{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:15:24Z","timestamp":1777594524153,"version":"3.51.4"},"reference-count":29,"publisher":"Elsevier BV","issue":"18","license":[{"start":{"date-parts":[[2013,12,1]],"date-time":"2013-12-01T00:00:00Z","timestamp":1385856000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,12,1]],"date-time":"2013-12-01T00:00:00Z","timestamp":1385856000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P20RR020171"],"award-info":[{"award-number":["P20RR020171"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01NS070899"],"award-info":[{"award-number":["R01NS070899"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["U24NS050606"],"award-info":[{"award-number":["U24NS050606"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["CA 95616"],"award-info":[{"award-number":["CA 95616"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000179","name":"Office of the Director","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000179","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000097","name":"National Center for Research Resources","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000097","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Clinical Biochemistry"],"published-print":{"date-parts":[[2013,12]]},"DOI":"10.1016\/j.clinbiochem.2013.08.016","type":"journal-article","created":{"date-parts":[[2013,9,5]],"date-time":"2013-09-05T22:16:06Z","timestamp":1378419366000},"page":"1869-1876","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["A bioassay for Lafora disease and laforin glucan phosphatase activity"],"prefix":"10.1016","volume":"46","author":[{"given":"Amanda R.","family":"Sherwood","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mary Beth","family":"Johnson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Antonio V.","family":"Delgado-Escueta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew S.","family":"Gentry","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0005","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/S0887-8994(00)00276-9","article-title":"Lafora's disease: towards a clinical, pathologic, and molecular synthesis","volume":"25","author":"Minassian","year":"2001","journal-title":"Pediatr Neurol"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0010","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1016\/j.tibs.2009.08.002","article-title":"Lafora disease: insights into neurodegeneration from plant metabolism","volume":"34","author":"Gentry","year":"2009","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0015","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1001\/archneur.1968.00480010033002","article-title":"Studies in myoclonus epilepsy (Lafora body form). I. Isolation and preliminary characterization of Lafora bodies in two cases","volume":"19","author":"Yokoi","year":"1968","journal-title":"Arch Neurol"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0020","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":"10.1016\/j.clinbiochem.2013.08.016_bb0025","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":"10.1016\/j.clinbiochem.2013.08.016_bb0030","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/ajmg.1575","article-title":"Advances in the genetics of progressive myoclonus epilepsy","volume":"106","author":"Delgado-Escueta","year":"2001","journal-title":"Am J Med Genet"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0035","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":"10.1016\/j.clinbiochem.2013.08.016_bb0040","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 U S A"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0045","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":"10.1016\/j.clinbiochem.2013.08.016_bb0050","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":"10.1016\/j.clinbiochem.2013.08.016_bb0055","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 U S A"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0060","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":"10.1016\/j.clinbiochem.2013.08.016_bb0065","doi-asserted-by":"crossref","first-page":"2377","DOI":"10.1074\/jbc.C100686200","article-title":"A unique carbohydrate binding domain targets the Lafora disease phosphatase to glycogen","volume":"277","author":"Wang","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0070","series-title":"Encyclopedia of signaling molecules","first-page":"1003","article-title":"Laforin: function and action of a glucan phosphatase","author":"Sherwood","year":"2012"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0075","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1111\/j.1742-4658.2012.08549.x","article-title":"Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii","volume":"280","author":"Gentry","year":"2013","journal-title":"FEBS J"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0080","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1186\/1471-2148-9-138","article-title":"Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glycogen metabolism of the organism","volume":"9","author":"Gentry","year":"2009","journal-title":"BMC Evol Biol"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0085","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1002\/humu.20954","article-title":"Lafora progressive myoclonus epilepsy: a meta-analysis of reported mutations in the first decade following the discovery of the EPM2A and NHLRC1 genes","volume":"30","author":"Singh","year":"2009","journal-title":"Hum Mutat"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0090","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1093\/hmg\/11.11.1251","article-title":"Targeted disruption of the EPM2A gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice","volume":"11","author":"Ganesh","year":"2002","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0095","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.cmet.2011.01.017","article-title":"Phosphate incorporation during glycogen synthesis and Lafora disease","volume":"13","author":"Tagliabracci","year":"2011","journal-title":"Cell Metab"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0100","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.cmet.2013.04.006","article-title":"Hyperphosphorylation of glucosyl c6 carbons and altered structure of glycogen in the neurodegenerative epilepsy Lafora disease","volume":"17","author":"Nitschke","year":"2013","journal-title":"Cell Metab"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0105","doi-asserted-by":"crossref","first-page":"549","DOI":"10.2165\/11319250-000000000-00000","article-title":"Lafora disease: epidemiology, pathophysiology and management","volume":"24","author":"Monaghan","year":"2010","journal-title":"CNS Drugs"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0110","doi-asserted-by":"crossref","first-page":"7567","DOI":"10.1073\/pnas.130187497","article-title":"Noninvasive gene targeting to the brain","volume":"97","author":"Shi","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0115","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/j.tig.2008.08.010","article-title":"Introducing sense into nonsense in treatments of human genetic diseases","volume":"24","author":"Linde","year":"2008","journal-title":"Trends Genet"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0120","doi-asserted-by":"crossref","first-page":"e1002037","DOI":"10.1371\/journal.pgen.1002037","article-title":"PTG depletion removes Lafora bodies and rescues the fatal epilepsy of Lafora disease","volume":"7","author":"Turnbull","year":"2011","journal-title":"PLoS Genet"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0125","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1002\/emmm.201100174","article-title":"Neurodegeneration and functional impairments associated with glycogen synthase accumulation in a mouse model of Lafora disease","volume":"3","author":"Valles-Ortega","year":"2011","journal-title":"EMBO Mol Med"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0130","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1097\/00004691-199107010-00003","article-title":"Progressive myoclonus epilepsies: clinical and neurophysiological diagnosis","volume":"8","author":"Berkovic","year":"1991","journal-title":"J Clin Neurophysiol"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0135","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.ab.2012.10.044","article-title":"A malachite green-based assay to assess glucan phosphatase activity","volume":"435","author":"Sherwood","year":"2013","journal-title":"Anal Biochem"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0140","doi-asserted-by":"crossref","first-page":"15379","DOI":"10.1073\/pnas.1009386107","article-title":"Structural basis for the glucan phosphatase activity of starch excess4","volume":"107","author":"Vander Kooi","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.clinbiochem.2013.08.016_bb0145","doi-asserted-by":"crossref","first-page":"3796","DOI":"10.1074\/jbc.270.8.3796","article-title":"The purification and characterization of a human dual-specific protein tyrosine phosphatase","volume":"270","author":"Denu","year":"1995","journal-title":"J Biol Chem"}],"container-title":["Clinical Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009912013003950?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009912013003950?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T20:33:11Z","timestamp":1777408391000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009912013003950"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,12]]},"references-count":29,"journal-issue":{"issue":"18","published-print":{"date-parts":[[2013,12]]}},"alternative-id":["S0009912013003950"],"URL":"https:\/\/doi.org\/10.1016\/j.clinbiochem.2013.08.016","relation":{},"ISSN":["0009-9120"],"issn-type":[{"value":"0009-9120","type":"print"}],"subject":[],"published":{"date-parts":[[2013,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A bioassay for Lafora disease and laforin glucan phosphatase activity","name":"articletitle","label":"Article Title"},{"value":"Clinical Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.clinbiochem.2013.08.016","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2013 The Canadian Society of Clinical Chemists. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}