{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T12:56:22Z","timestamp":1789908982339,"version":"4.0.1"},"reference-count":88,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,18]],"date-time":"2020-09-18T00:00:00Z","timestamp":1600387200000},"content-version":"vor","delay-in-days":2087,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["U01 HL099773"],"award-info":[{"award-number":["U01 HL099773"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["P41GM10349010"],"award-info":[{"award-number":["P41GM10349010"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2015,1]]},"DOI":"10.1074\/jbc.m114.628628","type":"journal-article","created":{"date-parts":[[2014,12,9]],"date-time":"2014-12-09T05:06:56Z","timestamp":1418101616000},"page":"3121-3136","source":"Crossref","is-referenced-by-count":84,"title":["Pompe Disease Results in a Golgi-based Glycosylation Deficit in Human Induced Pluripotent Stem Cell-derived Cardiomyocytes"],"prefix":"10.1016","volume":"290","author":[{"given":"Kunil K.","family":"Raval","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ran","family":"Tao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brent E.","family":"White","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Willem J.","family":"De Lange","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chad H.","family":"Koonce","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junying","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Priya S.","family":"Kishnani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James A.","family":"Thomson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deane F.","family":"Mosher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John C.","family":"Ralphe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timothy J.","family":"Kamp","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M114.628628_bib1","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1016\/S0140-6736(08)61555-X","article-title":"Pompe's disease","volume":"372","author":"van der Ploeg","year":"2008","journal-title":"Lancet"},{"key":"10.1074\/jbc.M114.628628_bib2","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":"Kishnani","year":"2006","journal-title":"J. Pediatr"},{"key":"10.1074\/jbc.M114.628628_bib3","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ymgme.2009.08.003","article-title":"Cross-reactive immunologic material status affects treatment outcomes in Pompe disease infants","volume":"99","author":"Kishnani","year":"2010","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.M114.628628_bib4","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":"10.1074\/jbc.M114.628628_bib5","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.jpeds.2009.03.015","article-title":"Reversal of cardiac dysfunction after enzyme replacement in patients with infantile-onset Pompe disease","volume":"155","author":"Chen","year":"2009","journal-title":"J. Pediatr"},{"key":"10.1074\/jbc.M114.628628_bib6","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1097\/GIM.0b013e318183722f","article-title":"Arrhythmias in patients receiving enzyme replacement therapy for infantile Pompe disease","volume":"10","author":"McDowell","year":"2008","journal-title":"Genet. Med"},{"key":"10.1074\/jbc.M114.628628_bib7","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":"Thurberg","year":"2006","journal-title":"Lab. Invest"},{"key":"10.1074\/jbc.M114.628628_bib8","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1152\/japplphysiol.01253.2009","article-title":"Impaired organization and function of myofilaments in single muscle fibers from a mouse model of Pompe disease","volume":"108","author":"Xu","year":"2010","journal-title":"J. Appl. Physiol"},{"key":"10.1074\/jbc.M114.628628_bib9","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.1038\/cdd.2012.52","article-title":"The role of autophagy in the pathogenesis of glycogen storage disease type II (GSDII)","volume":"19","author":"Nascimbeni","year":"2012","journal-title":"Cell Death Differ"},{"key":"10.1074\/jbc.M114.628628_bib10","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.ymgme.2010.08.001","article-title":"Differences in the predominance of lysosomal and autophagic pathologies between infants and adults with Pompe disease: implications for therapy","volume":"101","author":"Raben","year":"2010","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.M114.628628_bib11","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":"Raben","year":"2008","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.628628_bib12","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.ymgme.2008.12.012","article-title":"Murine muscle cell models for Pompe disease and their use in studying therapeutic approaches","volume":"96","author":"Takikita","year":"2009","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.M114.628628_bib13","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1002\/ajmg.c.31317","article-title":"Autophagy and mitochondria in Pompe disease: nothing is so new as what has long been forgotten","volume":"160","author":"Raben","year":"2012","journal-title":"Am. J. Med. Genet. C Semin. Med. Genet"},{"key":"10.1074\/jbc.M114.628628_bib14","doi-asserted-by":"crossref","first-page":"719","DOI":"10.4161\/auto.19469","article-title":"Autophagy in lysosomal storage disorders","volume":"8","author":"Lieberman","year":"2012","journal-title":"Autophagy"},{"key":"10.1074\/jbc.M114.628628_bib15","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1161\/CIRCRESAHA.110.223842","article-title":"Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motor","volume":"111","author":"Moore","year":"2012","journal-title":"Circ. Res"},{"key":"10.1074\/jbc.M114.628628_bib16","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1085\/jgp.201311018","article-title":"E258K HCM-causing mutation in cardiac MyBP-C reduces contractile force and accelerates twitch kinetics by disrupting the cMyBP-C and myosin S2 interaction","volume":"142","author":"De Lange","year":"2013","journal-title":"J. Gen. Physiol"},{"key":"10.1074\/jbc.M114.628628_bib17","doi-asserted-by":"crossref","first-page":"S313","DOI":"10.1007\/s10545-009-1262-1","article-title":"Cardiomyopathy in the congenital disorders of glycosylation (CDG): a case of late presentation and literature review","volume":"32","author":"Footitt","year":"2009","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.M114.628628_bib18","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1001\/jama.2009.371","article-title":"Clinical outcome and phenotypic expression in LAMP2 cardiomyopathy","volume":"301","author":"Maron","year":"2009","journal-title":"JAMA"},{"key":"10.1074\/jbc.M114.628628_bib19","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1126\/science.1172482","article-title":"Human induced pluripotent stem cells free of vector and transgene sequences","volume":"324","author":"Yu","year":"2009","journal-title":"Science"},{"key":"10.1074\/jbc.M114.628628_bib20","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nbt1177","article-title":"Derivation of human embryonic stem cells in defined conditions","volume":"24","author":"Ludwig","year":"2006","journal-title":"Nat. Biotechnol"},{"key":"10.1074\/jbc.M114.628628_bib21","first-page":"132","article-title":"Biochemical, immunological, and cell genetic studies in glycogenosis type II","volume":"30","author":"Reuser","year":"1978","journal-title":"Am. J. Hum. Genet"},{"key":"10.1074\/jbc.M114.628628_bib22","doi-asserted-by":"crossref","first-page":"E1848","DOI":"10.1073\/pnas.1200250109","article-title":"Robust cardiomyocyte differentiation from human pluripotent stem cells via temporal modulation of canonical Wnt signaling","volume":"109","author":"Lian","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.628628_bib23","doi-asserted-by":"crossref","first-page":"e26397","DOI":"10.1371\/journal.pone.0026397","article-title":"Human engineered heart tissue as a versatile tool in basic research and preclinical toxicology","volume":"6","author":"Schaaf","year":"2011","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M114.628628_bib24","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1161\/CIRCRESAHA.109.211458","article-title":"Development of a drug screening platform based on engineered heart tissue","volume":"107","author":"Hansen","year":"2010","journal-title":"Circ. Res"},{"key":"10.1074\/jbc.M114.628628_bib25","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1161\/CIRCRESAHA.111.242354","article-title":"Neonatal mouse-derived engineered cardiac tissue: a novel model system for studying genetic heart disease","volume":"109","author":"de Lange","year":"2011","journal-title":"Circ. Res"},{"key":"10.1074\/jbc.M114.628628_bib26","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0003-2697(84)90782-6","article-title":"A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids","volume":"138","author":"Wessel","year":"1984","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M114.628628_bib27","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/nature00837","article-title":"Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies","volume":"418","author":"Michele","year":"2002","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.628628_bib28","doi-asserted-by":"crossref","first-page":"4007","DOI":"10.1016\/S0021-9258(19)41496-8","article-title":"High resolution two-dimensional electrophoresis of proteins","volume":"250","author":"O'Farrell","year":"1975","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.628628_bib29","doi-asserted-by":"crossref","first-page":"2297","DOI":"10.1093\/clinchem\/35.12.2297","article-title":"Computerized quantitative analysis of Coomassie-blue-stained serum proteins separated by two-dimensional electrophoresis","volume":"35","author":"Burgess-Cassler","year":"1989","journal-title":"Clin. Chem"},{"key":"10.1074\/jbc.M114.628628_bib30","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/0003-2697(92)90048-C","article-title":"A comprehensive procedure for preparation of partially methylated alditol acetates from glycoprotein carbohydrates","volume":"203","author":"Anumula","year":"1992","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M114.628628_bib31","doi-asserted-by":"crossref","first-page":"1917","DOI":"10.1126\/science.1151526","article-title":"Induced pluripotent stem cell lines derived from human somatic cells","volume":"318","author":"Yu","year":"2007","journal-title":"Science"},{"key":"10.1074\/jbc.M114.628628_bib32","doi-asserted-by":"crossref","first-page":"6780","DOI":"10.1074\/jbc.M404008200","article-title":"Lysosomal acid \u03b1-glucosidase consists of four different peptides processed from a single chain precursor","volume":"280","author":"Moreland","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.628628_bib33","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1111\/j.1399-0004.1996.tb03801.x","article-title":"Homozygous deletion of exon 18 leads to degradation of the lysosomal \u03b1-glucosidase precursor and to the infantile form of glycogen storage disease type II","volume":"49","author":"Ausems","year":"1996","journal-title":"Clin. Genet"},{"key":"10.1074\/jbc.M114.628628_bib34","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1177\/002215540505300108","article-title":"High-resolution light microscopy (HRLM) and digital analysis of Pompe disease pathology","volume":"53","author":"Lynch","year":"2005","journal-title":"J. Histochem. Cytochem"},{"key":"10.1074\/jbc.M114.628628_bib35","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1002\/(SICI)1097-0185(199706)248:2<233::AID-AR10>3.0.CO;2-Q","article-title":"Ultrastructural changes of the myocardium in the embryonic rat heart","volume":"248","author":"Knaapen","year":"1997","journal-title":"Anat. Rec"},{"key":"10.1074\/jbc.M114.628628_bib36","doi-asserted-by":"crossref","first-page":"445","DOI":"10.4161\/auto.19496","article-title":"Guidelines for the use and interpretation of assays for monitoring autophagy","volume":"8","author":"Klionsky","year":"2012","journal-title":"Autophagy"},{"key":"10.1074\/jbc.M114.628628_bib37","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1093\/clinchem\/43.8.1325","article-title":"Diagnosis of lysosomal storage disorders: evaluation of lysosome-associated membrane protein LAMP-1 as a diagnostic marker","volume":"43","author":"Meikle","year":"1997","journal-title":"Clin. Chem"},{"key":"10.1074\/jbc.M114.628628_bib38","doi-asserted-by":"crossref","first-page":"18911","DOI":"10.1016\/S0021-9258(18)37369-1","article-title":"Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2: major sialoglycoproteins carrying polylactosaminoglycan","volume":"263","author":"Carlsson","year":"1988","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.628628_bib39","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1006\/abbi.1993.1322","article-title":"Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2","volume":"304","author":"Carlsson","year":"1993","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M114.628628_bib40","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1093\/glycob\/8.9.947","article-title":"The extent of polylactosamine glycosylation of MDCK LAMP-2 is determined by its Golgi residence time","volume":"8","author":"Nabi","year":"1998","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.M114.628628_bib41","doi-asserted-by":"crossref","first-page":"20488","DOI":"10.1016\/S0021-9258(17)30530-6","article-title":"The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2: localization on the peptide backbones","volume":"265","author":"Carlsson","year":"1990","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.628628_bib42","doi-asserted-by":"crossref","first-page":"18545","DOI":"10.1016\/S0021-9258(19)81393-5","article-title":"Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum","volume":"263","author":"Fujiwara","year":"1988","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.628628_bib43","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1006\/excr.1999.4755","article-title":"Regulation of the lysosome-associated membrane protein in a sucrose model of lysosomal storage","volume":"254","author":"Isaac","year":"2000","journal-title":"Exp. Cell Res"},{"key":"10.1074\/jbc.M114.628628_bib44","series-title":"Molecular Biology of the Cell","article-title":"Transport from the ER through the Golgi apparatus","author":"Alberts","year":"2002"},{"key":"10.1074\/jbc.M114.628628_bib45","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1016\/0003-9861(85)90727-1","article-title":"Lysosome-associated membrane proteins: characterization of LAMP-1 of macrophage P388 and mouse embryo 3T3 cultured cells","volume":"239","author":"Chen","year":"1985","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M114.628628_bib46","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0092-8674(00)80322-0","article-title":"\u03b1-Mannosidase-II deficiency results in dyserythropoiesis and unveils an alternate pathway in oligosaccharide biosynthesis","volume":"90","author":"Chui","year":"1997","journal-title":"Cell"},{"key":"10.1074\/jbc.M114.628628_bib47","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1093\/hmg\/ddi062","article-title":"Localization and functional analysis of the LARGE family of glycosyltransferases: significance for muscular dystrophy","volume":"14","author":"Brockington","year":"2005","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.628628_bib48","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1126\/science.1214115","article-title":"Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE","volume":"335","author":"Inamori","year":"2012","journal-title":"Science"},{"key":"10.1074\/jbc.M114.628628_bib49","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/j.cell.2004.06.003","article-title":"Molecular recognition by LARGE is essential for expression of functional dystroglycan","volume":"117","author":"Kanagawa","year":"2004","journal-title":"Cell"},{"key":"10.1074\/jbc.M114.628628_bib50","author":"Sparks","year":"1993"},{"key":"10.1074\/jbc.M114.628628_bib51","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1083\/jcb.122.4.809","article-title":"A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin","volume":"122","author":"Ervasti","year":"1993","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M114.628628_bib52","doi-asserted-by":"crossref","first-page":"15457","DOI":"10.1074\/jbc.R200031200","article-title":"Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function","volume":"278","author":"Michele","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.628628_bib53","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1083\/jcb.136.5.1047","article-title":"Laminin-induced clustering of dystroglycan on embryonic muscle cells: comparison with agrin-induced clustering","volume":"136","author":"Cohen","year":"1997","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M114.628628_bib54","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1083\/jcb.145.6.1325","article-title":"alpha-Dystroglycan is a laminin receptor involved in extracellular matrix assembly on myotubes and muscle cell viability","volume":"145","author":"Montanaro","year":"1999","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M114.628628_bib55","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1017\/S1047951103000702","article-title":"Cardiomyopathy in congenital disorders of glycosylation","volume":"13","author":"Gehrmann","year":"2003","journal-title":"Cardiol. Young"},{"key":"10.1074\/jbc.M114.628628_bib56","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1002\/ajmg.a.31791","article-title":"Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality","volume":"143A","author":"Kranz","year":"2007","journal-title":"Am. J. Med. Genet. A"},{"key":"10.1074\/jbc.M114.628628_bib57","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s10741-012-9302-6","article-title":"From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG)","volume":"18","author":"Kapusta","year":"2013","journal-title":"Heart Fail. Rev"},{"key":"10.1074\/jbc.M114.628628_bib58","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1016\/j.cardfail.2011.07.011","article-title":"Left ventricular geometry, global function, and dyssynchrony in infants and children with Pompe cardiomyopathy undergoing enzyme replacement therapy","volume":"17","author":"Chen","year":"2011","journal-title":"J. Card. Fail"},{"key":"10.1074\/jbc.M114.628628_bib59","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.ymgme.2003.08.022","article-title":"Enzyme replacement therapy in the mouse model of Pompe disease","volume":"80","author":"Raben","year":"2003","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.M114.628628_bib60","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.ymthe.2004.09.017","article-title":"Replacing acid \u03b1-glucosidase in Pompe disease: recombinant and transgenic enzymes are equipotent, but neither completely clears glycogen from type II muscle fibers","volume":"11","author":"Raben","year":"2005","journal-title":"Mol. Ther"},{"key":"10.1074\/jbc.M114.628628_bib61","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1093\/hmg\/ddt630","article-title":"Cohen syndrome is associated with major glycosylation defects","volume":"23","author":"Duplomb","year":"2014","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.628628_bib62","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1111\/j.1600-0854.2005.00376.x","article-title":"COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation","volume":"7","author":"Shestakova","year":"2006","journal-title":"Traffic"},{"key":"10.1074\/jbc.M114.628628_bib63","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.ajhg.2012.05.002","article-title":"TMEM165 deficiency causes a congenital disorder of glycosylation","volume":"91","author":"Foulquier","year":"2012","journal-title":"Am. J. Hum. Genet"},{"key":"10.1074\/jbc.M114.628628_bib64","author":"Sparks","year":"2005"},{"key":"10.1074\/jbc.M114.628628_bib65","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1373\/clinchem.2003.022541","article-title":"Apolipoprotein C-III isofocusing in the diagnosis of genetic defects in O-glycan biosynthesis","volume":"49","author":"Wopereis","year":"2003","journal-title":"Clin. Chem"},{"key":"10.1074\/jbc.M114.628628_bib66","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1373\/clinchem.2003.021568","article-title":"Diagnosis of congenital disorders of glycosylation by capillary zone electrophoresis of serum transferrin","volume":"50","author":"Carchon","year":"2004","journal-title":"Clin. Chem"},{"key":"10.1074\/jbc.M114.628628_bib67","series-title":"Essentials of Glycobiology","article-title":"Genetic disorders of glycosylation","author":"Freeze","year":"2009"},{"key":"10.1074\/jbc.M114.628628_bib68","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1016\/j.sbi.2005.08.010","article-title":"Altered glycan structures: the molecular basis of congenital disorders of glycosylation","volume":"15","author":"Freeze","year":"2005","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.M114.628628_bib69","doi-asserted-by":"crossref","first-page":"e56181","DOI":"10.1371\/journal.pone.0056181","article-title":"Dysregulation of multiple facets of glycogen metabolism in a murine model of Pompe disease","volume":"8","author":"Taylor","year":"2013","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M114.628628_bib70","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1111\/j.1432-1033.1994.tb18590.x","article-title":"Differential secretion of \u03b11-acid glycoprotein occurs in the Golgi complex of isolated rat hepatocytes: evidence of partial retention in the Golgi","volume":"219","author":"Po\u00fcs","year":"1994","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.M114.628628_bib71","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1093\/glycob\/cwr023","article-title":"G6PC3 mutations are associated with a major defect of glycosylation: a novel mechanism for neutrophil dysfunction","volume":"21","author":"Hayee","year":"2011","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.M114.628628_bib72","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.ajhg.2013.10.024","article-title":"Solving glycosylation disorders: fundamental approaches reveal complicated pathways","volume":"94","author":"Freeze","year":"2014","journal-title":"Am. J. Hum. Genet"},{"key":"10.1074\/jbc.M114.628628_bib73","doi-asserted-by":"crossref","first-page":"5498","DOI":"10.1021\/bi00391a043","article-title":"Purification and properties of the glycoprotein processing N-acetylglucosaminyltransferase II from plants","volume":"26","author":"Szumilo","year":"1987","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M114.628628_bib74","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1093\/oxfordjournals.jbchem.a022793","article-title":"Kinetic basis for the donor nucleotide-sugar specificity of \u03b21,4-N-acetylglucosaminyltransferase III","volume":"128","author":"Ikeda","year":"2000","journal-title":"J. Biochem"},{"key":"10.1074\/jbc.M114.628628_bib75","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1093\/glycob\/12.2.119","article-title":"UDP-GlcNAc concentration is an important factor in the biosynthesis of \u03b21,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V","volume":"12","author":"Sasai","year":"2002","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.M114.628628_bib76","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0008-6215(90)80050-D","article-title":"Initiation of poly-N-acetyllactosamine chain biosynthesis occurs preferentially on complex multiantennary asparagine-linked oligosaccharides","volume":"203","author":"Elices","year":"1990","journal-title":"Carbohydr. Res"},{"key":"10.1074\/jbc.M114.628628_bib77","doi-asserted-by":"crossref","first-page":"8983","DOI":"10.1073\/pnas.0603248103","article-title":"Essential and mutually compensatory roles of \u03b1-mannosidase II and \u03b1-mannosidase IIx in N-glycan processing in vivo in mice","volume":"103","author":"Akama","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.628628_bib78","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1021\/pr401043r","article-title":"Filter-aided N-glycan separation (FANGS): a convenient sample preparation method for mass spectrometric N-glycan profiling","volume":"13","author":"Abdul Rahman","year":"2014","journal-title":"J. Proteome Res"},{"key":"10.1074\/jbc.M114.628628_bib79","doi-asserted-by":"crossref","first-page":"6930","DOI":"10.1074\/jbc.R112.438978","article-title":"The O-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy","volume":"288","author":"Wells","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.628628_bib80","doi-asserted-by":"crossref","first-page":"3346","DOI":"10.1093\/hmg\/ddr240","article-title":"Sarcolemma instability during mechanical activity in Largemyd cardiac myocytes with loss of dystroglycan extracellular matrix receptor function","volume":"20","author":"Kabaeva","year":"2011","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.M114.628628_bib81","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1007\/s00431-002-1136-0","article-title":"Congenital disorders of glycosylation: review of their molecular bases, clinical presentations and specific therapies","volume":"162","author":"Marquardt","year":"2003","journal-title":"Eur. J. Pediatr"},{"key":"10.1074\/jbc.M114.628628_bib82","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1006\/jmcc.1997.0579","article-title":"Dependence of cardiac cell Ca2+ permeability on sialic acid-containing sarcolemmal gangliosides","volume":"30","author":"Marengo","year":"1998","journal-title":"J. Mol. Cell. Cardiol"},{"key":"10.1074\/jbc.M114.628628_bib83","first-page":"H147","article-title":"Removal of sarcolemmal sialic acid residues results in a loss of sarcolemmal functioning and integrity","volume":"263","author":"Post","year":"1992","journal-title":"Am. J. Physiol"},{"key":"10.1074\/jbc.M114.628628_bib84","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1016\/j.bbrc.2004.07.121","article-title":"Calcium-calcineurin signaling in the regulation of cardiac hypertrophy","volume":"322","author":"Wilkins","year":"2004","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M114.628628_bib85","doi-asserted-by":"crossref","first-page":"16517","DOI":"10.1073\/pnas.0905414106","article-title":"Regulated and aberrant glycosylation modulate cardiac electrical signaling","volume":"106","author":"Montpetit","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.628628_bib86","first-page":"H735","article-title":"Removal of sialic acid alters both T- and L-type calcium currents in cardiac myocytes","volume":"260","author":"Fermini","year":"1991","journal-title":"Am. J. Physiol"},{"key":"10.1074\/jbc.M114.628628_bib87","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1096\/fj.12-214387","article-title":"Channel sialic acids limit hERG channel activity during the ventricular action potential","volume":"27","author":"Norring","year":"2013","journal-title":"FASEB J"},{"key":"10.1074\/jbc.M114.628628_bib88","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.yjmcc.2013.02.013","article-title":"Expression of the sialyltransferase, ST3Gal4, impacts cardiac voltage-gated sodium channel activity, refractory period, and ventricular conduction","volume":"59","author":"Ednie","year":"2013","journal-title":"J. Mol. Cell Cardiol"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820492786?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820492786?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M114.628628","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T18:03:56Z","timestamp":1641319436000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820492786"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,1]]},"references-count":88,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2015,1]]}},"alternative-id":["S0021925820492786"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m114.628628","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2015,1]]}}}