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Chem."},{"key":"10.1194\/jlr.M073510_bib69","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/0925-4439(94)90021-3","article-title":"Free sphingoid bases in tissues from patients with type C Niemann-Pick disease and other lysosomal storage disorders","volume":"1226","author":"Rodriguez-Lafrasse","year":"1994","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.M073510_bib70","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/0005-2760(92)90236-O","article-title":"Type C Niemann-Pick disease: a murine model of the lysosomal cholesterol lipidosis accumulates sphingosine and sphinganine in liver","volume":"1127","author":"Goldin","year":"1992","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.M073510_bib71","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/S0014-5793(04)00033-X","article-title":"Interactions of acid sphingomyelinase and lipid bilayers in the presence of the tricyclic antidepressant desipramine","volume":"559","author":"K\u00f6lzer","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1194\/jlr.M073510_bib72","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1111\/j.1471-4159.1982.tb07950.x","article-title":"Accumulation of glucosylceramide and glucosylsphingosine (psychosine) in cerebrum and cerebellum in infantile and juvenile Gaucher disease","volume":"39","author":"Nilsson","year":"1982","journal-title":"J. Neurochem."},{"key":"10.1194\/jlr.M073510_bib73","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/978-1-4684-7735-1_8","article-title":"Chemical pathology of Krabbe disease: the occurrence of psychosine and other neutral sphingoglycolipids","volume":"68","author":"Vanier","year":"1976","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1194\/jlr.M073510_bib74","doi-asserted-by":"crossref","first-page":"2812","DOI":"10.1073\/pnas.0712309105","article-title":"Elevated globotriaosylsphingosine is a hallmark of Fabry disease","volume":"105","author":"Aerts","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.M073510_bib75","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1023\/A:1022501702403","article-title":"Sphingosylphos\u00adphorylcholine in Niemann-Pick disease brain: accumulation in type A but not in type B","volume":"24","author":"Rodriguez-Lafrasse","year":"1999","journal-title":"Neurochem. Res."},{"key":"10.1194\/jlr.M073510_bib76","doi-asserted-by":"crossref","first-page":"6534","DOI":"10.1016\/S0021-9258(18)68674-0","article-title":"1,2-Diacylglycerols, but not phorbol esters, activate a potential inhibitory pathway for protein kinase C in GH3 pituitary cells. Evidence for involvement of a sphingomyelinase","volume":"263","author":"Kolesnick","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M073510_bib77","doi-asserted-by":"crossref","first-page":"16759","DOI":"10.1016\/S0021-9258(18)45447-6","article-title":"1,2-Diacylglycerols but not phorbol esters stimulate sphingomyelin hydrolysis in GH3 pituitary cells","volume":"262","author":"Kolesnick","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M073510_bib78","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/S0006-3495(99)77201-2","article-title":"Ceramides in phospholipid membranes: effects on bilayer stability and transition to nonlamellar phases","volume":"76","author":"Veiga","year":"1999","journal-title":"Biophys. J."},{"key":"10.1194\/jlr.M073510_bib79","doi-asserted-by":"crossref","first-page":"7092","DOI":"10.1021\/bi00346a011","article-title":"Diacylglycerols, lysolecithin, or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines","volume":"24","author":"Epand","year":"1985","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.M073510_bib80","doi-asserted-by":"crossref","first-page":"2630","DOI":"10.1016\/S0006-3495(97)78906-9","article-title":"Morphological changes induced by phospholipase C and by sphingomyelinase on large unilamellar vesicles: a cryo-transmission electron microscopy study of liposome fusion","volume":"72","author":"Bas\u00e1\u00f1ez","year":"1997","journal-title":"Biophys. J."},{"key":"10.1194\/jlr.M073510_bib81","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0014-5793(95)00631-I","article-title":"Topological properties of two cubic phases of a phospholipid:cholesterol:diacylglycerol aqueous system and their possible implications in the phospholipase C-induced liposome fusion","volume":"368","author":"Nieva","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1194\/jlr.M073510_bib82","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":"10.1194\/jlr.M073510_bib83","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/0014-5793(94)00659-8","article-title":"Saposin-C induces pH-dependent destabilization and fusion of phosphatidylserine-containing vesicles","volume":"349","author":"Vaccaro","year":"1994","journal-title":"FEBS Lett."},{"key":"10.1194\/jlr.M073510_bib84","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1038\/ni1035","article-title":"Saposin C is required for lipid presentation by human CD1b","volume":"5","author":"Winau","year":"2004","journal-title":"Nat. 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