{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T13:08:54Z","timestamp":1781788134454,"version":"3.54.5"},"reference-count":127,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,2,27]],"date-time":"2024-02-27T00:00:00Z","timestamp":1708992000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2024,2,27]],"date-time":"2024-02-27T00:00:00Z","timestamp":1708992000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/100000062","name":"National Institute of Diabetes and Digestive and Kidney Diseases","doi-asserted-by":"publisher","award":["P01NS097197"],"award-info":[{"award-number":["P01NS097197"]}],"id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["22H04988"],"award-info":[{"award-number":["22H04988"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Acta Neuropathol"],"published-print":{"date-parts":[[2024,6]]},"DOI":"10.1007\/s00401-024-02698-x","type":"journal-article","created":{"date-parts":[[2024,2,27]],"date-time":"2024-02-27T12:02:30Z","timestamp":1709035350000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Myofiber-type-dependent \u2018boulder\u2019 or \u2018multitudinous pebble\u2019 formations across distinct amylopectinoses"],"prefix":"10.1007","volume":"147","author":[{"given":"Sharmistha","family":"Mitra","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Baozhi","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John M.","family":"Shelton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvia","family":"Nitschke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lindsay","family":"Covington","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mathew","family":"Dear","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tori","family":"Lynn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mayank","family":"Verma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Felix","family":"Nitschke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuhiro","family":"Fuseya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuhiro","family":"Iwai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bret M.","family":"Evers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6258-0328","authenticated-orcid":false,"given":"Berge A.","family":"Minassian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,2,27]]},"reference":[{"key":"2698_CR1","doi-asserted-by":"publisher","first-page":"2443","DOI":"10.1042\/BST20210838","volume":"49","author":"A Aboujaoude","year":"2021","unstructured":"Aboujaoude A, Minassian B, Mitra S (2021) LUBAC: a new player in polyglucosan body disease. Biochem Soc Trans 49:2443\u20132454. https:\/\/doi.org\/10.1042\/BST20210838","journal-title":"Biochem Soc Trans"},{"key":"2698_CR2","doi-asserted-by":"publisher","first-page":"2867","DOI":"10.1093\/hmg\/ddq190","volume":"19","author":"C Aguado","year":"2010","unstructured":"Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, Boya P et al (2010) Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum Mol Genet 19:2867\u20132876. https:\/\/doi.org\/10.1093\/hmg\/ddq190","journal-title":"Hum Mol Genet"},{"key":"2698_CR3","doi-asserted-by":"publisher","first-page":"2985","DOI":"10.1093\/brain\/awab194","volume":"144","author":"S Ahonen","year":"2021","unstructured":"Ahonen S, Nitschke S, Grossman TR, Kordasiewicz H, Wang P, Zhao X et al (2021) Gys1 antisense therapy rescues neuropathological bases of murine Lafora disease. Brain 144:2985\u20132993. https:\/\/doi.org\/10.1093\/brain\/awab194","journal-title":"Brain"},{"key":"2698_CR4","doi-asserted-by":"publisher","first-page":"4430","DOI":"10.1093\/hmg\/ddr371","volume":"20","author":"HO Akman","year":"2011","unstructured":"Akman HO, Sheiko T, Tay SK, Finegold MJ, Dimauro S, Craigen WJ (2011) Generation of a novel mouse model that recapitulates early and adult onset glycogenosis type IV. Hum Mol Genet 20:4430\u20134439. https:\/\/doi.org\/10.1093\/hmg\/ddr371","journal-title":"Hum Mol Genet"},{"key":"2698_CR5","doi-asserted-by":"publisher","first-page":"13525","DOI":"10.1038\/s41598-018-31766-y","volume":"8","author":"E Auge","year":"2018","unstructured":"Auge E, Duran J, Guinovart JJ, Pelegri C, Vilaplana J (2018) Exploring the elusive composition of corpora amylacea of human brain. Sci Rep 8:13525. https:\/\/doi.org\/10.1038\/s41598-018-31766-y","journal-title":"Sci Rep"},{"key":"2698_CR6","doi-asserted-by":"publisher","first-page":"2094","DOI":"10.1002\/glia.23463","volume":"66","author":"E Auge","year":"2018","unstructured":"Auge E, Pelegri C, Manich G, Cabezon I, Guinovart JJ, Duran J et al (2018) Astrocytes and neurons produce distinct types of polyglucosan bodies in Lafora disease. Glia 66:2094\u20132107. https:\/\/doi.org\/10.1002\/glia.23463","journal-title":"Glia"},{"key":"2698_CR7","first-page":"89","volume":"21","author":"VPRC Augusto","year":"2004","unstructured":"Augusto VPRC, Campos ERG (2004) Skeletal muscle fiber types in C57BL6J mice. Braz J morphol sci 21:89\u201394","journal-title":"Braz J morphol sci"},{"key":"2698_CR8","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1111\/j.1471-4159.2006.03913.x","volume":"98","author":"LK Bak","year":"2006","unstructured":"Bak LK, Schousboe A, Waagepetersen HS (2006) The glutamate\/GABA-glutamine cycle: aspects of transport, neurotransmitter homeostasis and ammonia transfer. J Neurochem 98:641\u2013653. https:\/\/doi.org\/10.1111\/j.1471-4159.2006.03913.x","journal-title":"J Neurochem"},{"key":"2698_CR9","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1002\/ana.410140116","volume":"14","author":"RJ Baumann","year":"1983","unstructured":"Baumann RJ, Kocoshis SA, Wilson D (1983) Lafora disease: liver histopathology in presymptomatic children. Ann Neurol 14:86\u201389. https:\/\/doi.org\/10.1002\/ana.410140116","journal-title":"Ann Neurol"},{"key":"2698_CR10","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1007\/BF00410522","volume":"212","author":"M Berard-Badier","year":"1980","unstructured":"Berard-Badier M, Pellissier JF, Gambarelli D, de Barsy T, Roger J, Toga M (1980) The retina in Lafora disease: light and electron microscopy. Albrecht Von Graefes Arch Klin Exp Ophthalmol 212:285\u2013294. https:\/\/doi.org\/10.1007\/BF00410522","journal-title":"Albrecht Von Graefes Arch Klin Exp Ophthalmol"},{"key":"2698_CR11","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1203\/00006450-198701000-00017","volume":"21","author":"J Bijman","year":"1987","unstructured":"Bijman J, Quinton PM (1987) Lactate and bicarbonate uptake in the sweat duct of cystic fibrosis and normal subjects. Pediatr Res 21:79\u201382. https:\/\/doi.org\/10.1203\/00006450-198701000-00017","journal-title":"Pediatr Res"},{"key":"2698_CR12","doi-asserted-by":"publisher","first-page":"939","DOI":"10.1084\/jem.20141130","volume":"212","author":"B Boisson","year":"2015","unstructured":"Boisson B, Laplantine E, Dobbs K, Cobat A, Tarantino N, Hazen M et al (2015) Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia. J Exp Med 212:939\u2013951. https:\/\/doi.org\/10.1084\/jem.20141130","journal-title":"J Exp Med"},{"key":"2698_CR13","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1249\/00005768-198606000-00019","volume":"18","author":"GA Brooks","year":"1986","unstructured":"Brooks GA (1986) The lactate shuttle during exercise and recovery. Med Sci Sports Exerc 18:360\u2013368. https:\/\/doi.org\/10.1249\/00005768-198606000-00019","journal-title":"Med Sci Sports Exerc"},{"key":"2698_CR14","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1016\/j.neuint.2003.11.005","volume":"45","author":"AM Brown","year":"2004","unstructured":"Brown AM, Baltan Tekkok S, Ransom BR (2004) Energy transfer from astrocytes to axons: the role of CNS glycogen. Neurochem Int 45:529\u2013536. https:\/\/doi.org\/10.1016\/j.neuint.2003.11.005","journal-title":"Neurochem Int"},{"key":"2698_CR15","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1002\/ana.410330114","volume":"33","author":"C Bruno","year":"1993","unstructured":"Bruno C, Servidei S, Shanske S, Karpati G, Carpenter S, McKee D et al (1993) Glycogen branching enzyme deficiency in adult polyglucosan body disease. Ann Neurol 33:88\u201393. https:\/\/doi.org\/10.1002\/ana.410330114","journal-title":"Ann Neurol"},{"key":"2698_CR16","first-page":"257","volume":"59","author":"HC Eyster","year":"1959","unstructured":"Eyster HC (1959) The optimum pH for diastase of malt activity. Ohio J Sci 59:257\u2013262","journal-title":"Ohio J Sci"},{"key":"2698_CR17","doi-asserted-by":"publisher","first-page":"1564","DOI":"10.1212\/wnl.31.12.1564","volume":"31","author":"S Carpenter","year":"1981","unstructured":"Carpenter S, Karpati G (1981) Sweat gland duct cells in Lafora disease: diagnosis by skin biopsy. Neurology 31:1564\u20131568. https:\/\/doi.org\/10.1212\/wnl.31.12.1564","journal-title":"Neurology"},{"key":"2698_CR18","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1212\/wnl.24.6.531","volume":"24","author":"S Carpenter","year":"1974","unstructured":"Carpenter S, Karpati G, Andermann F, Jacob JC, Andermann E (1974) Lafora\u2019s disease: peroxisomal storage in skeletal muscle. Neurology 24:531\u2013538. https:\/\/doi.org\/10.1212\/wnl.24.6.531","journal-title":"Neurology"},{"key":"2698_CR19","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1007\/s00428-019-02633-6","volume":"475","author":"G Cenacchi","year":"2019","unstructured":"Cenacchi G, Papa V, Costa R, Pegoraro V, Marozzo R, Fanin M et al (2019) Update on polyglucosan storage diseases. Virchows Arch 475:671\u2013686. https:\/\/doi.org\/10.1007\/s00428-019-02633-6","journal-title":"Virchows Arch"},{"key":"2698_CR20","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.tplants.2013.08.004","volume":"19","author":"U Cenci","year":"2014","unstructured":"Cenci U, Nitschke F, Steup M, Minassian BA, Colleoni C, Ball SG (2014) Transition from glycogen to starch metabolism in Archaeplastida. Trends Plant Sci 19:18\u201328. https:\/\/doi.org\/10.1016\/j.tplants.2013.08.004","journal-title":"Trends Plant Sci"},{"key":"2698_CR21","doi-asserted-by":"publisher","first-page":"543","DOI":"10.1177\/0300985818758471","volume":"55","author":"JK Chambers","year":"2018","unstructured":"Chambers JK, Thongtharb A, Shiga T, Azakami D, Saito M, Sato M et al (2018) Accumulation of laforin and other related proteins in canine Lafora disease with EPM2B repeat expansion. Vet Pathol 55:543\u2013551. https:\/\/doi.org\/10.1177\/0300985818758471","journal-title":"Vet Pathol"},{"key":"2698_CR22","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1038\/ng1238","volume":"35","author":"EM Chan","year":"2003","unstructured":"Chan EM, Young EJ, Ianzano L, Munteanu I, Zhao X, Christopoulos CC et al (2003) Mutations in NHLRC1 cause progressive myoclonus epilepsy. Nat Genet 35:125\u2013127. https:\/\/doi.org\/10.1038\/ng1238","journal-title":"Nat Genet"},{"key":"2698_CR23","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1186\/s12891-020-03884-0","volume":"22","author":"L Chen","year":"2021","unstructured":"Chen L, Wang N, Hu W, Yu X, Yang R, Han Y et al (2021) Polyglucosan body myopathy 1 may cause cognitive impairment: a case report from China. BMC Musculoskelet Disord 22:35. https:\/\/doi.org\/10.1186\/s12891-020-03884-0","journal-title":"BMC Musculoskelet Disord"},{"key":"2698_CR24","doi-asserted-by":"publisher","first-page":"2186","DOI":"10.1002\/acn3.51211","volume":"7","author":"EE Chown","year":"2020","unstructured":"Chown EE, Wang P, Zhao X, Crowder JJ, Strober JW, Sullivan MA et al (2020) GYS1 or PPP1R3C deficiency rescues murine adult polyglucosan body disease. Ann Clin Transl Neurol 7:2186\u20132198. https:\/\/doi.org\/10.1002\/acn3.51211","journal-title":"Ann Clin Transl Neurol"},{"key":"2698_CR25","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbior.2019.100666","volume":"75","author":"P Cohen","year":"2020","unstructured":"Cohen P, Kelsall IR, Nanda SK, Zhang J (2020) HOIL-1, an atypical E3 ligase that controls MyD88 signalling by forming ester bonds between ubiquitin and components of the Myddosome. Adv Biol Regul 75:100666. https:\/\/doi.org\/10.1016\/j.jbior.2019.100666","journal-title":"Adv Biol Regul"},{"key":"2698_CR26","doi-asserted-by":"publisher","first-page":"396","DOI":"10.1001\/archneur.1974.00490420062007","volume":"31","author":"DL Coleman","year":"1974","unstructured":"Coleman DL, Gambetti P, Mauro SD, Blume RE (1974) Muscle in Lafora disease. Arch Neurol 31:396\u2013406. https:\/\/doi.org\/10.1001\/archneur.1974.00490420062007","journal-title":"Arch Neurol"},{"key":"2698_CR27","doi-asserted-by":"publisher","first-page":"1521","DOI":"10.1093\/hmg\/ddr590","volume":"21","author":"O Criado","year":"2012","unstructured":"Criado O, Aguado C, Gayarre J, Duran-Trio L, Garcia-Cabrero AM, Vernia S et al (2012) Lafora bodies and neurological defects in malin-deficient mice correlate with impaired autophagy. Hum Mol Genet 21:1521\u20131533. https:\/\/doi.org\/10.1093\/hmg\/ddr590","journal-title":"Hum Mol Genet"},{"key":"2698_CR28","doi-asserted-by":"publisher","first-page":"376","DOI":"10.1016\/j.gene.2012.12.065","volume":"515","author":"L Dainese","year":"2013","unstructured":"Dainese L, Monin ML, Demeret S, Brochier G, Froissart R, Spraul A et al (2013) Abnormal glycogen in astrocytes is sufficient to cause adult polyglucosan body disease. Gene 515:376\u2013379. https:\/\/doi.org\/10.1016\/j.gene.2012.12.065","journal-title":"Gene"},{"key":"2698_CR29","first-page":"635","volume":"33","author":"JM Delgado-Garcia","year":"2001","unstructured":"Delgado-Garcia JM (2001) Structure and function of the cerebellum. Rev Neurol 33:635\u2013642","journal-title":"Rev Neurol"},{"key":"2698_CR30","doi-asserted-by":"publisher","first-page":"25372","DOI":"10.1074\/jbc.M110.148668","volume":"285","author":"AA DePaoli-Roach","year":"2010","unstructured":"DePaoli-Roach AA, Tagliabracci VS, Segvich DM, Meyer CM, Irimia JM, Roach PJ (2010) Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin. J Biol Chem 285:25372\u201325381. https:\/\/doi.org\/10.1074\/jbc.M110.148668","journal-title":"J Biol Chem"},{"key":"2698_CR31","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2019.101183","volume":"24","author":"I Dimauro","year":"2019","unstructured":"Dimauro I, Antonioni A, Mercatelli N, Grazioli E, Fantini C, Barone R et al (2019) The early response of alphaB-crystallin to a single bout of aerobic exercise in mouse skeletal muscles depends upon fiber oxidative features. Redox Biol 24:101183. https:\/\/doi.org\/10.1016\/j.redox.2019.101183","journal-title":"Redox Biol"},{"key":"2698_CR32","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1016\/0006-8993(93)91429-v","volume":"623","author":"R Dringen","year":"1993","unstructured":"Dringen R, Gebhardt R, Hamprecht B (1993) Glycogen in astrocytes: possible function as lactate supply for neighboring cells. Brain Res 623:208\u2013214. https:\/\/doi.org\/10.1016\/0006-8993(93)91429-v","journal-title":"Brain Res"},{"key":"2698_CR33","volume-title":"Muscle biopsy: A practical approach","author":"V Dubowitz","year":"2020","unstructured":"Dubowitz V, Sewry AC, Oldfors A (2020) Muscle biopsy: A practical approach. Elsevier, London"},{"key":"2698_CR34","doi-asserted-by":"publisher","first-page":"2349","DOI":"10.1093\/brain\/awab110","volume":"144","author":"J Duran","year":"2021","unstructured":"Duran J, Hervera A, Markussen KH, Varea O, Lopez-Soldado I, Sun RC et al (2021) Astrocytic glycogen accumulation drives the pathophysiology of neurodegeneration in Lafora disease. Brain 144:2349\u20132360. https:\/\/doi.org\/10.1093\/brain\/awab110","journal-title":"Brain"},{"key":"2698_CR35","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1111\/imr.12307","volume":"266","author":"L Elton","year":"2015","unstructured":"Elton L, Carpentier I, Verhelst K, Staal J, Beyaert R (2015) The multifaceted role of the E3 ubiquitin ligase HOIL-1: beyond linear ubiquitination. Immunol Rev 266:208\u2013221. https:\/\/doi.org\/10.1111\/imr.12307","journal-title":"Immunol Rev"},{"key":"2698_CR36","doi-asserted-by":"publisher","first-page":"334","DOI":"10.1016\/B978-0-12-800883-6.00030-6","volume-title":"Quantitative Human Physiology","author":"J Feher","year":"2017","unstructured":"Feher J (2017) Muscle Energetics, Fatigue, and Training. Quantitative Human Physiology, 2nd edn. Academic Press, Cambridge, pp 334\u2013348","edition":"2"},{"key":"2698_CR37","doi-asserted-by":"publisher","first-page":"1192","DOI":"10.1016\/j.celrep.2018.03.112","volume":"23","author":"H Fujita","year":"2018","unstructured":"Fujita H, Tokunaga A, Shimizu S, Whiting AL, Aguilar-Alonso F, Takagi K et al (2018) Cooperative domain formation by homologous motifs in HOIL-1L and SHARPIN plays a crucial role in LUBAC stabilization. Cell Rep 23:1192\u20131204. https:\/\/doi.org\/10.1016\/j.celrep.2018.03.112","journal-title":"Cell Rep"},{"key":"2698_CR38","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1038\/s41556-020-0517-9","volume":"22","author":"Y Fuseya","year":"2020","unstructured":"Fuseya Y, Fujita H, Kim M, Ohtake F, Nishide A, Sasaki K et al (2020) The HOIL-1L ligase modulates immune signalling and cell death via monoubiquitination of LUBAC. Nat Cell Biol 22:663\u2013673. https:\/\/doi.org\/10.1038\/s41556-020-0517-9","journal-title":"Nat Cell Biol"},{"key":"2698_CR39","doi-asserted-by":"publisher","DOI":"10.3390\/cells10102706","author":"Y Fuseya","year":"2021","unstructured":"Fuseya Y, Iwai K (2021) Biochemistry, pathophysiology, and regulation of linear ubiquitination: intricate regulation by coordinated functions of the associated ligase and deubiquitinase. Cells. https:\/\/doi.org\/10.3390\/cells10102706","journal-title":"Cells"},{"key":"2698_CR40","doi-asserted-by":"publisher","first-page":"1251","DOI":"10.1093\/hmg\/11.11.1251","volume":"11","author":"S Ganesh","year":"2002","unstructured":"Ganesh S, Delgado-Escueta AV, Sakamoto T, Avila MR, Machado-Salas J, Hoshii Y et al (2002) Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice. Hum Mol Genet 11:1251\u20131262. https:\/\/doi.org\/10.1093\/hmg\/11.11.1251","journal-title":"Hum Mol Genet"},{"key":"2698_CR41","doi-asserted-by":"publisher","first-page":"8501","DOI":"10.1073\/pnas.0503285102","volume":"102","author":"MS Gentry","year":"2005","unstructured":"Gentry MS, Worby CA, Dixon JE (2005) Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc Natl Acad Sci U S A 102:8501\u20138506. https:\/\/doi.org\/10.1073\/pnas.0503285102","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2698_CR42","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1097\/00005072-199201000-00004","volume":"51","author":"HH Goebel","year":"1992","unstructured":"Goebel HH, Shin YS, Gullotta F, Yokota T, Alroy J, Voit T et al (1992) Adult polyglucosan body myopathy. J Neuropathol Exp Neurol 51:24\u201335. https:\/\/doi.org\/10.1097\/00005072-199201000-00004","journal-title":"J Neuropathol Exp Neurol"},{"key":"2698_CR43","doi-asserted-by":"publisher","first-page":"411","DOI":"10.1016\/0022-2836(82)90336-9","volume":"156","author":"E Goldsmith","year":"1982","unstructured":"Goldsmith E, Sprang S, Fletterick R (1982) Structure of maltoheptaose by difference Fourier methods and a model for glycogen. J Mol Biol 156:411\u2013427. https:\/\/doi.org\/10.1016\/0022-2836(82)90336-9","journal-title":"J Mol Biol"},{"key":"2698_CR44","doi-asserted-by":"publisher","first-page":"459","DOI":"10.1097\/00005072-198807000-00007","volume":"47","author":"F Gray","year":"1988","unstructured":"Gray F, Gherardi R, Marshall A, Janota I, Poirier J (1988) Adult polyglucosan body disease (APBD). J Neuropathol Exp Neurol 47:459\u2013474. https:\/\/doi.org\/10.1097\/00005072-198807000-00007","journal-title":"J Neuropathol Exp Neurol"},{"key":"2698_CR45","doi-asserted-by":"publisher","first-page":"1414","DOI":"10.1007\/s13311-021-01040-7","volume":"18","author":"E Gumusgoz","year":"2021","unstructured":"Gumusgoz E, Guisso DR, Kasiri S, Wu J, Dear M, Verhalen B et al (2021) Targeting Gys1 with AAV-SaCas9 decreases pathogenic polyglucosan bodies and neuroinflammation in adult polyglucosan body and Lafora disease mouse models. Neurotherapeutics 18:1414\u20131425. https:\/\/doi.org\/10.1007\/s13311-021-01040-7","journal-title":"Neurotherapeutics"},{"key":"2698_CR46","doi-asserted-by":"publisher","first-page":"982","DOI":"10.1007\/s13311-022-01218-7","volume":"19","author":"E Gumusgoz","year":"2022","unstructured":"Gumusgoz E, Kasiri S, Guisso DR, Wu J, Dear M, Verhalen B et al (2022) AAV-mediated artificial miRNA reduces pathogenic polyglucosan bodies and neuroinflammation in adult polyglucosan body and Lafora disease mouse models. Neurotherapeutics 19:982\u2013993. https:\/\/doi.org\/10.1007\/s13311-022-01218-7","journal-title":"Neurotherapeutics"},{"key":"2698_CR47","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1093\/brain\/78.3.325","volume":"78","author":"DG Harriman","year":"1955","unstructured":"Harriman DG, Millar JH, Stevenson AC (1955) Progressive familial myoclonic epilepsy in three families: its clinical features and pathological basis. Brain 78:325\u2013349. https:\/\/doi.org\/10.1093\/brain\/78.3.325","journal-title":"Brain"},{"key":"2698_CR48","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1016\/j.mam.2015.08.006","volume":"46","author":"C Hedberg-Oldfors","year":"2015","unstructured":"Hedberg-Oldfors C, Oldfors A (2015) Polyglucosan storage myopathies. Mol Aspects Med 46:85\u2013100. https:\/\/doi.org\/10.1016\/j.mam.2015.08.006","journal-title":"Mol Aspects Med"},{"key":"2698_CR49","doi-asserted-by":"publisher","DOI":"10.1016\/j.ajoc.2021.101146","volume":"23","author":"H Heitkotter","year":"2021","unstructured":"Heitkotter H, Linderman RE, Cava JA, Woertz EN, Mastey RR, Summerfelt P et al (2021) Retinal alterations in patients with Lafora disease. Am J Ophthalmol Case Rep 23:101146. https:\/\/doi.org\/10.1016\/j.ajoc.2021.101146","journal-title":"Am J Ophthalmol Case Rep"},{"key":"2698_CR50","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1016\/j.molcel.2017.09.001","volume":"68","author":"M Hrdinka","year":"2017","unstructured":"Hrdinka M, Gyrd-Hansen M (2017) The Met1-linked ubiquitin machinery: emerging themes of (de)regulation. Mol Cell 68:265\u2013280. https:\/\/doi.org\/10.1016\/j.molcel.2017.09.001","journal-title":"Mol Cell"},{"key":"2698_CR51","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1146\/annurev.nu.16.070196.001143","volume":"16","author":"K Jungermann","year":"1996","unstructured":"Jungermann K, Kietzmann T (1996) Zonation of parenchymal and nonparenchymal metabolism in liver. Annu Rev Nutr 16:179\u2013203. https:\/\/doi.org\/10.1146\/annurev.nu.16.070196.001143","journal-title":"Annu Rev Nutr"},{"key":"2698_CR52","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.28899","author":"MA Kanow","year":"2017","unstructured":"Kanow MA, Giarmarco MM, Jankowski CS, Tsantilas K, Engel AL, Du J et al (2017) Biochemical adaptations of the retina and retinal pigment epithelium support a metabolic ecosystem in the vertebrate eye. Elife. https:\/\/doi.org\/10.7554\/eLife.28899","journal-title":"Elife"},{"key":"2698_CR53","doi-asserted-by":"publisher","first-page":"1246","DOI":"10.1212\/wnl.43.6.1246","volume":"43","author":"MA Kaufman","year":"1993","unstructured":"Kaufman MA, Dwork AJ, Willson NJ, John S, Liu JD (1993) Late-onset Lafora\u2019s disease with typical intraneuronal inclusions. Neurology 43:1246\u20131248. https:\/\/doi.org\/10.1212\/wnl.43.6.1246","journal-title":"Neurology"},{"key":"2698_CR54","doi-asserted-by":"publisher","DOI":"10.15252\/embj.2021109700","volume":"41","author":"IR Kelsall","year":"2022","unstructured":"Kelsall IR, McCrory EH, Xu Y, Scudamore CL, Nanda SK, Mancebo-Gamella P et al (2022) HOIL-1 ubiquitin ligase activity targets unbranched glucosaccharides and is required to prevent polyglucosan accumulation. EMBO J 41:e109700. https:\/\/doi.org\/10.15252\/embj.2021109700","journal-title":"EMBO J"},{"key":"2698_CR55","doi-asserted-by":"publisher","first-page":"13293","DOI":"10.1073\/pnas.1905873116","volume":"116","author":"IR Kelsall","year":"2019","unstructured":"Kelsall IR, Zhang J, Knebel A, Arthur JSC, Cohen P (2019) The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells. Proc Natl Acad Sci U S A 116:13293\u201313298. https:\/\/doi.org\/10.1073\/pnas.1905873116","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2698_CR56","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1007\/s10545-014-9785-5","volume":"38","author":"MW Kilimann","year":"2015","unstructured":"Kilimann MW, Oldfors A (2015) Glycogen pathways in disease: new developments in a classical field of medical genetics. J Inherit Metab Dis 38:483\u2013487. https:\/\/doi.org\/10.1007\/s10545-014-9785-5","journal-title":"J Inherit Metab Dis"},{"key":"2698_CR57","doi-asserted-by":"publisher","first-page":"701","DOI":"10.4161\/auto.19522","volume":"8","author":"E Knecht","year":"2012","unstructured":"Knecht E, Criado-Garcia O, Aguado C, Gayarre J, Duran-Trio L, Garcia-Cabrero AM et al (2012) Malin knockout mice support a primary role of autophagy in the pathogenesis of Lafora disease. Autophagy 8:701\u2013703. https:\/\/doi.org\/10.4161\/auto.19522","journal-title":"Autophagy"},{"key":"2698_CR58","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1111\/j.1528-1167.1990.tb06306.x","volume":"31","author":"K Kobayashi","year":"1990","unstructured":"Kobayashi K, Iyoda K, Ohtsuka Y, Ohtahara S, Yamada M (1990) Longitudinal clinicoelectrophysiologic study of a case of Lafora disease proven by skin biopsy. Epilepsia 31:194\u2013201. https:\/\/doi.org\/10.1111\/j.1528-1167.1990.tb06306.x","journal-title":"Epilepsia"},{"key":"2698_CR59","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/BF02863929","volume":"6","author":"GRG Lafora","year":"1911","unstructured":"Lafora GRG, B. (1911) Beitrag zur histopathogie der myoklonischen epilepsie [German]. Z Gesamte Neurol Psychiatr 6:1\u201314","journal-title":"Z Gesamte Neurol Psychiatr"},{"key":"2698_CR60","doi-asserted-by":"publisher","first-page":"1607","DOI":"10.1007\/s12035-019-01842-z","volume":"57","author":"M Lahuerta","year":"2020","unstructured":"Lahuerta M, Gonzalez D, Aguado C, Fathinajafabadi A, Garcia-Gimenez JL, Moreno-Estelles M et al (2020) Reactive glia-derived neuroinflammation: a novel hallmark in Lafora progressive myoclonus epilepsy that progresses with age. Mol Neurobiol 57:1607\u20131621. https:\/\/doi.org\/10.1007\/s12035-019-01842-z","journal-title":"Mol Neurobiol"},{"key":"2698_CR61","doi-asserted-by":"publisher","first-page":"546","DOI":"10.1038\/nature16511","volume":"529","author":"BC Lechtenberg","year":"2016","unstructured":"Lechtenberg BC, Rajput A, Sanishvili R, Dobaczewska MK, Ware CF, Mace PD et al (2016) Structure of a HOIP\/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation. Nature 529:546\u2013550. https:\/\/doi.org\/10.1038\/nature16511","journal-title":"Nature"},{"key":"2698_CR62","doi-asserted-by":"publisher","first-page":"39991","DOI":"10.1074\/jbc.M006251200","volume":"275","author":"C Lerin","year":"2000","unstructured":"Lerin C, Montell E, Berman HK, Newgard CB, Gomez-Foix AM (2000) Overexpression of protein targeting to glycogen in cultured human muscle cells stimulates glycogen synthesis independent of glycogen and glucose 6-phosphate levels. J Biol Chem 275:39991\u201339995. https:\/\/doi.org\/10.1074\/jbc.M006251200","journal-title":"J Biol Chem"},{"key":"2698_CR63","doi-asserted-by":"publisher","first-page":"3119","DOI":"10.1007\/s12035-016-9884-4","volume":"54","author":"I Lopez-Gonzalez","year":"2017","unstructured":"Lopez-Gonzalez I, Viana R, Sanz P, Ferrer I (2017) Inflammation in Lafora disease: evolution with disease progression in laforin and malin knock-out mouse models. Mol Neurobiol 54:3119\u20133130. https:\/\/doi.org\/10.1007\/s12035-016-9884-4","journal-title":"Mol Neurobiol"},{"key":"2698_CR64","doi-asserted-by":"publisher","first-page":"867","DOI":"10.1002\/ana.410440604","volume":"44","author":"A Lossos","year":"1998","unstructured":"Lossos A, Meiner Z, Barash V, Soffer D, Schlesinger I, Abramsky O et al (1998) Adult polyglucosan body disease in Ashkenazi Jewish patients carrying the Tyr329Ser mutation in the glycogen-branching enzyme gene. Ann Neurol 44:867\u2013872. https:\/\/doi.org\/10.1002\/ana.410440604","journal-title":"Ann Neurol"},{"key":"2698_CR65","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1113\/expphysiol.2010.053157","volume":"96","author":"PJ Magistretti","year":"2011","unstructured":"Magistretti PJ (2011) Neuron-glia metabolic coupling and plasticity. Exp Physiol 96:407\u2013410. https:\/\/doi.org\/10.1113\/expphysiol.2010.053157","journal-title":"Exp Physiol"},{"key":"2698_CR66","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1016\/0306-4522(88)90338-7","volume":"24","author":"PJ Magistretti","year":"1988","unstructured":"Magistretti PJ, Morrison JH (1988) Noradrenaline and vasoactive intestinal peptide-containing neuronal systems in neocortex: functional convergence with contrasting morphology. Neuroscience 24:367\u2013378. https:\/\/doi.org\/10.1016\/0306-4522(88)90338-7","journal-title":"Neuroscience"},{"key":"2698_CR67","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1126\/science.283.5401.496","volume":"283","author":"PJ Magistretti","year":"1999","unstructured":"Magistretti PJ, Pellerin L, Rothman DL, Shulman RG (1999) Energy on demand. Science 283:496\u2013497. https:\/\/doi.org\/10.1126\/science.283.5401.496","journal-title":"Science"},{"key":"2698_CR68","doi-asserted-by":"publisher","first-page":"3388","DOI":"10.1016\/j.bbagen.2016.08.021","volume":"1861","author":"CA Maile","year":"2017","unstructured":"Maile CA, Hingst JR, Mahalingan KK, O\u2019Reilly AO, Cleasby ME, Mickelson JR et al (2017) A highly prevalent equine glycogen storage disease is explained by constitutive activation of a mutant glycogen synthase. Biochim Biophys Acta Gen Subj 1861:3388\u20133398. https:\/\/doi.org\/10.1016\/j.bbagen.2016.08.021","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"2698_CR69","doi-asserted-by":"publisher","first-page":"10707","DOI":"10.1073\/pnas.93.20.10707","volume":"93","author":"J Manchester","year":"1996","unstructured":"Manchester J, Skurat AV, Roach P, Hauschka SD, Lawrence JC Jr (1996) Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle. Proc Natl Acad Sci U S A 93:10707\u201310711. https:\/\/doi.org\/10.1073\/pnas.93.20.10707","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2698_CR70","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1038\/2470","volume":"20","author":"BA Minassian","year":"1998","unstructured":"Minassian BA, Lee JR, Herbrick JA, Huizenga J, Soder S, Mungall AJ et al (1998) Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat Genet 20:171\u2013174. https:\/\/doi.org\/10.1038\/2470","journal-title":"Nat Genet"},{"key":"2698_CR71","doi-asserted-by":"publisher","DOI":"10.1242\/dmm.049802","author":"S Mitra","year":"2023","unstructured":"Mitra S, Chen B, Wang P, Chown EE, Dear M, Guisso DR et al (2023) Laforin targets malin to glycogen in Lafora progressive myoclonus epilepsy. Dis Model Mech. https:\/\/doi.org\/10.1242\/dmm.049802","journal-title":"Dis Model Mech"},{"key":"2698_CR72","doi-asserted-by":"publisher","first-page":"C1146","DOI":"10.1152\/ajpcell.00252.2012","volume":"303","author":"RM Murphy","year":"2012","unstructured":"Murphy RM, Xu H, Latchman H, Larkins NT, Gooley PR, Stapleton DI (2012) Single fiber analyses of glycogen-related proteins reveal their differential association with glycogen in rat skeletal muscle. Am J Physiol Cell Physiol 303:C1146-1155. https:\/\/doi.org\/10.1152\/ajpcell.00252.2012","journal-title":"Am J Physiol Cell Physiol"},{"key":"2698_CR73","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1001\/archneur.1974.00490360042009","volume":"30","author":"HE Neville","year":"1974","unstructured":"Neville HE, Brooke MH, Austin JH (1974) Studies in myoclonus epilepsy. (Lafora body form). IV Skeletal muscle abnormalities Arch Neurol 30:466\u2013474. https:\/\/doi.org\/10.1001\/archneur.1974.00490360042009","journal-title":"IV Skeletal muscle abnormalities Arch Neurol"},{"key":"2698_CR74","doi-asserted-by":"publisher","first-page":"914","DOI":"10.1002\/ana.23963","volume":"74","author":"J Nilsson","year":"2013","unstructured":"Nilsson J, Schoser B, Laforet P, Kalev O, Lindberg C, Romero NB et al (2013) Polyglucosan body myopathy caused by defective ubiquitin ligase RBCK1. Ann Neurol 74:914\u2013919. https:\/\/doi.org\/10.1002\/ana.23963","journal-title":"Ann Neurol"},{"key":"2698_CR75","doi-asserted-by":"publisher","first-page":"906","DOI":"10.15252\/emmm.201707608","volume":"9","author":"F Nitschke","year":"2017","unstructured":"Nitschke F, Sullivan MA, Wang P, Zhao X, Chown EE, Perri AM et al (2017) Abnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease. EMBO Mol Med 9:906\u2013917. https:\/\/doi.org\/10.15252\/emmm.201707608","journal-title":"EMBO Mol Med"},{"key":"2698_CR76","doi-asserted-by":"publisher","first-page":"2361","DOI":"10.1093\/brain\/awac017","volume":"145","author":"S Nitschke","year":"2022","unstructured":"Nitschke S, Sullivan MA, Mitra S, Marchioni CR, Lee JPY, Smith BH et al (2022) Glycogen synthase downregulation rescues the amylopectinosis of murine RBCK1 deficiency. Brain 145:2361\u20132377. https:\/\/doi.org\/10.1093\/brain\/awac017","journal-title":"Brain"},{"key":"2698_CR77","doi-asserted-by":"publisher","first-page":"479","DOI":"10.3389\/fimmu.2019.00479","volume":"10","author":"H Oda","year":"2019","unstructured":"Oda H, Beck DB, Kuehn HS, Sampaio Moura N, Hoffmann P, Ibarra M et al (2019) Second case of HOIP deficiency expands clinical features and defines inflammatory transcriptome regulated by LUBAC. Front Immunol 10:479. https:\/\/doi.org\/10.3389\/fimmu.2019.00479","journal-title":"Front Immunol"},{"key":"2698_CR78","doi-asserted-by":"publisher","first-page":"6801","DOI":"10.1093\/hmg\/ddv385","volume":"24","author":"H Orhan Akman","year":"2015","unstructured":"Orhan Akman H, Emmanuele V, Kurt YG, Kurt B, Sheiko T, DiMauro S et al (2015) A novel mouse model that recapitulates adult-onset glycogenosis type 4. Hum Mol Genet 24:6801\u20136810. https:\/\/doi.org\/10.1093\/hmg\/ddv385","journal-title":"Hum Mol Genet"},{"key":"2698_CR79","doi-asserted-by":"publisher","first-page":"10625","DOI":"10.1073\/pnas.91.22.10625","volume":"91","author":"L Pellerin","year":"1994","unstructured":"Pellerin L, Magistretti PJ (1994) Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization. Proc Natl Acad Sci U S A 91:10625\u201310629. https:\/\/doi.org\/10.1073\/pnas.91.22.10625","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2698_CR80","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1038\/s41586-018-0064-8","volume":"557","author":"N Peltzer","year":"2018","unstructured":"Peltzer N, Darding M, Montinaro A, Draber P, Draberova H, Kupka S et al (2018) LUBAC is essential for embryogenesis by preventing cell death and enabling haematopoiesis. Nature 557:112\u2013117. https:\/\/doi.org\/10.1038\/s41586-018-0064-8","journal-title":"Nature"},{"key":"2698_CR81","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.celrep.2014.08.066","volume":"9","author":"N Peltzer","year":"2014","unstructured":"Peltzer N, Rieser E, Taraborrelli L, Draber P, Darding M, Pernaute B et al (2014) HOIP deficiency causes embryonic lethality by aberrant TNFR1-mediated endothelial cell death. Cell Rep 9:153\u2013165. https:\/\/doi.org\/10.1016\/j.celrep.2014.08.066","journal-title":"Cell Rep"},{"key":"2698_CR82","doi-asserted-by":"publisher","first-page":"1002","DOI":"10.1002\/jimd.12234","volume":"43","author":"R Phadke","year":"2020","unstructured":"Phadke R, Hedberg-Oldfors C, Scalco RS, Lowe DM, Ashworth M, Novelli M et al (2020) RBCK1-related disease: a rare multisystem disorder with polyglucosan storage, auto-inflammation, recurrent infections, skeletal, and cardiac myopathy-Four additional patients and a review of the current literature. J Inherit Metab Dis 43:1002\u20131013. https:\/\/doi.org\/10.1002\/jimd.12234","journal-title":"J Inherit Metab Dis"},{"key":"2698_CR83","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0085666","volume":"9","author":"CS Potter","year":"2014","unstructured":"Potter CS, Wang Z, Silva KA, Kennedy VE, Stearns TM, Burzenski L et al (2014) Chronic proliferative dermatitis in Sharpin null mice: development of an autoinflammatory disease in the absence of B and T lymphocytes and IL4\/IL13 signaling. PLoS ONE 9:e85666. https:\/\/doi.org\/10.1371\/journal.pone.0085666","journal-title":"PLoS ONE"},{"key":"2698_CR84","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1093\/hmg\/ddr452","volume":"21","author":"R Puri","year":"2012","unstructured":"Puri R, Suzuki T, Yamakawa K, Ganesh S (2012) Dysfunctions in endosomal-lysosomal and autophagy pathways underlie neuropathology in a mouse model for Lafora disease. Hum Mol Genet 21:175\u2013184. https:\/\/doi.org\/10.1093\/hmg\/ddr452","journal-title":"Hum Mol Genet"},{"key":"2698_CR85","doi-asserted-by":"publisher","first-page":"1739","DOI":"10.1212\/wnl.56.12.1739","volume":"56","author":"N Raben","year":"2001","unstructured":"Raben N, Danon M, Lu N, Lee E, Shliselfeld L, Skurat AV et al (2001) Surprises of genetic engineering: a possible model of polyglucosan body disease. Neurology 56:1739\u20131745. https:\/\/doi.org\/10.1212\/wnl.56.12.1739","journal-title":"Neurology"},{"key":"2698_CR86","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1016\/s0387-7604(12)80277-4","volume":"14","author":"E Reusche","year":"1992","unstructured":"Reusche E, Aksu F, Goebel HH, Shin YS, Yokota T, Reichmann H (1992) A mild juvenile variant of type IV glycogenosis. Brain Dev 14:36\u201343. https:\/\/doi.org\/10.1016\/s0387-7604(12)80277-4","journal-title":"Brain Dev"},{"key":"2698_CR87","doi-asserted-by":"publisher","first-page":"1176","DOI":"10.3389\/fnins.2019.01176","volume":"13","author":"LR Rich","year":"2019","unstructured":"Rich LR, Harris W, Brown AM (2019) The role of brain glycogen in supporting physiological function. Front Neurosci 13:1176. https:\/\/doi.org\/10.3389\/fnins.2019.01176","journal-title":"Front Neurosci"},{"key":"2698_CR88","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1042\/BJ20111416","volume":"441","author":"PJ Roach","year":"2012","unstructured":"Roach PJ, Depaoli-Roach AA, Hurley TD, Tagliabracci VS (2012) Glycogen and its metabolism: some new developments and old themes. Biochem J 441:763\u2013787. https:\/\/doi.org\/10.1042\/BJ20111416","journal-title":"Biochem J"},{"key":"2698_CR89","first-page":"609","volume-title":"Handbook of physiology","author":"PJ Roach","year":"2001","unstructured":"Roach PJ, Skurat AV, Harris RA (2001) Regulation of Glycogen Metabolism. Handbook of physiology, vol II. Lippincott Company, Philadelphia, pp 609\u2013647"},{"key":"2698_CR90","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1093\/brain\/103.2.315","volume":"103","author":"Y Robitaille","year":"1980","unstructured":"Robitaille Y, Carpenter S, Karpati G, DiMauro SD (1980) A distinct form of adult polyglucosan body disease with massive involvement of central and peripheral neuronal processes and astrocytes: a report of four cases and a review of the occurrence of polyglucosan bodies in other conditions such as Lafora\u2019s disease and normal ageing. Brain 103:315\u2013336. https:\/\/doi.org\/10.1093\/brain\/103.2.315","journal-title":"Brain"},{"issue":"10","key":"2698_CR91","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.60660","volume":"10","author":"A Rodriguez Carvajal","year":"2021","unstructured":"Rodriguez Carvajal A, Grishkovskaya I, Gomez Diaz C, Vogel A, Sonn-Segev A, Kushwah MS et al (2021) The linear ubiquitin chain assembly complex (LUBAC) generates heterotypic ubiquitin chains. Elife 10(10):e60660. https:\/\/doi.org\/10.7554\/eLife.60660","journal-title":"Elife"},{"key":"2698_CR92","doi-asserted-by":"publisher","first-page":"1290","DOI":"10.1093\/hmg\/ddy044","volume":"27","author":"C Rubio-Villena","year":"2018","unstructured":"Rubio-Villena C, Viana R, Bonet J, Garcia-Gimeno MA, Casado M, Heredia M et al (2018) Astrocytes: new players in progressive myoclonus epilepsy of Lafora type. Hum Mol Genet 27:1290\u20131300. https:\/\/doi.org\/10.1093\/hmg\/ddy044","journal-title":"Hum Mol Genet"},{"key":"2698_CR93","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2019.118613","volume":"1867","author":"P Sanchez-Martin","year":"2020","unstructured":"Sanchez-Martin P, Lahuerta M, Viana R, Knecht E, Sanz P (2020) Regulation of the autophagic PI3KC3 complex by laforin\/malin E3-ubiquitin ligase, two proteins involved in Lafora disease. Biochim Biophys Acta Mol Cell Res 1867:118613. https:\/\/doi.org\/10.1016\/j.bbamcr.2019.118613","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"2698_CR94","doi-asserted-by":"publisher","DOI":"10.7860\/JCDR\/2017\/28570.10552","author":"P Sathiah","year":"2017","unstructured":"Sathiah P, Gochhait D, Dehuri P, Subramanian H (2017) Diagnosis of Lafora disease by skin biopsy. J Clin Diagn Res. https:\/\/doi.org\/10.7860\/JCDR\/2017\/28570.10552","journal-title":"J Clin Diagn Res"},{"key":"2698_CR95","doi-asserted-by":"publisher","first-page":"1447","DOI":"10.1152\/physrev.00031.2010","volume":"91","author":"S Schiaffino","year":"2011","unstructured":"Schiaffino S, Reggiani C (2011) Fiber types in mammalian skeletal muscles. Physiol Rev 91:1447\u20131531. https:\/\/doi.org\/10.1152\/physrev.00031.2010","journal-title":"Physiol Rev"},{"key":"2698_CR96","doi-asserted-by":"publisher","first-page":"172","DOI":"10.1001\/archneur.1965.00460260062008","volume":"12","author":"GA Schwarz","year":"1965","unstructured":"Schwarz GA, Yanoff M (1965) Lafora\u2019s Disease. Distinct clinico-pathologic form of Unverricht\u2019s syndrome. Arch Neurol 12:172\u2013188. https:\/\/doi.org\/10.1001\/archneur.1965.00460260062008","journal-title":"Arch Neurol"},{"key":"2698_CR97","doi-asserted-by":"publisher","first-page":"1810","DOI":"10.1093\/ptj\/81.11.1810","volume":"81","author":"W Scott","year":"2001","unstructured":"Scott W, Stevens J, Binder-Macleod SA (2001) Human skeletal muscle fiber type classifications. Phys Ther 81:1810\u20131816","journal-title":"Phys Ther"},{"key":"2698_CR98","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/s0022-3476(87)80341-4","volume":"111","author":"S Servidei","year":"1987","unstructured":"Servidei S, Riepe RE, Langston C, Tani LY, Bricker JT, Crisp-Lindgren N et al (1987) Severe cardiopathy in branching enzyme deficiency. J Pediatr 111:51\u201356. https:\/\/doi.org\/10.1016\/s0022-3476(87)80341-4","journal-title":"J Pediatr"},{"key":"2698_CR99","volume-title":"Theory and practice of histotechnology","author":"DC Sheehan","year":"1980","unstructured":"Sheehan DC, Hrapchak BB (1980) Theory and practice of histotechnology. Mosby, Maryland Heights"},{"key":"2698_CR100","doi-asserted-by":"publisher","first-page":"3833","DOI":"10.1038\/emboj.2012.217","volume":"31","author":"JJ Smit","year":"2012","unstructured":"Smit JJ, Monteferrario D, Noordermeer SM, van Dijk WJ, van der Reijden BA, Sixma TK (2012) The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension. EMBO J 31:3833\u20133844. https:\/\/doi.org\/10.1038\/emboj.2012.217","journal-title":"EMBO J"},{"key":"2698_CR101","doi-asserted-by":"publisher","first-page":"31728","DOI":"10.1074\/jbc.M113.495846","volume":"288","author":"JJ Smit","year":"2013","unstructured":"Smit JJ, van Dijk WJ, El Atmioui D, Merkx R, Ovaa H, Sixma TK (2013) Target specificity of the E3 ligase LUBAC for ubiquitin and NEMO relies on different minimal requirements. J Biol Chem 288:31728\u201331737. https:\/\/doi.org\/10.1074\/jbc.M113.495846","journal-title":"J Biol Chem"},{"key":"2698_CR102","doi-asserted-by":"publisher","first-page":"840","DOI":"10.1038\/embor.2012.105","volume":"13","author":"B Stieglitz","year":"2012","unstructured":"Stieglitz B, Morris-Davies AC, Koliopoulos MG, Christodoulou E, Rittinger K (2012) LUBAC synthesizes linear ubiquitin chains via a thioester intermediate. EMBO Rep 13:840\u2013846. https:\/\/doi.org\/10.1038\/embor.2012.105","journal-title":"EMBO Rep"},{"key":"2698_CR103","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1038\/nature12638","volume":"503","author":"B Stieglitz","year":"2013","unstructured":"Stieglitz B, Rana RR, Koliopoulos MG, Morris-Davies AC, Schaeffer V, Christodoulou E et al (2013) Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP. Nature 503:422\u2013426. https:\/\/doi.org\/10.1038\/nature12638","journal-title":"Nature"},{"issue":"1334\u20131344","key":"2698_CR104","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2019.04.017","volume":"27","author":"MA Sullivan","year":"2019","unstructured":"Sullivan MA, Nitschke S, Skwara EP, Wang P, Zhao X, Pan XS et al (2019) Skeletal muscle glycogen chain length correlates with insolubility in mouse models of polyglucosan-associated neurodegenerative diseases. Cell Rep 27(1334\u20131344):e1336. https:\/\/doi.org\/10.1016\/j.celrep.2019.04.017","journal-title":"Cell Rep"},{"key":"2698_CR105","doi-asserted-by":"publisher","DOI":"10.1016\/j.cmet.2021.05.003","author":"RC Sun","year":"2021","unstructured":"Sun RC, Young LEA, Bruntz RC, Markussen KH, Zhou Z, Conroy LR et al (2021) Brain glycogen serves as a critical glucosamine cache required for protein glycosylation. Cell Metab. https:\/\/doi.org\/10.1016\/j.cmet.2021.05.003","journal-title":"Cell Metab"},{"key":"2698_CR106","first-page":"553","volume":"19","author":"T Minagawa","year":"1943","unstructured":"Minagawa T (1943) Purified diastases: properties of diastase action. PJAB 19:553\u2013556","journal-title":"PJAB"},{"key":"2698_CR107","doi-asserted-by":"publisher","first-page":"33816","DOI":"10.1074\/jbc.M807428200","volume":"283","author":"VS Tagliabracci","year":"2008","unstructured":"Tagliabracci VS, Girard JM, Segvich D, Meyer C, Turnbull J, Zhao X et al (2008) Abnormal metabolism of glycogen phosphate as a cause for Lafora disease. J Biol Chem 283:33816\u201333825. https:\/\/doi.org\/10.1074\/jbc.M807428200","journal-title":"J Biol Chem"},{"key":"2698_CR108","doi-asserted-by":"publisher","first-page":"19262","DOI":"10.1073\/pnas.0707952104","volume":"104","author":"VS Tagliabracci","year":"2007","unstructured":"Tagliabracci VS, Turnbull J, Wang W, Girard JM, Zhao X, Skurat AV et al (2007) Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc Natl Acad Sci U S A 104:19262\u201319266. https:\/\/doi.org\/10.1073\/pnas.0707952104","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2698_CR109","doi-asserted-by":"publisher","first-page":"3538","DOI":"10.1021\/acs.jmedchem.9b01851","volume":"63","author":"B Tang","year":"2020","unstructured":"Tang B, Frasinyuk MS, Chikwana VM, Mahalingan KK, Morgan CA, Segvich DM et al (2020) Discovery and development of small-molecule inhibitors of glycogen synthase. J Med Chem 63:3538\u20133551. https:\/\/doi.org\/10.1021\/acs.jmedchem.9b01851","journal-title":"J Med Chem"},{"key":"2698_CR110","doi-asserted-by":"publisher","DOI":"10.1111\/nan.12761","author":"C Thomsen","year":"2022","unstructured":"Thomsen C, Malfatti E, Jovanovic A, Roberts M, Kalev O, Lindberg C et al (2022) Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency. Neuropathol Appl Neurobiol. https:\/\/doi.org\/10.1111\/nan.12761","journal-title":"Neuropathol Appl Neurobiol"},{"key":"2698_CR111","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1507\/endocrj.ej12-0148","volume":"59","author":"F Tokunaga","year":"2012","unstructured":"Tokunaga F, Iwai K (2012) Linear ubiquitination: a novel NF-kappaB regulatory mechanism for inflammatory and immune responses by the LUBAC ubiquitin ligase complex. Endocr J 59:641\u2013652. https:\/\/doi.org\/10.1507\/endocrj.ej12-0148","journal-title":"Endocr J"},{"key":"2698_CR112","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1038\/ncb1821","volume":"11","author":"F Tokunaga","year":"2009","unstructured":"Tokunaga F, Sakata S, Saeki Y, Satomi Y, Kirisako T, Kamei K et al (2009) Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation. Nat Cell Biol 11:123\u2013132. https:\/\/doi.org\/10.1038\/ncb1821","journal-title":"Nat Cell Biol"},{"key":"2698_CR113","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1002\/ana.24104","volume":"75","author":"J Turnbull","year":"2014","unstructured":"Turnbull J, Epp JR, Goldsmith D, Zhao X, Pencea N, Wang P et al (2014) PTG protein depletion rescues malin-deficient Lafora disease in mouse. Ann Neurol 75:442\u2013446. https:\/\/doi.org\/10.1002\/ana.24104","journal-title":"Ann Neurol"},{"key":"2698_CR114","doi-asserted-by":"publisher","first-page":"2684","DOI":"10.1093\/brain\/aws205","volume":"135","author":"J Turnbull","year":"2012","unstructured":"Turnbull J, Girard JM, Lohi H, Chan EM, Wang P, Tiberia E et al (2012) Early-onset Lafora body disease. Brain 135:2684\u20132698. https:\/\/doi.org\/10.1093\/brain\/aws205","journal-title":"Brain"},{"key":"2698_CR115","doi-asserted-by":"publisher","first-page":"1674","DOI":"10.1212\/WNL.0b013e318219faf6","volume":"76","author":"J Turnbull","year":"2011","unstructured":"Turnbull J, Girard JM, Pencea N, Zhao X, Graham TE, Wang P et al (2011) Lafora bodies in skeletal muscle are fiber type specific. Neurology 76:1674\u20131676. https:\/\/doi.org\/10.1212\/WNL.0b013e318219faf6","journal-title":"Neurology"},{"key":"2698_CR116","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1684\/epd.2016.0842","volume":"18","author":"J Turnbull","year":"2016","unstructured":"Turnbull J, Tiberia E, Striano P, Genton P, Carpenter S, Ackerley CA et al (2016) Lafora disease. Epileptic Disord 18:38\u201362. https:\/\/doi.org\/10.1684\/epd.2016.0842","journal-title":"Epileptic Disord"},{"key":"2698_CR117","doi-asserted-by":"publisher","first-page":"925","DOI":"10.1002\/ana.22156","volume":"68","author":"J Turnbull","year":"2010","unstructured":"Turnbull J, Wang P, Girard JM, Ruggieri A, Wang TJ, Draginov AG et al (2010) Glycogen hyperphosphorylation underlies lafora body formation. Ann Neurol 68:925\u2013933. https:\/\/doi.org\/10.1002\/ana.22156","journal-title":"Ann Neurol"},{"key":"2698_CR118","doi-asserted-by":"publisher","first-page":"667","DOI":"10.1002\/emmm.201100174","volume":"3","author":"J Valles-Ortega","year":"2011","unstructured":"Valles-Ortega J, Duran J, Garcia-Rocha M, Bosch C, Saez I, Pujadas L et al (2011) Neurodegeneration and functional impairments associated with glycogen synthase accumulation in a mouse model of Lafora disease. EMBO Mol Med 3:667\u2013681. https:\/\/doi.org\/10.1002\/emmm.201100174","journal-title":"EMBO Mol Med"},{"key":"2698_CR119","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1007\/BF00688087","volume":"7","author":"F Van Hoof","year":"1967","unstructured":"Van Hoof F, Hageman-Bal M (1967) Progressive familial myoclonic epilepsy with Lafora bodies. Electron microscopic and histochemical study of a cerebral biopsy. Acta Neuropathol 7:315\u2013336. https:\/\/doi.org\/10.1007\/BF00688087","journal-title":"Acta Neuropathol"},{"key":"2698_CR120","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2020.105173","volume":"147","author":"O Varea","year":"2021","unstructured":"Varea O, Duran J, Aguilera M, Prats N, Guinovart JJ (2021) Suppression of glycogen synthesis as a treatment for Lafora disease: Establishing the window of opportunity. Neurobiol Dis 147:105173. https:\/\/doi.org\/10.1016\/j.nbd.2020.105173","journal-title":"Neurobiol Dis"},{"key":"2698_CR121","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1055\/s-0038-1675238","volume":"49","author":"B Verhalen","year":"2018","unstructured":"Verhalen B, Arnold S, Minassian BA (2018) Lafora Disease: a review of molecular mechanisms and pathology. Neuropediatrics 49:357\u2013362. https:\/\/doi.org\/10.1055\/s-0038-1675238","journal-title":"Neuropediatrics"},{"key":"2698_CR122","doi-asserted-by":"publisher","first-page":"1407","DOI":"10.1038\/nn1998","volume":"10","author":"D Vilchez","year":"2007","unstructured":"Vilchez D, Ros S, Cifuentes D, Pujadas L, Valles J, Garcia-Fojeda B et al (2007) Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy. Nat Neurosci 10:1407\u20131413. https:\/\/doi.org\/10.1038\/nn1998","journal-title":"Nat Neurosci"},{"key":"2698_CR123","doi-asserted-by":"publisher","first-page":"1878","DOI":"10.1016\/j.jmb.2019.03.005","volume":"431","author":"R Vohra","year":"2019","unstructured":"Vohra R, Aldana BI, Bulli G, Skytt DM, Waagepetersen H, Bergersen LH et al (2019) Lactate-mediated protection of retinal ganglion cells. J Mol Biol 431:1878\u20131888. https:\/\/doi.org\/10.1016\/j.jmb.2019.03.005","journal-title":"J Mol Biol"},{"key":"2698_CR124","volume-title":"Laboratory histopathology: a complete reference","author":"AE Woods","year":"1994","unstructured":"Woods AE, Roy C (1994) Laboratory histopathology: a complete reference. Churchill Livingstone Press, London"},{"key":"2698_CR125","doi-asserted-by":"publisher","first-page":"30412","DOI":"10.1074\/jbc.M606117200","volume":"281","author":"CA Worby","year":"2006","unstructured":"Worby CA, Gentry MS, Dixon JE (2006) Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J Biol Chem 281:30412\u201330418. https:\/\/doi.org\/10.1074\/jbc.M606117200","journal-title":"J Biol Chem"},{"key":"2698_CR126","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1111\/j.1440-1827.1992.tb01879.x","volume":"42","author":"S Yamanami","year":"1992","unstructured":"Yamanami S, Ishihara T, Takahashi M, Uchino F (1992) Comparative study of intraneuronal polyglucosan bodies in brains from patients with Lafora disease and aged dogs. Acta Pathol Jpn 42:787\u2013792. https:\/\/doi.org\/10.1111\/j.1440-1827.1992.tb01879.x","journal-title":"Acta Pathol Jpn"},{"key":"2698_CR127","first-page":"13","volume":"4","author":"N Yoshimura","year":"2013","unstructured":"Yoshimura N (2013) Brain pathology of Lafora Disease: localization of polyglucosan aggrgations (Lafora bodies) within neuronal networks of cerebrellar cortex. J Hirosaki Univ Health Welfare 4:13\u201324","journal-title":"J Hirosaki Univ Health Welfare"}],"container-title":["Acta Neuropathologica"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00401-024-02698-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00401-024-02698-x\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00401-024-02698-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,2,27]],"date-time":"2024-02-27T12:09:07Z","timestamp":1709035747000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00401-024-02698-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,2,27]]},"references-count":127,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2024,6]]}},"alternative-id":["2698"],"URL":"https:\/\/doi.org\/10.1007\/s00401-024-02698-x","relation":{},"ISSN":["0001-6322","1432-0533"],"issn-type":[{"value":"0001-6322","type":"print"},{"value":"1432-0533","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,2,27]]},"assertion":[{"value":"23 November 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"13 January 2024","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 January 2024","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 February 2024","order":4,"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 that they do not have any competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interests"}}],"article-number":"46"}}