메뉴 건너뛰기




Volumn 290, Issue 25, 2015, Pages 15475-15486

UDP-galactose (SLC35A2) and UDP-N-acetylglucosamine (SLC35A3) transporters form glycosylation-related complexes with mannoside acetylglucosaminyltransferases (Mgats)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; NUCLEOTIDES;

EID: 84940175650     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.636670     Document Type: Article
Times cited : (42)

References (49)
  • 3
    • 0032482961 scopus 로고    scopus 로고
    • Mammalian cytidine 5′-monophosphate N-acetylneuraminic acid synthetase: A nuclear protein with evolutionarily conserved structural motifs
    • Münster, A. K., Eckhardt, M., Potvin, B., Mühlenhoff, M., Stanley, P., and Gerardy-Schahn, R. (1998) Mammalian cytidine 5′-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs. Proc. Natl. Acad. Sci. U.S.A. 95, 9140-9145
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9140-9145
    • Münster, A.K.1    Eckhardt, M.2    Potvin, B.3    Mühlenhoff, M.4    Stanley, P.5    Gerardy-Schahn, R.6
  • 4
    • 0034851008 scopus 로고    scopus 로고
    • Nucleotide sugar transporters: Biological and functional aspects
    • Gerardy-Schahn, R., Oelmann, S., and Bakker, H. (2001) Nucleotide sugar transporters: Biological and functional aspects. Biochimie 83, 775-782
    • (2001) Biochimie , vol.83 , pp. 775-782
    • Gerardy-Schahn, R.1    Oelmann, S.2    Bakker, H.3
  • 5
    • 33845478747 scopus 로고    scopus 로고
    • Nucleotide sugar transporters of the Golgi apparatus: From basic science to diseases
    • Caffaro, C. E., and Hirschberg, C. B. (2006) Nucleotide sugar transporters of the Golgi apparatus: from basic science to diseases. Acc. Chem. Res. 39, 805-812
    • (2006) Acc. Chem. Res. , vol.39 , pp. 805-812
    • Caffaro, C.E.1    Hirschberg, C.B.2
  • 6
    • 0021740347 scopus 로고
    • Mechanism of glycosylation and sulfation in the Golgi apparatus: Evidence for nucleotide sugar/nucleoside monophosphate and nucleotide sulfate/nucleoside monophosphate antiports in the Golgi apparatus membrane
    • Capasso, J. M., and Hirschberg, C. B. (1984) Mechanism of glycosylation and sulfation in the Golgi apparatus: evidence for nucleotide sugar/nucleoside monophosphate and nucleotide sulfate/nucleoside monophosphate antiports in the Golgi apparatus membrane. Proc. Natl. Acad. Sci. U.S.A. 81, 7051-7055
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 7051-7055
    • Capasso, J.M.1    Hirschberg, C.B.2
  • 7
    • 0033605555 scopus 로고    scopus 로고
    • Membrane topology of the mammalian CMP-sialic acid transporter
    • Eckhardt, M., Gotza, B., and Gerardy-Schahn, R. (1999) Membrane topology of the mammalian CMP-sialic acid transporter. J. Biol. Chem. 274, 8779-8787
    • (1999) J. Biol. Chem. , vol.274 , pp. 8779-8787
    • Eckhardt, M.1    Gotza, B.2    Gerardy-Schahn, R.3
  • 8
    • 0032876435 scopus 로고    scopus 로고
    • Molecular characterization of Vig4/Vrg4 GDP-mannose transporter of the yeast Saccharomyces cerevisiae
    • Abe, M., Hashimoto, H., and Yoda, K. (1999) Molecular characterization of Vig4/Vrg4 GDP-mannose transporter of the yeast Saccharomyces cerevisiae. FEBS Lett. 458, 309-312
    • (1999) FEBS Lett. , vol.458 , pp. 309-312
    • Abe, M.1    Hashimoto, H.2    Yoda, K.3
  • 9
    • 0033544853 scopus 로고    scopus 로고
    • Reconstitution, identification and purification of the rat liver Golgi membrane GDP-fucose transporter
    • Puglielli, L., and Hirschberg, C. B. (1999) Reconstitution, identification and purification of the rat liver Golgi membrane GDP-fucose transporter. J. Biol. Chem. 274, 35596-35600
    • (1999) J. Biol. Chem. , vol.274 , pp. 35596-35600
    • Puglielli, L.1    Hirschberg, C.B.2
  • 10
    • 0033548088 scopus 로고    scopus 로고
    • Identification and purification of the rat liver Golgi membrane UDP-N-acetylgalactosamine transporter
    • Puglielli, L., Mandon, E. C., Rancour, D. M., Menon, A. K., and Hirschberg, C. B. (1999) Identification and purification of the rat liver Golgi membrane UDP-N-acetylgalactosamine transporter. J. Biol. Chem. 274, 4474-4479
    • (1999) J. Biol. Chem. , vol.274 , pp. 4474-4479
    • Puglielli, L.1    Mandon, E.C.2    Rancour, D.M.3    Menon, A.K.4    Hirschberg, C.B.5
  • 11
    • 0034728358 scopus 로고    scopus 로고
    • The Leishmania GDP-mannose transporter is an autonomous, multispecific, hexameric complex of LPG2 subunits
    • Hong, K., Ma, D., Beverley, S. M., and Turco, S. J. (2000) The Leishmania GDP-mannose transporter is an autonomous, multispecific, hexameric complex of LPG2 subunits. Biochemistry 39, 2013-2022
    • (2000) Biochemistry , vol.39 , pp. 2013-2022
    • Hong, K.1    Ma, D.2    Beverley, S.M.3    Turco, S.J.4
  • 13
    • 84869490772 scopus 로고    scopus 로고
    • UDP-N-acetylglucosamine transporter and UDP-galactose transporter form heterologous complexes in the Golgi membrane
    • Maszczak-Seneczko, D., Sosicka, P., Majkowski, M., Olczak, T., and Olczak, M. (2012) UDP-N-acetylglucosamine transporter and UDP-galactose transporter form heterologous complexes in the Golgi membrane. FEBS Lett. 586, 4082-4087
    • (2012) FEBS Lett. , vol.586 , pp. 4082-4087
    • Maszczak-Seneczko, D.1    Sosicka, P.2    Majkowski, M.3    Olczak, T.4    Olczak, M.5
  • 14
    • 0042970585 scopus 로고    scopus 로고
    • Association of the Golgi UDP-galactose transporter with UDP-galactose:Ceramide galactosyltransferase allows UDP-galactose import in the endoplasmic reticulum
    • Sprong, H., Degroote, S., Nilsson, T., Kawakita, M., Ishida, N., van der Sluijs, P., and van Meer, G. (2003) Association of the Golgi UDP-galactose transporter with UDP-galactose:ceramide galactosyltransferase allows UDP-galactose import in the endoplasmic reticulum. Mol. Biol. Cell 14, 3482-3493
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3482-3493
    • Sprong, H.1    Degroote, S.2    Nilsson, T.3    Kawakita, M.4    Ishida, N.5    Van Der Sluijs, P.6    Van Meer, G.7
  • 15
    • 84881259716 scopus 로고    scopus 로고
    • UDP-N-acetylglucosamine transporter (SLC35A3) regulates biosynthesis of highly branched N-glycans and keratan sulfate
    • Maszczak-Seneczko, D., Sosicka, P., Olczak, T., Jakimowicz, P., Majkowski, M., and Olczak, M., (2013) UDP-N-acetylglucosamine transporter (SLC35A3) regulates biosynthesis of highly branched N-glycans and keratan sulfate. J. Biol. Chem. 288, 21850-21860
    • (2013) J. Biol. Chem. , vol.288 , pp. 21850-21860
    • Maszczak-Seneczko, D.1    Sosicka, P.2    Olczak, T.3    Jakimowicz, P.4    Majkowski, M.5    Olczak, M.6
  • 16
    • 0029682399 scopus 로고    scopus 로고
    • Human UDP-galactose translocator: Molecular cloning of a complementary DNA that complements the genetic defect of a mutant cell line deficient in UDP-galactose translocator
    • Miura, N., Ishida, N., Hoshino, M., Yamauchi, M., Hara, T., Ayusawa, D., and Kawakita, M. (1996) Human UDP-galactose translocator: molecular cloning of a complementary DNA that complements the genetic defect of a mutant cell line deficient in UDP-galactose translocator. J. Biochem. 120, 236-241
    • (1996) J. Biochem. , vol.120 , pp. 236-241
    • Miura, N.1    Ishida, N.2    Hoshino, M.3    Yamauchi, M.4    Hara, T.5    Ayusawa, D.6    Kawakita, M.7
  • 17
    • 0030448616 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel isoform of the human UDP-galactose transporter, and of related complementary DNAs belonging to the nucleotide-sugar transporter gene family
    • Ishida, N., Miura, N., Yoshioka, S., and Kawakita, M. (1996) Molecular cloning and characterization of a novel isoform of the human UDP-galactose transporter, and of related complementary DNAs belonging to the nucleotide-sugar transporter gene family. J Biochem. 120, 1074-1078
    • (1996) J Biochem. , vol.120 , pp. 1074-1078
    • Ishida, N.1    Miura, N.2    Yoshioka, S.3    Kawakita, M.4
  • 18
    • 0035854833 scopus 로고    scopus 로고
    • Point mutations identified in Lec8 Chinese hamster ovary glycosylation mutants that inactivate both the UDP-galactose and CMP-sialic acid transporters
    • Oelmann, S., Stanley, P., and Gerardy-Schahn, R. (2001) Point mutations identified in Lec8 Chinese hamster ovary glycosylation mutants that inactivate both the UDP-galactose and CMP-sialic acid transporters. J. Biol. Chem. 276, 26291-26300
    • (2001) J. Biol. Chem. , vol.276 , pp. 26291-26300
    • Oelmann, S.1    Stanley, P.2    Gerardy-Schahn, R.3
  • 19
    • 82955232361 scopus 로고    scopus 로고
    • Comparative analysis of involvement of UGT1 and UGT2 splice variants of UDP-galactose transporter in glycosylation of macromolecules in MDCK and CHO cell lines
    • Maszczak-Seneczko, D., Olczak, T., Wunderlich, L., and Olczak, M. (2011) Comparative analysis of involvement of UGT1 and UGT2 splice variants of UDP-galactose transporter in glycosylation of macromolecules in MDCK and CHO cell lines. Glycoconj. J. 28, 481-492
    • (2011) Glycoconj. J. , vol.28 , pp. 481-492
    • Maszczak-Seneczko, D.1    Olczak, T.2    Wunderlich, L.3    Olczak, M.4
  • 20
    • 0023739416 scopus 로고
    • A polarized epithelial cell mutant deficient in translocation of UDP-galactose into the Golgi complex
    • Brändli, A. W., Hansson, G. C., Rodriguez-Boulan, E., and Simons K (1988) A polarized epithelial cell mutant deficient in translocation of UDP-galactose into the Golgi complex. J. Biol. Chem. 263, 16283-16290
    • (1988) J. Biol. Chem. , vol.263 , pp. 16283-16290
    • Brändli, A.W.1    Hansson, G.C.2    Rodriguez-Boulan, E.3    Simons, K.4
  • 21
    • 0021029861 scopus 로고
    • Lectin-resistant CHO cells: Selection of new mutant phenotypes
    • Stanley, P. (1983) Lectin-resistant CHO cells: selection of new mutant phenotypes. Somatic Cell Genet. 9, 593-608
    • (1983) Somatic Cell Genet. , vol.9 , pp. 593-608
    • Stanley, P.1
  • 22
    • 0024322548 scopus 로고
    • Elucidation of the phenotypic change on the surface of Had-1 cell, a mutant cell line of mouse FM3A carcinoma cells selected by resistance to Newcastle disease virus infection
    • Hara, T., Endo, T., Furukawa, K., Kawakita, M., and Kobata, A. (1989) Elucidation of the phenotypic change on the surface of Had-1 cell, a mutant cell line of mouse FM3A carcinoma cells selected by resistance to Newcastle disease virus infection. J. Biochem. 106, 236-247
    • (1989) J. Biochem. , vol.106 , pp. 236-247
    • Hara, T.1    Endo, T.2    Furukawa, K.3    Kawakita, M.4    Kobata, A.5
  • 23
    • 0030699080 scopus 로고    scopus 로고
    • Expression of the human UDP-galactose transporter in the Golgi membranes of murine Had-1 cells that lack the endogenous transporter
    • Yoshioka, S., Sun-Wada, G. H., Ishida, N., and Kawakita, M. (1997) Expression of the human UDP-galactose transporter in the Golgi membranes of murine Had-1 cells that lack the endogenous transporter. J. Biochem. 122, 691-695
    • (1997) J. Biochem. , vol.122 , pp. 691-695
    • Yoshioka, S.1    Sun-Wada, G.H.2    Ishida, N.3    Kawakita, M.4
  • 24
    • 81355135247 scopus 로고    scopus 로고
    • Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters
    • Maszczak-Seneczko, D., Olczak, T., and Olczak, M. (2011) Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters. Acta Biochim. Pol. 58, 413-419
    • (2011) Acta Biochim. Pol. , vol.58 , pp. 413-419
    • Maszczak-Seneczko, D.1    Olczak, T.2    Olczak, M.3
  • 25
    • 80053227611 scopus 로고    scopus 로고
    • Overexpression of UDP-GlcNAc transporter partially corrects galactosylation defect caused by UDP-Gal transporter mutation
    • Maszczak-Seneczko, D., Olczak, T., Jakimowicz, P., and Olczak, M. (2011) Overexpression of UDP-GlcNAc transporter partially corrects galactosylation defect caused by UDP-Gal transporter mutation. FEBS Lett. 585, 3090-3094
    • (2011) FEBS Lett. , vol.585 , pp. 3090-3094
    • Maszczak-Seneczko, D.1    Olczak, T.2    Jakimowicz, P.3    Olczak, M.4
  • 26
    • 84880463727 scopus 로고    scopus 로고
    • UDP-Gal/UDP-GlcNAc chimeric transporter complements mutation defect in mammalian cells deficient in UDP-Gal transporter
    • Olczak, M., Maszczak-Seneczko, D., Sosicka, P., Jakimowicz, P., and Olczak, T. (2013) UDP-Gal/UDP-GlcNAc chimeric transporter complements mutation defect in mammalian cells deficient in UDP-Gal transporter. Biochem. Biophys. Res. Commun. 434, 473-478
    • (2013) Biochem. Biophys. Res. Commun. , vol.434 , pp. 473-478
    • Olczak, M.1    Maszczak-Seneczko, D.2    Sosicka, P.3    Jakimowicz, P.4    Olczak, T.5
  • 27
    • 84910672674 scopus 로고    scopus 로고
    • Short N-terminal region of UDP-galactose transporter (SLC35A2) is crucial for galactosylation of N-glycans
    • Sosicka, P., Jakimowicz, P., Olczak, T., and Olczak, M. (2014) Short N-terminal region of UDP-galactose transporter (SLC35A2) is crucial for galactosylation of N-glycans. Biochem. Biophys. Res. Commun. 454, 486-492
    • (2014) Biochem. Biophys. Res. Commun. , vol.454 , pp. 486-492
    • Sosicka, P.1    Jakimowicz, P.2    Olczak, T.3    Olczak, M.4
  • 29
    • 0001813430 scopus 로고
    • Molecular cloning of glycosyltransferase genes
    • Fukuda, M., and Hindsgaul, O., eds Oxford University Press, Oxford
    • Schachter, H. (1994) Molecular cloning of glycosyltransferase genes. In Molecular Glycobiology (Fukuda, M., and Hindsgaul, O., eds) pp. 88-162, Oxford University Press, Oxford
    • (1994) Molecular Glycobiology , pp. 88-162
    • Schachter, H.1
  • 30
    • 0029144380 scopus 로고
    • Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: A survey
    • Field, M. C., and Wainwright, L. J. (1995) Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: a survey. Glycobiology 5, 463-472
    • (1995) Glycobiology , vol.5 , pp. 463-472
    • Field, M.C.1    Wainwright, L.J.2
  • 31
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille, C., Hui, N., Hunte, F., Kieckbusch, R., Berger, E. G., Warren, G., and Nilsson, T. (1995) Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci. 108, 1617-1627
    • (1995) J. Cell Sci. , vol.108 , pp. 1617-1627
    • Rabouille, C.1    Hui, N.2    Hunte, F.3    Kieckbusch, R.4    Berger, E.G.5    Warren, G.6    Nilsson, T.7
  • 32
    • 53049084874 scopus 로고    scopus 로고
    • N-Glycans in cancer progression
    • Lau, K. S., and Dennis, J. W. (2008) N-Glycans in cancer progression. Glycobiology 18, 750-760
    • (2008) Glycobiology , vol.18 , pp. 750-760
    • Lau, K.S.1    Dennis, J.W.2
  • 33
    • 84864287727 scopus 로고    scopus 로고
    • Glycosyltransferase complexes improve glycolipid synthesis
    • Spessott, W., Crespo, P. M., Daniotti, J. L., and Maccioni, H. J. (2012) Glycosyltransferase complexes improve glycolipid synthesis. FEBS Lett. 586, 2346-2350
    • (2012) FEBS Lett. , vol.586 , pp. 2346-2350
    • Spessott, W.1    Crespo, P.M.2    Daniotti, J.L.3    Maccioni, H.J.4
  • 34
    • 84862844767 scopus 로고    scopus 로고
    • Spatial organization and stoichiometry of N-terminal domain-mediated glycosyltransferase complexes in Golgi membranes determined by FRET microscopy
    • Ferrari, M. L., Gomez, G. A., and Maccioni, H. J. (2012) Spatial organization and stoichiometry of N-terminal domain-mediated glycosyltransferase complexes in Golgi membranes determined by FRET microscopy. Neurochem. Res. 37, 1325-1334
    • (2012) Neurochem. Res. , vol.37 , pp. 1325-1334
    • Ferrari, M.L.1    Gomez, G.A.2    Maccioni, H.J.3
  • 35
    • 77952944920 scopus 로고    scopus 로고
    • Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells
    • Hassinen, A., Rivinoja, A., Kauppila, A., and Kellokumpu, S. (2010) Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells. J. Biol. Chem. 285, 17771-17777
    • (2010) J. Biol. Chem. , vol.285 , pp. 17771-17777
    • Hassinen, A.1    Rivinoja, A.2    Kauppila, A.3    Kellokumpu, S.4
  • 36
    • 84871719148 scopus 로고    scopus 로고
    • Golgi-localized enzyme complexes for plant cell wall biosynthesis
    • Oikawa, A., Lund, C. H., Sakuragi, Y., and Scheller, H. V. (2013) Golgi-localized enzyme complexes for plant cell wall biosynthesis. Trends Plant Sci. 18, 49-58
    • (2013) Trends Plant Sci. , vol.18 , pp. 49-58
    • Oikawa, A.1    Lund, C.H.2    Sakuragi, Y.3    Scheller, H.V.4
  • 37
    • 84875714380 scopus 로고    scopus 로고
    • Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta
    • Schoberer, J., Liebminger, E., Botchway, S. W., Strasser, R., and Hawes, C. (2013) Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta. Plant Physiol. 161, 1737-1754
    • (2013) Plant Physiol. , vol.161 , pp. 1737-1754
    • Schoberer, J.1    Liebminger, E.2    Botchway, S.W.3    Strasser, R.4    Hawes, C.5
  • 38
    • 0034625183 scopus 로고    scopus 로고
    • Distinct protein domains of the yeast Golgi GDP-mannose transporter mediate oligomer assembly and export from the endoplasmic reticulum
    • Gao, X.-D., and Dean, N. (2000) Distinct protein domains of the yeast Golgi GDP-mannose transporter mediate oligomer assembly and export from the endoplasmic reticulum. J. Biol. Chem. 275, 17718-17727
    • (2000) J. Biol. Chem. , vol.275 , pp. 17718-17727
    • Gao, X.-D.1    Dean, N.2
  • 39
    • 33749166219 scopus 로고    scopus 로고
    • Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes
    • Oguri, S., Yoshida, A., Minowa, M. T., and Takeuchi, M. (2006) Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes. Glycoconj. J. 23, 473-480
    • (2006) Glycoconj. J. , vol.23 , pp. 473-480
    • Oguri, S.1    Yoshida, A.2    Minowa, M.T.3    Takeuchi, M.4
  • 41
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau, K. S., Partridge, E. A., Grigorian, A., Silvescu, C. I., Reinhold, V. N., Demetriou, M., and Dennis, J. W. (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129, 123-134
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 42
    • 0029890064 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells
    • Nilsson, T., Rabouille, C., Hui, N., Watson, R., and Warren, G. (1996) The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells. J. Cell Sci. 109, 1975-1989
    • (1996) J. Cell Sci. , vol.109 , pp. 1975-1989
    • Nilsson, T.1    Rabouille, C.2    Hui, N.3    Watson, R.4    Warren, G.5
  • 43
    • 0034697118 scopus 로고    scopus 로고
    • Medial Golgi but not late Golgi glycosyltransferases exist as high molecular weight complexes: Role of luminal domain in complex formation and localization
    • Opat, A. S., Houghton, F., and Gleeson, P. A. (2000) Medial Golgi but not late Golgi glycosyltransferases exist as high molecular weight complexes: role of luminal domain in complex formation and localization. J. Biol. Chem. 275, 11836-11845
    • (2000) J. Biol. Chem. , vol.275 , pp. 11836-11845
    • Opat, A.S.1    Houghton, F.2    Gleeson, P.A.3
  • 45
    • 0020356007 scopus 로고
    • A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: α-D-mannoside β1,6 N-acetylglucosaminyltransferase
    • Cummings, R. D., Trowbridge, I. S., and Kornfeld, S. (1982) A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: α-D-mannoside β1,6 N-acetylglucosaminyltransferase. J. Biol. Chem. 257, 13421-13427
    • (1982) J. Biol. Chem. , vol.257 , pp. 13421-13427
    • Cummings, R.D.1    Trowbridge, I.S.2    Kornfeld, S.3
  • 46
    • 0030884451 scopus 로고    scopus 로고
    • Purification and characterization of UDP-N-acetylglucosamine: α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase (Nacetylglucosaminyltransferase-IV) from bovine small intestine
    • Oguri, S., Minowa, M. T., Ihara, Y., Taniguchi, N., Ikenaga, H., and Takeuchi, M. (1997) Purification and characterization of UDP-N-acetylglucosamine: α1,3-D-mannoside β1,4-N-acetylglucosaminyltransferase (Nacetylglucosaminyltransferase-IV) from bovine small intestine. J. Biol. Chem. 272, 22721-22727
    • (1997) J. Biol. Chem. , vol.272 , pp. 22721-22727
    • Oguri, S.1    Minowa, M.T.2    Ihara, Y.3    Taniguchi, N.4    Ikenaga, H.5    Takeuchi, M.6
  • 47
    • 0035808485 scopus 로고    scopus 로고
    • The critical role of the stem region as a functional domain responsible for the oligomerization and Golgi localization of N-acetylglucosaminyltransferase V: The involvement of a domain homophilic interaction
    • Sasai, K., Ikeda, Y., Tsuda, T., Ihara, H., Korekane, H., Shiota, K., and Taniguchi, N. (2001) The critical role of the stem region as a functional domain responsible for the oligomerization and Golgi localization of N-acetylglucosaminyltransferase V: the involvement of a domain homophilic interaction. J. Biol. Chem. 276, 759-765
    • (2001) J. Biol. Chem. , vol.276 , pp. 759-765
    • Sasai, K.1    Ikeda, Y.2    Tsuda, T.3    Ihara, H.4    Korekane, H.5    Shiota, K.6    Taniguchi, N.7
  • 49
    • 80055094003 scopus 로고    scopus 로고
    • Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells
    • Hassinen, A., Pujol, F. M., Kokkonen, N., Pieters, C., Kihlström, M., Korhonen, K., and Kellokumpu, S. (2011) Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells. J. Biol. Chem. 286, 38329-38340
    • (2011) J. Biol. Chem. , vol.286 , pp. 38329-38340
    • Hassinen, A.1    Pujol, F.M.2    Kokkonen, N.3    Pieters, C.4    Kihlström, M.5    Korhonen, K.6    Kellokumpu, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.