{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:36:25Z","timestamp":1791293785968,"version":"4.1.0"},"reference-count":192,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,6,1]],"date-time":"2016-06-01T00:00:00Z","timestamp":1464739200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2016,6]]},"DOI":"10.1016\/j.biochi.2015.11.009","type":"journal-article","created":{"date-parts":[[2015,11,12]],"date-time":"2015-11-12T17:50:37Z","timestamp":1447350637000},"page":"267-280","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":50,"special_numbering":"C","title":["Glucosylceramidases and malignancies in mammals"],"prefix":"10.1016","volume":"125","author":[{"given":"Leonardo","family":"Astudillo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicole","family":"Therville","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9line","family":"Colacios","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruno","family":"S\u00e9gui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathalie","family":"Andrieu-Abadie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3793-2584","authenticated-orcid":false,"given":"Thierry","family":"Levade","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2015.11.009_bib1","series-title":"A\u00a0Treatise on the Chemical Constitution of the Brain","first-page":"149","author":"Thudichum","year":"1884"},{"key":"10.1016\/j.biochi.2015.11.009_bib2","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/sj.embor.7400208","article-title":"The complex life of simple sphingolipids","volume":"5","author":"Futerman","year":"2004","journal-title":"EMBO Rep."},{"key":"10.1016\/j.biochi.2015.11.009_bib3","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1038\/nrm2329","article-title":"Principles of bioactive lipid signalling: lessons from sphingolipids","volume":"9","author":"Hannun","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.biochi.2015.11.009_bib4","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/nrc3398","article-title":"Ceramide-orchestrated signalling in cancer cells","volume":"13","author":"Morad","year":"2013","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.biochi.2015.11.009_bib5","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1038\/nrc1411","article-title":"Biologically active sphingolipids in cancer pathogenesis and treatment","volume":"4","author":"Ogretmen","year":"2004","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.biochi.2015.11.009_bib6","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/S1388-1981(02)00331-1","article-title":"Ceramide in apoptosis: an overview and current perspectives","volume":"1585","author":"Pettus","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib7","doi-asserted-by":"crossref","first-page":"R11","DOI":"10.1152\/ajpregu.00416.2005","article-title":"Physiological and pathophysiological aspects of ceramide","volume":"290","author":"Gulbins","year":"2006","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"10.1016\/j.biochi.2015.11.009_bib8","doi-asserted-by":"crossref","first-page":"30701","DOI":"10.1074\/jbc.270.51.30701","article-title":"Role of ceramide in cellular senescence","volume":"270","author":"Venable","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib9","doi-asserted-by":"crossref","first-page":"2985","DOI":"10.1172\/JCI29224","article-title":"Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility","volume":"116","author":"Yildiz","year":"2006","journal-title":"J.\u00a0Clin. Investig."},{"key":"10.1016\/j.biochi.2015.11.009_bib10","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1007\/BF02531119","article-title":"Sphingolipid long chain bases","volume":"5","author":"Karlsson","year":"1970","journal-title":"Lipids"},{"key":"10.1016\/j.biochi.2015.11.009_bib11","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.semcdb.2004.03.007","article-title":"The cell biology of glycosphingolipids","volume":"15","author":"Degroote","year":"2004","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.biochi.2015.11.009_bib12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-4419-6741-1_1","article-title":"An overview of sphingolipid metabolism: from synthesis to breakdown","volume":"688","author":"Gault","year":"2010","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.biochi.2015.11.009_bib13","doi-asserted-by":"crossref","first-page":"a004788","DOI":"10.1101\/cshperspect.a011874","article-title":"Glycosphingolipid functions","volume":"3","author":"Lingwood","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.biochi.2015.11.009_bib14","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.plipres.2013.02.001","article-title":"Cell-specific in\u00a0vivo functions of glycosphingolipids: Lessons from genetic deletions of enzymes involved in glycosphingolipid synthesis","volume":"52","author":"Jennemann","year":"2013","journal-title":"Prog. Lipid Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib15","doi-asserted-by":"crossref","first-page":"9142","DOI":"10.1073\/pnas.96.16.9142","article-title":"A\u00a0vital role for glycosphingolipid synthesis during development and differentiation","volume":"96","author":"Yamashita","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib16","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/j.bbalip.2013.06.001","article-title":"New insights on glucosylated lipids: metabolism and functions","volume":"1831","author":"Ishibashi","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib17","doi-asserted-by":"crossref","first-page":"27855","DOI":"10.1074\/jbc.R111.254359","article-title":"Many ceramides","volume":"286","author":"Hannun","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib18","doi-asserted-by":"crossref","first-page":"5802","DOI":"10.1016\/S0021-9258(18)91935-6","article-title":"Enzymatic synthesis of ceramide-glucose and ceramide-lactose by glycosyltransferases from embryonic chicken brain","volume":"243","author":"Basu","year":"1968","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib19","doi-asserted-by":"crossref","first-page":"4638","DOI":"10.1073\/pnas.93.10.4638","article-title":"Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis","volume":"93","author":"Ichikawa","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib20","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1038\/nature02188","article-title":"Molecular machinery for non-vesicular trafficking of ceramide","volume":"426","author":"Hanada","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2015.11.009_bib21","first-page":"40","article-title":"Ceramide traffic in C6 glioma cells: evidence for CERT-dependent and independent transport from ER to the Golgi apparatus","volume":"1781","author":"Giussani","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib22","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1159\/000134731","article-title":"Assignment of a UDP-glucose:ceramide glucosyltransferase gene (UGCG) to human chromosome band 9q31 by in situ hybridization","volume":"79","author":"Ichikawa","year":"1997","journal-title":"Cytogenet. Cell Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib23","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1074\/jbc.274.1.451","article-title":"Oligomerization and topology of the golgi membrane protein glucosylceramide synthase","volume":"274","author":"Marks","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib24","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1038\/nature06097","article-title":"Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide","volume":"449","author":"D'Angelo","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2015.11.009_bib25","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1083\/jcb.200704091","article-title":"Pre- and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis","volume":"179","author":"Halter","year":"2007","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.biochi.2015.11.009_bib26","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1098\/rstb.2003.1266","article-title":"The fate and function of glycosphingolipid glucosylceramide","volume":"358","author":"van Meer","year":"2003","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"10.1016\/j.biochi.2015.11.009_bib27","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1111\/j.1600-0854.2011.01263.x","article-title":"Hyperacidification of trans-golgi network and endo\/lysosomes in melanocytes by glucosylceramide-dependent V-ATPase activity","volume":"12","author":"van der Poel","year":"2011","journal-title":"Traffic"},{"key":"10.1016\/j.biochi.2015.11.009_bib28","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1016\/j.febslet.2009.10.021","article-title":"Lysosomal degradation of membrane lipids","volume":"584","author":"Kolter","year":"2010","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2015.11.009_bib29","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1007\/BF00499084","article-title":"Human lactase and the molecular basis of lactase persistence","volume":"23","author":"Potter","year":"1985","journal-title":"Biochem. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib30","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0021-9258(18)97611-8","article-title":"The metabolism of glucocerebrosides. I. Purification and properties of a glucocerebroside-cleaving enzyme from spleen tissue","volume":"240","author":"Brady","year":"1965","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib31","doi-asserted-by":"crossref","first-page":"385","DOI":"10.3109\/10409239009090616","article-title":"Acid beta-glucosidase: enzymology and molecular biology of Gaucher disease","volume":"25","author":"Grabowski","year":"1990","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.biochi.2015.11.009_bib32","doi-asserted-by":"crossref","first-page":"7090","DOI":"10.1073\/pnas.92.15.7090","article-title":"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases","volume":"92","author":"Henrissat","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib33","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1016\/j.bbrc.2013.10.145","article-title":"Cholesterol glucosylation is catalyzed by transglucosylation reaction of beta-glucosidase 1","volume":"441","author":"Akiyama","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2015.11.009_bib34","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/BF00279398","article-title":"Assignment of the gene coding for human beta-glucocerebrosidase to the region q21-q31 of chromosome 1 using monoclonal antibodies","volume":"64","author":"Barneveld","year":"1983","journal-title":"Hum. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib35","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1016\/0006-291X(84)90268-7","article-title":"Isolation of cDNA clones for human beta-glucocerebrosidase using the lambda gt11 expression system","volume":"123","author":"Ginns","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2015.11.009_bib36","doi-asserted-by":"crossref","first-page":"7289","DOI":"10.1073\/pnas.82.21.7289","article-title":"Molecular cloning and nucleotide sequence of human glucocerebrosidase cDNA","volume":"82","author":"Sorge","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib37","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib38","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.biochi.2015.11.009_bib39","doi-asserted-by":"crossref","first-page":"4321","DOI":"10.1038\/ncomms5321","article-title":"Lysosome sorting of beta-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor","volume":"5","author":"Zhao","year":"2014","journal-title":"Nat. Commun."},{"issue":"10","key":"10.1016\/j.biochi.2015.11.009_bib40","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1111\/tra.12313","article-title":"Mannose 6-phosphate-independent Lysosomal Sorting of LIMP-2","volume":"16","author":"Blanz","year":"2015","journal-title":"Traffic"},{"key":"10.1016\/j.biochi.2015.11.009_bib41","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/0006-291X(90)92388-G","article-title":"Human acid beta-glucosidase: glycosylation is required for catalytic activity","volume":"168","author":"Grace","year":"1990","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2015.11.009_bib42","doi-asserted-by":"crossref","first-page":"10975","DOI":"10.1016\/S0021-9258(19)78077-6","article-title":"Identification of Glu340 as the active-site nucleophile in human glucocerebrosidase by use of electrospray tandem mass spectrometry","volume":"269","author":"Miao","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib43","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1038\/sj.embor.embor873","article-title":"X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease","volume":"4","author":"Dvir","year":"2003","journal-title":"EMBO Rep."},{"key":"10.1016\/j.biochi.2015.11.009_bib44","doi-asserted-by":"crossref","first-page":"23815","DOI":"10.1074\/jbc.M502799200","article-title":"X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease","volume":"280","author":"Premkumar","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib45","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1093\/glycob\/10.11.1217","article-title":"Human glucocerebrosidase: heterologous expression of active site mutants in murine null cells","volume":"10","author":"Fabrega","year":"2000","journal-title":"Glycobiology"},{"key":"10.1016\/j.biochi.2015.11.009_bib46","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1051\/jbio\/2002196020151","article-title":"The active site of human glucocerebrosidase: structural predictions and experimental validations","volume":"196","author":"Fabrega","year":"2002","journal-title":"J.\u00a0Soc. Biol."},{"key":"10.1016\/j.biochi.2015.11.009_bib47","doi-asserted-by":"crossref","first-page":"29052","DOI":"10.1074\/jbc.M705005200","article-title":"Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase: insights into the mechanism of chemical chaperone action in Gaucher disease","volume":"282","author":"Brumshtein","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib48","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/0006-291X(91)92016-D","article-title":"Cyclophellitol: a naturally occurring mechanism-based inactivator of beta-glucosidases","volume":"177","author":"Withers","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2015.11.009_bib49","doi-asserted-by":"crossref","first-page":"8263","DOI":"10.1016\/S0021-9258(19)83905-4","article-title":"Human acid beta-glucosidase. Use of conduritol B epoxide derivatives to investigate the catalytically active normal and Gaucher disease enzymes","volume":"261","author":"Grabowski","year":"1986","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib50","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/0014-4827(87)90019-X","article-title":"Glucocerebrosidase deficiency and lysosomal storage of glucocerebroside induced in cultured macrophages","volume":"168","author":"Das","year":"1987","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib51","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0005-2760(86)90126-8","article-title":"beta-Glucosidase inhibition in murine peritoneal macrophages by conduritol-B-epoxide: an in\u00a0vitro model of the Gaucher cell","volume":"877","author":"Newburg","year":"1986","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib52","doi-asserted-by":"crossref","first-page":"3181","DOI":"10.1182\/blood-2009-02-205708","article-title":"Characterization of Gaucher disease bone marrow mesenchymal stromal cells reveals an altered inflammatory secretome","volume":"114","author":"Campeau","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2015.11.009_bib53","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.ymgme.2007.08.001","article-title":"Secondary sphingolipid accumulation in a macrophage model of Gaucher disease","volume":"92","author":"Hein","year":"2007","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.biochi.2015.11.009_bib54","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1016\/j.bbamem.2006.08.017","article-title":"Inhibitors of sphingolipid metabolism enzymes","volume":"1758","author":"Delgado","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib55","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/0006-291X(65)90743-6","article-title":"Metabolism of Glucocerebrosides. Ii. Evidence of an enzymatic deficiency in Gaucher's disease","volume":"18","author":"Brady","year":"1965","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2015.11.009_bib56","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1016\/S0140-6736(08)61522-6","article-title":"Phenotype, diagnosis, and treatment of Gaucher's disease","volume":"372","author":"Grabowski","year":"2008","journal-title":"Lancet"},{"key":"10.1016\/j.biochi.2015.11.009_bib57","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1002\/humu.22124","article-title":"Gaucher disease paradigm: from ERAD to comorbidity","volume":"33","author":"Bendikov-Bar","year":"2012","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.biochi.2015.11.009_bib58","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1073\/pnas.85.7.2349","article-title":"Genetic heterogeneity in type 1 Gaucher disease: multiple genotypes in Ashkenazic and non-Ashkenazic individuals","volume":"85","author":"Tsuji","year":"1988","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib59","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1056\/NEJM198703053161002","article-title":"A\u00a0mutation in the human glucocerebrosidase gene in neuronopathic Gaucher's disease","volume":"316","author":"Tsuji","year":"1987","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib60","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1212\/WNL.54.1.261","article-title":"Gaucher disease with oculomotor apraxia and cardiovascular calcification (Gaucher type IIIC)","volume":"54","author":"Bohlega","year":"2000","journal-title":"Neurology"},{"key":"10.1016\/j.biochi.2015.11.009_bib61","doi-asserted-by":"crossref","first-page":"2387","DOI":"10.1093\/hmg\/ddi240","article-title":"ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity","volume":"14","author":"Ron","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib62","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1001\/jama.281.3.249","article-title":"Prevalence of lysosomal storage disorders","volume":"281","author":"Meikle","year":"1999","journal-title":"Jama"},{"key":"10.1016\/j.biochi.2015.11.009_bib63","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1242\/dmm.008185","article-title":"Animal models for Gaucher disease research","volume":"4","author":"Farfel-Becker","year":"2011","journal-title":"Dis. Model Mech."},{"key":"10.1016\/j.biochi.2015.11.009_bib64","doi-asserted-by":"crossref","first-page":"e1005065","DOI":"10.1371\/journal.pgen.1005065","article-title":"Viable neuronopathic Gaucher disease model in Medaka (Oryzias latipes) displays axonal accumulation of alpha-synuclein","volume":"11","author":"Uemura","year":"2015","journal-title":"PLoS Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib65","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.bcmd.2013.04.005","article-title":"Miglustat therapy in type 1 Gaucher disease: clinical and safety outcomes in a multicenter retrospective cohort study","volume":"51","author":"Kuter","year":"2013","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib66","doi-asserted-by":"crossref","first-page":"4095","DOI":"10.1182\/blood-2010-06-293902","article-title":"Improvement in hematological, visceral, and skeletal manifestations of Gaucher disease type 1 with oral eliglustat tartrate (Genz-112638) treatment: 2-year results of a phase 2 study","volume":"116","author":"Lukina","year":"2010","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2015.11.009_bib67","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/0014-5793(91)80760-Z","article-title":"Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease","volume":"284","author":"Schnabel","year":"1991","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2015.11.009_bib68","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1007\/s00439-005-1288-x","article-title":"A\u00a0mutation within the saposin D domain in a Gaucher disease patient with normal glucocerebrosidase activity","volume":"117","author":"Diaz-Font","year":"2005","journal-title":"Hum. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib69","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.ymgme.2012.04.024","article-title":"The role of saposin C in Gaucher disease","volume":"106","author":"Tamargo","year":"2012","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.biochi.2015.11.009_bib70","doi-asserted-by":"crossref","first-page":"30271","DOI":"10.1074\/jbc.273.46.30271","article-title":"Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators","volume":"273","author":"Wilkening","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib71","doi-asserted-by":"crossref","first-page":"30576","DOI":"10.1074\/jbc.270.51.30576","article-title":"pH-dependent conformational properties of saposins and their interactions with phospholipid membranes","volume":"270","author":"Vaccaro","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib72","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/j.ajhg.2007.12.019","article-title":"Array-based gene discovery with three unrelated subjects shows SCARB2\/LIMP-2 deficiency causes myoclonus epilepsy and glomerulosclerosis","volume":"82","author":"Berkovic","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib73","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.ymgme.2009.04.011","article-title":"Biochemical and molecular findings in a patient with myoclonic epilepsy due to a mistarget of the beta-glucosidase enzyme","volume":"97","author":"Dardis","year":"2009","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.biochi.2015.11.009_bib74","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1002\/humu.21566","article-title":"A\u00a0mutation in SCARB2 is a modifier in Gaucher disease","volume":"32","author":"Velayati","year":"2011","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.biochi.2015.11.009_bib75","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1056\/NEJMoa0901281","article-title":"Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease","volume":"361","author":"Sidransky","year":"2009","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib76","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.cell.2011.06.001","article-title":"Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies","volume":"146","author":"Mazzulli","year":"2011","journal-title":"Cell"},{"key":"10.1016\/j.biochi.2015.11.009_bib77","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.molmed.2011.05.003","article-title":"Exploring the link between glucocerebrosidase mutations and Parkinsonism","volume":"17","author":"Westbroek","year":"2011","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib78","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0925-4439(93)90090-N","article-title":"Demonstration of the existence of a second, non-lysosomal glucocerebrosidase that is not deficient in Gaucher disease","volume":"1181","author":"van Weely","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib79","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1074\/jbc.M610544200","article-title":"Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2","volume":"282","author":"Boot","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib80","doi-asserted-by":"crossref","first-page":"3381","DOI":"10.1074\/jbc.M112.414714","article-title":"The non-lysosomal beta-glucosidase GBA2 is a non-integral membrane-associated protein at the ER and golgi","volume":"288","author":"Koerschen","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib81","doi-asserted-by":"crossref","first-page":"11261","DOI":"10.1074\/jbc.272.17.11261","article-title":"Purification and characterization of a microsomal bile acid beta-glucosidase from human liver","volume":"272","author":"Matern","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib82","doi-asserted-by":"crossref","first-page":"37929","DOI":"10.1074\/jbc.M104290200","article-title":"Molecular cloning and expression of human bile acid beta-glucosidase","volume":"276","author":"Matern","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib83","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1111\/j.1478-3231.2012.02841.x","article-title":"Beta-glucosidase 2 knockout mice with increased glucosylceramide show impaired liver regeneration","volume":"32","author":"Gonzalez-Carmona","year":"2012","journal-title":"Liver Int."},{"issue":"36","key":"10.1016\/j.biochi.2015.11.009_bib84","doi-asserted-by":"crossref","first-page":"626052","DOI":"10.1074\/jbc.M113.463562","article-title":"Beta-glucosidase 2 (GBA2) activity and imino sugar pharmacology","volume":"288","author":"Ridley","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib85","doi-asserted-by":"crossref","first-page":"26522","DOI":"10.1074\/jbc.273.41.26522","article-title":"Generation of specific deoxynojirimycin-type inhibitors of the non-lysosomal glucosylceramidase","volume":"273","author":"Overkleeft","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib86","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1021\/ml100192b","article-title":"Identification of potent and selective glucosylceramide synthase inhibitors from a library of N-alkylated iminosugars","volume":"2","author":"Ghisaidoobe","year":"2010","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.biochi.2015.11.009_bib87","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.ajhg.2012.11.021","article-title":"Loss of function of glucocerebrosidase GBA2 is responsible for motor neuron defects in hereditary spastic paraplegia","volume":"92","author":"Martin","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib88","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1111\/ahg.12045","article-title":"A\u00a0novel GBA2 gene missense mutation in spastic ataxia","volume":"78","author":"Votsi","year":"2014","journal-title":"Ann. Hum. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib89","first-page":"373","article-title":"Mutations in CYP2U1, DDHD2 and GBA2 genes are rare causes of complicated forms of hereditary spastic paraparesis","volume":"261","author":"Citterio","year":"2014","journal-title":"J.\u00a0Neurol."},{"key":"10.1016\/j.biochi.2015.11.009_bib90","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.ajhg.2012.12.012","article-title":"Mutations in GBA2 cause autosomal-recessive cerebellar ataxia with spasticity","volume":"92","author":"Hammer","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.biochi.2015.11.009_bib91","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0005-2744(76)90018-8","article-title":"Isolation and characterization of beta-glucosidase from the cytosol of rat kidney cortex","volume":"422","author":"Glew","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib92","doi-asserted-by":"crossref","first-page":"13004","DOI":"10.1016\/S0021-9258(18)42997-3","article-title":"Purification and characterization of a cytosolic broad specificity beta-glucosidase from human liver","volume":"256","author":"Daniels","year":"1981","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib93","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1046\/j.0014-2956.2001.02641.x","article-title":"Functional expression of human liver cytosolic beta-glucosidase in Pichia pastoris. Insights into its role in the metabolism of dietary glucosides","volume":"269","author":"Berrin","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biochi.2015.11.009_bib94","doi-asserted-by":"crossref","first-page":"30889","DOI":"10.1074\/jbc.M700832200","article-title":"Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase","volume":"282","author":"Hayashi","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib95","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.bcmd.2010.07.009","article-title":"The cytosolic beta-glucosidase GBA3 does not influence type 1 Gaucher disease manifestation","volume":"46","author":"Dekker","year":"2011","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib96","doi-asserted-by":"crossref","first-page":"19530","DOI":"10.1074\/jbc.271.32.19530","article-title":"Accumulation of glucosylceramides in multidrug-resistant cancer cells","volume":"271","author":"Lavie","year":"1996","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib97","first-page":"475","article-title":"Glucosylceramide: a marker for multiple-drug resistant cancers","volume":"18","author":"Lucci","year":"1998","journal-title":"Anticancer Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib98","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/S0169-409X(01)00144-2","article-title":"Upregulation of caveolin in multidrug resistant cancer cells: functional implications","volume":"49","author":"Lavie","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.biochi.2015.11.009_bib99","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1074\/jbc.274.2.1140","article-title":"Expression of glucosylceramide synthase, converting ceramide to glucosylceramide, confers adriamycin resistance in human breast cancer cells","volume":"274","author":"Liu","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib100","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1006\/excr.1999.4649","article-title":"Glycosylation of ceramide potentiates cellular resistance to tumor necrosis factor-alpha-induced apoptosis","volume":"252","author":"Liu","year":"1999","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib101","first-page":"415","article-title":"Possible role of ceramide as an indicator of chemoresistance: decrease of the ceramide content via activation of glucosylceramide synthase and sphingomyelin synthase in chemoresistant leukemia","volume":"9","author":"Itoh","year":"2003","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib102","doi-asserted-by":"crossref","first-page":"24901","DOI":"10.1074\/jbc.M100314200","article-title":"Role of ceramide in mediating the inhibition of telomerase activity in A549 human lung adenocarcinoma cells","volume":"276","author":"Ogretmen","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib103","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/B978-0-12-394274-6.00003-0","article-title":"Ceramide glycosylation catalyzed by glucosylceramide synthase and cancer drug resistance","volume":"117","author":"Liu","year":"2013","journal-title":"Adv. Cancer Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib104","doi-asserted-by":"crossref","first-page":"7138","DOI":"10.1074\/jbc.275.10.7138","article-title":"Uncoupling ceramide glycosylation by transfection of glucosylceramide synthase antisense reverses adriamycin resistance","volume":"275","author":"Liu","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib105","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1093\/jnci\/92.11.912","article-title":"Influence of cellular ganglioside depletion on tumor formation","volume":"92","author":"Deng","year":"2000","journal-title":"J.\u00a0Natl. Cancer Inst."},{"key":"10.1016\/j.biochi.2015.11.009_bib106","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0304-3835(03)00459-2","article-title":"N-butyldeoxynojirimycin inhibits murine melanoma cell ganglioside metabolism and delays tumor onset","volume":"201","author":"Guerrera","year":"2003","journal-title":"Cancer Lett."},{"key":"10.1016\/j.biochi.2015.11.009_bib107","first-page":"3654","article-title":"Inhibition of melanoma tumor growth by a novel inhibitor of glucosylceramide synthase","volume":"63","author":"Weiss","year":"2003","journal-title":"Cancer Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib108","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1186\/1476-4598-9-145","article-title":"Glucosylceramide synthase upregulates MDR1 expression in the regulation of cancer drug resistance through cSrc and beta-catenin signaling","volume":"9","author":"Liu","year":"2010","journal-title":"Mol. Cancer"},{"key":"10.1016\/j.biochi.2015.11.009_bib109","doi-asserted-by":"crossref","first-page":"34810","DOI":"10.1074\/jbc.M005142200","article-title":"Glucosylceramide synthase does not attenuate the ceramide pool accumulating during apoptosis induced by CD95 or anti-cancer regimens","volume":"275","author":"Tepper","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib110","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1096\/fj.02-1053fje","article-title":"The absence of functional glucosylceramide synthase does not sensitize melanoma cells for anticancer drugs","volume":"17","author":"Veldman","year":"2003","journal-title":"Faseb J."},{"key":"10.1016\/j.biochi.2015.11.009_bib111","first-page":"425","article-title":"Glucosylceramide synthase, a factor in modulating drug resistance, is overexpressed in metastatic breast carcinoma","volume":"39","author":"Liu","year":"2011","journal-title":"Int. J. Oncol."},{"key":"10.1016\/j.biochi.2015.11.009_bib112","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.urolonc.2010.04.012","article-title":"Up-regulation of glucosylceramide synthase in urinary bladder neoplasms","volume":"30","author":"Sun","year":"2012","journal-title":"Urol. Oncol."},{"key":"10.1016\/j.biochi.2015.11.009_bib113","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1007\/s00432-008-0436-9","article-title":"Prognostic relevance of glucosylceramide synthase (GCS) expression in breast cancer","volume":"135","author":"Ruckhaberle","year":"2009","journal-title":"J.\u00a0Cancer Res. Clin. Oncol."},{"key":"10.1016\/j.biochi.2015.11.009_bib114","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/1746-1596-9-22","article-title":"Expression of glucosylceramide synthase in invasive ductal breast cancer may be correlated with high estrogen receptor status and low HER-2 status","volume":"9","author":"Liu","year":"2014","journal-title":"Diagn Pathol."},{"key":"10.1016\/j.biochi.2015.11.009_bib115","doi-asserted-by":"crossref","first-page":"3071","DOI":"10.3760\/cma.j.issn.0366-6999.20141331","article-title":"Overexpression of glucosylceramide synthase and its significance in the clinical outcome of non-small cell lung cancer","volume":"127","author":"Zhang","year":"2014","journal-title":"Chin. Med. J. Engl."},{"key":"10.1016\/j.biochi.2015.11.009_bib116","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.leukres.2007.07.006","article-title":"Overexpression of glucosylceramide synthase in associated with multidrug resistance of leukemia cells","volume":"32","author":"Xie","year":"2008","journal-title":"Leuk. Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib117","doi-asserted-by":"crossref","first-page":"5730","DOI":"10.1158\/1078-0432.CCR-04-2225","article-title":"Gene signatures of progression and metastasis in renal cell cancer","volume":"11","author":"Jones","year":"2005","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib118","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/0005-2760(95)00217-0","article-title":"Induction of glucosylceramide synthase by synthase inhibitors and ceramide","volume":"1299","author":"Abe","year":"1996","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib119","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0014-5793(00)01696-3","article-title":"Regulation of UDP-glucose: ceramide glucosyltransferase-1 by ceramide","volume":"475","author":"Komori","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2015.11.009_bib120","doi-asserted-by":"crossref","first-page":"2541","DOI":"10.1096\/fj.07-092981","article-title":"A\u00a0role for ceramide in driving cancer cell resistance to doxorubicin","volume":"22","author":"Liu","year":"2008","journal-title":"Faseb J."},{"key":"10.1016\/j.biochi.2015.11.009_bib121","doi-asserted-by":"crossref","first-page":"6271","DOI":"10.1158\/0008-5472.CAN-03-1476","article-title":"Ceramide reduction and transcriptional up-regulation of glucosylceramide synthase through doxorubicin-activated Sp1 in drug-resistant HL-60\/ADR cells","volume":"64","author":"Uchida","year":"2004","journal-title":"Cancer Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib122","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1111\/j.1349-7006.2007.00538.x","article-title":"Mechanism of multidrug recognition by MDR1\/ABCB1","volume":"98","author":"Kimura","year":"2007","journal-title":"Cancer Sci."},{"key":"10.1016\/j.biochi.2015.11.009_bib123","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1016\/j.bbalip.2007.09.005","article-title":"Ceramide and glucosylceramide upregulate expression of the multidrug resistance gene MDR1 in cancer cells","volume":"1771","author":"Gouaze-Andersson","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib124","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1158\/1535-7163.633.3.5","article-title":"Overexpression of glucosylceramide synthase and P-glycoprotein in cancer cells selected for resistance to natural product chemotherapy","volume":"3","author":"Gouaze","year":"2004","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.biochi.2015.11.009_bib125","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1111\/j.1600-0609.1979.tb00419.x","article-title":"Nonsecretory IgD-kappa multiple myeloma in a patient with Gaucher's disease","volume":"22","author":"Benjamin","year":"1979","journal-title":"Scand. J. Haematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib126","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1016\/0002-9343(80)90313-7","article-title":"Gaucher's disease associated with Hodgkin's disease","volume":"68","author":"Bruckstein","year":"1980","journal-title":"Am. J. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib127","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1111\/j.1600-0609.1985.tb02269.x","article-title":"Association of Gaucher's disease and lymphoid malignancy in 2 children","volume":"35","author":"Burstein","year":"1985","journal-title":"Scand. J. Haematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib128","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1002\/path.1711160403","article-title":"Gaucher's disease associated with chronic lymphocytic leukaemia, gout and carcinoma","volume":"116","author":"Chang-Lo","year":"1975","journal-title":"J.\u00a0Pathol."},{"key":"10.1016\/j.biochi.2015.11.009_bib129","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1136\/pgmj.63.744.899","article-title":"Adult Gaucher disease in association with acute leukaemia","volume":"63","author":"Corbett","year":"1987","journal-title":"Postgrad. Med. J."},{"key":"10.1016\/j.biochi.2015.11.009_bib130","doi-asserted-by":"crossref","first-page":"2229","DOI":"10.1001\/archinte.1982.00340250195035","article-title":"Coexistence of Gaucher's disease and multiple myeloma","volume":"142","author":"Garfinkel","year":"1982","journal-title":"Arch. Intern. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib131","first-page":"177","article-title":"The pathology of Gaucher disease","volume":"95","author":"Lee","year":"1982","journal-title":"Prog. Clin. Biol. Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib132","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1002\/ajh.2830290403","article-title":"Polyclonal B-cell lymphocytosis and hypergammaglobulinemia in patients with Gaucher disease","volume":"29","author":"Marti","year":"1988","journal-title":"Am. J. Hematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib133","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/s00277-008-0441-8","article-title":"Immunoglobulin and free light chain abnormalities in Gaucher disease type I: data from an adult cohort of 63 patients and review of the literature","volume":"87","author":"de Fost","year":"2008","journal-title":"Ann. Hematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib134","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.bcmd.2003.10.007","article-title":"Effect of enzyme replacement therapy on gammopathies in Gaucher disease","volume":"32","author":"Brautbar","year":"2004","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib135","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1002\/1097-0142(19930701)72:1<219::AID-CNCR2820720139>3.0.CO;2-Y","article-title":"Increased risk of cancer in patients with Gaucher disease","volume":"72","author":"Shiran","year":"1993","journal-title":"Cancer"},{"key":"10.1016\/j.biochi.2015.11.009_bib136","doi-asserted-by":"crossref","first-page":"4569","DOI":"10.1182\/blood-2004-12-4672","article-title":"Gaucher disease and cancer incidence: a study from the Gaucher registry","volume":"105","author":"Rosenbloom","year":"2005","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2015.11.009_bib137","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.bcmd.2005.03.004","article-title":"Incidence of malignancies among patients with type I Gaucher disease from a single referral clinic","volume":"34","author":"Zimran","year":"2005","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib138","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.bcmd.2005.08.004","article-title":"Increased incidence of cancer in adult Gaucher disease in Western Europe","volume":"36","author":"de Fost","year":"2006","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib139","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1001\/archinte.167.11.1189","article-title":"Risk of malignant disease among 1525 adult male US Veterans with Gaucher disease","volume":"167","author":"Landgren","year":"2007","journal-title":"Arch. Intern. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib140","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1001\/archinternmed.2007.128","article-title":"Prevalence of type 1 Gaucher disease in the United States","volume":"168","author":"Weinreb","year":"2008","journal-title":"Arch. Intern. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib141","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1002\/ajh.21362","article-title":"The underrecognized progressive nature of N370S Gaucher disease and assessment of cancer risk in 403 patients","volume":"84","author":"Taddei","year":"2009","journal-title":"Am. J. Hematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib142","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1111\/bjh.12335","article-title":"Malignancies and monoclonal gammopathy in Gaucher disease; a systematic review of the literature","volume":"161","author":"Arends","year":"2013","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib143","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.bcmd.2010.10.007","article-title":"A\u00a0monozygotic twin pair with highly discordant Gaucher phenotypes","volume":"46","author":"Biegstraaten","year":"2011","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib144","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1023\/B:BOLI.0000042983.60840.f3","article-title":"Gaucher disease: variability in phenotype among siblings","volume":"27","author":"Amato","year":"2004","journal-title":"J.\u00a0Inherit. Metab. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib145","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.ymgme.2004.08.015","article-title":"Gaucher disease: complexity in a \u201csimple\u201d disorder","volume":"83","author":"Sidransky","year":"2004","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.biochi.2015.11.009_bib146","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1002\/ajh.23118","article-title":"Genome-wide association study of N370S homozygous Gaucher disease reveals the candidacy of CLN8 gene as a genetic modifier contributing to extreme phenotypic variation","volume":"87","author":"Zhang","year":"2012","journal-title":"Am. J. Hematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib147","doi-asserted-by":"crossref","first-page":"4731","DOI":"10.1182\/blood-2011-10-386862","article-title":"Phenotype diversity in type 1 Gaucher disease: discovering the genetic basis of Gaucher disease\/hematologic malignancy phenotype by individual genome analysis","volume":"119","author":"Lo","year":"2012","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2015.11.009_bib148","first-page":"388","article-title":"Gaucher's disease: a disease with chronic stimulation of the immune system","volume":"106","author":"Shoenfeld","year":"1982","journal-title":"Arch. Pathol. Lab. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib149","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/s00401-007-0296-4","article-title":"Immune system irregularities in lysosomal storage disorders","volume":"115","author":"Castaneda","year":"2008","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.biochi.2015.11.009_bib150","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1182\/blood-2003-05-1612","article-title":"Marked elevation of the chemokine CCL18\/PARC in Gaucher disease: a novel surrogate marker for assessing therapeutic intervention","volume":"103","author":"Boot","year":"2004","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2015.11.009_bib151","first-page":"205","article-title":"Cytokines in Gaucher's disease","volume":"10","author":"Barak","year":"1999","journal-title":"Eur. Cytokine Netw."},{"key":"10.1016\/j.biochi.2015.11.009_bib152","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1006\/bcmd.1997.0137","article-title":"Elevated levels of M-CSF, sCD14 and IL8 in type 1 Gaucher disease","volume":"23","author":"Hollak","year":"1997","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib153","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/S0925-4439(96)00056-7","article-title":"Plasma tumor necrosis factor-a (TNF-a) levels in Gaucher disease","volume":"1317","author":"Michelakakis","year":"1996","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.11.009_bib154","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1093\/qjmed\/90.1.19","article-title":"Pro-inflammatory cytokines and the pathogenesis of Gaucher's disease: increased release of interleukin-6 and interleukin-10","volume":"90","author":"Allen","year":"1997","journal-title":"QJM"},{"key":"10.1016\/j.biochi.2015.11.009_bib155","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.bcmd.2013.01.001","article-title":"Altered innate function of plasmacytoid dendritic cells restored by enzyme replacement therapy in Gaucher disease","volume":"50","author":"Braudeau","year":"2013","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib156","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1309\/BG5VA8JRDQH1M7HN","article-title":"Gaucher cells demonstrate a distinct macrophage phenotype and resemble alternatively activated macrophages","volume":"122","author":"Boven","year":"2004","journal-title":"Am. J. Clin. Pathol."},{"key":"10.1016\/j.biochi.2015.11.009_bib157","first-page":"149","article-title":"Abnormalities of cellular immunity and natural killer cells in Gaucher's disease","volume":"23","author":"Burstein","year":"1987","journal-title":"J.\u00a0Clin. Lab. Immunol."},{"key":"10.1016\/j.biochi.2015.11.009_bib158","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.bcmd.2005.12.029","article-title":"Dendritic cells in patients with type I Gaucher disease are decreased in number but functionally normal","volume":"36","author":"Micheva","year":"2006","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib159","doi-asserted-by":"crossref","first-page":"13433","DOI":"10.1073\/pnas.1415357111","article-title":"Activation of iNKT cells by a distinct constituent of the endogenous glucosylceramide fraction","volume":"111","author":"Brennan","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib160","doi-asserted-by":"crossref","first-page":"1202","DOI":"10.1038\/ni.2143","article-title":"Invariant natural killer T cells recognize lipid self antigen induced by microbial danger signals","volume":"12","author":"Brennan","year":"2011","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.biochi.2015.11.009_bib161","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1182\/blood-2014-09-600270","article-title":"Type II NKT-TFH cells against Gaucher lipids regulate B-cell immunity and inflammation","volume":"125","author":"Nair","year":"2015","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2015.11.009_bib162","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1111\/j.1365-2141.2005.05503.x","article-title":"Evidence for a link between sphingolipid metabolism and expression of CD1d and MHC-class II: monocytes from Gaucher disease patients as a model","volume":"129","author":"Balreira","year":"2005","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.biochi.2015.11.009_bib163","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/j.imbio.2009.07.002","article-title":"Uncoupling between CD1d upregulation induced by retinoic acid and conduritol-B-epoxide and iNKT cell responsiveness","volume":"215","author":"Balreira","year":"2010","journal-title":"Immunobiology"},{"key":"10.1016\/j.biochi.2015.11.009_bib164","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1172\/JCI0214530","article-title":"Systemic inflammation in glucocerebrosidase-deficient mice with minimal glucosylceramide storage","volume":"109","author":"Mizukami","year":"2002","journal-title":"J.\u00a0Clin. Investig."},{"key":"10.1016\/j.biochi.2015.11.009_bib165","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/j.ymgme.2012.04.020","article-title":"Immunological cell type characterization and Th1-Th17 cytokine production in a mouse model of Gaucher disease","volume":"106","author":"Pandey","year":"2012","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.biochi.2015.11.009_bib166","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/1471-2164-12-20","article-title":"Global gene expression profile progression in Gaucher disease mouse models","volume":"12","author":"Xu","year":"2011","journal-title":"BMC Genomics"},{"key":"10.1016\/j.biochi.2015.11.009_bib167","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.bcmd.2009.03.006","article-title":"Impaired IL-10 transcription and release in animal models of Gaucher disease macrophages","volume":"43","author":"Kacher","year":"2009","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.biochi.2015.11.009_bib168","doi-asserted-by":"crossref","first-page":"10018","DOI":"10.1073\/pnas.1200941109","article-title":"Gaucher disease gene GBA functions in immune regulation","volume":"109","author":"Liu","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib169","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1002\/path.4227","article-title":"B\u00a0cell lymphoma and myeloma in murine Gaucher's disease","volume":"231","author":"Pavlova","year":"2013","journal-title":"J.\u00a0Pathol."},{"key":"10.1016\/j.biochi.2015.11.009_bib170","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1002\/path.4452","article-title":"Inhibition of UDP-glucosylceramide synthase in mice prevents Gaucher disease-associated B-cell malignancy","volume":"235","author":"Pavlova","year":"2015","journal-title":"J.\u00a0Pathol."},{"key":"10.1016\/j.biochi.2015.11.009_bib171","doi-asserted-by":"crossref","first-page":"2903","DOI":"10.1172\/JCI117997","article-title":"Glucosylceramides stimulate murine epidermal hyperproliferation","volume":"95","author":"Marsh","year":"1995","journal-title":"J.\u00a0Clin. Investig."},{"key":"10.1016\/j.biochi.2015.11.009_bib172","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1007\/BF02535529","article-title":"Stimulation of liver growth and DNA synthesis by glucosylceramide","volume":"23","author":"Datta","year":"1988","journal-title":"Lipids"},{"key":"10.1016\/j.biochi.2015.11.009_bib173","doi-asserted-by":"crossref","first-page":"22968","DOI":"10.1016\/S0021-9258(18)54449-5","article-title":"Modulation of renal epithelial cell growth by glucosylceramide. Association with protein kinase C, sphingosine, and diacylglycerol","volume":"266","author":"Shayman","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib174","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1038\/nm.2171","article-title":"Inhibition of glucosylceramide accumulation results in effective blockade of polycystic kidney disease in mouse models","volume":"16","author":"Natoli","year":"2010","journal-title":"Nat. Med."},{"key":"10.1016\/j.biochi.2015.11.009_bib175","doi-asserted-by":"crossref","first-page":"1334","DOI":"10.1016\/S0022-2275(20)39163-X","article-title":"Role of lactosylceramide and MAP kinase in the proliferation of proximal tubular cells in human polycystic kidney disease","volume":"37","author":"Chatterjee","year":"1996","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.biochi.2015.11.009_bib176","doi-asserted-by":"crossref","first-page":"7461","DOI":"10.1073\/pnas.0902368106","article-title":"Specific glycosphingolipids mediate epithelial-to-mesenchymal transition of human and mouse epithelial cell lines","volume":"106","author":"Guan","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2015.11.009_bib177","doi-asserted-by":"crossref","first-page":"15001","DOI":"10.1038\/cddiscovery.2015.1","article-title":"Sphingolipids modulate the epithelial-mesenchymal transition in cancer","volume":"1","author":"Levade","year":"2015","journal-title":"Cell Death Discov."},{"key":"10.1016\/j.biochi.2015.11.009_bib178","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1002\/ijc.1449","article-title":"Elevation of glucosylceramide in multidrug-resistant cancer cells and accumulation in cytoplasmic droplets","volume":"94","author":"Morjani","year":"2001","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.biochi.2015.11.009_bib179","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/j.ccr.2007.04.011","article-title":"Regulators of mitotic arrest and ceramide metabolism are determinants of sensitivity to paclitaxel and other chemotherapeutic drugs","volume":"11","author":"Swanton","year":"2007","journal-title":"Cancer Cell"},{"key":"10.1016\/j.biochi.2015.11.009_bib180","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.4161\/cbt.10.11.13438","article-title":"Inhibition of NADPH oxidase by glucosylceramide confers chemoresistance","volume":"10","author":"Barth","year":"2010","journal-title":"Cancer Biol. Ther."},{"key":"10.1016\/j.biochi.2015.11.009_bib181","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1615\/CritRevOncog.2013005814","article-title":"Gaucher's disease and cancer: a sphingolipid perspective","volume":"18","author":"Barth","year":"2013","journal-title":"Crit. Rev. Oncog."},{"key":"10.1016\/j.biochi.2015.11.009_bib182","doi-asserted-by":"crossref","first-page":"12972","DOI":"10.1074\/jbc.M802790200","article-title":"Involvement of acid beta-glucosidase 1 in the salvage pathway of ceramide formation","volume":"284","author":"Kitatani","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib183","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1172\/JCI0214146","article-title":"Protein kinase Cdelta amplifies ceramide formation via mitochondrial signaling in prostate cancer cells","volume":"109","author":"Sumitomo","year":"2002","journal-title":"J.\u00a0Clin. Investig."},{"key":"10.1016\/j.biochi.2015.11.009_bib184","doi-asserted-by":"crossref","first-page":"12979","DOI":"10.1074\/jbc.M809500200","article-title":"Acid beta-glucosidase 1 counteracts p38delta-dependent induction of interleukin-6: possible role for ceramide as an anti-inflammatory lipid","volume":"284","author":"Kitatani","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.11.009_bib185","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.pneurobio.2014.12.001","article-title":"Gaucher-related synucleinopathies: the examination of sporadic neurodegeneration from a rare (disease) angle","volume":"125","author":"Sardi","year":"2015","journal-title":"Prog. Neurobiol."},{"key":"10.1016\/j.biochi.2015.11.009_bib186","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1038\/nrc3150","article-title":"Parkinson's disease and cancer: two wars, one front","volume":"11","author":"Devine","year":"2011","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.biochi.2015.11.009_bib187","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1212\/WNL.0b013e31821e554e","article-title":"Meta-analysis of the relationship between Parkinson disease and melanoma","volume":"76","author":"Liu","year":"2011","journal-title":"Neurology"},{"key":"10.1016\/j.biochi.2015.11.009_bib188","doi-asserted-by":"crossref","first-page":"e10481","DOI":"10.1371\/journal.pone.0010481","article-title":"Parkinson's disease-related protein, alpha-synuclein, in malignant melanoma","volume":"5","author":"Matsuo","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2015.11.009_bib189","doi-asserted-by":"crossref","first-page":"e19622","DOI":"10.1371\/journal.pone.0019622","article-title":"alpha-Synuclein expression selectively affects tumorigenesis in mice modeling Parkinson's disease","volume":"6","author":"Israeli","year":"2011","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.biochi.2015.11.009_bib190","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1096\/fj.12-215152","article-title":"The nonlysosomal beta-glucosidase GBA2 promotes endoplasmic reticulum stress and impairs tumorigenicity of human melanoma cells","volume":"27","author":"Sorli","year":"2013","journal-title":"Faseb J."},{"key":"10.1016\/j.biochi.2015.11.009_bib191","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1007\/s001090000131","article-title":"Molecular cloning and expression of a novel klotho-related protein","volume":"78","author":"Yahata","year":"2000","journal-title":"J.\u00a0Mol. Med. Berl."},{"key":"10.1016\/j.biochi.2015.11.009_bib192","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1053\/j.gastro.2010.04.008","article-title":"Gene expression profiling of metaplastic lineages identifies CDH17 as a prognostic marker in early stage gastric cancer","volume":"139","author":"Lee","year":"2010","journal-title":"Gastroenterology"}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908415003569?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908415003569?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,12]],"date-time":"2024-06-12T12:01:23Z","timestamp":1718193683000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908415003569"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,6]]},"references-count":192,"alternative-id":["S0300908415003569"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2015.11.009","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2016,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Glucosylceramidases and malignancies in mammals","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2015.11.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2015 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights reserved.","name":"copyright","label":"Copyright"}]}}