{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T05:00:59Z","timestamp":1777525259326,"version":"3.51.4"},"reference-count":45,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"ShelbyBioTech LLC","award":["75994-00 01"],"award-info":[{"award-number":["75994-00 01"]}]},{"name":"University of Medicine and Dentistry Biomedical Research Support","award":["75745-00 01"],"award-info":[{"award-number":["75745-00 01"]}]},{"DOI":"10.13039\/100006462","name":"City University of New York","doi-asserted-by":"publisher","award":["68407-01 01"],"award-info":[{"award-number":["68407-01 01"]}],"id":[{"id":"10.13039\/100006462","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006462","name":"City University of New York","doi-asserted-by":"publisher","award":["2109012500"],"award-info":[{"award-number":["2109012500"]}],"id":[{"id":"10.13039\/100006462","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008261","name":"City College of New York","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008261","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000097","name":"National Center for Research Resources","doi-asserted-by":"publisher","award":["2G12RR03060-26A1"],"award-info":[{"award-number":["2G12RR03060-26A1"]}],"id":[{"id":"10.13039\/100000097","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Protein Expression and Purification"],"published-print":{"date-parts":[[2020,11]]},"DOI":"10.1016\/j.pep.2020.105710","type":"journal-article","created":{"date-parts":[[2020,7,29]],"date-time":"2020-07-29T08:02:23Z","timestamp":1596009743000},"page":"105710","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"special_numbering":"C","title":["Prediction of improved therapeutics for fabry disease patients generated by mutagenesis of the \u03b1-galactosidase A active site, dimer interface, and glycosylation region"],"prefix":"10.1016","volume":"175","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5142-838X","authenticated-orcid":false,"given":"Erin S.","family":"Stokes","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. Lane","family":"Gilchrist","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David H.","family":"Calhoun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"Pt 3","key":"10.1016\/j.pep.2020.105710_bib1","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1042\/bj3320789","article-title":"Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility","volume":"332","author":"Ioannou","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.pep.2020.105710_bib2","series-title":"The Metabolic Basis of Inherited Disease","article-title":"A-galactosidase A defiency: fabry disease","author":"Desnick","year":"1995"},{"key":"10.1016\/j.pep.2020.105710_bib3","series-title":"Fabry Disease: Perspectives from 5 Years of FOS","article-title":"History of lysosomal storage diseases: an overview","author":"Mehta","year":"2006"},{"issue":"1","key":"10.1016\/j.pep.2020.105710_bib4","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.pharmthera.2009.01.003","article-title":"Fabry disease","volume":"122","author":"Schiffmann","year":"2009","journal-title":"Pharmacol. Ther."},{"issue":"4","key":"10.1016\/j.pep.2020.105710_bib5","doi-asserted-by":"crossref","first-page":"338","DOI":"10.7326\/0003-4819-138-4-200302180-00014","article-title":"Fabry disease, an under-recognized multisystemic disorder: expert recommendations for diagnosis, management, and enzyme replacement therapy","volume":"138","author":"Desnick","year":"2003","journal-title":"Ann. Intern. Med."},{"issue":"1","key":"10.1016\/j.pep.2020.105710_bib6","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1086\/504601","article-title":"High incidence of later-onset fabry disease revealed by newborn screening","volume":"79","author":"Spada","year":"2006","journal-title":"Am. J. Hum. Genet."},{"issue":"5","key":"10.1016\/j.pep.2020.105710_bib7","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1161\/CIRCGENETICS.109.862920","article-title":"High incidence of the cardiac variant of Fabry disease revealed by newborn screening in the Taiwan Chinese population","volume":"2","author":"Lin","year":"2009","journal-title":"Circ. Cardiovasc. Genet."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib8","first-page":"4","article-title":"A review of fabry disease","volume":"23","author":"Chan","year":"2018","journal-title":"Skin Ther. Lett."},{"issue":"4","key":"10.1016\/j.pep.2020.105710_bib9","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"},{"issue":"1","key":"10.1016\/j.pep.2020.105710_bib10","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1073\/pnas.97.1.365","article-title":"Infusion of alpha-galactosidase A reduces tissue globotriaosylceramide storage in patients with Fabry disease","volume":"97","author":"Schiffmann","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.pep.2020.105710_bib11","series-title":"Fabry Disease 2007 Book","article-title":"Possible future therapies for Fabry disease","author":"Brady","year":"2007"},{"issue":"Suppl 1","key":"10.1016\/j.pep.2020.105710_bib12","first-page":"26","article-title":"Enzyme replacement therapy for lysosomal storage diseases","volume":"10","author":"Ohashi","year":"2012","journal-title":"Pediatr. Endocrinol. Rev."},{"issue":"6","key":"10.1016\/j.pep.2020.105710_bib13","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1007\/s10545-012-9472-3","article-title":"Lysosomal delivery of therapeutic enzymes in cell models of Fabry disease","volume":"35","author":"Marchesan","year":"2012","journal-title":"J. Inherit. Metab. Dis."},{"issue":"4","key":"10.1016\/j.pep.2020.105710_bib14","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/j.ymgme.2018.02.014","article-title":"Fabry disease revisited: management and treatment recommendations for adult patients","volume":"123","author":"Ortiz","year":"2018","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.pep.2020.105710_bib15","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/B978-0-12-396962-0.00011-2","article-title":"Reengineering biopharmaceuticals for targeted delivery across the blood-brain barrier","volume":"503","author":"Pardridge","year":"2012","journal-title":"Methods Enzymol."},{"issue":"7","key":"10.1016\/j.pep.2020.105710_bib16","doi-asserted-by":"crossref","first-page":"2616","DOI":"10.1073\/pnas.0712147105","article-title":"Chemically modified beta-glucuronidase crosses blood-brain barrier and clears neuronal storage in murine mucopolysaccharidosis VII","volume":"105","author":"Grubb","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"21","key":"10.1016\/j.pep.2020.105710_bib17","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"},{"issue":"1","key":"10.1016\/j.pep.2020.105710_bib18","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1056\/NEJM200107053450102","article-title":"Safety and efficacy of recombinant human alpha-galactosidase A replacement therapy in Fabry's disease","volume":"345","author":"Eng","year":"2001","journal-title":"N. Engl. J. Med."},{"issue":"5","key":"10.1016\/j.pep.2020.105710_bib19","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1007\/s40265-019-01090-4","article-title":"Migalastat: a review in fabry disease","volume":"79","author":"McCafferty","year":"2019","journal-title":"Drugs"},{"issue":"1","key":"10.1016\/j.pep.2020.105710_bib20","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1186\/s13023-018-0813-7","article-title":"Migalastat improves diarrhea in patients with Fabry disease: clinical-biomarker correlations from the phase 3 FACETS trial","volume":"13","author":"Schiffmann","year":"2018","journal-title":"Orphanet J. Rare Dis."},{"issue":"4","key":"10.1016\/j.pep.2020.105710_bib21","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1136\/jmedgenet-2016-104178","article-title":"Oral pharmacological chaperone migalastat compared with enzyme replacement therapy in Fabry disease: 18-month results from the randomised phase III ATTRACT study","volume":"54","author":"Hughes","year":"2017","journal-title":"J. Med. Genet."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib22","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21020489","article-title":"Pharmacological chaperones: a therapeutic approach for diseases caused by destabilizing missense mutations","volume":"21","author":"Liguori","year":"2020","journal-title":"Int. J. Mol. Sci."},{"issue":"5","key":"10.1016\/j.pep.2020.105710_bib23","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1002\/emmm.200900036","article-title":"Treating lysosomal storage diseases with pharmacological chaperones: from concept to clinics","volume":"1","author":"Parenti","year":"2009","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.pep.2020.105710_bib24","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/1750-1172-5-36","article-title":"Prediction of the responsiveness to pharmacological chaperones: lysosomal human alpha-galactosidase, a case of study","volume":"5","author":"Andreotti","year":"2010","journal-title":"Orphanet J. Rare Dis."},{"issue":"3","key":"10.1016\/j.pep.2020.105710_bib25","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1007\/s10545-011-9424-3","article-title":"Synergy between the pharmacological chaperone 1-deoxygalactonojirimycin and the human recombinant alpha-galactosidase A in cultured fibroblasts from patients with Fabry disease","volume":"35","author":"Porto","year":"2012","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.pep.2020.105710_bib26","doi-asserted-by":"crossref","DOI":"10.2174\/1381612826666200317142412","article-title":"Treatment of anderson-fabry disease","author":"Simonetta","year":"2020","journal-title":"Curr. Pharmaceut. Des."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib27","doi-asserted-by":"crossref","first-page":"96","DOI":"10.2174\/1566523218666180404161315","article-title":"Genetics and gene therapy of anderson-fabry disease","volume":"18","author":"Simonetta","year":"2018","journal-title":"Curr. Gene Ther."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib28","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/j.jmb.2004.01.035","article-title":"The molecular defect leading to Fabry disease: structure of human alpha-galactosidase","volume":"337","author":"Garman","year":"2004","journal-title":"J. Mol. Biol."},{"issue":"6","key":"10.1016\/j.pep.2020.105710_bib29","doi-asserted-by":"crossref","first-page":"3625","DOI":"10.1074\/jbc.M109.060145","article-title":"Catalytic mechanism of human alpha-galactosidase","volume":"285","author":"Guce","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib30","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.ymgme.2014.08.002","article-title":"Characterization of a chemically modified plant cell culture expressed human alpha-Galactosidase-A enzyme for treatment of Fabry disease","volume":"114","author":"Kizhner","year":"2015","journal-title":"Mol. Genet. Metabol."},{"issue":"11","key":"10.1016\/j.pep.2020.105710_bib31","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1093\/protein\/gzh093","article-title":"Disulfide bonds, their stereospecific environment and conservation in protein structures","volume":"17","author":"Bhattacharyya","year":"2004","journal-title":"Protein Eng. Des. Sel."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib32","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0118341","article-title":"Carboxyl-terminal truncations alter the activity of the human alpha-galactosidase A","volume":"10","author":"Meghdari","year":"2015","journal-title":"PloS One"},{"key":"10.1016\/j.pep.2020.105710_bib33","first-page":"1","article-title":"Elementary steps in enzyme reactions (as studied by relaxation spectrometry)","volume":"25","author":"Eigen","year":"1963","journal-title":"Adv. Enzymol. Relat. Subj. Biochem."},{"issue":"3","key":"10.1016\/j.pep.2020.105710_bib34","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1006\/prep.2000.1325","article-title":"Expression and characterization of glycosylated and catalytically active recombinant human alpha-galactosidase A produced in Pichia pastoris","volume":"20","author":"Chen","year":"2000","journal-title":"Protein Expr. Purif."},{"issue":"1","key":"10.1016\/j.pep.2020.105710_bib35","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0167-4838(96)00108-2","article-title":"Trp-16 is essential for the activity of alpha-galactosidase and alpha-N-acetylgalactosaminidase","volume":"1297","author":"Zhu","year":"1996","journal-title":"Biochim. Biophys. Acta"},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib36","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0003-2697(89)90602-7","article-title":"Calculation of protein extinction coefficients from amino-acid sequence data","volume":"182","author":"Gill","year":"1989","journal-title":"Anal. Biochem."},{"issue":"3","key":"10.1016\/j.pep.2020.105710_bib37","doi-asserted-by":"crossref","DOI":"10.2144\/00283bm07","article-title":"Heating greatly speeds coomassie blue staining and destaining (vol 28, pg 426, 2000)","volume":"29","author":"Wong","year":"2000","journal-title":"Biotechniques"},{"key":"10.1016\/j.pep.2020.105710_bib38","series-title":"Biochemistry & Molecular Biology","first-page":"42","article-title":"Investigation of the effect of dimerization on human \u03b1-galactosidase activity","author":"Dooley","year":"2014"},{"key":"10.1016\/j.pep.2020.105710_bib39","first-page":"iv","article-title":"The possible effects of the aggregation of the molecules of h\u00e6moglobin on its dissociation curves","volume":"40","author":"Hill","year":"1910","journal-title":"J. Physiol."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib40","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/0304-4165(76)90017-9","article-title":"Properties of mouse alpha-galactosidase","volume":"437","author":"Lusis","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"issue":"20","key":"10.1016\/j.pep.2020.105710_bib41","doi-asserted-by":"crossref","first-page":"9994","DOI":"10.1016\/S0021-9258(19)86663-2","article-title":"Studies on human liver alpha-galactosidases. I. Purification of alpha-galactosidase A and its enzymatic properties with glycolipid and oligosaccharide substrates","volume":"254","author":"Dean","year":"1979","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.pep.2020.105710_bib42","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/S0021-9258(19)69965-5","article-title":"Affinity purification of alpha-galactosidase A from human spleen, placenta, and plasma with elimination of pyrogen contamination. Properties of the purified splenic enzyme compared to other forms","volume":"256","author":"Bishop","year":"1981","journal-title":"J. Biol. Chem."},{"issue":"36","key":"10.1016\/j.pep.2020.105710_bib43","doi-asserted-by":"crossref","first-page":"28020","DOI":"10.1074\/jbc.M110.144584","article-title":"Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH27 glycosidases","volume":"285","author":"Fernandez-Leiro","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.pep.2020.105710_bib44","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/S0021-9258(17)38286-8","article-title":"Purification and properties of the two major isozymes of alpha-galactosidase from human placenta","volume":"253","author":"Kusiak","year":"1978","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.pep.2020.105710_bib45","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/0005-2744(78)90235-8","article-title":"Plasma alpha-galactosidase A:properties and comparisons with tissue alpha-galactosidases","volume":"525","author":"Bishop","year":"1978","journal-title":"Biochim. Biophys. Acta"}],"container-title":["Protein Expression and Purification"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592820303016?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592820303016?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T01:55:02Z","timestamp":1760925302000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1046592820303016"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11]]},"references-count":45,"alternative-id":["S1046592820303016"],"URL":"https:\/\/doi.org\/10.1016\/j.pep.2020.105710","relation":{},"ISSN":["1046-5928"],"issn-type":[{"value":"1046-5928","type":"print"}],"subject":[],"published":{"date-parts":[[2020,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Prediction of improved therapeutics for fabry disease patients generated by mutagenesis of the \u03b1-galactosidase A active site, dimer interface, and glycosylation region","name":"articletitle","label":"Article Title"},{"value":"Protein Expression and Purification","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.pep.2020.105710","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"105710"}}