메뉴 건너뛰기




Volumn 7, Issue 7, 1997, Pages 987-996

β1, 4 N-Acetylgalactosaminyltransferase (GM2/GD2/GA2 synthase) forms homodimers in the endoplasmic reticulum: A strategy to test for dimerization of Golgi membrane proteins

Author keywords

Ganglioside; Glycosyltransferase

Indexed keywords

N ACETYLGALACTOSAMINYLTRANSFERASE;

EID: 0030681358     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.7.987     Document Type: Article
Times cited : (21)

References (51)
  • 1
    • 0028926420 scopus 로고
    • ERGIC-53, a membrane protein of the endoplasmic reticulumGolgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells
    • Arar. C., Carpentier. V., Le Caer, J. -P., Monsigny. M., Legrand. A. and Roche. A. C. (1995) ERGIC-53, a membrane protein of the endoplasmic reticulumGolgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells. J. Biol. Client., 270, 3551-3553.
    • (1995) J. Biol. Client. , vol.270 , pp. 3551-3553
    • Arar, C.1    Carpentier, V.2    Le Caer, J.-P.3    Monsigny, M.4    Legrand, A.5    Roche, A.C.6
  • 4
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher. M. S. and Munro. S. (1993) Cholesterol and the Golgi apparatus. Science, 261, 1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 5
    • 0018700703 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate
    • ChamberlainJ. P. (1979) Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem., 98, 132-135.
    • (1979) Anal. Biochem. , vol.98 , pp. 132-135
    • Chamberlainj, P.1
  • 6
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan. G. I., Lewis. G. K., Ramsay, G. and Bishop, J. M. (1985) Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Dial, 5, 3610-3616.
    • (1985) Mol. Cell Dial , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 7
    • 0027522748 scopus 로고
    • Target sizes of galacto-syltransferase, sialyltransferase, and uridine diphosphatase in Golgi apparatus of rat liver
    • Fleischer. B., McIntyre, J. O. and Kempner. E. S. (1993) Target sizes of galacto-syltransferase, sialyltransferase, and uridine diphosphatase in Golgi apparatus of rat liver. Biochemistry, 32, 2076-2081.
    • (1993) Biochemistry , vol.32 , pp. 2076-2081
    • Fleischer, B.1    McIntyre, J.O.2    Kempner, E.S.3
  • 8
    • 0028947864 scopus 로고
    • Purification and characterization of heparan sulfate 6-sulfotransferase from the culture medium of Chinese hamster ovary cells
    • Habuchi, H., Habuchi. O. and Kimata, K. (1995) Purification and characterization of heparan sulfate 6-sulfotransferase from the culture medium of Chinese hamster ovary cells. J. Biol. Chem., 270, 4172-4179.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4172-4179
    • Habuchi, H.1    Habuchi, O.2    Kimata, K.3
  • 9
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C. and Helenius. A. (1995) Quality control in the secretory pathway. Ciirr. Opin. Cell Biol., 7, 523-529.
    • (1995) Ciirr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 10
    • 0028173085 scopus 로고
    • Isolation of GD3 synthase gene by expression cloning of GM3 alpha-2, 8-sialyItransferase cDNA using anti-GD2 monoclonal antibody
    • Haraguchi. M., Yamashiro. S., Yamamoto. A., Furukawa. K., Takamiya. K., Lloyd, K. O. and Shiku. H. (1994) Isolation of GD3 synthase gene by expression cloning of GM3 alpha-2, 8-sialyItransferase cDNA using anti-GD2 monoclonal antibody. Proc. Natl. Acad. Sci. USA, 91, 10455-10459.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10455-10459
    • Haraguchi, M.1    Yamashiro, S.2    Yamamoto, A.3    Furukawa, K.4    Takamiya, K.5    Lloyd, K.O.6    Shiku, H.7
  • 11
    • 0027368911 scopus 로고
    • Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 Nacetylgalactosaminyltransferase from mouse liver
    • Hashimoto. Y., Sekine. M., Iwasaki. K. and Suzuki, A. (1993) Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 Nacetylgalactosaminyltransferase from mouse liver. J. Biol. Client., 268, 25857-25864.
    • (1993) J. Biol. Client. , vol.268 , pp. 25857-25864
    • Hashimoto, Y.1    Sekine, M.2    Iwasaki, K.3    Suzuki, A.4
  • 12
    • 0029746154 scopus 로고    scopus 로고
    • Expression cloning of Forssman glycolipid synthetase: A novel member of the histo-blood group ABO gene family
    • Haslam. D. B. and Baenziger. J. U. (1996) Expression cloning of Forssman glycolipid synthetase: A novel member of the histo-blood group ABO gene family. Proc. Natl. Acad. Sci. USA, 93, 10697-10702.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10697-10702
    • Haslam, D.B.1    Baenziger, J.U.2
  • 13
    • 0028230361 scopus 로고
    • Defining the minimal size of catalytically active primate a 1, 3 galactosyltransferase: Structurefunction studies on the recombinant truncated enzyme
    • Henion. T. R., Macher, B. A., Anaraki. F. and Galili. U. (1994) Defining the minimal size of catalytically active primate a 1, 3 galactosyltransferase: structurefunction studies on the recombinant truncated enzyme. Glycobiology, 4, 193-202.
    • (1994) Glycobiology , vol.4 , pp. 193-202
    • Henion, T.R.1    Macher, B.A.2    Anaraki, F.3    Galili, U.4
  • 14
    • 0029895702 scopus 로고    scopus 로고
    • Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis
    • Ichikawa, S., Sakiyama. H., Suzuki. G., Hidari. K. I. P. J. and Hirabayashi. Y. (1996) Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc. Natl. Acad Sci. USA, 93, 4638-4643.
    • (1996) Proc. Natl. Acad Sci. USA , vol.93 , pp. 4638-4643
    • Ichikawa, S.1    Sakiyama, H.2    Suzuki, G.3    Hidari, K.I.4    Hirabayashi, Y.5
  • 15
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M. R., Nilsson, T. and Peterson. P. A. (1993) Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol., 121, 317-333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 16
    • 0029662225 scopus 로고    scopus 로고
    • βl, 4 N-acetylgalactosaminyltransferase (GM2 synthase) is released from Golgi membranes as a neuraminidase sensitive, disulfide-bonded dimer by a cathepsin D-like protease
    • Jaskiewicz. E., Zhu. G., Bassi. R., Darling, D. S. and Young. W. W. (1996a) βl, 4 N-acetylgalactosaminyltransferase (GM2 synthase) is released from Golgi membranes as a neuraminidase sensitive, disulfide-bonded dimer by a cathepsin D-like protease. J. Biol. Client., 271, 26395-26403.
    • (1996) J. Biol. Client. , vol.271 , pp. 26395-26403
    • Jaskiewicz, E.1    Zhu, G.2    Bassi, R.3    Darling, D.S.4    Young, W.W.5
  • 17
    • 0030007254 scopus 로고    scopus 로고
    • Cloned βl, 4 N-acetylgalactosaminyltransferase: Subcellular localization and formation of disulfide bonded species
    • Jaskiewicz. E., Zhu, G., Taatjes. D. J., Darling, D. S., Zwanzig, G. E., and Young. W. W. (1996b) Cloned βl, 4 N-acetylgalactosaminyltransferase: subcellular localization and formation of disulfide bonded species. Glycoconjugate J., 13, 213-223.
    • (1996) Glycoconjugate J. , vol.13 , pp. 213-223
    • Jaskiewicz, E.1    Zhu, G.2    Taatjes, D.J.3    Darling, D.S.4    Zwanzig, G.E.5    Young, W.W.6
  • 18
    • 0027245456 scopus 로고
    • Novel predictions from radiation target analysis
    • Kempner. E. S. (1993) Novel predictions from radiation target analysis. Trends Kochern. Sei., 18, 236-239.
    • (1993) Trends Kochern. Sei. , vol.18 , pp. 236-239
    • Kempner, E.S.1
  • 19
    • 0029970785 scopus 로고    scopus 로고
    • Role of the cysteine residues in the alphal, 2-mannosidase involved in N-glycan biosynthesis in Saccharomyces cerevisiae
    • Lipari. F. and Herscovics. A. (1996) Role of the cysteine residues in the alphal, 2-mannosidase involved in N-glycan biosynthesis in Saccharomyces cerevisiae. J. Biol. Client., 271, 27615-27622.
    • (1996) J. Biol. Client. , vol.271 , pp. 27615-27622
    • Lipari, F.1    Herscovics, A.2
  • 20
    • 0023838784 scopus 로고
    • Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi
    • Lodish. H. F. (1988) Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi. J. Biol. Cltem., 263, 2107-2110.
    • (1988) J. Biol. Cltem. , vol.263 , pp. 2107-2110
    • Lodish, H.F.1
  • 21
    • 0029910016 scopus 로고    scopus 로고
    • The minimum functional unit of human P-glycoprotein appears to be a monomer
    • Loo, T. W. and Clarke, D. M. (1996) The minimum functional unit of human P-glycoprotein appears to be a monomer. J. Biol. Client., 271, 27488-27492.
    • (1996) J. Biol. Client. , vol.271 , pp. 27488-27492
    • Loo, T.W.1    Clarke, D.M.2
  • 23
    • 0029871352 scopus 로고    scopus 로고
    • A disulfide-bonded dimer of the Golgi βgalactoside a2, 6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose
    • Ma, J. Y. and Colley. K. J. (1996) A disulfide-bonded dimer of the Golgi βgalactoside a2, 6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose. J. Biol. Client., 271, 7758-7766.
    • (1996) J. Biol. Client. , vol.271 , pp. 7758-7766
    • Ma, J.Y.1    Colley, K.J.2
  • 24
    • 0027640284 scopus 로고
    • Targeting and retention of Golgi membrane proteins
    • Machamer, C. E. (1993) Targeting and retention of Golgi membrane proteins. Curr. Opin. Cell Biol., 5, 606-612.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 606-612
    • Machamer, C.E.1
  • 25
    • 0030036056 scopus 로고    scopus 로고
    • Recombinant soluble beta-l, 4-galactosyltransferases expressed in Saccharomyces cerevisiae: Purification, characterization and comparison with human enzyme
    • Malissard, M., Borsig. L., DiMarco. S., Griitter. M. G., Kragl. U., Wandrey. C. and Berger. E. G. (1996) Recombinant soluble beta-l, 4-galactosyltransferases expressed in Saccharomyces cerevisiae: purification, characterization and comparison with human enzyme. Ear. J. Biochem., 239, 340-348.
    • (1996) Ear. J. Biochem. , vol.239 , pp. 340-348
    • Malissard, M.1    Borsig, L.2    Dimarco, S.3    Griitter, M.G.4    Kragl, U.5    Wandrey, C.6    Berger, E.G.7
  • 26
    • 0028341131 scopus 로고
    • A monomeric protein in the Golgi membrane catalyzes both W-deacetylation and W-sulfation of heparan sulfate
    • Mandon, E. C, Kempner. E. S., Ishihara. M. and Hirschberg. C. B. (1994a) A monomeric protein in the Golgi membrane catalyzes both W-deacetylation and W-sulfation of heparan sulfate. J. Biol. Client., 269, 11729-11733.
    • (1994) J. Biol. Client. , vol.269 , pp. 11729-11733
    • Mandon, E.C.1    Kempner, E.S.2    Ishihara, M.3    Hirschberg, C.B.4
  • 27
    • 0027996905 scopus 로고
    • Purification of the Golgi adenosine 3'-phosphate 5'-phosphosulfate transporter, a homodimer within the membrane
    • Mandon, E. C, Milla. M. E., Kempner. E. and Hirschberg. C. B. (1994b) Purification of the Golgi adenosine 3'-phosphate 5'-phosphosulfate transporter, a homodimer within the membrane. Proc. Natl. Acad. Sci. USA, 91, 1070710711.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1070710711
    • Mandon, E.C.1    Milla, M.E.2    Kempner, E.3    Hirschberg, C.B.4
  • 28
    • 0025948387 scopus 로고
    • Novel purification of the catalytic domain of Golgi alpha-mannosidase II: Characterization and comparison with the intact enzyme
    • Moremen. K. W., Touster. O. and Robbins. P. W. (1991) Novel purification of the catalytic domain of Golgi alpha-mannosidase II: characterization and comparison with the intact enzyme. J. Biol. Client. . 266, 16876-16885.
    • (1991) J. Biol. Client. . , vol.266 , pp. 16876-16885
    • Moremen, K.W.1    Touster, O.2    Robbins, P.W.3
  • 29
    • 0029133322 scopus 로고
    • A comparison of the transmembrane domains of Golgi and plasma membrane proteins
    • Munro. S. (1995) A comparison of the transmembrane domains of Golgi and plasma membrane proteins. Biochem. Soc. Trans., 23, 527-530.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 527-530
    • Munro, S.1
  • 30
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S. and Pelham. H. R. B. (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell, 48, 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 31
    • 0026773370 scopus 로고
    • Expression cloning of beta 1, 4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides
    • Nagata, Y., Yamashiro. S., Yodoi, J., Lloyd. K. O. and Furukawa. K. (1992) Expression cloning of beta 1, 4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides. J. Biol. Client., 267, 12082-12089.
    • (1992) J. Biol. Client. , vol.267 , pp. 12082-12089
    • Nagata, Y.1    Yamashiro, S.2    Yodoi, J.3    Lloyd, K.O.4    Furukawa, K.5
  • 32
    • 0028334014 scopus 로고
    • Correction: Expression cloning of β1, 4 N-acetylgalactosaminyltrans-ferase cDNAs that determine the expression of GM2 and GD2 gangliosides
    • Nagata. Y., Yamashiro, S., Yodoi. J., Lloyd, K. O., Shiku, H. and Furukawa. K. (1994) Correction: expression cloning of β1, 4 N-acetylgalactosaminyltrans-ferase cDNAs that determine the expression of GM2 and GD2 gangliosides. J. Biol. Chem., 269, 7045
    • (1994) J. Biol. Chem. , vol.269 , pp. 7045
    • Nagata, Y.1    Yamashiro, S.2    Yodoi, J.3    Lloyd, K.O.4    Shiku, H.5    Furukawa, K.6
  • 33
    • 0028027284 scopus 로고
    • Expression cloning of a CMP-NeuAc:NeuAca2-3Galβl-4Glcβ1-1'Cer a2, 8-sialyltransferase (GD3 synthase) from human melanoma cells
    • Nara. K., Watanabe. Y., Maruyama. K., Kasahara, K., Nagai. Y. and Sanai, Y. (1994) Expression cloning of a CMP-NeuAc:NeuAca2-3Galβl-4Glcβ1-1'Cer a2, 8-sialyltransferase (GD3 synthase) from human melanoma cells. Proc. Natl. Acad. Sci. USA, 91, 7952-7956.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7952-7956
    • Nara, K.1    Watanabe, Y.2    Maruyama, K.3    Kasahara, K.4    Nagai, Y.5    Sanai, Y.6
  • 34
    • 0023911121 scopus 로고
    • Purification, properties and cation activation of galactosyltransferase from lactating-rat mammary Golgi membranes
    • Navaratnam, N., Ward. S., Fisher. C., Kuhn, N. J., Keen. J. N. and FindlayJ. B. C. (1988) Purification, properties and cation activation of galactosyltransferase from lactating-rat mammary Golgi membranes. Enr. J. Biochem., 171, 623-629.
    • (1988) Enr. J. Biochem. , vol.171 , pp. 623-629
    • Navaratnam, N.1    Ward, S.2    Fisher, C.3    Kuhn, N.J.4    Keen, J.N.5    Findlayj, B.C.6
  • 35
    • 0027472941 scopus 로고
    • Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells
    • Nilsson, T., Pypaert, M., Hoe. M. H., Slusarewicz. P., Berger. E. G. and Warren, G. (1993a) Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells. J. Cell Biol, 120, 5-13.
    • (1993) J. Cell Biol , vol.120 , pp. 5-13
    • Nilsson, T.1    Pypaert, M.2    Hoe, M.H.3    Slusarewicz, P.4    Berger, E.G.5    Warren, G.6
  • 36
    • 0027318045 scopus 로고
    • Kin recognition: A model for the retention of Golgi enzymes
    • Nilsson, T., Slusarewicz. P., Hoe. M. H. and Warren. G. (1993b) Kin recognition: a model for the retention of Golgi enzymes. FEBS Lett., 330, 1-4.
    • (1993) FEBS Lett. , vol.330 , pp. 1-4
    • Nilsson, T.1    Slusarewicz, P.2    Hoe, M.H.3    Warren, G.4
  • 38
    • 0024149621 scopus 로고
    • Regulation of protein export from the endoplasmic reticulum
    • Rose, J. K. and Doms, R. W. (1988) Regulation of protein export from the endoplasmic reticulum. Anna. Rev. Cell Biol., -4, 257-288.
    • (1988) Anna. Rev. Cell Biol. , vol.4 , pp. 257-288
    • Rose, J.K.1    Doms, R.W.2
  • 39
    • 0023617056 scopus 로고
    • Subcellular organization of glycosylation in mammalian cells
    • Roth. J. (1987) Subcellular organization of glycosylation in mammalian cells. Biochim. Biophys. Ada, 906, 405-436.
    • (1987) Biochim. Biophys. Ada , vol.906 , pp. 405-436
    • Roth, J.1
  • 40
    • 0023024461 scopus 로고
    • Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells
    • Roth, J., Taatjes, D. J., Weinstein, J., PauIson. J. C., Greenwell. P. and Watkins. W. M. (1986) Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells. J. Biol. Chem., 261, 14307-14312.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14307-14312
    • Roth, J.1    Taatjes, D.J.2    Weinstein, J.3    Pauison, J.C.4    Greenwell, P.5    Watkins, W.M.6
  • 42
    • 0027440258 scopus 로고
    • Ceramide UDPgalactosyltransferase from myelinating rat brain: Purification, cloning, and expression
    • Schulte. S. and Stoffel. W. (1993) Ceramide UDPgalactosyltransferase from myelinating rat brain: purification, cloning, and expression. Proc. Natl. Acad. Sci. USA, 90, 10265-10269.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10265-10269
    • Schulte, S.1    Stoffel, W.2
  • 43
    • 0028349810 scopus 로고
    • An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum
    • Schutze, M. -P., Peterson. P. A. and Jackson. M. R. (1994) An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum. EMBO J., 13, 1696-1705.
    • (1994) EMBO J. , vol.13 , pp. 1696-1705
    • Schutze, M.P.1    Peterson, P.A.2    Jackson, M.R.3
  • 45
    • 0028362977 scopus 로고
    • Isolation, characterization, and expression of cDNA clones that encode rat UDP-galactose: Ceramide galactosyltransferase
    • Stahl, N., Jurevics. H., Morell. P., Suzuki. K. and Popko, B. (1994) Isolation, characterization, and expression of cDNA clones that encode rat UDP-galactose: ceramide galactosyltransferase. J. Neurosci. Res., 38, 234-242.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 234-242
    • Stahl, N.1    Jurevics, H.2    Morell, P.3    Suzuki, K.4    Popko, B.5
  • 46
    • 0028104174 scopus 로고
    • Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere
    • Sullivan, K. F., Hechenberger. M. and Masri, K. (1994) Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere. J. Cell Biol., 127, 581-592.
    • (1994) J. Cell Biol. , vol.127 , pp. 581-592
    • Sullivan, K.F.1    Hechenberger, M.2    Masri, K.3
  • 47
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the Golgi apparatus
    • Teasdale. R. D. and Jackson. M. R. (1996) Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the Golgi apparatus. Annn. Rev. Cell Biol., 12, 27-54.
    • (1996) Annn. Rev. Cell Biol. , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 48
    • 0028361767 scopus 로고
    • The KKXX signal mediates retrieval of membrane proteins from the Golgi to the ER in yeast
    • Townsley. F. M. and Pelham. H. R. B. (1994) The KKXX signal mediates retrieval of membrane proteins from the Golgi to the ER in yeast. Eur. J. Cell Biol., 211-216.
    • (1994) Eur. J. Cell Biol. , pp. 211-216
    • Townsley, F.M.1    Pelham, H.R.B.2
  • 50
    • 0029067675 scopus 로고
    • Golgi retention mechanism of β-1, 4 galactosyltransferase
    • Yamaguchi. N. and Fukuda, M. N. (1995) Golgi retention mechanism of β-1, 4 galactosyltransferase. J. Biol. Chem., 270, 12170-12176.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 51
    • 0027349864 scopus 로고
    • Molecular approaches to studying the intracellular trafficking of glycosphingolipids
    • Young, W. W., (1993) Molecular approaches to studying the intracellular trafficking of glycosphingolipids. Adv. Lipid Res., 26, 161-179.
    • (1993) Adv. Lipid Res. , vol.26 , pp. 161-179
    • Young, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.