{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T21:08:30Z","timestamp":1791752910523,"version":"4.3.4"},"reference-count":56,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2014,5,1]],"date-time":"2014-05-01T00:00:00Z","timestamp":1398902400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100004319","name":"Pfizer","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004319","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["mgmjournal.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Genetics and Metabolism"],"published-print":{"date-parts":[[2014,5]]},"DOI":"10.1016\/j.ymgme.2014.02.011","type":"journal-article","created":{"date-parts":[[2014,3,2]],"date-time":"2014-03-02T09:45:12Z","timestamp":1393753512000},"page":"1-8","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":143,"title":["Taliglucerase alfa: An enzyme replacement therapy using plant cell expression technology"],"prefix":"10.1016","volume":"112","author":[{"given":"Gregory A.","family":"Grabowski","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Myriam","family":"Golembo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoseph","family":"Shaaltiel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ymgme.2014.02.011_bb0005","series-title":"The Metabolic and Molecular Basis of Inherited Disease","first-page":"1","article-title":"Gaucher disease","author":"Grabowski","year":"2010"},{"issue":"4 Suppl.","key":"10.1016\/j.ymgme.2014.02.011_bb0010","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1016\/j.jpeds.2009.07.004","article-title":"Recommendations on diagnosis, treatment, and monitoring for Gaucher disease","volume":"155","author":"Martins","year":"2009","journal-title":"J. Pediatr."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0015","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.ymgme.2014.02.011_bb0020","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1073\/pnas.75.3.1399","article-title":"Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages","volume":"75","author":"Stahl","year":"1978","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0025","first-page":"547","article-title":"Receptor-mediated uptake of lysosomal enzymes","volume":"23","author":"Sly","year":"1978","journal-title":"Prog. Clin. Biol. Res."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0030","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.ymgme.2014.02.011_bb0035","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.ymgme.2014.02.011_bb0040","series-title":"Cerezyme [Package Insert]","year":"2009"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0045","series-title":"VPRIV [Package Insert]","year":"2010"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0050","doi-asserted-by":"crossref","first-page":"285","DOI":"10.4155\/cli.10.21","article-title":"Velaglucerase alfa in the treatment of Gaucher disease type 1","volume":"1","author":"Burrow","year":"2011","journal-title":"Clin. Investig. (Lond.)"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0055","series-title":"Elelyso [Package Insert]","year":"2012"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0060","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/nbt0612-472","article-title":"First plant-made biologic approved","volume":"30","author":"Fox","year":"2012","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0065","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.jbiotec.2006.07.012","article-title":"Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes","volume":"127","author":"Yin","year":"2007","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0070","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.ymgme.2014.02.011_bb0075","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.320.5875.473","article-title":"Is the drought over for pharming?","volume":"320","author":"Kaiser","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0080","article-title":"Safety and immunogenicity of a plant-produced recombinant monomer hemagglutinin-based influenza vaccine derived from influenza A (H1N1)pdm09 virus: a phase 1 dose-escalation study in healthy adults","author":"Cummings","year":"2013","journal-title":"Vaccine"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0085","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1586\/erv.10.91","article-title":"Plant-derived vaccines and other therapeutics produced in contained systems","volume":"9","author":"Franconi","year":"2010","journal-title":"Expert Rev. Vaccines"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0090","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.pbi.2004.01.015","article-title":"Posttranslational modification of therapeutic proteins in plants","volume":"7","author":"Gomord","year":"2004","journal-title":"Curr. Opin. Plant Biol."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0095","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1016\/j.copbio.2009.10.008","article-title":"Expression systems for therapeutic glycoprotein production","volume":"20","author":"Durocher","year":"2009","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0100","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.pep.2013.05.009","article-title":"Use of baculovirus expression system for generation of virus-like particles: successes and challenges","volume":"90","author":"Liu","year":"2013","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0105","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1111\/j.1467-7652.2009.00497.x","article-title":"Plant-specific glycosylation patterns in the context of therapeutic protein production","volume":"8","author":"Gomord","year":"2010","journal-title":"Plant Biotechnol. J."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0110","author":"European Medicines Agency"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0115","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.ymgme.2014.02.011_bb0120","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1007\/s11627-009-9231-9","article-title":"Continued expression of plant-made vaccines following long-term cryopreservation of antigen-expressing tobacco cell cultures","volume":"45","author":"Van Eck","year":"2009","journal-title":"In Vitro Cell. Dev. Biol. Plant"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0125","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1042\/BSR20130081","article-title":"Glycosylation and functionality of recombinant glucocerebrosidase from various production systems","volume":"33","author":"Tekoah","year":"2013","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0130","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1093\/glycob\/cwp138","article-title":"Characterization of gene-activated human acid-beta-glucosidase: crystal structure, glycan composition, and internalization into macrophages","volume":"20","author":"Brumshtein","year":"2010","journal-title":"Glycobiology"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0135","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.ymgme.2014.02.011_bb0140","doi-asserted-by":"crossref","first-page":"e10750","DOI":"10.1371\/journal.pone.0010750","article-title":"Comparative therapeutic effects of velaglucerase alfa and imiglucerase in a Gaucher disease mouse model","volume":"5","author":"Xu","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0145","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.ymgme.2014.02.011_bb0150","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.ymgme.2014.02.011_bb0155","doi-asserted-by":"crossref","first-page":"10842","DOI":"10.1073\/pnas.1003247107","article-title":"Imaging of enzyme replacement therapy using PET","volume":"107","author":"Phenix","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0160","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1016\/j.cell.2007.10.018","article-title":"LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase","volume":"131","author":"Reczek","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0165","first-page":"741","article-title":"Posttranslational processing of human lysosomal acid beta-glucosidase: a continuum of defects in Gaucher disease type 1 and type 2 fibroblasts","volume":"44","author":"Bergmann","year":"1989","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0170","doi-asserted-by":"crossref","first-page":"2283","DOI":"10.1016\/S0021-9258(17)42166-1","article-title":"Analysis of human acid beta-glucosidase by site-directed mutagenesis and heterologous expression","volume":"269","author":"Grace","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0175","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1023\/A:1006012005654","article-title":"N-glycoprotein biosynthesis in plants: recent developments and future trends","volume":"38","author":"Lerouge","year":"1998","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0180","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.ymgme.2014.02.011_bb0185","doi-asserted-by":"crossref","first-page":"2807","DOI":"10.1182\/blood.V93.9.2807","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.ymgme.2014.02.011_bb0190","unstructured":"B. Friedman and M. Hayes, Enhanced in vivo uptake of glucocerebrosidase. Patent Number: 5,549,892, Genzyme Corporation, Cambridge, MA 1996."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0195","doi-asserted-by":"crossref","first-page":"15599","DOI":"10.1016\/S0021-9258(18)55439-9","article-title":"Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I","volume":"265","author":"Elbein","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0200","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. D Biol. Crystallogr."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0205","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1111\/j.1365-2141.2011.08989.x","article-title":"The uptake of recombinant glucocerebrosidases by blood monocytes from type 1 Gaucher disease patients is variable","volume":"157","author":"Berger","year":"2012","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0210","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1093\/glycob\/cwg024","article-title":"Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha(1,3)-fucose and core xylose","volume":"13","author":"Bardor","year":"2003","journal-title":"Glycobiology"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0215","doi-asserted-by":"crossref","first-page":"1646","DOI":"10.1194\/jlr.M700482-JLR200","article-title":"Wolman disease\/cholesteryl ester storage disease: efficacy of plant-produced human lysosomal acid lipase in mice","volume":"49","author":"Du","year":"2008","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0220","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1023\/A:1008976219939","article-title":"A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice","volume":"9","author":"Chargelegue","year":"2000","journal-title":"Transgenic Res."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0225","author":"ClinicalTrials.gov, National Institutes of Health"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0230","author":"ClinicalTrials.gov, National Institutes of Health"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0235","author":"ClinicalTrials.gov, National Institutes of Health"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0240","author":"ClinicalTrials.gov, National Institutes of Health"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0245","doi-asserted-by":"crossref","first-page":"5767","DOI":"10.1182\/blood-2011-07-366955","article-title":"Pivotal trial with plant cell-expressed recombinant glucocerebrosidase, taliglucerase alfa, a novel enzyme replacement therapy for Gaucher disease","volume":"118","author":"Zimran","year":"2011","journal-title":"Blood"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0250","doi-asserted-by":"crossref","first-page":"S102","DOI":"10.1016\/j.ymgme.2012.11.280","article-title":"Long-term safety and efficacy data of taliglucerase alfa, a plant cell-expressed recombinant glucocerebrosidase, in the treatment of naive Gaucher disease patients: 36-month results [abstract 266]","volume":"108","author":"Zimran","year":"2013","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0255","doi-asserted-by":"crossref","DOI":"10.1182\/blood.V120.21.2140.2140","article-title":"A multicenter, double-blind, randomized safety and efficacy study of two dose levels of taliglucerase alfa in pediatric patients with Gaucher disease [abstract 2140]","volume":"120","author":"Zimran","year":"2012","journal-title":"Blood"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0260","doi-asserted-by":"crossref","first-page":"S73","DOI":"10.1016\/j.ymgme.2012.11.193","article-title":"Plant cell-expressed recombinant glucocerebrosidase: taliglucerase alfa as therapy for Gaucher disease in adults patients previously treated with imiglucerase: 24-month results [abstract 179]","volume":"108","author":"Pastores","year":"2013","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0265","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/nrd3977","article-title":"The most transformative drugs of the past 25years: a survey of physicians","volume":"12","author":"Kesselheim","year":"2013","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ymgme.2014.02.011_bb0275","doi-asserted-by":"crossref","first-page":"1479","DOI":"10.1016\/S0140-6736(95)91038-7","article-title":"Replacement therapy with imiglucerase for type 1 Gaucher's disease","volume":"345","author":"Zimran","year":"1995","journal-title":"Lancet"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0280","doi-asserted-by":"crossref","first-page":"4651","DOI":"10.1182\/blood-2010-02-268649","article-title":"Phase 1\/2 and extension study of velaglucerase alfa replacement therapy in adults with type 1 Gaucher disease: 48-month experience","volume":"115","author":"Zimran","year":"2010","journal-title":"Blood"},{"key":"10.1016\/j.ymgme.2014.02.011_bb0285","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1086\/498652","article-title":"The role of mannosylated enzyme and the mannose receptor in enzyme replacement therapy","volume":"77","author":"Du","year":"2005","journal-title":"Am. J. Hum. Genet."}],"container-title":["Molecular Genetics and Metabolism"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1096719214000791?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1096719214000791?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,3,28]],"date-time":"2022-03-28T04:03:21Z","timestamp":1648440201000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1096719214000791"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,5]]},"references-count":56,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2014,5]]}},"alternative-id":["S1096719214000791"],"URL":"https:\/\/doi.org\/10.1016\/j.ymgme.2014.02.011","relation":{},"ISSN":["1096-7192"],"issn-type":[{"value":"1096-7192","type":"print"}],"subject":[],"published":{"date-parts":[[2014,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Taliglucerase alfa: An enzyme replacement therapy using plant cell expression technology","name":"articletitle","label":"Article Title"},{"value":"Molecular Genetics and Metabolism","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ymgme.2014.02.011","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}