메뉴 건너뛰기




Volumn 312, Issue 9, 2006, Pages 1540-1553

Palmitoyl protein thioesterase 1 (PPT1) deficiency causes endocytic defects connected to abnormal saposin processing

Author keywords

Endocytic pathway; Palmitoyl protein thioesterase 1; Saposin processing

Indexed keywords

MARKER; PALMITOYL PROTEIN THIOESTERASE; PALMITOYL PROTEIN THIOESTERASE 1; PROSAPOSIN; SPHINGOLIPID ACTIVATOR PROTEIN; SPHINGOLIPID ACTIVATOR PROTEIN A; SPHINGOLIPID ACTIVATOR PROTEIN D; UNCLASSIFIED DRUG;

EID: 33646490721     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.01.034     Document Type: Article
Times cited : (28)

References (50)
  • 1
    • 0015595210 scopus 로고
    • Infantile type of so-called neuronal ceroid-lipofuscinosis. A clinical study of 15 patients
    • Santavuori P., Haltia M., Rapola J., and Raitta C. Infantile type of so-called neuronal ceroid-lipofuscinosis. A clinical study of 15 patients. J. Neurol. Sci. 18 (1973) 257-267
    • (1973) J. Neurol. Sci. , vol.18 , pp. 257-267
    • Santavuori, P.1    Haltia, M.2    Rapola, J.3    Raitta, C.4
  • 2
    • 0028879016 scopus 로고
    • The neuronal ceroid-lipofuscinoses
    • Goebel H.H. The neuronal ceroid-lipofuscinoses. J. Child Neurol. 10 (1995) 424-437
    • (1995) J. Child Neurol. , vol.10 , pp. 424-437
    • Goebel, H.H.1
  • 3
    • 0027224115 scopus 로고
    • Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis
    • Tyynelä J., Palmer D.N., Baumann M., and Haltia M. Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis. FEBS Lett. 330 (1993) 8-12
    • (1993) FEBS Lett. , vol.330 , pp. 8-12
    • Tyynelä, J.1    Palmer, D.N.2    Baumann, M.3    Haltia, M.4
  • 4
    • 0029788513 scopus 로고    scopus 로고
    • Lipid thioesters accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase
    • Lu J.Y., Verkruyse L.A., and Hoffman S.L. Lipid thioesters accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 10046-10050
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 10046-10050
    • Lu, J.Y.1    Verkruyse, L.A.2    Hoffman, S.L.3
  • 5
    • 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 (1988) 317-328
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 317-328
    • Fürst, W.1    Machleidt, W.2    Sandhoff, K.3
  • 6
    • 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 (1992) 1-16
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 1-16
    • Fürst, W.1    Sandhoff, K.2
  • 7
    • 0030727680 scopus 로고    scopus 로고
    • Biochemistry of glycosphingolipid degradation
    • Sandhoff K., and Kolter T. Biochemistry of glycosphingolipid degradation. Clin Chim Acta 266 (1997) 51-61
    • (1997) Clin Chim Acta , vol.266 , pp. 51-61
    • Sandhoff, K.1    Kolter, T.2
  • 8
    • 0025294786 scopus 로고
    • Distribution of saposin proteins (sphingolipid activator proteins) in lysosomal storage and other diseases
    • Morimoto S., Yamamoto Y., O'Brien J.S., and Kishimoto Y. Distribution of saposin proteins (sphingolipid activator proteins) in lysosomal storage and other diseases. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 3493-3497
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3493-3497
    • Morimoto, S.1    Yamamoto, Y.2    O'Brien, J.S.3    Kishimoto, Y.4
  • 9
    • 0037339630 scopus 로고    scopus 로고
    • Analysis of phospholipid molecular species in brains from patients with infantile and juvenile neuronal-ceroid lipofuscinosis using liquid chromatography-electrospray ionization mass spectrometry
    • Käkelä A., Somerharju P., and Tyynelä J. Analysis of phospholipid molecular species in brains from patients with infantile and juvenile neuronal-ceroid lipofuscinosis using liquid chromatography-electrospray ionization mass spectrometry. J. Neurochem. 84 (2003) 1051-1065
    • (2003) J. Neurochem. , vol.84 , pp. 1051-1065
    • Käkelä, A.1    Somerharju, P.2    Tyynelä, J.3
  • 10
    • 0027518208 scopus 로고
    • Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras
    • Camp L.A., and Hofmann S.L. Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras. J. Biol. Chem. 268 (1993) 22566-22574
    • (1993) J. Biol. Chem. , vol.268 , pp. 22566-22574
    • Camp, L.A.1    Hofmann, S.L.2
  • 11
    • 0029843717 scopus 로고    scopus 로고
    • Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis
    • Hellsten E., Vesa J., Olkkonen V.M., Jalanko A., and Peltonen L. Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis. EMBO J. 15 (1996) 5240-5245
    • (1996) EMBO J. , vol.15 , pp. 5240-5245
    • Hellsten, E.1    Vesa, J.2    Olkkonen, V.M.3    Jalanko, A.4    Peltonen, L.5
  • 13
    • 0035167162 scopus 로고    scopus 로고
    • Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles: implications for infantile neuronal ceroid lipofuscinosis (INCL)
    • Lehtovirta M., Kyttälä A., Eskelinen E.-L., Hess M., Heinonen O., and Jalanko A. Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles: implications for infantile neuronal ceroid lipofuscinosis (INCL). Hum. Mol. Gen. 10 (2001) 69-75
    • (2001) Hum. Mol. Gen. , vol.10 , pp. 69-75
    • Lehtovirta, M.1    Kyttälä, A.2    Eskelinen, E.-L.3    Hess, M.4    Heinonen, O.5    Jalanko, A.6
  • 14
    • 0036407350 scopus 로고    scopus 로고
    • Status epilepticus induces changes in the expression and localization of endogenous palmitoyl protein thioesterase 1
    • Suopanki J., Lintunen M., Lahtinen H., Haltia M., Panula P., Baumann M., and Tyynelä J. Status epilepticus induces changes in the expression and localization of endogenous palmitoyl protein thioesterase 1. Neurobiol. Dis. 10 (2002) 247-257
    • (2002) Neurobiol. Dis. , vol.10 , pp. 247-257
    • Suopanki, J.1    Lintunen, M.2    Lahtinen, H.3    Haltia, M.4    Panula, P.5    Baumann, M.6    Tyynelä, J.7
  • 15
    • 0037434057 scopus 로고    scopus 로고
    • Palmitoyl protein thioesterase 1 is targeted to the axons in neurons
    • Ahtiainen L., Van Diggelen O.P., Jalanko A., and Kopra O. Palmitoyl protein thioesterase 1 is targeted to the axons in neurons. J. Comp. Neurol. 455 (2003) 368-377
    • (2003) J. Comp. Neurol. , vol.455 , pp. 368-377
    • Ahtiainen, L.1    Van Diggelen, O.P.2    Jalanko, A.3    Kopra, O.4
  • 16
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • Kamal A., Almenar-Queralt A., LeBlanc J.F., Roberts E.A., and Goldstein L.S. Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414 (2001) 643-648
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 17
    • 0034772310 scopus 로고    scopus 로고
    • CLN3 protein is targeted to neuronal synapses but excluded from synaptic vesicles: new clues to Batten disease
    • Luiro K., Kopra O., Lehtovirta M., and Jalanko A. CLN3 protein is targeted to neuronal synapses but excluded from synaptic vesicles: new clues to Batten disease. Hum. Mol. Genet. 10 (2001) 2123-2131
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2123-2131
    • Luiro, K.1    Kopra, O.2    Lehtovirta, M.3    Jalanko, A.4
  • 18
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan G., Parenti M., and Magee A.I. The dynamic role of palmitoylation in signal transduction. Trends Biochem. Sci. 20 (1995) 181-187
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 181-187
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 19
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby S.M. Reversible palmitoylation of signaling proteins. Curr. Opin. Cell Biol. 9 (1997) 148-154
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 21
    • 0029835573 scopus 로고    scopus 로고
    • Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization
    • Riikonen A., Rouvinen J., Tikkanen R., Julkunen I., Peltonen L., and Jalanko A. Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization. J. Biol. Chem. 271 (1996) 21340-21344
    • (1996) J. Biol. Chem. , vol.271 , pp. 21340-21344
    • Riikonen, A.1    Rouvinen, J.2    Tikkanen, R.3    Julkunen, I.4    Peltonen, L.5    Jalanko, A.6
  • 22
    • 0031921773 scopus 로고    scopus 로고
    • Fluid-phase markers in the basolateral endocytic pathway accumulate in response to the actin assembly-promoting drug Jasplakinolide
    • Shurety W., Stewart N.L., and Stow J.L. Fluid-phase markers in the basolateral endocytic pathway accumulate in response to the actin assembly-promoting drug Jasplakinolide. Mol. Biol. Cell 9 (1998) 957-975
    • (1998) Mol. Biol. Cell , vol.9 , pp. 957-975
    • Shurety, W.1    Stewart, N.L.2    Stow, J.L.3
  • 23
    • 0024525180 scopus 로고
    • Fluorescent labeling of endocytic compartments
    • Swanson J. Fluorescent labeling of endocytic compartments. Methods Cell Biol. 29 (1989) 137-151
    • (1989) Methods Cell Biol. , vol.29 , pp. 137-151
    • Swanson, J.1
  • 24
    • 0027419879 scopus 로고
    • Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport
    • Hollenbeck P.J. Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport. J. Cell Biol. 121 (1993) 305-315
    • (1993) J. Cell Biol. , vol.121 , pp. 305-315
    • Hollenbeck, P.J.1
  • 25
    • 0026089364 scopus 로고
    • Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
    • Ikonen E., Baumann M., Grön K., Syvänen A.C., Enomaa N., Halila R., Aula P., and Peltonen L. Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J. 10 (1991) 51-58
    • (1991) EMBO J. , vol.10 , pp. 51-58
    • Ikonen, E.1    Baumann, M.2    Grön, K.3    Syvänen, A.C.4    Enomaa, N.5    Halila, R.6    Aula, P.7    Peltonen, L.8
  • 26
    • 0025149021 scopus 로고
    • Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid
    • Alvarez E., Girones N., and Davis R.J. Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid. J. Biol. Chem. 265 (1990) 16644-16655
    • (1990) J. Biol. Chem. , vol.265 , pp. 16644-16655
    • Alvarez, E.1    Girones, N.2    Davis, R.J.3
  • 27
    • 0000857916 scopus 로고    scopus 로고
    • Sphingolipid activator proteins
    • Scriver C.R., Beaudet A.L., and Sly W.S. (Eds), McGraw-Hill, New York, NY
    • Sandhoff K., Kolter T., and Harzer K. Sphingolipid activator proteins. In: Scriver C.R., Beaudet A.L., and Sly W.S. (Eds). The Metabolic and Molecular Basis of Inherited Disease (2001), McGraw-Hill, New York, NY 3371-3388
    • (2001) The Metabolic and Molecular Basis of Inherited Disease , pp. 3371-3388
    • Sandhoff, K.1    Kolter, T.2    Harzer, K.3
  • 28
    • 0032541422 scopus 로고    scopus 로고
    • Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP)
    • Hiesberger T., Huttler S., Rohlmann A., Schneider W., Sandhoff K., and Herz J. Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP). EMBO J. 17 (1998) 4617-4625
    • (1998) EMBO J. , vol.17 , pp. 4617-4625
    • Hiesberger, T.1    Huttler, S.2    Rohlmann, A.3    Schneider, W.4    Sandhoff, K.5    Herz, J.6
  • 29
    • 0011913143 scopus 로고
    • Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman E.J., Siebers A., and Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 7972-7976
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 30
    • 0029730641 scopus 로고    scopus 로고
    • Biosynthesis, processing and targeting of sphingolipid activator protein (SAP) precursor in cultured human fibroblasts
    • Vielhaber G., Huewitz R., and Sandhoff K. Biosynthesis, processing and targeting of sphingolipid activator protein (SAP) precursor in cultured human fibroblasts. J. Biol. Chem. 271 (1996) 32438-32446
    • (1996) J. Biol. Chem. , vol.271 , pp. 32438-32446
    • Vielhaber, G.1    Huewitz, R.2    Sandhoff, K.3
  • 31
    • 0027945432 scopus 로고
    • 3-Methyladenine inhibits transport from late endosomes to lysosomes in cultured rat and mouse fibroblasts
    • Punnonen E.L., Marjomäki V.S., and Reunanen H. 3-Methyladenine inhibits transport from late endosomes to lysosomes in cultured rat and mouse fibroblasts. Eur. J. Cell Biol. 65 (1994) 14-25
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 14-25
    • Punnonen, E.L.1    Marjomäki, V.S.2    Reunanen, H.3
  • 33
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations
    • Cataldo A.M., Peterhoff C.M., Troncoso J.C., Gomez-Isla T., Hyman B.T., and Nixon R.A. Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am. J. Pathol. 157 (2000) 277-286
    • (2000) Am. J. Pathol. , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 34
    • 0032568565 scopus 로고    scopus 로고
    • Abnormal transport along the lysosomal pathway in mucolipidosis, type IV disease
    • Chen C.S., Bach G., and Pagano R.E. Abnormal transport along the lysosomal pathway in mucolipidosis, type IV disease. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6373-6378
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6373-6378
    • Chen, C.S.1    Bach, G.2    Pagano, R.E.3
  • 36
    • 9744254471 scopus 로고    scopus 로고
    • Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway
    • Luiro K., Yliannala K., Ahtiainen L., Maunu H., Järvelä I., Kyttälä A., and Jalanko A. Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway. Hum. Mol. Genet. 13 (2004) 3017-3027
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3017-3027
    • Luiro, K.1    Yliannala, K.2    Ahtiainen, L.3    Maunu, H.4    Järvelä, I.5    Kyttälä, A.6    Jalanko, A.7
  • 37
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations
    • Cataldo A.M., Peterhoff C.M., Troncoso J.C., Gomez-Isla T., Hyman B.T., and Nixon R.A. Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am. J. Pathol. 157 (2000) 277-286
    • (2000) Am. J. Pathol. , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 39
    • 0037436836 scopus 로고    scopus 로고
    • The yeast model for Batten disease: a role for Btn2p in the trafficking of the Golgi-associated vesicular targeting protein, Yif1p
    • Chattopadhyay S., Roberts P.M., and Pearce D.A. The yeast model for Batten disease: a role for Btn2p in the trafficking of the Golgi-associated vesicular targeting protein, Yif1p. Biochem. Biophys. Res. Commun. 302 (2003) 534-538
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 534-538
    • Chattopadhyay, S.1    Roberts, P.M.2    Pearce, D.A.3
  • 40
    • 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 (1986) 15339-15343
    • (1986) J. Biol. Chem. , vol.261 , pp. 15339-15343
    • Fujibayashi, S.1    Wenger, D.A.2
  • 42
    • 0030610528 scopus 로고    scopus 로고
    • Bafilomycin A1 treatment retards transferring receptor recycling more than bulk membrane recycling
    • Presley J.F., Mayor S., McGraw T.E., Dunn K.W., and Maxfield F.R. Bafilomycin A1 treatment retards transferring receptor recycling more than bulk membrane recycling. J. Biol. Chem. 23 (1997) 13929-13936
    • (1997) J. Biol. Chem. , vol.23 , pp. 13929-13936
    • Presley, J.F.1    Mayor, S.2    McGraw, T.E.3    Dunn, K.W.4    Maxfield, F.R.5
  • 43
    • 0029160297 scopus 로고
    • Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump
    • Van Weert A.W., Dunn K.W., Gueze H.J., Maxfield F.R., and Stoorvogel V. Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump. J. Cell Biol. 130 (1995) 821-834
    • (1995) J. Cell Biol. , vol.130 , pp. 821-834
    • Van Weert, A.W.1    Dunn, K.W.2    Gueze, H.J.3    Maxfield, F.R.4    Stoorvogel, V.5
  • 44
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague M.J., Urbe S., Aniento F., and Gruenberg J. Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J. Biol. Chem. 269 (1994) 21-24
    • (1994) J. Biol. Chem. , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbe, S.2    Aniento, F.3    Gruenberg, J.4
  • 45
    • 4544262273 scopus 로고    scopus 로고
    • Defective acidification of intracellular organelles results in aberrant secretion of cathepsin D in cancer cells
    • Kokkonen N., Rivinoja A., Kauppila A., Suokas M., Kellokumpu I., and Kellokumpu S. Defective acidification of intracellular organelles results in aberrant secretion of cathepsin D in cancer cells. J. Biol. Chem. 279 (2004) 39982-39988
    • (2004) J. Biol. Chem. , vol.279 , pp. 39982-39988
    • Kokkonen, N.1    Rivinoja, A.2    Kauppila, A.3    Suokas, M.4    Kellokumpu, I.5    Kellokumpu, S.6
  • 47
    • 0030016109 scopus 로고    scopus 로고
    • Proteolytic processing patterns of prosaposin in insect and mammalian cells
    • Leonova T., Qi X., Bencosme A., Ponce E., Sun Y., and Grabowski G.A. Proteolytic processing patterns of prosaposin in insect and mammalian cells. J. Biol. Chem. 271 (1996) 17312-17320
    • (1996) J. Biol. Chem. , vol.271 , pp. 17312-17320
    • Leonova, T.1    Qi, X.2    Bencosme, A.3    Ponce, E.4    Sun, Y.5    Grabowski, G.A.6
  • 49
    • 0029864731 scopus 로고    scopus 로고
    • Functional organization of saposin C. Definition of the neurotrophic and acid beta-glucosidase activation regions
    • Qi X., Qin W., Sun Y., Kondoh K., and Grabowski G.A. Functional organization of saposin C. Definition of the neurotrophic and acid beta-glucosidase activation regions. J. Biol. Chem. 271 (1996) 6874-6880
    • (1996) J. Biol. Chem. , vol.271 , pp. 6874-6880
    • Qi, X.1    Qin, W.2    Sun, Y.3    Kondoh, K.4    Grabowski, G.A.5
  • 50
    • 0030727680 scopus 로고    scopus 로고
    • Biochemistry of glycosphingolipid degradation
    • Sandhoff K., and Kolter T. Biochemistry of glycosphingolipid degradation. Clin. Chim. Acta 266 (1997) 51-61
    • (1997) Clin. Chim. Acta , vol.266 , pp. 51-61
    • Sandhoff, K.1    Kolter, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.