{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,25]],"date-time":"2025-10-25T18:44:54Z","timestamp":1761417894778,"version":"build-2065373602"},"reference-count":46,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,6,1]],"date-time":"2019-06-01T00:00:00Z","timestamp":1559347200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,6,1]],"date-time":"2019-06-01T00:00:00Z","timestamp":1559347200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"Advanced Production Technology Development Program of Ministry of Agriculture, Food and Rural Affairs","award":["312037-05"],"award-info":[{"award-number":["312037-05"]}]},{"name":"the Agriculture, Food and Rural Affairs Research Center Support Program of Ministry of Agriculture, Food and Rural Affairs","award":["714001-7"],"award-info":[{"award-number":["714001-7"]}]},{"name":"Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education","award":["NRF-2018R1A6A3A01011033"],"award-info":[{"award-number":["NRF-2018R1A6A3A01011033"]}]},{"name":"Next-Generation BioGreen 21 program of Rural Development Administration, Republic of Korea","award":["PJ01319803"],"award-info":[{"award-number":["PJ01319803"]}]},{"name":"NRF grant","award":["NRF-2013M3A9B6075887"],"award-info":[{"award-number":["NRF-2013M3A9B6075887"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Protein Expression and Purification"],"published-print":{"date-parts":[[2019,6]]},"DOI":"10.1016\/j.pep.2019.02.014","type":"journal-article","created":{"date-parts":[[2019,2,27]],"date-time":"2019-02-27T07:57:39Z","timestamp":1551254259000},"page":"81-88","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":13,"special_numbering":"C","title":["Production of recombinant human acid \u03b2-glucosidase with high mannose-type N-glycans in rice gnt1 mutant for potential treatment of Gaucher disease"],"prefix":"10.1016","volume":"158","author":[{"given":"Jae-Wan","family":"Jung","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hong-Yeol","family":"Choi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8744-0927","authenticated-orcid":false,"given":"Nguyen-Xuan","family":"Huy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Heajin","family":"Park","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ha Hyung","family":"Kim","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Moon-Sik","family":"Yang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seung-Hoon","family":"Kang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dong-Il","family":"Kim","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nan-Sun","family":"Kim","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.pep.2019.02.014_bib1","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1146\/annurev.genom.4.070802.110415","article-title":"Enzyme therapy for lysosomal storage disease: principles, practice, and prospects","volume":"4","author":"Grabowski","year":"2003","journal-title":"Annu. Rev. Genom. Hum. Genet."},{"key":"10.1016\/j.pep.2019.02.014_bib2","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1111\/j.1365-2141.2004.05351.x","article-title":"Gaucher disease: pathological mechanisms and modern management","volume":"129","author":"Jmoudiak","year":"2005","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.pep.2019.02.014_bib3","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1056\/NEJM199105233242104","article-title":"Replacement therapy for inherited enzyme deficiency--macrophage-targeted glucocerebrosidase for Gaucher's disease","volume":"324","author":"Barton","year":"1991","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.pep.2019.02.014_bib4","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1182\/blood.V82.2.408.408","article-title":"Enzyme therapy in Gaucher disease type 1: dosage efficacy and adverse effects in 33 patients treated for 6 to 24 months","volume":"82","author":"Pastores","year":"1993","journal-title":"Blood"},{"key":"10.1016\/j.pep.2019.02.014_bib5","doi-asserted-by":"crossref","first-page":"33","DOI":"10.7326\/0003-4819-122-1-199501010-00005","article-title":"Enzyme therapy in type 1 Gaucher disease: comparative efficacy of mannose-terminated glucocerebrosidase from natural and recombinant sources","volume":"122","author":"Grabowski","year":"1995","journal-title":"Ann. Intern. Med."},{"key":"10.1016\/j.pep.2019.02.014_bib6","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/S0002-9343(02)01150-6","article-title":"Effectiveness of enzyme replacement therapy in 1028 patients with type 1 Gaucher disease after 2 to 5 years of treatment: a report from the Gaucher Registry","volume":"113","author":"Weinreb","year":"2002","journal-title":"Am. J. Med."},{"key":"10.1016\/j.pep.2019.02.014_bib7","doi-asserted-by":"crossref","first-page":"e21","DOI":"10.1371\/journal.pmed.0010021","article-title":"Enzyme replacement in Gaucher disease","volume":"1","author":"Beutler","year":"2004","journal-title":"PLoS Med."},{"key":"10.1016\/j.pep.2019.02.014_bib8","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1111\/j.1467-7652.2007.00263.x","article-title":"Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system","volume":"5","author":"Shaaltiel","year":"2007","journal-title":"Plant Biotechnol. J"},{"key":"10.1016\/j.pep.2019.02.014_bib9","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1093\/glycob\/cwr157","article-title":"Production of active human glucocerebrosidase in seeds of Arabidopsis thaliana complex-glycan-deficient (cgl) plants","volume":"22","author":"He","year":"2012","journal-title":"Glycobiology"},{"key":"10.1016\/j.pep.2019.02.014_bib10","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1007\/s12010-016-2292-4","article-title":"Production and purification of recombinant glucocerebrosidase in transgenic rice cell suspension cultures","volume":"181","author":"Nam","year":"2017","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.pep.2019.02.014_bib11","doi-asserted-by":"crossref","DOI":"10.3390\/ijms19071972","article-title":"The production of human beta-glucocerebrosidase in Nicotiana benthamiana root culture","volume":"19","author":"Naphatsamon","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.pep.2019.02.014_bib12","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1172\/JCI116409","article-title":"Binding, internalization, and degradation of mannose-terminated glucocerebrosidase by macrophages","volume":"91","author":"Sato","year":"1993","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.pep.2019.02.014_bib13","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1111\/j.1432-1033.1996.00344.x","article-title":"Quantitative analysis of the targeting of mannose-terminal glucocerebrosidase. Predominant uptake by liver endothelial cells","volume":"237","author":"Bijsterbosch","year":"1996","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.pep.2019.02.014_bib14","doi-asserted-by":"crossref","first-page":"14861","DOI":"10.1016\/S0021-9258(18)82412-7","article-title":"Human acid beta-glucosidase. N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity","volume":"268","author":"Berg-Fussman","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2019.02.014_bib15","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1107\/S0907444906038303","article-title":"Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease","volume":"62","author":"Brumshtein","year":"2006","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.pep.2019.02.014_bib16","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/0304-4165(81)90474-8","article-title":"Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation","volume":"673","author":"Furbish","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.pep.2019.02.014_bib17","doi-asserted-by":"crossref","first-page":"2193","DOI":"10.1016\/S0021-9258(18)34905-6","article-title":"Enhanced macrophage uptake of synthetically glycosylated human placental beta-glucocerebrosidase","volume":"257","author":"Doebber","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2019.02.014_bib18","doi-asserted-by":"crossref","first-page":"2807","DOI":"10.1182\/blood.V93.9.2807.409k08_2807_2816","article-title":"A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived beta-glucocerebrosidase: implications for clinical efficacy in treatment of Gaucher disease","volume":"93","author":"Friedman","year":"1999","journal-title":"Blood"},{"key":"10.1016\/j.pep.2019.02.014_bib19","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1038\/nbt1027","article-title":"Plant cell cultures for the production of recombinant proteins","volume":"22","author":"Hellwig","year":"2004","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.pep.2019.02.014_bib20","doi-asserted-by":"crossref","first-page":"412","DOI":"10.3389\/fpls.2016.00412","article-title":"Semicontinuous bioreactor production of recombinant butyrylcholinesterase in transgenic rice cell suspension cultures","volume":"7","author":"Corbin","year":"2016","journal-title":"Front. Plant Sci."},{"key":"10.1016\/j.pep.2019.02.014_bib21","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.pep.2010.10.007","article-title":"Production of functional recombinant bovine trypsin in transgenic rice cell suspension cultures","volume":"76","author":"Kim","year":"2011","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.pep.2019.02.014_bib22","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.enzmictec.2014.05.007","article-title":"Production of functional human vascular endothelial growth factor(165) in transgenic rice cell suspension cultures","volume":"63","author":"Chung","year":"2014","journal-title":"Enzym. Microb. Technol."},{"key":"10.1016\/j.pep.2019.02.014_bib23","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.enzmictec.2014.04.010","article-title":"High-level production of recombinant trypsin in transgenic rice cell culture through utilization of an alternative carbon source and recycling system","volume":"63","author":"Kim","year":"2014","journal-title":"Enzym. Microb. Technol."},{"key":"10.1016\/j.pep.2019.02.014_bib24","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.jbiotec.2016.03.031","article-title":"Production and characterization of recombinant human acid alpha-glucosidase in transgenic rice cell suspension culture","volume":"226","author":"Jung","year":"2016","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.pep.2019.02.014_bib25","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.enzmictec.2010.06.007","article-title":"N-linked glycan analysis of glycoproteins secreted from rice cell suspension cultures under sugar starvation","volume":"47","author":"Shin","year":"2010","journal-title":"Enzym. Microb. Technol."},{"key":"10.1016\/j.pep.2019.02.014_bib26","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.jbiotec.2017.03.033","article-title":"Production of recombinant human acid alpha-glucosidase with high-mannose glycans in gnt1 rice for the treatment of Pompe disease","volume":"249","author":"Jung","year":"2017","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.pep.2019.02.014_bib27","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1111\/tpj.12087","article-title":"N-glycan maturation is crucial for cytokinin-mediated development and cellulose synthesis in Oryza sativa","volume":"73","author":"Fanata","year":"2013","journal-title":"Plant J."},{"key":"10.1016\/j.pep.2019.02.014_bib28","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1111\/j.1467-7652.2008.00330.x","article-title":"Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure","volume":"6","author":"Strasser","year":"2008","journal-title":"Plant Biotechnol. J"},{"key":"10.1016\/j.pep.2019.02.014_bib29","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/BF00036805","article-title":"Transgene expression variability (position effect) of CAT and GUS reporter genes driven by linked divergent T-DNA promoters","volume":"17","author":"Peach","year":"1991","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.pep.2019.02.014_bib30","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1111\/j.1467-7652.2006.00216.x","article-title":"Approaches to achieve high-level heterologous protein production in plants","volume":"5","author":"Streatfield","year":"2007","journal-title":"Plant Biotechnol. J"},{"key":"10.1016\/j.pep.2019.02.014_bib31","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1046\/j.1365-313X.1994.6050625.x","article-title":"Expression of \u03b1-amylases, carbohydrate metabolism, and autophagy in cultured rice cells is coordinately regulated by sugar nutrient","volume":"6","author":"Chen","year":"1994","journal-title":"Plant J."},{"key":"10.1016\/j.pep.2019.02.014_bib32","doi-asserted-by":"crossref","first-page":"8013","DOI":"10.1073\/pnas.0832472100","article-title":"Function and glycosylation of plant-derived antiviral monoclonal antibody","volume":"100","author":"Ko","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.pep.2019.02.014_bib33","doi-asserted-by":"crossref","first-page":"8926","DOI":"10.1038\/srep08926","article-title":"Effects of N-glycosylation on protein conformation and dynamics: protein Data Bank analysis and molecular dynamics simulation study","volume":"5","author":"Lee","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.pep.2019.02.014_bib34","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1007\/s11103-008-9367-8","article-title":"Improvement of recombinant hGM-CSF production by suppression of cysteine proteinase gene expression using RNA interference in a transgenic rice culture","volume":"68","author":"Kim","year":"2008","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.pep.2019.02.014_bib35","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.enzmictec.2017.09.006","article-title":"Spontaneous pepsin C-catalyzed activation of human pepsinogen C in transgenic rice cell suspension culture: production and characterization of human pepsin C","volume":"108","author":"Islam","year":"2018","journal-title":"Enzym. Microb. Technol."},{"key":"10.1016\/j.pep.2019.02.014_bib36","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1093\/glycob\/cwg024","article-title":"Immunoreactivity in mammals of two typical plant glyco-epitopes, core \u03b1(1,3)-fucose and core xylose","volume":"13","author":"Bardor","year":"2003","journal-title":"Glycobiology"},{"key":"10.1016\/j.pep.2019.02.014_bib37","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1038\/nbt.3359","article-title":"Using GlycoDelete to produce proteins lacking plant-specific N-glycan modification in seeds","volume":"33","author":"Piron","year":"2015","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.pep.2019.02.014_bib38","doi-asserted-by":"crossref","first-page":"11451","DOI":"10.1074\/jbc.275.15.11451","article-title":"\u03b2(1,2)-Xylose and \u03b1(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens","volume":"275","author":"van Ree","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2019.02.014_bib39","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1038\/nbt.3556","article-title":"Plant specific N-glycans do not have proven adverse effects in humans","volume":"34","author":"Shaaltiel","year":"2016","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.pep.2019.02.014_bib40","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0186211","article-title":"Immunogenicity of glycans on biotherapeutic drugs produced in plant expression systems-The taliglucerase alfa story","volume":"12","author":"Rup","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.pep.2019.02.014_bib41","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1093\/glycob\/cwm008","article-title":"Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease","volume":"17","author":"Van Patten","year":"2007","journal-title":"Glycobiology"},{"key":"10.1016\/j.pep.2019.02.014_bib42","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1007\/BF00014672","article-title":"The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation","volume":"25","author":"Hajdukiewicz","year":"1994","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.pep.2019.02.014_bib43","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1007\/s11240-013-0309-z","article-title":"Amylase and cysteine proteinase gene knockdown in rice cells using RNA interference for enhancing production of recombinant proteins","volume":"114","author":"Kim","year":"2013","journal-title":"Plant Cell Tissue Organ Cult. (PCTOC)"},{"key":"10.1016\/j.pep.2019.02.014_bib44","doi-asserted-by":"crossref","first-page":"4743","DOI":"10.1021\/bi00640a033","article-title":"RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination","volume":"16","author":"Lehrach","year":"1977","journal-title":"Biochemistry"},{"key":"10.1016\/j.pep.2019.02.014_bib45","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1007\/s10719-013-9498-2","article-title":"Type and branched pattern of N-glycans and their structural effect on the chicken egg allergen ovotransferrin: a comparison with ovomucoid","volume":"31","author":"Hwang","year":"2014","journal-title":"Glycoconj. J."},{"key":"10.1016\/j.pep.2019.02.014_bib46","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1023\/A:1006983125913","article-title":"A general approach to desalting oligosaccharides released from glycoproteins","volume":"15","author":"Packer","year":"1998","journal-title":"Glycoconj. J."}],"container-title":["Protein Expression and Purification"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592818305965?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592818305965?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T01:51:58Z","timestamp":1760925118000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1046592818305965"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,6]]},"references-count":46,"alternative-id":["S1046592818305965"],"URL":"https:\/\/doi.org\/10.1016\/j.pep.2019.02.014","relation":{},"ISSN":["1046-5928"],"issn-type":[{"type":"print","value":"1046-5928"}],"subject":[],"published":{"date-parts":[[2019,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Production of recombinant human acid \u03b2-glucosidase with high mannose-type N-glycans in rice gnt1 mutant for potential treatment of Gaucher disease","name":"articletitle","label":"Article Title"},{"value":"Protein Expression and Purification","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.pep.2019.02.014","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}