{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T09:28:21Z","timestamp":1790155701644,"version":"4.0.1"},"reference-count":16,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2008,7,1]],"date-time":"2008-07-01T00:00:00Z","timestamp":1214870400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Genetics and Metabolism"],"published-print":{"date-parts":[[2008,7]]},"DOI":"10.1016\/j.ymgme.2008.03.008","type":"journal-article","created":{"date-parts":[[2008,5,6]],"date-time":"2008-05-06T14:44:01Z","timestamp":1210085041000},"page":"313-318","source":"Crossref","is-referenced-by-count":48,"title":["Reduced \u03b1-Gal A enzyme activity in Fabry fibroblast cells and Fabry mice tissues induced by serum from antibody positive patients with Fabry disease"],"prefix":"10.1016","volume":"94","author":[{"given":"Toya","family":"Ohashi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sayoko","family":"Iizuka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyuki","family":"Ida","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshikatsu","family":"Eto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ymgme.2008.03.008_bib1","series-title":"The Metabolic and Molecular Bases of Inherited Disease","first-page":"3733","article-title":"Alpha-galactosidase A deficiency: Fabry disease","author":"Desnick","year":"2001"},{"key":"10.1016\/j.ymgme.2008.03.008_bib2","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1086\/345309","article-title":"Recombinant enzyme therapy for Fabry disease: absence of editing of human alpha-galactosidase A mRNA","volume":"72","author":"Blom","year":"2003","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.ymgme.2008.03.008_bib3","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1093\/glycob\/cwg034","article-title":"A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease","volume":"13","author":"Lee","year":"2003","journal-title":"Glycobiology"},{"key":"10.1016\/j.ymgme.2008.03.008_bib4","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1007\/s10038-005-0342-9","article-title":"Comparison of the effects of agalsidase alfa and agalsidase beta on cultured human Fabry fibroblasts and Fabry mice","volume":"51","author":"Sakuraba","year":"2006","journal-title":"J. Hum. Genet."},{"key":"10.1016\/j.ymgme.2008.03.008_bib5","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1056\/NEJM200107053450102","article-title":"International collaborative Fabry disease study group, safety and efficacy of recombinant human alpha-galactosidase A\u2014replacement therapy in Fabry\u2019s disease","volume":"345","author":"Eng","year":"2001","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.ymgme.2008.03.008_bib6","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1086\/422366","article-title":"International Fabry disease study group, long-term safety and efficacy of enzyme replacement therapy for Fabry disease","volume":"75","author":"Wilcox","year":"2004","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.ymgme.2008.03.008_bib7","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1111\/j.0022-202X.2004.22425.x","article-title":"Monitoring the 3-year efficacy of enzyme replacement therapy in fabry disease by repeated skin biopsies","volume":"122","author":"Thurberg","year":"2004","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.ymgme.2008.03.008_bib8","doi-asserted-by":"crossref","first-page":"2743","DOI":"10.1001\/jama.285.21.2743","article-title":"Enzyme replacement therapy in Fabry disease: a randomized controlled trial","volume":"285","author":"Schiffmann","year":"2001","journal-title":"JAMA"},{"key":"10.1016\/j.ymgme.2008.03.008_bib9","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1681\/ASN.2006080816","article-title":"Sustained, long-term renal stabilization after 54 months of agalsidase {beta} therapy in patients with Fabry disease","volume":"18","author":"Germain","year":"2007","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.ymgme.2008.03.008_bib10","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1093\/ndt\/gfi152","article-title":"Long-term therapy with agalsidase alfa for Fabry disease: safety and effects on renal function in a home infusion setting","volume":"21","author":"Schiffmann","year":"2006","journal-title":"Nephrol. Dial. Transplant."},{"key":"10.1016\/j.ymgme.2008.03.008_bib11","doi-asserted-by":"crossref","first-page":"77","DOI":"10.7326\/0003-4819-146-2-200701160-00148","article-title":"Fabry disease clinical trial study group, agalsidase-beta therapy for advanced Fabry disease: a randomized trial","volume":"146","author":"Banikazemi","year":"2007","journal-title":"Ann. Intern. Med."},{"key":"10.1016\/j.ymgme.2008.03.008_bib12","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1111\/j.1523-1755.2004.00924.x","article-title":"Enzyme therapy for Fabry disease: neutralizing antibodies toward agalsidase alpha and beta","volume":"66","author":"Linthorst","year":"2004","journal-title":"Kidney Int."},{"key":"10.1016\/j.ymgme.2008.03.008_bib13","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.ymgme.2007.06.013","article-title":"Influence of antibody formation on reduction of globotriaosylceramide (GL-3) in urine from Fabry patients during agalsidase beta therapy","volume":"92","author":"Ohashi","year":"2007","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.ymgme.2008.03.008_bib14","doi-asserted-by":"crossref","first-page":"1608","DOI":"10.1016\/S0140-6736(03)13311-9","article-title":"Immune tolerance after long-term enzyme-replacement therapy among patients who have mucopolysaccharidosis I","volume":"361","author":"Kakavanos","year":"2003","journal-title":"Lancet"},{"key":"10.1016\/j.ymgme.2008.03.008_bib15","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/j.jpeds.2005.12.014","volume":"148","author":"Harmatz","year":"2006","journal-title":"J. Pediatr."},{"key":"10.1016\/j.ymgme.2008.03.008_bib16","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1212\/01.wnl.0000251268.41188.04","article-title":"Recombinant human acid [alpha]-glucosidase: major clinical benefits in infantile-onset Pompe disease","volume":"68","author":"Kishnani","year":"2007","journal-title":"Neurology"}],"container-title":["Molecular Genetics and Metabolism"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1096719208000826?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1096719208000826?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,12,28]],"date-time":"2018-12-28T19:55:57Z","timestamp":1546026957000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1096719208000826"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2008,7]]},"references-count":16,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2008,7]]}},"alternative-id":["S1096719208000826"],"URL":"https:\/\/doi.org\/10.1016\/j.ymgme.2008.03.008","relation":{},"ISSN":["1096-7192"],"issn-type":[{"value":"1096-7192","type":"print"}],"subject":[],"published":{"date-parts":[[2008,7]]}}}