{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T03:42:27Z","timestamp":1781926947793,"version":"3.54.5"},"reference-count":45,"publisher":"Elsevier BV","issue":"37","license":[{"start":{"date-parts":[[2018,9,1]],"date-time":"2018-09-01T00:00:00Z","timestamp":1535760000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,20]],"date-time":"2020-08-20T00:00:00Z","timestamp":1597881600000},"content-version":"vor","delay-in-days":719,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health (NIH)","doi-asserted-by":"publisher","award":["P01GM107012"],"award-info":[{"award-number":["P01GM107012"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health (NIH)","doi-asserted-by":"publisher","award":["R01GM111939"],"award-info":[{"award-number":["R01GM111939"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2018,9]]},"DOI":"10.1074\/jbc.ra118.003014","type":"journal-article","created":{"date-parts":[[2018,7,26]],"date-time":"2018-07-26T18:40:54Z","timestamp":1532630454000},"page":"14534-14544","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"title":["Defective mucin-type glycosylation on \u03b1-dystroglycan in COG-deficient cells increases its susceptibility to bacterial proteases"],"prefix":"10.1016","volume":"293","author":[{"given":"Seok-Ho","family":"Yu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peng","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pradeep K.","family":"Prabhakar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tiantian","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron","family":"Beedle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geert-Jan","family":"Boons","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelley W.","family":"Moremen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lance","family":"Wells","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"Steet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA118.003014_bib1","doi-asserted-by":"crossref","first-page":"389","DOI":"10.2174\/156652407780831548","article-title":"Congenital disorders of glycosylation: CDG-I, CDG-II, and beyond","volume":"7","author":"Freeze","year":"2007","journal-title":"Curr. Mol. Med"},{"key":"10.1074\/jbc.RA118.003014_bib2","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1111\/j.1749-6632.2010.05840.x","article-title":"Congenital disorders of glycosylation","volume":"1214","author":"Jaeken","year":"2010","journal-title":"Ann. N.Y. Acad. Sci"},{"key":"10.1074\/jbc.RA118.003014_bib3","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev.genom.8.080706.092327","article-title":"Congenital disorders of glycosylation: a rapidly expanding disease family","volume":"8","author":"Jaeken","year":"2007","journal-title":"Annu. Rev. Genomics Hum. Genet"},{"key":"10.1074\/jbc.RA118.003014_bib4","doi-asserted-by":"crossref","first-page":"1628","DOI":"10.1002\/humu.21126","article-title":"Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides","volume":"30","author":"Haeuptle","year":"2009","journal-title":"Hum. Mutat"},{"key":"10.1074\/jbc.RA118.003014_bib5","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/s10038-017-0386-7","article-title":"Characteristic dysmorphic features in congenital disorders of glycosylation type IIb","volume":"63","author":"Kim","year":"2018","journal-title":"J. Hum. Genet"},{"key":"10.1074\/jbc.RA118.003014_bib6","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1002\/ajmg.c.30143","article-title":"Clinical features in adults with congenital disorders of glycosylation type Ia (CDG-Ia)","volume":"145C","author":"Krasnewich","year":"2007","journal-title":"Am. J. Med. Genet. C Semin. Med. Genet"},{"key":"10.1074\/jbc.RA118.003014_bib7","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/s10545-016-0012-4","article-title":"Liver involvement in congenital disorders of glycosylation (CDG): a systematic review of the literature","volume":"40","author":"Marques-da-Silva","year":"2017","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.RA118.003014_bib8","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1007\/s10545-017-0066-y","article-title":"Cardiac complications of congenital disorders of glycosylation (CDG): a systematic review of the literature","volume":"40","author":"Marques-da-Silva","year":"2017","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.RA118.003014_bib9","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1055\/s-0034-1387197","article-title":"Congenital disorders of glycosylation with emphasis on cerebellar involvement","volume":"34","author":"Barone","year":"2014","journal-title":"Semin. Neurol"},{"key":"10.1074\/jbc.RA118.003014_bib10","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1016\/j.bbagen.2012.02.001","article-title":"Diseases of glycosylation beyond classical congenital disorders of glycosylation","volume":"1820","author":"Hennet","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA118.003014_bib11","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1038\/nm1041","article-title":"Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder","volume":"10","author":"Wu","year":"2004","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.RA118.003014_bib12","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1083\/jcb.200202016","article-title":"Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function","volume":"157","author":"Ungar","year":"2002","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA118.003014_bib13","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1083\/jcb.200412003","article-title":"Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells","volume":"168","author":"Zolov","year":"2005","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA118.003014_bib14","doi-asserted-by":"crossref","first-page":"2423","DOI":"10.1091\/mbc.e03-09-0699","article-title":"The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins","volume":"15","author":"Oka","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.RA118.003014_bib15","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.RA118.003014_bib16","doi-asserted-by":"crossref","first-page":"3764","DOI":"10.1073\/pnas.0507685103","article-title":"Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II. Proc. Natl. Acad. Sci","volume":"103","author":"Foulquier","year":"2006","journal-title":"U.S.A"},{"key":"10.1074\/jbc.RA118.003014_bib17","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1093\/hmg\/ddm028","article-title":"COG8 deficiency causes new congenital disorder of glycosylation type IIh","volume":"16","author":"Kranz","year":"2007","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA118.003014_bib18","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1002\/jms.3936","article-title":"MALDI-MS profiling of serum O-glycosylation and N-glycosylation in COG5-CDG","volume":"52","author":"Palmigiano","year":"2017","journal-title":"J. Mass Spectrom"},{"key":"10.1074\/jbc.RA118.003014_bib19","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.ab.2013.07.037","article-title":"Serum N-glycan and O-glycan analysis by mass spectrometry for diagnosis of congenital disorders of glycosylation","volume":"442","author":"Xia","year":"2013","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.RA118.003014_bib20","doi-asserted-by":"crossref","first-page":"3637","DOI":"10.1242\/jcs.209049","article-title":"COG7 deficiency in Drosophila generates multifaceted developmental, behavioral and protein glycosylation phenotypes","volume":"130","author":"Frappaolo","year":"2017","journal-title":"J. Cell Sci"},{"key":"10.1074\/jbc.RA118.003014_bib21","doi-asserted-by":"crossref","first-page":"1576","DOI":"10.1083\/jcb.102.5.1576","article-title":"Three types of low density lipoprotein receptor-deficient mutant have pleiotropic defects in the synthesis of N-linked, O-linked, and lipid-linked carbohydrate chains","volume":"102","author":"Kingsley","year":"1986","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA118.003014_bib22","doi-asserted-by":"crossref","first-page":"5454","DOI":"10.1073\/pnas.81.17.5454","article-title":"Receptor-mediated endocytosis of low density lipoprotein: somatic cell mutants define multiple genes required for expression of surface-receptor activity","volume":"81","author":"Kingsley","year":"1984","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA118.003014_bib23","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1083\/jcb.102.5.1567","article-title":"Unusual forms of low density lipoprotein receptors in hamster cell mutants with defects in the receptor structural gene","volume":"102","author":"Kozarsky","year":"1986","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA118.003014_bib24","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1242\/dev.00199","article-title":"Dystroglycan is required for polarizing the epithelial cells and the oocyte in Drosophila","volume":"130","author":"Deng","year":"2003","journal-title":"Development"},{"key":"10.1074\/jbc.RA118.003014_bib25","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nchembio.2539","article-title":"Expression system for structural and functional studies of human glycosylation enzymes","volume":"14","author":"Moremen","year":"2018","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/jbc.RA118.003014_bib26","doi-asserted-by":"crossref","first-page":"3805","DOI":"10.1242\/dev.02549","article-title":"Perlecan and Dystroglycan act at the basal side of the Drosophila follicular epithelium to maintain epithelial organization","volume":"133","author":"Schneider","year":"2006","journal-title":"Development"},{"key":"10.1074\/jbc.RA118.003014_bib27","doi-asserted-by":"crossref","first-page":"5381","DOI":"10.1021\/ja3002666","article-title":"Polar dibenzocyclooctynes for selective labeling of extracellular glycoconjugates of living cells","volume":"134","author":"Friscourt","year":"2012","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.003014_bib28","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1038\/icb.1947.32","article-title":"Desquamation of intestinal epithelium in vitro by V. cholerae filtrates: characterization of mucinase and tissue disintegrating enzymes","volume":"25","author":"Burnet","year":"1947","journal-title":"Aust. J. Exp. Biol. Med. Sci"},{"key":"10.1074\/jbc.RA118.003014_bib29","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/S0969-2126(00)00053-8","article-title":"Crystal structure of Vibrio cholera neuraminidase reveals dual lectin-like domains in addition to the catalytic domain","volume":"2","author":"Crennell","year":"1994","journal-title":"Structure"},{"key":"10.1074\/jbc.RA118.003014_bib30","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1093\/infdis\/145.4.474","article-title":"Purification and characterization of the mucinase of Vibrio cholerae","volume":"145","author":"Schneider","year":"1982","journal-title":"J. Infect. Dis"},{"key":"10.1074\/jbc.RA118.003014_bib31","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1099\/00222615-22-4-325","article-title":"Studies on the Vibrio cholerae mucinase complex: I. enzymic activities associated with the complex","volume":"22","author":"Stewart-Tull","year":"1986","journal-title":"J. Med. Microbiol"},{"key":"10.1074\/jbc.RA118.003014_bib32","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1111\/j.1432-1033.1997.00166.x","article-title":"The N-terminal region of \u03b1-dystroglycan is an autonomous globular domain","volume":"246","author":"Brancaccio","year":"1997","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.RA118.003014_bib33","doi-asserted-by":"crossref","first-page":"4011","DOI":"10.1096\/fj.14-269456","article-title":"Posttranslational removal of \u03b1-dystroglycan N terminus by PC5\/6 cleavage is important for uterine preparation for embryo implantation in women","volume":"29","author":"Heng","year":"2015","journal-title":"FASEB J"},{"key":"10.1074\/jbc.RA118.003014_bib34","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1099\/mic.0.044529-0","article-title":"TagA is a secreted protease of Vibrio cholerae that specifically cleaves mucin glycoproteins","volume":"157","author":"Szabady","year":"2011","journal-title":"Microbiology"},{"key":"10.1074\/jbc.RA118.003014_bib35","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1126\/science.1252480","article-title":"Virus entry: lassa virus entry requires a trigger-induced receptor switch","volume":"344","author":"Jae","year":"2014","journal-title":"Science"},{"key":"10.1074\/jbc.RA118.003014_bib36","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1126\/science.1233675","article-title":"Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry","volume":"340","author":"Jae","year":"2013","journal-title":"Science"},{"key":"10.1074\/jbc.RA118.003014_bib37","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1093\/glycob\/cwp074","article-title":"Mutational and functional analysis of Large in a novel CHO glycosylation mutant","volume":"19","author":"Aguilan","year":"2009","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA118.003014_bib38","doi-asserted-by":"crossref","first-page":"3623","DOI":"10.1093\/hmg\/ddq278","article-title":"Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation","volume":"19","author":"L\u00fcbbehusen","year":"2010","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA118.003014_bib39","doi-asserted-by":"crossref","first-page":"4350","DOI":"10.1093\/hmg\/ddp389","article-title":"Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation","volume":"18","author":"Paesold-Burda","year":"2009","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA118.003014_bib40","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1186\/1750-1172-7-94","article-title":"COG5-CDG: expanding the clinical spectrum","volume":"7","author":"Rymen","year":"2012","journal-title":"Orphanet J. Rare Dis"},{"key":"10.1074\/jbc.RA118.003014_bib41","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.ymgme.2015.07.003","article-title":"Key features and clinical variability of COG6-CDG","volume":"116","author":"Rymen","year":"2015","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.RA118.003014_bib42","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.ajhg.2009.06.006","article-title":"Deficiency of Dol-P-Man synthase subunit DPM3 bridges the congenital disorders of glycosylation with the dystroglycanopathies","volume":"85","author":"Lefeber","year":"2009","journal-title":"Am. J. Hum. Genet"},{"key":"10.1074\/jbc.RA118.003014_bib43","doi-asserted-by":"crossref","first-page":"1912","DOI":"10.1002\/cbic.201100117","article-title":"Strain-promoted alkyne-azide cycloadditions (SPAAC) reveal new features of glycoconjugate biosynthesis","volume":"12","author":"Mbua","year":"2011","journal-title":"Chembiochem"},{"key":"10.1074\/jbc.RA118.003014_bib44","doi-asserted-by":"crossref","first-page":"3982","DOI":"10.1074\/jbc.M115.700369","article-title":"Selective exo-enzymatic labeling detects increased cell surface sialoglycoprotein expression upon megakaryocytic differentiation","volume":"291","author":"Yu","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.003014_bib45","doi-asserted-by":"crossref","first-page":"e97567","DOI":"10.1371\/journal.pone.0097567","article-title":"Development of rabbit monoclonal antibodies for detection of \u03b1-dystroglycan in normal and dystrophic tissue","volume":"9","author":"Fortunato","year":"2014","journal-title":"PLoS One"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820309224?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820309224?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA118.003014","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,7,8]],"date-time":"2024-07-08T17:55:59Z","timestamp":1720461359000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820309224"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,9]]},"references-count":45,"journal-issue":{"issue":"37","published-print":{"date-parts":[[2018,9]]}},"alternative-id":["S0021925820309224"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra118.003014","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2018,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Defective mucin-type glycosylation on \u03b1-dystroglycan in COG-deficient cells increases its susceptibility to bacterial proteases","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA118.003014","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Yu et al.","name":"copyright","label":"Copyright"}]}}