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Volumn 22, Issue 5, 2012, Pages 540-549

Recent structures, evolution and mechanisms of glycosyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSAMINOGLYCAN; GLYCOSYLTRANSFERASE; N ACETYLGLUCOSAMINE; PHOSPHATIDATE PHOSPHATASE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 84867747900     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2012.06.007     Document Type: Review
Times cited : (179)

References (55)
  • 3
    • 53249091825 scopus 로고    scopus 로고
    • Glycosyltransferases, glycoside hydrolases: surprise, surprise!
    • Henrissat B., Sulzenbacher G., Bourne Y. Glycosyltransferases, glycoside hydrolases: surprise, surprise!. Curr Opin Struct Biol 2008, 18:527-533.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 527-533
    • Henrissat, B.1    Sulzenbacher, G.2    Bourne, Y.3
  • 4
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
    • Hart G.W., Slawson C., Ramirez-Correa G., Lagerlof O. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem 2011, 80:825-858.
    • (2011) Annu Rev Biochem , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 5
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 2011, 469:564-567.
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 6
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • Schwarz F., Aebi M. Mechanisms and principles of N-linked protein glycosylation. Curr Opin Struct Biol 2011, 21:576-582.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 7
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak C., Gerber S., Numao S., Aebi M., Locher K.P. X-ray structure of a bacterial oligosaccharyltransferase. Nature 2011, 474:350-355.
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 8
    • 77954080496 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin
    • Grass S., Lichti C.F., Townsend R.R., Gross J., St Geme J.W. The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin. PLoS Pathog 2010, 6:e1000919.
    • (2010) PLoS Pathog , vol.6
    • Grass, S.1    Lichti, C.F.2    Townsend, R.R.3    Gross, J.4    St Geme, J.W.5
  • 9
    • 80055095714 scopus 로고    scopus 로고
    • Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein
    • Kawai F., Grass S., Kim Y., Choi K.J., St Geme J.W., Yeo H.J. Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein. J Biol Chem 2011, 286:38546-38557.
    • (2011) J Biol Chem , vol.286 , pp. 38546-38557
    • Kawai, F.1    Grass, S.2    Kim, Y.3    Choi, K.J.4    St Geme, J.W.5    Yeo, H.J.6
  • 11
    • 80053570445 scopus 로고    scopus 로고
    • Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
    • Rana N.A., Haltiwanger R.S. Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors. Curr Opin Struct Biol 2011, 21:583-589.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 583-589
    • Rana, N.A.1    Haltiwanger, R.S.2
  • 12
    • 33646088973 scopus 로고    scopus 로고
    • Bioinformatics for comprehensive finding and analysis of glycosyltransferases
    • Kikuchi N., Narimatsu H. Bioinformatics for comprehensive finding and analysis of glycosyltransferases. Biochim Biophys Acta 2006, 1760:578-583.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 578-583
    • Kikuchi, N.1    Narimatsu, H.2
  • 13
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl J.O., Grishin N.V. Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J Mol Biol 2001, 314:365-374.
    • (2001) J Mol Biol , vol.314 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 14
    • 0038309565 scopus 로고    scopus 로고
    • Three monophyletic superfamilies account for the majority of the known glycosyltransferases
    • Liu J., Mushegian A. Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci 2003, 12:1418-1431.
    • (2003) Protein Sci , vol.12 , pp. 1418-1431
    • Liu, J.1    Mushegian, A.2
  • 15
    • 33750974777 scopus 로고    scopus 로고
    • Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4
    • Martinez-Fleites C., Proctor M., Roberts S., Bolam D.N., Gilbert H.J., Davies G.J. Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4. Chem Biol 2006, 13:1143-1152.
    • (2006) Chem Biol , vol.13 , pp. 1143-1152
    • Martinez-Fleites, C.1    Proctor, M.2    Roberts, S.3    Bolam, D.N.4    Gilbert, H.J.5    Davies, G.J.6
  • 16
    • 78049437295 scopus 로고    scopus 로고
    • Structure-based evolutionary relationship of glycosyltransferases: a case study of vertebrate β1,4-galactosyltransferase, invertebrate β1,4-N-acetylgalactosaminyltransferase and α-polypeptidyl-N-acetylgalactosaminyltransferase
    • Ramakrishnan B., Qasba P.K. Structure-based evolutionary relationship of glycosyltransferases: a case study of vertebrate β1,4-galactosyltransferase, invertebrate β1,4-N-acetylgalactosaminyltransferase and α-polypeptidyl-N-acetylgalactosaminyltransferase. Curr Opin Struct Biol 2010, 20:536-542.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 536-542
    • Ramakrishnan, B.1    Qasba, P.K.2
  • 17
    • 77953081364 scopus 로고    scopus 로고
    • Functional states of homooligomers: insights from the evolution of glycosyltransferases
    • Hashimoto K., Madej T., Bryant S.H., Panchenko A.R. Functional states of homooligomers: insights from the evolution of glycosyltransferases. J Mol Biol 2010, 399:196-206.
    • (2010) J Mol Biol , vol.399 , pp. 196-206
    • Hashimoto, K.1    Madej, T.2    Bryant, S.H.3    Panchenko, A.R.4
  • 18
    • 82555168211 scopus 로고    scopus 로고
    • Structural and mechanistic characterization of leukocyte-type core 2 β1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A glycosyltransferase
    • Pak J.E., Satkunarajah M., Seetharaman J., Rini J.M. Structural and mechanistic characterization of leukocyte-type core 2 β1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A glycosyltransferase. J Mol Biol 2011, 414:798-811.
    • (2011) J Mol Biol , vol.414 , pp. 798-811
    • Pak, J.E.1    Satkunarajah, M.2    Seetharaman, J.3    Rini, J.M.4
  • 19
    • 80053045813 scopus 로고    scopus 로고
    • Involvement of human natural killer-1 (HNK-1) sulfotransferase in the biosynthesis of the GlcUA(3-O-sulfate)-Gal-Gal-Xyl tetrasaccharide found in α-thrombomodulin from human urine
    • Hashiguchi T., Mizumoto S., Nishimura Y., Tamura J., Yamada S., Sugahara K. Involvement of human natural killer-1 (HNK-1) sulfotransferase in the biosynthesis of the GlcUA(3-O-sulfate)-Gal-Gal-Xyl tetrasaccharide found in α-thrombomodulin from human urine. J Biol Chem 2011, 286:33003-33011.
    • (2011) J Biol Chem , vol.286 , pp. 33003-33011
    • Hashiguchi, T.1    Mizumoto, S.2    Nishimura, Y.3    Tamura, J.4    Yamada, S.5    Sugahara, K.6
  • 21
    • 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., Fournel-Gigleux S. 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 2005, 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
  • 22
    • 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 L.C., Yamamoto T., Izumikawa T., Kitagawa H., Nishihara J., Tamura J., Negishi M., Sugahara K. 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 2008, 283:16801-16807.
    • (2008) J Biol Chem , vol.283 , 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
  • 23
    • 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 M.W., Ouzzine M., Fournel-Gigleux S. 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 2010, 285:37342-37358.
    • (2010) J Biol Chem , vol.285 , 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
  • 24
    • 84857936904 scopus 로고    scopus 로고
    • Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) involved in chondroitin sulfate initiation: impact of sulfation on activity and specificity
    • Gulberti S., Jacquinet J.C., Chabel M., Ramalanjaona N., Magdalou J., Netter P., Coughtrie M.W., Ouzzine M., Fournel-Gigleux S. Chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) involved in chondroitin sulfate initiation: impact of sulfation on activity and specificity. Glycobiology 2012, 22:561-571.
    • (2012) Glycobiology , vol.22 , pp. 561-571
    • Gulberti, S.1    Jacquinet, J.C.2    Chabel, M.3    Ramalanjaona, N.4    Magdalou, J.5    Netter, P.6    Coughtrie, M.W.7    Ouzzine, M.8    Fournel-Gigleux, S.9
  • 25
    • 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., Negishi M. Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. J Biol Chem 2000, 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
  • 26
    • 0012784535 scopus 로고    scopus 로고
    • Crystal structure of an α1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
    • Pedersen L.C., Dong J., Taniguchi F., Kitagawa H., Krahn J.M., Pedersen L.G., Sugahara K., Negishi M. Crystal structure of an α1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. J Biol Chem 2003, 278:14420-14428.
    • (2003) J Biol Chem , vol.278 , pp. 14420-14428
    • Pedersen, L.C.1    Dong, J.2    Taniguchi, F.3    Kitagawa, H.4    Krahn, J.M.5    Pedersen, L.G.6    Sugahara, K.7    Negishi, M.8
  • 27
    • 77952024581 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of Drosophila β1,4-Galactosyltransferase-7
    • Ramakrishnan B., Qasba P.K. Crystal structure of the catalytic domain of Drosophila β1,4-Galactosyltransferase-7. J Biol Chem 2010, 285:15619-15626.
    • (2010) J Biol Chem , vol.285 , pp. 15619-15626
    • Ramakrishnan, B.1    Qasba, P.K.2
  • 28
    • 77956937211 scopus 로고    scopus 로고
    • Molecular characterization of β1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS)
    • Bui C., Talhaoui I., Chabel M., Mulliert G., Coughtrie M.W., Ouzzine M., Fournel-Gigleux S. Molecular characterization of β1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS). FEBS Lett 2010, 584:3962-3968.
    • (2010) FEBS Lett , vol.584 , pp. 3962-3968
    • Bui, C.1    Talhaoui, I.2    Chabel, M.3    Mulliert, G.4    Coughtrie, M.W.5    Ouzzine, M.6    Fournel-Gigleux, S.7
  • 30
    • 67651027850 scopus 로고    scopus 로고
    • FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan-protein linkage region
    • Koike T., Izumikawa T., Tamura J., Kitagawa H. FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan-protein linkage region. Biochem J 2009, 421:157-162.
    • (2009) Biochem J , vol.421 , pp. 157-162
    • Koike, T.1    Izumikawa, T.2    Tamura, J.3    Kitagawa, H.4
  • 31
    • 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. Sulfation of the galactose residues in the glycosaminoglycan-protein linkage region by recombinant human chondroitin 6-O-sulfotransferase-1. J Biol Chem 2008, 283:27438-27443.
    • (2008) J Biol Chem , vol.283 , 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
  • 32
    • 80055072048 scopus 로고    scopus 로고
    • Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity
    • Chang A., Singh S., Helmich K.E., Goff R.D., Bingman C.A., Thorson J.S., Phillips G.N. Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity. Proc Natl Acad Sci USA 2011, 108:17649-17654.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 17649-17654
    • Chang, A.1    Singh, S.2    Helmich, K.E.3    Goff, R.D.4    Bingman, C.A.5    Thorson, J.S.6    Phillips, G.N.7
  • 33
    • 33845584643 scopus 로고    scopus 로고
    • A chemical rescue of α3-glactosyltransferase. Implications in the mechanism of retaining glycosyltransferases
    • Monegal A., Planas A. A chemical rescue of α3-glactosyltransferase. Implications in the mechanism of retaining glycosyltransferases. J Am Chem Soc 2006, 128:16030-16031.
    • (2006) J Am Chem Soc , vol.128 , pp. 16030-16031
    • Monegal, A.1    Planas, A.2
  • 34
    • 79953884100 scopus 로고    scopus 로고
    • Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases
    • Soya N., Fang Y., Palcic M.M., Klassen J.C. Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases. Glycobiology 2011, 21:547-552.
    • (2011) Glycobiology , vol.21 , pp. 547-552
    • Soya, N.1    Fang, Y.2    Palcic, M.M.3    Klassen, J.C.4
  • 37
    • 80855133537 scopus 로고    scopus 로고
    • The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: evidence for a short-lived oxocarbenium-like species
    • Ardèvol A., Rovira C. The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: evidence for a short-lived oxocarbenium-like species. Angew Chem Intl Ed Engl 2011, 50:10897-10901.
    • (2011) Angew Chem Intl Ed Engl , vol.50 , pp. 10897-10901
    • Ardèvol, A.1    Rovira, C.2
  • 38
    • 11844280851 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in glycosyltransferases
    • Qasba P.K., Ramakrishnan B., Boeggeman E. Substrate-induced conformational changes in glycosyltransferases. Trends Biochem Sci 2005, 30:53-62.
    • (2005) Trends Biochem Sci , vol.30 , pp. 53-62
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 39
    • 77951298440 scopus 로고    scopus 로고
    • Structural and mechanistic implications for a new mode of glycosyltransferase inhibition
    • Pesnot T., Jorgensen R., Palcic M.M., Wagner G.K. Structural and mechanistic implications for a new mode of glycosyltransferase inhibition. Nat Chem Biol 2010, 6:321-323.
    • (2010) Nat Chem Biol , vol.6 , pp. 321-323
    • Pesnot, T.1    Jorgensen, R.2    Palcic, M.M.3    Wagner, G.K.4
  • 41
    • 77952396239 scopus 로고    scopus 로고
    • UDP-(5F)GlcNAc acts as a slow-binding inhibitor of MshA, a retaining glycosyltransferase
    • Frantom P.A., Coward J.K., Blanchard J.S. UDP-(5F)GlcNAc acts as a slow-binding inhibitor of MshA, a retaining glycosyltransferase. J Am Chem Soc 2010, 132:6626-6627.
    • (2010) J Am Chem Soc , vol.132 , pp. 6626-6627
    • Frantom, P.A.1    Coward, J.K.2    Blanchard, J.S.3
  • 42
    • 84856574217 scopus 로고    scopus 로고
    • A new concept for glycosyltransferase inhibitors: nonionic mimics of the nucleotide donor of the human blood group B galactosyltransferase
    • Schaefer K., Albers J., Sindhuwinata N., Peters T., Meyer B. A new concept for glycosyltransferase inhibitors: nonionic mimics of the nucleotide donor of the human blood group B galactosyltransferase. ChemBioChem 2012, 13:443-450.
    • (2012) ChemBioChem , vol.13 , pp. 443-450
    • Schaefer, K.1    Albers, J.2    Sindhuwinata, N.3    Peters, T.4    Meyer, B.5
  • 43
    • 84855309983 scopus 로고    scopus 로고
    • The inhibition of lipooligosaccharide heptosyltransferase WaaC with multivalent glycosylated fullerenes: a new mode of glycosyltransferase inhibition
    • Durka M., Buffet K., Iehl J., Holler M., Nierengarten J.F., Vincent S.P. The inhibition of lipooligosaccharide heptosyltransferase WaaC with multivalent glycosylated fullerenes: a new mode of glycosyltransferase inhibition. Chem Eur J 2012, 18:641-651.
    • (2012) Chem Eur J , vol.18 , pp. 641-651
    • Durka, M.1    Buffet, K.2    Iehl, J.3    Holler, M.4    Nierengarten, J.F.5    Vincent, S.P.6
  • 44
    • 0013624871 scopus 로고
    • Stimulation of synthesis of free chondroitin sulfate chains by β-d-xylosides in cultured cells
    • Schwartz N.B., Galligani L., Ho P.L., Dorfman A. Stimulation of synthesis of free chondroitin sulfate chains by β-d-xylosides in cultured cells. Proc Natl Acad Sci USA 1974, 71:4047-4051.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4047-4051
    • Schwartz, N.B.1    Galligani, L.2    Ho, P.L.3    Dorfman, A.4
  • 45
    • 2142854239 scopus 로고
    • Animal cell mutants defective in glycosaminoglycan biosynthesis
    • Esko J.D., Stewart T.E., Taylor W.H. Animal cell mutants defective in glycosaminoglycan biosynthesis. Proc Natl Acad Sci USA 1985, 82:3197-31201.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3197-31201
    • Esko, J.D.1    Stewart, T.E.2    Taylor, W.H.3
  • 46
    • 78449293027 scopus 로고    scopus 로고
    • 4-Deoxy-4-fluoro-xyloside derivatives as inhibitors of glycosaminoglycan biosynthesis
    • Tsuzuki Y., Nguyen T.K., Garud D.R., Kuberan B., Koketsu M. 4-Deoxy-4-fluoro-xyloside derivatives as inhibitors of glycosaminoglycan biosynthesis. Bioorg Med Chem Lett 2010, 20:7269-7273.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 7269-7273
    • Tsuzuki, Y.1    Nguyen, T.K.2    Garud, D.R.3    Kuberan, B.4    Koketsu, M.5
  • 47
    • 79952689995 scopus 로고    scopus 로고
    • Synthesis and evaluation of xylopyranoside derivatives as "decoy acceptors" of human β-1,4-galactosyltransferase 7
    • García-García J.F., Corrales G., Casas J., Fernández-Mayoralas A., García-Junceda E. Synthesis and evaluation of xylopyranoside derivatives as "decoy acceptors" of human β-1,4-galactosyltransferase 7. Mol Biosyst 2011, 7:1312-1321.
    • (2011) Mol Biosyst , vol.7 , pp. 1312-1321
    • García-García, J.F.1    Corrales, G.2    Casas, J.3    Fernández-Mayoralas, A.4    García-Junceda, E.5
  • 48
    • 77951741986 scopus 로고    scopus 로고
    • Attenuation of tumor growth by formation of antiproliferative glycosaminoglycans correlates with low acetylation of histone H3
    • Nilsson U., Johnsson R., Fransson L.A., Ellervik U., Mani K. Attenuation of tumor growth by formation of antiproliferative glycosaminoglycans correlates with low acetylation of histone H3. Cancer Res 2010, 70:3771-3779.
    • (2010) Cancer Res , vol.70 , pp. 3771-3779
    • Nilsson, U.1    Johnsson, R.2    Fransson, L.A.3    Ellervik, U.4    Mani, K.5
  • 49
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • Bennett-Lovsey R.M., Herbert A.D., Sternberg M.J., Kelley L.A. Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 2008, 70:611-625.
    • (2008) Proteins , vol.70 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.3    Kelley, L.A.4
  • 53
    • 33646828699 scopus 로고    scopus 로고
    • Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2
    • Fritz T.A., Raman J., Tabak L.A. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2. J Biol Chem 2006, 281:8613-8619.
    • (2006) J Biol Chem , vol.281 , pp. 8613-8619
    • Fritz, T.A.1    Raman, J.2    Tabak, L.A.3
  • 54
    • 34250829050 scopus 로고    scopus 로고
    • Structural analysis of the α-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms
    • Chiu C.P., Lairson L.L., Gilbert M., Wakarchuk W.W., Withers S.G., Strynadka N.C. Structural analysis of the α-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms. Biochemistry 2007, 46:7196-7204.
    • (2007) Biochemistry , vol.46 , pp. 7196-7204
    • Chiu, C.P.1    Lairson, L.L.2    Gilbert, M.3    Wakarchuk, W.W.4    Withers, S.G.5    Strynadka, N.C.6
  • 55
    • 34447305187 scopus 로고    scopus 로고
    • Catalytic domains of glycosyltransferases with 'add-on' domains
    • Qasba P.K., Ramakrishnan B. Catalytic domains of glycosyltransferases with 'add-on' domains. Glycobiology 2007, 17:7G-9G.
    • (2007) Glycobiology , vol.17
    • Qasba, P.K.1    Ramakrishnan, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.