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Volumn 8, Issue 1, 1998, Pages 77-85

Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae

Author keywords

Complementation cloning; Conditional lethality; Dolichol cycle; Glycosyltransferase; Heterologous expression

Indexed keywords

GLYCOSYLTRANSFERASE;

EID: 0031910552     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/8.1.77     Document Type: Article
Times cited : (30)

References (55)
  • 2
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J.D., Truehyrt, J., Natsoulis, G. and Fink, G. (1987) 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol., 154, 164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Truehyrt, J.2    Natsoulis, G.3    Fink, G.4
  • 3
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-cholroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-cholroform extraction. Anal. Biochem., 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 4
    • 0027180887 scopus 로고
    • Both potential dolichol recognition sequences of hamster GlcNAc-1 -phosphate transferase are necessary for normal enzyme function
    • Datta, A. and Lehrman, M.A. (1993) Both potential dolichol recognition sequences of hamster GlcNAc-1 -phosphate transferase are necessary for normal enzyme function. J. Biol. Chem., 268, 12663-12668.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12663-12668
    • Datta, A.1    Lehrman, M.A.2
  • 5
    • 0002358832 scopus 로고    scopus 로고
    • GPI-anchors: Structure and functions
    • Gabius, H.-J. and Gabius, S. (eds.) Chapman and Hall, Weinheim, Germany
    • Eckert, V., Gerold, P. and Schwarz, R.T. (1997) GPI-anchors: structure and functions. In Gabius, H.-J. and Gabius, S. (eds.) Glycosciences. Chapman and Hall, Weinheim, Germany, pp. 223-243.
    • (1997) Glycosciences , pp. 223-243
    • Eckert, V.1    Gerold, P.2    Schwarz, R.T.3
  • 6
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein, A.D. (1987) Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem., 56, 497-534.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 7
    • 0025894942 scopus 로고
    • A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus EG1
    • Elledge, J.S. and Spottswood, M.R. (1991) A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus EG1. EMBO J., 19, 2653-2659.
    • (1991) EMBO J. , vol.19 , pp. 2653-2659
    • Elledge, J.S.1    Spottswood, M.R.2
  • 8
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K. and Simons, K. (1995) The role of N-glycans in the secretory pathway. Cell, 81, 309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 9
    • 0028086445 scopus 로고
    • Glycosylphosphatidylinositols synthesized by asexuell erythrocytic stages of the malaria parasite Plasmodium falciparum
    • Gerold, P., Dieckmann-Schuppert, A. and Schwarz, R.T. (1994) Glycosylphosphatidylinositols synthesized by asexuell erythrocytic stages of the malaria parasite Plasmodium falciparum. J. Biol. Chem., 269, 2597-2606.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2597-2606
    • Gerold, P.1    Dieckmann-Schuppert, A.2    Schwarz, R.T.3
  • 10
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C. Braakman, I. and Helenius, A. (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA, 91, 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 11
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C. and Helenius, A. (1995) Quality control in the secretory pathway. Curr. Opinion Cell. Biol., 7, 523-529.
    • (1995) Curr. Opinion Cell. Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 12
    • 0011647008 scopus 로고
    • Genomic sequence coding for tunicamycin resistance in yeast
    • Hartog, K.O. and Bishop, B. (1987) Genomic sequence coding for tunicamycin resistance in yeast. Nucleic Acids Res., 15, 3627.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3627
    • Hartog, K.O.1    Bishop, B.2
  • 13
    • 50549218525 scopus 로고
    • The limited in vitro lifetime of human diploid cell strains
    • Hayflick, L. (1965) The limited in vitro lifetime of human diploid cell strains. Exp. Cell Res., 37, 614-636.
    • (1965) Exp. Cell Res. , vol.37 , pp. 614-636
    • Hayflick, L.1
  • 14
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformantion of Escherichia coli
    • Hoffman, C.S. and Winston, F. (1987) A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformantion of Escherichia coli. Gene, 57, 267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 15
    • 0021067823 scopus 로고
    • Yeast mutants deficient in protein glycosylation
    • Huffaker, T.C. and Robbins, P.W. (1983) Yeast mutants deficient in protein glycosylation. Proc. Natl. Acad. Sci. USA., 80, 7466-7470.
    • (1983) Proc. Natl. Acad. Sci. USA. , vol.80 , pp. 7466-7470
    • Huffaker, T.C.1    Robbins, P.W.2
  • 16
    • 0028012014 scopus 로고
    • Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates
    • Ioffe, E. and Stanley, P. (1994) Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates. Proc. Natl. Acad. Sci. USA, 91, 728-732.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 728-732
    • Ioffe, E.1    Stanley, P.2
  • 17
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukada, Y., Murata, K. and Kimura, (1983) Transformation of intact yeast cells treated with alkali cations. J. Bacteriol., 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura4
  • 18
    • 0021471049 scopus 로고
    • Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae
    • Johnston, M. and Davis, R.W. (1984) Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae. Mol. Cell. Biol., 4, 1440-1448.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1440-1448
    • Johnston, M.1    Davis, R.W.2
  • 19
    • 0028194854 scopus 로고
    • Glycosidase inhibitors in study of glycoconjugates
    • Kaushal, G.P. and Elbein, A.D. (1994) Glycosidase inhibitors in study of glycoconjugates. Methods Enzymol., 239, 316-329.
    • (1994) Methods Enzymol. , vol.239 , pp. 316-329
    • Kaushal, G.P.1    Elbein, A.D.2
  • 20
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 21
    • 0023228402 scopus 로고
    • Protein glycosylation in yeast: Tanscript heterogeneity of the ALG7 gene
    • Kukuruzinska, M.A. and Robbins, P.W. (1987) Protein glycosylation in yeast: tanscript heterogeneity of the ALG7 gene. Proc. Natl. Acad. Sci. USA, 84, 2145-2149.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2145-2149
    • Kukuruzinska, M.A.1    Robbins, P.W.2
  • 22
    • 0026332261 scopus 로고
    • Biosynthesis of N-aetylglucosamine-P-P-dolichol, the committed step of asparagine-linked oligosaccharide assembly
    • Lehrman, M.A. (1991) Biosynthesis of N-aetylglucosamine-P-P-dolichol, the committed step of asparagine-linked oligosaccharide assembly. Glycobiology, 1, 553-562.
    • (1991) Glycobiology , vol.1 , pp. 553-562
    • Lehrman, M.A.1
  • 23
    • 0024259876 scopus 로고
    • Amplification and molecular cloning of the hamster tunicamycin-sensitive N-acetylglucosamine-1- Phosphate transferase gene
    • Lehrman, M.A., Zhu, X. and Khounlo, S. (1988) Amplification and molecular cloning of the hamster tunicamycin-sensitive N-acetylglucosamine-1- phosphate transferase gene. J. Biol. Chem., 263, 19796-19803.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19796-19803
    • Lehrman, M.A.1    Zhu, X.2    Khounlo, S.3
  • 24
    • 0026709847 scopus 로고
    • The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania amazonensis contains a functional N-acetylglucosamine-1-phosphate transferase gene that can be used as a dominant selectable marker in transfection
    • Liu, X. and Chang, K.-P. (1992) The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania amazonensis contains a functional N-acetylglucosamine-1-phosphate transferase gene that can be used as a dominant selectable marker in transfection. Mol. Cell. Biol., 12, 4112-4122.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4112-4122
    • Liu, X.1    Chang, K.-P.2
  • 25
    • 0029042961 scopus 로고
    • Gene disruption with PCR products in Saccharomyces cerevisiae
    • Lorenz, M.C., Muir, R.S., Lim, E., McElver, J., Weber, S.C. and Heitman, J. (1995) Gene disruption with PCR products in Saccharomyces cerevisiae. Gene, 158, 113-117.
    • (1995) Gene , vol.158 , pp. 113-117
    • Lorenz, M.C.1    Muir, R.S.2    Lim, E.3    McElver, J.4    Weber, S.C.5    Heitman, J.6
  • 26
    • 0029120399 scopus 로고
    • Microhomology mediated PCR targeting in Saccharomyces cerevisiae
    • Manivasakam, P., Weber, S.C., McElver, J. and Schistel, R.H. (1995) Microhomology mediated PCR targeting in Saccharomyces cerevisiae. Nucleic Acids Res., 23, 2799-2800.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2799-2800
    • Manivasakam, P.1    Weber, S.C.2    McElver, J.3    Schistel, R.H.4
  • 27
    • 0028263131 scopus 로고
    • Will the transgenic mouse serve as a rosetta stone to glycoconjugate function?
    • Marth, J.D. (1994) Will the transgenic mouse serve as a rosetta stone to glycoconjugate function? Glycoconjugate J., 11, 3-8.
    • (1994) Glycoconjugate J. , vol.11 , pp. 3-8
    • Marth, J.D.1
  • 28
    • 0029838294 scopus 로고    scopus 로고
    • Cloning and functional expression of glycosyltransferases from parasitic protozoa by heterologous complementation in yeast: The Dol-P-Man synthase from Trypanosoma brucei brucei
    • Mazhari-Tabrizi, R., Eckert, V., Blank, M., Muller, R., Mumberg, D., Funk, M. and Schwarz, R.T. (1996) Cloning and functional expression of glycosyltransferases from parasitic protozoa by heterologous complementation in yeast: the Dol-P-Man synthase from Trypanosoma brucei brucei. Biochem. J., 316, 853-858.
    • (1996) Biochem. J. , vol.316 , pp. 853-858
    • Mazhari-Tabrizi, R.1    Eckert, V.2    Blank, M.3    Muller, R.4    Mumberg, D.5    Funk, M.6    Schwarz, R.T.7
  • 29
    • 2642707041 scopus 로고
    • Lipid-mediated protein glycosylation: Assembly of lipid linked oligosaccharides and post-translational oligosaccharide trimming
    • Brodbeck, U. and Bordier, C. (eds.), C. Springer, Berlin
    • McDowell, W. and Schwarz, R.T. (1988) Lipid-mediated protein glycosylation: assembly of lipid linked oligosaccharides and post-translational oligosaccharide trimming. In Brodbeck, U. and Bordier, C. (eds.), Posttranslational Modifications of Proteins by Lipids. C. Springer, Berlin, pp. 99-118.
    • (1988) Posttranslational Modifications of Proteins by Lipids , pp. 99-118
    • McDowell, W.1    Schwarz, R.T.2
  • 30
    • 0028213962 scopus 로고
    • Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development
    • Metzler, M., Gertz, A., Sarkar, M., Schachter, H., Schrader, J.W. and Marth, J.D. (1994) Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development. EMBO J., 13, 2056-2065.
    • (1994) EMBO J. , vol.13 , pp. 2056-2065
    • Metzler, M.1    Gertz, A.2    Sarkar, M.3    Schachter, H.4    Schrader, J.W.5    Marth, J.D.6
  • 31
    • 0026864596 scopus 로고
    • Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thalania cDNAs
    • Minet, M., Dufour, M.-E. and Lacroute, F. (1992) Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thalania cDNAs. Plant J., 2, 417-422.
    • (1992) Plant J. , vol.2 , pp. 417-422
    • Minet, M.1    Dufour, M.-E.2    Lacroute, F.3
  • 32
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: Comparison of transcriptional activity and their use for heterologous expression
    • Mumberg, D., Müller, R. and Funk, M. (1994) Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res., 22, 5767-5768.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Müller, R.2    Funk, M.3
  • 33
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S.B. and Wunsch, C.D. (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol., 48, 443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 34
    • 0026714548 scopus 로고
    • Mouse UDP-GlcNAc: Dolichyl-phosphate N-acetylglucosaminephosphotransferase. Molecular cloning of the cDNA, generation of anti-peptide antibodies and chromosomal location
    • Rajput, B., Ma, J., Munipappa, N., Schantz, L., Naylor, S.L., Lalley, P.A. and Vijay, I.K. (1992) Mouse UDP-GlcNAc: dolichyl-phosphate N-acetylglucosaminephosphotransferase. Molecular cloning of the cDNA, generation of anti-peptide antibodies and chromosomal location. Biochem. J., 285, 985-992.
    • (1992) Biochem. J. , vol.285 , pp. 985-992
    • Rajput, B.1    Ma, J.2    Munipappa, N.3    Schantz, L.4    Naylor, S.L.5    Lalley, P.A.6    Vijay, I.K.7
  • 35
    • 0028235766 scopus 로고
    • Structure and organization of mouse GlcNAc-1-phosphate transferase gene
    • Rajput, B., Ma, J. and Vijay, I.K. (1994) Structure and organization of mouse GlcNAc-1-phosphate transferase gene. J. Biol. Chem., 269, 9590-9597.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9590-9597
    • Rajput, B.1    Ma, J.2    Vijay, I.K.3
  • 36
    • 0003191839 scopus 로고
    • Targeted selection of recombinant clones through gene dosage effects
    • Rine, J., Hansen, W., Hardeman, E. and Davis, R.W. (1983) Targeted selection of recombinant clones through gene dosage effects. Proc. Natl. Acad. Sci. USA, 80, 6750-6754.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6750-6754
    • Rine, J.1    Hansen, W.2    Hardeman, E.3    Davis, R.W.4
  • 38
    • 0001709752 scopus 로고
    • Glycosyltransferases involved in the synthesis of N-glycan antennae
    • Montreul, J., Vliegenhthart, J.F.G. and Schachter, H. (eds.), Elsevier, Amsterdam
    • Schachter, H. (1995) Glycosyltransferases involved in the synthesis of N-glycan antennae. In Montreul, J., Vliegenhthart, J.F.G. and Schachter, H. (eds.), Glycoproteins 29a. Elsevier, Amsterdam, pp. 153-199.
    • (1995) Glycoproteins 29a , pp. 153-199
    • Schachter, H.1
  • 39
    • 0029025250 scopus 로고
    • The yeast spt14 gene is homologous to the human PIG-A gene and is required for GPI anchor synthesis
    • Schönbächler, M., Horvath, A., Fassler, J. and Riezman, H. (1995) The yeast spt14 gene is homologous to the human PIG-A gene and is required for GPI anchor synthesis. EMBO J., 14, 1637-1645.
    • (1995) EMBO J. , vol.14 , pp. 1637-1645
    • Schönbächler, M.1    Horvath, A.2    Fassler, J.3    Riezman, H.4
  • 40
    • 0025250562 scopus 로고
    • Sequence of a cDNA that specifies the uridine diphosphate N-acetyl-d-glucosamine:dolichol phosphate N-acetylglucosamine-1-phosphate transferase from Chinese hamster ovary cells
    • Scocca, J.R. and Krag, S.S. (1990) Sequence of a cDNA that specifies the uridine diphosphate N-acetyl-d-glucosamine:dolichol phosphate N-acetylglucosamine-1-phosphate transferase from Chinese hamster ovary cells. J. Biol. Chem., 265, 20621-20626.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20621-20626
    • Scocca, J.R.1    Krag, S.S.2
  • 41
    • 0028821431 scopus 로고
    • Genomic organization and expression of hamster UDP-N-acetylglucosamine: Dolichyl phosphate N-acetylglucosaminyl phosphoryl transferase
    • Scocca, J.R., Zou, J. and Krag, S.S. (1995) Genomic organization and expression of hamster UDP-N-acetylglucosamine: dolichyl phosphate N-acetylglucosaminyl phosphoryl transferase. Glycobiology, 5, 129-136.
    • (1995) Glycobiology , vol.5 , pp. 129-136
    • Scocca, J.R.1    Zou, J.2    Krag, S.S.3
  • 42
    • 0027363638 scopus 로고
    • The purification and characterisation of recombinant yeast dolichyl-phosphate-mannose synthase
    • Schutzbach, J.S., Zimmerman, J.W. and Forsee, T.W. (1993) The purification and characterisation of recombinant yeast dolichyl-phosphate-mannose synthase. J. Biol Chem., 268, 24190-24196.
    • (1993) J. Biol Chem. , vol.268 , pp. 24190-24196
    • Schutzbach, J.S.1    Zimmerman, J.W.2    Forsee, T.W.3
  • 43
    • 0002442740 scopus 로고
    • Inhibitors of protein glycosylation
    • Schwarz, R.T. and Datema, R. (1980) Inhibitors of protein glycosylation. Trends Biochem. Sci., 5, 65-67.
    • (1980) Trends Biochem. Sci. , vol.5 , pp. 65-67
    • Schwarz, R.T.1    Datema, R.2
  • 44
    • 0020389383 scopus 로고
    • The lipid pathway of protein glycosylation and its inhibitors: The biological significance of protein-bound carbohydrates
    • Schwarz, R.T. and Datema, R. (1982) The lipid pathway of protein glycosylation and its inhibitors: the biological significance of protein-bound carbohydrates. Adv. Carbohydr. Chem. Biochem., 40, 287-379.
    • (1982) Adv. Carbohydr. Chem. Biochem. , vol.40 , pp. 287-379
    • Schwarz, R.T.1    Datema, R.2
  • 45
    • 0016248170 scopus 로고
    • The role of dolicolmonophosphate in glycoprotein biosynthesis in Saccharomyces cerevisiae
    • Sharma, C.B., Babczinski, P., Uhle, and Tanner, W. (1974) The role of dolicolmonophosphate in glycoprotein biosynthesis in Saccharomyces cerevisiae. Eur. J. Biochem., 46, 35-41.
    • (1974) Eur. J. Biochem. , vol.46 , pp. 35-41
    • Sharma, C.B.1    Babczinski, P.2    Uhle3    Tanner, W.4
  • 46
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 47
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa, M.C., Ferrero-Garcia, M.A. and Parodi, A.J. (1992) Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry, 31, 95-107.
    • (1992) Biochemistry , vol.31 , pp. 95-107
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 48
    • 0028845998 scopus 로고
    • Glycosyltransferase mutants: Key to new insights in glycobiology
    • Stanley, p., and Ioffe, E. (1995) Glycosyltransferase mutants: key to new insights in glycobiology. FASEB J., 9, 1436-1444.
    • (1995) FASEB J. , vol.9 , pp. 1436-1444
    • Stanley, P.1    Ioffe, E.2
  • 50
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 51
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • Von Heijne, G. (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem., 133, 17-21.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 52
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Pöhlmann, R. and Philippsen, P. (1994) New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast, 10, 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pöhlmann, R.3    Philippsen, P.4
  • 53
    • 0028228350 scopus 로고
    • Role of the carboxyl terminus in stable expression of hamster UDP-GlcNAc:Dolichol-PGlcNAc-1-P transferase
    • Zara, J. and Lehrman, M.A. (1994) Role of the carboxyl terminus in stable expression of hamster UDP-GlcNAc:dolichol-PGlcNAc-1-P transferase. J. Biol. Chem., 269, 19108-19115.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19108-19115
    • Zara, J.1    Lehrman, M.A.2
  • 54
    • 0025143111 scopus 로고
    • Cloning, sequence and expression of a cDNA encoding hamster UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase
    • Zhu, X. and Lehrman, M.A. (1990) Cloning, sequence and expression of a cDNA encoding hamster UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase. J. Biol. Chem., 265, 14250-14255.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14250-14255
    • Zhu, X.1    Lehrman, M.A.2
  • 55
    • 0028928033 scopus 로고
    • Asparagine-linked glycosylation in Schizosaccharomyces pombe: Functional conservation of the first step in oligosaccharide-lipid assembly
    • Zou, J., Scocca, J.R. and Krag, S.S. (1995) Asparagine-linked glycosylation in Schizosaccharomyces pombe: functional conservation of the first step in oligosaccharide-lipid assembly. Arch. Biochem. Biophys., 317, 487-496.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 487-496
    • Zou, J.1    Scocca, J.R.2    Krag, S.S.3


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