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Volumn 9, Issue 11, 1999, Pages 1263-1271

A recessive deletion in the GlcNAc-1-phosphotransferase gene results in peri-implantation embryonic lethality

Author keywords

Embryogenesis; GPT gene; Mouse; Peri implantation

Indexed keywords

ASPARAGINE; DOLICHOL; OLIGOSACCHARIDE; PHOSPHOTRANSFERASE; TUNICAMYCIN;

EID: 0032743959     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/9.11.1263     Document Type: Article
Times cited : (122)

References (51)
  • 1
    • 0022552940 scopus 로고
    • N-Linked glycoprotein biosynthesis in the developing mouse embryo
    • Armant,D.R., Kaplan,H.A. and Lennarz,W.J. (1986) N-Linked glycoprotein biosynthesis in the developing mouse embryo. Dev. Biol., 113, 228-237.
    • (1986) Dev. Biol. , vol.113 , pp. 228-237
    • Armant, D.R.1    Kaplan, H.A.2    Lennarz, W.J.3
  • 2
    • 0019302861 scopus 로고
    • Effects of tunicamycin upon glycoprotein synthesis and development of early mouse embryos
    • Atienza-Samols,S.B., Pine,P.R. and Sherman,M.I. (1980) Effects of tunicamycin upon glycoprotein synthesis and development of early mouse embryos. Dev. Biol., 79, 19-32.
    • (1980) Dev. Biol. , vol.79 , pp. 19-32
    • Atienza-Samols, S.B.1    Pine, P.R.2    Sherman, M.I.3
  • 3
    • 0030025880 scopus 로고    scopus 로고
    • Immunological prevention of spontaneous early embryo resorption is mediated by non-specific immunosimulation
    • Baines,M.G., Duclos,A.J., de Fougerolles,A.R. and Gendron,R.L. (1996) Immunological prevention of spontaneous early embryo resorption is mediated by non-specific immunosimulation. Am J. Reprod Immunol., 35, 34-42.
    • (1996) Am J. Reprod Immunol. , vol.35 , pp. 34-42
    • Baines, M.G.1    Duclos, A.J.2    De Fougerolles, A.R.3    Gendron, R.L.4
  • 4
    • 0016827217 scopus 로고
    • Tunicamycin, an inhibitor or Bacillus peptidoglycan biosynthesis: A new site of inhibition
    • Bettinger,G.E. and Young,F.E. (1975) Tunicamycin, an inhibitor or Bacillus peptidoglycan biosynthesis: a new site of inhibition. Biochem. Biophys Res. Commun., 67, 16-21.
    • (1975) Biochem. Biophys Res. Commun. , vol.67 , pp. 16-21
    • Bettinger, G.E.1    Young, F.E.2
  • 6
    • 0030020795 scopus 로고    scopus 로고
    • Stimulatory effect of PDGF on HMG-CoA reductase activity and N-linked glycosylation contributes to increased expression of IGF-1 receptors in human fibroblasts
    • Carlberg,M. and Larsson,O. (1996) Stimulatory effect of PDGF on HMG-CoA reductase activity and N-linked glycosylation contributes to increased expression of IGF-1 receptors in human fibroblasts. Exp. Cell Res., 223, 142-148.
    • (1996) Exp. Cell Res. , vol.223 , pp. 142-148
    • Carlberg, M.1    Larsson, O.2
  • 8
    • 0027180887 scopus 로고
    • Both potential dolichol recognition sequences of hamster GlcNAc-1- phosphate transferase are necessary for normal enzyme function
    • Datta,A.K. 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.K.1    Lehrman, M.A.2
  • 9
    • 0019086931 scopus 로고
    • Inhibition of lysosomal alpha-mannosidase by swainsonine, an indolizidine alkaloid isolated from Swainsona canescens
    • Dorling,P.R., Huxtable,C.R. and Colegate,S.M. (1980) Inhibition of lysosomal alpha-mannosidase by swainsonine, an indolizidine alkaloid isolated from Swainsona canescens. Biochem. J., 191, 649-651.
    • (1980) Biochem. J. , vol.191 , pp. 649-651
    • Dorling, P.R.1    Huxtable, C.R.2    Colegate, S.M.3
  • 10
    • 0019161734 scopus 로고
    • Streptovirudin and tunicamycin, two inhibitors of glycolipid synthesis. Differentiation by use of gel chromatography, H.P.L.C. and hydrolysis
    • Eckardt,K., Wetzstein,H., Thrum,H. and Ihn,W. (1980) Streptovirudin and tunicamycin, two inhibitors of glycolipid synthesis. Differentiation by use of gel chromatography, H.P.L.C. and hydrolysis. J. Antibiot. (Tokyo), 33, 908-910.
    • (1980) J. Antibiot. (Tokyo) , vol.33 , pp. 908-910
    • Eckardt, K.1    Wetzstein, H.2    Thrum, H.3    Ihn, W.4
  • 11
    • 0031910552 scopus 로고    scopus 로고
    • 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 Saccaromyces cerevisiae
    • Eckert,V., Blank,M., Mazhari-Tabrizi,R., Mumberg,D., Funk,M and Schwarz,R.T. (1998) 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 Saccaromyces cerevisiae. Glycobiology, 8, 77-85.
    • (1998) Glycobiology , vol.8 , pp. 77-85
    • Eckert, V.1    Blank, M.2    Mazhari-Tabrizi, R.3    Mumberg, D.4    Funk, M.S.5
  • 13
    • 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
  • 14
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert,D.N., Foellmer,B. and Helenius,A. (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell, 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 15
    • 0017646948 scopus 로고
    • Studies of the mechanism of tunicamycin inhibition of IgA and IgE secretion by plasma cells
    • Hickman,S., Kulczycki,A., Lynch,R.G. and Kornfeld,S. (1977) Studies of the mechanism of tunicamycin inhibition of IgA and IgE secretion by plasma cells. J. Biol. Chem., 252, 4402-4408.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4402-4408
    • Hickman, S.1    Kulczycki, A.2    Lynch, R.G.3    Kornfeld, S.4
  • 17
    • 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
  • 18
    • 0030668548 scopus 로고    scopus 로고
    • Complex N-glycans in Mgat1 null preimplantation embryos arise from maternal Mgatl RNA
    • Ioffe,E., Liu,Y. and Stanley,P. (1997) Complex N-glycans in Mgat1 null preimplantation embryos arise from maternal Mgatl RNA. Glycobiology, 7, 913-919.
    • (1997) Glycobiology , vol.7 , pp. 913-919
    • Ioffe, E.1    Liu, Y.2    Stanley, P.3
  • 19
    • 0031019482 scopus 로고    scopus 로고
    • Syndrome of the month: Carbohydrate-deficient glycoprotein (CDG) syndrome type I
    • Jaeken,J., Matthijs,G., Barone,R. and Carchon,H. (1997) Syndrome of the month: carbohydrate-deficient glycoprotein (CDG) syndrome type I. J. Med. Genet., 34, 73-76.
    • (1997) J. Med. Genet. , vol.34 , pp. 73-76
    • Jaeken, J.1    Matthijs, G.2    Barone, R.3    Carchon, H.4
  • 20
    • 0027938489 scopus 로고
    • N-glycosylation of erythropoietin is critical for apical secretion by Mardin-Darby canine kidney cells
    • Kitagawa,Y., Sano,Y., Ueda,M., Higashio K., Narita H., Okano,M., Matsumoto,S. and Sasaki,R. (1994) N-glycosylation of erythropoietin is critical for apical secretion by Mardin-Darby canine kidney cells. Exp. Cell Res., 213, 449-457.
    • (1994) Exp. Cell Res. , vol.213 , pp. 449-457
    • Kitagawa, Y.1    Sano, Y.2    Ueda, M.3    Higashio, K.4    Narita, H.5    Okano, M.6    Matsumoto, S.7    Sasaki, R.8
  • 21
    • 0023919087 scopus 로고
    • Glycosylation of CD4. Tunicamycin inhibits surface expression
    • Konig,R., Ashwell,G. and Hanover,J.A. (1988) Glycosylation of CD4. Tunicamycin inhibits surface expression. J. Biol. Chem., 263, 9502-9507.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9502-9507
    • Konig, R.1    Ashwell, G.2    Hanover, J.A.3
  • 22
    • 0029085605 scopus 로고
    • Retention of glucose units added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
    • Labriola,C., Cazzulo,J.J. and Parodi,A.J. (1995) Retention of glucose units added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum. J. Cell Biol., 130, 771-779.
    • (1995) J. Cell Biol. , vol.130 , pp. 771-779
    • Labriola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 23
    • 0017181626 scopus 로고
    • The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivatives
    • Lehle,L. and Tanner,W. (1976) The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivatives. FEBS Lett., 71, 167-170.
    • (1976) FEBS Lett. , vol.71 , pp. 167-170
    • Lehle, L.1    Tanner, W.2
  • 24
    • 0031080163 scopus 로고    scopus 로고
    • Zp3-cre, a transgenic mouse line for the activation or inactivation of loxP-flanked target genes specifically in the female germ line
    • Lewandoski,M., Wassarman,K.M. and Martin,G.R. (1997) Zp3-cre, a transgenic mouse line for the activation or inactivation of loxP-flanked target genes specifically in the female germ line. Curr. Biol., 7, 148-151.
    • (1997) Curr. Biol. , vol.7 , pp. 148-151
    • Lewandoski, M.1    Wassarman, K.M.2    Martin, G.R.3
  • 25
    • 0029784528 scopus 로고    scopus 로고
    • Inactivation of the mouse Brcal gene leads to failure in the morphogenesis of the egg cylinder in early postimplantation development
    • Liu,C.Y., Flesken-Nikitin,A., Li,S., Zeng,Y. and Lee,W.H. (1996) Inactivation of the mouse Brcal gene leads to failure in the morphogenesis of the egg cylinder in early postimplantation development. Genes Dev., 10, 1835-1843.
    • (1996) Genes Dev. , vol.10 , pp. 1835-1843
    • Liu, C.Y.1    Flesken-Nikitin, A.2    Li, S.3    Zeng, Y.4    Lee, W.H.5
  • 26
    • 0021052508 scopus 로고
    • Formation of proteoglycan aggregates in rat chondrosarcoma chondrocyte cultures treated with tunicamycin
    • Lohmander,L.S., Fellini,S.A., Kimura,J.H., Stevens,R.L. and Hascall,V.C. (1983) Formation of proteoglycan aggregates in rat chondrosarcoma chondrocyte cultures treated with tunicamycin. J. Biol. Chem., 258, 12280-12286.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12280-12286
    • Lohmander, L.S.1    Fellini, S.A.2    Kimura, J.H.3    Stevens, R.L.4    Hascall, V.C.5
  • 27
    • 0029989219 scopus 로고    scopus 로고
    • Recent advances in gene mutagenesis by site-directed recombination
    • Marth,J.D. (1996) Recent advances in gene mutagenesis by site-directed recombination, J. Clin. Invest., 97, 1999-2002.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1999-2002
    • Marth, J.D.1
  • 28
    • 0025777285 scopus 로고
    • Glycosylation, activity and secretion of lipoprotein lipase in cultured brown adipocytes of newborn mice. Effect of tunicamycin, monensin, 1-deoxymannojirimycin and swainsonine
    • Masuno,H., Schultz,C.J., Park,J.W., Blanchette-Mackie,E.J., MAteo,C. and Scow,R.O. (1991) Glycosylation, activity and secretion of lipoprotein lipase in cultured brown adipocytes of newborn mice. Effect of tunicamycin, monensin, 1-deoxymannojirimycin and swainsonine. Biochem. J., 277, 801-809.
    • (1991) Biochem. J. , vol.277 , pp. 801-809
    • Masuno, H.1    Schultz, C.J.2    Park, J.W.3    Blanchette-Mackie, E.J.4    MAteo, C.5    Scow, R.O.6
  • 29
    • 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
  • 30
    • 0026437775 scopus 로고
    • Tunicamycin-induced inhibition of functional expression of glutamate receptors in Xenopus oocytes
    • Musshof,U., Madeja,M., Bloms,P., Musch-Nittel,K. and Speckmann,E.J. (1992) Tunicamycin-induced inhibition of functional expression of glutamate receptors in Xenopus oocytes. Neurosci. Lett., 147, 163-166.
    • (1992) Neurosci. Lett. , vol.147 , pp. 163-166
    • Musshof, U.1    Madeja, M.2    Bloms, P.3    Musch-Nittel, K.4    Speckmann, E.J.5
  • 31
    • 0026764280 scopus 로고
    • Tissue- and site-specific DNA recombination in transgenic mice
    • Orban,P.C., Chui,D. and Marth,J.D. (1992) Tissue- and site-specific DNA recombination in transgenic mice. Proc. Natl Acad. Sci. USA, 89, 6861-6865.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6861-6865
    • Orban, P.C.1    Chui, D.2    Marth, J.D.3
  • 32
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou,W.-J., Cameron,P.H., Thomas,D.Y. and Bergeron,J.J.M. (1993) Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature, 364, 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.-J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 33
    • 0028123665 scopus 로고
    • Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension
    • Patterson,S.I. and Skene,J.H. (1994) Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension. J. Cell Biol., 124, 521-536.
    • (1994) J. Cell Biol. , vol.124 , pp. 521-536
    • Patterson, S.I.1    Skene, J.H.2
  • 34
    • 0023186834 scopus 로고
    • Oocyte-specific expression and developmental regulation of ZP3, the sperm receptor of the mouse zona pellucida
    • Philpott,C.C., Ringuette,M.J. and Dean,J. (1987) Oocyte-specific expression and developmental regulation of ZP3, the sperm receptor of the mouse zona pellucida. Dev. Biol., 121, 568-575.
    • (1987) Dev. Biol. , vol.121 , pp. 568-575
    • Philpott, C.C.1    Ringuette, M.J.2    Dean, J.3
  • 35
    • 0031054637 scopus 로고    scopus 로고
    • Isolation, characterization and inactivation of the mouse Mgat3 gene: The bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction
    • Priatel,J.J., Sarkar,M., Schachter,H. and Marth,J.D. (1997) Isolation, characterization and inactivation of the mouse Mgat3 gene: the bisecting N-acetylglucosamine in asparagine-linked oligosaccharides appears dispensable for viability and reproduction. Glycobiology, 7, 45-56.
    • (1997) Glycobiology , vol.7 , pp. 45-56
    • Priatel, J.J.1    Sarkar, M.2    Schachter, H.3    Marth, J.D.4
  • 36
    • 0026714548 scopus 로고
    • Mouse UDP-GlcNAc: Dolichyl-phosphate N-acetylglucosaminephosphotransferase. Molecular cloning of the cDNA, generation of anti-peptide antibodies and chromosomal localization
    • Rajput,B., Ma,J., Muniappa,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 localization. Biochem. J., 285, 985-992.
    • (1992) Biochem. J. , vol.285 , pp. 985-992
    • Rajput, B.1    Ma, J.2    Muniappa, N.3    Schantz, L.4    Naylor, S.L.5    Lalley, P.A.6    Vijay, I.K.7
  • 37
    • 0028340566 scopus 로고
    • Developmental and hormonal regulation of UDP-GlcNAc:dolichol phosphate GlcNAc-1-P transferase in mouse mammary gland
    • Rajput,B., Muniappa,N. and Vijay,I.K. (1994a) Developmental and hormonal regulation of UDP-GlcNAc:dolichol phosphate GlcNAc-1-P transferase in mouse mammary gland. J. Biol. Chem., 269, 16054-16061.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16054-16061
    • Rajput, B.1    Muniappa, N.2    Vijay, I.K.3
  • 38
    • 0028235766 scopus 로고
    • Structure and organization of mouse GlcNAc-1-phosphate transferase gene
    • published erratum appears in J. Biol. Chem., 1994, 269, 18703
    • Rajput,B., Ma,J. and Vijay,I.K. (1994b) Structure and organization of mouse GlcNAc-1-phosphate transferase gene [published erratum appears in J. Biol. Chem., 1994, 269, 18703]. 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
  • 39
    • 0023907964 scopus 로고
    • Characterization of the transferrin receptor in tunicamycin-treated A431 cells
    • Reckow,C.L. and Enns,C.A. (1988) Characterization of the transferrin receptor in tunicamycin-treated A431 cells. J. Biol. Chem., 263, 7297-7301.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7297-7301
    • Reckow, C.L.1    Enns, C.A.2
  • 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
    • 0023723665 scopus 로고
    • Purification and characterization of UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase involved in the biosynthesis of asparagine-linked glycoproteins in the mammary gland
    • Shailubhai,K., Dong-Yu,B., Saxena,E.S. and Vijay,I.K. (1988) Purification and characterization of UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase involved in the biosynthesis of asparagine-linked glycoproteins in the mammary gland. J. Biol. Chem., 263, 15964-15972.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15964-15972
    • Shailubhai, K.1    Dong-Yu, B.2    Saxena, E.S.3    Vijay, I.K.4
  • 42
    • 0019959919 scopus 로고
    • Effect of tunicamycin on insulin binding and on proteoglycan synthesis and distribution in Swarm rat chondrosarcoma cell cultures
    • Stevens,R.L., Schwartz,L.B., Austen,K.F., Lohmander,L.S. and Kimura,J.H. (1982) Effect of tunicamycin on insulin binding and on proteoglycan synthesis and distribution in Swarm rat chondrosarcoma cell cultures. J. Biol. Chem., 257, 5745-5750.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5745-5750
    • Stevens, R.L.1    Schwartz, L.B.2    Austen, K.F.3    Lohmander, L.S.4    Kimura, J.H.5
  • 43
    • 0023772161 scopus 로고
    • Effect of tunicamycin on the expression of brain neurotransmitter receptors and voltage-operated channels in Xenopus oocytes
    • Sumikawa,K., Praker,I. and Miledi,R. (1988) Effect of tunicamycin on the expression of brain neurotransmitter receptors and voltage-operated channels in Xenopus oocytes. Brain Res., 464, 191-199.
    • (1988) Brain Res. , vol.464 , pp. 191-199
    • Sumikawa, K.1    Praker, I.2    Miledi, R.3
  • 44
    • 0018714570 scopus 로고
    • Glycoprotein synthesis and inhibition of glycosylation by tunicamycin in preimplantation mouse embryos: Compaction and trophoblast adhesion
    • Surani,M.A. (1979) Glycoprotein synthesis and inhibition of glycosylation by tunicamycin in preimplantation mouse embryos: compaction and trophoblast adhesion. Cell, 18, 217-227.
    • (1979) Cell , vol.18 , pp. 217-227
    • Surani, M.A.1
  • 45
    • 0019861579 scopus 로고
    • Synthesis and role of cell surface glycoproteins in preimplantation mouse development
    • Surani,M.A., Kimber,S.J. and Handyside,A.H. (1981) Synthesis and role of cell surface glycoproteins in preimplantation mouse development. Exp. Cell Res., 133, 331-339.
    • (1981) Exp. Cell Res. , vol.133 , pp. 331-339
    • Surani, M.A.1    Kimber, S.J.2    Handyside, A.H.3
  • 46
    • 0015156164 scopus 로고
    • Effect of tunicamycin on the synthesis of macromolecules in cultures of chick embryo fibroblasts infected with Newcastle disease virus
    • Takasuki,A. and Tamura,G. (1971) Effect of tunicamycin on the synthesis of macromolecules in cultures of chick embryo fibroblasts infected with Newcastle disease virus. J. Antibiot. (Tokyo), 24, 785-794.
    • (1971) J. Antibiot. (Tokyo) , vol.24 , pp. 785-794
    • Takasuki, A.1    Tamura, G.2
  • 47
    • 0031300055 scopus 로고    scopus 로고
    • Tunicamycin in combination with retinoic acid synergistically inhibits cell growth while decreasing palmitoylation and enhancing retinoylation of proteins in the human breast cancer cell line MCF-7
    • Takahashi,N., Iwahori,A., Breitman,T.R. and Fukui,T. (1997) Tunicamycin in combination with retinoic acid synergistically inhibits cell growth while decreasing palmitoylation and enhancing retinoylation of proteins in the human breast cancer cell line MCF-7. Oncol. Res., 9, 527-533.
    • (1997) Oncol. Res. , vol.9 , pp. 527-533
    • Takahashi, N.1    Iwahori, A.2    Breitman, T.R.3    Fukui, T.4
  • 48
    • 0028831386 scopus 로고
    • Tunicamycin inhibits the epxression of functional thrombin receptors on human T-lymphoblastoid cells
    • Tordai,A., Brass,L.F. and Gelfand,E.W. (1995) Tunicamycin inhibits the epxression of functional thrombin receptors on human T-lymphoblastoid cells. Biochem. Biophys. Res. Commun., 206, 857-862.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 857-862
    • Tordai, A.1    Brass, L.F.2    Gelfand, E.W.3
  • 49
    • 0019298350 scopus 로고
    • Biosynthesis of mammary glycoproteins. Partial characterization of the sequence for the assembly of lipid-linked saccharides
    • Vijay,I.K., Perdew,G.H. and Lewis,D.E. (1980) Biosynthesis of mammary glycoproteins. Partial characterization of the sequence for the assembly of lipid-linked saccharides. J. Biol. Chem., 255, 11210-11220.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11210-11220
    • Vijay, I.K.1    Perdew, G.H.2    Lewis, D.E.3
  • 50
    • 0022975113 scopus 로고
    • Tunicamycin inhibits proteoglycan biosynthesis in rat ovarian granulosa cells in culture
    • Yanagishita,M. (1986) Tunicamycin inhibits proteoglycan biosynthesis in rat ovarian granulosa cells in culture. Arch. Biochem. Biophys., 251, 287-298.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 287-298
    • Yanagishita, M.1
  • 51
    • 0025143111 scopus 로고
    • Cloning, sequence and expression of a cDNA encoding hamster UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase
    • Zhu,X.Y. 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.Y.1    Lehrman, M.A.2


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