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Volumn 21, Issue , 2005, Pages 81-103

Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids

Author keywords

Glycosphingolipids; GM2 activator; Lysosomes; Saposins; Sphingolipids

Indexed keywords

ANIONIC LYSOSOMAL LIPID; BIS(MONOACYLGLYCERO)PHOSPHATE; CD1 ANTIGEN; CERAMIDE; CHOLESTEROL; GALACTOSYLCERAMIDE; GANGLIOSIDE GM2; GLYCOSPHINGOLIPID; HYDROLASE; LIPID; LIPID ANTIGEN; LIPID BINDING PROTEIN; LIPID TRANSFER PROTEIN; LYSOPHOSPHATIDIC ACID; PROSAPOSIN; PROTEIN SAP A; PROTEIN SAP B; PROTEIN SAP C; PROTEIN SAP D; SPHINGOLIPID; SPHINGOLIPID ACTIVATOR PROTEIN; SPHINGOLIPID ACTIVATOR PROTEIN 2; SPHINGOMYELIN; UNCLASSIFIED DRUG;

EID: 25444443570     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.21.122303.120013     Document Type: Review
Times cited : (375)

References (121)
  • 2
    • 0029953488 scopus 로고    scopus 로고
    • Transacylase and phospholipases in the synthesis of bis(monoacylglycero) phosphate
    • Amidon B, Brown A, Waite M. 1996. Transacylase and phospholipases in the synthesis of bis(monoacylglycero)phosphate. Biochemistry 35:13995-4002
    • (1996) Biochemistry , vol.35 , pp. 13995-14002
    • Amidon, B.1    Brown, A.2    Waite, M.3
  • 3
    • 20144372085 scopus 로고    scopus 로고
    • The cellular pathway of CD1c in immature and maturing dendritic cells
    • Anǵnieux C, Fraisier V, Maître B, Racine V, van der Wel N, et al. 2005. The cellular pathway of CD1c in immature and maturing dendritic cells. Traffic 6:286-302
    • (2005) Traffic , vol.6 , pp. 286-302
    • Anǵnieux, C.1    Fraisier, V.2    Maître, B.3    Racine, V.4    Van Der Wel, N.5
  • 4
    • 0019513677 scopus 로고
    • Mechanism of activation of glucocerebrosidase by co-β-glucosidase (glucosidase activator protein)
    • Berent SL, Radin NS. 1981. Mechanism of activation of glucocerebrosidase by co-β-glucosidase (glucosidase activator protein). Biochim. Biophys. Acta 664:572-82
    • (1981) Biochim. Biophys. Acta , vol.664 , pp. 572-582
    • Berent, S.L.1    Radin, N.S.2
  • 5
    • 0029070822 scopus 로고
    • Purification, characterization, and biosynthesis of human acid ceramidase
    • Bernardo K, Hurwitz R, Zenk T, Desnick RJ, Ferlinz K, et al. 1995. Purification, characterization, and biosynthesis of human acid ceramidase. J. Biol. Chem. 70:11098-102
    • (1995) J. Biol. Chem. , vol.70 , pp. 11098-11102
    • Bernardo, K.1    Hurwitz, R.2    Zenk, T.3    Desnick, R.J.4    Ferlinz, K.5
  • 6
    • 0027186175 scopus 로고
    • Prosaposin deficiency: Further characterization of the sphingolipid activator protein-deficient sibs. Multiple glycolipid elevations (including lactosylceramidosis), partial enzyme deficiencies and ultrastructure of the skin in this generalized sphingolipid storage disease
    • Bradova V, Smid F, Ulrich-Bott B, Roggendorf W, Paton BC, Harzer K. 1993. Prosaposin deficiency: further characterization of the sphingolipid activator protein-deficient sibs. Multiple glycolipid elevations (including lactosylceramidosis), partial enzyme deficiencies and ultrastructure of the skin in this generalized sphingolipid storage disease. Hum. Genet. 92:143-52
    • (1993) Hum. Genet. , vol.92 , pp. 143-152
    • Bradova, V.1    Smid, F.2    Ulrich-Bott, B.3    Roggendorf, W.4    Paton, B.C.5    Harzer, K.6
  • 8
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- And cholesterol-rich membrane rafts
    • Brown DA, London E. 2000. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275:17221-24
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 9
    • 0343052042 scopus 로고    scopus 로고
    • Accumulation of sphingolipids in SAP-precursor (prosaposin)-deficient fibroblasts occurs as intralysosomal membrane structures and can be completely reversed by treatment with human SAP-precursor
    • Burkhardt JK, Hüttler S, Klein A, Möbius W, Habermann A, et al. 1997. Accumulation of sphingolipids in SAP-precursor (prosaposin)-deficient fibroblasts occurs as intralysosomal membrane structures and can be completely reversed by treatment with human SAP-precursor. Eur. J. Cell Biol. 73:10-18
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 10-18
    • Burkhardt, J.K.1    Hüttler, S.2    Klein, A.3    Möbius, W.4    Habermann, A.5
  • 10
    • 0030863352 scopus 로고    scopus 로고
    • Niemann-Pickl disease gene: Homology to mediators of cholesterol homeostasis
    • Carstea ED, Morris JA, Coleman KG, Loftus SK, Zhang D, et al. 1997. Niemann-Pickl disease gene: homology to mediators of cholesterol homeostasis. Science 277:228-31
    • (1997) Science , vol.277 , pp. 228-231
    • Carstea, E.D.1    Morris, J.A.2    Coleman, K.G.3    Loftus, S.K.4    Zhang, D.5
  • 11
    • 0023886858 scopus 로고
    • The biological role of dolichol
    • Chojnacki T, Dallner, G. 1988. The biological role of dolichol. Biochem. J. 251:1-9
    • (1988) Biochem. J. , vol.251 , pp. 1-9
    • Chojnacki, T.1    Dallner, G.2
  • 12
    • 0022782844 scopus 로고
    • Immunochemical characterization of two activator proteins stimulating enzymic sphingomyelin degradation in vitro. Absence of one of them in a human Gaucher disease variant
    • Christomanou H, Aignesberger A, Linke RP. 1986. Immunochemical characterization of two activator proteins stimulating enzymic sphingomyelin degradation in vitro. Absence of one of them in a human Gaucher disease variant. Biol. Chem. Hoppe-Seyler 367:879-90
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 879-890
    • Christomanou, H.1    Aignesberger, A.2    Linke, R.P.3
  • 14
    • 0032557156 scopus 로고    scopus 로고
    • Physiological properties and functions of intracellular fatty acid-binding proteins
    • Coe NR, Bernlohr DA. 1998. Physiological properties and functions of intracellular fatty acid-binding proteins. Biochim. Biophys. Acta 1391:287-306
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 287-306
    • Coe, N.R.1    Bernlohr, D.A.2
  • 15
    • 0020321725 scopus 로고
    • Complexing of glycolipids and their transfer between membranes by the activator protein for degradation of lysosomal ganglioside GM2
    • Conzelmann E, Burg J, Stephan G, Sandhoff K. 1982. Complexing of glycolipids and their transfer between membranes by the activator protein for degradation of lysosomal ganglioside GM2. Eur. J. Biochem. 123:455-64
    • (1982) Eur. J. Biochem. , vol.123 , pp. 455-464
    • Conzelmann, E.1    Burg, J.2    Stephan, G.3    Sandhoff, K.4
  • 16
    • 2642688117 scopus 로고
    • AB variant of infantile GM2 gangliosidosis: Deficiency of a factor necessary for stimulation of hexosaminidase A-catalyzed degradation of ganglioside GM2 and glycolipid GA2
    • Conzelmann E, Sandhoff K. 1978. AB variant of infantile GM2 gangliosidosis: deficiency of a factor necessary for stimulation of hexosaminidase A-catalyzed degradation of ganglioside GM2 and glycolipid GA2. Proc. Natl. Acad. Sci. USA 75:3979-83
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3979-3983
    • Conzelmann, E.1    Sandhoff, K.2
  • 17
    • 0018567163 scopus 로고
    • Purification and characterization of an activator protein for the degradation of glycolipids GM2 and GA2 by hexosaminidase A
    • Conzelmann E, Sandhoff K. 1979. Purification and characterization of an activator protein for the degradation of glycolipids GM2 and GA2 by hexosaminidase A. Hoppe Seylers Z. Physiol. Chem. 360:1837-49
    • (1979) Hoppe Seylers Z. Physiol. Chem. , vol.360 , pp. 1837-1849
    • Conzelmann, E.1    Sandhoff, K.2
  • 18
    • 0034704244 scopus 로고    scopus 로고
    • Transmembrane molecular pump activity of Niemann-Pick C1 protein
    • Davies JP, Chen FW, Ioannou YA. 2000. Transmembrane molecular pump activity of Niemann-Pick C1 protein. Science 290:2295-98
    • (2000) Science , vol.290 , pp. 2295-2298
    • Davies, J.P.1    Chen, F.W.2    Ioannou, Y.A.3
  • 19
    • 0347625853 scopus 로고    scopus 로고
    • Solution structure of human saposin C: PH-dependent interaction with phospholipid vesicles
    • de Alba E, Weiler S, Tjandra, N. 2003. Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles. Biochemistry 42:14729-40
    • (2003) Biochemistry , vol.42 , pp. 14729-14740
    • Alba, E.1    Weiler, S.2    Tjandra, N.3
  • 20
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: Emerging functions for lysosomal membrane proteins
    • Eskelinen E-L, Tanaka Y, Saftig P. 2003. At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol. 13:137-45
    • (2003) Trends Cell Biol , vol.13 , pp. 137-145
    • Eskelinen, E.-L.1    Tanaka, Y.2    Saftig, P.3
  • 21
    • 0025824346 scopus 로고
    • Human acid β-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites
    • Fabbro D, Grabowski GA. 1991. Human acid β-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites. J. Biol. Chem. 266:15021-27
    • (1991) J. Biol. Chem. , vol.266 , pp. 15021-15027
    • Fabbro, D.1    Grabowski, G.A.2
  • 22
    • 0017599450 scopus 로고
    • The activator of cerebroside sulphatase. Binding studies with enzyme and substrate demonstrating the detergent function of the activator protein
    • Fischer G, Jatzkewitz H. 1977. The activator of cerebroside sulphatase. Binding studies with enzyme and substrate demonstrating the detergent function of the activator protein. Biochim. Biophys. Acta 481:561-72
    • (1977) Biochim. Biophys. Acta , vol.481 , pp. 561-572
    • Fischer, G.1    Jatzkewitz, H.2
  • 23
    • 0037418188 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease
    • Friedland N, Liou HL, Lobel P, Stock AM. 2003. Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease. Proc. Natl. Acad. Sci. USA 100:2512-17
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2512-2517
    • Friedland, N.1    Liou, H.L.2    Lobel, P.3    Stock, A.M.4
  • 24
    • 0023947493 scopus 로고
    • The precursor of sulfatide activator protein is processed to three different proteins
    • Fürst W, Machleidt W, Sandhoff K. 1988. The precursor of sulfatide activator protein is processed to three different proteins. Biol. Chem. Hoppe Seyler 369:317-28
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 317-328
    • Fürst, W.1    Machleidt, W.2    Sandhoff, K.3
  • 25
    • 0026747197 scopus 로고
    • Activator proteins and topology of lysosomal sphingolipid catabolism
    • Fürst W, Sandhoff K. 1992. Activator proteins and topology of lysosomal sphingolipid catabolism. Biochim. Biophys. Acta 1126:1-16
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 1-16
    • Fürst, W.1    Sandhoff, K.2
  • 26
    • 0029982572 scopus 로고    scopus 로고
    • Targeted disruption of the mouse sphingolipid activator protein gene: A complex phenotype, including severe leukodystrophy and wide-spread storage of multiple sphingolipids
    • Fujita N, Suzuki K, Vanier MT, Popko B, Maeda N, et al. 1996. Targeted disruption of the mouse sphingolipid activator protein gene: a complex phenotype, including severe leukodystrophy and wide-spread storage of multiple sphingolipids. Hum. Mol. Genet. 5: 711-25
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 711-725
    • Fujita, N.1    Suzuki, K.2    Vanier, M.T.3    Popko, B.4    Maeda, N.5
  • 28
    • 0000223691 scopus 로고    scopus 로고
    • Interaction of the GM2-activator protein with phospholipid-ganglioside bilayer membranes and with monolayers at the air-water interface
    • Giehl A, Lemm T, Bartelsen O, Sandhoff K, Blume A. 1999. Interaction of the GM2-activator protein with phospholipid-ganglioside bilayer membranes and with monolayers at the air-water interface. Eur. J. Biochem. 261:650-58
    • (1999) Eur. J. Biochem. , vol.261 , pp. 650-658
    • Giehl, A.1    Lemm, T.2    Bartelsen, O.3    Sandhoff, K.4    Blume, A.5
  • 29
    • 0037201939 scopus 로고    scopus 로고
    • Sphingomyelinases: Enzymology and membrane activity
    • Goni FM, Alonso A. 2002. Sphingomyelinases: enzymology and membrane activity. FEBS Lett. 531:38-46
    • (2002) FEBS Lett , vol.531 , pp. 38-46
    • Goni, F.M.1    Alonso, A.2
  • 30
    • 0042026495 scopus 로고    scopus 로고
    • Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers
    • Gutsmann T, Riekens B, Bruhn H, Wiese A, Seydel U, Leippe M. 2003. Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers. Biochemistry 42:9804-12
    • (2003) Biochemistry , vol.42 , pp. 9804-9812
    • Gutsmann, T.1    Riekens, B.2    Bruhn, H.3    Wiese, A.4    Seydel, U.5    Leippe, M.6
  • 31
    • 0347611095 scopus 로고    scopus 로고
    • Molecular machinery for non-vesicular trafficking of ceramide
    • Hanada K, Kumagai K, Yasuda S, Miura Y, Kawano M, et al. 2003. Molecular machinery for non-vesicular trafficking of ceramide. Nature 426:803-9
    • (2003) Nature , vol.426 , pp. 803-809
    • Hanada, K.1    Kumagai, K.2    Yasuda, S.3    Miura, Y.4    Kawano, M.5
  • 32
    • 0024420051 scopus 로고
    • Sphingolipid activator protein (SAP) deficiency in a 16-week old atypical Gaucher disease patient and his fetal sibling; biochemical signs of combined sphingolipidosis
    • Harzer K, Paton BC, Poulos A. 1989. Sphingolipid activator protein (SAP) deficiency in a 16-week old atypical Gaucher disease patient and his fetal sibling; biochemical signs of combined sphingolipidosis. Eur. J. Pediatr. 149:31-39
    • (1989) Eur. J. Pediatr. , vol.149 , pp. 31-39
    • Harzer, K.1    Paton, B.C.2    Poulos, A.3
  • 34
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H. 2002. Triton promotes domain formation in lipid raft mixtures. Biophys. J. 83:2693-701
    • (2002) Biophys. J. , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 35
    • 0038730762 scopus 로고    scopus 로고
    • The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton
    • Heerklotz H, Szadkowska H, Anderson T, Seelig J. 2003. The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton. J. Mol. Biol. 329:793-99
    • (2003) J. Mol. Biol. , vol.329 , pp. 793-799
    • Heerklotz, H.1    Szadkowska, H.2    Anderson, T.3    Seelig, J.4
  • 38
    • 0032541422 scopus 로고    scopus 로고
    • Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP)
    • Hiesberger T, Hüttler S, Rohlmann A, Schneider W, Sandhoff K, Herz J. 1998. Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP). EMBO J. 17:4617-25
    • (1998) EMBO J. , vol.17 , pp. 4617-4625
    • Hiesberger, T.1    Hüttler, S.2    Rohlmann, A.3    Schneider, W.4    Sandhoff, K.5    Herz, J.6
  • 39
    • 0015154711 scopus 로고
    • Gaucher's disease: Deficiency of 'acid' β-glucosidase and reconstitution of enzyme activity in vitro
    • Ho MW, O'Brien JS. 1971. Gaucher's disease: deficiency of 'acid' β-glucosidase and reconstitution of enzyme activity in vitro. Proc. Natl. Acad. Sci. USA 68:2810-13
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2810-2813
    • Ho, M.W.1    O'Brien, J.S.2
  • 40
    • 0025281993 scopus 로고
    • Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum
    • Hopkins CR, Gibson A, Shipman M, Miller K. 1990. Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum. Nature 346:335-39
    • (1990) Nature , vol.346 , pp. 335-339
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Miller, K.4
  • 41
    • 1142263116 scopus 로고    scopus 로고
    • Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells
    • Kang SJ, Cresswell P. 2004. Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells. Nature Immunol. 5:175-81
    • (2004) Nature Immunol , vol.5 , pp. 175-181
    • Kang, S.J.1    Cresswell, P.2
  • 42
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann DJ, Babst M, Emr SD. 2001. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106:145-55
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 44
    • 0033145510 scopus 로고    scopus 로고
    • Late endosomal membranes rich in lysobisphosphatidic acid regulate cholesterol transport
    • Kobayashi T, Beuchat M-H, Lindsay M, Frias S, Palmiter RD. 1999. Late endosomal membranes rich in lysobisphosphatidic acid regulate cholesterol transport. Nature Cell Biol. 1:113-18
    • (1999) Nature Cell Biol , vol.1 , pp. 113-118
    • Kobayashi, T.1    Beuchat, M.-H.2    Lindsay, M.3    Frias, S.4    Palmiter, R.D.5
  • 45
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi T, Stang E, Fang KS, de Moerloose P, Parton RG, Gruenberg J. 1998. A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 392:193-97
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    De Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 46
    • 0037135608 scopus 로고    scopus 로고
    • Minireview: Combinatorial ganglioside biosynthesis
    • Kolter T, Proia RL, Sandhoff K. 2002. Minireview: combinatorial ganglioside biosynthesis. J. Biol. Chem. 277:25859-62
    • (2002) J. Biol. Chem. , vol.277 , pp. 25859-25862
    • Kolter, T.1    Proia, R.L.2    Sandhoff, K.3
  • 47
    • 0031973892 scopus 로고    scopus 로고
    • Recent advances in the biochemistry of sphingolipidoses
    • Kolter T, Sandhoff K. 1998. Recent advances in the biochemistry of sphingolipidoses. Brain Pathol. 8:79-100
    • (1998) Brain Pathol , vol.8 , pp. 79-100
    • Kolter, T.1    Sandhoff, K.2
  • 48
    • 0033152727 scopus 로고    scopus 로고
    • Sphingolipids-their metabolic pathways and the pathobiochemistry of neurodegenerative diseases
    • Kolter T, Sandhoff K. 1999. Sphingolipids-their metabolic pathways and the pathobiochemistry of neurodegenerative diseases. Angew. Chem. Int. Ed. 38:1532-68
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1532-1568
    • Kolter, T.1    Sandhoff, K.2
  • 50
    • 0345732689 scopus 로고    scopus 로고
    • The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin
    • Lefrancois S, Zeng J, Hassan AJ, Canuel M, Morales CR. 2003. The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin. EMBO J. 22:6430-37
    • (2003) EMBO J , vol.22 , pp. 6430-6437
    • Lefrancois, S.1    Zeng, J.2    Hassan, A.J.3    Canuel, M.4    Morales, C.R.5
  • 51
    • 0021946347 scopus 로고
    • Activator protein required for the enzymatic hydrolysis of cerebroside sulfate. Deficiency in urine of patients affected with cerebroside sulfatase activator deficiency and identity with activators for the enzymatic hydrolysis of GM1 ganglioside and globotriaosylceramide
    • Li SC, Kihara H, Serizawa S, Li YT, Fluharty AL, Mayes JS, Shapiro LJ. 1985. Activator protein required for the enzymatic hydrolysis of cerebroside sulfate. Deficiency in urine of patients affected with cerebroside sulfatase activator deficiency and identity with activators for the enzymatic hydrolysis of GM1 ganglioside and globotriaosylceramide. J. Biol. Chem. 260:1867-71
    • (1985) J. Biol. Chem. , vol.260 , pp. 1867-1871
    • Li, S.C.1    Kihara, H.2    Serizawa, S.3    Li, Y.T.4    Fluharty, A.L.5    Mayes, J.S.6    Shapiro, L.J.7
  • 52
    • 0023919106 scopus 로고
    • Characterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipids
    • Li SC, Sonnino S, Tettamanti G, Li YT. 1988. Characterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipids. J. Biol. Chem. 263:6588-91
    • (1988) J. Biol. Chem. , vol.263 , pp. 6588-6591
    • Li, S.C.1    Sonnino, S.2    Tettamanti, G.3    Li, Y.T.4
  • 54
    • 0035077616 scopus 로고    scopus 로고
    • Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins
    • Linke T, Wilkening G, Lansmann S, Moczall H, Bartelsen O, et al. 2001a. Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins. Biol. Chem. 382:283-90
    • (2001) Biol. Chem. , vol.382 , pp. 283-290
    • Linke, T.1    Wilkening, G.2    Lansmann, S.3    Moczall, H.4    Bartelsen, O.5
  • 55
    • 0035937146 scopus 로고    scopus 로고
    • Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins
    • Linke T, Wilkening G, Sadeghlar F, Mozcall H, Bernardo K, et al. 2001b. Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins. J. Biol. Chem. 276:5760-68
    • (2001) J. Biol. Chem. , vol.276 , pp. 5760-5768
    • Linke, T.1    Wilkening, G.2    Sadeghlar, F.3    Mozcall, H.4    Bernardo, K.5
  • 56
    • 0034639928 scopus 로고    scopus 로고
    • Alleviation of neuronal ganglioside storage does not improve the clinical course of the Niemann-Pick C disease mouse
    • Liu Y, Wu Y-P, Wada R, Neufeld EB, Mullin KA, et al. 2000. Alleviation of neuronal ganglioside storage does not improve the clinical course of the Niemann-Pick C disease mouse. Hum. Mol. Genet. 9:1087-92
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1087-1092
    • Liu, Y.1    Wu, Y.-P.2    Wada, R.3    Neufeld, E.B.4    Mullin, K.A.5
  • 57
    • 1642293929 scopus 로고    scopus 로고
    • Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): Implications for lipid raft structure and function
    • London M, London E. 2004. Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): implications for lipid raft structure and function. J. Biol. Chem. 279:9997-10004
    • (2004) J. Biol. Chem. , vol.279 , pp. 9997-10004
    • London, M.1    London, E.2
  • 58
    • 0036694756 scopus 로고    scopus 로고
    • Biochemical and structural information transduction at the mesoscopic level in biointerfaces containing sphingolipids
    • Maggio B, Fanani ML, Oliveira RG. 2002. Biochemical and structural information transduction at the mesoscopic level in biointerfaces containing sphingolipids. Neurochem. Res. 27:547-57
    • (2002) Neurochem. Res. , vol.27 , pp. 547-557
    • Maggio, B.1    Fanani, M.L.2    Oliveira, R.G.3
  • 59
    • 0037414455 scopus 로고    scopus 로고
    • The X-ray crystal structure of human β-hexosaminidase B provides new insights into Sandhoff disease
    • Maier T, Strater N, Schuette CG, Klingenstein R, Sandhoff K, Saenger W. 2003. The X-ray crystal structure of human β-hexosaminidase B provides new insights into Sandhoff disease. J. Mol. Biol. 328:669-81
    • (2003) J. Mol. Biol. , vol.328 , pp. 669-681
    • Maier, T.1    Strater, N.2    Schuette, C.G.3    Klingenstein, R.4    Sandhoff, K.5    Saenger, W.6
  • 61
    • 0344837327 scopus 로고    scopus 로고
    • Crystal structure of human β-hexosaminidase B: Understanding the molecular basis of Sandhoff and Tay-Sachs disease
    • Mark BL, Mahuran DJ, Cherney MM, Zhao D, Knapp S, James MN. 2003. Crystal structure of human β-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. J. Mol. Biol. 327:1093-109
    • (2003) J. Mol. Biol. , vol.327 , pp. 1093-1109
    • Mark, B.L.1    Mahuran, D.J.2    Cherney, M.M.3    Zhao, D.4    Knapp, S.5    James, M.N.6
  • 62
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressure in membranes
    • Marsh D. 1996. Lateral pressure in membranes. Biochim. Biophys. Acta 1286:183-223
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 63
    • 0035830645 scopus 로고    scopus 로고
    • Interaction of ceramides with phosphatidylcholine, sphingomyelin and sphingomyelin/cholesterol bilayers
    • Massey JB. 2001. Interaction of ceramides with phosphatidylcholine, sphingomyelin and sphingomyelin/cholesterol bilayers. Biochim. Biophys. Acta 1510:167-84
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 167-184
    • Massey, J.B.1
  • 64
    • 0035873272 scopus 로고    scopus 로고
    • A mutation in the saposin a domain of the sphingolipid activator protein (prosaposin) gene results in a late-onset, chronic form of globoid cell leukodystrophy in the mouse
    • Matsuda J, Vanier MT, Saito Y, Tohyama J, Suzuki K. 2001. A mutation in the saposin A domain of the sphingolipid activator protein (prosaposin) gene results in a late-onset, chronic form of globoid cell leukodystrophy in the mouse. Hum. Mol. Genet. 10:1191-99
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1191-1199
    • Matsuda, J.1    Vanier, M.T.2    Saito, Y.3    Tohyama, J.4    Suzuki, K.5
  • 65
    • 8444224225 scopus 로고    scopus 로고
    • Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in mouse
    • Matsuda J, Kido M, Tadano-Aritomi K, Ishizuka I, Tominaga K, et al. 2004. Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in mouse. Hum. Mol. Genet. 13:2709-23
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2709-2723
    • Matsuda, J.1    Kido, M.2    Tadano-Aritomi, K.3    Ishizuka, I.4    Tominaga, K.5
  • 66
    • 0018786885 scopus 로고
    • Degradation of bis(monoacylglycero)phosphate by an acid phosphodiesterase in rat liver lysosomes
    • Matsuzawa Y, Hostetler KY. 1979. Degradation of bis(monoacylglycero) phosphate by an acid phosphodiesterase in rat liver lysosomes. J. Biol. Chem. 254:5997-6001
    • (1979) J. Biol. Chem. , vol.254 , pp. 5997-6001
    • Matsuzawa, Y.1    Hostetler, K.Y.2
  • 69
    • 0037135536 scopus 로고    scopus 로고
    • De novo sphingolipid biosynthesis: A necessary, but dangerous, pathway
    • Merrill AH Jr. 2002. De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. J. Biol. Chem. 277:25843-46
    • (2002) J. Biol. Chem. , vol.277 , pp. 25843-25846
    • Merrill Jr., A.H.1
  • 70
    • 0033361755 scopus 로고    scopus 로고
    • Niemann-Pick C1 disease: The 1106 IT substitution is a frequent mutant allele in patients of Western European descent and correlates with a classic juvenile phenotype
    • Millat G, Marcais C, Rafi MA, Yamamoto T, Morris JA, et al. 1999. Niemann-Pick C1 disease: the 1106 IT substitution is a frequent mutant allele in patients of Western European descent and correlates with a classic juvenile phenotype. Am. J. Hum. Genet. 65:1321-29
    • (1999) Am. J. Hum. Genet. , vol.65 , pp. 1321-1329
    • Millat, G.1    Marcais, C.2    Rafi, M.A.3    Yamamoto, T.4    Morris, J.A.5
  • 71
    • 0034755958 scopus 로고    scopus 로고
    • Niemann-Pick disease type C: Spectrum of HE1 mutations and genotype/phenotype correlations in the NPC2 group
    • Millat G, Chikh K, Naureckiene S, Sleat DE, Fensom AH, et al. 2001. Niemann-Pick disease type C: spectrum of HE1 mutations and genotype/phenotype correlations in the NPC2 group. Am. J. Hum. Genet. 69:1013-21
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 1013-1021
    • Millat, G.1    Chikh, K.2    Naureckiene, S.3    Sleat, D.E.4    Fensom, A.H.5
  • 72
    • 0032799717 scopus 로고    scopus 로고
    • Intracellular distribution of a biotin-labeled ganglioside GM1 by immunoelectron microscopy after endocytosis in fibroblasts
    • Möbius W, Herzog V, Sandhoff K, Schwarzmann G. 1999a. Intracellular distribution of a biotin-labeled ganglioside GM1 by immunoelectron microscopy after endocytosis in fibroblasts. J. Histochem. Cytochem. 47:1005-14
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 1005-1014
    • Möbius, W.1    Herzog, V.2    Sandhoff, K.3    Schwarzmann, G.4
  • 73
    • 0032716881 scopus 로고    scopus 로고
    • Gangliosides are transported from the plasma membrane to intralysosomal membranes as revealed by immuno-electron microscopy
    • Möbius W, Herzog V, Sandhoff K, Schwarzmann G. 1999b. Gangliosides are transported from the plasma membrane to intralysosomal membranes as revealed by immuno-electron microscopy. Biosci. Rep. 19:307-16
    • (1999) Biosci. Rep. , vol.19 , pp. 307-316
    • Möbius, W.1    Herzog, V.2    Sandhoff, K.3    Schwarzmann, G.4
  • 74
    • 0038620205 scopus 로고    scopus 로고
    • Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway
    • Möbius W, van Donselaar E, Ohno-Iwashita Y, Shimada Y, Heijnen HF, et al. 2003. Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic 4:222-31
    • (2003) Traffic , vol.4 , pp. 222-231
    • Möbius, W.1    Van Donselaar, E.2    Ohno-Iwashita, Y.3    Shimada, Y.4    Heijnen, H.F.5
  • 76
    • 0029126584 scopus 로고
    • Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
    • Munford RS, Sheppard PO, O'Hara PJ. 1995. Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure. J. Lipid. Res. 36:1653-63
    • (1995) J. Lipid. Res. , vol.36 , pp. 1653-1663
    • Munford, R.S.1    Sheppard, P.O.2    O'Hara, P.J.3
  • 77
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S. 2003. Lipid rafts: elusive or illusive? Cell 115:377-88
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 78
    • 0024593996 scopus 로고
    • Structure of full-length cDNA coding for sulfatide activator, a Co-β-glucosidase and two other homologous proteins: Two alternate forms of the sulfatide activator
    • Nakano T, Sandhoff K, Stumper J, Christomanou H, Suzuki K. 1989. Structure of full-length cDNA coding for sulfatide activator, a Co-β-glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator. J. Biochem. 105:152-54
    • (1989) J. Biochem. , vol.105 , pp. 152-154
    • Nakano, T.1    Sandhoff, K.2    Stumper, J.3    Christomanou, H.4    Suzuki, K.5
  • 79
    • 0034704245 scopus 로고    scopus 로고
    • Identification of HE1 as the second gene of Niemann-Pick C disease
    • Naureckiene S, Sleat DE, Lackland H, Fensom A, Vanier MT, et al. 2000. Identification of HE1 as the second gene of Niemann-Pick C disease. Science 290:2298-301
    • (2000) Science , vol.290 , pp. 2298-2301
    • Naureckiene, S.1    Sleat, D.E.2    Lackland, H.3    Fensom, A.4    Vanier, M.T.5
  • 80
    • 0024297787 scopus 로고
    • Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus
    • O'Brien JS, Kretz KA, Dewji N, Wenger DA, Esch F, Fluharty AL. 1988. Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. Science 241: 1098-1101
    • (1988) Science , vol.241 , pp. 1098-1101
    • O'Brien, J.S.1    Kretz, K.A.2    Dewji, N.3    Wenger, D.A.4    Esch, F.5    Fluharty, A.L.6
  • 81
    • 0033542422 scopus 로고    scopus 로고
    • A porcine homolog of the major secretory protein of human epididymis, HE1, specifically binds cholesterol
    • Okamura N, Kiuchi S, Tamba M, Kashima T, Hiramoto S, et al. 1999. A porcine homolog of the major secretory protein of human epididymis, HE1, specifically binds cholesterol. Biochim. Biophys. Acta 1438:377-87
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 377-387
    • Okamura, N.1    Kiuchi, S.2    Tamba, M.3    Kashima, T.4    Hiramoto, S.5
  • 82
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirement of membrane proteins-a putative bottleneck in heterologous expression
    • Opekarová M, Tanner W. 2003. Specific lipid requirement of membrane proteins-a putative bottleneck in heterologous expression. Biochim. Biophys. Acta 1610:11-22
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 11-22
    • Opekarová, M.1    Tanner, W.2
  • 83
    • 0023716489 scopus 로고
    • Human acid β-glucosidase: Inhibition studies using glucose analogues and pH variation to characterize the normal and Gaucher disease glycon binding sites
    • Osiecki-Newman K, Legler G, Grace M, Dinur T, Gatt S, et al. 1988. Human acid β-glucosidase: inhibition studies using glucose analogues and pH variation to characterize the normal and Gaucher disease glycon binding sites. Enzyme 40:173-88
    • (1988) Enzyme , vol.40 , pp. 173-188
    • Osiecki-Newman, K.1    Legler, G.2    Grace, M.3    Dinur, T.4    Gatt, S.5
  • 84
    • 0344875214 scopus 로고    scopus 로고
    • A riddle wrapped in a mystery: Understanding Niemann-Pick disease, type C
    • Patterson MC. 2003. A riddle wrapped in a mystery: understanding Niemann-Pick disease, type C. Neurology 9:301-10
    • (2003) Neurology , vol.9 , pp. 301-310
    • Patterson, M.C.1
  • 85
    • 0000831301 scopus 로고    scopus 로고
    • Niemann-Pick disease type C: A lipid trafficking disorder
    • ed. CR Scriver, AL Beaudet, WS Sly, D Valle, New York: McGraw-Hill. 8th ed.
    • Patterson MC, Vanier MT, Suzuki K, Morris JA, Carstea E, et al. 2001. Niemann-Pick disease type C: a lipid trafficking disorder. In The Metabolic and Molecular Bases of Inherited Disease, ed. CR Scriver, AL Beaudet, WS Sly, D Valle, III:3611-33. New York: McGraw-Hill. 8th ed.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , vol.3 , pp. 3611-3633
    • Patterson, M.C.1    Vanier, M.T.2    Suzuki, K.3    Morris, J.A.4    Carstea, E.5
  • 86
    • 0021346802 scopus 로고
    • A genetic storage disorder in BALB/C mice with a metabolic block in esterification of exogenous cholesterol
    • Pentchev PG, Boothe AD, Kruth HS, Weintroub H, Stivers J, Brady RO. 1984. A genetic storage disorder in BALB/C mice with a metabolic block in esterification of exogenous cholesterol. J. Biol. Chem. 259:5784-91
    • (1984) J. Biol. Chem. , vol.259 , pp. 5784-5791
    • Pentchev, P.G.1    Boothe, A.D.2    Kruth, H.S.3    Weintroub, H.4    Stivers, J.5    Brady, R.O.6
  • 88
    • 10644282870 scopus 로고    scopus 로고
    • Lysosomal defects and storage
    • ed. FM Platt, SU Walkley, New York: Oxford Univ. Press
    • Platt FM, Walkley SU. 2004. Lysosomal defects and storage. In Lysosomal Disorders of the Brain, ed. FM Platt, SU Walkley, pp. 32-49. New York: Oxford Univ. Press
    • (2004) Lysosomal Disorders of the Brain , pp. 32-49
    • Platt, F.M.1    Walkley, S.U.2
  • 89
    • 0034697239 scopus 로고    scopus 로고
    • Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids
    • Salvioli R, Tatti M, Ciaffoni F, Vaccaro AM. 2000. Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids. FEBS Lett. 472:17-21
    • (2000) FEBS Lett , vol.472 , pp. 17-21
    • Salvioli, R.1    Tatti, M.2    Ciaffoni, F.3    Vaccaro, A.M.4
  • 90
    • 0000857916 scopus 로고    scopus 로고
    • Sphingolipid activator proteins
    • ed. CR Scriver, AL Beaudet, WS Sly, D Valle, New York: McGraw-Hill. 8th ed.
    • Sandhoff K, Kolter T, Harzer K. 2001. Sphingolipid activator proteins. In The Metabolic and Molecular Bases of Inherited Disease, ed. CR Scriver, AL Beaudet, WS Sly, D Valle, III:3371-88. New York: McGraw-Hill. 8th ed.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , vol.3 , pp. 3371-3388
    • Sandhoff, K.1    Kolter, T.2    Harzer, K.3
  • 91
    • 0029670774 scopus 로고    scopus 로고
    • Topology of glycosphingolipid degradation
    • Sandhoff K, Kolter T. 1996. Topology of glycosphingolipid degradation. Trends Cell Biol. 6:98-103
    • (1996) Trends Cell Biol , vol.6 , pp. 98-103
    • Sandhoff, K.1    Kolter, T.2
  • 92
    • 0022894809 scopus 로고
    • Specificity of human glucosylceramide β-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system
    • Sarmientos F, Schwarzmann G, Sandhoff K. 1986. Specificity of human glucosylceramide β-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system. Eur. J. Biochem. 160:527-35
    • (1986) Eur. J. Biochem. , vol.160 , pp. 527-535
    • Sarmientos, F.1    Schwarzmann, G.2    Sandhoff, K.3
  • 93
    • 0026705846 scopus 로고
    • Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene
    • Schnabel D, Schröder M, Fürst W, Klein A, Hurwitz R, et al. 1992. Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene. J. Biol. Chem. 267:3312-15
    • (1992) J. Biol. Chem. , vol.267 , pp. 3312-3315
    • Schnabel, D.1    Schröder, M.2    Fürst, W.3    Klein, A.4    Hurwitz, R.5
  • 94
    • 0025762364 scopus 로고
    • Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease
    • Schnabel D, Schröder M, Sandhoff K. 1991. Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease. FEBS Lett. 284:57-59
    • (1991) FEBS Lett , vol.284 , pp. 57-59
    • Schnabel, D.1    Schröder, M.2    Sandhoff, K.3
  • 95
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. 1997. Functional rafts in cell membranes. Nature 387:569-72
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 96
    • 12844280581 scopus 로고    scopus 로고
    • A mutation in the saposin a coding region of the prosaposin gene in an infant presenting as Krabbe disease: First report of saposin a deficiency in humans
    • Spiegel R, Bach G, Sury V, Mengistu G, Meidan B, et al. 2005. A mutation in the saposin A coding region of the prosaposin gene in an infant presenting as Krabbe disease: first report of saposin A deficiency in humans. Mol. Genet. Metab. 84:160-66
    • (2005) Mol. Genet. Metab. , vol.84 , pp. 160-166
    • Spiegel, R.1    Bach, G.2    Sury, V.3    Mengistu, G.4    Meidan, B.5
  • 97
    • 0041355292 scopus 로고    scopus 로고
    • Saposin C is required for normal resistance of acid β-glucosidase to proteolytic degradation
    • Sun Y, Qi X, Grabowski GA. 2003. Saposin C is required for normal resistance of acid β-glucosidase to proteolytic degradation. J. Biol. Chem. 278:31918-23
    • (2003) J. Biol. Chem. , vol.278 , pp. 31918-31923
    • Sun, Y.1    Qi, X.2    Grabowski, G.A.3
  • 98
    • 0013256537 scopus 로고
    • Genetic disorders of lipid, glycoprotein, and mucopolysaccharide metabolism
    • ed. GJ Siegel, BW Agranoff, RW Albers, PB Molinoff, New York: Raven. 5th ed.
    • Suzuki K. 1994. Genetic disorders of lipid, glycoprotein, and mucopolysaccharide metabolism. In Basic Neurochemistry: Molecular, Cellular, and Medical Aspects, ed. GJ Siegel, BW Agranoff, RW Albers, PB Molinoff, pp. 793-812. New York: Raven. 5th ed.
    • (1994) Basic Neurochemistry: Molecular, Cellular, and Medical Aspects , pp. 793-812
    • Suzuki, K.1
  • 99
    • 0014224649 scopus 로고
    • GM1-gangliosidosis (generalized gangliosidosis). Morphology and chemical pathology
    • Suzuki K, Chen GC. 1968. GM1-gangliosidosis (generalized gangliosidosis). Morphology and chemical pathology. Pathol. Eur. 3:389-408
    • (1968) Pathol. Eur. , vol.3 , pp. 389-408
    • Suzuki, K.1    Chen, G.C.2
  • 100
    • 0343844648 scopus 로고    scopus 로고
    • Lysosomal and peroxisomal diseases
    • ed. GJ Siegel, BW Agranoff, RW Albers, SK Fisher, MD Uhler, Philadelphia: Lippincott-Raven. 6th ed.
    • Suzuki K, Vanier MT. 1999. Lysosomal and peroxisomal diseases. In Basic Neurochemistry-Molecular, Cellular and Medical Aspects, ed. GJ Siegel, BW Agranoff, RW Albers, SK Fisher, MD Uhler, pp. 821-39. Philadelphia: Lippincott-Raven. 6th ed.
    • (1999) Basic Neurochemistry-Molecular, Cellular and Medical Aspects , pp. 821-839
    • Suzuki, K.1    Vanier, M.T.2
  • 101
    • 3543085572 scopus 로고    scopus 로고
    • Ganglioside/glycosphingolipid turnover: New concepts
    • Tettamanti G. 2004. Ganglioside/glycosphingolipid turnover: new concepts. Glycoconjugate J. 20:301-17
    • (2004) Glycoconjugate J , vol.20 , pp. 301-317
    • Tettamanti, G.1
  • 102
    • 1342268375 scopus 로고    scopus 로고
    • The roles of ubiquitin and lipids in protein sorting along the endocytic pathway
    • Umebayashi K. 2003. The roles of ubiquitin and lipids in protein sorting along the endocytic pathway. Cell. Struct. Funct. 28:443-53
    • (2003) Cell. Struct. Funct. , vol.28 , pp. 443-453
    • Umebayashi, K.1
  • 103
    • 0029417339 scopus 로고
    • PH-dependent conformational properties of saposins and their interactions with phospholipid membranes
    • Vaccaro AM, Ciaffoni F, Tatti M, Salvioli R, Barca A, et al. 1995. pH-dependent conformational properties of saposins and their interactions with phospholipid membranes. J. Biol. Chem. 270:30576-80
    • (1995) J. Biol. Chem. , vol.270 , pp. 30576-30580
    • Vaccaro, A.M.1    Ciaffoni, F.2    Tatti, M.3    Salvioli, R.4    Barca, A.5
  • 104
  • 105
    • 0037135518 scopus 로고    scopus 로고
    • Sphingolipid transport: Rafts and translocators
    • van Meer G, Lisman Q. 2002. Sphingolipid transport: rafts and translocators. J. Biol. Chem. 277:25855-58
    • (2002) J. Biol. Chem. , vol.277 , pp. 25855-25858
    • Meer, G.1    Lisman, Q.2
  • 106
    • 0027532181 scopus 로고
    • Demonstration of the existence of a second, non-lysosomal glucocerebrosidase that is not deficient in Gaucher disease
    • van Weely S, Brandsma M, Strijland A, Tager JM, Aerts JM. 1993. Demonstration of the existence of a second, non-lysosomal glucocerebrosidase that is not deficient in Gaucher disease. Biochim. Biophys. Acta 1181:55-62
    • (1993) Biochim. Biophys. Acta , vol.1181 , pp. 55-62
    • Weely, S.1    Brandsma, M.2    Strijland, A.3    Tager, J.M.4    Aerts, J.M.5
  • 107
    • 0025787230 scopus 로고
    • Glycosphingolipid specificity of the human sulfatide activator protein
    • Vogel A, Schwarzmann G, Sandhoff K. 1991. Glycosphingolipid specificity of the human sulfatide activator protein. Eur. J. Biochem. 200:591-97
    • (1991) Eur. J. Biochem. , vol.200 , pp. 591-597
    • Vogel, A.1    Schwarzmann, G.2    Sandhoff, K.3
  • 109
    • 0842330527 scopus 로고    scopus 로고
    • Photoaffinity labelling of the human GM2-activator protein. Mechanistic insight into ganglioside GM2 degradation
    • Wendeler M, Hoernschemeyer J, Hoffmann D, Kolter T, Schwarzmann G, Sandhoff K. 2004. Photoaffinity labelling of the human GM2-activator protein. Mechanistic insight into ganglioside GM2 degradation. Eur. J. Biochem. 271:614-27
    • (2004) Eur. J. Biochem. , vol.271 , pp. 614-627
    • Wendeler, M.1    Hoernschemeyer, J.2    Hoffmann, D.3    Kolter, T.4    Schwarzmann, G.5    Sandhoff, K.6
  • 110
    • 0035918181 scopus 로고    scopus 로고
    • Degradation of membrane-bound ganglioside GM2 by β-hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids
    • Werth N, Schuette CG, Wilkening G, Lemm T, Sandhoff K. 2001. Degradation of membrane-bound ganglioside GM2 by β-hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids. J. Biol. Chem. 276:12685-90
    • (2001) J. Biol. Chem. , vol.276 , pp. 12685-12690
    • Werth, N.1    Schuette, C.G.2    Wilkening, G.3    Lemm, T.4    Sandhoff, K.5
  • 111
    • 0032514902 scopus 로고    scopus 로고
    • Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators
    • Wilkening G, Linke T, Sandhoff K. 1998. Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators. J. Biol. Chem. 273:30271-78
    • (1998) J. Biol. Chem. , vol.273 , pp. 30271-30278
    • Wilkening, G.1    Linke, T.2    Sandhoff, K.3
  • 114
    • 24044463804 scopus 로고    scopus 로고
    • Primary defects in lysosomal enzymes
    • ed. FM Platt, SU Walkley, New York: Oxford Univ. Press
    • Winchester BG. 2004. Primary defects in lysosomal enzymes. In Lysosomal Disorders of the Brain, ed. FM Platt, SU Walkley, pp. 81-130. New York: Oxford Univ. Press
    • (2004) Lysosomal Disorders of the Brain , pp. 81-130
    • Winchester, B.G.1
  • 115
    • 0034406526 scopus 로고    scopus 로고
    • Crystal structure of human GM2-activator protein with a novel β-cup topology
    • Wright CS, Li SC, Rastinejad F. 2000. Crystal structure of human GM2-activator protein with a novel β-cup topology. J. Mol. Biol. 304:411-22
    • (2000) J. Mol. Biol. , vol.304 , pp. 411-422
    • Wright, C.S.1    Li, S.C.2    Rastinejad, F.3
  • 116
    • 0042667012 scopus 로고    scopus 로고
    • Structural analysis of lipid complexes of GM2-activator protein
    • Wright CS, Zhao Q, Rastinejad F. 2003. Structural analysis of lipid complexes of GM2-activator protein. J. Mol. Biol. 331:951-64
    • (2003) J. Mol. Biol. , vol.331 , pp. 951-964
    • Wright, C.S.1    Zhao, Q.2    Rastinejad, F.3
  • 117
    • 0035823586 scopus 로고    scopus 로고
    • Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide
    • Xu X, Bittman R, Duportail G, Heissler D, Vilcheze C, London E. 2001. Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide. J. Biol. Chem. 276:33540-46
    • (2001) J. Biol. Chem. , vol.276 , pp. 33540-33546
    • Xu, X.1    Bittman, R.2    Duportail, G.3    Heissler, D.4    Vilcheze, C.5    London, E.6
  • 119
    • 0043198070 scopus 로고    scopus 로고
    • Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 Å
    • Zajonc DM, Elsliger MA, Teyton L, Wilson IA. 2003. Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 Å. Nat. Immunol. 4:808-15
    • (2003) Nat. Immunol. , vol.4 , pp. 808-815
    • Zajonc, D.M.1    Elsliger, M.A.2    Teyton, L.3    Wilson, I.A.4
  • 120
    • 0035142802 scopus 로고    scopus 로고
    • Neurons in Niemann-Pick disease Type C accumulate gangliosides as well as unesterified cholesterol and undergo dendritic and axonal alterations
    • Zervas M, Dobrenis K, Walkley SU. 2001. Neurons in Niemann-Pick disease Type C accumulate gangliosides as well as unesterified cholesterol and undergo dendritic and axonal alterations. J. Neuropathol. Exp. Neurol. 60:49-64
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , pp. 49-64
    • Zervas, M.1    Dobrenis, K.2    Walkley, S.U.3
  • 121
    • 9144256638 scopus 로고    scopus 로고
    • Editing of CD1d-bound lipid antigens by endosomal lipid transfer proteins
    • Zhou D, Cantu C 3rd, Sagiv Y, Schrantz N, Kulkarni AB, et al. 2004. Editing of CD1d-bound lipid antigens by endosomal lipid transfer proteins. Science 303:523-27
    • (2004) Science , vol.303 , pp. 523-527
    • Zhou, D.1    Cantu III, C.2    Sagiv, Y.3    Schrantz, N.4    Kulkarni, A.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.