 (2016)"],"award-info":[{"award-number":["Project Grant No. 10877 (2016)"]}],"id":[{"id":"10.13039\/100014865","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008211","name":"Association France Parkinson","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008211","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["npj Parkinsons Dis."],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>ATP13A2 is a lysosomal P5-ATPase highly expressed in the central nervous system, regulating polyamine, metal cation, and calcium homeostasis. Loss-of-function mutations cause an autosomal recessive juvenile form of Parkinson\u2019s disease called Kufor-Rakeb syndrome and other neurodegenerative disorders. Since the first clinical discovery of the Kufor-Rakeb syndrome, numerous ATP13A2-related models have emerged, leading to significant advances in understanding the physiology and pathophysiology of this protein. This review summarizes ATP13A2 structure, function, pathology, and insights gained from cellular and animal models, highlighting their value for elucidating disease mechanisms and therapeutic development across species and experimental systems, relevant to neurodegeneration research broadly.<\/jats:p>","DOI":"10.1038\/s41531-026-01331-w","type":"journal-article","created":{"date-parts":[[2026,4,4]],"date-time":"2026-04-04T16:28:24Z","timestamp":1775320104000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Progress in modelling ATP13A2-linked neurodegeneration"],"prefix":"10.1038","volume":"12","author":[{"given":"Benedetta","family":"Balbo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R\u00e9mi","family":"Kinet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura","family":"Civiero","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin","family":"Dehay","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,4,4]]},"reference":[{"key":"1331_CR1","doi-asserted-by":"publisher","first-page":"1252400","DOI":"10.3389\/fneur.2023.1252400","volume":"14","author":"KM Croucher","year":"2023","unstructured":"Croucher, K. M. & Fleming, S. M. ATP13A2 (PARK9) and basal ganglia function. Front Neurol. 14, 1252400 (2023).","journal-title":"Front Neurol."},{"key":"1331_CR2","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1016\/j.bbrc.2009.03.151","volume":"383","author":"K Schmidt","year":"2009","unstructured":"Schmidt, K., Wolfe, D. M., Stiller, B. & Pearce, D. A. Cd2+, Mn2+, Ni2+ and Se2+ toxicity to Saccharomyces cerevisiae lacking YPK9p the orthologue of human ATP13A2. Biochem Biophys. Res Commun. 383, 198\u2013202 (2009).","journal-title":"Biochem Biophys. Res Commun."},{"key":"1331_CR3","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1038\/s41592-018-0232-7","volume":"16","author":"N Narayanaswamy","year":"2019","unstructured":"Narayanaswamy, N. et al. A pH-correctable, DNA-based fluorescent reporter for organellar calcium. Nat. Methods 16, 95\u2013102 (2019).","journal-title":"Nat. Methods"},{"key":"1331_CR4","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1007\/s10048-024-00767-7","volume":"25","author":"MA Colijn","year":"2024","unstructured":"Colijn, M. A. et al. Kufor-Rakeb syndrome-associated psychosis: a novel loss-of-function ATP13A2 variant and response to antipsychotic therapy. Neurogenetics. 25, 405\u2013415 (2024).","journal-title":"Neurogenetics"},{"key":"1331_CR5","doi-asserted-by":"publisher","first-page":"1184","DOI":"10.1038\/ng1884","volume":"38","author":"A Ramirez","year":"2006","unstructured":"Ramirez, A. et al. Hereditary Parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase. Nat. Genet. 38, 1184\u20131191 (2006).","journal-title":"Nat. Genet."},{"key":"1331_CR6","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1212\/WNL.0000000000012705","volume":"97","author":"HF Chien","year":"2021","unstructured":"Chien, H. F. et al. Neuropathologic Findings in a Patient With Juvenile-Onset Levodopa-Responsive Parkinsonism Due to ATP13A2 Mutation. Neurology 97, 763\u2013766 (2021).","journal-title":"Neurology"},{"key":"1331_CR7","doi-asserted-by":"publisher","DOI":"10.1016\/j.brainres.2020.147167","volume":"1750","author":"K Kirimtay","year":"2021","unstructured":"Kirimtay, K., Temizci, B., Gultekin, M., Yapici, Z. & Karabay, A. Novel mutations in ATP13A2 associated with mixed neurological presentations and iron toxicity due to nonsense-mediated decay. Brain Res. 1750, 147167 (2021).","journal-title":"Brain Res."},{"key":"1331_CR8","doi-asserted-by":"publisher","first-page":"2646","DOI":"10.1093\/hmg\/dds089","volume":"21","author":"J Bras","year":"2012","unstructured":"Bras, J., Verloes, A., Schneider, S. A., Mole, S. E. & Guerreiro, R. J. Mutation of the Parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis. Hum. Mol. Genet. 21, 2646\u20132650 (2012).","journal-title":"Hum. Mol. Genet."},{"key":"1331_CR9","doi-asserted-by":"publisher","DOI":"10.1002\/mgg3.1052","volume":"8","author":"MA Estiar","year":"2020","unstructured":"Estiar, M. A. et al. Clinical and genetic analysis of ATP13A2 in hereditary spastic paraplegia expands the phenotype. Mol. Genet Genom. Med. 8, e1052 (2020).","journal-title":"Mol. Genet Genom. Med."},{"key":"1331_CR10","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1093\/brain\/aww307","volume":"140","author":"A Estrada-Cuzcano","year":"2017","unstructured":"Estrada-Cuzcano, A. et al. Loss-of-function mutations in the ATP13A2\/PARK9 gene cause complicated hereditary spastic paraplegia (SPG78). Brain 140, 287\u2013305 (2017).","journal-title":"Brain"},{"key":"1331_CR11","doi-asserted-by":"publisher","DOI":"10.1186\/s40246-019-0203-9","volume":"13","author":"R Spataro","year":"2019","unstructured":"Spataro, R. et al. Mutations in ATP13A2 (PARK9) are associated with an amyotrophic lateral sclerosis-like phenotype, implicating this locus in further phenotypic expansion. Hum. Genomics 13, 19 (2019).","journal-title":"Hum. Genomics"},{"key":"1331_CR12","doi-asserted-by":"publisher","unstructured":"Vrijsen S. El et al. Functional characterization of ATP13A2 variants associated with distinct neurodegenerative disorders. bioRxiv 2023.08.21.552829. https:\/\/doi.org\/10.1101\/2023.08.21.5528292023 (2023).","DOI":"10.1101\/2023.08.21.5528292023"},{"key":"1331_CR13","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1111\/j.1600-0404.1994.tb02645.x","volume":"89","author":"Najim al-Din","year":"1994","unstructured":"al-Din, N. ajim, Wriekat, A. S., Mubaidin, A., Dasouki, A. & Hiari, M. M. Pallido-pyramidal degeneration, supranuclear upgaze paresis and dementia: Kufor-Rakeb syndrome. Acta Neurol. Scand. 89, 347\u2013352 (1994).","journal-title":"Acta Neurol. Scand."},{"key":"1331_CR14","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1007\/s12098-019-03167-0","volume":"87","author":"VK Gowda","year":"2020","unstructured":"Gowda, V. K., Srinivasan, V. M. & Shivappa, S. K. Kufor-Rakeb Syndrome\/ Parkinson Disease Type 9. Indian J. Pediatr. 87, 231\u2013232 (2020).","journal-title":"Indian J. Pediatr."},{"key":"1331_CR15","doi-asserted-by":"publisher","first-page":"1264","DOI":"10.1002\/mds.20511","volume":"20","author":"DR Williams","year":"2005","unstructured":"Williams, D. R., Hadeed, A., al-Din, A. S., Wreikat, A. L. & Lees, A. J. Kufor Rakeb disease: autosomal recessive, levodopa-responsive Parkinsonism with pyramidal degeneration, supranuclear gaze palsy, and dementia. Mov. Disord. 20, 1264\u20131271 (2005).","journal-title":"Mov. Disord."},{"key":"1331_CR16","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1002\/mdc3.13933","volume":"11","author":"E Amini","year":"2024","unstructured":"Amini, E. et al. Estimation of Ambulation and Survival in Neurodegeneration with Brain Iron Accumulation Disorders. Mov. Disord. Clin. Pr. 11, 53\u201362 (2024).","journal-title":"Mov. Disord. Clin. Pr."},{"key":"1331_CR17","doi-asserted-by":"publisher","first-page":"3723","DOI":"10.1007\/s10072-023-06899-2","volume":"44","author":"S Satolli","year":"2023","unstructured":"Satolli, S., Di Fonzo, A., Zanobio, M., Pezzullo, G. & De Micco, R. Kufor Rakeb syndrome without gaze palsy and pyramidal signs due to novel ATP13A2 mutations. Neurol. Sci. 44, 3723\u20133725 (2023).","journal-title":"Neurol. Sci."},{"key":"1331_CR18","doi-asserted-by":"publisher","first-page":"2104","DOI":"10.1002\/mds.22728","volume":"24","author":"A Djarmati","year":"2009","unstructured":"Djarmati, A. et al. ATP13A2 variants in early-onset Parkinson\u2019s disease patients and controls. Mov. Disord. 24, 2104\u20132111 (2009).","journal-title":"Mov. Disord."},{"key":"1331_CR19","doi-asserted-by":"publisher","first-page":"770","DOI":"10.1002\/mds.26243","volume":"30","author":"JS Park","year":"2015","unstructured":"Park, J. S., Blair, N. F. & Sue, C. M. The role of ATP13A2 in Parkinson\u2019s disease: Clinical phenotypes and molecular mechanisms. Mov. Disord. 30, 770\u2013779 (2015).","journal-title":"Mov. Disord."},{"key":"1331_CR20","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1002\/mds.22399","volume":"24","author":"A Rakovic","year":"2009","unstructured":"Rakovic, A. et al. Genetic association study of the P-type ATPase ATP13A2 in late-onset Parkinson\u2019s disease. Mov. Disord. 24, 429\u2013433 (2009).","journal-title":"Mov. Disord."},{"key":"1331_CR21","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-37741-0","volume":"14","author":"J Mu","year":"2023","unstructured":"Mu, J. et al. Conformational cycle of human polyamine transporter ATP13A2. Nat. Commun. 14, 1978 (2023).","journal-title":"Nat. Commun."},{"key":"1331_CR22","doi-asserted-by":"publisher","first-page":"4635","DOI":"10.1016\/j.molcel.2021.08.017","volume":"81","author":"SI Sim","year":"2021","unstructured":"Sim, S. I., von Bulow, S., Hummer, G. & Park, E. Structural basis of polyamine transport by human ATP13A2 (PARK9). Mol. Cell 81, 4635\u201349 e8 (2021).","journal-title":"Mol. Cell"},{"key":"1331_CR23","doi-asserted-by":"publisher","first-page":"4650","DOI":"10.1016\/j.molcel.2021.10.002","volume":"81","author":"J Tillinghast","year":"2021","unstructured":"Tillinghast, J., Drury, S., Bowser, D., Benn, A. & Lee, K. P. K. Structural mechanisms for gating and ion selectivity of the human polyamine transporter ATP13A2. Mol. Cell 81, 4650\u201362 e4 (2021).","journal-title":"Mol. Cell"},{"key":"1331_CR24","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1038\/s41421-021-00334-6","volume":"7","author":"X Chen","year":"2021","unstructured":"Chen, X. et al. Cryo-EM structures and transport mechanism of human P5B type ATPase ATP13A2. Cell Discov. 7, 106 (2021).","journal-title":"Cell Discov."},{"key":"1331_CR25","doi-asserted-by":"publisher","first-page":"4799","DOI":"10.1016\/j.molcel.2021.11.001","volume":"81","author":"A Tomita","year":"2021","unstructured":"Tomita, A. et al. Cryo-EM reveals mechanistic insights into lipid-facilitated polyamine export by human ATP13A2. Mol. Cell 81, 4799\u2013809 e5 (2021).","journal-title":"Mol. Cell"},{"key":"1331_CR26","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1038\/s41586-020-1968-7","volume":"578","author":"S van Veen","year":"2020","unstructured":"van Veen, S. et al. ATP13A2 deficiency disrupts lysosomal polyamine export. Nature 578, 419\u2013424 (2020).","journal-title":"Nature"},{"key":"1331_CR27","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1016\/j.jtemb.2019.05.005","volume":"55","author":"J Baesler","year":"2019","unstructured":"Baesler, J. et al. Zn homeostasis in genetic models of Parkinson\u2019s disease in Caenorhabditis elegans. J. Trace Elem. Med. Biol. 55, 44\u201349 (2019).","journal-title":"J. Trace Elem. Med. Biol."},{"key":"1331_CR28","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2020.104786","volume":"139","author":"N Anand","year":"2020","unstructured":"Anand, N. et al. Dysregulated iron metabolism in C. elegans catp-6\/ATP13A2 mutant impairs mitochondrial function. Neurobiol. Dis. 139, 104786 (2020).","journal-title":"Neurobiol. Dis."},{"key":"1331_CR29","doi-asserted-by":"publisher","first-page":"e0220849","DOI":"10.1371\/journal.pone.0220849","volume":"14","author":"J Ugolino","year":"2019","unstructured":"Ugolino, J. et al. Overexpression of human Atp13a2Isoform-1 protein protects cells against manganese and starvation-induced toxicity. PLoS One 14, e0220849 (2019).","journal-title":"PLoS One"},{"key":"1331_CR30","doi-asserted-by":"publisher","first-page":"9611","DOI":"10.1073\/pnas.1112368109","volume":"109","author":"B Dehay","year":"2012","unstructured":"Dehay, B. et al. Loss of P-type ATPase ATP13A2\/PARK9 function induces general lysosomal deficiency and leads to Parkinson's disease neurodegeneration. Proc. Natl. Acad. Sci. USA 109, 9611\u20139616 (2012).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"1331_CR31","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-37815-z","volume":"14","author":"T Fujii","year":"2023","unstructured":"Fujii, T. et al. Parkinson\u2019s disease-associated ATP13A2\/PARK9 functions as a lysosomal H(+),K(+)-ATPase. Nat. Commun. 14, 2174 (2023).","journal-title":"Nat. Commun."},{"key":"1331_CR32","doi-asserted-by":"publisher","first-page":"1656","DOI":"10.1093\/hmg\/ddx070","volume":"26","author":"S Demirsoy","year":"2017","unstructured":"Demirsoy, S. et al. ATP13A2\/PARK9 regulates endo-\/lysosomal cargo sorting and proteostasis through a novel PI(3, 5)P2-mediated scaffolding function. Hum. Mol. Genet 26, 1656\u20131669 (2017).","journal-title":"Hum. Mol. Genet"},{"key":"1331_CR33","doi-asserted-by":"publisher","first-page":"31198","DOI":"10.1073\/pnas.1922342117","volume":"117","author":"S Vrijsen","year":"2020","unstructured":"Vrijsen, S. et al. ATP13A2-mediated endo-lysosomal polyamine export counters mitochondrial oxidative stress. Proc. Natl. Acad. Sci. USA 117, 31198\u201331207 (2020).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"1331_CR34","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1083\/jcb.201804165","volume":"218","author":"R Wang","year":"2019","unstructured":"Wang, R. et al. ATP13A2 facilitates HDAC6 recruitment to lysosome to promote autophagosome-lysosome fusion. J. Cell Biol. 218, 267\u2013284 (2019).","journal-title":"J. Cell Biol."},{"key":"1331_CR35","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamem.2019.05.015","volume":"1861","author":"AL Marcos","year":"2019","unstructured":"Marcos, A. L. et al. The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid homeostasis. Biochim Biophys. Acta Biomembr. 1861, 182993 (2019).","journal-title":"Biochim Biophys. Acta Biomembr."},{"key":"1331_CR36","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2025.116179","volume":"44","author":"M Samaddar","year":"2025","unstructured":"Samaddar, M. et al. Lysosomal polyamine storage upon ATP13A2 loss impairs beta-glucocerebrosidase via altered lysosomal pH and electrostatic hydrolase-lipid interactions. Cell Rep. 44, 116179 (2025).","journal-title":"Cell Rep."},{"key":"1331_CR37","doi-asserted-by":"publisher","first-page":"1646","DOI":"10.1016\/j.bbamem.2015.04.008","volume":"1848","author":"Rinaldi DE","year":"2015","unstructured":"Rinaldi DE, Corradi, G. R., Cuesta, L. M., Adamo, H. P. & de Tezanos Pinto, F. The Parkinson-associated human P5B-ATPase ATP13A2 protects against the iron-induced cytotoxicity. Biochim Biophys. Acta 1848, 1646\u20131655 (2015).","journal-title":"Biochim Biophys. Acta"},{"key":"1331_CR38","doi-asserted-by":"publisher","first-page":"2689","DOI":"10.3390\/ijms22052689","volume":"22","author":"J Si","year":"2021","unstructured":"Si, J. et al. ATP13A2 Regulates Cellular alpha-Synuclein Multimerization, Membrane Association, and Externalization. Int J Mol Sci. 22, 2689 (2021).","journal-title":"Int J Mol Sci."},{"key":"1331_CR39","doi-asserted-by":"publisher","first-page":"962","DOI":"10.1016\/j.nbd.2011.12.015","volume":"45","author":"AM Gusdon","year":"2012","unstructured":"Gusdon, A. M., Zhu, J., Van Houten, B. & Chu, C. T. ATP13A2 regulates mitochondrial bioenergetics through macroautophagy. Neurobiol. Dis. 45, 962\u2013972 (2012).","journal-title":"Neurobiol. Dis."},{"key":"1331_CR40","doi-asserted-by":"publisher","first-page":"e0276823","DOI":"10.1371\/journal.pone.0276823","volume":"17","author":"Y Hatori","year":"2022","unstructured":"Hatori, Y., Kanda, Y., Nonaka, S., Nakanishi, H. & Kitazawa, T. ATP13A2 modifies mitochondrial localization of overexpressed TOM20 to autolysosomal pathway. PLoS One 17, e0276823 (2022).","journal-title":"PLoS One"},{"key":"1331_CR41","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1007\/978-3-319-49969-7_9","volume":"14","author":"Y Xiong","year":"2017","unstructured":"Xiong, Y., Dawson, T. M. & Dawson, V. L. Models of LRRK2-Associated Parkinson\u2019s Disease. Adv. Neurobiol. 14, 163\u2013191 (2017).","journal-title":"Adv. Neurobiol."},{"key":"1331_CR42","doi-asserted-by":"publisher","first-page":"229","DOI":"10.3233\/JPD-2011-11041","volume":"1","author":"M Oliveras-Salva","year":"2011","unstructured":"Oliveras-Salva, M., Van Rompuy, A. S., Heeman, B., Van den Haute, C. & Baekelandt, V. Loss-of-function rodent models for parkin and PINK1. J. Parkinsons Dis. 1, 229\u2013251 (2011).","journal-title":"J. Parkinsons Dis."},{"key":"1331_CR43","doi-asserted-by":"publisher","first-page":"1396","DOI":"10.1080\/15548627.2022.2139080","volume":"19","author":"R Han","year":"2023","unstructured":"Han, R., Liu, Y., Li, S., Li, X. J. & Yang, W. PINK1-PRKN mediated mitophagy: differences between in vitro and in vivo models. Autophagy. 19, 1396\u20131405 (2023).","journal-title":"Autophagy"},{"key":"1331_CR44","doi-asserted-by":"publisher","first-page":"e0194451","DOI":"10.1371\/journal.pone.0194451","volume":"13","author":"J Zielich","year":"2018","unstructured":"Zielich, J. et al. Overlapping expression patterns and functions of three paralogous P5B ATPases in Caenorhabditis elegans. PLoS One. 13, e0194451 (2018).","journal-title":"PLoS One"},{"key":"1331_CR45","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1038\/ng.300","volume":"41","author":"AD Gitler","year":"2009","unstructured":"Gitler, A. D. et al. Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat. Genet. 41, 308\u2013315 (2009).","journal-title":"Nat. Genet."},{"key":"1331_CR46","doi-asserted-by":"publisher","first-page":"3785","DOI":"10.1093\/hmg\/dds206","volume":"21","author":"M Usenovic","year":"2012","unstructured":"Usenovic, M. et al. Identification of novel ATP13A2 interactors and their role in alpha-synuclein misfolding and toxicity. Hum. Mol. Genet. 21, 3785\u20133794 (2012).","journal-title":"Hum. Mol. Genet."},{"key":"1331_CR47","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1016\/j.expneurol.2018.09.001","volume":"310","author":"JF Cooper","year":"2018","unstructured":"Cooper, J. F. et al. alpha-synuclein expression from a single copy transgene increases sensitivity to stress and accelerates neuronal loss in genetic models of Parkinson\u2019s disease. Exp. Neurol. 310, 58\u201369 (2018).","journal-title":"Exp. Neurol."},{"key":"1331_CR48","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1080\/19336934.2022.2087484","volume":"16","author":"Y Nitta","year":"2022","unstructured":"Nitta, Y. & Sugie, A. Studies of neurodegenerative diseases using Drosophila and the development of novel approaches for their analysis. Fly 16, 275\u2013298 (2022).","journal-title":"Fly"},{"key":"1331_CR49","doi-asserted-by":"publisher","first-page":"3055","DOI":"10.3390\/ijms21093055","volume":"21","author":"H Bolus","year":"2020","unstructured":"Bolus, H., Crocker, K., Boekhoff-Falk, G. & Chtarbanova, S. Modeling neurodegenerative disorders in Drosophila melanogaster. Int. J. Mol. Sci. 21, 3055 (2020).","journal-title":"Int. J. Mol. Sci."},{"key":"1331_CR50","doi-asserted-by":"publisher","first-page":"5","DOI":"10.3389\/neuro.04.005.2009","volume":"3","author":"Z Mao","year":"2009","unstructured":"Mao, Z. & Davis, R. L. Eight different types of dopaminergic neurons innervate the Drosophila mushroom body neuropil: anatomical and physiological heterogeneity. Front Neural Circuits 3, 5 (2009).","journal-title":"Front Neural Circuits"},{"key":"1331_CR51","doi-asserted-by":"publisher","first-page":"10993","DOI":"10.1523\/JNEUROSCI.2993-04.2004","volume":"24","author":"H Coulom","year":"2004","unstructured":"Coulom, H. & Birman, S. Chronic exposure to rotenone models sporadic Parkinson\u2019s disease in Drosophila melanogaster. J. Neurosci. 24, 10993\u201310998 (2004).","journal-title":"J. Neurosci."},{"key":"1331_CR52","doi-asserted-by":"publisher","first-page":"205","DOI":"10.3389\/fnins.2010.00205","volume":"4","author":"KE White","year":"2010","unstructured":"White, K. E., Humphrey, D. M. & Hirth, F. The dopaminergic system in the aging brain of Drosophila. Front Neurosci. 4, 205 (2010).","journal-title":"Front Neurosci."},{"key":"1331_CR53","doi-asserted-by":"publisher","first-page":"1634","DOI":"10.1016\/S0960-9822(02)70787-2","volume":"6","author":"SP Koushika","year":"1996","unstructured":"Koushika, S. P., Lisbin, M. J. & White, K. ELAV, a Drosophila neuron-specific protein, mediates the generation of an alternatively spliced neural protein isoform. Curr. Biol. 6, 1634\u20131641 (1996).","journal-title":"Curr. Biol."},{"key":"1331_CR54","doi-asserted-by":"publisher","first-page":"1997","DOI":"10.4238\/2012.August.6.4","volume":"11","author":"WZ Li","year":"2012","unstructured":"Li, W. Z., Li, S. L., Zheng, H. Y., Zhang, S. P. & Xue, L. A broad expression profile of the GMR-GAL4 driver in Drosophila melanogaster. Genet Mol. Res. 11, 1997\u20132002 (2012).","journal-title":"Genet Mol. Res."},{"key":"1331_CR55","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1007\/s12041-015-0535-8","volume":"94","author":"M Ray","year":"2015","unstructured":"Ray, M. & Lakhotia, S. C. The commonly used eye-specific sev-GAL4 and GMR-GAL4 drivers in Drosophila melanogaster are expressed in tissues other than eyes also. J. Genet 94, 407\u2013416 (2015).","journal-title":"J. Genet"},{"key":"1331_CR56","doi-asserted-by":"crossref","unstructured":"Dhanushkodi N. R., Abul Khair S. B., Ardah M. T. & Haque M. E. ATP13A2 Gene Silencing in Drosophila affects autophagic degradation of A53T Mutant alpha-Synuclein. Int. J. Mol. Sci. 24, 1775 (2023).","DOI":"10.3390\/ijms24021775"},{"key":"1331_CR57","doi-asserted-by":"crossref","unstructured":"Xu, B. et al. Distinct effects of familial Parkinson\u2019s disease-associated mutations on alpha-Synuclein phase separation and amyloid aggregation. Biomolecules. 13, 726 (2023).","DOI":"10.3390\/biom13050726"},{"key":"1331_CR58","doi-asserted-by":"publisher","first-page":"676","DOI":"10.1101\/gad.3.5.676","volume":"3","author":"WA Johnson","year":"1989","unstructured":"Johnson, W. A., McCormick, C. A., Bray, S. J. & Hirsh, J. A neuron-specific enhancer of the Drosophila dopa decarboxylase gene. Genes Dev. 3, 676\u2013686 (1989).","journal-title":"Genes Dev."},{"key":"1331_CR59","doi-asserted-by":"publisher","first-page":"1651","DOI":"10.1056\/NEJMoa0901281","volume":"361","author":"E Sidransky","year":"2009","unstructured":"Sidransky, E. et al. Multicenter analysis of glucocerebrosidase mutations in Parkinson\u2019s disease. N. Engl. J. Med. 361, 1651\u20131661 (2009).","journal-title":"N. Engl. J. Med."},{"key":"1331_CR60","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1186\/s13024-025-00923-z","volume":"21","author":"M Gu","year":"2026","unstructured":"Gu, M. et al. Two lysosomal genes ATP13A2 and GBA1 interact to drive neurodegeneration. Mol. Neurodegener 21, 18 (2026).","journal-title":"Mol. Neurodegener"},{"key":"1331_CR61","doi-asserted-by":"publisher","DOI":"10.3389\/fnmol.2022.940484","volume":"15","author":"K Chia","year":"2022","unstructured":"Chia, K., Klingseisen, A., Sieger, D. & Priller, J. Zebrafish as a model organism for neurodegenerative disease. Front Mol. Neurosci. 15, 940484 (2022).","journal-title":"Front Mol. Neurosci."},{"key":"1331_CR62","doi-asserted-by":"publisher","DOI":"10.3389\/fphar.2021.713963","volume":"12","author":"X Wang","year":"2021","unstructured":"Wang, X., Zhang, J. B., He, K. J., Wang, F. & Liu, C. F. Advances of Zebrafish in neurodegenerative disease: from models to drug discovery. Front. Pharm. 12, 713963 (2021).","journal-title":"Front. Pharm."},{"key":"1331_CR63","doi-asserted-by":"publisher","first-page":"115","DOI":"10.3389\/fnana.2016.00115","volume":"10","author":"Y Du","year":"2016","unstructured":"Du, Y. et al. Spatial and temporal distribution of dopaminergic neurons during development in Zebrafish. Front Neuroanat. 10, 115 (2016).","journal-title":"Front Neuroanat."},{"key":"1331_CR64","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1002\/cne.20280","volume":"480","author":"DL McLean","year":"2004","unstructured":"McLean, D. L. & Fetcho, J. R. Ontogeny and innervation patterns of dopaminergic, noradrenergic, and serotonergic neurons in larval zebrafish. J. Comp. Neurol. 480, 38\u201356 (2004).","journal-title":"J. Comp. Neurol."},{"key":"1331_CR65","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms1171","volume":"2","author":"TL Tay","year":"2011","unstructured":"Tay, T. L., Ronneberger, O., Ryu, S., Nitschke, R. & Driever, W. Comprehensive catecholaminergic projectome analysis reveals single-neuron integration of zebrafish ascending and descending dopaminergic systems. Nat. Commun. 2, 171 (2011).","journal-title":"Nat. Commun."},{"key":"1331_CR66","doi-asserted-by":"publisher","first-page":"118","DOI":"10.1016\/j.brainresbull.2012.09.017","volume":"90","author":"T Lopes da Fonseca","year":"2013","unstructured":"Lopes da Fonseca, T. et al. The zebrafish homologue of Parkinson\u2019s disease ATP13A2 is essential for embryonic survival. Brain Res Bull. 90, 118\u2013126 (2013).","journal-title":"Brain Res Bull."},{"key":"1331_CR67","doi-asserted-by":"publisher","DOI":"10.1093\/braincomms\/fcz019","volume":"1","author":"U Heins-Marroquin","year":"2019","unstructured":"Heins-Marroquin, U., Jung, P. P., Cordero-Maldonado, M. L., Crawford, A. D. & Linster, C. L. Phenotypic assays in yeast and zebrafish reveal drugs that rescue ATP13A2 deficiency. Brain Commun. 1, fcz019 (2019).","journal-title":"Brain Commun."},{"key":"1331_CR68","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ibror.2020.05.002","volume":"9","author":"H Nyuzuki","year":"2020","unstructured":"Nyuzuki, H. et al. Degeneration of dopaminergic neurons and impaired intracellular trafficking in Atp13a2-deficient zebrafish. IBRO Rep. 9, 1\u20138 (2020).","journal-title":"IBRO Rep."},{"key":"1331_CR69","doi-asserted-by":"publisher","first-page":"714","DOI":"10.1038\/nature05846","volume":"447","author":"M Kasahara","year":"2007","unstructured":"Kasahara, M. et al. The medaka draft genome and insights into vertebrate genome evolution. Nature. 447, 714\u2013719 (2007).","journal-title":"Nature"},{"key":"1331_CR70","doi-asserted-by":"publisher","first-page":"559","DOI":"10.1038\/nature751","volume":"417","author":"M Matsuda","year":"2002","unstructured":"Matsuda, M. et al. DMY is a Y-specific DM-domain gene required for male development in the medaka fish. Nature 417, 559\u2013563 (2002).","journal-title":"Nature"},{"key":"1331_CR71","doi-asserted-by":"publisher","first-page":"783818","DOI":"10.3389\/fevo.2022.783818","volume":"10","author":"K Chowdhury","year":"2022","unstructured":"Chowdhury, K., Lin, S. & Lai, S.-L. Comparative study in Zebrafish and Medaka unravels the mechanisms of tissue regeneration. Front. Ecol. Evol. 10, 783818 (2022).","journal-title":"Front. Ecol. Evol."},{"key":"1331_CR72","doi-asserted-by":"publisher","first-page":"1316","DOI":"10.1016\/j.febslet.2013.02.046","volume":"587","author":"H Matsui","year":"2013","unstructured":"Matsui, H. et al. ATP13A2 deficiency induces a decrease in cathepsin D activity, fingerprint-like inclusion body formation, and selective degeneration of dopaminergic neurons. FEBS Lett. 587, 1316\u20131325 (2013).","journal-title":"FEBS Lett."},{"key":"1331_CR73","doi-asserted-by":"publisher","first-page":"2306","DOI":"10.1002\/jnr.23112","volume":"90","author":"JP Covy","year":"2012","unstructured":"Covy, J. P., Waxman, E. A. & Giasson, B. I. Characterization of cellular protective effects of ATP13A2\/PARK9 expression and alterations resulting from pathogenic mutants. J. Neurosci. Res. 90, 2306\u20132316 (2012).","journal-title":"J. Neurosci. Res."},{"key":"1331_CR74","doi-asserted-by":"publisher","first-page":"1725","DOI":"10.1093\/hmg\/ddr606","volume":"21","author":"D Ramonet","year":"2012","unstructured":"Ramonet, D. et al. PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity. Hum. Mol. Genet. 21, 1725\u20131743 (2012).","journal-title":"Hum. Mol. Genet."},{"key":"1331_CR75","doi-asserted-by":"publisher","first-page":"1843.e1","DOI":"10.1016\/j.neurobiolaging.2011.12.035","volume":"33","author":"A Grunewald","year":"2012","unstructured":"Grunewald, A. et al. ATP13A2 mutations impair mitochondrial function in fibroblasts from patients with Kufor-Rakeb syndrome. Neurobiol. Aging 33, 1843.e1\u20131843 e7 (2012).","journal-title":"Neurobiol. Aging"},{"key":"1331_CR76","doi-asserted-by":"publisher","first-page":"2816","DOI":"10.1093\/hmg\/ddu099","volume":"23","author":"SM Kong","year":"2014","unstructured":"Kong, S. M. et al. Parkinson\u2019s disease-linked human PARK9\/ATP13A2 maintains zinc homeostasis and promotes alpha-Synuclein externalization via exosomes. Hum. Mol. Genet. 23, 2816\u20132833 (2014).","journal-title":"Hum. Mol. Genet."},{"key":"1331_CR77","doi-asserted-by":"publisher","first-page":"163","DOI":"10.3390\/cells14030163","volume":"14","author":"T Tsunemi","year":"2025","unstructured":"Tsunemi, T., Ishiguro, Y., Yoroisaka, A., Feng, D. & Hattori, N. Altered ATP13A2\/PARK9 Levels influence alpha-Synuclein accumulation in neurons via phagocytosis and secretion in glial cells. Cells 14, 163 (2025).","journal-title":"Cells"},{"key":"1331_CR78","doi-asserted-by":"publisher","first-page":"8618","DOI":"10.1523\/JNEUROSCI.0954-20.2020","volume":"40","author":"T Tsunemi","year":"2020","unstructured":"Tsunemi, T. et al. Astrocytes protect Human Dopaminergic neurons from alpha-Synuclein accumulation and propagation. J. Neurosci. 40, 8618\u20138628 (2020).","journal-title":"J. Neurosci."},{"key":"1331_CR79","doi-asserted-by":"publisher","first-page":"2067","DOI":"10.1093\/hmg\/ddt057","volume":"22","author":"PJ Schultheis","year":"2013","unstructured":"Schultheis, P. J. et al. Atp13a2-deficient mice exhibit neuronal ceroid lipofuscinosis, limited alpha-synuclein accumulation and age-dependent sensorimotor deficits. Hum. Mol. Genet. 22, 2067\u20132082 (2013).","journal-title":"Hum. Mol. Genet."},{"key":"1331_CR80","doi-asserted-by":"publisher","first-page":"5724","DOI":"10.1523\/JNEUROSCI.0632-14.2015","volume":"35","author":"LR Kett","year":"2015","unstructured":"Kett, L. R. et al. alpha-Synuclein-independent histopathological and motor deficits in mice lacking the endolysosomal Parkinsonism protein Atp13a2. J. Neurosci. 35, 5724\u20135742 (2015).","journal-title":"J. Neurosci."},{"key":"1331_CR81","doi-asserted-by":"publisher","first-page":"3074","DOI":"10.1016\/j.ajpath.2016.08.006","volume":"186","author":"S Sato","year":"2016","unstructured":"Sato, S. et al. Lysosomal Storage of Subunit c of Mitochondrial ATP Synthase in Brain-Specific Atp13a2-Deficient Mice. Am. J. Pathol. 186, 3074\u20133082 (2016).","journal-title":"Am. J. Pathol."},{"key":"1331_CR82","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1038\/s41531-024-00748-5","volume":"10","author":"ML Erb","year":"2024","unstructured":"Erb, M. L., Sipple, K., Levine, N., Chen, X. & Moore, D. J. Adult-onset deletion of ATP13A2 in mice induces progressive nigrostriatal pathway dopaminergic degeneration and lysosomal abnormalities. NPJ Parkinsons Dis. 10, 133 (2024).","journal-title":"NPJ Parkinsons Dis."},{"key":"1331_CR83","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1111\/cns.12514","volume":"22","author":"C Qiao","year":"2016","unstructured":"Qiao, C. et al. Atp13a2 deficiency aggravates astrocyte-mediated neuroinflammation via NLRP3 inflammasome activation. CNS Neurosci. Ther. 22, 451\u2013460 (2016).","journal-title":"CNS Neurosci. Ther."},{"key":"1331_CR84","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2024.106701","volume":"202","author":"CM Massari","year":"2024","unstructured":"Massari, C. M. et al. Neuropathology in an alpha-synuclein preformed fibril mouse model occurs independent of the Parkinson\u2019s disease-linked lysosomal ATP13A2 protein. Neurobiol. Dis. 202, 106701 (2024).","journal-title":"Neurobiol. Dis."},{"key":"1331_CR85","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1038\/s41531-024-00757-4","volume":"10","author":"J Sikora","year":"2024","unstructured":"Sikora, J. et al. Nigral ATP13A2 depletion induces Parkinson\u2019s disease-related neurodegeneration in a pilot study in non-human primates. NPJ Parkinsons Dis. 10, 141 (2024).","journal-title":"NPJ Parkinsons Dis."},{"key":"1331_CR86","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/j.neuro.2017.06.005","volume":"64","author":"SM Fleming","year":"2018","unstructured":"Fleming, S. M. et al. The effect of manganese exposure in Atp13a2-deficient mice. Neurotoxicology 64, 256\u2013266 (2018).","journal-title":"Neurotoxicology"},{"key":"1331_CR87","doi-asserted-by":"crossref","unstructured":"Croucher K. et al. Phenotype differences between ATP13A2 heterozygous and knockout mice across aging. Int. J. Mol. Sci. 26, (2025).","DOI":"10.3390\/ijms26157030"},{"key":"1331_CR88","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1016\/j.nbd.2014.10.007","volume":"73","author":"G Daniel","year":"2015","unstructured":"Daniel, G. et al. alpha-Synuclein-induced dopaminergic neurodegeneration in a rat model of Parkinson\u2019s disease occurs independent of ATP13A2 (PARK9). Neurobiol. Dis. 73, 229\u2013243 (2015).","journal-title":"Neurobiol. Dis."},{"key":"1331_CR89","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1038\/s41531-025-01171-0","volume":"11","author":"R Kinet","year":"2025","unstructured":"Kinet, R. et al. Phenotypic characterization of an Atp13a2 knockout rat model of Parkinson\u2019s disease. NPJ Parkinsons Dis. 11, 321 (2025).","journal-title":"NPJ Parkinsons Dis."},{"key":"1331_CR90","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1177\/030098589703400601","volume":"34","author":"RD Jolly","year":"1997","unstructured":"Jolly, R. D. & Walkley, S. U. Lysosomal storage diseases of animals: an essay in comparative pathology. Vet. Pathol. 34, 527\u2013548 (1997).","journal-title":"Vet. Pathol."},{"key":"1331_CR91","doi-asserted-by":"publisher","first-page":"468","DOI":"10.1016\/j.nbd.2011.02.009","volume":"42","author":"FH Farias","year":"2011","unstructured":"Farias, F. H. et al. A truncating mutation in ATP13A2 is responsible for adult-onset neuronal ceroid lipofuscinosis in Tibetan terriers. Neurobiol. Dis. 42, 468\u2013474 (2011).","journal-title":"Neurobiol. Dis."},{"key":"1331_CR92","doi-asserted-by":"publisher","first-page":"67","DOI":"10.2460\/ajvr.2005.66.67","volume":"66","author":"ML Katz","year":"2005","unstructured":"Katz, M. L., Narfstrom, K., Johnson, G. S. & O\u2019Brien, D. P. Assessment of retinal function and characterization of lysosomal storage body accumulation in the retinas and brains of Tibetan Terriers with ceroid-lipofuscinosis. Am. J. Vet. Res. 66, 67\u201376 (2005).","journal-title":"Am. J. Vet. Res."},{"key":"1331_CR93","doi-asserted-by":"publisher","first-page":"e1002304","DOI":"10.1371\/journal.pgen.1002304","volume":"7","author":"A Wohlke","year":"2011","unstructured":"Wohlke, A. et al. A one base pair deletion in the canine ATP13A2 gene causes exon skipping and late-onset neuronal ceroid lipofuscinosis in the Tibetan terrier. PLoS Genet. 7, e1002304 (2011).","journal-title":"PLoS Genet."},{"key":"1331_CR94","doi-asserted-by":"publisher","first-page":"1929","DOI":"10.1002\/mds.22996","volume":"25","author":"MI Behrens","year":"2010","unstructured":"Behrens, M. I. et al. Clinical spectrum of Kufor-Rakeb syndrome in the Chilean kindred with ATP13A2 mutations. Mov. Disord. 25, 1929\u20131937 (2010).","journal-title":"Mov. Disord."},{"key":"1331_CR95","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1007\/s10048-010-0259-0","volume":"12","author":"L Santoro","year":"2011","unstructured":"Santoro, L. et al. Novel ATP13A2 (PARK9) homozygous mutation in a family with marked phenotype variability. Neurogenetics 12, 33\u201339 (2011).","journal-title":"Neurogenetics"},{"key":"1331_CR96","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.ymgme.2018.11.015","volume":"127","author":"I Schmutz","year":"2019","unstructured":"Schmutz, I. et al. ATP13A2 missense variant in Australian Cattle Dogs with late onset neuronal ceroid lipofuscinosis. Mol. Genet Metab. 127, 95\u2013106 (2019).","journal-title":"Mol. Genet Metab."},{"key":"1331_CR97","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1038\/s41531-024-00814-y","volume":"10","author":"V Baekelandt","year":"2024","unstructured":"Baekelandt, V. Depletion of ATP13A2 in adult brain induces a Parkinsonian phenotype in mice and non-human primates. NPJ Parkinsons Dis. 10, 193 (2024).","journal-title":"NPJ Parkinsons Dis."},{"key":"1331_CR98","doi-asserted-by":"publisher","first-page":"979","DOI":"10.1002\/mds.22947","volume":"25","author":"SA Schneider","year":"2010","unstructured":"Schneider, S. A. et al. ATP13A2 mutations (PARK9) cause neurodegeneration with brain iron accumulation. Mov. Disord. 25, 979\u2013984 (2010).","journal-title":"Mov. Disord."},{"key":"1331_CR99","doi-asserted-by":"publisher","first-page":"1357","DOI":"10.1001\/archneurol.2010.281","volume":"67","author":"N Bruggemann","year":"2010","unstructured":"Bruggemann, N. et al. Recessively inherited Parkinsonism: effect of ATP13A2 mutations on the clinical and neuroimaging phenotype. Arch. Neurol. 67, 1357\u20131363 (2010).","journal-title":"Arch. Neurol."}],"container-title":["npj Parkinson's Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41531-026-01331-w","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41531-026-01331-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41531-026-01331-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T00:04:14Z","timestamp":1780445054000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41531-026-01331-w"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4,4]]},"references-count":99,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["1331"],"URL":"https:\/\/doi.org\/10.1038\/s41531-026-01331-w","relation":{},"ISSN":["2373-8057"],"issn-type":[{"value":"2373-8057","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,4,4]]},"assertion":[{"value":"24 December 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 March 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 April 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"132"}}