메뉴 건너뛰기




Volumn 44, Issue 47, 2005, Pages 15619-15635

Analysis of the specificity of sialy1transferases toward mucin core 2, globo, and related structures. Identification of the sialylation sequence and the effects of sulfate, fucose, methyl, and fluoro substituents of the carbohydrate chain in the biosynthesis of selectin and siglec ligands, and novel sialylation by cloned α2,3(O)sialyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CHROMATOGRAPHY; CLONING; MASS SPECTROMETRY; TUMORS;

EID: 28244486825     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050246m     Document Type: Article
Times cited : (28)

References (62)
  • 1
    • 0026541128 scopus 로고
    • Diversity in the sialic acids
    • Varki, A. (1992) Diversity in the sialic acids, Glycobiology 2, 25-40.
    • (1992) Glycobiology , vol.2 , pp. 25-40
    • Varki, A.1
  • 2
    • 0030792933 scopus 로고    scopus 로고
    • Sialic acids in molecular and cellular interactions
    • Keim, S., and Schauer, R. (1997) Sialic acids in molecular and cellular interactions, Int. Rev. Cytol. 175, 137-240.
    • (1997) Int. Rev. Cytol. , vol.175 , pp. 137-240
    • Keim, S.1    Schauer, R.2
  • 3
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki, A. (1997) Sialic acids as ligands in recognition phenomena, FASEB J. 11, 248-255.
    • (1997) FASEB J. , vol.11 , pp. 248-255
    • Varki, A.1
  • 4
    • 0031872407 scopus 로고    scopus 로고
    • Meaning and therapeutic potential of microbial recognition of host glycoconjugates
    • Karlsson, K. A. (1998) Meaning and therapeutic potential of microbial recognition of host glycoconjugates, Mol. Microbiol. 29, 1-11.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1-11
    • Karlsson, K.A.1
  • 6
    • 0029054907 scopus 로고
    • I-type lectins
    • Powell, L. D., and Varki, A. (1995) I-type lectins, J. Biol. Chem. 270, 14243-14246.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14243-14246
    • Powell, L.D.1    Varki, A.2
  • 7
    • 0029731590 scopus 로고    scopus 로고
    • The sialoadhesins: A family of sialic acid-dependent cellular recognition molecules within the immunoglobulin superfamily
    • Kelm, S., Schauer, R., and Crocker, P. R. (1996) The sialoadhesins: A family of sialic acid-dependent cellular recognition molecules within the immunoglobulin superfamily, Glycoconjugate J. 13, 913-926.
    • (1996) Glycoconjugate J. , vol.13 , pp. 913-926
    • Kelm, S.1    Schauer, R.2    Crocker, P.R.3
  • 8
    • 0027511875 scopus 로고
    • Natural ligands of the B-cell adhesion molecule CD22-β carry N-linked oligosaccharides with α-2,6-linked sialic acids that are required for recognition
    • Powell, L. D., Sgroi, D., Sjoberg, E. R., Stamenkovic, I., and Varki, A. (1993) Natural ligands of the B-cell adhesion molecule CD22-β carry N-linked oligosaccharides with α-2,6-linked sialic acids that are required for recognition, J. Biol. Chem. 268, 7019-7027.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7019-7027
    • Powell, L.D.1    Sgroi, D.2    Sjoberg, E.R.3    Stamenkovic, I.4    Varki, A.5
  • 10
    • 0034124378 scopus 로고    scopus 로고
    • Siglec-7: A sialic acid-binding lectin of the immunoglobulin superfamily
    • Angata, T., and Varki, A. (2000) Siglec-7: A sialic acid-binding lectin of the immunoglobulin superfamily, Glycobiology 10, 431-438.
    • (2000) Glycobiology , vol.10 , pp. 431-438
    • Angata, T.1    Varki, A.2
  • 11
    • 0345129981 scopus 로고    scopus 로고
    • Cell surface sialic acid and the regulation of immune cell interactions: The neuraminidase effect reconsidered
    • Bagriacik, E. U., and Miller, K. S. (1999) Cell surface sialic acid and the regulation of immune cell interactions: The neuraminidase effect reconsidered, Glycobiology 9, 267-275.
    • (1999) Glycobiology , vol.9 , pp. 267-275
    • Bagriacik, E.U.1    Miller, K.S.2
  • 14
    • 0029001510 scopus 로고
    • Selectin-carbohydrate interactions and the initiation of the inflammatory response
    • Lasky, L. A. (1995) Selectin-carbohydrate interactions and the initiation of the inflammatory response, Annu. Rev. Biochem. 64, 113-139.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 113-139
    • Lasky, L.A.1
  • 18
    • 0025666651 scopus 로고
    • Carbohydrate ligands of the lee cell-adhesion molecules
    • Brandley, B. K., Swiedler, S. J., and Robbins, P. W. (1990) Carbohydrate ligands of the lee cell-adhesion molecules, Cell 63, 861-863.
    • (1990) Cell , vol.63 , pp. 861-863
    • Brandley, B.K.1    Swiedler, S.J.2    Robbins, P.W.3
  • 19
    • 0031052021 scopus 로고    scopus 로고
    • Selectin inhibition: Synthesis and evaluation of novel sialylated, sulfated and fucosylated oligosaccharides, including the major capping group of GlyCAM-1
    • Koenig, A., Jain, R., Vig, R., Norgard-Sumnicht, K. E., Matta, K. L., and Varki, A. (1997) Selectin inhibition: Synthesis and evaluation of novel sialylated, sulfated and fucosylated oligosaccharides, including the major capping group of GlyCAM-1, Glycobiology 7, 79-93.
    • (1997) Glycobiology , vol.7 , pp. 79-93
    • Koenig, A.1    Jain, R.2    Vig, R.3    Norgard-Sumnicht, K.E.4    Matta, K.L.5    Varki, A.6
  • 20
    • 0031876395 scopus 로고    scopus 로고
    • Inhibition of L- and P-selectin by a rationally synthesized novel core 2-like branched structure containing GalNAc-Lewis(X) and Neu5Ac α2-3Galβ1-3GalNAc sequences
    • Jain, R. K., Piskorz, C. F., Huang, B.-G., Locke, R. D., Han, H,-L., Koenig, A., Varki, A., and Matta, K. L. (1998) Inhibition of L- and P-selectin by a rationally synthesized novel core 2-like branched structure containing GalNAc-Lewis(X) and Neu5Ac α2-3Galβ1-3GalNAc sequences, Glycobiology 8, 707-717.
    • (1998) Glycobiology , vol.8 , pp. 707-717
    • Jain, R.K.1    Piskorz, C.F.2    Huang, B.-G.3    Locke, R.D.4    Han, H.-L.5    Koenig, A.6    Varki, A.7    Matta, K.L.8
  • 21
    • 0028925953 scopus 로고
    • Selectin ligands and tumor-associated carbohydrate structures: Specificities of α-2,3-sialyltransferases in the assembly of 3′-sialyl-6-sulfo/sialyl lewis-a and lewis-x, 3′-sialyl-6′- sulfo lewis-x, and 3′-sialyl-6-sialyl/sulfo blood-group T-hapten
    • Chandrasekaran, E. V., Jain, R. K., Larsen, R. D., Wlasichuk, K., and Matta, K. L. (1995) Selectin ligands and tumor-associated carbohydrate structures: Specificities of α-2,3-sialyltransferases in the assembly of 3′-sialyl-6-sulfo/sialyl lewis-a and lewis-x, 3′-sialyl-6′- sulfo lewis-x, and 3′-sialyl-6-sialyl/sulfo blood-group T-hapten, Biochemistry 34, 2925-2936.
    • (1995) Biochemistry , vol.34 , pp. 2925-2936
    • Chandrasekaran, E.V.1    Jain, R.K.2    Larsen, R.D.3    Wlasichuk, K.4    Matta, K.L.5
  • 22
    • 0027911180 scopus 로고
    • A convenient synthesis of n-acetyllactosamine-linked oligosaccharides from phenyl 3,6,2′,3′,4′,6′-hexa-o-acetyl-2-deoxy-2- phthalimido-1-thio-β-lactopyranoside
    • Jain, R. K., Piskorz, C. F., and Matta, K. L. (1993) A convenient synthesis of n-acetyllactosamine-linked oligosaccharides from phenyl 3,6,2′,3′,4′,6′-hexa-o-acetyl-2-deoxy-2-phthalimido-1- thio-β-lactopyranoside, Carbohydr. Res. 243, 385-391.
    • (1993) Carbohydr. Res. , vol.243 , pp. 385-391
    • Jain, R.K.1    Piskorz, C.F.2    Matta, K.L.3
  • 23
    • 0030026075 scopus 로고    scopus 로고
    • Chemical synthesis of a hexasaccharide comprising the Lewis(x) determinant linked β-(1→6) to a linear trimannosyl core and the precursor pentasaccharide lacking fucose
    • Jain, R. K., and Matta, K. L. (1996) Chemical synthesis of a hexasaccharide comprising the Lewis(x) determinant linked β-(1→6) to a linear trimannosyl core and the precursor pentasaccharide lacking fucose, Carbohydr. Res. 282, 101 -111.
    • (1996) Carbohydr. Res. , vol.282 , pp. 101-111
    • Jain, R.K.1    Matta, K.L.2
  • 24
    • 0032462506 scopus 로고    scopus 로고
    • Synthesis of Gal-β-(1→4)-GlcNAc-β-(1→6)-[Gal-β- (1→3)]-GalNAc-α-OBn oligosaccharides bearing O-methyl or O-sulfo groups at C-3 of the Gal residue: Specific acceptors for Gal:3-O- sulfotransferases
    • Jain, R. K., Piskorz, C. F., Chandrasekaran, E. V., and Matta, K. L. (1998) Synthesis of Gal-β-(1→4)-GlcNAc-β-(1→6)-[Gal-β- (1→3)]-GalNAc-α-OBn oligosaccharides bearing O-methyl or O-sulfo groups at C-3 of the Gal residue: Specific acceptors for Gal:3-O- sulfotransferases, Glycoconjugate J. 15, 951-959.
    • (1998) Glycoconjugate J. , vol.15 , pp. 951-959
    • Jain, R.K.1    Piskorz, C.F.2    Chandrasekaran, E.V.3    Matta, K.L.4
  • 25
    • 0037765605 scopus 로고    scopus 로고
    • Synthesis of fluorine-containing core-2 tetrasaccharides
    • Xia, J., Alderfer, J. L., Piskorz, C. F., Locke, R. D., and Matta, K. L. (2003) Synthesis of fluorine-containing core-2 tetrasaccharides, Synlett 9, 1291-1294.
    • (2003) Synlett , vol.9 , pp. 1291-1294
    • Xia, J.1    Alderfer, J.L.2    Piskorz, C.F.3    Locke, R.D.4    Matta, K.L.5
  • 26
    • 0017918339 scopus 로고
    • Studies on lectins. 35. Water-soluble o-glycosyl polyacrylamide derivatives for specific precipitation of lectins
    • Horejsi, V., Smolek, P., and Kocurek, J. (1978) Studies on lectins. 35. Water-soluble o-glycosyl polyacrylamide derivatives for specific precipitation of lectins, Biochim. Biophys. Acta 538, 293-298.
    • (1978) Biochim. Biophys. Acta , vol.538 , pp. 293-298
    • Horejsi, V.1    Smolek, P.2    Kocurek, J.3
  • 27
    • 0028279682 scopus 로고
    • Lactose as affinity eluant and a synthetic sulfated copolymer as inhibitor, in conjunction with synthetic and natural acceptors, differentiate human-milk lewis-type and plasma-type α-1-fucosyltransferases
    • Chandrasekaran, E. V., Rhodes, J. M., Jain, R. K., and Matta, K. L. (1994) Lactose as affinity eluant and a synthetic sulfated copolymer as inhibitor, in conjunction with synthetic and natural acceptors, differentiate human-milk lewis-type and plasma-type α-1-fucosyltransferases, Biochem. Biophys. Res. Commun. 198, 350-358.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 350-358
    • Chandrasekaran, E.V.1    Rhodes, J.M.2    Jain, R.K.3    Matta, K.L.4
  • 28
    • 0028358742 scopus 로고
    • A biosynthetic control on structures serving as ligands for selectins: The precursor structures, 3-sialyl/sulfo Gal-β-1,3/4GlcNAc-β-OR, which are high-affinity substrates for α-1,3/4-L-fucosyl-transferases, exhibit the phenomenon of substrate inhibition
    • Chandrasekaran, E. V., Rhodes, J. M., Jain, R. K., Bernacki, R. J., and Matta, K. L. (1994) A biosynthetic control on structures serving as ligands for selectins: The precursor structures, 3-sialyl/sulfo Gal-β-1,3/4GlcNAc- β-OR, which are high-affinity substrates for α-1,3/4-L-fucosyl- transferases, exhibit the phenomenon of substrate inhibition, Biochem. Biophys. Res. Commun. 201, 78-89.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 78-89
    • Chandrasekaran, E.V.1    Rhodes, J.M.2    Jain, R.K.3    Bernacki, R.J.4    Matta, K.L.5
  • 29
    • 0028965660 scopus 로고
    • Expression of blood-group Lewis-b determinant from Lewis-a: Association of this novel α-(1,2)-L-fucosylating activity with the Lewis type α(1,3/4)-L-fucosyl-transferase
    • Chandrasekaran, E. V., Jain, R. K., Rhodes, J. M., Srnka, C. A., Larsen, R. D., and Matta, K. L. (1995) Expression of blood-group Lewis-b determinant from Lewis-a: Association of this novel α-(1,2)-L-fucosylating activity with the Lewis type α(1,3/4)-L-fucosyl-transferase Biochemistry 34, 4748-4756.
    • (1995) Biochemistry , vol.34 , pp. 4748-4756
    • Chandrasekaran, E.V.1    Jain, R.K.2    Rhodes, J.M.3    Srnka, C.A.4    Larsen, R.D.5    Matta, K.L.6
  • 30
    • 0023946335 scopus 로고
    • The use of hydrophobic synthetic glycosides as acceptors in glycosyltransferase assays
    • Palcic, M. M., Heerze, L. D., Pierce, M., and Hindsgaul, O. (1988) The use of hydrophobic synthetic glycosides as acceptors in glycosyltransferase assays, Glycoconjugate J. 5, 49-63.
    • (1988) Glycoconjugate J. , vol.5 , pp. 49-63
    • Palcic, M.M.1    Heerze, L.D.2    Pierce, M.3    Hindsgaul, O.4
  • 31
    • 4043100373 scopus 로고    scopus 로고
    • Determination of linkage position and anomeric configuration in Hex-Fuc disaccharides using electrospray ionization tandem mass spectrometry
    • Xue, J., Song, L., Khaja, D. S., Locke, D. R., West, C. M., Laine, R. A., and Matta, K. L. (2004) Determination of linkage position and anomeric configuration in Hex-Fuc disaccharides using electrospray ionization tandem mass spectrometry, Rapid Commun. Mass Spectrom. 18, 1947-1955.
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 1947-1955
    • Xue, J.1    Song, L.2    Khaja, D.S.3    Locke, D.R.4    West, C.M.5    Laine, R.A.6    Matta, K.L.7
  • 32
    • 0037131166 scopus 로고    scopus 로고
    • Gycosulfopeptides with O-glycans containing sialylated and polyfucosylated polylactosamine bind with low affinity to P-selectin
    • Leppanen, A., Penttila, L., Renkonen, O., McEver, R. P., and Cummings, R. D. (2002) Gycosulfopeptides with O-glycans containing sialylated and polyfucosylated polylactosamine bind with low affinity to P-selectin, J. Biol. Chem. 277, 39749-39759.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39749-39759
    • Leppanen, A.1    Penttila, L.2    Renkonen, O.3    McEver, R.P.4    Cummings, R.D.5
  • 33
    • 0029763034 scopus 로고    scopus 로고
    • Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells
    • Wilkins, P. P., McEver, R. P., and Cummings, R. D. (1996) Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells, J. Biol. Chem. 271, 18732-18742.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18732-18742
    • Wilkins, P.P.1    McEver, R.P.2    Cummings, R.D.3
  • 34
    • 0032512835 scopus 로고    scopus 로고
    • Complementary acceptor and site specificities of Fuc-TIV and Fuc-TVII allow effective biosynthesis of sialyl-TriLex and related polylactosamines present on glycoprotein counterreceptors of selectins
    • Niemela, R., Natunen, J., Majuri, M. L., Maaheimo, H., Helin, J., Lowe, J. B., Renkonen, O., and Renkonen, R. (1998) Complementary acceptor and site specificities of Fuc-TIV and Fuc-TVII allow effective biosynthesis of sialyl-TriLex and related polylactosamines present on glycoprotein counterreceptors of selectins, J. Biol. Chem. 273, 4021-4026.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4021-4026
    • Niemela, R.1    Natunen, J.2    Majuri, M.L.3    Maaheimo, H.4    Helin, J.5    Lowe, J.B.6    Renkonen, O.7    Renkonen, R.8
  • 36
    • 0031559820 scopus 로고    scopus 로고
    • Fucosylation of complex glycosphingolipids by recombinant fucosyltransferase-VII
    • Stroud, M. R., and Holmes, E. H. (1997) Fucosylation of complex glycosphingolipids by recombinant fucosyltransferase-VII, Biochem. Bioplys. Res. Commun. 238, 165-168.
    • (1997) Biochem. Bioplys. Res. Commun. , vol.238 , pp. 165-168
    • Stroud, M.R.1    Holmes, E.H.2
  • 37
    • 0034599364 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of sialyl-trimeric-Lewis x
    • Koeller, K. M., and Wong, C. H. (2000) Chemoenzymatic synthesis of sialyl-trimeric-Lewis x, Chem.-Eur. J. 6, 1243-1251.
    • (2000) Chem.-Eur. J. , vol.6 , pp. 1243-1251
    • Koeller, K.M.1    Wong, C.H.2
  • 38
    • 0030691076 scopus 로고    scopus 로고
    • Characterization of an N-acetylglucosamine-6-O-sulfotransferase from human respiratory mucosa active on mucin carbohydrate chains
    • Degroote, S., Lo-Guidice, J. M., Strecker, G., Ducourouble, M. P., Roussel, P., and Lamblin, G. (1997) Characterization of an N-acetylglucosamine- 6-O-sulfotransferase from human respiratory mucosa active on mucin carbohydrate chains. J. Biol. Chem. 272, 29493-29501.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29493-29501
    • Degroote, S.1    Lo-Guidice, J.M.2    Strecker, G.3    Ducourouble, M.P.4    Roussel, P.5    Lamblin, G.6
  • 39
    • 0029831271 scopus 로고    scopus 로고
    • Characterization of a rat liver Golgi sulphotransferase responsible for the 6-O-sulphation of N-acetylglucosamine residues in β-linkage to mannose: Role in assembly of sialyl-galactosyl-N-acetylglucosamine 6-sulphate sequence of N-linked oligosaccharides
    • Spiro, R. G., Yashimoto, Y., and Bhoyroo, V. (1996) Characterization of a rat liver Golgi sulphotransferase responsible for the 6-O-sulphation of N-acetylglucosamine residues in β-linkage to mannose: Role in assembly of sialyl-galactosyl-N-acetylglucosamine 6-sulphate sequence of N-linked oligosaccharides, Biochem. J. 319, 209-216.
    • (1996) Biochem. J. , vol.319 , pp. 209-216
    • Spiro, R.G.1    Yashimoto, Y.2    Bhoyroo, V.3
  • 40
    • 0033497820 scopus 로고    scopus 로고
    • Characterization of distinct Gal:3-O-sulfotransferase activities in human tumor epithelial cell lines and of calf lymph node GlcNAc:6-O-sulfotransferase activity
    • Chandrasekaran, E. V, Jain, R. K., Rhodes, J. M., Chawda, R., Piskorz, C., and Matta, K. L. (1999) Characterization of distinct Gal:3-O- sulfotransferase activities in human tumor epithelial cell lines and of calf lymph node GlcNAc:6-O-sulfotransferase activity, Glycoconjugate J. 16, 523-536.
    • (1999) Glycoconjugate J. , vol.16 , pp. 523-536
    • Chandrasekaran, E.V.1    Jain, R.K.2    Rhodes, J.M.3    Chawda, R.4    Piskorz, C.5    Matta, K.L.6
  • 41
    • 0030015609 scopus 로고    scopus 로고
    • Specificity analysis of three clonal and five non-clonal α1,3-L-fucosyltransferases with sulfated, sialylated, pr fucosylated synthetic carbohydrates as acceptors in relation to the assembly of 3′-sialyl-6′-sulfo Lewis x (the L-selectin ligand) and related complex structures
    • Chandrasekaran, E. V., Jain, R. K., Larsen, R. D., Wlasichuk, K., DiCioccio, R. A., and Matta, K. L. (1996) Specificity analysis of three clonal and five non-clonal α1,3-L-fucosyltransferases with sulfated, sialylated, pr fucosylated synthetic carbohydrates as acceptors in relation to the assembly of 3′-sialyl-6′-sulfo Lewis x (the L-selectin ligand) and related complex structures, Biochemistry 35, 8925-8933
    • (1996) Biochemistry , vol.35 , pp. 8925-8933
    • Chandrasekaran, E.V.1    Jain, R.K.2    Larsen, R.D.3    Wlasichuk, K.4    Dicioccio, R.A.5    Matta, K.L.6
  • 42
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB MS/MS spectra of glycoconjugates
    • Domon, B., and Costello, C. E. (1988) A systematic nomenclature for carbohydrate fragmentations in FAB MS/MS spectra of glycoconjugates, Glycoconjugate J. 5, 397-409.
    • (1988) Glycoconjugate J. , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 43
    • 0037258065 scopus 로고    scopus 로고
    • Comparison between electrochemistry/mass spectrometry and cytochrome P450 catalyzed oxidation reactions
    • Jurva, U., Wikström, H. V., Weidolf, L., and Bruins, A. P. (2003) Comparison between electrochemistry/mass spectrometry and cytochrome P450 catalyzed oxidation reactions, Rapid Commun. Mass Spectrom. 17, 800-810.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 800-810
    • Jurva, U.1    Wikström, H.V.2    Weidolf, L.3    Bruins, A.P.4
  • 44
    • 0141643399 scopus 로고    scopus 로고
    • Solid-phase synthesis of core 2 O-linked glycopeptide and its enzymatic sialylation
    • Takano, Y., Kojima, N., Nakahara, Y., Hojo, H., and Nakahara, Y. (2003) Solid-phase synthesis of core 2 O-linked glycopeptide and its enzymatic sialylation, Tetrahedron 59, 8415-8427.
    • (2003) Tetrahedron , vol.59 , pp. 8415-8427
    • Takano, Y.1    Kojima, N.2    Nakahara, Y.3    Hojo, H.4    Nakahara, Y.5
  • 45
    • 0037967958 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of siaiylated oligosaccharides for their evaluation in a polysialyltransferase assay
    • Sengupta, P., Misa, A. K., Suzuki, M., Fukuda, M., and Hindsgual, O. (2003) Chemoenzymatic synthesis of siaiylated oligosaccharides for their evaluation in a polysialyltransferase assay. Tetrahedron Lett. 44, 6037-6042.
    • (2003) Tetrahedron Lett. , vol.44 , pp. 6037-6042
    • Sengupta, P.1    Misa, A.K.2    Suzuki, M.3    Fukuda, M.4    Hindsgual, O.5
  • 46
    • 0018787254 scopus 로고
    • Sugar chains of cold-insoluble globulin: Protein related to fibronectin
    • Takasaki, S., Yamashita, K., Suzuki, K., Iwanaga, S., and Kobata, A. (1979) Sugar chains of cold-insoluble globulin: Protein related to fibronectin, J. Biol. Chem. 254, 8548-8553.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8548-8553
    • Takasaki, S.1    Yamashita, K.2    Suzuki, K.3    Iwanaga, S.4    Kobata, A.5
  • 47
    • 0028761759 scopus 로고
    • A novel mono-sulfated pentaglycosylceramide with the isoglobo-series core structure in rat kidney
    • Tadano-Aritomi, K., Okuda, M., Ishizuka, I., Kubo, H., and Ireland, P. (1994) A novel mono-sulfated pentaglycosylceramide with the isoglobo-series core structure in rat kidney, Carbohydr. Res. 265, 49-59.
    • (1994) Carbohydr. Res. , vol.265 , pp. 49-59
    • Tadano-Aritomi, K.1    Okuda, M.2    Ishizuka, I.3    Kubo, H.4    Ireland, P.5
  • 49
    • 0042232205 scopus 로고    scopus 로고
    • Sialoside specificity of the siglec family assessed using novel multivalent probes: Identification of potent inhibitors of myelin-associated glycoprotein
    • Blixt, O., Collins, B. E., van den Nieuwenhof, I. M., Crocker, P. R., and Paulson, J. C. (2003) Sialoside specificity of the siglec family assessed using novel multivalent probes: Identification of potent inhibitors of myelin-associated glycoprotein, J. Biol. Chem. 278, 31007-31019.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31007-31019
    • Blixt, O.1    Collins, B.E.2    Van Den Nieuwenhof, I.M.3    Crocker, P.R.4    Paulson, J.C.5
  • 51
    • 0036262863 scopus 로고    scopus 로고
    • Biosynthesis of the carbohydrate antigenic determinants, Globo H, blood group H, and Lewis b: A role for prostate cancer cell α1,2-L- fucosyltransferase
    • Chandrasekaran, E. V., Chawda, R., Locke, R. D., Piskorz, C. F., and Matta, K. L. (2002) Biosynthesis of the carbohydrate antigenic determinants, Globo H, blood group H, and Lewis b: A role for prostate cancer cell α1,2-L-fucosyltransferase, Glycobiology 12, 153-162.
    • (2002) Glycobiology , vol.12 , pp. 153-162
    • Chandrasekaran, E.V.1    Chawda, R.2    Locke, R.D.3    Piskorz, C.F.4    Matta, K.L.5
  • 52
    • 1642396332 scopus 로고    scopus 로고
    • Identification of physiologically relevant substrates for cloned Gal:3-O-sulfotransferases (GalSSTs): Distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the Globo H backbone, Gal3ST-3 for N-glycan multiterminalGalβ1,4GlcNAc β units and 6-sulfoGalβ1,-4GlcNAc β, and Gal3ST-4 for the mucin core-2 trisaccharide
    • Chandrasekaran, E. V., Lakhaman, S. L., Chawda, R., Piskorz, C. F., Neelamegham, S., and Matta, K. L. (2004) Identification of physiologically relevant substrates for cloned Gal:3-O-sulfotransferases (GalSSTs): Distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the Globo H backbone, Gal3ST-3 for N-glycan multiterminalGalβ1,4GlcNAc β units and 6-sulfoGalβ1,-4GlcNAc β, and Gal3ST-4 for the mucin core-2 trisaccharide, J. Biol. Chem. 279, 10032-10041.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10032-10041
    • Chandrasekaran, E.V.1    Lakhaman, S.L.2    Chawda, R.3    Piskorz, C.F.4    Neelamegham, S.5    Matta, K.L.6
  • 53
    • 0027467841 scopus 로고
    • A conserved disulfide bond in sialyltransferases
    • Drickamer, K. (1993) A conserved disulfide bond in sialyltransferases, Glycobiology 3, 2-3.
    • (1993) Glycobiology , vol.3 , pp. 2-3
    • Drickamer, K.1
  • 55
    • 0031086055 scopus 로고    scopus 로고
    • Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: Implications for their mechanism of action
    • Geremia, R. A., Harduin-Lepers, A., and Delannoy, P. (1997) Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: Implications for their mechanism of action, Glycobiology 7, v-vii.
    • (1997) Glycobiology , vol.7
    • Geremia, R.A.1    Harduin-Lepers, A.2    Delannoy, P.3
  • 56
    • 0028985664 scopus 로고
    • The sialyltransferase sialyl motif participates in binding the donor substrate CMP-NeuAc
    • Datta, A. K., and Paulson, J. D. (1995) The sialyltransferase sialyl motif participates in binding the donor substrate CMP-NeuAc, J. Biol. Chem. 270, 1497-1500.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1497-1500
    • Datta, A.K.1    Paulson, J.D.2
  • 57
    • 0032540299 scopus 로고    scopus 로고
    • Mutation of the sialyltransferase S-sialyl motif alters the kinetics of the donor and acceptor substrates
    • Datta, A. K., Shinha, A., and Paulson, J. C. (1998) Mutation of the sialyltransferase S-sialyl motif alters the kinetics of the donor and acceptor substrates, J. Biol. Chem. 273, 9608-9614.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9608-9614
    • Datta, A.K.1    Shinha, A.2    Paulson, J.C.3
  • 58
    • 0035844295 scopus 로고    scopus 로고
    • Differential biosynthesis of polysialic or disialic acid structure by STSSia II and STSSia IV
    • Kitazume-Kawaguchi, S., Kabata, S., and Arita, M. (2001) Differential biosynthesis of polysialic or disialic acid structure by STSSia II and STSSia IV, J. Biol. Chem. 276, 15696-15703.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15696-15703
    • Kitazume-Kawaguchi, S.1    Kabata, S.2    Arita, M.3
  • 59
    • 0029043212 scopus 로고
    • Three genes that encode human β-galactoside α-2,3- sialyltransferases: Structural analysis and chromosomal mapping studies
    • Chang. M.-L., Eddy, R. L., Shows, T. B., and Lau, J. T. Y. (1995) Three genes that encode human β-galactoside α-2,3-sialyltransferases: Structural analysis and chromosomal mapping studies, Glycobiology 5, 319-325.
    • (1995) Glycobiology , vol.5 , pp. 319-325
    • Chang, M.-L.1    Eddy, R.L.2    Shows, T.B.3    Lau, J.T.Y.4
  • 60
    • 0024364391 scopus 로고
    • Tissue-specific expression of sialyltransferases
    • Paulson, J. C., Weinstein, J., and Schauer, A. (1989) Tissue-specific expression of sialyltransferases, J. Biol. Chem. 264,10931-10934.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10931-10934
    • Paulson, J.C.1    Weinstein, J.2    Schauer, A.3
  • 61
    • 0028291625 scopus 로고
    • Differential expression of 5 sialyltransferase genes in human tissues
    • Kitagawa, H., and Paulson, J. C. (1994) Differential expression of 5 sialyltransferase genes in human tissues, J. Biol. Chem. 269. 17872-17878.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17872-17878
    • Kitagawa, H.1    Paulson, J.C.2
  • 62
    • 0037031849 scopus 로고    scopus 로고
    • Genetically altered mice with different sialyltransferase deficiencies show tissue alterations in sialylation and sialic acid 9-O-acetylation
    • Martin, L. T., Marth, J. D., Varki, A., and Varki, N. M. (2002) Genetically altered mice with different sialyltransferase deficiencies show tissue alterations in sialylation and sialic acid 9-O-acetylation, J. Biol. Chem. 277, 32930-32938.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32930-32938
    • Martin, L.T.1    Marth, J.D.2    Varki, A.3    Varki, N.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.