{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T05:19:47Z","timestamp":1773292787740,"version":"3.50.1"},"reference-count":58,"publisher":"Public Library of Science (PLoS)","issue":"12","license":[{"start":{"date-parts":[[2010,12,13]],"date-time":"2010-12-13T00:00:00Z","timestamp":1292198400000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/publicdomain\/zero\/1.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0015239","type":"journal-article","created":{"date-parts":[[2010,12,14]],"date-time":"2010-12-14T14:31:45Z","timestamp":1292337105000},"page":"e15239","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":58,"title":["Fiber Type Conversion by PGC-1\u03b1 Activates Lysosomal and Autophagosomal Biogenesis in Both Unaffected and Pompe Skeletal Muscle"],"prefix":"10.1371","volume":"5","author":[{"given":"Shoichi","family":"Takikita","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cynthia","family":"Schreiner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rebecca","family":"Baum","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tao","family":"Xie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Evelyn","family":"Ralston","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul H.","family":"Plotz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nina","family":"Raben","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2010,12,13]]},"reference":[{"key":"ref1","first-page":"3389","article-title":"Glycogen Storage Disease Type II: Acid alpha-Glucosidase (Acid Maltase) Deficiency.","author":"R Hirschhorn","year":"2000"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/j.jpeds.2005.11.033","article-title":"A retrospective, multinational, multicenter study on the natural history of infantile-onset Pompe disease.","volume":"148","author":"PS Kishnani","year":"2006","journal-title":"J Pediatr"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1007\/s00415-005-0922-9","article-title":"The natural course of non-classic Pompe&apos;s disease; a review of 225 published cases.","volume":"252","author":"LP Winkel","year":"2005","journal-title":"J Neurol"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1542\/peds.112.2.332","article-title":"The natural course of infantile Pompe&apos;s disease: 20 original cases compared with 133 cases from the literature.","volume":"112","author":"HM Van den Hout","year":"2003","journal-title":"Pediatrics"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1212\/01.wnl.0000251268.41188.04","article-title":"Recombinant human acid [alpha]-glucosidase: major clinical benefits in infantile-onset Pompe disease.","volume":"68","author":"PS Kishnani","year":"2007","journal-title":"Neurology"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1097\/GIM.0b013e31819d0996","article-title":"Clinical outcomes after long-term treatment with alglucosidase alfa in infants and children with advanced Pompe disease.","volume":"11","author":"M Nicolino","year":"2009","journal-title":"Genet Med"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s00415-009-5275-3","article-title":"Enzyme replacement therapy with alglucosidase alfa in 44 patients with late-onset glycogen storage disease type 2: 12-month results of an observational clinical trial.","volume":"257","author":"S Strothotte","year":"2009","journal-title":"J Neurol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1056\/NEJMoa0909859","article-title":"A randomized study of alglucosidase alfa in late-onset Pompe&apos;s disease.","volume":"362","author":"AT Van der Ploeg","year":"2010","journal-title":"N Engl J Med"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1146\/annurev-genet-102808-114910","article-title":"Regulation Mechanisms and Signaling Pathways of Autophagy.","volume":"43","author":"C He","year":"2009","journal-title":"Annu Rev Genet"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1038\/nature06639","article-title":"Autophagy fights disease through cellular self-digestion.","volume":"451","author":"N Mizushima","year":"2008","journal-title":"Nature"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s11910-007-0024-4","article-title":"Acid Alpha-Glucosidase Deficiency (Pompe Disease).","volume":"7","author":"T Fukuda","year":"2007","journal-title":"Current Neurology and Neuroscience Reports"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"111","DOI":"10.4161\/auto.5.1.7293","article-title":"When more is less: excess and deficiency of autophagy coexist in skeletal muscle in Pompe disease.","volume":"5","author":"N Raben","year":"2009","journal-title":"Autophagy"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"546","DOI":"10.4161\/auto.4591","article-title":"Deconstructing Pompe disease by analyzing single muscle fibers.","volume":"3","author":"N Raben","year":"2007","journal-title":"Autophagy"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1038\/labinvest.3700484","article-title":"Characterization of pre- and post-treatment pathology after enzyme replacement therapy for pompe disease.","volume":"86","author":"BL Thurberg","year":"2006","journal-title":"Lab Invest"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1172\/JCI27794","article-title":"PGC-1 coactivators: inducible regulators of energy metabolism in health and disease.","volume":"116","author":"BN Finck","year":"2006","journal-title":"J Clin Invest"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1210\/er.2006-0037","article-title":"Peroxisome proliferator-activated receptor gamma coactivator 1 coactivators, energy homeostasis, and metabolism.","volume":"27","author":"C Handschin","year":"2006","journal-title":"Endocr Rev"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.gde.2008.07.018","article-title":"PGC-1 coactivators and skeletal muscle adaptations in health and disease.","volume":"18","author":"Z Arany","year":"2008","journal-title":"Curr Opin Genet Dev"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1038\/nature00904","article-title":"Transcriptional co-activator PGC-1 alpha drives the formation of slow-twitch muscle fibres.","volume":"418","author":"J Lin","year":"2002","journal-title":"Nature"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"19460","DOI":"10.1074\/jbc.M110.113092","article-title":"PGC-1{alpha} or PGC-1{beta} (peroxisome proliferator-activated receptor {gamma} coactivator 1{alpha} or 1{beta}) overexpression inhibits muscle protein degradation, induction of ubiquitin ligases, and disuse atrophy.","volume":"285","author":"JJ Brault","year":"2010","journal-title":"J Biol Chem"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"20405","DOI":"10.1073\/pnas.0911570106","article-title":"Increased muscle PGC-1alpha expression protects from sarcopenia and metabolic disease during aging.","volume":"106","author":"T Wenz","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"16260","DOI":"10.1073\/pnas.0607795103","article-title":"PGC-1alpha protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription.","volume":"103","author":"M Sandri","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"3897","DOI":"10.1093\/hmg\/ddn292","article-title":"Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease.","volume":"17","author":"N Raben","year":"2008","journal-title":"Hum Mol Genet"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"30014","DOI":"10.1074\/jbc.M704817200","article-title":"Skeletal muscle fiber-type switching, exercise intolerance, and myopathy in PGC-1alpha muscle-specific knock-out animals.","volume":"282","author":"C Handschin","year":"2007","journal-title":"J Biol Chem"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1093\/hmg\/ddm294","article-title":"A rational mechanism for combination treatment of Huntington&apos;s disease using lithium and rapamycin.","volume":"17","author":"S Sarkar","year":"2008","journal-title":"Hum Mol Genet"},{"key":"ref25","doi-asserted-by":"crossref","DOI":"10.4161\/auto.6.8.13378","article-title":"Suppression of autophagy permits successful enzyme replacement therapy in a lysosomal storage disorder-murine Pompe disease.","volume":"6","author":"N Raben","year":"2010","journal-title":"Autophagy"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.ymthe.2004.09.017","article-title":"Replacing acid alpha-glucosidase in Pompe disease: recombinant and transgenic enzymes are equipotent, but neither completely clears glycogen from type II muscle fibers.","volume":"11","author":"N Raben","year":"2005","journal-title":"Mol Ther"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/j.ymthe.2006.08.009","article-title":"Autophagy and mistargeting of therapeutic enzyme in skeletal muscle in Pompe disease.","volume":"14","author":"T Fukuda","year":"2006","journal-title":"Mol Ther"},{"key":"ref28","article-title":"Differences in the predominance of lysosomal and autophagic pathologies between infants and adults with Pompe disease: implications for therapy.","volume":"6","author":"N Raben","year":"2010","journal-title":"Mol Genet Metab"},{"key":"ref29","first-page":"425","article-title":"Mitochondrial dysfunction and oxidative stress mediate the physiological impairment induced by the disruption of autophagy.","volume":"1","author":"JJ Wu","year":"2009","journal-title":"Aging (Albany NY)"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.cmet.2009.10.008","article-title":"Autophagy is required to maintain muscle mass.","volume":"10","author":"E Masiero","year":"2009","journal-title":"Cell Metab"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"307","DOI":"10.4161\/auto.6.2.11137","article-title":"Autophagy inhibition induces atrophy and myopathy in adult skeletal muscles.","volume":"6","author":"E Masiero","year":"2010","journal-title":"Autophagy"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1152\/physiol.00009.2007","article-title":"Activity-dependent signaling pathways controlling muscle diversity and plasticity.","volume":"22","author":"S Schiaffino","year":"2007","journal-title":"Physiology (Bethesda)"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.2353\/ajpath.2006.060034","article-title":"Overexpression of peroxisome proliferator-activated receptor gamma co-activator-1alpha leads to muscle atrophy with depletion of ATP.","volume":"169","author":"S Miura","year":"2006","journal-title":"Am J Pathol"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"31385","DOI":"10.1074\/jbc.M304312200","article-title":"Overexpression of peroxisome proliferator-activated receptor gamma coactivator-1alpha down-regulates GLUT4 mRNA in skeletal muscles.","volume":"278","author":"S Miura","year":"2003","journal-title":"J Biol Chem"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"19926","DOI":"10.1073\/pnas.0810339105","article-title":"Paradoxical effects of increased expression of PGC-1alpha on muscle mitochondrial function and insulin-stimulated muscle glucose metabolism.","volume":"105","author":"CS Choi","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"3820","DOI":"10.1073\/pnas.061035098","article-title":"Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1.","volume":"98","author":"LF Michael","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"36642","DOI":"10.1074\/jbc.M707006200","article-title":"A role for the transcriptional coactivator PGC-1alpha in muscle refueling.","volume":"282","author":"AR Wende","year":"2007","journal-title":"J Biol Chem"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/j.ymgme.2007.04.018","article-title":"Differential muscular glycogen clearance after enzyme replacement therapy in a mouse model of Pompe disease.","volume":"91","author":"ML Hawes","year":"2007","journal-title":"Mol Genet Metab"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1002\/jemt.20046","article-title":"Glycogen autophagy.","volume":"64","author":"OB Kotoulas","year":"2004","journal-title":"Microsc Res Tech"},{"key":"ref40","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":"DJ Kondomerkos","year":"2005","journal-title":"Histol Histopathol"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1083\/jcb.52.1.41","article-title":"Autophagic degradation of glycogen in skeletal muscles of the newborn rat.","volume":"52","author":"S Schiaffino","year":"1972","journal-title":"J Cell Biol"},{"key":"ref42","doi-asserted-by":"crossref","DOI":"10.4161\/auto.6143","article-title":"The role of autophagy in neonatal tissues: just a response to amino acid starvation?","volume":"4","author":"S Schiaffino","year":"2008","journal-title":"Autophagy"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.yjmcc.2007.10.013","article-title":"Stimulation of mitochondrial biogenesis and autophagy by lipopolysaccharide in the neonatal rat cardiomyocyte protects against programmed cell death.","volume":"44","author":"DL Hickson-Bick","year":"2008","journal-title":"J Mol Cell Cardiol"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.1016\/j.biocel.2009.06.007","article-title":"PPARgamma activation induces autophagy in breast cancer cells.","volume":"41","author":"J Zhou","year":"2009","journal-title":"Int J Biochem Cell Biol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"2635","DOI":"10.1016\/j.febslet.2010.04.041","article-title":"Fighting disease by selective autophagy of aggregate-prone proteins.","volume":"584","author":"H Knaevelsrud","year":"2010","journal-title":"FEBS Lett"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"4228","DOI":"10.1074\/jbc.M704332200","article-title":"Modest PGC-1alpha overexpression in muscle in vivo is sufficient to increase insulin sensitivity and palmitate oxidation in subsarcolemmal, not intermyofibrillar, mitochondria.","volume":"283","author":"CR Benton","year":"2008","journal-title":"J Biol Chem"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"E960","DOI":"10.1152\/ajpendo.00237.2005","article-title":"Endurance training increases skeletal muscle LKB1 and PGC-1alpha protein abundance: effects of time and intensity.","volume":"289","author":"EB Taylor","year":"2005","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1016\/j.devcel.2009.10.013","article-title":"A family of microRNAs encoded by myosin genes governs myosin expression and muscle performance.","volume":"17","author":"E Van Rooij","year":"2009","journal-title":"Dev Cell"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"19086","DOI":"10.1074\/jbc.273.30.19086","article-title":"Targeted disruption of the acid alpha-glucosidase gene in mice causes an illness with critical features of both infantile and adult human glycogen storage disease type II.","volume":"273","author":"N Raben","year":"1998","journal-title":"J Biol Chem"},{"key":"ref50","article-title":"Carbohydrate-remodeled acid alpha-glucosidase with higher affinity for the cation-independent mannose 6-phosphate receptor demonstrates improved delivery to muscles of Pompe mice.","author":"Y Zhu","year":"2005"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S0076-6879(08)04021-4","article-title":"Monitoring autophagy in lysosomal storage disorders.","volume":"453","author":"N Raben","year":"2009","journal-title":"Methods Enzymol"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1177\/42.9.8064136","article-title":"Improved method for post-embedding cytochemistry using reduced osmium and LR white resin.","volume":"42","author":"H Tamaki","year":"1994","journal-title":"J Histochem Cytochem"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"3876","DOI":"10.1093\/hmg\/ddn290","article-title":"Modulation of glycogen synthesis by RNA interference: towards a new therapeutic approach for glycogenosis type II.","volume":"17","author":"G Douillard-Guilloux","year":"2008","journal-title":"Hum Mol Genet"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1002\/mus.21211","article-title":"Preclinical drug trials in the mdx mouse: assessment of reliable and sensitive outcome measures.","volume":"39","author":"CF Spurney","year":"2009","journal-title":"Muscle Nerve"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"2805","DOI":"10.1242\/jcs.01131","article-title":"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation.","volume":"117","author":"Y Kabeya","year":"2004","journal-title":"J Cell Sci"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1093\/embo-reports\/kve061","article-title":"Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network.","volume":"2","author":"A Kihara","year":"2001","journal-title":"EMBO Rep"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"S114","DOI":"10.1038\/onc.2009.49","article-title":"BNIP3 subfamily BH3-only proteins: mitochondrial stress sensors in normal and pathological functions.","volume":"27","author":"G Chinnadurai","year":"2008","journal-title":"Oncogene"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1523\/JNEUROSCI.21-03-00875.2001","article-title":"Golgi complex, endoplasmic reticulum exit sites, and microtubules in skeletal muscle fibers are organized by patterned activity.","volume":"21","author":"E Ralston","year":"2001","journal-title":"J Neurosci"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0015239","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,5,8]],"date-time":"2020-05-08T20:32:22Z","timestamp":1588969942000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0015239"}},"subtitle":[],"editor":[{"given":"Patricia T.","family":"Bozza","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2010,12,13]]},"references-count":58,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2010,12,13]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0015239","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,12,13]]}}}