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Volumn 16, Issue 10, 2006, Pages 947-958

Identification of core 1 O-glycan T-synthase from Caenorhabditis elegans

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; AMINO ACID; CHAPERONE; COMPLEMENTARY DNA; CYSTEINE; DISACCHARIDE; GALACTOSE; GALACTOSYLTRANSFERASE; GLYCOPROTEIN; GREEN FLUORESCENT PROTEIN; GUANINE; PROTEIN; RECOMBINANT ENZYME;

EID: 33748702275     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwl008     Document Type: Article
Times cited : (41)

References (49)
  • 1
    • 0033022809 scopus 로고    scopus 로고
    • Modifying secretion and post-translational processing in insect cells
    • Ailor, E. and Betenbaugh, M.J. (1999) Modifying secretion and post-translational processing in insect cells. Curr. Opin. Biotechnol., 10, 142-145.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 142-145
    • Ailor, E.1    Betenbaugh, M.J.2
  • 2
    • 0034838433 scopus 로고    scopus 로고
    • Genetic model organisms in the study of N-glycans
    • Altmann, F., Fabini, G., Ahorn, H., and Wilson, I.B. (2001) Genetic model organisms in the study of N-glycans. Biochimie, 83, 703-712.
    • (2001) Biochimie , vol.83 , pp. 703-712
    • Altmann, F.1    Fabini, G.2    Ahorn, H.3    Wilson, I.B.4
  • 3
    • 23944438373 scopus 로고    scopus 로고
    • Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57
    • Bedard, K., Szabo, E., Michalak, M., and Opas, M. (2005) Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57. Int. Rev. Cytol., 245, 91-121.
    • (2005) Int. Rev. Cytol. , vol.245 , pp. 91-121
    • Bedard, K.1    Szabo, E.2    Michalak, M.3    Opas, M.4
  • 4
    • 0043071534 scopus 로고    scopus 로고
    • The N-terminal stem region of bovine and human beta1,4-galactosyltransferase I increases the in vitro folding efficiency of their catalytic domain from inclusion bodies
    • Boeggeman, E.E., Ramakrishnan, B., and Qasba, P.K. (2003) The N-terminal stem region of bovine and human beta1,4-galactosyltransferase I increases the in vitro folding efficiency of their catalytic domain from inclusion bodies. Protein Expr. Purif., 30, 219-229.
    • (2003) Protein Expr. Purif. , vol.30 , pp. 219-229
    • Boeggeman, E.E.1    Ramakrishnan, B.2    Qasba, P.K.3
  • 5
    • 0031723937 scopus 로고    scopus 로고
    • Glycoproteins and their relationship to human disease
    • Brockhausen, I., Schutzbach, J., and Kuhns, W. (1998) Glycoproteins and their relationship to human disease. Acta Anat. (Basel), 161, 36-78.
    • (1998) Acta Anat. (Basel) , vol.161 , pp. 36-78
    • Brockhausen, I.1    Schutzbach, J.2    Kuhns, W.3
  • 6
  • 7
    • 0142214543 scopus 로고    scopus 로고
    • Murine neutrophils require alpha1,3-fucosylation but not PSGL-1 for productive infection with Anaplasma phagocytophilum
    • Carlyon, J.A., Akkoyunlu, M., Xia, L., Yago, T., Wang, T., Cummings, R.D., McEver, R.P., and Fikrig, E. (2003) Murine neutrophils require alpha1,3-fucosylation but not PSGL-1 for productive infection with Anaplasma phagocytophilum. Blood, 102, 3387-3395.
    • (2003) Blood , vol.102 , pp. 3387-3395
    • Carlyon, J.A.1    Akkoyunlu, M.2    Xia, L.3    Yago, T.4    Wang, T.5    Cummings, R.D.6    McEver, R.P.7    Fikrig, E.8
  • 8
    • 22544463401 scopus 로고    scopus 로고
    • N-Glycans of Caenorhabditis elegans are specific to developmental stages
    • Cipollo, J.F., Awad, A.M., Costello, C.E., and Hirschberg, C.B. (2005) N-Glycans of Caenorhabditis elegans are specific to developmental stages. J. Biol. Chem., 280, 26063-26072.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26063-26072
    • Cipollo, J.F.1    Awad, A.M.2    Costello, C.E.3    Hirschberg, C.B.4
  • 9
    • 0348209615 scopus 로고    scopus 로고
    • The fine structure of Caenorhabditis elegans N-glycans
    • Cipollo, J.F., Costello, C.E., and Hirschberg, C.B. (2002) The fine structure of Caenorhabditis elegans N-glycans. J. Biol. Chem., 277, 49143-49157.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49143-49157
    • Cipollo, J.F.1    Costello, C.E.2    Hirschberg, C.B.3
  • 10
    • 0142106350 scopus 로고    scopus 로고
    • Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans
    • Cram, E.J., Clark, S.G., and Schwarzbauer, J.E. (2003) Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans. J. Cell Sci., 116, 3871-3878.
    • (2003) J. Cell Sci. , vol.116 , pp. 3871-3878
    • Cram, E.J.1    Clark, S.G.2    Schwarzbauer, J.E.3
  • 11
    • 3543040594 scopus 로고    scopus 로고
    • Molecular cloning and characterization of an alpha1,3 fucosyltransferase, CEFT-1, from Caenorhabditis elegans
    • DeBose-Boyd, R.A., Nyame, A.K., and Cummings, R.D. (1998) Molecular cloning and characterization of an alpha1,3 fucosyltransferase, CEFT-1, from Caenorhabditis elegans. Glycobiology, 8, 905-917.
    • (1998) Glycobiology , vol.8 , pp. 905-917
    • DeBose-Boyd, R.A.1    Nyame, A.K.2    Cummings, R.D.3
  • 13
    • 0022639709 scopus 로고
    • Mechanism of galactosylation in the Golgi apparatus. A Chinese hamster ovary cell mutant deficient in translocation of UDP-galactose across Golgi vesicle membranes
    • Deutscher, S.L. and Hirschberg, C.B. (1986) Mechanism of galactosylation in the Golgi apparatus. A Chinese hamster ovary cell mutant deficient in translocation of UDP-galactose across Golgi vesicle membranes. J. Biol. Chem., 261, 96-100.
    • (1986) J. Biol. Chem. , vol.261 , pp. 96-100
    • Deutscher, S.L.1    Hirschberg, C.B.2
  • 14
    • 0021702358 scopus 로고
    • Translocation across Golgi vesicle membranes: A CHO glycosylation mutant deficient in CMP-sialic acid transport
    • Deutscher, S.L., Nuwayhid, N., Stanley, P., Briles, E.I., and Hirschberg, C.B. (1984) Translocation across Golgi vesicle membranes: A CHO glycosylation mutant deficient in CMP-sialic acid transport. Cell, 39, 295-299.
    • (1984) Cell , vol.39 , pp. 295-299
    • Deutscher, S.L.1    Nuwayhid, N.2    Stanley, P.3    Briles, E.I.4    Hirschberg, C.B.5
  • 15
    • 0020169707 scopus 로고
    • Endo-beta-N-acetylglucosaminidase F: Endoglycosidase from Flavobacterium meningosepticum that cleaves both high-mannose and complex glycoproteins
    • Elder, J.H. and Alexander, S. (1982) Endo-beta-N-acetylglucosaminidase F: Endoglycosidase from Flavobacterium meningosepticum that cleaves both high-mannose and complex glycoproteins. Proc. Natl. Acad. Sci. U. S. A., 79, 4540-4544.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 4540-4544
    • Elder, J.H.1    Alexander, S.2
  • 16
    • 0017182324 scopus 로고
    • Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the culture of medium of Diplococcus pneumoniae
    • Endo, Y. and Kobata, A. (1976) Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the culture of medium of Diplococcus pneumoniae. J. Biochem. (Tokyo), 80, 1-8.
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 1-8
    • Endo, Y.1    Kobata, A.2
  • 18
    • 0035396643 scopus 로고    scopus 로고
    • The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: Identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides
    • Guerardel, Y., Balanzino, L., Maes, E., Leroy, Y., Coddeville, B., Oriol, R., and Strecker, G. (2001) The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: Identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides. Biochem. J., 357, 167-182.
    • (2001) Biochem. J. , vol.357 , pp. 167-182
    • Guerardel, Y.1    Balanzino, L.2    Maes, E.3    Leroy, Y.4    Coddeville, B.5    Oriol, R.6    Strecker, G.7
  • 19
    • 0038514006 scopus 로고    scopus 로고
    • Hallmarks of Caenorhabditis elegans N-glycosylation: Complexity and controversy
    • Haslam, S.M. and Dell, A. (2003) Hallmarks of Caenorhabditis elegans N-glycosylation: Complexity and controversy. Biochimie, 85, 25-32.
    • (2003) Biochimie , vol.85 , pp. 25-32
    • Haslam, S.M.1    Dell, A.2
  • 20
    • 0038078591 scopus 로고    scopus 로고
    • The glycomes of Caenorhabditis elegans and other model organisms
    • Haslam, S.M., Gems, D., Morris, H.R., and Dell, A. (2002) The glycomes of Caenorhabditis elegans and other model organisms. Biochem. Soc. Symp., 117-134.
    • (2002) Biochem. Soc. Symp. , pp. 117-134
    • Haslam, S.M.1    Gems, D.2    Morris, H.R.3    Dell, A.4
  • 21
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A. and Aebi, M. (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem., 73, 1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 22
    • 0038645115 scopus 로고    scopus 로고
    • The fucosyltransferase gene family: An amazing summary of the underlying mechanisms of gene evolution
    • Javaud, C., Dupuy, F., Maftah, A., Julien, R., and Petit, J.M. (2003) The fucosyltransferase gene family: An amazing summary of the underlying mechanisms of gene evolution. Genetica, 118, 157-170.
    • (2003) Genetica , vol.118 , pp. 157-170
    • Javaud, C.1    Dupuy, F.2    Maftah, A.3    Julien, R.4    Petit, J.M.5
  • 23
    • 0037016720 scopus 로고    scopus 로고
    • Cloning and expression of human core 1 beta1,3-galactosyltransferase
    • Ju, T., Brewer, K., D'Souza, A., Cummings, R.D., and Canfield, W.M. (2002) Cloning and expression of human core 1 beta1,3-galactosyltransferase. J. Biol. Chem., 277, 178-186.
    • (2002) J. Biol. Chem. , vol.277 , pp. 178-186
    • Ju, T.1    Brewer, K.2    D'Souza, A.3    Cummings, R.D.4    Canfield, W.M.5
  • 24
    • 0037168608 scopus 로고    scopus 로고
    • A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase
    • Ju, T. and Cummings, R.D. (2002) A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase. Proc. Natl. Acad. Sci. U. S. A., 99, 16613-16618.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16613-16618
    • Ju, T.1    Cummings, R.D.2
  • 25
    • 27644442375 scopus 로고    scopus 로고
    • Protein glycosylation: Chaperone mutation in Tn syndrome
    • Ju, T. and Cummings, R.D. (2005) Protein glycosylation: Chaperone mutation in Tn syndrome. Nature, 437, 1252.
    • (2005) Nature , vol.437 , pp. 1252
    • Ju, T.1    Cummings, R.D.2
  • 26
    • 0037016738 scopus 로고    scopus 로고
    • Purification, characterization, and subunit structure of rat core 1 beta1,3-galactosyltransferase
    • Ju, T., Cummings, R.D., and Canfield, W.M. (2002) Purification, characterization, and subunit structure of rat core 1 beta1,3-galactosyltransferase. J. Biol. Chem., 277, 169-177.
    • (2002) J. Biol. Chem. , vol.277 , pp. 169-177
    • Ju, T.1    Cummings, R.D.2    Canfield, W.M.3
  • 28
    • 0037144495 scopus 로고    scopus 로고
    • Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans
    • Kawar, Z.S., Van Die, I., and Cummings, R.D. (2002) Molecular cloning and enzymatic characterization of a UDP-GalNAc:GLcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans. J. Biol. Chem., 277, 34924-34932.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34924-34932
    • Kawar, Z.S.1    Van Die, I.2    Cummings, R.D.3
  • 29
    • 0037033072 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel UDP-Gal: GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan
    • Kudo, T., Iwai, T., Kubota, T., Iwasaki, H., Takayma, Y., Hiruma, T., Inaba, N., Zhang, Y., Gotoh, M., Togayachi, A., and Narimatsu, H. (2002) Molecular cloning and characterization of a novel UDP-Gal: GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan. J. Biol. Chem., 277, 47724-47731.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47724-47731
    • Kudo, T.1    Iwai, T.2    Kubota, T.3    Iwasaki, H.4    Takayma, Y.5    Hiruma, T.6    Inaba, N.7    Zhang, Y.8    Gotoh, M.9    Togayachi, A.10    Narimatsu, H.11
  • 31
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • Lowe, J.B. and Marth, J.D. (2003) A genetic approach to mammalian glycan function. Annu. Rev. Biochem., 72, 643-691.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 32
    • 0030854107 scopus 로고    scopus 로고
    • Perspectives series: Cell adhesion in vascular biology. Role of PSGL-1 binding to selectins in leukocyte recruitment
    • McEver, R.P. and Cummings, R.D. (1997) Perspectives series: Cell adhesion in vascular biology. Role of PSGL-1 binding to selectins in leukocyte recruitment. J. Clin. Invest., 100, 485-491.
    • (1997) J. Clin. Invest. , vol.100 , pp. 485-491
    • McEver, R.P.1    Cummings, R.D.2
  • 33
    • 24644457201 scopus 로고    scopus 로고
    • Characterization of mucin-type core-1 beta1-3 galactosyltransferase homologous enzymes in Drosophila melanogaster
    • Muller, R., Hulsmeier, A.J., Altmann, F., Ten Hagen, K., Tiemeyer, M., and Hennet, T. (2005) Characterization of mucin-type core-1 beta1-3 galactosyltransferase homologous enzymes in Drosophila melanogaster. FEBS J., 272, 4295-4305.
    • (2005) FEBS J. , vol.272 , pp. 4295-4305
    • Muller, R.1    Hulsmeier, A.J.2    Altmann, F.3    Ten Hagen, K.4    Tiemeyer, M.5    Hennet, T.6
  • 35
    • 0032906430 scopus 로고    scopus 로고
    • Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
    • Oriol, R., Mollicone, R., Cailleau, A., Balanzino, L., and Breton, C. (1999) Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria. Glycobiology, 9, 323-334.
    • (1999) Glycobiology , vol.9 , pp. 323-334
    • Oriol, R.1    Mollicone, R.2    Cailleau, A.3    Balanzino, L.4    Breton, C.5
  • 36
    • 1942542931 scopus 로고    scopus 로고
    • Ligands for L-selectin: Homing, inflammation, and beyond
    • Rosen, S.D. (2004) Ligands for L-selectin: Homing, inflammation, and beyond. Annu. Rev. Immunol., 22, 129-156.
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 129-156
    • Rosen, S.D.1
  • 37
    • 33744951303 scopus 로고    scopus 로고
    • Null mutations in Drosophila N-acetylglucosaminyltransferase I produce defects in locomotion and a reduced life span
    • Sarkar, M., Leventis, P.A., Silvescu, C.I., Reinhold, V.N., Schachter, H., and Boulianne, G.L. (2006) Null mutations in Drosophila N-acetylglucosaminyltransferase I produce defects in locomotion and a reduced life span. J. Biol. Chem., 281, 12776-12785.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12776-12785
    • Sarkar, M.1    Leventis, P.A.2    Silvescu, C.I.3    Reinhold, V.N.4    Schachter, H.5    Boulianne, G.L.6
  • 38
    • 0034441282 scopus 로고    scopus 로고
    • The joys of HexNAc. The synthesis and function of N- and O-glycan branches
    • Schachter, H. (2000) The joys of HexNAc. The synthesis and function of N- and O-glycan branches. Glycoconj. J., 17, 465-483.
    • (2000) Glycoconj. J. , vol.17 , pp. 465-483
    • Schachter, H.1
  • 39
    • 0030848719 scopus 로고    scopus 로고
    • Immunoreactive T and Tn epitopes in cancer diagnosis, prognosis, and immunotherapy
    • Springer, G.F. (1997) Immunoreactive T and Tn epitopes in cancer diagnosis, prognosis, and immunotherapy. J. Mol. Med., 75, 594-602.
    • (1997) J. Mol. Med. , vol.75 , pp. 594-602
    • Springer, G.F.1
  • 40
    • 0010209342 scopus 로고
    • Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine - Glycoprotein N-acetylglucosaminyltransferase activity
    • Stanley, P., Narasimhan, S., Siminovitch, L., and Schachter, H. (1975) Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine - glycoprotein N-acetylglucosaminyltransferase activity. Proc. Natl. Acad. Sci. U. S. A., 72, 3323-3327.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 3323-3327
    • Stanley, P.1    Narasimhan, S.2    Siminovitch, L.3    Schachter, H.4
  • 41
    • 0018863515 scopus 로고
    • Differential involvement of cell surface sialic acid residues in wheat germ agglutinin binding to parental and wheat germ agglutinin-resistant Chinese hamster ovary cells
    • Stanley, P., Sudo, T., and Carver, J.P. (1980) Differential involvement of cell surface sialic acid residues in wheat germ agglutinin binding to parental and wheat germ agglutinin-resistant Chinese hamster ovary cells. J. Cell Biol., 85, 60-69.
    • (1980) J. Cell Biol. , vol.85 , pp. 60-69
    • Stanley, P.1    Sudo, T.2    Carver, J.P.3
  • 42
    • 0017869154 scopus 로고
    • Endo-beta-N-acetylglucosaminidase from Streptomyces plicatus
    • Tarentino, A.L., Trimble, R.B., and Maley, F. (1978) Endo-beta-N-acetylglucosaminidase from Streptomyces plicatus. Methods Enzymol., 50, 574-580.
    • (1978) Methods Enzymol. , vol.50 , pp. 574-580
    • Tarentino, A.L.1    Trimble, R.B.2    Maley, F.3
  • 43
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferases
    • Ten Hagen, K.G., Fritz, T.A., and Tabak, L.A. (2003) All in the family: the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases. Glycobiology, 13, 1R-16R.
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 44
    • 0037151043 scopus 로고    scopus 로고
    • A UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster
    • Ten Hagen, K.G. and Tran, D.T. (2002) A UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster. J. Biol. Chem., 277, 22616-22622.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22616-22622
    • Ten Hagen, K.G.1    Tran, D.T.2
  • 45
    • 0035137134 scopus 로고    scopus 로고
    • Roles of O-linked oligosaccharides in immune responses
    • Tsuboi, S. and Fukuda, M. (2001) Roles of O-linked oligosaccharides in immune responses. Bioessays, 23, 46-53.
    • (2001) Bioessays , vol.23 , pp. 46-53
    • Tsuboi, S.1    Fukuda, M.2
  • 47
    • 0141733062 scopus 로고    scopus 로고
    • Structurally distinct requirements for binding of P-selectin glycoprotein ligand-1 and sialyl Lewis x to Anaplasma phagocytophilum and P-selectin
    • Yago, T., Leppanen, A., Carlyon, J.A., Akkoyunlu, M., Karmakar, S., Fikrig, E., Cummings, R.D., and McEver, R.P. (2003) Structurally distinct requirements for binding of P-selectin glycoprotein ligand-1 and sialyl Lewis x to Anaplasma phagocytophilum and P-selectin. J. Biol. Chem., 278, 37987-37997.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37987-37997
    • Yago, T.1    Leppanen, A.2    Carlyon, J.A.3    Akkoyunlu, M.4    Karmakar, S.5    Fikrig, E.6    Cummings, R.D.7    McEver, R.P.8
  • 48
    • 0037131298 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel alpha 1,2-fucosyltransferase (CE2FT-1) from Caenorhabditis elegans
    • Zheng, Q., Van Die, I., and Cummings, R.D. (2002) Molecular cloning and characterization of a novel alpha 1,2-fucosyltransferase (CE2FT-1) from Caenorhabditis elegans. J. Biol. Chem., 277, 39823-39832.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39823-39832
    • Zheng, Q.1    Van Die, I.2    Cummings, R.D.3
  • 49
    • 4744347867 scopus 로고    scopus 로고
    • Caenorhabditis elegans triple null mutant lacking UDP-N-acetyl-D-glucosamine: Alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I
    • Zhu, S., Hanneman, A., Reinhold, V.N., Spence, A.M., and Schachter, H. (2004) Caenorhabditis elegans triple null mutant lacking UDP-N-acetyl-D-glucosamine: Alpha-3-D-mannoside beta1,2-N-acetylglucosaminyltransferase I. Biochem. J., 382, 995-1001.
    • (2004) Biochem. J. , vol.382 , pp. 995-1001
    • Zhu, S.1    Hanneman, A.2    Reinhold, V.N.3    Spence, A.M.4    Schachter, H.5


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