{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T03:48:39Z","timestamp":1790999319364,"version":"4.1.0"},"reference-count":51,"publisher":"Oxford University Press (OUP)","issue":"14","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,7,15]]},"DOI":"10.1093\/hmg\/ddq190","type":"journal-article","created":{"date-parts":[[2010,5,8]],"date-time":"2010-05-08T01:36:00Z","timestamp":1273282560000},"page":"2867-2876","source":"Crossref","is-referenced-by-count":171,"title":["Laforin, the most common protein mutated in Lafora disease, regulates autophagy"],"prefix":"10.1093","volume":"19","author":[{"given":"Carmen","family":"Aguado","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sovan","family":"Sarkar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Viktor I.","family":"Korolchuk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga","family":"Criado","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Santiago","family":"Vernia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia","family":"Boya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pascual","family":"Sanz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Santiago Rodr\u00edguez","family":"de C\u00f3rdoba","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erwin","family":"Knecht","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David C.","family":"Rubinsztein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2010,5,7]]},"reference":[{"key":"key\n\t\t\t\t20170522135758_DDQ190C1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/BF02863929","article-title":"Beitrag zur Histopathologie der myoklonischen Epilepsie","volume":"6","author":"Lafora","year":"1911","journal-title":"Z. Gesammte Neurol. Psychiatr."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C2","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1007\/BF00688087","article-title":"Progressive familial myoclonic epilepsy with Lafora bodies. Electron microscopic and histochemical study of a cerebral biopsy","volume":"7","author":"Van Hoof","year":"1967","journal-title":"Acta Neuropathol."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C3","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/0009-8981(75)90093-5","article-title":"Biochemical studies on tissues from a patient with Lafora disease","volume":"62","author":"Yokoi","year":"1975","journal-title":"Clin. Chim. Acta"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C4","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1093\/hmg\/11.11.1263","article-title":"Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype","volume":"11","author":"Ganesh","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C5","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.jns.2006.09.021","article-title":"Progressive myoclonic epilepsy: a clinical, electrophysiological and pathological study from South India","volume":"252","author":"Sinha","year":"2007","journal-title":"J. Neurol. Sci."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C6","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1001\/archneur.1968.00480010033002","article-title":"Studies in myoclonus epilepsy (Lafora body form). Isolation and preliminary characterization of Lafora bodies in two cases","volume":"19","author":"Yokoi","year":"1968","journal-title":"Arch. Neurol."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C7","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1038\/2470","article-title":"Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy","volume":"20","author":"Minassian","year":"1998","journal-title":"Nat. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C8","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1093\/hmg\/8.2.345","article-title":"A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2)","volume":"8","author":"Serratosa","year":"1999","journal-title":"Hum. Mol. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C9","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/ng1238","article-title":"Mutations in NHLRC1 cause progressive myoclonus epilepsy","volume":"35","author":"Chan","year":"2003","journal-title":"Nat. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C10","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1212\/01.WNL.0000133215.65836.03","article-title":"Progressive myoclonus epilepsy with polyglucosans (Lafora disease): evidence for a third locus","volume":"63","author":"Chan","year":"2004","journal-title":"Neurology"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C11","doi-asserted-by":"crossref","first-page":"8501","DOI":"10.1073\/pnas.0503285102","article-title":"Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin","volume":"102","author":"Gentry","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C12","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1093\/hmg\/ddm339","article-title":"Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway","volume":"17","author":"Solaz-Fuster","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C13","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1038\/nn1998","article-title":"Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy","volume":"10","author":"Vilchez","year":"2007","journal-title":"Nat. Neurosci."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C14","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.1101\/gad.1553207","article-title":"A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease","volume":"21","author":"Cheng","year":"2007","journal-title":"Genes Dev."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C15","doi-asserted-by":"crossref","first-page":"4069","DOI":"10.1074\/jbc.M708712200","article-title":"Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)","volume":"283","author":"Worby","year":"2008","journal-title":"J. Biol. Chem."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C16","doi-asserted-by":"crossref","first-page":"30412","DOI":"10.1074\/jbc.M606117200","article-title":"Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates","volume":"281","author":"Worby","year":"2006","journal-title":"J. Biol. Chem."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C17","doi-asserted-by":"crossref","first-page":"19262","DOI":"10.1073\/pnas.0707952104","article-title":"Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo","volume":"104","author":"Tagliabracci","year":"2007","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C18","doi-asserted-by":"crossref","first-page":"33816","DOI":"10.1074\/jbc.M807428200","article-title":"Abnormal metabolism of glycogen phosphate as a cause for Lafora disease","volume":"283","author":"Tagliabracci","year":"2008","journal-title":"J. Biol. Chem."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C19","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1083\/jcb.200704094","article-title":"The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease","volume":"178","author":"Gentry","year":"2007","journal-title":"J. Cell Biol."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C20","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1007\/s11910-007-0066-7","article-title":"Advances in Lafora progressive myoclonus epilepsy","volume":"7","author":"Delgado-Escueta","year":"2007","journal-title":"Curr. Neurol. Neurosci. Rep."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C21","doi-asserted-by":"crossref","first-page":"413","DOI":"10.4161\/auto.4377","article-title":"How shall I eat thee?","volume":"3","author":"Klionsky","year":"2007","journal-title":"Autophagy"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C22","author":"Garc\u00eda-Arencibia","year":"2010","journal-title":"Semin. Cell Dev. Biol"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C23","doi-asserted-by":"crossref","first-page":"2427","DOI":"10.1007\/s00018-009-0030-6","article-title":"Intracellular protein degradation in mammalian cells: recent developments","volume":"66","author":"Knecht","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C24","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1242\/jcs.031773","article-title":"Mammalian macroautophagy at a glance","volume":"122","author":"Ravikumar","year":"2009","journal-title":"J. Cell Sci."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C25","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1038\/nature04723","article-title":"Loss of autophagy in the central nervous system causes neurodegeneration in mice","volume":"441","author":"Komatsu","year":"2006","journal-title":"Nature"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C26","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.prp.2006.04.001","article-title":"Glycogen autophagy in glucose homeostasis","volume":"202","author":"Kotoulas","year":"2006","journal-title":"Pathol. Res. Pract."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C27","first-page":"S42","article-title":"Autophagy in skeletal muscle: implications for Pompe disease","volume":"47","author":"Shea","year":"2009","journal-title":"Int. J. Clin. Pharmacol. Ther."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C28","doi-asserted-by":"crossref","first-page":"84","DOI":"10.4161\/auto.1.2.1697","article-title":"Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy","volume":"1","author":"Tanida","year":"2005","journal-title":"Autophagy"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C29","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.mam.2006.08.002","article-title":"Signalling and autophagy regulation in health, aging and disease","volume":"27","author":"Meijer","year":"2006","journal-title":"Mol. Aspects Med."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C30","doi-asserted-by":"crossref","first-page":"2445","DOI":"10.1016\/j.biocel.2004.02.002","article-title":"Regulation and role of autophagy in mammalian cells","volume":"36","author":"Meijer","year":"2004","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C31","doi-asserted-by":"crossref","first-page":"4263","DOI":"10.1111\/j.1742-4658.2008.06562.x","article-title":"Huntington's disease: degradation of mutant huntingtin by autophagy","volume":"275","author":"Sarkar","year":"2008","journal-title":"FEBS J."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C32","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1172\/JCI200317222","article-title":"Loss of Tsc1\/Tsc2 activates mTOR and disrupts PI3K-Akt signaling through downregulation of PDGFR","volume":"112","author":"Zhang","year":"2003","journal-title":"J. Clin. Invest."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C33","doi-asserted-by":"crossref","first-page":"4153","DOI":"10.1093\/hmg\/ddp367","article-title":"Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing","volume":"18","author":"Wang","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C34","doi-asserted-by":"crossref","first-page":"22657","DOI":"10.1074\/jbc.M109.009688","article-title":"Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease","volume":"284","author":"Puri","year":"2009","journal-title":"J. Biol. Chem."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C35","doi-asserted-by":"crossref","first-page":"138","DOI":"10.4161\/auto.2.2.2405","article-title":"p62\/SQSTM1: a missing link between protein aggregates and the autophagy machinery","volume":"2","author":"Bj\u00f8rk\u00f8y","year":"2006","journal-title":"Autophagy"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C36","first-page":"4259","article-title":"A role for ubiquitin in selective autophagy","volume":"3","author":"Kirin","year":"2009","journal-title":"Mol. Cell"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C37","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.molcel.2009.01.021","article-title":"Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates","volume":"33","author":"Korolchuk","year":"2009","journal-title":"Mol. Cell"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C38","doi-asserted-by":"crossref","first-page":"34768","DOI":"10.1074\/jbc.M607778200","article-title":"Dimerization of laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling","volume":"281","author":"Liu","year":"2006","journal-title":"J. Biol. Chem."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C39","first-page":"689","article-title":"Glycogen autophagy in the liver and heart of newborn rats. The effects of glucagon, adrenalin or rapamycin","volume":"20","author":"Kondomerkos","year":"2005","journal-title":"Histol. Histopathol."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C40","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1093\/hmg\/ddl036","article-title":"Rapamycin pre-treatment protects against apoptosis","volume":"15","author":"Ravikumar","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C41","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1136\/jmg.36.10.739","article-title":"A molecular investigation of true dominance in Huntington's disease","volume":"36","author":"Narain","year":"1999","journal-title":"J. Med. Genet."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C42","doi-asserted-by":"crossref","first-page":"5720","DOI":"10.1093\/emboj\/19.21.5720","article-title":"LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing","volume":"19","author":"Kabeya","year":"2000","journal-title":"EMBO J."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C43","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.ccr.2006.08.008","article-title":"Epm2a suppresses tumor growth in an immunocompromised host by inhibiting Wnt signaling","volume":"10","author":"Wang","year":"2006","journal-title":"Cancer Cell"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C44","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1038\/nature03029","article-title":"The role of autophagy during the early neonatal starvation period","volume":"432","author":"Kuma","year":"2004","journal-title":"Nature"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C45","doi-asserted-by":"crossref","first-page":"3415","DOI":"10.1016\/j.febslet.2007.06.043","article-title":"Regulation of various proteolytic pathways by insulin and amino acids in human fibroblasts","volume":"581","author":"Esteban","year":"2007","journal-title":"FEBS Lett."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C46","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0076-6879(08)04005-6","article-title":"Autophagic clearance of aggregate-prone proteins associated with neurodegeneration","volume":"453","author":"Sarkar","year":"2009","journal-title":"Methods Enzymol."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C47","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1042\/bj20030282","article-title":"Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions","volume":"375","author":"Fuertes","year":"2003","journal-title":"Biochem. J."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C48","doi-asserted-by":"crossref","first-page":"849","DOI":"10.4161\/auto.6845","article-title":"Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?","volume":"4","author":"Klionsky","year":"2008","journal-title":"Autophagy"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C49","doi-asserted-by":"crossref","first-page":"585","DOI":"10.4161\/auto.5.5.8823","article-title":"In search of an \u2018autophagomometer","volume":"5","author":"Rubinsztein","year":"2009","journal-title":"Autophagy"},{"key":"key\n\t\t\t\t20170522135758_DDQ190C50","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nchembio883","article-title":"Small molecules enhance autophagy and reduce toxicity in Huntington's disease models","volume":"3","author":"Sarkar","year":"2007","journal-title":"Nat. Chem. Biol."},{"key":"key\n\t\t\t\t20170522135758_DDQ190C51","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/nchembio.79","article-title":"Novel targets for Huntington's disease in an mTOR-independent autophagy pathway","volume":"4","author":"Williams","year":"2008","journal-title":"Nat. Chem. Biol."}],"container-title":["Human Molecular Genetics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/hmg\/article-pdf\/19\/14\/2867\/17249842\/ddq190.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2017,8,23]],"date-time":"2017-08-23T08:48:45Z","timestamp":1503478125000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/hmg\/article-lookup\/doi\/10.1093\/hmg\/ddq190"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,5,7]]},"references-count":51,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2010,5,7]]},"published-print":{"date-parts":[[2010,7,15]]}},"URL":"https:\/\/doi.org\/10.1093\/hmg\/ddq190","relation":{},"ISSN":["1460-2083","0964-6906"],"issn-type":[{"value":"1460-2083","type":"electronic"},{"value":"0964-6906","type":"print"}],"subject":[],"published":{"date-parts":[[2010,5,7]]}}}