메뉴 건너뛰기




Volumn 10, Issue 4, 2000, Pages 347-355

N-glycan processing by a lepidopteran insect α1,2-mannosidase

Author keywords

GST; Insect; N glycosylation; Substrate specificity; 1,2 mannosidase

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; ALPHA MANNOSIDASE; CALCIUM; COMPLEMENTARY DNA; GLYCAN; MANNOSE; OLIGOSACCHARIDE;

EID: 0034031180     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/10.4.347     Document Type: Article
Times cited : (30)

References (53)
  • 1
    • 0025313449 scopus 로고
    • Isolation, characterization and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects
    • Ballou, C.E. (1990) Isolation, characterization and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects. Methods Enzymol., 185, 440-470.
    • (1990) Methods Enzymol. , vol.185 , pp. 440-470
    • Ballou, C.E.1
  • 2
    • 0026760542 scopus 로고
    • Effect of substrate structure on the activity of Man9-mannosidase from pig liver involved in N-linked oligosaccharide processing
    • Bause, E., Breuer, W., Schweden, J., Roeser, R. and Geyer, R. (1992) Effect of substrate structure on the activity of Man9-mannosidase from pig liver involved in N-linked oligosaccharide processing. Eur. J. Biochem., 208, 451-457.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 451-457
    • Bause, E.1    Breuer, W.2    Schweden, J.3    Roeser, R.4    Geyer, R.5
  • 3
    • 0028972747 scopus 로고
    • Man9-mannosidase from human kidney is expressed in COS cells as a Golgi-resident type II transmembrane N-glycoprotein
    • Bieberich, E. and Bause, E. (1995) Man9-mannosidase from human kidney is expressed in COS cells as a Golgi-resident type II transmembrane N-glycoprotein. Eur. J. Biochem., 233, 644-649.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 644-649
    • Bieberich, E.1    Bause, E.2
  • 4
    • 0030610470 scopus 로고    scopus 로고
    • Man9-mannosidase from pig liver is a type-II membrane protein that resides in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in COS 1 cells
    • Bieberich, E., Treml, K., Volker, C., Rolfs, A., Kalz-Fuller, B. and Bause, E. (1997) Man9-mannosidase from pig liver is a type-II membrane protein that resides in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in COS 1 cells. Eur. J. Biochem., 246, 681-689.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 681-689
    • Bieberich, E.1    Treml, K.2    Volker, C.3    Rolfs, A.4    Kalz-Fuller, B.5    Bause, E.6
  • 5
    • 0021099732 scopus 로고
    • Evidence for an α-mannosidase in endoplasmic reticulum of rat liver
    • Bischoff, J. and Kornfeld, R. (1983) Evidence for an α-mannosidase in endoplasmic reticulum of rat liver. J. Biol. Chem., 258, 7907-7910.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7907-7910
    • Bischoff, J.1    Kornfeld, R.2
  • 6
    • 0022976402 scopus 로고
    • The use of 1-deoxymannojirimycin to evaluate the role of various α-mannosidases in oligosaccharide processing in intact cells
    • Bischoff, J., Liscum, L. and Kornfeld, R. (1986) The use of 1-deoxymannojirimycin to evaluate the role of various α-mannosidases in oligosaccharide processing in intact cells. J. Biol. Chem., 261, 4766-4774.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4766-4774
    • Bischoff, J.1    Liscum, L.2    Kornfeld, R.3
  • 7
    • 0021321955 scopus 로고
    • A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots
    • Blake, M.S., Johnston, K.H., Russell-Jones, G.J. and Gotschlich, E.C. (1984) A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal. Biochem., 136, 175-179.
    • (1984) Anal. Biochem. , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnston, K.H.2    Russell-Jones, G.J.3    Gotschlich, E.C.4
  • 8
    • 0033005666 scopus 로고    scopus 로고
    • Isolation and purification of a neutral α (1,2)-mannosidase from Trypanosoma cruzi
    • Bonay, P. and Fresno, M. (1999) Isolation and purification of a neutral α (1,2)-mannosidase from Trypanosoma cruzi. Glycobiology, 9, 423-433.
    • (1999) Glycobiology , vol.9 , pp. 423-433
    • Bonay, P.1    Fresno, M.2
  • 9
    • 0020491529 scopus 로고
    • Glycoprotein synthesis in yeast. Identification of Man8GlcNAc2 as an essential intermediate in oligosaccharide processing
    • Byrd, J.C., Tarentino, A.L., Maley, F., Atkinson, P.H. and Trimble, R.B. (1982) Glycoprotein synthesis in yeast. Identification of Man8GlcNAc2 as an essential intermediate in oligosaccharide processing. J. Biol. Chem., 257, 14657-14666.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14657-14666
    • Byrd, J.C.1    Tarentino, A.L.2    Maley, F.3    Atkinson, P.H.4    Trimble, R.B.5
  • 10
    • 0030926537 scopus 로고    scopus 로고
    • Phylogenetic survey of endomannosidase indicates late evolutionary appearance of this N-linked oligosaccharide processing enzyme
    • Dairaku, and Spiro, R.G. (1997) Phylogenetic survey of endomannosidase indicates late evolutionary appearance of this N-linked oligosaccharide processing enzyme. Glycobiology, 7, 579-586.
    • (1997) Glycobiology , vol.7 , pp. 579-586
    • Dairaku, K.1    Spiro, R.G.2
  • 11
    • 0033597781 scopus 로고    scopus 로고
    • Identification, expression and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis
    • Gonzalez, D.S., Karaveg, K., Vandersall-Nairn, A.S., Lal, A. and Moremen, K.W. (1999) Identification, expression and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J. Biol. Chem., 274, 21375-21386.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21375-21386
    • Gonzalez, D.S.1    Karaveg, K.2    Vandersall-Nairn, A.S.3    Lal, A.4    Moremen, K.W.5
  • 12
    • 0014025745 scopus 로고
    • Establishment of a line of mosquito (Aedes aegypti L.) cells grown in vitro
    • Grace, T.D. (1966) Establishment of a line of mosquito (Aedes aegypti L.) cells grown in vitro. Nature, 211, 366-367.
    • (1966) Nature , vol.211 , pp. 366-367
    • Grace, T.D.1
  • 13
    • 0002529316 scopus 로고    scopus 로고
    • Glycosidases of the asparagine-linked oligosaccharide processing pathway
    • Pinto, B.M. (ed.), Elsevier, Amsterdam
    • Herscovics, A. (1999a) Glycosidases of the asparagine-linked oligosaccharide processing pathway. In Pinto, B.M. (ed.), Comprehensive Natural Products Chemistry. Elsevier, Amsterdam, Vol. 3, pp. 13-35.
    • (1999) Comprehensive Natural Products Chemistry , vol.3 , pp. 13-35
    • Herscovics, A.1
  • 14
    • 0032714568 scopus 로고    scopus 로고
    • Importance of glycosidases in mammalian glycoprotein biosynthesis
    • in press
    • Herscovics, A. (1999b) Importance of glycosidases in mammalian glycoprotein biosynthesis. Biochim. Biophys. Acta., in press.
    • (1999) Biochim. Biophys. Acta.
    • Herscovics, A.1
  • 15
    • 0032903636 scopus 로고    scopus 로고
    • Processing glycosidases of Saccharomyces cerevisiae
    • Herscovics, A. (1999c) Processing glycosidases of Saccharomyces cerevisiae. Biochim. Biophys. Acta, 1426, 275-285.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 275-285
    • Herscovics, A.1
  • 16
    • 0028200803 scopus 로고
    • Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family conserved from yeast to mammals
    • Herscovics, A., Schneikert, J., Athanassiadis, A. and Moremen, K.W. (1994) Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family conserved from yeast to mammals. J. Biol. Chem., 269, 9864-9871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9864-9871
    • Herscovics, A.1    Schneikert, J.2    Athanassiadis, A.3    Moremen, K.W.4
  • 17
    • 0031819849 scopus 로고    scopus 로고
    • Preventing proteolytic artifacts in the baculovirus expression system
    • Hom, L.G. and Volkman, L.E. (1998) Preventing proteolytic artifacts in the baculovirus expression system. Biotechniques, 25, 18-20.
    • (1998) Biotechniques , vol.25 , pp. 18-20
    • Hom, L.G.1    Volkman, L.E.2
  • 19
    • 0027962493 scopus 로고
    • Biosynthesis and processing of the Autographa californica nuclear polyhedrosis virus gp64 protein
    • Jarvis, D.L. and Garcia, A., Jr. (1994) Biosynthesis and processing of the Autographa californica nuclear polyhedrosis virus gp64 protein. Virology, 205, 300-313.
    • (1994) Virology , vol.205 , pp. 300-313
    • Jarvis, D.L.1    Garcia A., Jr.2
  • 20
    • 0024574726 scopus 로고
    • Glycosylation and secretion of human tissue plasminogen activator in recombinant baculovirus-infected insect cells
    • Jarvis, D.L. and Summers, M.D. (1989) Glycosylation and secretion of human tissue plasminogen activator in recombinant baculovirus-infected insect cells. Mol. Cell Biol., 9, 214-223.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 214-223
    • Jarvis, D.L.1    Summers, M.D.2
  • 21
    • 0032190659 scopus 로고    scopus 로고
    • Engineering N-glycosylation pathways in the baculovirus-insect cell system
    • Jarvis, D.L., Kawar, Z.S. and Hollister, J.R. (1998) Engineering N-glycosylation pathways in the baculovirus-insect cell system. Curr. Opin. Biotechnol., 9, 528-533.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 528-533
    • Jarvis, D.L.1    Kawar, Z.S.2    Hollister, J.R.3
  • 22
    • 0023754150 scopus 로고
    • Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the α-mannosidase which removes one specific mannose residue from Man9GlcNAc
    • Jelinek-Kelly, S. and Herscovics, A. (1988) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the α-mannosidase which removes one specific mannose residue from Man9GlcNAc. J. Biol. Chem., 263, 14757-14763.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14757-14763
    • Jelinek-Kelly, S.1    Herscovics, A.2
  • 23
    • 0030903568 scopus 로고    scopus 로고
    • Isolation and characterization of an alpha 1,2-mannosidase cDNA from the lepidopteran insect cell line Sf9
    • Kawar, Z., Herscovics, A. and Jarvis, D.L. (1997) Isolation and characterization of an alpha 1,2-mannosidase cDNA from the lepidopteran insect cell line Sf9. Glycobiology, 7, 433-443.
    • (1997) Glycobiology , vol.7 , pp. 433-443
    • Kawar, Z.1    Herscovics, A.2    Jarvis, D.L.3
  • 24
    • 0028907758 scopus 로고
    • Molecular and genetic analysis of the Drosophila mas-1 (mannosidase-1) gene which encodes a glycoprotein processing α 1,2-mannosidase
    • Kerscher, S., Albert, S., Wucherpfennig, D., Heisenberg, M. and Schneuwly, S. (1995) Molecular and genetic analysis of the Drosophila mas-1 (mannosidase-1) gene which encodes a glycoprotein processing α 1,2-mannosidase. Dev. Biol., 168, 613-626.
    • (1995) Dev. Biol. , vol.168 , pp. 613-626
    • Kerscher, S.1    Albert, S.2    Wucherpfennig, D.3    Heisenberg, M.4    Schneuwly, S.5
  • 25
    • 0027273755 scopus 로고
    • A method for producing recombinant baculovirus expression vectors at high frequency
    • Kitts, P.A. and Possee, R.D. (1993) A method for producing recombinant baculovirus expression vectors at high frequency. Biotechniques, 14, 810-817.
    • (1993) Biotechniques , vol.14 , pp. 810-817
    • Kitts, P.A.1    Possee, R.D.2
  • 26
    • 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
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0031712231 scopus 로고    scopus 로고
    • Substrate specificities of recombinant murine golgi α1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and golgi processing α1,2-mannosidases
    • Lal, A., Pang, P., Kalelkar, S., Romero, P.A., Herscovics, A. and Moremen, K.W. (1998) Substrate specificities of recombinant murine golgi α1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and golgi processing α1,2-mannosidases. Glycobiology, 8, 981-995.
    • (1998) Glycobiology , vol.8 , pp. 981-995
    • Lal, A.1    Pang, P.2    Kalelkar, S.3    Romero, P.A.4    Herscovics, A.5    Moremen, K.W.6
  • 29
    • 0028342606 scopus 로고
    • Isolation and expression of murine and rabbit cDNAs encoding an α1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides
    • Lal, A., Schutzbach, J.S., Forsee, W.T., Neame, P.J. and Moremen, K.W. (1994) Isolation and expression of murine and rabbit cDNAs encoding an α1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides. J. Biol. Chem., 269, 9872-9881.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9872-9881
    • Lal, A.1    Schutzbach, J.S.2    Forsee, W.T.3    Neame, P.J.4    Moremen, K.W.5
  • 30
    • 0027945345 scopus 로고
    • Production, purification and characterization of recombinant yeast processing α1,2-mannosidase
    • Lipari, F. and Herscovics, A. (1994) Production, purification and characterization of recombinant yeast processing α1,2-mannosidase. Glycobiology, 4, 697-702.
    • (1994) Glycobiology , vol.4 , pp. 697-702
    • Lipari, F.1    Herscovics, A.2
  • 31
    • 0023654288 scopus 로고
    • Golgi endo-α-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme
    • Lubas, W.A. and Spiro, R.G. (1987) Golgi endo-α-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme. J. Biol. Chem., 262, 3775-3781.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3775-3781
    • Lubas, W.A.1    Spiro, R.G.2
  • 32
    • 0032959442 scopus 로고    scopus 로고
    • The KTR and MNN1 mannosyltransferase families of Saccharomyces cerevisiae
    • Lussier, M., Sdicu, A.M. and Bussey, H. (1999) The KTR and MNN1 mannosyltransferase families of Saccharomyces cerevisiae. Biochim. Biophys. Acta, 1426, 323-334.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 323-334
    • Lussier, M.1    Sdicu, A.M.2    Bussey, H.3
  • 33
    • 77956850407 scopus 로고
    • Protein glycosylation in insects
    • Montreuil, J., Vliegenthart, J.F.G. and Schachter, H. (eds.), Elsevier, Amsterdam
    • Marz, L., Altmann, F., Staudacher, E. and Kubelka, V. (1995) Protein glycosylation in insects. In Montreuil, J., Vliegenthart, J.F.G. and Schachter, H. (eds.), Glycoproteins. Elsevier, Amsterdam, Vol. 29a, pp. 543-563.
    • (1995) Glycoproteins , vol.29 A , pp. 543-563
    • Marz, L.1    Altmann, F.2    Staudacher, E.3    Kubelka, V.4
  • 34
    • 0028213490 scopus 로고
    • Glycosidases of the asparagine-linked oligosaccharide processing pathway
    • Moremen, K.W., Trimble, R.G. and Herscovics, A. (1994) Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology, 4, 113-125.
    • (1994) Glycobiology , vol.4 , pp. 113-125
    • Moremen, K.W.1    Trimble, R.G.2    Herscovics, A.3
  • 35
    • 0024263783 scopus 로고
    • Scaleup of insect cell cultures: Protective effects of pluronic F-68
    • Murhammer, D.W. and Goochee, C.F. (1988) Scaleup of insect cell cultures: protective effects of pluronic F-68. Bio/Technology, 6, 1411-1418.
    • (1988) Bio/Technology , vol.6 , pp. 1411-1418
    • Murhammer, D.W.1    Goochee, C.F.2
  • 36
    • 0024258424 scopus 로고
    • Investigation of the role of glycans for the biological activity of Semliki Forest virus grown in Aedes albopictus cells using inhibitors of asparagine-linked oligosaccharides trimming
    • Naim, H.Y. and Koblet, H. (1988) Investigation of the role of glycans for the biological activity of Semliki Forest virus grown in Aedes albopictus cells using inhibitors of asparagine-linked oligosaccharides trimming. Arch. Virol., 102, 73-89.
    • (1988) Arch. Virol. , vol.102 , pp. 73-89
    • Naim, H.Y.1    Koblet, H.2
  • 38
    • 0028917793 scopus 로고
    • Purification and properties of a Golgi-derived (α 1,2)-mannosidase-I from baculovirus-infected lepidopteran insect cells (IPLB-SF21 AE) with preferential activity toward mannose6-N-acetylglucosamine2
    • Ren, J., Bretthauer, R.K. and Castellino, F.J. (1995) Purification and properties of a Golgi-derived (α 1,2)-mannosidase-I from baculovirus-infected lepidopteran insect cells (IPLB-SF21 AE) with preferential activity toward mannose6-N-acetylglucosamine2. Biochemistry, 34, 2489-2495.
    • (1995) Biochemistry , vol.34 , pp. 2489-2495
    • Ren, J.1    Bretthauer, R.K.2    Castellino, F.J.3
  • 39
    • 0023940624 scopus 로고
    • Post-translational protein modification in the endoplasmic reticulum. Demonstration of fatty acylase and deoxymannojirimycin-sensitive α-mannosidase activities
    • Rizzolo, L.J. and Kornfeld, R. (1988) Post-translational protein modification in the endoplasmic reticulum. Demonstration of fatty acylase and deoxymannojirimycin-sensitive α-mannosidase activities. J. Biol. Chem., 263, 9520-9525.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9520-9525
    • Rizzolo, L.J.1    Kornfeld, R.2
  • 40
    • 0032522793 scopus 로고    scopus 로고
    • Mutant analysis reveals an alternative pathway for N-linked glycosylation in Drosophila melanogaster
    • Roberts, D.B., Mulvany, W.J., Dwek, R.A. and Rudd, P.M. (1998) Mutant analysis reveals an alternative pathway for N-linked glycosylation in Drosophila melanogaster. Eur. J. Biochem., 253, 494-498.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 494-498
    • Roberts, D.B.1    Mulvany, W.J.2    Dwek, R.A.3    Rudd, P.M.4
  • 41
    • 0024961697 scopus 로고
    • Glycoprotein biosynthesis in Saccharomyces cerevisiae. Characterization of α-1,6-mannosyltransferase which initiates outer chain formation
    • Romero, P.A. and Herscovics, A. (1989) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Characterization of α-1,6-mannosyltransferase which initiates outer chain formation. J. Biol. Chem., 264, 1946-1950.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1946-1950
    • Romero, P.A.1    Herscovics, A.2
  • 42
    • 0021981555 scopus 로고
    • Comparison between I-deoxynojirimycin and N-methyl-1-deoxynojirimycin as inhibitors of oligosaccharide processing in intestinal epithelial cells
    • Romero, P.A., Saunier, B. and Herscovics, A. (1985) Comparison between I-deoxynojirimycin and N-methyl-1-deoxynojirimycin as inhibitors of oligosaccharide processing in intestinal epithelial cells. Biochem. J., 226, 733-740.
    • (1985) Biochem. J. , vol.226 , pp. 733-740
    • Romero, P.A.1    Saunier, B.2    Herscovics, A.3
  • 43
    • 0030703140 scopus 로고    scopus 로고
    • Molecular cloning and expression of rat liver endo-α-mannosidase, an N-linked oligosaccharide processing enzyme
    • Spiro, M.J., Bhoyroo, V.D. and Spiro, R.G. (1997) Molecular cloning and expression of rat liver endo-α-mannosidase, an N-linked oligosaccharide processing enzyme. J. Biol. Chem., 272, 29356-29363.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29356-29363
    • Spiro, M.J.1    Bhoyroo, V.D.2    Spiro, R.G.3
  • 44
    • 0001962451 scopus 로고
    • A manual of methods for baculovirus vectors and insect cell culture procedures
    • Summers, M.D. and Smith, G.E. (1987). A manual of methods for baculovirus vectors and insect cell culture procedures. Texas Agric. Exp. Station Bull., 1555.
    • (1987) Texas Agric. Exp. Station Bull. , pp. 1555
    • Summers, M.D.1    Smith, G.E.2
  • 45
    • 0018801562 scopus 로고
    • Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharides
    • Tabas, I. and Kornfeld, S. (1979) Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharides. J. Biol. Chem., 254, 11655-11663.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11655-11663
    • Tabas, I.1    Kornfeld, S.2
  • 46
    • 0023222622 scopus 로고
    • Protein glycosylation in yeast
    • Tanner, W. and Lehle, L. (1987) Protein glycosylation in yeast. Biochim. Biophys. Acta., 906, 81-99.
    • (1987) Biochim. Biophys. Acta. , vol.906 , pp. 81-99
    • Tanner, W.1    Lehle, L.2
  • 47
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA, 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 48
    • 0031840130 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human α1,2-mannosidase gene involved in N-glycan maturation
    • Tremblay, L.O., Campbell Dyke, N. and Herscovics, A. (1998) Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human α1,2-mannosidase gene involved in N-glycan maturation. Glycobiology, 8, 585-595.
    • (1998) Glycobiology , vol.8 , pp. 585-595
    • Tremblay, L.O.1    Campbell Dyke, N.2    Herscovics, A.3
  • 49
    • 0032860902 scopus 로고    scopus 로고
    • Cloning and expression of a specific human α1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis
    • Tremblay, L.O. and Herscovics, A. (1999) Cloning and expression of a specific human α1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology, 10, 1073-1078.
    • (1999) Glycobiology , vol.10 , pp. 1073-1078
    • Tremblay, L.O.1    Herscovics, A.2
  • 50
    • 0017475358 scopus 로고
    • The establishment of two insect cell lines from the insect Spodoptera frugiperda (Lepidoptera:Noctuidae)
    • Vaughn, J.L., Goodwin, R.H., Thompkins, G.J. and McCawley, P. (1977) The establishment of two insect cell lines from the insect Spodoptera frugiperda (Lepidoptera:Noctuidae). In Vitro, 13, 213-217.
    • (1977) In Vitro , vol.13 , pp. 213-217
    • Vaughn, J.L.1    Goodwin, R.H.2    Thompkins, G.J.3    McCawley, P.4
  • 51
    • 0027331577 scopus 로고
    • Demonstration that a kifunensine-resistant alpha-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells
    • Weng, S. and Spiro, R.G. (1993) Demonstration that a kifunensine-resistant alpha-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells. J. Biol. Chem., 268, 25656-25663.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25656-25663
    • Weng, S.1    Spiro, R.G.2
  • 52
    • 0030029938 scopus 로고    scopus 로고
    • Endoplasmic reticulum kifunensine-resistant α-mannosidase is enzymatically and immunologically related to the cytosolic α-mannosidase
    • Weng, S. and Spiro, R.G. (1996) Endoplasmic reticulum kifunensine-resistant α-mannosidase is enzymatically and immunologically related to the cytosolic α-mannosidase. Arch. Biochem. Biophys., 325, 113-123.
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 113-123
    • Weng, S.1    Spiro, R.G.2
  • 53
    • 0031989252 scopus 로고    scopus 로고
    • Overproduction of 1,2-α-mannosidase, a glycochain processing enzyme, by Aspergillus oryzae
    • Yoshida, T., Nakajima, T. and Ichishima, E. (1998) Overproduction of 1,2-α-mannosidase, a glycochain processing enzyme, by Aspergillus oryzae. Biosci. Biotechnol. Biochem., 62, 309-315.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 309-315
    • Yoshida, T.1    Nakajima, T.2    Ichishima, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.