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Volumn , Issue , 2006, Pages 67-84

Saposin C and other sphingolipid activator proteins

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EID: 81455135648     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420005509     Document Type: Chapter
Times cited : (3)

References (105)
  • 1
    • 0026747197 scopus 로고
    • Activator proteins and topology of lysosomal sphingolipid catabolism
    • Fürst, W. and Sandhoff, K., Activator proteins and topology of lysosomal sphingolipid catabolism, Biochim. Biophys. Acta. 1126, 1, 1992.
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 1
    • Fürst, W.1    Sandhoff, K.2
  • 2
    • 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. et al., Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway, Traffic. 4, 222, 2003.
    • (2003) Traffic , vol.4 , pp. 222
    • Möbius, W.1
  • 3
    • 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, J.K. et al., 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, 1997.
    • (1997) Eur. J. Cell Biol , vol.73 , pp. 10
    • Burkhardt, J.K.1
  • 4
    • 0034680858 scopus 로고    scopus 로고
    • Degradation of membrane-bound ganglioside GM1. Stimulation by bis(monoacylglycero)phosphate and the activator proteins SAP-B and GM2-AP
    • Wilkening, G. et al., Degradation of membrane-bound ganglioside GM1. Stimulation by bis(monoacylglycero)phosphate and the activator proteins SAP-B and GM2-AP, J. Biol. Chem. 275, 35814, 2000.
    • (2000) J. Biol. Chem , vol.275 , pp. 35814
    • Wilkening, G.1
  • 5
    • 0035918181 scopus 로고    scopus 로고
    • Degradation of membrane-bound ganglioside GM2 by beta-hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids
    • Werth, N. et al., Degradation of membrane-bound ganglioside GM2 by beta-hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids, J. Biol. Chem.,276, 12685, 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 12685
    • Werth, N.1
  • 6
    • 0019513677 scopus 로고
    • Mechanism of activation of glucocerebrosidase by cobeta- glucosidase (glucosidase activator protein)
    • Berent, S.L. and Radin, N.S., Mechanism of activation of glucocerebrosidase by cobeta- glucosidase (glucosidase activator protein), Biochim. Biophys. Acta. 664, 572, 1981.
    • (1981) Biochim. Biophys. Acta , vol.664 , pp. 572
    • Berent, S.L.1    Radin, N.S.2
  • 7
    • 0022894809 scopus 로고
    • Specificity of human glucosylceramide beta-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system
    • Sarmientos, F., Schwarzmann, G., and Sandhoff, K., Specificity of human glucosylceramide beta-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system, Eur. J. Biochem. 160, 527, 1986.
    • (1986) Eur. J. Biochem , vol.160 , pp. 527
    • Sarmientos, F.1    Schwarzmann, G.2    Sandhoff, K.3
  • 8
    • 0034697239 scopus 로고    scopus 로고
    • Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids
    • Salvioli, R. et al., Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids, FEBS Lett. 472, 17, 2000.
    • (2000) FEBS Lett , vol.472 , pp. 17
    • Salvioli, R.1
  • 9
    • 0000956850 scopus 로고    scopus 로고
    • Sphingolipid activator proteins
    • Scriver, C.R., Beaudet, A.L., Sly, W.S., and Valle, D., Eds., McGraw-Hill, New York, chapter 134
    • Sandhoff K. et al., Sphingolipid activator proteins, in The Metabolic and Molecular Bases of Inherited Disease, Scriver, C.R., Beaudet, A.L., Sly, W.S., and Valle, D., Eds., McGraw-Hill, New York, 2004, chapter 134.
    • (2004) The Metabolic and Molecular Bases of Inherited Disease
    • Sandhoff, K.1
  • 11
    • 0015154711 scopus 로고
    • Gaucher’s disease: Deficiency of ‘acid’-glucosidase and reconstitution of enzyme activity in vitro
    • Ho, M.W. and O’Brien, J.S., Gaucher’s disease: deficiency of ‘acid’-glucosidase and reconstitution of enzyme activity in vitro, Proc. Natl. Acad. Sci. U.S.A. 68, 2810, 1971.
    • (1971) Proc. Natl. Acad. Sci. U.S.A , vol.68 , pp. 2810
    • Ho, M.W.1    O’Brien, J.S.2
  • 12
    • 0021983644 scopus 로고
    • Further studies on the activation of glucocerebrosidase by a heatstable factor from Gaucher spleen
    • Prence, E. et al., Further studies on the activation of glucocerebrosidase by a heatstable factor from Gaucher spleen, Arch. Biochem. Biophys. 236, 98, 1985.
    • (1985) Arch. Biochem. Biophys , vol.236 , pp. 98
    • Prence, E.1
  • 13
    • 0025824346 scopus 로고
    • Human acid beta-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme’s catalytic mechanism and saposin A and C binding sites
    • Fabbro, D. and Grabowski, G.A., Human acid beta-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, 1991.
    • (1991) J. Biol. Chem , vol.266 , pp. 15021
    • Fabbro, D.1    Grabowski, G.A.2
  • 14
    • 0017492554 scopus 로고
    • The biochemistry of sphingolipid storage diseases
    • Sandhoff, K., The biochemistry of sphingolipid storage diseases, Angew. Chem. Int. Ed. Engl. 16, 273, 1977.
    • (1977) Angew. Chem. Int. Ed. Engl , vol.16 , pp. 273
    • Sandhoff, K.1
  • 15
    • 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. and Sandhoff, K., 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. U.S.A. 75, 3979, 1978.
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 3979
    • Conzelmann, E.1    Sandhoff, K.2
  • 16
    • 0018567163 scopus 로고
    • Purification and characterization of an activator protein for the degradation of glycolipids GM2 and GA2 by hexosaminidase A
    • Conzelmann, E. and Sandhoff, K., 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, 1979.
    • (1979) Hoppe Seylers Z. Physiol. Chem , vol.360 , pp. 1837
    • Conzelmann, E.1    Sandhoff, K.2
  • 17
    • 0023030611 scopus 로고
    • Synthesis and processing of sphingolipid activator protein-2 (SAP-2) in cultured human fibroblasts
    • Fujibayashi, S. and Wenger, D.A., Synthesis and processing of sphingolipid activator protein-2 (SAP-2) in cultured human fibroblasts, J. Biol. Chem. 261, 15339, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 15339
    • Fujibayashi, S.1    Wenger, D.A.2
  • 18
    • 0022908217 scopus 로고
    • Biosynthesis of the sulfatide/GM1 activator protein (SAP-1) in control and mutant cultured skin fibroblasts
    • Fujibayashi, S. and Wenger, D.A., Biosynthesis of the sulfatide/GM1 activator protein (SAP-1) in control and mutant cultured skin fibroblasts, Biochim. Biophys. Acta. 875, 554, 1986.
    • (1986) Biochim. Biophys. Acta , vol.875 , pp. 554
    • Fujibayashi, S.1    Wenger, D.A.2
  • 19
    • 0023947493 scopus 로고
    • The precursor of sulfatide activator protein is processed to three different proteins
    • Fürst, W., Machleidt, W., and Sandhoff, K., The precursor of sulfatide activator protein is processed to three different proteins, Biol. Chem. Hoppe Seyler. 369, 317, 1988.
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 317
    • Fürst, W.1    Machleidt, W.2    Sandhoff, K.3
  • 20
    • 0025118444 scopus 로고
    • The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein
    • Furst, W. et al., The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein, Eur. J. Biochem. 192, 709, 1990.
    • (1990) Eur. J. Biochem , vol.192 , pp. 709
    • Furst, W.1
  • 21
    • 0024597716 scopus 로고
    • Saposin A: Second cerebrosidase activator protein
    • Morimoto, S. et al., Saposin A: second cerebrosidase activator protein, Proc. Natl. Acad. Sci. U.S.A. 86, 3389, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 3389
    • Morimoto, S.1
  • 22
    • 0024297787 scopus 로고
    • Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus
    • O’Brien, J.S. et al., Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus, Science. 241, 1098, 1988.
    • (1988) Science , vol.241 , pp. 1098
    • O’Brien, J.S.1
  • 23
    • 0024593996 scopus 로고
    • Structure of full-length cDNA coding for sulfatide activator, a Co-beta-glucosidase and two other homologous proteins: Two alternate forms of the sulfatide activator
    • Nakano, T., Sandhoff, K., Stumper, J., Christomanou, H., and Suzuki, K., Structure of full-length cDNA coding for sulfatide activator, a Co-beta-glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator, J. Biochem. (Tokyo), 105, 152 (1989).
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 152
    • Nakano, T.1    Sandhoff, K.2    Stumper, J.3    Christomanou, H.4    Suzuki, K.5
  • 24
    • 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., and Linke, R.P., 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, 1986.
    • (1986) Biol. Chem. Hoppe Seyler , vol.367 , pp. 879
    • Christomanou, H.1    Aignesberger, A.2    Linke, R.P.3
  • 25
    • 0025762364 scopus 로고
    • Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease
    • Schnabel, D., Schröder, M., and Sandhoff, K., Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease, FEBS Lett. 284, 57, 1991.
    • (1991) FEBS Lett , vol.284 , pp. 57
    • Schnabel, D.1    Schröder, M.2    Sandhoff, K.3
  • 26
    • 0028948823 scopus 로고
    • Structural analysis of saposin C and B. Complete localization of disulfide bridges
    • Vaccaro, A.M. et al., Structural analysis of saposin C and B. Complete localization of disulfide bridges, J. Biol. Chem. 270, 9953, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 9953
    • Vaccaro, A.M.1
  • 27
    • 0026768211 scopus 로고
    • Saposins: Structure, function, distribution, and molecular genetics
    • Kishimoto, Y., Hiraiwa, M., and O’Brien, J.S., Saposins: structure, function, distribution, and molecular genetics, J. Lipid Res. 33, 1255, 1992.
    • (1992) J. Lipid Res , vol.33 , pp. 1255
    • Kishimoto, Y.1    Hiraiwa, M.2    O’Brien, J.S.3
  • 28
    • 0029126584 scopus 로고
    • Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
    • Munford, R.S., Sheppard, P.O., and O’Hara, P.J., Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure, J. Lipid Res. 36, 1653, 1995.
    • (1995) J. Lipid Res , vol.36 , pp. 1653
    • Munford, R.S.1    Sheppard, P.O.2    O’Hara, P.J.3
  • 29
    • 0031253938 scopus 로고    scopus 로고
    • Saposin fold revealed by the NMR structure of NK-lysin
    • Liepinsh, E. et al., Saposin fold revealed by the NMR structure of NK-lysin, Nat. Struct. Biol. 4, 793, 1997.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 793
    • Liepinsh, E.1
  • 30
    • 2342445863 scopus 로고    scopus 로고
    • Solution structure of the pore-forming protein of Entamoeba histolytica
    • Hecht, O. et al., Solution structure of the pore-forming protein of Entamoeba histolytica, J. Biol. Chem. 279, 17834, 2004.
    • (2004) J. Biol. Chem , vol.279 , pp. 17834
    • Hecht, O.1
  • 31
    • 11444262537 scopus 로고    scopus 로고
    • Ancient weapons: The three-dimensional structure of amoebapore A
    • Leippe, M. et al., Ancient weapons: the three-dimensional structure of amoebapore A, Trends Parasitol. 21, 5, 2005.
    • (2005) Trends Parasitol , vol.21 , pp. 5
    • Leippe, M.1
  • 32
    • 0024593996 scopus 로고
    • Structure of full-length cDNA coding for sulfatide activator, a Cobeta- glucosidase and two other homologous proteins: Two alternate forms of the sulfatide activator
    • Nakano, T. et al., Structure of full-length cDNA coding for sulfatide activator, a Cobeta- glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator, J. Biochem. (Tokyo). 105, 152, 1989.
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 152
    • Nakano, T.1
  • 33
    • 0027177509 scopus 로고
    • Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins)
    • Hiraiwa, M. et al., Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins), Arch. Biochem. Biophys., 304, 110, 1993.
    • (1993) Arch. Biochem. Biophys , vol.304 , pp. 110
    • Hiraiwa, M.1
  • 34
    • 0345732689 scopus 로고    scopus 로고
    • The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin
    • Lefrancois, S. et al., The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin, Embo J. 22, 6430, 2003.
    • (2003) Embo J , vol.22 , pp. 6430
    • Lefrancois, S.1
  • 35
    • 21544461315 scopus 로고    scopus 로고
    • Inactivation of sortilin (a novel lysosomal sorting receptor) by dominant negative competition and RNA interference
    • Lefrancois, S., Canuel, M., Zeng, J., and Morales, C.R., Inactivation of sortilin (a novel lysosomal sorting receptor) by dominant negative competition and RNA interference, Biol. Proced. Online. 7, 17, 2005.
    • (2005) Biol. Proced. Online , vol.7 , pp. 17
    • Lefrancois, S.1    Canuel, M.2    Zeng, J.3    Morales, C.R.4
  • 36
    • 0029730641 scopus 로고    scopus 로고
    • Biosynthesis, processing, and targeting of sphingolipid activator protein (SAP) precursor in cultured human fibroblasts. Mannose 6-phosphate receptor-independent endocytosis of SAP precursor
    • Vielhaber, G., Hurwitz, R., and Sandhoff, K., Biosynthesis, processing, and targeting of sphingolipid activator protein (SAP) precursor in cultured human fibroblasts. Mannose 6-phosphate receptor-independent endocytosis of SAP precursor, J. Biol. Chem. 271, 32438, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 32438
    • Vielhaber, G.1    Hurwitz, R.2    Sandhoff, K.3
  • 37
    • 0019870169 scopus 로고
    • Beta-Glucosidase activator protein from bovine spleen (“coglucosidase”)
    • Berent, B.L. and Radin, N.S., beta-Glucosidase activator protein from bovine spleen (“coglucosidase”), Arch. Biochem. Biophys. 208, 248, 1981.
    • (1981) Arch. Biochem. Biophys , vol.208 , pp. 248
    • Berent, B.L.1    Radin, N.S.2
  • 38
    • 0023470815 scopus 로고
    • Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant
    • Kleinschmidt, T., Christomanou, H., and Braunitzer, G., Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant, Biol. Chem. Hoppe Seyler. 368, 1571, 1987.
    • (1987) Biol. Chem. Hoppe Seyler , vol.368 , pp. 1571
    • Kleinschmidt, T.1    Christomanou, H.2    Braunitzer, G.3
  • 39
    • 0023810855 scopus 로고
    • The carbohydrate moiety of the activator protein for glucosylceramide beta-glucosidase
    • Sano, A. and Radin, N.S., The carbohydrate moiety of the activator protein for glucosylceramide beta-glucosidase, Biochem. Biophys. Res. Commun. 154, 1197, 1988.
    • (1988) Biochem. Biophys. Res. Commun , vol.154 , pp. 1197
    • Sano, A.1    Radin, N.S.2
  • 40
    • 0023470815 scopus 로고
    • Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant
    • Kleinschmidt, T., Christomanou, H., and Braunitzer, G., Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant, Biol. Chem. Hoppe Seyler. 368, 1571, 1987.
    • (1987) Biol. Chem. Hoppe Seyler , vol.368 , pp. 1571
    • Kleinschmidt, T.1    Christomanou, H.2    Braunitzer, G.3
  • 41
    • 0028948823 scopus 로고
    • Structural analysis of saposin C and B. Complete localization of disulfide bridges
    • Vaccaro, A.M. et al., Structural analysis of saposin C and B. Complete localization of disulfide bridges, J. Biol. Chem. 270, 9953, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 9953
    • Vaccaro, A.M.1
  • 42
    • 0041355292 scopus 로고    scopus 로고
    • Saposin C is required for normal resistance of acid beta-glucosidase to proteolytic degradation
    • Sun, Y., Qi, X., and Grabowski, G.A., Saposin C is required for normal resistance of acid beta-glucosidase to proteolytic degradation, J. Biol. Chem. 278, 31918, 2003.
    • (2003) J. Biol. Chem , vol.278 , pp. 31918
    • Sun, Y.1    Qi, X.2    Grabowski, G.A.3
  • 43
    • 0028275240 scopus 로고
    • Sphingolipid activator protein D (sap-D) stimulates the lysosomal degradation of ceramide in vivo
    • Klein, A. et al., Sphingolipid activator protein D (sap-D) stimulates the lysosomal degradation of ceramide in vivo, Biochem. Biophys. Res. Commun. 200, 1440, 1994.
    • (1994) Biochem. Biophys. Res. Commun , vol.200 , pp. 1440
    • Klein, A.1
  • 44
    • 0028303294 scopus 로고
    • Hydrolysis of lactosylceramide by human galactosylceramidase and GM1-beta-galactosidase in a detergent-free system and its stimulation by sphingolipid Eur J activator proteins, sap-B and sap-C. Activator proteins stimulate lactosylceramide hydrolysis
    • Zschoche, A. et al., Hydrolysis of lactosylceramide by human galactosylceramidase and GM1-beta-galactosidase in a detergent-free system and its stimulation by sphingolipid Eur J activator proteins, sap-B and sap-C. Activator proteins stimulate lactosylceramide hydrolysis, Eur. J. Biochem. 222, 83, 1994.
    • (1994) Eur. J. Biochem , vol.222 , pp. 83
    • Zschoche, A.1
  • 45
    • 0020482329 scopus 로고
    • A protein activator of galactosylceramide beta-galactosidase
    • Wenger, D.A., Sattler, M., and Roth, S., A protein activator of galactosylceramide beta-galactosidase, Biochim. Biophys. Acta. 712, 639, 1982.
    • (1982) Biochim. Biophys. Acta , vol.712 , pp. 639
    • Wenger, D.A.1    Sattler, M.2    Roth, S.3
  • 46
    • 0021679619 scopus 로고
    • Studies on the activation of sphingomyelinase activity in Niemann-Pick type A, B, and C fibroblasts: Enzymological differentiation of types A and B
    • Poulos, A. et al., Studies on the activation of sphingomyelinase activity in Niemann-Pick type A, B, and C fibroblasts: enzymological differentiation of types A and B, Pediatr. Res. 18, 1088, 1984.
    • (1984) Pediatr. Res , vol.18 , pp. 1088
    • Poulos, A.1
  • 47
    • 0347625853 scopus 로고    scopus 로고
    • Solution structure of human saposin C: PHdependent interaction with phospholipid vesicles
    • de Alba, E., Weiler, S., and Tjandra, N., Solution structure of human saposin C: pHdependent interaction with phospholipid vesicles, Biochemistry. 42, 14729, 2003.
    • (2003) Biochemistry , vol.42 , pp. 14729
    • De Alba, E.1    Weiler, S.2    Tjandra, N.3
  • 48
    • 13844299352 scopus 로고    scopus 로고
    • Solution structure of human saposin C in a detergent environment
    • Hawkins, C.A., Alba, E., and Tjandra, N., Solution structure of human saposin C in a detergent environment, J. Mol. Biol. 346, 1381, 2005.
    • (2005) J. Mol. Biol , vol.346 , pp. 1381
    • Hawkins, C.A.1    Alba, E.2    Tjandra, N.3
  • 49
    • 0016835979 scopus 로고
    • Glucocerebrosidase: Stoichiometry of association between effector and catalytic proteins
    • Ho, M.W. and Rigby, M., Glucocerebrosidase: stoichiometry of association between effector and catalytic proteins, Biochim. Biophys. Acta. 397, 267, 1975.
    • (1975) Biochim. Biophys. Acta , vol.397 , pp. 267
    • Ho, M.W.1    Rigby, M.2
  • 50
    • 0015698354 scopus 로고
    • Glucocerebrosidase: Reconstitution from macromolecular components depends on acidic phospholipids
    • Ho, M.W. and Light, N.D., Glucocerebrosidase: reconstitution from macromolecular components depends on acidic phospholipids, Biochem. J. 136, 821, 1973.
    • (1973) Biochem. J , vol.136 , pp. 821
    • Ho, M.W.1    Light, N.D.2
  • 51
    • 0029417339 scopus 로고
    • Ph-dependent conformational properties of saposins and their interactions with phospholipid membranes
    • Vaccaro, A.M. et al., pH-dependent conformational properties of saposins and their interactions with phospholipid membranes, J. Biol. Chem. 270, 30576, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 30576
    • Vaccaro, A.M.1
  • 52
    • 0028945615 scopus 로고
    • Identification of the binding and activating sites of the sphingolipid activator protein, saposin C, with glucocerebrosidase
    • Weiler, S. et al., Identification of the binding and activating sites of the sphingolipid activator protein, saposin C, with glucocerebrosidase, Protein Sci. 4, 756, 1995.
    • (1995) Protein Sci , vol.4 , pp. 756
    • Weiler, S.1
  • 53
    • 7644235520 scopus 로고    scopus 로고
    • Direct AFM observation of saposin C-induced membrane domains in lipid bilayers: From simple to complex lipid mixtures
    • You, H.X., Qi, X., and Yu, L., Direct AFM observation of saposin C-induced membrane domains in lipid bilayers: from simple to complex lipid mixtures, Chem. Phys. Lipids. 132, 15, 2004.
    • (2004) Chem. Phys. Lipids , vol.132 , pp. 15
    • You, H.X.1    Qi, X.2    Yu, L.3
  • 54
    • 0032514902 scopus 로고    scopus 로고
    • Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators
    • Wilkening, G., Linke, T., and Sandhoff, K., Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators, J. Biol. Chem. 273, 30271, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 30271
    • Wilkening, G.1    Linke, T.2    Sandhoff, K.3
  • 55
    • 12344305490 scopus 로고    scopus 로고
    • Saposin C-LBPA interaction in late-endosomes/lysosomes
    • Chu, Z., Witte, D.P., and Qi, X., Saposin C-LBPA interaction in late-endosomes/lysosomes, Exp. Cell Res. 303, 300, 2005.
    • (2005) Exp. Cell Res , vol.303 , pp. 300
    • Chu, Z.1    Witte, D.P.2    Qi, X.3
  • 56
    • 1642504446 scopus 로고    scopus 로고
    • Fusogenic domain and lysines in saposin C
    • Qi, X. and Chu, Z., Fusogenic domain and lysines in saposin C, Arch. Biochem. Biophys. 424, 210, 2004.
    • (2004) Arch. Biochem. Biophys , vol.424 , pp. 210
    • Qi, X.1    Chu, Z.2
  • 57
    • 2342436735 scopus 로고    scopus 로고
    • Glucosylceramidase mass and subcellular localization are modulated by cholesterol in Niemann-Pick disease type C
    • Salvioli, R. et al., Glucosylceramidase mass and subcellular localization are modulated by cholesterol in Niemann-Pick disease type C, J. Biol. Chem. 279, 17674, 2004.
    • (2004) J. Biol. Chem , vol.279 , pp. 17674
    • Salvioli, R.1
  • 58
    • 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. et al., 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, 2005.
    • (2005) Mol. Genet. Metab , vol.84 , pp. 160
    • Spiegel, R.1
  • 59
    • 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. et al., 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, 2001.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1191
    • Matsuda, J.1
  • 60
    • 0024597716 scopus 로고
    • Saposin A: Second cerebrosidase activator protein
    • Morimoto, S. et al., Saposin A: second cerebrosidase activator protein, Proc. Natl. Acad. Sci. U.S.A. 86, 3389, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 3389
    • Morimoto, S.1
  • 61
    • 0025127278 scopus 로고
    • Interaction of saposins, acidic lipids, and glucosylceramidase
    • Morimoto, S. et al., Interaction of saposins, acidic lipids, and glucosylceramidase, J. Biol. Chem. 265, 1933, 1990.
    • (1990) J. Biol. Chem , vol.265 , pp. 1933
    • Morimoto, S.1
  • 62
    • 0025321793 scopus 로고
    • Characterization of a mutation in a family with saposin B deficiency: A glycosylation site defect
    • Kretz, K.A. et al., Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect, Proc. Natl. Acad. Sci. U.S A. 87, 2541, 1990.
    • (1990) Proc. Natl. Acad. Sci. U.S A , vol.87 , pp. 2541
    • Kretz, K.A.1
  • 63
    • 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, S.C. et al., 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, 1985.
    • (1985) J. Biol. Chem , vol.260 , pp. 1867
    • Li, S.C.1
  • 64
    • 0345242618 scopus 로고
    • The physiological roles of activator proteins for lysosomal glycolipid degradation
    • Salvayre, R., Douste-Blazy, L., and Gatt, S., Eds., Plenum Publishing, New York
    • Conzelmann, E., Lee-Vaupel, M., and Sandhoff, K., The physiological roles of activator proteins for lysosomal glycolipid degradation, in Lipid storage disorders, Salvayre, R., Douste-Blazy, L., and Gatt, S., Eds., Plenum Publishing, New York, 1988, p. 323.
    • (1988) Lipid storage disorders , pp. 323
    • Conzelmann, E.1    Lee-Vaupel, M.2    Sandhoff, K.3
  • 65
    • 0037422574 scopus 로고    scopus 로고
    • Crystal structure of saposin B reveals a dimeric shell for lipid binding
    • Ahn, V.E. et al., Crystal structure of saposin B reveals a dimeric shell for lipid binding, Proc. Natl. Acad. Sci. U.S.A. 100, 38, 2003.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 38
    • Ahn, V.E.1
  • 66
    • 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. et al., 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, 2004.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 2709
    • Matsuda, J.1
  • 67
    • 0024791636 scopus 로고
    • Sphingolipid hydrolase activator proteins and their precursors
    • Sano, A. et al., Sphingolipid hydrolase activator proteins and their precursors, Biochem. Biophys. Res. Commun., 165, 1191, 1989.
    • (1989) Biochem. Biophys. Res. Commun , vol.165 , pp. 1191
    • Sano, A.1
  • 68
    • 0026328108 scopus 로고
    • Isolation and characterization of prosaposin from human milk
    • Kondoh, K. et al., Isolation and characterization of prosaposin from human milk, Biochem. Biophys. Res. Commun. 181, 286, 1991.
    • (1991) Biochem. Biophys. Res. Commun , vol.181 , pp. 286
    • Kondoh, K.1
  • 69
    • 0025728991 scopus 로고
    • Secretion of sphingolipid hydrolase activator precursor, prosaposin
    • Hineno, T. et al., Secretion of sphingolipid hydrolase activator precursor, prosaposin, Biochem. Biophys. Res. Commun. 176, 668, 1991.
    • (1991) Biochem. Biophys. Res. Commun , vol.176 , pp. 668
    • Hineno, T.1
  • 70
    • 0029013931 scopus 로고
    • Identification of the neurotrophic factor sequence of prosaposin
    • O’Brien, J.S. et al., Identification of the neurotrophic factor sequence of prosaposin, Faseb J. 9, 681, 1995.
    • (1995) Faseb J , vol.9 , pp. 681
    • O’Brien, J.S.1
  • 71
    • 0032190625 scopus 로고    scopus 로고
    • Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture
    • Tsuboi, K., Hiraiwa, M., and O’Brien, J.S., Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture, Brain Res. Dev. Brain Res. 110, 249, 1998.
    • (1998) Brain Res. Dev. Brain Res , vol.110 , pp. 249
    • Tsuboi, K.1    Hiraiwa, M.2    O’Brien, J.S.3
  • 72
    • 0029970341 scopus 로고    scopus 로고
    • Prosaposin facilitates sciatic nerve regeneration in vivo
    • Kotani, Y. et al., Prosaposin facilitates sciatic nerve regeneration in vivo, J. Neurochem., 66, 2019, 1996.
    • (1996) J. Neurochem , vol.66 , pp. 2019
    • Kotani, Y.1
  • 73
    • 0029996085 scopus 로고    scopus 로고
    • A hydrophilic peptide comprising 18 amino acid residues of the prosaposin sequence has neurotrophic activity in vitro and in vivo
    • Kotani, Y. et al., A hydrophilic peptide comprising 18 amino acid residues of the prosaposin sequence has neurotrophic activity in vitro and in vivo, J. Neurochem., 66, 2197, 1996.
    • (1996) J. Neurochem , vol.66 , pp. 2197
    • Kotani, Y.1
  • 74
    • 0034736222 scopus 로고    scopus 로고
    • Prosaptide exacerbates ischemia-induced behavioral deficits in vivo; an effect that does not involve mitogen-activated protein kinase activation
    • Lapchak, P.A. et al., Prosaptide exacerbates ischemia-induced behavioral deficits in vivo; an effect that does not involve mitogen-activated protein kinase activation, Neuroscience. 101, 811, 2000.
    • (2000) Neuroscience , vol.101 , pp. 811
    • Lapchak, P.A.1
  • 75
    • 0030971534 scopus 로고    scopus 로고
    • Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides
    • Hiraiwa, M. et al., Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides, Proc. Natl. Acad. Sci. U.S.A. 94, 4778, 1997.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 4778
    • Hiraiwa, M.1
  • 76
    • 0035000532 scopus 로고    scopus 로고
    • Prosaposin is immunolocalized to muscle and prosaptides promote myoblast fusion and attenuate loss of muscle mass after nerve injury
    • Rende, M. et al., Prosaposin is immunolocalized to muscle and prosaptides promote myoblast fusion and attenuate loss of muscle mass after nerve injury, Muscle Nerve. 24, 799, 2001.
    • (2001) Muscle Nerve , vol.24 , pp. 799
    • Rende, M.1
  • 77
    • 0037357780 scopus 로고    scopus 로고
    • Prosaposin ablation inactivates the MAPK and Akt signaling pathways and interferes with the development of the prostate gland
    • Morales, C.R., and Badran, H., Prosaposin ablation inactivates the MAPK and Akt signaling pathways and interferes with the development of the prostate gland, Asian J. Androl. 5, 57, 2003.
    • (2003) Asian J. Androl , vol.5 , pp. 57
    • Morales, C.R.1    Badran, H.2
  • 78
    • 0032995276 scopus 로고    scopus 로고
    • Exposure of thawed frozen bull sperm to a synthetic peptide before artificial insemination increases fertility
    • Amann, R.P., Seidel, G.E., Jr., and Brink, Z.A., Exposure of thawed frozen bull sperm to a synthetic peptide before artificial insemination increases fertility, J. Androl. 20, 42, 1999.
    • (1999) J. Androl , vol.20 , pp. 42
    • Amann, R.P.1    Seidel, G.E.2    Brink, Z.A.3
  • 79
    • 0034939951 scopus 로고    scopus 로고
    • Sphingolipid activator proteins: Proteins with complex functions in lipid degradation and skin biogenesis
    • Schuette, C.G. et al., Sphingolipid activator proteins: proteins with complex functions in lipid degradation and skin biogenesis, Glycobiology, 11, 81R, 2001.
    • (2001) Glycobiology , vol.11 , pp. 81
    • Schuette, C.G.1
  • 80
    • 0027316078 scopus 로고
    • Processing of epidermal glucosylceramides is required for optimal mammalian cutaneous permeability barrier function
    • Holleran, W.M. et al., Processing of epidermal glucosylceramides is required for optimal mammalian cutaneous permeability barrier function, J. Clin. Invest. 91, 1656, 1993.
    • (1993) J. Clin. Invest , vol.91 , pp. 1656
    • Holleran, W.M.1
  • 81
    • 0032970258 scopus 로고    scopus 로고
    • Accumulation of protein-bound epidermal glucosylceramides in beta-glucocerebrosidase deficient type 2 Gaucher mice
    • Doering, T., Proia, R.L., and Sandhoff, K., Accumulation of protein-bound epidermal glucosylceramides in beta-glucocerebrosidase deficient type 2 Gaucher mice, FEBS Lett., 447, 167 (1999).
    • (1999) FEBS Lett , vol.447 , pp. 167
    • Doering, T.1    Proia, R.L.2    Sandhoff, K.3
  • 83
    • 12344317686 scopus 로고    scopus 로고
    • Nitric oxide regulates synthesis of gene products involved in keratinocyte differentiation and ceramide metabolism
    • Gallala, H., Macheleidt, O., Doering, T., Schreiner, V., and Sandhoff, K., Nitric oxide regulates synthesis of gene products involved in keratinocyte differentiation and ceramide metabolism, Eur. J. Cell Biol. 83, 667, 2004.
    • (2004) Eur. J. Cell Biol , vol.83 , pp. 667
    • Gallala, H.1    Macheleidt, O.2    Doering, T.3    Schreiner, V.4    Sandhoff, K.5
  • 84
    • 0036794552 scopus 로고    scopus 로고
    • Sphingolipid metabolism during epidermal barrier development in mice
    • Doering, T., Brade, H., and Sandhoff, K., Sphingolipid metabolism during epidermal barrier development in mice, J. Lipid Res. 43, 1727, 2002.
    • (2002) J. Lipid Res , vol.43 , pp. 1727
    • Doering, T.1    Brade, H.2    Sandhoff, K.3
  • 85
    • 0026731660 scopus 로고
    • Gaucher disease in the neonate: A distinct Gaucher phenotype is analogous to a mouse model created by targeted disruption of the glucocerebrosidase gene
    • Sidransky, E., Sherer, D.M., and Ginns, E.I., Gaucher disease in the neonate: a distinct Gaucher phenotype is analogous to a mouse model created by targeted disruption of the glucocerebrosidase gene, Pediatr. Res. 32, 494, 1992.
    • (1992) Pediatr. Res , vol.32 , pp. 494
    • Sidransky, E.1    Sherer, D.M.2    Ginns, E.I.3
  • 86
    • 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. et al., 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, 1996.
    • (1996) Hum. Mol. Genet , vol.5 , pp. 711
    • Fujita, N.1
  • 87
    • 1142263122 scopus 로고    scopus 로고
    • Presenting fats with SAPs
    • Kronenberg, M., Presenting fats with SAPs, Nat. Immunol. 5, 126, 2004.
    • (2004) Nat. Immunol , vol.5 , pp. 126
    • Kronenberg, M.1
  • 88
    • 10744232076 scopus 로고    scopus 로고
    • Saposin C is required for lipid presentation by human CD1b
    • Winau, F. et al., Saposin C is required for lipid presentation by human CD1b, Nat. Immunol., 5, 169, 2004.
    • (2004) Nat. Immunol , vol.5 , pp. 169
    • Winau, F.1
  • 89
    • 1142263116 scopus 로고    scopus 로고
    • Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells
    • Kang, S.J. and Cresswell, P., Saposins facilitate CD1d-restricted presentation of an exogenous lipid antigen to T cells, Nat. Immunol. 5, 175, 2004.
    • (2004) Nat. Immunol , vol.5 , pp. 175
    • Kang, S.J.1    Cresswell, P.2
  • 90
    • 9144256638 scopus 로고    scopus 로고
    • Editing of CD1d-bound lipid antigens by endosomal lipid transfer proteins
    • Zhou, D. et al., Editing of CD1d-bound lipid antigens by endosomal lipid transfer proteins, Science. 303, 523, 2004.
    • (2004) Science , vol.303 , pp. 523
    • Zhou, D.1
  • 91
    • 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. et al., 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, 1993.
    • (1993) Hum. Genet , vol.92 , pp. 143
    • Bradova, V.1
  • 92
    • 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. et al., 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, 1992.
    • (1992) J. Biol. Chem , vol.267 , pp. 3312
    • Schnabel, D.1
  • 93
    • 23644446418 scopus 로고    scopus 로고
    • Prosaposin deficiency - a rarely diagnosed, rapidly progressing, neonatal neurovisceral lipid storage disease. Report of a further patient
    • Elleder, M. et al., Prosaposin deficiency - a rarely diagnosed, rapidly progressing, neonatal neurovisceral lipid storage disease. Report of a further patient, Neuropediatrics. 36, 171, 2005.
    • (2005) Neuropediatrics , vol.36 , pp. 171
    • Elleder, M.1
  • 94
    • 0035871255 scopus 로고    scopus 로고
    • A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation
    • Hulkova, H. et al., A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation, Hum. Mol. Genet. 10, 927, 2001.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 927
    • Hulkova, H.1
  • 95
    • 0024435444 scopus 로고
    • Activator protein deficient Gaucher’s disease. A second patient with the newly identified lipid storage disorder
    • Christomanou, H. et al., Activator protein deficient Gaucher’s disease. A second patient with the newly identified lipid storage disorder, Klin Wochenschr. 67, 999, 1989.
    • (1989) Klin Wochenschr , vol.67 , pp. 999
    • Christomanou, H.1
  • 96
    • 0027192992 scopus 로고
    • Mutational analysis in a patient with a variant form of Gaucher disease caused by SAP-2 deficiency
    • Rafi, M.A. et al., Mutational analysis in a patient with a variant form of Gaucher disease caused by SAP-2 deficiency, Somat. Cell. Mol. Genet. 19, 1, 1993.
    • (1993) Somat. Cell. Mol. Genet , vol.19 , pp. 1
    • Rafi, M.A.1
  • 97
    • 0033028948 scopus 로고    scopus 로고
    • Neuronopathic juvenile glucosylceramidosis due to sap-C deficiency: Clinical course, neuropathology and brain lipid composition in this Gaucher disease variant
    • Pampols, T., Pineda, M., Giros, M.L., Ferrer, I., Cusi, V., Chabas, A., Sanmarti, F.X., Vanier, M.T., and Christomanou, H., Neuronopathic juvenile glucosylceramidosis due to sap-C deficiency: clinical course, neuropathology and brain lipid composition in this Gaucher disease variant, Acta Neuropathol. (Berl.). 97, 91, 1999.
    • (1999) Acta Neuropathol. (Berl.) , vol.97 , pp. 91
    • Pampols, T.1    Pineda, M.2    Giros, M.L.3    Ferrer, I.4    Cusi, V.5    Chabas, A.6    Sanmarti, F.X.7    Vanier, M.T.8    Christomanou, H.9
  • 98
    • 0029670774 scopus 로고    scopus 로고
    • Topology of glycosphingolipid degradation
    • Sandhoff, K. and Kolter, T. Topology of glycosphingolipid degradation, Trends Cell. Biol. 6, 98, 1996.
    • (1996) Trends Cell. Biol , vol.6 , pp. 98
    • Sandhoff, K.1    Kolter, T.2
  • 99
    • 0031973892 scopus 로고    scopus 로고
    • Recent advances in the biochemistry of sphingolipidoses
    • Kolter, T. and Sandhoff, K., Recent advances in the biochemistry of sphingolipidoses, Brain Pathol. 8, 79, 1998.
    • (1998) Brain Pathol , vol.8 , pp. 79
    • Kolter, T.1    Sandhoff, K.2
  • 100
    • 0029656306 scopus 로고    scopus 로고
    • Analysis of a splice site mutation in the SAP precursor gene of a patient with metachromatic leukodystrophy
    • Henseler, M. et al., Analysis of a splice site mutation in the SAP precursor gene of a patient with metachromatic leukodystrophy, Am. J. Hum. Genet. 58, 65, 1996.
    • (1996) Am. J. Hum. Genet , vol.58 , pp. 65
    • Henseler, M.1
  • 101
    • 0025017535 scopus 로고
    • Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy
    • Rafi, M.A. et al., Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy, Biochem. Biophys. Res. Commun. 166, 1017, 1990.
    • (1990) Biochem. Biophys. Res. Commun , vol.166 , pp. 1017
    • Rafi, M.A.1
  • 102
    • 0025743034 scopus 로고
    • Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease
    • Holtschmidt, H. et al., Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease, J. Biol. Chem., 266, 7556, 1991.
    • (1991) J. Biol. Chem , vol.266 , pp. 7556
    • Holtschmidt, H.1
  • 103
    • 0025056561 scopus 로고
    • Insertion in the mRNA of a metachromatic leukodystrophy patient with sphingolipid activator protein-1 deficiency
    • Zhang, X-L. et al., Insertion in the mRNA of a metachromatic leukodystrophy patient with sphingolipid activator protein-1 deficiency, Proc. Natl. Acad. Sci. U.S.A. 87, 1426, 1990.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 1426
    • Zhang, X.-L.1
  • 104
    • 0025908730 scopus 로고
    • The mechanism for a 33-nucleotide insertion in messenger RNA causing sphingolipid activator protein (SAP-1)-deficient metachromatic leukodystrophy
    • Zhang, X.L. et al., The mechanism for a 33-nucleotide insertion in messenger RNA causing sphingolipid activator protein (SAP-1)-deficient metachromatic leukodystrophy, Hum. Genet., 87, 211, 1991.
    • (1991) Hum. Genet , vol.87 , pp. 211
    • Zhang, X.L.1
  • 105
    • 0033971433 scopus 로고    scopus 로고
    • A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD)
    • Wrobe, D. et al., A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD), J. Inherit. Metab. Dis., 23, 63, 2000.
    • (2000) J. Inherit. Metab. Dis , vol.23 , pp. 63
    • Wrobe, D.1


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