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Volumn 15, Issue 7, 2006, Pages 1667-1678

Phylogenetic and mutational analyses reveal key residues for UDP-glucuronic acid binding and activity of β1,3-glucuronosyltransferase I (GlcAT-I)

Author keywords

Enzyme kinetics; Glucuronosyltransferase family; Glycosaminoglycan synthesis; Phylogeny; Site directed mutagenesis; UDP glucuronic acid binding site

Indexed keywords

AMINO ACID DERIVATIVE; BETA1,3 GLUCURONOSYLTRANSFERASE 1 ENZYME; GLUCURONOSYLTRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCURONIC ACID;

EID: 33745712764     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062089106     Document Type: Article
Times cited : (16)

References (47)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation 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
    • 31144449168 scopus 로고    scopus 로고
    • Structures and mechanisms of glycosyltransferases superfamily
    • Breton, C., Snajdrova, L., Jeanneau, C., Koea, J., and Imberty, A. 2006. Structures and mechanisms of glycosyltransferases superfamily. Glycobiology 16: 29-37.
    • (2006) Glycobiology , vol.16 , pp. 29-37
    • Breton, C.1    Snajdrova, L.2    Jeanneau, C.3    Koea, J.4    Imberty, A.5
  • 4
    • 0034718491 scopus 로고    scopus 로고
    • sqv-3, -7, and -8, a set of genes affecting morphogenesis in Caenorhabditis elegans, encode enzymes required for glycosaminoglycan biosynthesis
    • Bulik, D.A., Wei, G., Toyoda, H., Kinoshita-Toyoda, A., Waldrip, W.R., Esko, J.D., Robbins, P.W., and Selleck, S.B. 2000. sqv-3, -7, and -8, a set of genes affecting morphogenesis in Caenorhabditis elegans, encode enzymes required for glycosaminoglycan biosynthesis. Proc. Natl. Acad. Sci. 97: 10838-10843.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 10838-10843
    • Bulik, D.A.1    Wei, G.2    Toyoda, H.3    Kinoshita-Toyoda, A.4    Waldrip, W.R.5    Esko, J.D.6    Robbins, P.W.7    Selleck, S.B.8
  • 5
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana, J. 2000. Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol. Biol. Evol. 17: 540-552.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 540-552
    • Castresana, J.1
  • 6
    • 0023008691 scopus 로고
    • Structure of sulfated glucuronyl glycolipids in the nervous system reacting with HNK-1 antibody and some IgM paraproteins in neuropathy
    • Chou, D.K., Ilyas, A.A., Evans, J.E., Costello, C., Quarles, R.H., and Jungalwala, F.B. 1986. Structure of sulfated glucuronyl glycolipids in the nervous system reacting with HNK-1 antibody and some IgM paraproteins in neuropathy. J. Biol. Chem. 261: 11717-11725.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11717-11725
    • Chou, D.K.1    Ilyas, A.A.2    Evans, J.E.3    Costello, C.4    Quarles, R.H.5    Jungalwala, F.B.6
  • 8
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho, P.M., Deleury, E., Davies, G.J., and Henrissat, B. 2003. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328: 307-317.
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 9
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using bootstraps
    • Felsenstein, J. 1985. Confidence limits on phylogenies: An approach using bootstraps. Evolution Int. J. Org. Evolution 39: 783-791.
    • (1985) Evolution Int. J. Org. Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 10
    • 0030464460 scopus 로고    scopus 로고
    • SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny
    • Galtier, N., Gouy, M., and Gautier, C. 1996. SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny. Comput. Appl. Biosci. 12: 543-548.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2    Gautier, C.3
  • 11
    • 0033168184 scopus 로고    scopus 로고
    • Crystal structures of the bovine β4-galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
    • Gastinel, L.N., Cambillau, C., and Bourne, Y. 1999. Crystal structures of the bovine β4-galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J. 18: 3546-3557.
    • (1999) EMBO J. , vol.18 , pp. 3546-3557
    • Gastinel, L.N.1    Cambillau, C.2    Bourne, Y.3
  • 12
    • 0042357069 scopus 로고    scopus 로고
    • The functional glycosyltransferase signature sequence of the human β1,3-glucuronosyltransferase is a XDD motif
    • Gulberti, S., Fournel-Gigleux, S., Mulliert, G., Aubry, A., Netter, P., Magdalou, J., and Ouzzine, M. 2003. The functional glycosyltransferase signature sequence of the human β1,3-glucuronosyltransferase is a XDD motif. J. Biol. Chem. 278: 32219-32226.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32219-32226
    • Gulberti, S.1    Fournel-Gigleux, S.2    Mulliert, G.3    Aubry, A.4    Netter, P.5    Magdalou, J.6    Ouzzine, M.7
  • 13
    • 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, J.C., Mulliert, G., Netter, P., Magdalou, J., Ouzzine, M., and 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: 1417-1425.
    • (2005) J. Biol. Chem. , vol.280 , 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
  • 14
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • Haltiwanger, R.S. and Lowe, J.B. 2004. Role of glycosylation in development. Annu. Rev. Biochem. 73: 491-537.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 15
    • 25144501600 scopus 로고    scopus 로고
    • The animal sialyltransferases and sialyltransferase-related genes: A phylogenetic approach
    • Harduin-Lepers, A., Mollicone, R., Delannoy, P., and Oriol, R. 2005. The animal sialyltransferases and sialyltransferase-related genes: A phylogenetic approach. Glycobiology 15: 805-817.
    • (2005) Glycobiology , vol.15 , pp. 805-817
    • Harduin-Lepers, A.1    Mollicone, R.2    Delannoy, P.3    Oriol, R.4
  • 16
    • 0032849859 scopus 로고    scopus 로고
    • CAP3: A DNA sequence assembly program
    • Huang, X. and Madan, A. 1999. CAP3: A DNA sequence assembly program. Genome Res. 9: 868-877.
    • (1999) Genome Res. , vol.9 , pp. 868-877
    • Huang, X.1    Madan, A.2
  • 17
    • 0037058926 scopus 로고    scopus 로고
    • A pectin glucuronyltransferase gene is essential for intercellular attachment in the plant meristem
    • Iwai, H., Masaoka, N., Ishii, T., and Satoh, S. 2002. A pectin glucuronyltransferase gene is essential for intercellular attachment in the plant meristem. Proc. Natl. Acad. Sci. 99: 16319-16324.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 16319-16324
    • Iwai, H.1    Masaoka, N.2    Ishii, T.3    Satoh, S.4
  • 18
    • 2542420721 scopus 로고    scopus 로고
    • Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1
    • Kakuda, S., Shiba, T., Ishiguro, M., Tagawa, H., Oka, S., Kajihara, Y., Kawasaki, T., Wakatsuki, S., and Kato, R. 2004. Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1. J. Biol. Chem. 279: 22693-22703.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22693-22703
    • Kakuda, S.1    Shiba, T.2    Ishiguro, M.3    Tagawa, H.4    Oka, S.5    Kajihara, Y.6    Kawasaki, T.7    Wakatsuki, S.8    Kato, R.9
  • 19
    • 0038439209 scopus 로고    scopus 로고
    • Identification and characterization of three Drosophila melanogaster glucuronyltransferases responsible for the synthesis of the conserved glycosaminoglycan-protein linkage region of proteoglycans. Two novel homologs exhibit broad specificity toward oligosaccharides from proteoglycans, glycoproteins, and glycosphingolipids
    • Kim, B.T., Tsuchida, K., Lincecum, J., Kitagawa, H., Bernfield, M., and Sugahara, K. 2003. Identification and characterization of three Drosophila melanogaster glucuronyltransferases responsible for the synthesis of the conserved glycosaminoglycan-protein linkage region of proteoglycans. Two novel homologs exhibit broad specificity toward oligosaccharides from proteoglycans, glycoproteins, and glycosphingolipids. J. Biol. Chem. 278: 9116-9124.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9116-9124
    • Kim, B.T.1    Tsuchida, K.2    Lincecum, J.3    Kitagawa, H.4    Bernfield, M.5    Sugahara, K.6
  • 20
    • 0032549523 scopus 로고    scopus 로고
    • Molecular cloning of glucuronosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
    • Kitagawa, H., Tone, Y., Tamura, J., Neumann, K.W., Ogawa, T., Oka, O., Kawasaki, T., and Sugahara, K. 1998. Molecular cloning of glucuronosyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273: 6615-6618.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6615-6618
    • Kitagawa, H.1    Tone, Y.2    Tamura, J.3    Neumann, K.W.4    Ogawa, T.5    Oka, O.6    Kawasaki, T.7    Sugahara, K.8
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0141429012 scopus 로고    scopus 로고
    • Developmental roles of heparan sulfate proteoglycans in Drosophila
    • Lin, X. and Perrimon, N. 2002. Developmental roles of heparan sulfate proteoglycans in Drosophila. Glycoconj. J. 19: 363-368.
    • (2002) Glycoconj. J. , vol.19 , pp. 363-368
    • Lin, X.1    Perrimon, N.2
  • 24
    • 0036952252 scopus 로고    scopus 로고
    • Cloning, characterization, and chromosome mapping of the human GlcAT-S gene
    • Marcos, I., Galan, J.J., Borrego, S., and Antinolo, G. 2002. Cloning, characterization, and chromosome mapping of the human GlcAT-S gene. J. Hum. Genet. 47: 677-680.
    • (2002) J. Hum. Genet. , vol.47 , pp. 677-680
    • Marcos, I.1    Galan, J.J.2    Borrego, S.3    Antinolo, G.4
  • 25
    • 0021062674 scopus 로고
    • Recognition of myelin-associated glycoprotein by the monoclonal antibody HNK-1
    • McGarry, R.C., Helfand, S.L., Quarles, R.H., and Roder, J.C. 1983. Recognition of myelin-associated glycoprotein by the monoclonal antibody HNK-1. Nature 306: 376-378.
    • (1983) Nature , vol.306 , pp. 376-378
    • McGarry, R.C.1    Helfand, S.L.2    Quarles, R.H.3    Roder, J.C.4
  • 26
    • 0037418741 scopus 로고    scopus 로고
    • Glucosaminylglycan biosynthesis: What we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2
    • Negishi, M., Dong, J., Darden, T.A., Pedersen, L.G., and Pedersen, L.C. 2003. Glucosaminylglycan biosynthesis: What we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2. Biochem. Biophys. Res. Commun. 303: 393-398.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 393-398
    • Negishi, M.1    Dong, J.2    Darden, T.A.3    Pedersen, L.G.4    Pedersen, L.C.5
  • 27
    • 0033850774 scopus 로고    scopus 로고
    • Studies in the structure-function relationship of the HNK-1 associated glucuronosyltransferase, GlcAT-P, by computer modeling and sitedirected mutagenesis
    • Ohtsubo, K., Imajo, S., Ishiguro, M., Nakatani, T., Oka, S., and Kawasaki, T. 2000. Studies in the structure-function relationship of the HNK-1 associated glucuronosyltransferase, GlcAT-P, by computer modeling and sitedirected mutagenesis. J. Biochem. 128: 283-291.
    • (2000) J. Biochem. , vol.128 , pp. 283-291
    • Ohtsubo, K.1    Imajo, S.2    Ishiguro, M.3    Nakatani, T.4    Oka, S.5    Kawasaki, T.6
  • 28
    • 0032973964 scopus 로고    scopus 로고
    • Expression of functionally active human hepatic UDP- glucuronosyltransferase (UGT1A6) lacking the N-terminal signal sequence in the endoplasmic reticulum
    • Ouzzine, M., Magdalou, J., Burchell, B., and Fournel-Gigleux, S. 1999. Expression of functionally active human hepatic UDP-glucuronosyltransferase (UGT1A6) lacking the N-terminal signal sequence in the endoplasmic reticulum. FEBS Lett. 454: 187-191.
    • (1999) FEBS Lett. , vol.454 , pp. 187-191
    • Ouzzine, M.1    Magdalou, J.2    Burchell, B.3    Fournel-Gigleux, S.4
  • 29
    • 0033675536 scopus 로고    scopus 로고
    • Importance of histidine residues for the function of the human liver UDP-glucuronosyltransferase UGT1A6: Evidence for the catalytic role of histidine 370
    • Ouzzine, M., Antonio, L., Burchell, B., Netter, P., Fournel-Gigleux, S., and Magdalou, J. 2000a. Importance of histidine residues for the function of the human liver UDP-glucuronosyltransferase UGT1A6: Evidence for the catalytic role of histidine 370. Mol. Pharmacol. 58: 1609-1615.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1609-1615
    • Ouzzine, M.1    Antonio, L.2    Burchell, B.3    Netter, P.4    Fournel-Gigleux, S.5    Magdalou, J.6
  • 30
    • 0034623230 scopus 로고    scopus 로고
    • Structure/function of the human Ga1β1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues
    • Ouzzine, M., Gulberti, S., Netter, P., Magdalou, J., and Fournel-Gigleux, S. 2000b. Structure/function of the human Ga1β1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues. J. Biol. Chem. 275: 28254-28260.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28254-28260
    • Ouzzine, M.1    Gulberti, S.2    Netter, P.3    Magdalou, J.4    Fournel-Gigleux, S.5
  • 31
    • 0037067755 scopus 로고    scopus 로고
    • The donor substrate specificity of the human β1,3- glucuronosyltransferase I (GlcAT-I) towards UDP-glucuronic acid is determined by two crucial histidine and arginine residues
    • _. 2002. The donor substrate specificity of the human β1,3-glucuronosyltransferase I (GlcAT-I) towards UDP-glucuronic acid is determined by two crucial histidine and arginine residues. J. Biol. Chem. 277: 25439-25445.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25439-25445
  • 32
    • 0034602394 scopus 로고    scopus 로고
    • Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I
    • Pedersen, L.C., Tsuchida, K., Kitagawa, H., Sugahara, K., Darden, T.A., and Negishi, M. 2000. Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. J. Biol. Chem. 275: 34580-34585.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34580-34585
    • Pedersen, L.C.1    Tsuchida, K.2    Kitagawa, H.3    Sugahara, K.4    Darden, T.A.5    Negishi, M.6
  • 33
    • 0037077202 scopus 로고    scopus 로고
    • Crystal structure of β1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA
    • Pedersen, L.C., Darden, T.A., and Negishi, M. 2002. Crystal structure of β1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA. J. Biol. Chem. 277: 21869-21873.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21869-21873
    • Pedersen, L.C.1    Darden, T.A.2    Negishi, M.3
  • 34
    • 0035113472 scopus 로고    scopus 로고
    • Higher plant glycosyltransferases
    • Ross, J., Li, Y., Lim, E., and Bowles, D.J. 2001. Higher plant glycosyltransferases. Genome Biol. 2: http://genomebiology.com.
    • (2001) Genome Biol. , vol.2
    • Ross, J.1    Li, Y.2    Lim, E.3    Bowles, D.J.4
  • 35
    • 0036019912 scopus 로고    scopus 로고
    • Chondrodysplasias due to proreoglycan defects
    • Schwartz, N.B. and Domowicz, M. 2002. Chondrodysplasias due to proreoglycan defects. Glycobiology 12: 57-68.
    • (2002) Glycobiology , vol.12 , pp. 57-68
    • Schwartz, N.B.1    Domowicz, M.2
  • 36
    • 0003518480 scopus 로고
    • John Wiley & Sons, New York
    • Segel, I.H. 1975. Enzyme kinetics.. John Wiley & Sons, New York.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 37
    • 0035824876 scopus 로고    scopus 로고
    • Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: A comparison with related NDP-sugar glycosyltransferases
    • Tarbouriech, N., Charnock, S.J., and Davies, G.J. 2001. Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: A comparison with related NDP-sugar glycosyltransferases. J. Mol. Biol. 314: 655-661.
    • (2001) J. Mol. Biol. , vol.314 , pp. 655-661
    • Tarbouriech, N.1    Charnock, S.J.2    Davies, G.J.3
  • 38
    • 0030911792 scopus 로고    scopus 로고
    • Cloning and functional expression of a novel glucuronosyltransferase involved in the biosynthesis of the carbohydrate epitope HNK1
    • Terayama, K., Oka, S., Sejki, T., Miki, Y., Nakamura, A., Kozutsumi, Y., Takio, K., and Kawasaki, T. 1997. Cloning and functional expression of a novel glucuronosyltransferase involved in the biosynthesis of the carbohydrate epitope HNK1. Proc. Natl. Acad. Sci. 94: 6093-6098.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 6093-6098
    • Terayama, K.1    Oka, S.2    Sejki, T.3    Miki, Y.4    Nakamura, A.5    Kozutsumi, Y.6    Takio, K.7    Kawasaki, T.8
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0034723308 scopus 로고    scopus 로고
    • Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo
    • Toyoda, H., Kinoshita-Toyoda, A., and Selleck, S.B. 2000. Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo. J. Biol. Chem. 275: 2269-2275.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2269-2275
    • Toyoda, H.1    Kinoshita-Toyoda, A.2    Selleck, S.B.3
  • 41
    • 0033787822 scopus 로고    scopus 로고
    • Glycosyltransferase structure and mechanism
    • Unligil, U.M. and Rini, J.M. 2000. Glycosyltransferase structure and mechanism. Curr. Opin. Struct. Biol. 10: 510-517..
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 510-517
    • Unligil, U.M.1    Rini, J.M.2
  • 42
    • 0034675845 scopus 로고    scopus 로고
    • X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: Catalytic mechanism and a new protein superfamily
    • Unligil, U.M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H., and Rini, J.M. 2000. X-ray crystal structure of rabbit N- acetylglucosaminyltransferase I: Catalytic mechanism and a new protein superfamily. EMBO J. 19: 5269-5280.
    • (2000) EMBO J. , vol.19 , pp. 5269-5280
    • Unligil, U.M.1    Zhou, S.2    Yuwaraj, S.3    Sarkar, M.4    Schachter, H.5    Rini, J.M.6
  • 44
    • 11144240780 scopus 로고    scopus 로고
    • Stimulation of proteoglycan synthesis by glucuronosyltransferase-I gene delivery: A strategy to promote cartilage repair
    • Venkatesan, N., Barré, L., Benani, A., Netter, P., Magdalou, J., Fournel-Gigleux, S., and Ouzzine, M. 2004. Stimulation of proteoglycan synthesis by glucuronosyltransferase-I gene delivery: A strategy to promote cartilage repair. Proc. Natl. Acad. Sci. 101: 18087-18092.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 18087-18092
    • Venkatesan, N.1    Barré, L.2    Benani, A.3    Netter, P.4    Magdalou, J.5    Fournel-Gigleux, S.6    Ouzzine, M.7
  • 45
    • 0021179121 scopus 로고
    • Structural characterisation of oligosaccharides by high-performance liquid chromatography, fast-atom bombardment-mass and exoglycosidase digestion
    • Wang, W.T., Le Donne, N.C., Ackerman, B., and Sweely, C.C. 1984. Structural characterisation of oligosaccharides by high-performance liquid chromatography, fast-atom bombardment-mass and exoglycosidase digestion. Anal. Biochem. 141: 366-381.
    • (1984) Anal. Biochem. , vol.141 , pp. 366-381
    • Wang, W.T.1    Le Donne, N.C.2    Ackerman, B.3    Sweely, C.C.4
  • 46
    • 1342343091 scopus 로고    scopus 로고
    • Involvement of stromal proteoglycans in tumour progression
    • Wegrowski, Y. and Maquart, F.X. 2004. Involvement of stromal proteoglycans in tumour progression. Crit. Rev. Oncol. Hematol. 49: 259-268.
    • (2004) Crit. Rev. Oncol. Hematol. , vol.49 , pp. 259-268
    • Wegrowski, Y.1    Maquart, F.X.2
  • 47
    • 0026744148 scopus 로고
    • Cell surface heparan sulfate proteoglycans
    • Yanagishita, M. and Hascall, V.C. 1992. Cell surface heparan sulfate proteoglycans. J. Biol. Chem. 267: 9451-9454.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9451-9454
    • Yanagishita, M.1    Hascall, V.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.