메뉴 건너뛰기




Volumn 25, Issue 4, 2015, Pages 448-464

Enzymatic properties and subtle differences in the substrate specificity of phylogenetically distinct invertebrate N-glycan processing hexosaminidases

Author keywords

fused lobes; hexosaminidase; insect; invertebrate; N glycans

Indexed keywords

BETA N ACETYLHEXOSAMINIDASE; GLYCAN; GLYCOCONJUGATE; GLYCOSYLTRANSFERASE; N ACETYLGALACTOSAMINE; N ACETYLGLUCOSAMINE; RECOMBINANT ENZYME; CAENORHABDITIS ELEGANS PROTEIN; DROSOPHILA PROTEIN; GLYCOPEPTIDE; POLYSACCHARIDE;

EID: 84941088376     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwu132     Document Type: Article
Times cited : (27)

References (59)
  • 1
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane-bound-N-acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altmann F, Schwihla H, Staudacher E, Glössl J, März L. 1995. Insect cells contain an unusual, membrane-bound-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J Biol Chem. 270:17344-17349.
    • (1995) J Biol Chem. , vol.270 , pp. 17344-17349
    • Altmann, F.1    Schwihla, H.2    Staudacher, E.3    Glössl, J.4    März, L.5
  • 2
    • 0028926641 scopus 로고
    • Kinetic comparison of peptide: N-glycosidases F and A reveals several differences in substrate specificity
    • Altmann F, Schweiszer S, Weber C. 1995. Kinetic comparison of peptide: N-glycosidases F and A reveals several differences in substrate specificity. Glycoconj J. 12:84-93.
    • (1995) Glycoconj J. , vol.12 , pp. 84-93
    • Altmann, F.1    Schweiszer, S.2    Weber, C.3
  • 3
    • 34247849493 scopus 로고    scopus 로고
    • Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo
    • Aoki K, Perlman M, Lim JM, Cantu R, Wells L, Tiemeyer M. 2007. Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo. J Biol Chem. 282:9127-9142.
    • (2007) J Biol Chem. , vol.282 , pp. 9127-9142
    • Aoki, K.1    Perlman, M.2    Lim, J.M.3    Cantu, R.4    Wells, L.5    Tiemeyer, M.6
  • 4
    • 0038243176 scopus 로고    scopus 로고
    • A transgenic insect cell line engineered to produce CMP-sialic acid and sialylated glycoproteins
    • Aumiller JJ, Hollister JR, Jarvis DL. 2003. A transgenic insect cell line engineered to produce CMP-sialic acid and sialylated glycoproteins. Glycobiology. 13:497-507.
    • (2003) Glycobiology. , vol.13 , pp. 497-507
    • Aumiller, J.J.1    Hollister, J.R.2    Jarvis, D.L.3
  • 5
    • 84856298339 scopus 로고    scopus 로고
    • A new glycoengineered insect cell line with an inducibly mammalianized protein N-glycosylation pathway
    • Aumiller JJ, Mabashi-Asazuma H, Hillar A, Shi X, Jarvis DL. 2012. A new glycoengineered insect cell line with an inducibly mammalianized protein N-glycosylation pathway. Glycobiology. 22:417-428.
    • (2012) Glycobiology. , vol.22 , pp. 417-428
    • Aumiller, J.J.1    Mabashi-Asazuma, H.2    Hillar, A.3    Shi, X.4    Jarvis, D.L.5
  • 6
    • 0023664264 scopus 로고
    • Control of glycoprotein synthesis. Kinetic mechanism, substrate specificity, and inhibition characteristics of UDP-N-acetylglucosamine:-D-mannoside 1-2 N-acetylglucosaminyltransferase II from rat liver
    • Bendiak B, Schachter H. 1987. Control of glycoprotein synthesis. Kinetic mechanism, substrate specificity, and inhibition characteristics of UDP-N-acetylglucosamine:-D-mannoside 1-2 N-acetylglucosaminyltransferase II from rat liver. J Biol Chem. 262:5784-5790.
    • (1987) J Biol Chem. , vol.262 , pp. 5784-5790
    • Bendiak, B.1    Schachter, H.2
  • 7
    • 84856690548 scopus 로고    scopus 로고
    • MultiBac: Expanding the research toolbox for multiprotein complexes
    • Bieniossek C, Imasaki T, Takagi Y, Berger I. 2012. MultiBac: Expanding the research toolbox for multiprotein complexes. Trends Biochem Sci. 37: 49-57.
    • (2012) Trends Biochem Sci. , vol.37 , pp. 49-57
    • Bieniossek, C.1    Imasaki, T.2    Takagi, Y.3    Berger, I.4
  • 8
    • 0033980373 scopus 로고    scopus 로고
    • Central brain postembryonic development in Drosophila: Implication of genes expressed at the interhemispheric junction
    • Boquet I, Hitier R, Dumas M, Chaminade M, Preat T. 2000. Central brain postembryonic development in Drosophila: Implication of genes expressed at the interhemispheric junction. J Neurobiol. 42:33-48.
    • (2000) J Neurobiol. , vol.42 , pp. 33-48
    • Boquet, I.1    Hitier, R.2    Dumas, M.3    Chaminade, M.4    Preat, T.5
  • 9
    • 84857455818 scopus 로고    scopus 로고
    • Recombinant protein vaccines produced in insect cells
    • Cox MM. 2012. Recombinant protein vaccines produced in insect cells. Vaccine. 30:1759-1766.
    • (2012) Vaccine. , vol.30 , pp. 1759-1766
    • Cox, M.M.1
  • 12
    • 0035958916 scopus 로고    scopus 로고
    • Identification of core ? 1, 3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural antihorseadish peroxidase epitope
    • Fabini G, Freilinger A, Altmann F, Wilson IBH. 2001. Identification of core ? 1, 3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural antihorseadish peroxidase epitope. J Biol Chem. 276:28058-28067.
    • (2001) J Biol Chem. , vol.276 , pp. 28058-28067
    • Fabini, G.1    Freilinger, A.2    Altmann, F.3    Wilson, I.B.H.4
  • 14
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: Cloning and characterization of a neutral, cytosolic-N-acetylglucosaminidase from human brain
    • Gao Y, Wells L, Comer FI, Parker GJ, Hart GW. 2001. Dynamic O-glycosylation of nuclear and cytosolic proteins: Cloning and characterization of a neutral, cytosolic-N-acetylglucosaminidase from human brain. J Biol Chem. 276:9838-9845.
    • (2001) J Biol Chem. , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 15
    • 78049451375 scopus 로고    scopus 로고
    • Engineering of biotinprototrophy in Pichia pastoris for robust production processes
    • Gasser B, Dragosits M, Mattanovich D. 2010. Engineering of biotinprototrophy in Pichia pastoris for robust production processes. Metab Eng. 12:573-580.
    • (2010) Metab Eng. , vol.12 , pp. 573-580
    • Gasser, B.1    Dragosits, M.2    Mattanovich, D.3
  • 16
    • 45549087961 scopus 로고    scopus 로고
    • A fused lobes gene encodes the processing-N-acetylglucosaminidase in Sf9 cells
    • Geisler C, Aumiller JJ, Jarvis DL. 2008. A fused lobes gene encodes the processing-N-acetylglucosaminidase in Sf9 cells. J Biol Chem. 283: 11330-11339.
    • (2008) J Biol Chem. , vol.283 , pp. 11330-11339
    • Geisler, C.1    Aumiller, J.J.2    Jarvis, D.L.3
  • 17
    • 76849096485 scopus 로고    scopus 로고
    • Identification of genes encoding N-glycan processing-N-acetylglucosaminidases in Trichoplusia ni and Bombyx mori: Implications for glycoengineering of baculovirus expression systems
    • Geisler C, Jarvis DL. 2010. Identification of genes encoding N-glycan processing-N-acetylglucosaminidases in Trichoplusia ni and Bombyx mori: Implications for glycoengineering of baculovirus expression systems. Biotechnol Prog. 26:34-44.
    • (2010) Biotechnol Prog. , vol.26 , pp. 34-44
    • Geisler, C.1    Jarvis, D.L.2
  • 18
    • 84857711440 scopus 로고    scopus 로고
    • Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway
    • Geisler C, Jarvis DL. 2012. Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway. J Biol Chem. 287:7084-7097.
    • (2012) J Biol Chem. , vol.287 , pp. 7084-7097
    • Geisler, C.1    Jarvis, D.L.2
  • 21
    • 0038514006 scopus 로고    scopus 로고
    • Hallmarks of Caenorhabditis elegans N-glycosylation: Complexity and controversy
    • Haslam SM, 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
  • 23
    • 0442309687 scopus 로고    scopus 로고
    • Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris
    • Hohenblum H, Gasser B, Maurer M, Borth N, Mattanovich D. 2004. Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris. Biotechnol Bioeng. 85:367-375.
    • (2004) Biotechnol Bioeng. , vol.85 , pp. 367-375
    • Hohenblum, H.1    Gasser, B.2    Maurer, M.3    Borth, N.4    Mattanovich, D.5
  • 24
    • 2242455924 scopus 로고    scopus 로고
    • Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans
    • Hollister J, Grabenhorst E, Nimtz M, Conradt H, Jarvis DL. 2002. Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans. Biochemistry. 41:15093-15104.
    • (2002) Biochemistry. , vol.41 , pp. 15093-15104
    • Hollister, J.1    Grabenhorst, E.2    Nimtz, M.3    Conradt, H.4    Jarvis, D.L.5
  • 25
    • 84883152992 scopus 로고    scopus 로고
    • Biochemical characterization of a novel-N-acetylhexosaminidase from the insect Ostrinia furnacalis
    • Huo Y, Chen L, QuM, Chen Q, YangQ. 2013. Biochemical characterization of a novel-N-acetylhexosaminidase from the insect Ostrinia furnacalis. Arch Insect Biochem Physiol. 83:115-126.
    • (2013) Arch Insect Biochem Physiol. , vol.83 , pp. 115-126
    • Huo, Y.1    Chen, L.2    Qu, M.3    Chen, Q.4    Yang, Q.5
  • 26
    • 48749102098 scopus 로고    scopus 로고
    • Phylogenetic analyses suggest multiple changes of substrate specificity within the glycosyl hydrolase 20 family
    • Intra J, Pavesi G, Horner DS. 2008. Phylogenetic analyses suggest multiple changes of substrate specificity within the glycosyl hydrolase 20 family. BMC Evol Biol. 8:214.
    • (2008) BMC Evol Biol. , vol.8 , pp. 214
    • Intra, J.1    Pavesi, G.2    Horner, D.S.3
  • 27
    • 58949100354 scopus 로고    scopus 로고
    • Suppression of-N-acetylglucosaminidase in the N-glycosylation pathway for complex glycoprotein formation in Drosophila S2 cells
    • Kim YK, Kim KR, Kang DG, Jang SY, Kim YH, Cha HJ. 2009. Suppression of-N-acetylglucosaminidase in the N-glycosylation pathway for complex glycoprotein formation in Drosophila S2 cells. Glycobiology. 19:301-308.
    • (2009) Glycobiology. , vol.19 , pp. 301-308
    • Kim, Y.K.1    Kim, K.R.2    Kang, D.G.3    Jang, S.Y.4    Kim, Y.H.5    Cha, H.J.6
  • 28
    • 36248936100 scopus 로고    scopus 로고
    • Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster
    • Koles K, Lim JM, Aoki K, Porterfield M, Tiemeyer M, Wells L, Panin V. 2007. Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster. Glycobiology. 17:1388-1403.
    • (2007) Glycobiology. , vol.17 , pp. 1388-1403
    • Koles, K.1    Lim, J.M.2    Aoki, K.3    Porterfield, M.4    Tiemeyer, M.5    Wells, L.6    Panin, V.7
  • 30
    • 84865289490 scopus 로고    scopus 로고
    • A carboxyterminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates
    • Krammer F, Margine I, Tan GS, Pica N, Krause JC, Palese P. 2012. A carboxyterminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates. PLoS One. 7:e43603.
    • (2012) PLoS One. , vol.7 , pp. e43603
    • Krammer, F.1    Margine, I.2    Tan, G.S.3    Pica, N.4    Krause, J.C.5    Palese, P.6
  • 31
    • 33646178162 scopus 로고    scopus 로고
    • The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing
    • Léonard R, Rendic D, Rabouille C, Wilson IBH, Preat T, Altmann F. 2006. The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing. J Biol Chem. 281:4867-4875.
    • (2006) J Biol Chem. , vol.281 , pp. 4867-4875
    • Léonard, R.1    Rendic, D.2    Rabouille, C.3    Wilson, I.B.H.4    Preat, T.5    Altmann, F.6
  • 32
    • 0014940534 scopus 로고
    • Studies on the glycosidases of jack beanmeal. 3. Crystallization and properties of-N-acetylhexosaminidase
    • Li SC, LiYT. 1970. Studies on the glycosidases of jack beanmeal. 3. Crystallization and properties of-N-acetylhexosaminidase. J Biol Chem. 245:5153-5160.
    • (1970) J Biol Chem. , vol.245 , pp. 5153-5160
    • Li, S.C.1    LiY, T.2
  • 33
    • 79953221436 scopus 로고    scopus 로고
    • N-Acetylhexosaminidases HEXO1 and HEXO3 are responsible for the formation of paucimannosidic N-glycans in Arabidopsis thaliana
    • Liebminger E, Veit C, Pabst M, Batoux M, Zipfel C, Altmann F, Mach L, Strasser R. 2011.-N-Acetylhexosaminidases HEXO1 and HEXO3 are responsible for the formation of paucimannosidic N-glycans in Arabidopsis thaliana. J Biol Chem. 286:10793-10802.
    • (2011) J Biol Chem. , vol.286 , pp. 10793-10802
    • Liebminger, E.1    Veit, C.2    Pabst, M.3    Batoux, M.4    Zipfel, C.5    Altmann, F.6    Mach, L.7    Strasser, R.8
  • 34
    • 79953006384 scopus 로고    scopus 로고
    • Structural determinants of an insect-N-Acetyl-D-hexosaminidase specialized as a chitinolytic enzyme
    • Liu T, Zhang H, Liu F, Wu Q, Shen X, Yang Q. 2011. Structural determinants of an insect-N-Acetyl-D-hexosaminidase specialized as a chitinolytic enzyme. J Biol Chem. 286:4049-4058.
    • (2011) J Biol Chem. , vol.286 , pp. 4049-4058
    • Liu, T.1    Zhang, H.2    Liu, F.3    Wu, Q.4    Shen, X.5    Yang, Q.6
  • 35
    • 84871658643 scopus 로고    scopus 로고
    • Structural insights into cellulolytic and chitinolytic enzymes revealing crucial residues of insect-N-acetyl-D-hexosaminidase
    • Liu T, Zhou Y, Chen L, ChenW, Liu L, Shen X, ZhangW, Zhang J, Yang Q. 2012. Structural insights into cellulolytic and chitinolytic enzymes revealing crucial residues of insect-N-acetyl-D-hexosaminidase. PLoS One. 7:e52225.
    • (2012) PLoS One. , vol.7 , pp. e52225
    • Liu, T.1    Zhou, Y.2    Chen, L.3    Chen, W.4    Liu, L.5    Shen, X.6    Zhang, W.7    Zhang, J.8    Yang, Q.9
  • 36
    • 4344685875 scopus 로고    scopus 로고
    • The Drosophila melanogaster homologue of the human histo-blood group Pk gene encodes a glycolipidmodifying 1, 4-N-acetylgalactosaminyltransferase
    • Mucha J, Domlatil J, Lochnit G, Rendic D, Paschinger K, Hinterkörner G, Hofinger A, Kosma P, Wilson IBH. 2004. The Drosophila melanogaster homologue of the human histo-blood group Pk gene encodes a glycolipidmodifying 1, 4-N-acetylgalactosaminyltransferase. Biochem J. 382:67-74.
    • (2004) Biochem J. , vol.382 , pp. 67-74
    • Mucha, J.1    Domlatil, J.2    Lochnit, G.3    Rendic, D.4    Paschinger, K.5    Hinterkörner, G.6    Hofinger, A.7    Kosma, P.8    Wilson, I.B.H.9
  • 40
    • 84859237513 scopus 로고    scopus 로고
    • SweetBac: A new approach for the production of mammalianised glycoproteins in insect cells
    • Palmberger D, Wilson IBH, Berger I, Grabherr R, Rendic D. 2012. SweetBac: A new approach for the production of mammalianised glycoproteins in insect cells. PLoS One. 7:e34226.
    • (2012) PLoS One. , vol.7 , pp. e34226
    • Palmberger, D.1    Wilson, I.B.H.2    Berger, I.3    Grabherr, R.4    Rendic, D.5
  • 43
    • 24044466162 scopus 로고    scopus 로고
    • Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates
    • Paschinger K, Staudacher E, Stemmer U, Fabini G, Wilson IBH. 2005. Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates. Glycobiology. 15:463-474.
    • (2005) Glycobiology. , vol.15 , pp. 463-474
    • Paschinger, K.1    Staudacher, E.2    Stemmer, U.3    Fabini, G.4    Wilson, I.B.H.5
  • 45
    • 33645641542 scopus 로고    scopus 로고
    • Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells
    • Rendic D, Linder A, Paschinger K, Borth N, Wilson IBH, Fabini G. 2006. Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells. J Biol Chem. 281:3343-3353.
    • (2006) J Biol Chem. , vol.281 , pp. 3343-3353
    • Rendic, D.1    Linder, A.2    Paschinger, K.3    Borth, N.4    Wilson, I.B.H.5    Fabini, G.6
  • 46
    • 37149040344 scopus 로고    scopus 로고
    • Adaptation of the "in-gel release method" to N-glycome analysis of lowmilligram amounts of material
    • Rendic D, Wilson IBH, Lubec G, Gutternigg M, Altmann F, Leonard R. 2007. Adaptation of the "in-gel release method" to N-glycome analysis of lowmilligram amounts of material. Electrophoresis. 28:4484-4492.
    • (2007) Electrophoresis. , vol.28 , pp. 4484-4492
    • Rendic, D.1    Wilson, I.B.H.2    Lubec, G.3    Gutternigg, M.4    Altmann, F.5    Leonard, R.6
  • 48
    • 84901610078 scopus 로고    scopus 로고
    • Mutations in four glycosyl hydrolases reveal a highly coordinated pathway for rhodopsin biosynthesis and N-glycan trimming in Drosophila melanogaster
    • Rosenbaum EE, Vasiljevic E, Brehm KS, Colley NJ. 2014. Mutations in four glycosyl hydrolases reveal a highly coordinated pathway for rhodopsin biosynthesis and N-glycan trimming in Drosophila melanogaster. PLoS Genet. 10: e1004349.
    • (2014) PLoS Genet. , vol.10 , pp. e1004349
    • Rosenbaum, E.E.1    Vasiljevic, E.2    Brehm, K.S.3    Colley, N.J.4
  • 49
    • 0023664882 scopus 로고
    • Purification and properties of the glycoprotein processing N-acetylglucosaminyltransferase II from plants
    • Szumilo T, Kaushal GP, Elbein AD. 1987. Purification and properties of the glycoprotein processing N-acetylglucosaminyltransferase II from plants. Biochemistry. 26:5498-5505.
    • (1987) Biochemistry. , vol.26 , pp. 5498-5505
    • Szumilo, T.1    Kaushal, G.P.2    Elbein, A.D.3
  • 50
    • 0026100208 scopus 로고
    • Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide
    • Tessier DC, Thomas DY, Khouri HE, Laliberte F, Vernet T. 1991. Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide. Gene. 98:177-183.
    • (1991) Gene. , vol.98 , pp. 177-183
    • Tessier, D.C.1    Thomas, D.Y.2    Khouri, H.E.3    Laliberte, F.4    Vernet, T.5
  • 51
    • 73649148725 scopus 로고    scopus 로고
    • Molecular basis for galactosylation of core fucose residues in invertebrates: Identification of Caenorhabditis elegans N-glycan core 1, 6-fucoside 1, 4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family
    • Titz A, Butschi A, Henrissat B, Fan YY, Hennet T, Razzazi-Fazeli E, Hengartner MO, Wilson IBH, Künzler M, Aebi M. 2009. Molecular basis for galactosylation of core fucose residues in invertebrates: Identification of Caenorhabditis elegans N-glycan core 1, 6-fucoside 1, 4-galactosyltransferase GALT-1 as a member of a novel glycosyltransferase family. J Biol Chem. 284:36223-36233.
    • (2009) J Biol Chem. , vol.284 , pp. 36223-36233
    • Titz, A.1    Butschi, A.2    Henrissat, B.3    Fan, Y.Y.4    Hennet, T.5    Razzazi-Fazeli, E.6    Hengartner, M.O.7    Wilson, I.B.H.8    Künzler, M.9    Aebi, M.10
  • 52
    • 0042474189 scopus 로고    scopus 로고
    • Humanization of lepidopteran insect-cell-produced glycoproteins
    • Tomiya N, Betenbaugh MJ, Lee YC. 2003. Humanization of lepidopteran insect-cell-produced glycoproteins. Acc Chem Res. 36:613-620.
    • (2003) Acc Chem Res. , vol.36 , pp. 613-620
    • Tomiya, N.1    Betenbaugh, M.J.2    Lee, Y.C.3
  • 53
    • 33745865149 scopus 로고    scopus 로고
    • Purification, characterization, and cloning of a Spodoptera frugiperda Sf9-N-acetylhexosaminidase that hydrolyzes terminal N-acetylglucosamine on the N-glycan core
    • Tomiya N, Narang S, Park J, Abdul-Rahman B, Choi O, Singh S, Hiratake J, Sakata K, Betenbaugh MJ, Palter KB, et al. 2006. Purification, characterization, and cloning of a Spodoptera frugiperda Sf9-N-acetylhexosaminidase that hydrolyzes terminal N-acetylglucosamine on the N-glycan core. J Biol Chem. 281:19545-19560.
    • (2006) J Biol Chem. , vol.281 , pp. 19545-19560
    • Tomiya, N.1    Narang, S.2    Park, J.3    Abdul-Rahman, B.4    Choi, O.5    Singh, S.6    Hiratake, J.7    Sakata, K.8    Betenbaugh, M.J.9    Palter, K.B.10
  • 54
    • 0021274996 scopus 로고
    • Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: Attachment in the Golgi apparatus and removal in protein bodies
    • Vitale A, Chrispeels MJ. 1984. Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: Attachment in the Golgi apparatus and removal in protein bodies. J Cell Biol. 99:133-140.
    • (1984) J Cell Biol. , vol.99 , pp. 133-140
    • Vitale, A.1    Chrispeels, M.J.2
  • 55
    • 0029950110 scopus 로고    scopus 로고
    • N-acetyl-glucosaminidase accounts for differences in glycosylation of influenza virus hemagglutinin expressed in insect cells from a baculovirus vector
    • Wagner R, Geyer H, Geyer R, Klenk HD. 1996. N-acetyl-glucosaminidase accounts for differences in glycosylation of influenza virus hemagglutinin expressed in insect cells from a baculovirus vector. J Virol. 70:4103-4109.
    • (1996) J Virol. , vol.70 , pp. 4103-4109
    • Wagner, R.1    Geyer, H.2    Geyer, R.3    Klenk, H.D.4
  • 56
    • 0037085295 scopus 로고    scopus 로고
    • Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under-N-acetylglucosaminidase inhibition
    • Watanabe S, Kokuho T, Takahashi H, Takahashi M, Kubota T, Inumaru S. 2002. Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under-N-acetylglucosaminidase inhibition. J Biol Chem. 277: 5090-5093
    • (2002) J Biol Chem. , vol.277 , pp. 5090-5093
    • Watanabe, S.1    Kokuho, T.2    Takahashi, H.3    Takahashi, M.4    Kubota, T.5    Inumaru, S.6
  • 57
    • 0037127198 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: Further characterization of the nucleocytoplasmic-N-acetylglucosaminidase, O-GlcNAcase
    • Wells L, Gao Y, Mahoney JA, Vosseller K, Chen C, Rosen A, Hart GW. 2002. Dynamic O-glycosylation of nuclear and cytosolic proteins: Further characterization of the nucleocytoplasmic-N-acetylglucosaminidase, O-GlcNAcase. J Biol Chem. 277:1755-1761.
    • (2002) J Biol Chem. , vol.277 , pp. 1755-1761
    • Wells, L.1    Gao, Y.2    Mahoney, J.A.3    Vosseller, K.4    Chen, C.5    Rosen, A.6    Hart, G.W.7
  • 59
    • 84865266275 scopus 로고    scopus 로고
    • Galactosylated fucose epitopes in nematodes: Increased expression in a Caenorhabditis mutant associated with altered lectin sensitivity and occurrence in parasitic species
    • Yan S, Bleuler-Martinez S, Plaza DF, Künzler M, Aebi M, Joachim A, Razzazi-Fazeli E, Jantsch V, Geyer R, Wilson IBH, et al. 2012. Galactosylated fucose epitopes in nematodes: Increased expression in a Caenorhabditis mutant associated with altered lectin sensitivity and occurrence in parasitic species. J Biol Chem. 287:28276-28290.
    • (2012) J Biol Chem. , vol.287 , pp. 28276-28290
    • Yan, S.1    Bleuler-Martinez, S.2    Plaza, D.F.3    Künzler, M.4    Aebi, M.5    Joachim, A.6    Razzazi-Fazeli, E.7    Jantsch, V.8    Geyer, R.9    Wilson, I.B.H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.