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Volumn 22, Issue 4, 2012, Pages 561-571

Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) involved in chondroitin sulfate initiation: Impact of sulfation on activity and specificity

Author keywords

chondroitin sulfate; glycosaminoglycan synthesis; glycosyltransferase; linkage region; sulfation

Indexed keywords

CHONDROITIN SULFATE; CHONDROITIN SULFATE N ACETYLGALACTOSAMINYLTRANSFERASE 1; DISACCHARIDE; GALACTOSE; N ACETYLGALACTOSAMINE; N ACETYLGALACTOSAMINYLTRANSFERASE; OLIGOSACCHARIDE; RECOMBINANT ENZYME; SULFATE; TRISACCHARIDE; UNCLASSIFIED DRUG;

EID: 84857936904     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr172     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 0035930615 scopus 로고    scopus 로고
    • Biosynthesis of the linkage region of glycosaminoglycans: Cloning and activity of galactosyltransferase-II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6)
    • Bai X, Zhou D, Brown JR, Crawford BE, Hennet T, Esko JD. 2001. Biosynthesis of the linkage region of glycosaminoglycans: Cloning and activity of galactosyltransferase-II, the sixth member of the β1,3- galactosyltransferase family (β3GalT6). J Biol Chem. 276:48189-48195.
    • (2001) J Biol Chem , vol.276 , pp. 48189-48195
    • Bai, X.1    Zhou, D.2    Brown, J.R.3    Crawford, B.E.4    Hennet, T.5    Esko, J.D.6
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 34547728713 scopus 로고    scopus 로고
    • Molecular basis for acceptor substrate specificity of the human β1,3-glucuronosyltransferases GlcAT-I and GlcAT-P involved in glycosaminoglycan and HNK-1 carbohydrate epitope biosynthesis, respectively
    • DOI 10.1093/glycob/cwm055
    • Fondeur-Gelinotte M, Lattard V, Gulberti S, Oriol R, Mulliert G, Coughtrie M, Magdalou J, Netter P, Ouzzine M, Fournel-Gigleux S. 2007. Molecular basis for acceptor substrate specificity of the human β1,3- glucuronosyltransferases GlcAT-I and GlcAT-P involved in glycosaminoglycans and HNK-1 carbohydrate epitope biosynthesis, respectively. Glycobiology. 17:857-867. (Pubitemid 47241822)
    • (2007) Glycobiology , vol.17 , Issue.8 , pp. 857-867
    • Fondeur-Gelinotte, M.1    Lattard, V.2    Gulberti, S.3    Oriol, R.4    Mulliert, G.5    Coughtrie, M.W.H.6    Magdalou, J.7    Netter, P.8    Ouzzine, M.9    Fournel-Gigleux, S.10
  • 5
    • 0034624041 scopus 로고    scopus 로고
    • Molecular cloning and expression of human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II
    • DOI 10.1006/jmbi.2000.4261
    • Götting C, Kuhn J, Zahn R, Brinkmann T, Kleesiek K. 2000. Molecular cloning and expression of human UDP-D-xylose-proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. J Mol Biol. 304:517-528. (Pubitemid 32006187)
    • (2000) Journal of Molecular Biology , vol.304 , Issue.4 , pp. 517-528
    • Gotting, C.1    Kuhn, J.2    Zahn, R.3    Brinkmann, T.4    Kleesiek, K.5
  • 6
    • 12544255428 scopus 로고    scopus 로고
    • Phosphorylation and sulfation of oligosaccharide substrates critically influence the activity of human β1,4-galactosyltransferase 7 (GalT-I) and β1,3-glucuronosyltransferase i (GlcAT-I) involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
    • Gulberti S, Lattard V, Fondeur M, Jacquinet JC, Mulliert G, Netter P, Magdalou J, Ouzzine M, Fournel-Gigleux S. 2005. Phosphorylation and sulfation of oligosaccharide substrates critically influence the activity of human β1,4-galactosyltransferase 7 (GalT-I) and β1,3-glucuronosyltransferase I (GlcAT-I) involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J Biol Chem. 280(2):1417-1425.
    • (2005) J Biol Chem , vol.280 , Issue.2 , pp. 1417-1425
    • Gulberti, S.1    Lattard, V.2    Fondeur, M.3    Jacquinet, J.C.4    Mulliert, G.5    Netter, P.6    Magdalou, J.7    Ouzzine, M.8    Fournel-Gigleux, S.9
  • 8
    • 79951535271 scopus 로고    scopus 로고
    • Chondroitin 4-O-sulfotransferase-1 regulates the chain length of chondroitin sulfate in co-operation with chondroitin N- acetylgalactosaminyltransferase-2
    • Izumikawa T, Okuura Y, Koike T, Sakoda N, Kitagawa H. 2011. Chondroitin 4-O-sulfotransferase-1 regulates the chain length of chondroitin sulfate in co-operation with chondroitin N-acetylgalactosaminyltransferase-2. Biochem J. 434(2):321-331.
    • (2011) Biochem J. , vol.434 , Issue.2 , pp. 321-331
    • Izumikawa, T.1    Okuura, Y.2    Koike, T.3    Sakoda, N.4    Kitagawa, H.5
  • 9
    • 0346154834 scopus 로고    scopus 로고
    • An expeditious preparation of various sulfoforms of the disaccharide β-D-Galp-(1→3)-D-Galp, a partial structure of the linkage region of proteoglycans, as their 4-methoxyphenyl β-D-glycosides
    • DOI 10.1016/j.carres.2003.10.012
    • Jacquinet J-C. 2004. An expeditious preparation of various sulfoforms of the disaccharide β-D-Galp-(1→3)-β-D-Galp, a partial structure of the linkage region of proteoglycans, as their 4-methoxyphenyl-β-D- glycosides. Carbohydr Res. 339(2):349-359. (Pubitemid 38043940)
    • (2004) Carbohydrate Research , vol.339 , Issue.2 , pp. 349-359
    • Jacquinet, J.-C.1
  • 10
    • 70349268369 scopus 로고    scopus 로고
    • From polymer to size-defined oligomers: A highly divergent and stereocontrolled construction of chondroitin sulfate A, C, D, E, K, L and M oligomers from a single precursor
    • Jacquinet J-C, Lopin-Bon C, Vibert A. 2009. From polymer to size-defined oligomers: A highly divergent and stereocontrolled construction of chondroitin sulfate A, C, D, E, K, L and M oligomers from a single precursor. Chem Eur J. 15(37):9579-9595.
    • (2009) Chem Eur J. , vol.15 , Issue.37 , pp. 9579-9595
    • Jacquinet, J.-C.1    Lopin-Bon, C.2    Vibert, A.3
  • 12
    • 0028981379 scopus 로고
    • N-Acetylgalactosamine (GalNAc) transfer to the common carbohydrate-protein linkage region of sulfated glycosaminoglycans: Identification of UDP-GalNAc:chondro-oligosaccharide α-N- acetylgalactosaminyltransferase in fetal bovine serum
    • Kitagawa H, Tanaka Y, Tsuchida K, Goto F, Ogawa T, Lidholt K, Lindahl U, Sugahara K. 1995. N-Acetylgalactosamine (GalNAc) transfer to the common carbohydrate-protein linkage region of sulfated glycosaminoglycans: Identification of UDP-GalNAc:chondro-oligosaccharide α-N- acetylgalactosaminyltransferase in fetal bovine serum. J Biol Chem. 270(38):22190-22195.
    • (1995) J Biol Chem , vol.270 , Issue.38 , pp. 22190-22195
    • Kitagawa, H.1    Tanaka, Y.2    Tsuchida, K.3    Goto, F.4    Ogawa, T.5    Lidholt, K.6    Lindahl, U.7    Sugahara, K.8
  • 13
    • 0032549523 scopus 로고    scopus 로고
    • Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
    • DOI 10.1074/jbc.273.12.6615
    • Kitagawa H, Tone Y, Tamura JI, Neumann KW, Ogawa T, Oka S, Kawasaki T, Sugahara K. 1998. Molecular cloning and expression of glucuronosyltransferase-I involved in the biosynthesis of glycosaminoglycan-protein linkage region of proteoglycans. J Biol Chem. 273:6615-6618. (Pubitemid 28160318)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 6615-6618
    • Kitagawa, H.1    Tone, Y.2    Tamura, J.-I.3    Neumann, K.W.4    Ogawa, T.5    Oka, S.6    Kawasaki, T.7    Sugahara, K.8
  • 14
    • 55549128589 scopus 로고    scopus 로고
    • Sulfation of the galactose residues in the glycosaminoglycan-protein linkage region by recombinant human chondroitin 6-O-sulfotransferase-1
    • Kitagawa H, Tsutsumi K, Ikegami-Kuzuhara A, Nadanaka S, Goto F, Ogawa T, Sugahara K. 2008. Sulfation of the galactose residues in the glycosaminoglycan-protein linkage region by recombinant human chondroitin 6-O-sulfotransferase-1. J Biol Chem. 283(41):27438-27443.
    • (2008) J Biol Chem , vol.283 , Issue.41 , pp. 27438-27443
    • Kitagawa, H.1    Tsutsumi, K.2    Ikegami-Kuzuhara, A.3    Nadanaka, S.4    Goto, F.5    Ogawa, T.6    Sugahara, K.7
  • 15
    • 0031465169 scopus 로고    scopus 로고
    • Developmental regulation of the sulfation profile of chondroitin sulfate chains in the chicken embryo brain
    • DOI 10.1074/jbc.272.50.31377
    • Kitagawa H, Tsutsumi K, Tone Y, Sugahara K. 1997. Developmental regulation of the sulfation profile of chondroitin sulfate chains in the chicken embryo brain. J Biol Chem. 272(50):31377-31381. (Pubitemid 28013273)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.50 , pp. 31377-31381
    • Kitagawa, H.1    Tsutsumi, K.2    Tone, Y.3    Sugahara, K.4
  • 16
    • 0033799418 scopus 로고    scopus 로고
    • Molecular structure of the carbohydrate-protein linkage region fragments from connective-tissue proteoglycans
    • Krishna NR, Agrawal PK. 2000. Molecular structure of the carbohydrate-protein linkage region fragments from connective-tissue proteoglycans. Adv Carbohydr Chem Biochem. 56:201-234.
    • (2000) Adv Carbohydr Chem Biochem , vol.56 , pp. 201-234
    • Krishna, N.R.1    Agrawal, P.K.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 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
  • 18
    • 77951139823 scopus 로고    scopus 로고
    • Structural variation of chondroitin sulfate and its roles in the central nervous system
    • Maeda N. 2010. Structural variation of chondroitin sulfate and its roles in the central nervous system. Cent Nerv Syst Agents Med Chem. 10(1):22-31.
    • (2010) Cent Nerv Syst Agents Med Chem. , vol.10 , Issue.1 , pp. 22-31
    • Maeda, N.1
  • 19
    • 0030928652 scopus 로고    scopus 로고
    • Biosynthesis of the proteoglycan decorin: Transient 2-phosphorylation of xylose during formation of the trisaccharide linkage region
    • Moses J, Oldberg A, Cheng F, Fransson LA. 1997. Biosynthesis of the proteoglycan decorin-transient 2-phosphorylation of xylose during formation of the trisaccharide linkage region. Eur J Biochem. 248(2):521-526. (Pubitemid 27387500)
    • (1997) European Journal of Biochemistry , vol.248 , Issue.2 , pp. 521-526
    • Moses, J.1    Oldberg, A.2    Cheng, F.3    Fransson, L.-A.4
  • 20
    • 0033152919 scopus 로고    scopus 로고
    • Involvement of the core protein in the first β-N-acetylgalactosamine transfer to the glycosaminoglycan-protein linkage-region tetrasaccharide and in the subsequent polymerization: The critical determining step for chondroitin sulphate biosynthesis
    • DOI 10.1042/0264-6021:3400353
    • Nadanaka S, Kitagawa H, Goto F, Tamura JI, Neumann KW, Ogawa T. 1999. Involvement of the core protein in the first β-N-acetylgalactosamine transfer to the glycosaminoglycan-protein linkage region tetrasaccharide and in the subsequent polymerization: The critical determining step for the chondroitin sulfate biosynthesis. Biochem J. 340:353-357. (Pubitemid 29286551)
    • (1999) Biochemical Journal , vol.340 , Issue.2 , pp. 353-357
    • Nadanaka, S.1    Kitagawa, H.2    Goto, F.3    Tamura, J.-I.4    Neumann, K.W.5    Ogawa, T.6    Sugahara, K.7
  • 21
    • 0033551690 scopus 로고    scopus 로고
    • Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase-I involved in the glycosaminoglycan-protein linkage region of proteoglycans
    • Okajima T, Yoshida K, Kondo T, Furukawa K. 1999. Human homolog of Caenorhabditis elegans sqv-3 gene is galactosyltransferase-I involved in the glycosaminoglycan-protein linkage region of proteoglycans. J Biol Chem. 274:22915-22918.
    • (1999) J Biol Chem , vol.274 , pp. 22915-22918
    • Okajima, T.1    Yoshida, K.2    Kondo, T.3    Furukawa, K.4
  • 22
    • 0037036376 scopus 로고    scopus 로고
    • Structure-based design of β1,4-galactosyltransferase I (β4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: Point mutation broadens β4Gal-T1 donor specificity
    • DOI 10.1074/jbc.M111183200
    • Ramakrishnan B, Qasba PK. 2002. Structure-based design of β1,4-galactosyltransferase I (β4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: Point mutation broadens beta 4Gal-T1 donor specificity. J Biol Chem. 277(23):20833-20839. (Pubitemid 34967390)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20833-20839
    • Ramakrishnan, B.1    Qasba, P.K.2
  • 23
    • 79952127774 scopus 로고    scopus 로고
    • Chondroitin β-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies
    • Saigoh K, Izumikawa T, Koike T, Shimizu J, Kitagawa H, Kusunoki S. 2011. Chondroitin β-1,4-N-acetylgalactosaminyltransferase-1 missense mutations are associated with neuropathies. J Hum Genet. 56(2):143-146.
    • (2011) J Hum Genet , vol.56 , Issue.2 , pp. 143-146
    • Saigoh, K.1    Izumikawa, T.2    Koike, T.3    Shimizu, J.4    Kitagawa, H.5    Kusunoki, S.6
  • 24
    • 33947537983 scopus 로고    scopus 로고
    • Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a critical role in chondroitin sulfate synthesis in cartilage
    • DOI 10.1074/jbc.M606870200
    • Sakai K, Kimata K, Sato T, Gotoh M, Narimatsu H, Shinomiya K, Watanabe H. 2007. Chondroitin sulfate N-acetylgalactosaminyltransferase-1 plays a critical role in chondroitin sulfate synthesis in cartilage. J Biol Chem. 282 (6):4152-4161. (Pubitemid 47084455)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 4152-4161
    • Sakai, K.1    Kimata, K.2    Sato, T.3    Gotoh, M.4    Narimatsu, H.5    Shinomiya, K.6    Watanabe, H.7
  • 26
    • 79953133504 scopus 로고    scopus 로고
    • Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is necessary for normal endochondral ossification and aggrecan metabolism
    • Sato T, Kudo T, Ikehara Y, Ogawa H, Hirano T, Kiyohara K, Hagiwara K, Togayachi A, Ema M, Takahashi S, et al. 2011. Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is necessary for normal endochondral ossification and aggrecan metabolism. J Biol Chem. 286(7):5803-5812.
    • (2011) J Biol Chem , vol.286 , Issue.7 , pp. 5803-5812
    • Sato, T.1    Kudo, T.2    Ikehara, Y.3    Ogawa, H.4    Hirano, T.5    Kiyohara, K.6    Hagiwara, K.7    Togayachi, A.8    Ema, M.9    Takahashi, S.10
  • 27
    • 0033794318 scopus 로고    scopus 로고
    • Recent advances in the study of the biosynthesis functions of sulfated glycosaminoglycans
    • Sugahara K, Kitagawa H. 2000. Recent advances in the study of the biosynthesis functions of sulfated glycosaminoglycans. Curr Opin Struct Biol. 10:518-527.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 518-527
    • Sugahara, K.1    Kitagawa, H.2
  • 28
    • 0026352534 scopus 로고
    • Structural studies on sulfated oligosaccharides derived from the carbohydrate-protein linkage region of chondroitin sulfate proteoglycans of whale cartilage
    • Sugahara K, Masuda M, Harada T, Yamashina I, de Waard P, Vliegenthart JF. 1991. Structural studies on sulfated oligosaccharides derived from the carbohydrate-protein linkage region of chondroitin sulfate proteoglycans of whale cartilage. Eur J Biochem. 202(3):805-811.
    • (1991) Eur J Biochem , vol.202 , Issue.3 , pp. 805-811
    • Sugahara, K.1    Masuda, M.2    Harada, T.3    Yamashina, I.4    De Waard, P.5    Vliegenthart, J.F.6
  • 29
    • 0026540831 scopus 로고
    • The phosphorylated and/or sulfated structure of the carbohydrate-protein linkage region isolated from chondroitin sulfate in the hybrid proteoglycans of Engelbreth-Holm-Swarm mouse tumor
    • Sugahara K, Mizuno N, Okumura Y, Kawasaki T. 1992. The phosphorylated and/or sulfated structure of the carbohydrate-protein linkage region isolated from chondroitin sulfate in the hybrid proteoglycans of Engelbreth-Holm-Swarm mouse tumor. Eur J Biochem. 204:401-406.
    • (1992) Eur J Biochem , vol.204 , pp. 401-406
    • Sugahara, K.1    Mizuno, N.2    Okumura, Y.3    Kawasaki, T.4
  • 30
    • 0028949086 scopus 로고
    • Structural studies on the hexasaccharide alditols isolated from the carbohydrate-protein linkage region of dermatan sulfate proteoglycans of bovine aorta: Demonstration of iduronic acid-containing components
    • Sugahara K, Yamashina I, De Waard P, Van Halbeek H, Vliegenthart JF. 1995. Structural studies on the hexasaccharide alditols isolated from the carbohydrate-protein linkage region of dermatan sulfate proteoglycans of bovine aorta: Demonstration of iduronic acid-containing components. J Biol Chem. 270:7204-7212.
    • (1995) J Biol Chem , vol.270 , pp. 7204-7212
    • Sugahara, K.1    Yamashina, I.2    De Waard, P.3    Van Halbeek, H.4    Vliegenthart, J.F.5
  • 31
    • 0023786534 scopus 로고
    • Structural studies on sulfated glycopeptides from the carbohydrate-protein linkage region of chondroitin 4-sulfate proteoglycans of swarm rat chondrosarcoma: Demonstration of the structure Gal(4-O-sulfate)beta 1-3Galβ1-4Xylβ1-O-Ser
    • Sugahara K, Yamashina I, De Waard P, Van Halbeek H, Vliegenthart JF. 1988. Structural studies on sulfated glycopeptides from the carbohydrate-protein linkage region of chondroitin 4-sulfate proteoglycans of swarm rat chondrosarcoma: Demonstration of the structure Gal(4-O-sulfate)beta 1-3Galβ1-4Xylβ1-O-Ser. J Biol Chem. 263(21):10168-10174.
    • (1988) J Biol Chem , vol.263 , Issue.21 , pp. 10168-10174
    • Sugahara, K.1    Yamashina, I.2    De Waard, P.3    Van Halbeek, H.4    Vliegenthart, J.F.5
  • 32
    • 78549282816 scopus 로고    scopus 로고
    • Identification of key functional residues in the active site of human β1,4-galactosyltransferase 7: A major enzyme in the glycosaminoglycan synthesis pathway
    • Talhaoui I, Bui C, Oriol R, Mulliert G, Gulberti S, Netter P, Coughtrie MW, Ouzzine M, Fournel-Gigleux S. 2010. Identification of key functional residues in the active site of human β1,4-galactosyltransferase 7: A major enzyme in the glycosaminoglycan synthesis pathway. J Biol Chem. 285 (48):37342-37358.
    • (2010) J Biol Chem , vol.285 , Issue.48 , pp. 37342-37358
    • Talhaoui, I.1    Bui, C.2    Oriol, R.3    Mulliert, G.4    Gulberti, S.5    Netter, P.6    Coughtrie, M.W.7    Ouzzine, M.8    Fournel-Gigleux, S.9
  • 33
    • 1342263521 scopus 로고    scopus 로고
    • Synthesis of various sulfoforms of the trisaccharide β-D-GlcpA- (1→3)-β-D-Galp-(1→3)-β-D-Galp-(1→OMP) as probes for the study of the biosynthesis and sorting of proteoglycans
    • Thollas B, Jacquinet J-C. 2004. Synthesis of various sulfoforms of the trisaccharide β-D-GlcpA-(1→3)-β-D-Galp-(1→3)-β-D-Galp- (1→OMP) as probes for the study of the biosynthesis and sorting of proteoglycans. Org Biomol Chem. 2(3):434-442.
    • (2004) Org Biomol Chem , vol.2 , Issue.3 , pp. 434-442
    • Thollas, B.1    Jacquinet, J.-C.2
  • 34
    • 47749118405 scopus 로고    scopus 로고
    • 2-O-Phosphorylation of xylose and 6-O-sulfation of galactose in the protein linkage region of glycosaminoglycans influence the glucuronyltransferase-I activity involved in the linkage region synthesis
    • Tone Y, Pedersen LC, Yamamoto T, Izumikawa T, Kitagawa H, Nishihara J, Tamura J, Negishi M, Sugahara K. 2008. 2-O-Phosphorylation of xylose and 6-O-sulfation of galactose in the protein linkage region of glycosaminoglycans influence the glucuronyltransferase-I activity involved in the linkage region synthesis. J Biol Chem. 283(24):16801-16807.
    • (2008) J Biol Chem , vol.283 , Issue.24 , pp. 16801-16807
    • Tone, Y.1    Pedersen, L.C.2    Yamamoto, T.3    Izumikawa, T.4    Kitagawa, H.5    Nishihara, J.6    Tamura, J.7    Negishi, M.8    Sugahara, K.9
  • 35
    • 33846010772 scopus 로고    scopus 로고
    • Chondroitin 4-O-sulfotransferase-1 regulates E disaccharide expression of chondroitin sulfate required for herpes simplex virus infectivity
    • DOI 10.1074/jbc.M609320200
    • Uyama T, Ishida M, Izumikawa T, Trybala E, Tufaro F, Bergström T, Sugahara K, Kitagawa H. 2006. Chondroitin 4-O-sulfotransferase-1 regulates E disaccharide expression of chondroitin sulfate required for herpes simplex virus infectivity. J Biol Chem. 281 (50):38668-38674. (Pubitemid 46041992)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38668-38674
    • Uyama, T.1    Ishida, M.2    Izumikawa, T.3    Trybala, E.4    Tufaro, F.5    Bergstrom, T.6    Sugahara, K.7    Kitagawa, H.8
  • 36
    • 0037088673 scopus 로고    scopus 로고
    • Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase. The key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate
    • DOI 10.1074/jbc.M111434200
    • Uyama T, Kitagawa H, Tamura JI, Sugahara K. 2002. Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: The key enzyme for the chain initiation and elongation of chondroitin-dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin-heparan sulphate. J Biol Chem. 277:8841-8846. (Pubitemid 34952951)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8841-8846
    • Uyama, T.1    Kitagawa, H.2    Tamura, J.-I.3    Sugahara, K.4
  • 39
    • 0037200168 scopus 로고    scopus 로고
    • Determination of the glycosaminoglycan-protein linkage region oligosaccharide structures of proteoglycans from Drosophila melanogaster and Caenorhabditis elegans
    • DOI 10.1074/jbc.M205078200
    • Yamada S, Okada Y, Ueno M, Iwata S, Deepa SS, Nishimura S, Fujita M, Van Die I, Hirabayashi Y, Sugahara K. 2002. Determination of the glycosaminoglycan-protein linkage region oligosaccharide structures of proteoglycans from Drosophila melanogaster and Caenorhabditis elegans. J Biol Chem. 277(35):31877-31886. (Pubitemid 34975659)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 31877-31886
    • Yamada, S.1    Okada, Y.2    Ueno, M.3    Iwata, S.4    Deepa, S.S.5    Nishimura, S.6    Fujita, M.7    Van Die, I.8    Hirabayashi, Y.9    Sugahara, K.10
  • 40
    • 48949098167 scopus 로고    scopus 로고
    • Optimized conditions for high-performance liquid chromatography analysis of oligosaccharides using 7-amino-4-methylcoumarin as a reductive amination reagent
    • Yodoshi M, Tani A, Ohta Y, Suzuki S. 2008. Optimized conditions for high-performance liquid chromatography analysis of oligosaccharides using 7-amino-4-methylcoumarin as a reductive amination reagent. J Chromatogr A. 1203(2):137-145.
    • (2008) J Chromatogr A , vol.1203 , Issue.2 , pp. 137-145
    • Yodoshi, M.1    Tani, A.2    Ohta, Y.3    Suzuki, S.4


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