메뉴 건너뛰기




Volumn 1841, Issue 5, 2014, Pages 799-810

Sphingolipids and lysosomal pathologies

Author keywords

Lipid storage; Lysosomal lipids; Membrane degradation; Sphingolipid catabolism

Indexed keywords

CERAMIDE GLUCOSYLTRANSFERASE; CERAMIDE SYNTHASE 1; CERAMIDE SYNTHASE 2; CERAMIDE SYNTHASE 3; CERAMIDE SYNTHASE 6; CEREBROSIDE SULFOTRANSFERASE; ENZYME; GALACTOSYLCERAMIDE; GANGLIOSIDE; GANGLIOSIDE GM2; GANGLIOSIDE GM2 ACTIVATOR PROTEIN; GANGLIOSIDE GM3; GLUCOSYLCERAMIDE; GLYCOSPHINGOLIPID; LACTOSYLCERAMIDE ALPHA2,3 SIALYLTRANSFERASE; MIGLUSTAT; OLIGOSACCHARIDE; SERINE PALMITOYLTRANSFERASE; SPHINGOLIPID; SPHINGOLIPID ACTIVATOR PROTEIN; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOSINE KINASE 1; SPHINGOSINE KINASE 2; SULFATIDE; UNCLASSIFIED DRUG;

EID: 84897954529     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2013.10.015     Document Type: Review
Times cited : (77)

References (201)
  • 3
    • 77954225471 scopus 로고    scopus 로고
    • Common and uncommon pathogenic cascades in lysosomal storage diseases
    • E.B. Vitner, F.M. Platt, and A.H. Futerman Common and uncommon pathogenic cascades in lysosomal storage diseases J. Biol. Chem. 285 2010 20423 20427
    • (2010) J. Biol. Chem. , vol.285 , pp. 20423-20427
    • Vitner, E.B.1    Platt, F.M.2    Futerman, A.H.3
  • 5
    • 2942652829 scopus 로고    scopus 로고
    • The pathogenesis of glycosphingolipid storage disorders
    • DOI 10.1016/j.semcdb.2004.03.003, PII S1084952104000333
    • L. Ginzburg, Y. Kacher, and A.H. Futerman The pathogenesis of glycosphingolipid storage disorders Semin. Cell Dev. Biol. 15 2004 417 431 (Pubitemid 38781904)
    • (2004) Seminars in Cell and Developmental Biology , vol.15 , Issue.4 , pp. 417-431
    • Ginzburg, L.1    Kacher, Y.2    Futerman, A.H.3
  • 6
    • 33845343984 scopus 로고    scopus 로고
    • Sphingolipid metabolism diseases
    • DOI 10.1016/j.bbamem.2006.05.027, PII S0005273606002069, Sphingolipids, Apoptosis and Disease
    • T. Kolter, and K. Sandhoff Sphingolipid metabolism diseases Biochim. Biophys. Acta 1758 2006 2057 2079 (Pubitemid 44879358)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.12 , pp. 2057-2079
    • Kolter, T.1    Sandhoff, K.2
  • 8
    • 0020997754 scopus 로고
    • Stage-specific embryonic antigens (SSEA-3 and -4) are epitopes of a unique globo-series ganglioside isolated from human teratocarcinoma cells
    • R. Kannagi, N.A. Cochran, F. Ishigami, S. Hakomori, P.W. Andrews, B.B. Knowles, and D. Solter Stage-specific embryonic antigens (SSEA-3 and -4) are epitopes of a unique globo-series ganglioside isolated from human teratocarcinoma cells EMBO J. 2 1983 2355 2361
    • (1983) EMBO J. , vol.2 , pp. 2355-2361
    • Kannagi, R.1    Cochran, N.A.2    Ishigami, F.3    Hakomori, S.4    Andrews, P.W.5    Knowles, B.B.6    Solter, D.7
  • 9
    • 0024474715 scopus 로고
    • Specific interaction between Le(x) and Le(x) determinants. A possible basis for cell recognition in preimplantation embryos and in embryonal carcinoma cells
    • I. Eggens, B. Fenderson, T. Toyokuni, B. Dean, M. Stroud, and S. Hakomori Specific interaction between Lex and Lex determinants. A possible basis for cell recognition in preimplantation embryos and in embryonal carcinoma cells J. Biol. Chem. 264 1989 9476 9484 (Pubitemid 19157590)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.16 , pp. 9476-9484
    • Eggens, I.1    Fenderson, B.2    Toyokuni, T.3    Dean, B.4    Stroud, M.5    Hakomori, S.-I.6
  • 10
    • 0027467490 scopus 로고
    • Ganglioside metabolism. Enzymology, topology, and regulation
    • G. van Echten, and K. Sandhoff Ganglioside metabolism. Enzymology, topology, and regulation J. Biol. Chem. 268 1993 5341 5344 (Pubitemid 23090844)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.8 , pp. 5341-5344
    • Van Echten, G.1    Sandhoff, K.2
  • 11
    • 80053060999 scopus 로고    scopus 로고
    • Structures, biosynthesis, and functions of gangliosides - An overview
    • R.K. Yu, Y.T. Tsai, T. Ariga, and M. Yanagisawa Structures, biosynthesis, and functions of gangliosides - an overview J. Oleo Sci. 60 2011 537 544
    • (2011) J. Oleo Sci. , vol.60 , pp. 537-544
    • Yu, R.K.1    Tsai, Y.T.2    Ariga, T.3    Yanagisawa, M.4
  • 12
    • 0032504164 scopus 로고    scopus 로고
    • Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope
    • DOI 10.1074/jbc.273.28.17763
    • L.N. Marekov, and P.M. Steinert Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope J. Biol. Chem. 273 1998 17763 17770 (Pubitemid 28355119)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.28 , pp. 17763-17770
    • Marekov, L.N.1    Steinert, P.M.2
  • 13
    • 77951886452 scopus 로고    scopus 로고
    • Very long chain sphingolipids: Tissue expression, function and synthesis
    • R. Sandhoff Very long chain sphingolipids: tissue expression, function and synthesis FEBS Lett. 584 2010 1907 1913
    • (2010) FEBS Lett. , vol.584 , pp. 1907-1913
    • Sandhoff, R.1
  • 14
    • 84896723076 scopus 로고    scopus 로고
    • The role of sphingolipid metabolism in cutaneous permeabilitybarrier formation
    • 10.1016/j.bbalip.2013.08.010 (accepted article preview online August 15, 2013)
    • B. Breiden, and K. Sandhoff The role of sphingolipid metabolism in cutaneous permeabilitybarrier formation Biochim. Biophys. Acta 2013 10.1016/j.bbalip.2013.08.010 (accepted article preview online August 15, 2013)
    • (2013) Biochim. Biophys. Acta
    • Breiden, B.1    Sandhoff, K.2
  • 15
    • 77953561361 scopus 로고    scopus 로고
    • Mammalian ceramide synthases
    • M. Levy, and A.H. Futerman Mammalian ceramide synthases IUBMB Life 62 2010 347 356
    • (2010) IUBMB Life , vol.62 , pp. 347-356
    • Levy, M.1    Futerman, A.H.2
  • 16
    • 0037135536 scopus 로고    scopus 로고
    • De novo sphingolipid biosynthesis: A necessary, but dangerous, pathway
    • DOI 10.1074/jbc.R200009200
    • A.H. Merrill Jr. De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway J. Biol. Chem. 277 2002 25843 25846 (Pubitemid 34967059)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 25843-25846
    • Merrill Jr., A.H.1
  • 18
    • 0347611095 scopus 로고    scopus 로고
    • Molecular machinery for non-vesicular trafficking of ceramide
    • DOI 10.1038/nature02188
    • K. Hanada, K. Kumagai, S. Yasuda, Y. Miura, M. Kawano, M. Fukasawa, and M. Nishijima Molecular machinery for non-vesicular trafficking of ceramide Nature 426 2003 803 809 (Pubitemid 38056858)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 803-809
    • Hanada, K.1    Kumagai, K.2    Yasuda, S.3    Miura, Y.4    Kawano, M.5    Fukasawa, M.6    Nishijima, M.7
  • 19
    • 0028288399 scopus 로고
    • Lactosylceramide is synthesized in the lumen of the Golgi apparatus
    • DOI 10.1016/0014-5793(94)80591-1
    • H. Lannert, C. Bunning, D. Jeckel, and F.T. Wieland Lactosylceramide is synthesized in the lumen of the Golgi apparatus FEBS Lett. 342 1994 91 96 (Pubitemid 24101400)
    • (1994) FEBS Letters , vol.342 , Issue.1 , pp. 91-96
    • Jeckel, D.1
  • 20
    • 1542319939 scopus 로고    scopus 로고
    • Role of Multiple Drug Resistance Protein 1 in Neutral but Not Acidic Glycosphingolipid Biosynthesis
    • DOI 10.1074/jbc.M305645200
    • M.F. De Rosa, D. Sillence, C. Ackerley, and C. Lingwood Role of multiple drug resistance protein 1 in neutral but not acidic glycosphingolipid biosynthesis J. Biol. Chem. 279 2004 7867 7876 (Pubitemid 38294673)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7867-7876
    • De Rosa, M.F.1    Sillence, D.2    Ackerley, C.3    Lingwood, C.4
  • 21
    • 22544457473 scopus 로고    scopus 로고
    • The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids
    • DOI 10.1042/BJ20050047
    • P.D. Eckford, and F.J. Sharom The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids Biochem. J. 389 2005 517 526 (Pubitemid 41021155)
    • (2005) Biochemical Journal , vol.389 , Issue.2 , pp. 517-526
    • Eckford, P.D.W.1    Sharom, F.J.2
  • 25
    • 0031661695 scopus 로고    scopus 로고
    • Variations among cell lines in the synthesis of sphingolipids in de novo and recycling pathways
    • B.K. Gillard, R.G. Clement, and D.M. Marcus Variations among cell lines in the synthesis of sphingolipids in de novo and recycling pathways Glycobiology 8 1998 885 890 (Pubitemid 28398985)
    • (1998) Glycobiology , vol.8 , Issue.9 , pp. 885-890
    • Gillard, B.K.1    Clement, R.G.2    Marcus, D.M.3
  • 26
    • 0037518448 scopus 로고    scopus 로고
    • Salvage pathways in glycosphingolipid metabolism
    • DOI 10.1016/S0300-9084(03)00047-6
    • G. Tettamanti, R. Bassi, P. Viani, and L. Riboni Salvage pathways in glycosphingolipid metabolism Biochimie 85 2003 423 437 (Pubitemid 36626013)
    • (2003) Biochimie , vol.85 , Issue.3-4 , pp. 423-437
    • Tettamanti, G.1    Bassi, R.2    Viani, P.3    Riboni, L.4
  • 28
    • 0037135608 scopus 로고    scopus 로고
    • Combinatorial ganglioside biosynthesis
    • DOI 10.1074/jbc.R200001200
    • T. Kolter, R.L. Proia, and K. Sandhoff Combinatorial ganglioside biosynthesis J. Biol. Chem. 277 2002 25859 25862 (Pubitemid 34967063)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 25859-25862
    • Kolter, T.1    Proia, R.L.2    Sandhoff, K.3
  • 33
    • 0035093829 scopus 로고    scopus 로고
    • Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I
    • DOI 10.1038/85879
    • J.L. Dawkins, D.J. Hulme, S.B. Brahmbhatt, M. Auer-Grumbach, and G.A. Nicholson Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I Nat. Genet. 27 2001 309 312 (Pubitemid 32201853)
    • (2001) Nature Genetics , vol.27 , Issue.3 , pp. 309-312
    • Dawkins, J.L.1    Hulme, D.J.2    Brahmbhatt, S.B.3    Auer-Grumbach, M.4    Nicholson, G.A.5
  • 34
    • 84862768394 scopus 로고    scopus 로고
    • Autophagy proteins in macroendocytic engulfment
    • O. Florey, and M. Overholtzer Autophagy proteins in macroendocytic engulfment Trends Cell Biol. 22 2012 374 380
    • (2012) Trends Cell Biol. , vol.22 , pp. 374-380
    • Florey, O.1    Overholtzer, M.2
  • 38
    • 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
    • J.K. Burkhardt, S. Hüttler, A. Klein, W. Möbius, A. Habermann, G. Griffiths, and K. Sandhoff 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 1997 10 18 (Pubitemid 27226186)
    • (1997) European Journal of Cell Biology , vol.73 , Issue.1 , pp. 10-18
    • Burkhardt, J.K.1    Huttler, S.2    Klein, A.3    Mobius, W.4    Habermann, A.5    Griffiths, G.6    Sandhoff, K.7
  • 39
    • 0032799717 scopus 로고    scopus 로고
    • Intracellular distribution of a biotin-labeled ganglioside, GM1, by immunoelectron microscopy after endocytosis in fibroblasts
    • W. Möbius, V. Herzog, K. Sandhoff, and G. Schwarzmann Intracellular distribution of a biotin-labeled ganglioside, GM1, by immunoelectron microscopy after endocytosis in fibroblasts J. Histochem. Cytochem. 47 1999 1005 1014 (Pubitemid 29379899)
    • (1999) Journal of Histochemistry and Cytochemistry , vol.47 , Issue.8 , pp. 1005-1014
    • Mobius, W.1    Herzog, V.2    Sandhoff, K.3    Schwarzmann, G.4
  • 40
    • 0026747197 scopus 로고
    • Activator proteins and topology of lysosomal sphingolipid catabolism
    • W. Fürst, and K. Sandhoff Activator proteins and topology of lysosomal sphingolipid catabolism Biochim. Biophys. Acta 1126 1992 1 16
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 1-16
    • Fürst, W.1    Sandhoff, K.2
  • 41
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • T. Wollert, and J.H. Hurley Molecular mechanism of multivesicular body biogenesis by ESCRT complexes Nature 464 2010 864 869
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 42
    • 25444443570 scopus 로고    scopus 로고
    • Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids
    • DOI 10.1146/annurev.cellbio.21.122303.120013
    • T. Kolter, and K. Sandhoff Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids Annu. Rev. Cell Dev. Biol. 21 2005 81 103 (Pubitemid 41740628)
    • (2005) Annual Review of Cell and Developmental Biology , vol.21 , pp. 81-103
    • Kolter, T.1    Sandhoff, K.2
  • 43
    • 79851476846 scopus 로고    scopus 로고
    • Regulation of the NPC2 protein-mediated cholesterol trafficking by membrane lipids
    • H.D. Gallala, B. Breiden, and K. Sandhoff Regulation of the NPC2 protein-mediated cholesterol trafficking by membrane lipids J. Neurochem. 116 2011 702 707
    • (2011) J. Neurochem. , vol.116 , pp. 702-707
    • Gallala, H.D.1    Breiden, B.2    Sandhoff, K.3
  • 44
    • 40049084797 scopus 로고    scopus 로고
    • Cell biology. No ESCRTs for exosomes
    • M. Marsh, and G. van Meer Cell biology. No ESCRTs for exosomes Science 319 2008 1191 1192
    • (2008) Science , vol.319 , pp. 1191-1192
    • Marsh, M.1    Van Meer, G.2
  • 45
    • 67249110996 scopus 로고    scopus 로고
    • Multivesicular endosome biogenesis in the absence of ESCRTs
    • S. Stuffers, C. Sem Wegner, H. Stenmark, and A. Brech Multivesicular endosome biogenesis in the absence of ESCRTs Traffic 10 2009 925 937
    • (2009) Traffic , vol.10 , pp. 925-937
    • Stuffers, S.1    Sem Wegner, C.2    Stenmark, H.3    Brech, A.4
  • 46
    • 54349098469 scopus 로고    scopus 로고
    • Regulation of sterol transport between membranes and NPC2
    • Z. Xu, W. Farver, and J. Storch Regulation of sterol transport between membranes and NPC2 Biochemistry 47 2008 11134 11143
    • (2008) Biochemistry , vol.47 , pp. 11134-11143
    • Xu, Z.1    Farver, W.2    Storch, J.3
  • 48
  • 49
    • 55749083068 scopus 로고    scopus 로고
    • NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes
    • R.E. Infante, M.L. Wang, A. Radhakrishnan, H.J. Kwon, M.S. Brown, and J.L. Goldstein NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes Proc. Natl. Acad. Sci. U. S. A. 105 2008 15287 15292
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15287-15292
    • Infante, R.E.1    Wang, M.L.2    Radhakrishnan, A.3    Kwon, H.J.4    Brown, M.S.5    Goldstein, J.L.6
  • 50
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • H.J. Kwon, L. Abi-Mosleh, M.L. Wang, J. Deisenhofer, J.L. Goldstein, M.S. Brown, and R.E. Infante Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol Cell 137 2009 1213 1224
    • (2009) Cell , vol.137 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6    Infante, R.E.7
  • 51
    • 79957903652 scopus 로고    scopus 로고
    • Function of the Niemann-Pick type C proteins and their bypass by cyclodextrin
    • J.E. Vance, and K.B. Peake Function of the Niemann-Pick type C proteins and their bypass by cyclodextrin Curr. Opin. Lipidol. 22 2011 204 209
    • (2011) Curr. Opin. Lipidol. , vol.22 , pp. 204-209
    • Vance, J.E.1    Peake, K.B.2
  • 52
    • 33845938485 scopus 로고    scopus 로고
    • Saposin A mobilizes lipids from low cholesterol and high bis(monoacylglycerol)phosphate-containing membranes: Patient variant saposin a lacks lipid extraction capacity
    • DOI 10.1074/jbc.M607281200
    • S. Locatelli-Hoops, N. Remmel, R. Klingenstein, B. Breiden, M. Rossocha, M. Schöniger, C. Königs, W. Saenger, and K. Sandhoff Saposin A mobilizes lipids from low cholesterol and high bis(monoacylglycerol)phosphate- containing membranes: patient variant Saposin A lacks lipid extraction capacity J. Biol. Chem. 281 2006 32451 32460 (Pubitemid 46036800)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32451-32460
    • Locatelli-Hoops, S.1    Remmel, N.2    Klingenstein, R.3    Breiden, B.4    Rossocha, M.5    Schoeniger, M.6    Koenigs, C.7    Saenger, W.8    Sandhoff, K.9
  • 53
    • 34347405277 scopus 로고    scopus 로고
    • Saposin B mobilizes lipids from cholesterol-poor and bis(monoacylglycero) phosphate-rich membranes at acidic pH: Unglycosylated patient variant saposin B lacks lipid-extraction capacity
    • DOI 10.1111/j.1742-4658.2007.05873.x
    • N. Remmel, S. Locatelli-Hoops, B. Breiden, G. Schwarzmann, and K. Sandhoff Saposin B mobilizes lipids from cholesterol-poor and bis(monoacylglycero)phosphate-rich membranes at acidic pH. Unglycosylated patient variant saposin B lacks lipid-extraction capacity FEBS J. 274 2007 3405 3420 (Pubitemid 47024974)
    • (2007) FEBS Journal , vol.274 , Issue.13 , pp. 3405-3420
    • Remmel, N.1    Locatelli-Hoops, S.2    Breiden, B.3    Schwarzmann, G.4    Sandhoff, K.5
  • 54
    • 67649255316 scopus 로고    scopus 로고
    • Niemann-Pick C2 (NPC2) and intracellular cholesterol trafficking
    • J. Storch, and Z. Xu Niemann-Pick C2 (NPC2) and intracellular cholesterol trafficking Biochim. Biophys. Acta 1791 2009 671 678
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 671-678
    • Storch, J.1    Xu, Z.2
  • 56
    • 84897954429 scopus 로고    scopus 로고
    • V.O. Oninla, B. Breiden, J.O. Babalola, K. Sandhoff, in preparation, (2013)
    • V.O. Oninla, B. Breiden, J.O. Babalola, K. Sandhoff, in preparation, (2013).
  • 57
    • 0020658595 scopus 로고
    • Biochemical studies in Niemann-Pick disease. I. Major sphingolipids of liver and spleen
    • M.T. Vanier Biochemical studies in Niemann-Pick disease. I. Major sphingolipids of liver and spleen Biochim. Biophys. Acta 750 1983 178 184 (Pubitemid 13184757)
    • (1983) Biochimica et Biophysica Acta , vol.750 , Issue.1 , pp. 178-184
    • Vanier, M.T.1
  • 58
    • 80755163636 scopus 로고    scopus 로고
    • Biological function of the cellular lipid BMP - BMP as a key activator for cholesterol sorting and membrane digestion
    • H. Gallala, and K. Sandhoff Biological function of the cellular lipid BMP - BMP as a key activator for cholesterol sorting and membrane digestion Neurochem. Res. 36 2011 1594 1600
    • (2011) Neurochem. Res. , vol.36 , pp. 1594-1600
    • Gallala, H.1    Sandhoff, K.2
  • 59
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: Emerging functions for lysosomal membrane proteins
    • DOI 10.1016/S0962-8924(03)00005-9
    • E.L. Eskelinen, Y. Tanaka, and P. Saftig At the acidic edge: emerging functions for lysosomal membrane proteins Trends Cell Biol. 13 2003 137 145 (Pubitemid 36293786)
    • (2003) Trends in Cell Biology , vol.13 , Issue.3 , pp. 137-145
    • Eskelinen, E.-L.1    Tanaka, Y.2    Saftig, P.3
  • 60
    • 84878998458 scopus 로고    scopus 로고
    • Lysosomal membrane proteins and their central role in physiology
    • M. Schwake, B. Schroder, and P. Saftig Lysosomal membrane proteins and their central role in physiology Traffic 14 2013 739 748
    • (2013) Traffic , vol.14 , pp. 739-748
    • Schwake, M.1    Schroder, B.2    Saftig, P.3
  • 62
    • 84869223682 scopus 로고    scopus 로고
    • Sensitivity to lysosome-dependent cell death is directly regulated by lysosomal cholesterol content
    • H. Appelqvist, L. Sandin, K. Bjornstrom, P. Saftig, B. Garner, K. Ollinger, and K. Kagedal Sensitivity to lysosome-dependent cell death is directly regulated by lysosomal cholesterol content PLoS One 7 2012 e50262
    • (2012) PLoS One , vol.7 , pp. 50262
    • Appelqvist, H.1    Sandin, L.2    Bjornstrom, K.3    Saftig, P.4    Garner, B.5    Ollinger, K.6    Kagedal, K.7
  • 64
    • 0000223691 scopus 로고    scopus 로고
    • Interaction of the GM2-activator protein with phospholipid-ganglioside bilayer membranes and with monolayers at the air-water interface
    • DOI 10.1046/j.1432-1327.1999.00302.x
    • A. Giehl, T. Lemm, O. Bartelsen, K. Sandhoff, and A. Blume Interaction of the GM2-activator protein with phospholipid-ganglioside bilayer membranes and with monolayers at the air-water interface Eur. J. Biochem. 261 1999 650 658 (Pubitemid 29226061)
    • (1999) European Journal of Biochemistry , vol.261 , Issue.3 , pp. 650-658
    • Giehl, A.1    Lemm, T.2    Bartelsen, O.3    Sandhoff, K.4    Blume, A.5
  • 65
    • 0035918181 scopus 로고    scopus 로고
    • Degradation of membrane-bound ganglioside GM2 by beta -hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids
    • N. Werth, C.G. Schuette, G. Wilkening, T. Lemm, and K. Sandhoff Degradation of membrane-bound ganglioside GM2 by beta -hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids J. Biol. Chem. 276 2001 12685 12690
    • (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
  • 66
    • 0032514902 scopus 로고    scopus 로고
    • Lysosomal degradation on vesicular membrane surfaces: Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators
    • DOI 10.1074/jbc.273.46.30271
    • G. Wilkening, T. Linke, and K. Sandhoff Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators J. Biol. Chem. 273 1998 30271 30278 (Pubitemid 28545494)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.46 , pp. 30271-30278
    • Wilkening, G.1    Linke, T.2    Sandhoff, K.3
  • 67
    • 0035937146 scopus 로고    scopus 로고
    • Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins
    • T. Linke, G. Wilkening, F. Sadeghlar, H. Mozcall, K. Bernardo, E. Schuchman, and K. Sandhoff Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins J. Biol. Chem. 276 2001 5760 5768
    • (2001) J. Biol. Chem. , vol.276 , pp. 5760-5768
    • Linke, T.1    Wilkening, G.2    Sadeghlar, F.3    Mozcall, H.4    Bernardo, K.5    Schuchman, E.6    Sandhoff, K.7
  • 69
    • 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
    • DOI 10.1074/jbc.271.50.32438
    • G. Vielhaber, R. Hurwitz, and K. Sandhoff 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 1996 32438 32446 (Pubitemid 26422287)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.50 , pp. 32438-32446
    • Vielhaber, G.1    Hurwitz, R.2    Sandhoff, K.3
  • 70
    • 19244385377 scopus 로고    scopus 로고
    • Lysosomal proteolysis of prosaposin, the precursor of saposins (sphingolipid activator proteins): Its mechanism and inhibition by ganglioside
    • DOI 10.1006/abbi.1997.9958
    • M. Hiraiwa, B.M. Martin, Y. Kishimoto, G.E. Conner, S. Tsuji, and J.S. O'Brien Lysosomal proteolysis of prosaposin, the precursor of saposins (sphingolipid activator proteins): its mechanism and inhibition by ganglioside Arch. Biochem. Biophys. 341 1997 17 24 (Pubitemid 27198026)
    • (1997) Archives of Biochemistry and Biophysics , vol.341 , Issue.1 , pp. 17-24
    • Hiraiwa, M.1    Martin, B.M.2    Kishimoto, Y.3    Conner, G.E.4    Tsuji, S.5    O'Brien, J.S.6
  • 71
    • 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
    • DOI 10.1016/j.ymgme.2004.10.004, PII S1096719204002756
    • R. Spiegel, G. Bach, V. Sury, G. Mengistu, B. Meidan, S. Shalev, Y. Shneor, H. Mandel, and M. Zeigler 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 2005 160 166 (Pubitemid 40164576)
    • (2005) Molecular Genetics and Metabolism , vol.84 , Issue.2 , pp. 160-166
    • Spiegel, R.1    Bach, G.2    Sury, V.3    Mengistu, G.4    Meidan, B.5    Shalev, S.6    Shneor, Y.7    Mandel, H.8    Zeigler, M.9
  • 72
    • 0019789442 scopus 로고
    • Cerebroside sulfatase activator deficiency induced metachromatic leukodystrophy
    • R.L. Stevens, A.L. Fluharty, H. Kihara, M.M. Kaback, L.J. Shapiro, B. Marsh, K. Sandhoff, and G. Fischer Cerebroside sulfatase activator deficiency induced metachromatic leukodystrophy Am. J. Hum. Genet. 33 1981 900 906 (Pubitemid 12194877)
    • (1981) American Journal of Human Genetics , vol.33 , Issue.6 , pp. 900-906
    • Stevens, R.L.1    Fluharty, A.L.2    Kihara, H.3
  • 74
    • 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
    • H. Christomanou, A. Aignesberger, and R.P. Linke 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 1986 879 890
    • (1986) Biol. Chem. Hoppe Seyler , vol.367 , pp. 879-890
    • Christomanou, H.1    Aignesberger, A.2    Linke, R.P.3
  • 75
    • 26944464611 scopus 로고    scopus 로고
    • A mutation within the saposin D domain in a Gaucher disease patient with normal glucocerebrosidase activity
    • DOI 10.1007/s00439-005-1288-x
    • A. Diaz-Font, B. Cormand, R. Santamaria, L. Vilageliu, D. Grinberg, and A. Chabas A mutation within the saposin D domain in a Gaucher disease patient with normal glucocerebrosidase activity Hum. Genet. 117 2005 275 277 (Pubitemid 43136805)
    • (2005) Human Genetics , vol.117 , Issue.2-3 , pp. 275-277
    • Diaz-Font, A.1    Cormand, B.2    Santamaria, R.3    Vilageliu, L.4    Grinberg, D.5    Chabas, A.6
  • 76
    • 84871368269 scopus 로고    scopus 로고
    • My journey into the world of sphingolipids and sphingolipidoses
    • K. Sandhoff My journey into the world of sphingolipids and sphingolipidoses Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 88 2012 554 582
    • (2012) Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. , vol.88 , pp. 554-582
    • Sandhoff, K.1
  • 78
    • 0034939951 scopus 로고    scopus 로고
    • Sphingolipid activator proteins: Proteins with complex functions in lipid degradation and skin biogenesis
    • C.G. Schütte, B. Pierstorff, S. Hüttler, and K. Sandhoff Sphingolipid activator proteins: proteins with complex functions in lipid degradation and skin biogenesis Glycobiology 11 2001 81R 90R (Pubitemid 32655236)
    • (2001) Glycobiology , vol.11 , Issue.6
    • Schuette, C.G.1    Pierstorff, B.2    Huettler, S.3    Sandhoff, K.4
  • 79
    • 0028331151 scopus 로고
    • Consequences of beta-glucocerebrosidase deficiency in epidermis. Ultrastructure and permeability barrier alterations in Gaucher disease
    • W.M. Holleran, E.I. Ginns, G.K. Menon, J.U. Grundmann, M. Fartasch, C.E. McKinney, P.M. Elias, and E. Sidransky Consequences of beta-glucocerebrosidase deficiency in epidermis. Ultrastructure and permeability barrier alterations in Gaucher disease J. Clin. Invest. 93 1994 1756 1764
    • (1994) J. Clin. Invest. , vol.93 , pp. 1756-1764
    • Holleran, W.M.1    Ginns, E.I.2    Menon, G.K.3    Grundmann, J.U.4    Fartasch, M.5    McKinney, C.E.6    Elias, P.M.7    Sidransky, E.8
  • 81
    • 0032970258 scopus 로고    scopus 로고
    • Accumulation of protein-bound epidermal glucosylceramides in β-glucocerebrosidase deficient type 2 Gaucher mice
    • DOI 10.1016/S0014-5793(99)00274-4, PII S0014579399002744
    • T. Doering, R.L. Proia, and K. Sandhoff Accumulation of protein-bound epidermal glucosylceramides in beta-glucocerebrosidase deficient type 2 Gaucher mice FEBS Lett. 447 1999 167 170 (Pubitemid 29146079)
    • (1999) FEBS Letters , vol.447 , Issue.2-3 , pp. 167-170
    • Doering, T.1    Proia, R.L.2    Sandhoff, K.3
  • 83
    • 84879143450 scopus 로고    scopus 로고
    • Gangliosides and gangliosidoses, Principles of molecular and metabolic pathogenesis
    • K. Sandhoff, and K. Harzer Gangliosides and gangliosidoses, Principles of molecular and metabolic pathogenesis J. Neurosci. 33 2013 10195 10208
    • (2013) J. Neurosci. , vol.33 , pp. 10195-10208
    • Sandhoff, K.1    Harzer, K.2
  • 84
    • 0442323490 scopus 로고    scopus 로고
    • Interactions of acid sphingomyelinase and lipid bilayers in the presence of the tricyclic antidepressant desipramine
    • DOI 10.1016/S0014-5793(04)00033-X
    • M. Kölzer, N. Werth, and K. Sandhoff Interactions of acid sphingomyelinase and lipid bilayers in the presence of the tricyclic antidepressant desipramine FEBS Lett. 559 2004 96 98 (Pubitemid 38186710)
    • (2004) FEBS Letters , vol.559 , Issue.1-3 , pp. 96-98
    • Kolzer, M.1    Werth, N.2    Sandhoff, K.3
  • 85
    • 0028468309 scopus 로고
    • The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts
    • R. Hurwitz, K. Ferlinz, and K. Sandhoff The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts Biol. Chem. Hoppe Seyler 375 1994 447 450 (Pubitemid 2120332)
    • (1994) Biological Chemistry Hoppe-Seyler , vol.375 , Issue.7 , pp. 447-450
    • Hurwitz, R.1    Ferlinz, K.2    Sandhoff, K.3
  • 86
    • 50549200398 scopus 로고
    • On a biochemically special form of infantile amaturotic idiocy
    • H. Jatzkewitz, and K. Sandhoff On a biochemically special form of infantile amaturotic idiocy Biochim. Biophys. Acta 70 1963 354 356
    • (1963) Biochim. Biophys. Acta , vol.70 , pp. 354-356
    • Jatzkewitz, H.1    Sandhoff, K.2
  • 87
    • 0014436233 scopus 로고
    • Generalized gangliosidosis: Beta-galactosidase deficiency
    • S. Okada, and J.S. O'Brien Generalized gangliosidosis: beta-galactosidase deficiency Science 160 1968 1002 1004
    • (1968) Science , vol.160 , pp. 1002-1004
    • Okada, S.1    O'Brien, J.S.2
  • 88
    • 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
    • G. Wilkening, T. Linke, G. Uhlhorn-Dierks, and K. Sandhoff Degradation of membrane-bound ganglioside GM1. Stimulation by bis(monoacylglycero)phosphate and the activator proteins SAP-B and GM2-AP J. Biol. Chem. 275 2000 35814 35819
    • (2000) J. Biol. Chem. , vol.275 , pp. 35814-35819
    • Wilkening, G.1    Linke, T.2    Uhlhorn-Dierks, G.3    Sandhoff, K.4
  • 90
    • 0035224941 scopus 로고    scopus 로고
    • Lysosomal multienzyme complex: Biochemistry, genetics, and molecular pathophysiology
    • A.V. Pshezhetsky, and M. Ashmarina Lysosomal multienzyme complex: biochemistry, genetics, and molecular pathophysiology Prog. Nucleic Acid Res. Mol. Biol. 69 2001 81 114
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.69 , pp. 81-114
    • Pshezhetsky, A.V.1    Ashmarina, M.2
  • 91
    • 0000869162 scopus 로고    scopus 로고
    • The mucopolysaccharidoses
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, V. D. McGraw-Hill New York
    • E.F. Neufeld, and J. Muenzer The mucopolysaccharidoses C.R. Scriver, A.L. Beaudet, W.S. Sly, V. D. The Metabolic and Molecular Bases of Inherited Disease 2001 McGraw-Hill New York 3421 3452
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3421-3452
    • Neufeld, E.F.1    Muenzer, J.2
  • 92
    • 0346666894 scopus 로고    scopus 로고
    • Imbalanced substrate specificity of mutant β-galactosidase in patients with Morquio B disease
    • DOI 10.1016/S1096-7192(02)00199-3, PII S1096719202001993
    • T. Okumiya, H. Sakuraba, R. Kase, and T. Sugiura Imbalanced substrate specificity of mutant beta-galactosidase in patients with Morquio B disease Mol. Genet. Metab. 78 2003 51 58 (Pubitemid 36268742)
    • (2003) Molecular Genetics and Metabolism , vol.78 , Issue.1 , pp. 51-58
    • Okumiya, T.1    Sakuraba, H.2    Kase, R.3    Sugiura, T.4
  • 94
    • 0021885280 scopus 로고
    • Evidence for two different active sites on human β-hexosaminidase A. Interaction of G(M2) activator protein with β-hexosaminidase A
    • H.J. Kytzia, and K. Sandhoff Evidence for two different active sites on human beta-hexosaminidase A. Interaction of GM2 activator protein with beta-hexosaminidase A J. Biol. Chem. 260 1985 7568 7572 (Pubitemid 15063038)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.12 , pp. 7568-7572
    • Kytzia, H.-J.1    Sandhoff, K.2
  • 95
    • 0037414455 scopus 로고    scopus 로고
    • The X-ray crystal structure of human β-hexosaminidase B provides new insights into Sandhoff disease
    • DOI 10.1016/S0022-2836(03)00311-5
    • T. Maier, N. Strater, C.G. Schütte, R. Klingenstein, K. Sandhoff, and W. Saenger The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease J. Mol. Biol. 328 2003 669 681 (Pubitemid 36438580)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.3 , pp. 669-681
    • Maier, T.1    Strater, N.2    Schuette, C.G.3    Klingenstein, R.4    Sandhoff, K.5    Saenger, W.6
  • 97
    • 0020686110 scopus 로고
    • Variant of GM2-gangliosidosis with hexosaminidase A having a severely changed substrate specificity
    • H.J. Kytzia, U. Hinrichs, I. Maire, K. Suzuki, and K. Sandhoff Variant of GM2-gangliosidosis with hexosaminidase A having a severely changed substrate specificity EMBO J. 2 1983 1201 1205
    • (1983) EMBO J. , vol.2 , pp. 1201-1205
    • Kytzia, H.J.1    Hinrichs, U.2    Maire, I.3    Suzuki, K.4    Sandhoff, K.5
  • 98
    • 0014225180 scopus 로고
    • Deficient hexosaminidase activity in an exceptional case of Tay-Sachs disease with additional storage of kidney globoside in visceral organs
    • K. Sandhoff, U. Andreae, and H. Jatzkewitz Deficient hexosaminidase activity in an exceptional case of Tay-Sachs disease with additional storage of kidney globoside in visceral organs Pathol. Eur. 3 1968 278 285
    • (1968) Pathol. Eur. , vol.3 , pp. 278-285
    • Sandhoff, K.1    Andreae, U.2    Jatzkewitz, H.3
  • 101
    • 0000889058 scopus 로고    scopus 로고
    • α-Galactosidase A deficiency fabry disease
    • B.A. C.R. Scriver, W.S. Sly, D. Valle, McGraw-Hill New York
    • I.Y., and R.J. Desnick α-Galactosidase A deficiency fabry disease B.A. C.R. Scriver, W.S. Sly, D. Valle, The Metabolic and Molecular Bases of inherited Disease 2001 McGraw-Hill New York 3733 3774
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3733-3774
    • Desnick, R.J.1
  • 102
    • 0000216808 scopus 로고    scopus 로고
    • Gaucher disease
    • B.A. C. Scriver, W.S. Sly, D. Valle, McGraw-Hill New York
    • G.G., and E. Beutler Gaucher disease B.A. C. Scriver, W.S. Sly, D. Valle, The Metabolic and Molecular Bases of Inherited Disease 2001 McGraw-Hill New York 3635 3668
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3635-3668
    • Beutler, E.1
  • 103
    • 50549198437 scopus 로고
    • Metabolism of glucocerebrosides. II. Evidence of an enzymatic deficiency in Gaucher's disease
    • R.O. Brady, J.N. Kanfer, and D. Shapiro Metabolism of glucocerebrosides. II. Evidence of an enzymatic deficiency in Gaucher's disease Biochem. Biophys. Res. Commun. 18 1965 221 225
    • (1965) Biochem. Biophys. Res. Commun. , vol.18 , pp. 221-225
    • Brady, R.O.1    Kanfer, J.N.2    Shapiro, D.3
  • 104
    • 0001973683 scopus 로고
    • Short communications: A deficiency of glucocerebrosidase in Gaucher's disease
    • A.D. Patrick Short communications: a deficiency of glucocerebrosidase in Gaucher's disease Biochem. J. 97 1965 17C 18C
    • (1965) Biochem. J. , vol.97
    • Patrick, A.D.1
  • 105
    • 0022894809 scopus 로고
    • Specificity of human glucosylceramide β-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system
    • DOI 10.1111/j.1432-1033.1986.tb10071.x
    • F. Sarmientos, G. Schwarzmann, and K. Sandhoff Specificity of human glucosylceramide beta-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system Eur. J. Biochem. 160 1986 527 535 (Pubitemid 17044425)
    • (1986) European Journal of Biochemistry , vol.160 , Issue.3 , pp. 527-535
    • Sarmientos, F.1    Schwarzmann, G.2    Sandhoff, K.3
  • 106
    • 0020320060 scopus 로고
    • Accumulation of glucosylceramide and glucosylsphingosine (psychosine) in cerebrum and cerebellum in infantile and juvenile Gaucher disease
    • DOI 10.1111/j.1471-4159.1982.tb07950.x
    • O. Nilsson, and L. Svennerholm Accumulation of glucosylceramide and glucosylsphingosine (psychosine) in cerebrum and cerebellum in infantile and juvenile Gaucher disease J. Neurochem. 39 1982 709 718 (Pubitemid 12034962)
    • (1982) Journal of Neurochemistry , vol.39 , Issue.3 , pp. 709-718
    • Nilsson, O.1    Svennerholm, L.2
  • 107
    • 0020403317 scopus 로고
    • The occurrence of psychosine and other glycolipids in spleen and liver from the three major types of Gaucher's disease
    • O. Nilsson, J.E. Mansson, G. Hakansson, and L. Svennerholm The occurrence of psychosine and other glycolipids in spleen and liver from the three major types of Gaucher's disease Biochim. Biophys. Acta 712 1982 453 463 (Pubitemid 13198976)
    • (1982) Biochimica et Biophysica Acta , vol.712 , Issue.3 , pp. 453-463
    • Nilsson, O.1    Mansson, J.E.2    Hakansson, G.3    Svennerholm, L.4
  • 108
    • 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
    • DOI 10.1007/s004010050960
    • T. Pampols, M. Pineda, M.L. Giros, I. Ferrer, V. Cusi, A. Chabas, F.X. Sanmarti, M.T. Vanier, and H. Christomanou Neuronopathic juvenile glucosylceramidosis due to sap-C deficiency: clinical course, neuropathology and brain lipid composition in this Gaucher disease variant Acta Neuropathol. 97 1999 91 97 (Pubitemid 29132651)
    • (1999) Acta Neuropathologica , vol.97 , Issue.1 , pp. 91-97
    • 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
  • 109
    • 77958185918 scopus 로고    scopus 로고
    • Saposin C mutations in Gaucher disease patients resulting in lysosomal lipid accumulation, saposin C deficiency, but normal prosaposin processing and sorting
    • A.M. Vaccaro, M. Motta, M. Tatti, S. Scarpa, L. Masuelli, M. Bhat, M.T. Vanier, A. Tylki-Szymanska, and R. Salvioli Saposin C mutations in Gaucher disease patients resulting in lysosomal lipid accumulation, saposin C deficiency, but normal prosaposin processing and sorting Hum. Mol. Genet. 19 2010 2987 2997
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2987-2997
    • Vaccaro, A.M.1    Motta, M.2    Tatti, M.3    Scarpa, S.4    Masuelli, L.5    Bhat, M.6    Vanier, M.T.7    Tylki-Szymanska, A.8    Salvioli, R.9
  • 113
    • 84871720426 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein interacts with glucocerebrosidase and inhibits enzyme activity
    • T.L. Yap, A. Velayati, E. Sidransky, and J.C. Lee Membrane-bound alpha-synuclein interacts with glucocerebrosidase and inhibits enzyme activity Mol. Genet. Metab. 108 2013 56 64
    • (2013) Mol. Genet. Metab. , vol.108 , pp. 56-64
    • Yap, T.L.1    Velayati, A.2    Sidransky, E.3    Lee, J.C.4
  • 114
    • 84886020944 scopus 로고    scopus 로고
    • Saposin C protects glucocerebrosidase against alpha-synuclein inhibition
    • T.L. Yap, J.M. Gruschus, A. Velayati, E. Sidransky, and J.C. Lee Saposin C protects glucocerebrosidase against alpha-synuclein inhibition Biochemistry 52 2013 7161 7163
    • (2013) Biochemistry , vol.52 , pp. 7161-7163
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3    Sidransky, E.4    Lee, J.C.5
  • 115
    • 36048935960 scopus 로고    scopus 로고
    • LIMP-2 Is a Receptor for Lysosomal Mannose-6-Phosphate-Independent Targeting of β-Glucocerebrosidase
    • DOI 10.1016/j.cell.2007.10.018, PII S0092867407012901
    • D. Reczek, M. Schwake, J. Schroder, H. Hughes, J. Blanz, X. Jin, W. Brondyk, S. Van Patten, T. Edmunds, and P. Saftig LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase Cell 131 2007 770 783 (Pubitemid 350087202)
    • (2007) Cell , vol.131 , Issue.4 , pp. 770-783
    • Reczek, D.1    Schwake, M.2    Schroder, J.3    Hughes, H.4    Blanz, J.5    Jin, X.6    Brondyk, W.7    Van Patten, S.8    Edmunds, T.9    Saftig, P.10
  • 116
    • 0018821962 scopus 로고
    • Krabbe disease: A galactosylsphingosine (psychosine) lipidosis
    • L. Svennerholm, M.T. Vanier, and J.E. Mansson Krabbe disease: a galactosylsphingosine (psychosine) lipidosis J. Lipid Res. 21 1980 53 64 (Pubitemid 10120438)
    • (1980) Journal of Lipid Research , vol.21 , Issue.1 , pp. 53-64
    • Svennerholm, L.1    Vanier, M.T.2    Mansson, J.E.3
  • 117
    • 0022656315 scopus 로고
    • 3-neu5Ac- gangliotriaosylsphingosine) in G(M2) gangliodosis brain
    • S. Neuenhofer, E. Conzelmann, G. Schwarzmann, H. Egge, and K. Sandhoff Occurrence of lysoganglioside lyso-GM2 (II3-Neu5Ac-gangliotriaosylsphingosine) in GM2 gangliosidosis brain Biol. Chem. Hoppe Seyler 367 1986 241 244 (Pubitemid 16137509)
    • (1986) Biological Chemistry Hoppe-Seyler , vol.367 , Issue.3 , pp. 241-244
    • Neuenhofer, S.1    Conzelmann, E.2    Schwarzmann, G.3
  • 119
    • 0031932297 scopus 로고    scopus 로고
    • Twenty five years of the "psychosine hypothesis": A personal perspective of its history and present status
    • K. Suzuki Twenty five years of the "psychosine hypothesis": a personal perspective of its history and present status Neurochem. Res. 23 1998 251 259
    • (1998) Neurochem. Res. , vol.23 , pp. 251-259
    • Suzuki, K.1
  • 122
    • 0017184904 scopus 로고
    • Low molecular weight proteins in secondary lysosomes as activators of different sphingolipid hydrolases
    • W. Mraz, G. Fischer, and H. Jatzkewitz Low molecular weight proteins in secondary lysosomes as activators of different sphingolipid hydrolases FEBS Lett. 67 1976 104 109
    • (1976) FEBS Lett. , vol.67 , pp. 104-109
    • Mraz, W.1    Fischer, G.2    Jatzkewitz, H.3
  • 123
    • 0021026543 scopus 로고
    • Activator protein for the degradation of globotriaosylceramide by human α-galactosidase
    • S. Gartner, E. Conzelmann, and K. Sandhoff Activator protein for the degradation of globotriaosylceramide by human alpha-galactosidase J. Biol. Chem. 258 1983 12378 12385 (Pubitemid 14231163)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.20 , pp. 12378-12385
    • Gartner, S.1    Conzelmann, E.2    Sandhoff, K.3
  • 125
    • 0023919106 scopus 로고
    • Characterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipids
    • S.C. Li, S. Sonnino, G. Tettamanti, and Y.T. Li Characterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipids J. Biol. Chem. 263 1988 6588 6591
    • (1988) J. Biol. Chem. , vol.263 , pp. 6588-6591
    • Li, S.C.1    Sonnino, S.2    Tettamanti, G.3    Li, Y.T.4
  • 126
    • 0014806327 scopus 로고
    • Globoid cell leucodystrophy (Krabbe's disease): Deficiency of galactocerebroside beta-galactosidase
    • K. Suzuki, and Y. Suzuki Globoid cell leucodystrophy (Krabbe's disease): deficiency of galactocerebroside beta-galactosidase Proc. Natl. Acad. Sci. U. S. A. 66 1970 302 309
    • (1970) Proc. Natl. Acad. Sci. U. S. A. , vol.66 , pp. 302-309
    • Suzuki, K.1    Suzuki, Y.2
  • 127
    • 0002054185 scopus 로고    scopus 로고
    • Galactosylceramide lipidosis: Globoid cell leukodystrophy (Krabbe disease)
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, V. D. McGraw-Hill New York
    • D.A. Wenger, K. Suzuki, Y. Suzuki, and K. Suzuki Galactosylceramide lipidosis: globoid cell leukodystrophy (Krabbe disease) C.R. Scriver, A.L. Beaudet, W.S. Sly, V. D. The Metabolic and Molecular Bases of Inherited Disease 2001 McGraw-Hill New York
    • (2001) The Metabolic and Molecular Bases of Inherited Disease
    • Wenger, D.A.1    Suzuki, K.2    Suzuki, Y.3    Suzuki, K.4
  • 128
    • 0030728211 scopus 로고    scopus 로고
    • Saposins (sap) A and C activate the degradation of galactosylceramide in living cells
    • DOI 10.1016/S0014-5793(97)01302-1, PII S0014579397013021
    • K. Harzer, B.C. Paton, H. Christomanou, M. Chatelut, T. Levade, M. Hiraiwa, and J.S. O'Brien Saposins (sap) A and C activate the degradation of galactosylceramide in living cells FEBS Lett. 417 1997 270 274 (Pubitemid 27511602)
    • (1997) FEBS Letters , vol.417 , Issue.3 , pp. 270-274
    • Harzer, K.1    Paton, B.C.2    Christomanou, H.3    Chatelut, M.4    Levade, T.5    Hiraiwa, M.6    O'Brien, J.S.7
  • 129
    • 0001745899 scopus 로고    scopus 로고
    • Niemann-Pick disease types A B: Acid sphingomyelinase deficiencies
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, V. D. McGraw-Hill New York
    • E.H. Schuchman, and R.J. Desnick Niemann-Pick disease types A B: acid sphingomyelinase deficiencies C.R. Scriver, A.L. Beaudet, W.S. Sly, V. D. The Metabolic and Molecular Bases of Inherited Disease 2001 McGraw-Hill New York 3589 3610
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3589-3610
    • Schuchman, E.H.1    Desnick, R.J.2
  • 130
    • 77649223760 scopus 로고    scopus 로고
    • The pathogenesis and treatment of acid sphingomyelinase-deficient Niemann-Pick disease
    • E.H. Schuchman The pathogenesis and treatment of acid sphingomyelinase-deficient Niemann-Pick disease Int. J. Clin. Pharmacol. Ther. 47 Suppl. 1 2009 S48 S57
    • (2009) Int. J. Clin. Pharmacol. Ther. , vol.47 , Issue.SUPPL. 1
    • Schuchman, E.H.1
  • 132
    • 77954709548 scopus 로고    scopus 로고
    • The acid sphingomyelinase/ceramide pathway: Biomedical significance and mechanisms of regulation
    • Y.H. Zeidan, and Y.A. Hannun The acid sphingomyelinase/ceramide pathway: biomedical significance and mechanisms of regulation Curr. Mol. Med. 10 2010 454 466
    • (2010) Curr. Mol. Med. , vol.10 , pp. 454-466
    • Zeidan, Y.H.1    Hannun, Y.A.2
  • 134
    • 0027932927 scopus 로고
    • Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells
    • D. Graber, R. Salvayre, and T. Levade Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells J. Neurochem. 63 1994 1060 1068 (Pubitemid 24266620)
    • (1994) Journal of Neurochemistry , vol.63 , Issue.3 , pp. 1060-1068
    • Graber, D.1    Salvayre, R.2    Levade, T.3
  • 135
    • 0035077616 scopus 로고    scopus 로고
    • Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins
    • DOI 10.1515/BC.2001.035
    • T. Linke, G. Wilkening, S. Lansmann, H. Moczall, O. Bartelsen, J. Weisgerber, and K. Sandhoff Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins Biol. Chem. 382 2001 283 290 (Pubitemid 32243936)
    • (2001) Biological Chemistry , vol.382 , Issue.2 , pp. 283-290
    • Linke, T.1    Wilkening, G.2    Lansmann, S.3    Moczall, H.4    Bartelsen, O.5    Weisgerber, J.6    Sandhoff, K.7
  • 137
    • 0037135572 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate, a key cell signaling molecule
    • DOI 10.1074/jbc.R200007200
    • S. Spiegel, and S. Milstien Sphingosine 1-phosphate, a key cell signaling molecule J. Biol. Chem. 277 2002 25851 25854 (Pubitemid 34967061)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 25851-25854
    • Spiegel, S.1    Milstien, S.2
  • 139
    • 74149083982 scopus 로고    scopus 로고
    • Deregulation of sphingolipid metabolism in Alzheimer's disease
    • X. He, Y. Huang, B. Li, C.X. Gong, and E.H. Schuchman Deregulation of sphingolipid metabolism in Alzheimer's disease Neurobiol. Aging 31 2010 398 408
    • (2010) Neurobiol. Aging , vol.31 , pp. 398-408
    • He, X.1    Huang, Y.2    Li, B.3    Gong, C.X.4    Schuchman, E.H.5
  • 141
    • 84878418606 scopus 로고    scopus 로고
    • Recombinant human acid sphingomyelinase as an adjuvant to sorafenib treatment of experimental liver cancer
    • R. Savic, X. He, I. Fiel, and E.H. Schuchman Recombinant human acid sphingomyelinase as an adjuvant to sorafenib treatment of experimental liver cancer PLoS One 8 2013 e65620
    • (2013) PLoS One , vol.8 , pp. 65620
    • Savic, R.1    He, X.2    Fiel, I.3    Schuchman, E.H.4
  • 144
    • 34247554203 scopus 로고    scopus 로고
    • Acid ceramidase is a novel factor required for early embryo survival
    • DOI 10.1096/fj.06-7016com
    • E. Eliyahu, J.H. Park, N. Shtraizent, X. He, and E.H. Schuchman Acid ceramidase is a novel factor required for early embryo survival FASEB J. 21 2007 1403 1409 (Pubitemid 46684843)
    • (2007) FASEB Journal , vol.21 , Issue.7 , pp. 1403-1409
    • Eliyahu, E.1    Park, J.-H.2    Shtraizent, N.3    He, X.4    Schuchman, E.H.5
  • 146
    • 0021233226 scopus 로고
    • Diagnosis of infantile and juvenile forms of G(M2)-gangliosidosis variant 0. Residual activities toward natural and different synthetic substrates
    • H.J. Kytzia, U. Hinrichs, and K. Sandhoff Diagnosis of infantile and juvenile forms of GM2 gangliosidosis variant 0. Residual activities toward natural and different synthetic substrates Hum. Genet. 67 1984 414 418 (Pubitemid 14047392)
    • (1984) Human Genetics , vol.67 , Issue.4 , pp. 414-418
    • Kytzia, H.-J.1    Hinrichs, U.2    Sandhoff, K.3
  • 147
    • 0026572112 scopus 로고
    • Quantitative correlation between the residual activity of beta-hexosaminidase A and arylsulfatase A and the severity of the resulting lysosomal storage disease
    • P. Leinekugel, S. Michel, E. Conzelmann, and K. Sandhoff Quantitative correlation between the residual activity of beta-hexosaminidase A and arylsulfatase A and the severity of the resulting lysosomal storage disease Hum. Genet. 88 1992 513 523
    • (1992) Hum. Genet. , vol.88 , pp. 513-523
    • Leinekugel, P.1    Michel, S.2    Conzelmann, E.3    Sandhoff, K.4
  • 148
    • 0016201884 scopus 로고
    • Replacement therapy for inherited enzyme deficiency. Use of purified glucocerebrosidase in Gaucher's disease
    • R.O. Brady, P.G. Pentchev, A.E. Gal, S.R. Hibbert, and A.S. Dekaban Replacement therapy for inherited enzyme deficiency. Use of purified glucocerebrosidase in Gaucher's disease N. Engl. J. Med. 291 1974 989 993
    • (1974) N. Engl. J. Med. , vol.291 , pp. 989-993
    • Brady, R.O.1    Pentchev, P.G.2    Gal, A.E.3    Hibbert, S.R.4    Dekaban, A.S.5
  • 150
    • 0025236339 scopus 로고
    • Therapeutic response to intravenous infusions of glucocerebrosidase in a patient with Gaucher disease
    • N.W. Barton, F.S. Furbish, G.J. Murray, M. Garfield, and R.O. Brady Therapeutic response to intravenous infusions of glucocerebrosidase in a patient with Gaucher disease Proc. Natl. Acad. Sci. U. S. A. 87 1990 1913 1916
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 1913-1916
    • Barton, N.W.1    Furbish, F.S.2    Murray, G.J.3    Garfield, M.4    Brady, R.O.5
  • 151
    • 84872479464 scopus 로고    scopus 로고
    • Enzyme replacement therapy for lysosomal diseases: Lessons from 20 years of experience and remaining challenges
    • R.J. Desnick, and E.H. Schuchman Enzyme replacement therapy for lysosomal diseases: lessons from 20 years of experience and remaining challenges Annu. Rev. Genomics Hum. Genet. 13 2012 307 335
    • (2012) Annu. Rev. Genomics Hum. Genet. , vol.13 , pp. 307-335
    • Desnick, R.J.1    Schuchman, E.H.2
  • 154
    • 84883742110 scopus 로고    scopus 로고
    • Long-term outcome of enzyme-replacement therapy in advanced Fabry disease: Evidence for disease progression towards serious complications
    • F. Weidemann, M. Niemann, S. Stork, F. Breunig, M. Beer, C. Sommer, S. Herrmann, G. Ertl, and C. Wanner Long-term outcome of enzyme-replacement therapy in advanced Fabry disease: evidence for disease progression towards serious complications J. Intern. Med. 274 2013 331 341
    • (2013) J. Intern. Med. , vol.274 , pp. 331-341
    • Weidemann, F.1    Niemann, M.2    Stork, S.3    Breunig, F.4    Beer, M.5    Sommer, C.6    Herrmann, S.7    Ertl, G.8    Wanner, C.9
  • 155
    • 70449088871 scopus 로고    scopus 로고
    • GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2 +)-dependent mitochondrial apoptosis
    • R. Sano, I. Annunziata, A. Patterson, S. Moshiach, E. Gomero, J. Opferman, M. Forte, and A. d'Azzo GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2 +)-dependent mitochondrial apoptosis Mol. Cell 36 2009 500 511
    • (2009) Mol. Cell , vol.36 , pp. 500-511
    • Sano, R.1    Annunziata, I.2    Patterson, A.3    Moshiach, S.4    Gomero, E.5    Opferman, J.6    Forte, M.7    D'Azzo, A.8
  • 157
    • 34948880765 scopus 로고    scopus 로고
    • Oral maintenance clinical trial with miglustat for type I Gaucher disease: Switch from or combination with intravenous enzyme replacement
    • DOI 10.1182/blood-2007-02-075960
    • D. Elstein, A. Dweck, D. Attias, I. Hadas-Halpern, S. Zevin, G. Altarescu, J.F. Aerts, S. van Weely, and A. Zimran Oral maintenance clinical trial with miglustat for type I Gaucher disease: switch from or combination with intravenous enzyme replacement Blood 110 2007 2296 2301 (Pubitemid 47523147)
    • (2007) Blood , vol.110 , Issue.7 , pp. 2296-2301
    • Elstein, D.1    Dweck, A.2    Attias, D.3    Hadas-Halpern, I.4    Zevin, S.5    Altarescu, G.6    Aerts, J.F.M.G.7    Van Weely, S.8    Zimran, A.9
  • 158
    • 0036308444 scopus 로고    scopus 로고
    • Low-dose N-butyldeoxynojirimycin (OGT 918) for type I Gaucher disease
    • DOI 10.1006/bcmd.2002.0497
    • R. Heitner, D. Elstein, J. Aerts, S. Weely, and A. Zimran Low-dose N-butyldeoxynojirimycin (OGT 918) for type I Gaucher disease Blood Cells Mol. Dis. 28 2002 127 133 (Pubitemid 34743745)
    • (2002) Blood Cells, Molecules, and Diseases , vol.28 , Issue.2 , pp. 127-133
    • Heitner, R.1    Elstein, D.2    Aerts, J.3    Zimran, A.4
  • 159
    • 44049107178 scopus 로고    scopus 로고
    • Review of miglustat for clinical management in Gaucher disease type I
    • C. Ficicioglu Review of miglustat for clinical management in Gaucher disease type 1 Ther. Clin. Risk Manag. 4 2008 425 431 (Pubitemid 351712001)
    • (2008) Therapeutics and Clinical Risk Management , vol.4 , Issue.2 , pp. 425-431
    • Ficicioglu, C.1
  • 160
    • 37349013379 scopus 로고    scopus 로고
    • A counterintuitive approach to treat enzyme deficiencies: Use of enzyme inhibitors for restoring mutant enzyme activity
    • J.Q. Fan A counterintuitive approach to treat enzyme deficiencies: use of enzyme inhibitors for restoring mutant enzyme activity Biol. Chem. 389 2008 1 11
    • (2008) Biol. Chem. , vol.389 , pp. 1-11
    • Fan, J.Q.1
  • 161
    • 0033018496 scopus 로고    scopus 로고
    • Accelerated transport and maturation of lysosomal α-galactosidase A in fabry lymphoblasts by an enzyme inhibitor
    • DOI 10.1038/4801
    • J.Q. Fan, S. Ishii, N. Asano, and Y. Suzuki Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor Nat. Med. 5 1999 112 115 (Pubitemid 29051008)
    • (1999) Nature Medicine , vol.5 , Issue.1 , pp. 112-115
    • Fan, J.-Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 162
    • 84856411368 scopus 로고    scopus 로고
    • Pharmacological chaperone therapy for Fabry disease
    • S. Ishii Pharmacological chaperone therapy for Fabry disease Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 88 2012 18 30
    • (2012) Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. , vol.88 , pp. 18-30
    • Ishii, S.1
  • 165
    • 1842741341 scopus 로고    scopus 로고
    • Pharmacological Enhancement of β-Hexosaminidase Activity in Fibroblasts from Adult Tay-Sachs and Sandhoff Patients
    • DOI 10.1074/jbc.M308523200
    • M.B. Tropak, S.P. Reid, M. Guiral, S.G. Withers, and D. Mahuran Pharmacological enhancement of beta-hexosaminidase activity in fibroblasts from adult Tay-Sachs and Sandhoff Patients J. Biol. Chem. 279 2004 13478 13487 (Pubitemid 38468872)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13478-13487
    • Tropak, M.B.1    Reid, S.P.2    Guiral, M.3    Withers, S.G.4    Mahuran, D.5
  • 166
    • 33645861655 scopus 로고    scopus 로고
    • Gene therapy for lysosomal storage diseases
    • M.S. Sands, and B.L. Davidson Gene therapy for lysosomal storage diseases Mol. Ther. 13 2006 839 849
    • (2006) Mol. Ther. , vol.13 , pp. 839-849
    • Sands, M.S.1    Davidson, B.L.2
  • 170
    • 5744238700 scopus 로고    scopus 로고
    • Cell mediated delivery system
    • W.S. F.M. Platt, Oxford Univ. Press Inc. New York
    • K. Dobrenis Cell mediated delivery system W.S. F.M. Platt, Lysosomal Disorders of the Brain 2004 Oxford Univ. Press Inc. New York 339 380
    • (2004) Lysosomal Disorders of the Brain , pp. 339-380
    • Dobrenis, K.1
  • 171
    • 11144325072 scopus 로고    scopus 로고
    • Allogeneic stem cell transplantation for the treatment of lysosomal and peroxisomal metabolic diseases
    • DOI 10.1007/s00281-004-0166-2
    • W. Krivit Allogeneic stem cell transplantation for the treatment of lysosomal and peroxisomal metabolic diseases Springer Semin. Immunopathol. 26 2004 119 132 (Pubitemid 40021961)
    • (2004) Springer Seminars in Immunopathology , vol.26 , Issue.1-2 , pp. 119-132
    • Krivit, W.1
  • 172
    • 0032693385 scopus 로고    scopus 로고
    • Bone marrow transplantation for globoid cell leukodystrophy, adrenoleukodystrophy, metachromatic leukodystrophy, and Hurler syndrome
    • DOI 10.1097/00062752-199911000-00004
    • W. Krivit, P. Aubourg, E. Shapiro, and C. Peters Bone marrow transplantation for globoid cell leukodystrophy, adrenoleukodystrophy, metachromatic leukodystrophy, and Hurler syndrome Curr. Opin. Hematol. 6 1999 377 382 (Pubitemid 29503144)
    • (1999) Current Opinion in Hematology , vol.6 , Issue.6 , pp. 377-382
    • Krivit, W.1    Aubourg, P.2    Shapiro, E.3    Peters, C.4
  • 173
    • 0032941197 scopus 로고    scopus 로고
    • Bone marrow transplantation as effective treatment of central nervous system disease in globoid cell leukodystrophy, metachromatic leukodystrophy, adrenoleukodystrophy, mannosidosis, fucosidosis, aspartylglucosaminuria, Hurler, Maroteaux-Lamy, and Sly syndromes, and Gaucher disease type III
    • DOI 10.1097/00019052-199904000-00007
    • W. Krivit, C. Peters, and E.G. Shapiro Bone marrow transplantation as effective treatment of central nervous system disease in globoid cell leukodystrophy, metachromatic leukodystrophy, adrenoleukodystrophy, mannosidosis, fucosidosis, aspartylglucosaminuria, Hurler, Maroteaux-Lamy, and Sly syndromes, and Gaucher disease type III Curr. Opin. Neurol. 12 1999 167 176 (Pubitemid 29209802)
    • (1999) Current Opinion in Neurology , vol.12 , Issue.2 , pp. 167-176
    • Krivit, W.1    Peters, C.2    Shapiro, E.G.3
  • 176
    • 84860877959 scopus 로고    scopus 로고
    • Lysosomal lipid storage diseases
    • pii: a004804. doi: 10.1101/cshperspect.a004804
    • H. Schulze, and K. Sandhoff Lysosomal lipid storage diseases Cold Spring Harb Perspect Biol 3 2011 pii: a004804. doi: 10.1101/cshperspect.a004804
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Schulze, H.1    Sandhoff, K.2
  • 177
    • 0842330527 scopus 로고    scopus 로고
    • Photoaffinity labelling of the Human GM2-activator protein Mechanistic insight into ganglioside GM2 degradation
    • DOI 10.1111/j.1432-1033.2003.03964.x
    • M. Wendeler, J. Hörnschemeyer, D. Hoffmann, T. Kolter, G. Schwarzmann, and K. Sandhoff Photoaffinity labelling of the human GM2-activator protein. Mechanistic insight into ganglioside GM2 degradation Eur. J. Biochem. 271 2004 614 627 (Pubitemid 38183636)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.3 , pp. 614-627
    • Wendeler, M.1    Hoernschemeyer, J.2    Hoffmann, D.3    Kolter, T.4    Schwarzmann, G.5    Sandhoff, K.6
  • 178
    • 84892639259 scopus 로고    scopus 로고
    • A mutation in a ganglioside biosynthetic enzyme, ST3GAL5, results in salt & pepper syndrome, a neurocutaneous disorder with altered glycolipid and glycoprotein glycosylation
    • 10.1093/hmg/ddt434 (first published online: September 10, 2013)
    • L. Boccuto, K. Aoki, H. Flanagan-Steet, C.F. Chen, X. Fan, F. Bartel, M. Petukh, A. Pittman, R. Saul, A. Chaubey, E. Alexov, M. Tiemeyer, R. Steet, and C.E. Schwartz A mutation in a ganglioside biosynthetic enzyme, ST3GAL5, results in salt & pepper syndrome, a neurocutaneous disorder with altered glycolipid and glycoprotein glycosylation Hum. Mol. Genet. 2013 10.1093/hmg/ddt434 (first published online: September 10, 2013)
    • (2013) Hum. Mol. Genet.
    • Boccuto, L.1    Aoki, K.2    Flanagan-Steet, H.3    Chen, C.F.4    Fan, X.5    Bartel, F.6    Petukh, M.7    Pittman, A.8    Saul, R.9    Chaubey, A.10    Alexov, E.11    Tiemeyer, M.12    Steet, R.13    Schwartz, C.E.14
  • 190
    • 0030201110 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the mouse CGT gene encoding UDP-galactose ceramide-galactosyltransferase (cerebroside synthetase)
    • DOI 10.1006/geno.1996.0342
    • A. Bosio, E. Binczek, and W. Stoffel Molecular cloning and characterization of the mouse CGT gene encoding UDP-galactose ceramide-galactosyltransferase (cerebroside synthetase) Genomics 35 1996 223 226 (Pubitemid 26236171)
    • (1996) Genomics , vol.35 , Issue.1 , pp. 223-226
    • Bosio, A.1    Binczek, E.2    Stoffel, W.3
  • 191
    • 0030200940 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal mapping, and characterization of the mouse UDP-galactose:ceramide galactosyltransferase gene
    • DOI 10.1006/geno.1996.0341
    • T. Coetzee, X. Li, N. Fujita, J. Marcus, K. Suzuki, U. Francke, and B. Popko Molecular cloning, chromosomal mapping, and characterization of the mouse UDP-galactose:ceramide galactosyltransferase gene Genomics 35 1996 215 222 (Pubitemid 26236170)
    • (1996) Genomics , vol.35 , Issue.1 , pp. 215-222
    • Coetzee, T.1    Li, X.2    Fujita, N.3    Marcus, J.4    Suzuki, K.5    Francke, U.6    Popko, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.