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Volumn 22, Issue 6, 2002, Pages 637-654

Sulfotransferases and sulfated oligosaccharides

Author keywords

Oligosaccharides; Sulfotransferases

Indexed keywords

ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; ADENYLYLSULFATE KINASE; CHONDROITIN SULFATE; DERMATAN SULFATE; GLYCOLIPID; GLYCOPROTEIN; GLYCOSAMINOGLYCAN; GLYCOSYLTRANSFERASE; HEPARAN SULFATE; HEPARIN; KERATAN SULFATE; LUTEINIZING HORMONE; OLIGOSACCHARIDE; PROOPIOMELANOCORTIN; PROTEOGLYCAN; SELECTIN; SULFATE ADENYLYLTRANSFERASE; SULFATIDE; SULFOTRANSFERASE; THYROTROPIN;

EID: 0036846183     PISSN: 01986325     EISSN: None     Source Type: Journal    
DOI: 10.1002/med.10020     Document Type: Review
Times cited : (108)

References (141)
  • 3
    • 0028030298 scopus 로고
    • A defect in the metabolic activation of sulfate in a patient with achondrogenesis type IB
    • Superti-Furga, A. A defect in the metabolic activation of sulfate in a patient with achondrogenesis type IB. Am J Hum Genet 1994;55:1137-1145.
    • (1994) Am J Hum Genet , vol.55 , pp. 1137-1145
    • Superti-Furga, A.1
  • 4
    • 0023840720 scopus 로고
    • Purification of rat liver N-heparan-sulfate sulfotransferase
    • Brandan E, Hirschberg CB. Purification of rat liver N-heparan-sulfate sulfotransferase. J Biol Chem 1988;263:2417-2422.
    • (1988) J Biol Chem , vol.263 , pp. 2417-2422
    • Brandan, E.1    Hirschberg, C.B.2
  • 5
    • 0026650464 scopus 로고
    • Molecular cloning and expression of rat liver N-heparan sulfate sulfotransferase
    • Hashimoto Y, Orellana A, Gil G, Hirschberg CB. Molecular cloning and expression of rat liver N-heparan sulfate sulfotransferase. J Biol Chem 1992;267:15744-15750.
    • (1992) J Biol Chem , vol.267 , pp. 15744-15750
    • Hashimoto, Y.1    Orellana, A.2    Gil, G.3    Hirschberg, C.B.4
  • 6
    • 0030721537 scopus 로고    scopus 로고
    • Expression cloning of a cDNA encoding a sulfotransferase involved in the biosynthesis of the HNK-1 carbohydrate epitope
    • Bakker H, Friedmann I, Oka S, Kawasaki T, Nifant'ev N, Schachner M, Mantei N. Expression cloning of a cDNA encoding a sulfotransferase involved in the biosynthesis of the HNK-1 carbohydrate epitope. J Biol Chem;272:29942-29946.
    • J Biol Chem , vol.272 , pp. 29942-29946
    • Bakker, H.1    Friedmann, I.2    Oka, S.3    Kawasaki, T.4    Nifant'ev, N.5    Schachner, M.6    Mantei, N.7
  • 8
    • 0031464184 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human keratan sulfate Gal-6-sulfotransferase
    • Fukuta M, Inazawa J, Torii T, Tsuzuki K, Shimada E, Habuchi O. Molecular cloning and characterization of human keratan sulfate Gal-6-sulfotransferase. J Biol Chem 1997;272:32321-32328.
    • (1997) J Biol Chem , vol.272 , pp. 32321-32328
    • Fukuta, M.1    Inazawa, J.2    Torii, T.3    Tsuzuki, K.4    Shimada, E.5    Habuchi, O.6
  • 12
    • 0033600831 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian N-acetylglucosamine-6-sulfotransferase that is highly restricted to intestinal tissue
    • Lee JK, Bhakta S, Rosen SD, Hemmerich S. Cloning and characterization of a mammalian N-acetylglucosamine-6-sulfotransferase that is highly restricted to intestinal tissue. Biochem Biophys Res Commun 1999;263:543-549.
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 543-549
    • Lee, J.K.1    Bhakta, S.2    Rosen, S.D.3    Hemmerich, S.4
  • 13
    • 0029966104 scopus 로고    scopus 로고
    • Purification and characterization of 3′-phosphoadenosine-5′-phosphosulfate:GalCer sulfotransferase from human renal cancer cells
    • Honke K, Yamane M, Ishii A, Kobayashi T, Makita A. Purification and characterization of 3′-phosphoadenosine-5′-phosphosulfate:GalCer sulfotransferase from human renal cancer cells. J Biochem 1996;119:421-427.
    • (1996) J Biochem , vol.119 , pp. 421-427
    • Honke, K.1    Yamane, M.2    Ishii, A.3    Kobayashi, T.4    Makita, A.5
  • 14
    • 0035808299 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a human β-Gal-3′-sulfotransferase that acts on both type 1 and type 2 (Gal β1-3/1-4GlcNAc-R) oligosaccharides
    • Honke K, Tsuda M, Koyota S, Wada Y, Tanaka N, Ishizuka I, Nakayama J, Taniguchi N. Molecular cloning and characterization of a human β-Gal-3′-sulfotransferase that acts on both type 1 and type 2 (Gal β1-3/1-4GlcNAc-R) oligosaccharides. J Biol Chem 2001;276:267-274.
    • (2001) J Biol Chem , vol.276 , pp. 267-274
    • Honke, K.1    Tsuda, M.2    Koyota, S.3    Wada, Y.4    Tanaka, N.5    Ishizuka, I.6    Nakayama, J.7    Taniguchi, N.8
  • 15
    • 0034027989 scopus 로고    scopus 로고
    • cDNA cloning, genomic cloning, and tissue-specific regulation of mouse cerebroside sulfotransferase
    • Hirahara Y, Tsuda M, Wada Y, Honke K. cDNA cloning, genomic cloning, and tissue-specific regulation of mouse cerebroside sulfotransferase. Eur J Biochem 2000;267:1909-1916.
    • (2000) Eur J Biochem , vol.267 , pp. 1909-1916
    • Hirahara, Y.1    Tsuda, M.2    Wada, Y.3    Honke, K.4
  • 17
    • 0035818480 scopus 로고    scopus 로고
    • Enzyme interactions in heparan sulfate biosynthesis: Uronosyl 5-epimerase and 2-O-sulfotransferase interact in vivo
    • Pinhal MA, Smith B, Olson S, Aikawa J, Kimata K, Esko JD. Enzyme interactions in heparan sulfate biosynthesis: Uronosyl 5-epimerase and 2-O-sulfotransferase interact in vivo. Proc Natl Acad Sci USA 2001;98:12984-12989.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12984-12989
    • Pinhal, M.A.1    Smith, B.2    Olson, S.3    Aikawa, J.4    Kimata, K.5    Esko, J.D.6
  • 18
    • 0033574660 scopus 로고    scopus 로고
    • Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/N-sulfotransferase 1
    • Kakuta Y, Sueyoshi T, Negishi M, Pedersen LC. Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/N-sulfotransferase 1. J Biol Chem 1999;274:10673-10676.
    • (1999) J Biol Chem , vol.274 , pp. 10673-10676
    • Kakuta, Y.1    Sueyoshi, T.2    Negishi, M.3    Pedersen, L.C.4
  • 21
    • 0032555376 scopus 로고    scopus 로고
    • A role of Lys614 in the sulfotransferase activity of human heparan sulfate N-deacetylase/N-sulfotransferase
    • Sueyoshi T, Kakuta Y, Pedersen LC, Wall FE, Pedersen LG, Negishi M. A role of Lys614 in the sulfotransferase activity of human heparan sulfate N-deacetylase/N-sulfotransferase. FEBS Lett 1998;433:211-214.
    • (1998) FEBS Lett , vol.433 , pp. 211-214
    • Sueyoshi, T.1    Kakuta, Y.2    Pedersen, L.C.3    Wall, F.E.4    Pedersen, L.G.5    Negishi, M.6
  • 22
    • 0033520425 scopus 로고    scopus 로고
    • Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis
    • Ong E, Yeh JC, Ding Y, Hindsgaul O, Pedersen LC, Negishi M, Fukuda M. Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis. J Biol Chem 1999;274:25608-25612.
    • (1999) J Biol Chem , vol.274 , pp. 25608-25612
    • Ong, E.1    Yeh, J.C.2    Ding, Y.3    Hindsgaul, O.4    Pedersen, L.C.5    Negishi, M.6    Fukuda, M.7
  • 23
    • 0029583379 scopus 로고
    • Pyridoxal 5′-phosphate binds to a lysine residue in the adenosine 3′-phosphate 5′-phosphosulfate recognition site of glycolipid sulfotransferase from human renal cancer cells
    • Kamio K, Honke K, Makita A. Pyridoxal 5′-phosphate binds to a lysine residue in the adenosine 3′-phosphate 5′-phosphosulfate recognition site of glycolipid sulfotransferase from human renal cancer cells. Glycoconj J 1995;12:762-766.
    • (1995) Glycoconj J , vol.12 , pp. 762-766
    • Kamio, K.1    Honke, K.2    Makita, A.3
  • 24
    • 0035477414 scopus 로고    scopus 로고
    • Portable sulphotransferase domain determines sequence specificity of heparan sulphate 3-O-sulphotransferases
    • Yabe T, Shukla D, Spear PG, Rosenberg RD, Seeberger PH, Shworak NW. Portable sulphotransferase domain determines sequence specificity of heparan sulphate 3-O-sulphotransferases. Biochem J 2001;359:235-241.
    • (2001) Biochem J , vol.359 , pp. 235-241
    • Yabe, T.1    Shukla, D.2    Spear, P.G.3    Rosenberg, R.D.4    Seeberger, P.H.5    Shworak, N.W.6
  • 25
    • 0036293586 scopus 로고    scopus 로고
    • Identification of structural motifs and amino acids within the structure of human heparan sulfate 3-O-sulfotransferase that mediate enzymatic function
    • Raman R, Myette J, Venkataraman G, Sasisekharan V, Sasisekharan R. Identification of structural motifs and amino acids within the structure of human heparan sulfate 3-O-sulfotransferase that mediate enzymatic function. Biochem Biophys Res Commun 2002;290:1214-1219.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1214-1219
    • Raman, R.1    Myette, J.2    Venkataraman, G.3    Sasisekharan, V.4    Sasisekharan, R.5
  • 26
    • 0035782690 scopus 로고    scopus 로고
    • Genetic dissection of proteoglycan function in Drosophila and C. elegans
    • Selleck SB. Genetic dissection of proteoglycan function in Drosophila and C. elegans. Semin Cell Dev Biol 2001;12:127-134.
    • (2001) Semin Cell Dev Biol , vol.12 , pp. 127-134
    • Selleck, S.B.1
  • 27
    • 0029041333 scopus 로고
    • Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes
    • Rogerson SJ, Chaiyaroj SC, Ng K, Reeder JC, Brown GV. Chondroitin sulfate A is a cell surface receptor for Plasmodium falciparum-infected erythrocytes. J Exp Med 1995;182:15-20.
    • (1995) J Exp Med , vol.182 , pp. 15-20
    • Rogerson, S.J.1    Chaiyaroj, S.C.2    Ng, K.3    Reeder, J.C.4    Brown, G.V.5
  • 28
    • 0029992826 scopus 로고    scopus 로고
    • Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta
    • Fried M, Duffy PE. Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta. Science 1996;272:1502-1504.
    • (1996) Science , vol.272 , pp. 1502-1504
    • Fried, M.1    Duffy, P.E.2
  • 29
    • 0027282460 scopus 로고
    • The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44
    • Naujokas MF, Morin M, Anderson MS, Peterson M, Miller J. The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44. Cell 1993;74:257-268.
    • (1993) Cell , vol.74 , pp. 257-268
    • Naujokas, M.F.1    Morin, M.2    Anderson, M.S.3    Peterson, M.4    Miller, J.5
  • 30
    • 0028965095 scopus 로고
    • A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation
    • Toyama-Sorimachi N, Sorimachi H, Tobita Y, Kitamura F, Yagita H, Suzuki K, Miyasaka M. A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation. J Biol Chem 1995;270:7437-7444.
    • (1995) J Biol Chem , vol.270 , pp. 7437-7444
    • Toyama-Sorimachi, N.1    Sorimachi, H.2    Tobita, Y.3    Kitamura, F.4    Yagita, H.5    Suzuki, K.6    Miyasaka, M.7
  • 31
    • 0024389990 scopus 로고
    • Regulation of cell-substrate adhesion by proteoglycans immobilized on extracellular substrates
    • Yamagata M, Suzuki S, Akiyama SK, Yamada KM, Kimata K. Regulation of cell-substrate adhesion by proteoglycans immobilized on extracellular substrates. J Biol Chem 1989;264:8012-8018.
    • (1989) J Biol Chem , vol.264 , pp. 8012-8018
    • Yamagata, M.1    Suzuki, S.2    Akiyama, S.K.3    Yamada, K.M.4    Kimata, K.5
  • 32
    • 0027264507 scopus 로고
    • Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction
    • Sugiura N, Sakurai K, Hori Y, Karasawa K, Suzuki S, Kimata K. Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction. J Biol Chem 1993;268:15779-15787.
    • (1993) J Biol Chem , vol.268 , pp. 15779-15787
    • Sugiura, N.1    Sakurai, K.2    Hori, Y.3    Karasawa, K.4    Suzuki, S.5    Kimata, K.6
  • 33
    • 0033134190 scopus 로고    scopus 로고
    • Chondroitin-4-sulfate protects high-density lipoprotein against copper-dependent oxidation
    • Albertini R, De Luca G, Passi A, Moratti R, Abuja PM. Chondroitin-4-sulfate protects high-density lipoprotein against copper-dependent oxidation. Arch Biochem Biophys 1999;365:143-149.
    • (1999) Arch Biochem Biophys , vol.365 , pp. 143-149
    • Albertini, R.1    De Luca, G.2    Passi, A.3    Moratti, R.4    Abuja, P.M.5
  • 35
    • 0034733751 scopus 로고    scopus 로고
    • Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family
    • Hiraoka N, Nakagawa H, Ong E, Akama TO, Fukuda MN, Fukuda M. Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family. J Biol Chem 2000;275:20188-20196.
    • (2000) J Biol Chem , vol.275 , pp. 20188-20196
    • Hiraoka, N.1    Nakagawa, H.2    Ong, E.3    Akama, T.O.4    Fukuda, M.N.5    Fukuda, M.6
  • 36
    • 0033593466 scopus 로고    scopus 로고
    • Purification and characterization of chondroitin 4-sulfotransferase from the culture medium of a rat chondrosarcoma cell line
    • Yamauchi S, Hirahara Y, Usui H, Takeda Y, Hoshino M, Fukuta M, Kimura JH, Habuchi O. Purification and characterization of chondroitin 4-sulfotransferase from the culture medium of a rat chondrosarcoma cell line. J Biol Chem 1999;274:2456-2463.
    • (1999) J Biol Chem , vol.274 , pp. 2456-2463
    • Yamauchi, S.1    Hirahara, Y.2    Usui, H.3    Takeda, Y.4    Hoshino, M.5    Fukuta, M.6    Kimura, J.H.7    Habuchi, O.8
  • 37
    • 0035965285 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase
    • Evers MR, Xia G, Kang HG, Schachner M, Baenziger JU. Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase. J Biol Chem 2001;276:36344-36353.
    • (2001) J Biol Chem , vol.276 , pp. 36344-36353
    • Evers, M.R.1    Xia, G.2    Kang, H.G.3    Schachner, M.4    Baenziger, J.U.5
  • 38
    • 0029834975 scopus 로고    scopus 로고
    • 6B4 proteoglycan/phosphacan, an extracellular variant of receptor-like protein-tyrosine phosphataseζ/RPTPβ, binds pleiotrophin/heparin-binding growth-associated molecule (HB-GAM)
    • Maeda N, Nishiwaki T, Shintani T, Hamanaka H, Noda M. 6B4 proteoglycan/phosphacan, an extracellular variant of receptor-like protein-tyrosine phosphataseζ/RPTPβ, binds pleiotrophin/heparin-binding growth-associated molecule (HB-GAM). J Biol Chem 1996;271:21446-21452.
    • (1996) J Biol Chem , vol.271 , pp. 21446-21452
    • Maeda, N.1    Nishiwaki, T.2    Shintani, T.3    Hamanaka, H.4    Noda, M.5
  • 39
    • 0033617313 scopus 로고    scopus 로고
    • A receptor-like protein-tyrosine phosphatase PTPζ/RPTPβ binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPζ
    • Maeda N, Ichihara-Tanaka K, Kimura T, Kadomatsu K, Muramatsu T, Noda M. A receptor-like protein-tyrosine phosphatase PTPζ/RPTPβ binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPζ. J Biol Chem 1999;274:12474-12479.
    • (1999) J Biol Chem , vol.274 , pp. 12474-12479
    • Maeda, N.1    Ichihara-Tanaka, K.2    Kimura, T.3    Kadomatsu, K.4    Muramatsu, T.5    Noda, M.6
  • 40
    • 0029967498 scopus 로고    scopus 로고
    • Enzymatic sulfation of galactose residue of keratan sulfate by chondroitin 6-sulfotransferase
    • Habuchi O, Hirahara Y, Uchimura K, Fukuta M. Enzymatic sulfation of galactose residue of keratan sulfate by chondroitin 6-sulfotransferase. Glycobiology 1996;6:51-57.
    • (1996) Glycobiology , vol.6 , pp. 51-57
    • Habuchi, O.1    Hirahara, Y.2    Uchimura, K.3    Fukuta, M.4
  • 41
    • 0030897938 scopus 로고    scopus 로고
    • Sulfation of sialyl lactosamine oligosaccharides by chondroitin 6-sulfotransferase
    • Habuchi O, Suzuki Y, Fukuta M. Sulfation of sialyl lactosamine oligosaccharides by chondroitin 6-sulfotransferase. Glycobiology 1997;7:405-412.
    • (1997) Glycobiology , vol.7 , pp. 405-412
    • Habuchi, O.1    Suzuki, Y.2    Fukuta, M.3
  • 43
    • 0035941228 scopus 로고    scopus 로고
    • Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to human B cell recombination activating gene-associated gene
    • Ohtake S, Ito Y, Fukuta M, Habuchi O. Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to human B cell recombination activating gene-associated gene. J Biol Chem 2001;276:43894-43900.
    • (2001) J Biol Chem , vol.276 , pp. 43894-43900
    • Ohtake, S.1    Ito, Y.2    Fukuta, M.3    Habuchi, O.4
  • 44
    • 0034602170 scopus 로고    scopus 로고
    • Purification and characterization of N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase from the squid cartilage
    • Ito Y, Habuchi O. Purification and characterization of N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase from the squid cartilage. J Biol Chem 2000;275:34728-34736.
    • (2000) J Biol Chem , vol.275 , pp. 34728-34736
    • Ito, Y.1    Habuchi, O.2
  • 45
    • 0033538061 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a human uronyl 2-sulfotransferase that sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate
    • Kobayashi M, Sugumaran G, Liu J, Shworak NW, Silbert JE, Rosenberg RD. Molecular cloning and characterization of a human uronyl 2-sulfotransferase that sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate. J Biol Chem 1999;274:10474-10480.
    • (1999) J Biol Chem , vol.274 , pp. 10474-10480
    • Kobayashi, M.1    Sugumaran, G.2    Liu, J.3    Shworak, N.W.4    Silbert, J.E.5    Rosenberg, R.D.6
  • 46
    • 0033135173 scopus 로고    scopus 로고
    • Dermatan sulfate activates nuclear factor-κb and induces endothelial and circulating intercellular adhesion molecule-1
    • Penc SF, Pomahac B, Eriksson E, Detmar M, Gallo RL. Dermatan sulfate activates nuclear factor-κb and induces endothelial and circulating intercellular adhesion molecule-1. J Clin Invest 1999;103:1329-1335.
    • (1999) J Clin Invest , vol.103 , pp. 1329-1335
    • Penc, S.F.1    Pomahac, B.2    Eriksson, E.3    Detmar, M.4    Gallo, R.L.5
  • 47
    • 0026727774 scopus 로고
    • Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate
    • Turnbull JE, Fernig DG, Ke Y, Wilkinson MC, Gallagher JT. Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. J Biol Chem 1992;267:10337-10341.
    • (1992) J Biol Chem , vol.267 , pp. 10337-10341
    • Turnbull, J.E.1    Fernig, D.G.2    Ke, Y.3    Wilkinson, M.C.4    Gallagher, J.T.5
  • 48
    • 0025059489 scopus 로고
    • Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity
    • Maimone MM, Tollefsen DM. Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity. J Biol Chem 1990;265:18263-18271.
    • (1990) J Biol Chem , vol.265 , pp. 18263-18271
    • Maimone, M.M.1    Tollefsen, D.M.2
  • 49
    • 0035799627 scopus 로고    scopus 로고
    • Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence
    • Park PW, Pier GB, Hinkes MT, Bernfield M. Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence. Nature 2001;411:98-102.
    • (2001) Nature , vol.411 , pp. 98-102
    • Park, P.W.1    Pier, G.B.2    Hinkes, M.T.3    Bernfield, M.4
  • 50
    • 0027294764 scopus 로고
    • A single protein catalyzes both N-deacetylation and N-sulfation during the biosynthesis of heparan sulfate
    • Wei Z, Swiedler SJ, Ishihara M, Orellana A, Hirschberg CB. A single protein catalyzes both N-deacetylation and N-sulfation during the biosynthesis of heparan sulfate. Proc Natl Acad Sci USA 1993;90:3885-3888.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3885-3888
    • Wei, Z.1    Swiedler, S.J.2    Ishihara, M.3    Orellana, A.4    Hirschberg, C.B.5
  • 51
    • 0025777094 scopus 로고
    • Biosynthesis of heparin. Purification of a 110-kDa mouse mastocytoma protein required for both glucosaminyl N-deacetylation and N-sulfation
    • Pettersson I, Kusche M, Unger E, Wlad H, Nylund L, Lindahl U, Kjellen L. Biosynthesis of heparin. Purification of a 110-kDa mouse mastocytoma protein required for both glucosaminyl N-deacetylation and N-sulfation. J Biol Chem 1991;266:8044-8049.
    • (1991) J Biol Chem , vol.266 , pp. 8044-8049
    • Pettersson, I.1    Kusche, M.2    Unger, E.3    Wlad, H.4    Nylund, L.5    Lindahl, U.6    Kjellen, L.7
  • 52
    • 0028107570 scopus 로고
    • Molecular cloning and expression of a glycosaminoglycan N-acetylglucosaminyl N-deacetylase/N-sulfotransferase from a heparin-producing cell line
    • Oellana A, Hirschberg CB, Wei Z, Swiedler SJ, Ishihara M. Molecular cloning and expression of a glycosaminoglycan N-acetylglucosaminyl N-deacetylase/N-sulfotransferase from a heparin-producing cell line. J Biol Chem 1994;269:2270-2276.
    • (1994) J Biol Chem , vol.269 , pp. 2270-2276
    • Oellana, A.1    Hirschberg, C.B.2    Wei, Z.3    Swiedler, S.J.4    Ishihara, M.5
  • 53
    • 0028364618 scopus 로고
    • cDNA cloning and sequencing of mouse mastocytoma glucosaminyl N-deacetylase/N-sulfotransferase, an enzyme involved in the biosynthesis of heparin
    • Eriksson I, Sandback D, Ek B, Lindahl U, Kjellen L. cDNA cloning and sequencing of mouse mastocytoma glucosaminyl N-deacetylase/N-sulfotransferase, an enzyme involved in the biosynthesis of heparin. J Biol Chem 1994;269:10438-10443.
    • (1994) J Biol Chem , vol.269 , pp. 10438-10443
    • Eriksson, I.1    Sandback, D.2    Ek, B.3    Lindahl, U.4    Kjellen, L.5
  • 54
    • 0033613948 scopus 로고    scopus 로고
    • Molecular cloning and expression of a third member of the heparan sulfate/heparin GlcNAc N-deacetylase/N-sulfotransferase family
    • Aikawa J, Esko JD. Molecular cloning and expression of a third member of the heparan sulfate/heparin GlcNAc N-deacetylase/N-sulfotransferase family. J Biol Chem 1999;274:2690-2695.
    • (1999) J Biol Chem , vol.274 , pp. 2690-2695
    • Aikawa, J.1    Esko, J.D.2
  • 55
    • 0035937147 scopus 로고    scopus 로고
    • Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-sulfotransferase. Structure and activity of the fourth member, NDST4
    • Aikawa J, Grobe K, Tsujimoto M, Esko JD. Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-sulfotransferase. Structure and activity of the fourth member, NDST4. J Biol Chem 2001;276:5876-5882.
    • (2001) J Biol Chem , vol.276 , pp. 5876-5882
    • Aikawa, J.1    Grobe, K.2    Tsujimoto, M.3    Esko, J.D.4
  • 57
    • 0033979749 scopus 로고    scopus 로고
    • Targeted disruption of NDST-1 gene leads to pulmonary hypoplasia and neonatal respiratory distress in mice
    • Fan G, Xiao L, Cheng L, Wang X, Sun B, Hu G. Targeted disruption of NDST-1 gene leads to pulmonary hypoplasia and neonatal respiratory distress in mice. FEBS Lett 2000;467:7-11.
    • (2000) FEBS Lett , vol.467 , pp. 7-11
    • Fan, G.1    Xiao, L.2    Cheng, L.3    Wang, X.4    Sun, B.5    Hu, G.6
  • 59
    • 0034643323 scopus 로고    scopus 로고
    • Specificities of heparan sulphate proteoglycans in developmental processes
    • Perrimon N, Bernfield M. Specificities of heparan sulphate proteoglycans in developmental processes. Nature 2000;404:725-728.
    • (2000) Nature , vol.404 , pp. 725-728
    • Perrimon, N.1    Bernfield, M.2
  • 60
    • 0033566126 scopus 로고    scopus 로고
    • Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling
    • Lin X, Perrimon N. Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling. Nature 1999;400:281-284.
    • (1999) Nature , vol.400 , pp. 281-284
    • Lin, X.1    Perrimon, N.2
  • 62
    • 0032841757 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development
    • Lin X, Buff EM, Perrimon N, Michelson AM. Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development. Development 1999;126:3715-3723.
    • (1999) Development , vol.126 , pp. 3715-3723
    • Lin, X.1    Buff, E.M.2    Perrimon, N.3    Michelson, A.M.4
  • 63
    • 0032496217 scopus 로고    scopus 로고
    • Identification and expression in mouse of two heparan sulfate glucosaminyl N-deacetylase/N-sulfotransferase genes
    • Kusche-Gullberg M, Eriksson I, Pikas DS, Kjellen L. Identification and expression in mouse of two heparan sulfate glucosaminyl N-deacetylase/N-sulfotransferase genes. J Biol Chem 1998;273:11902-11907.
    • (1998) J Biol Chem , vol.273 , pp. 11902-11907
    • Kusche-Gullberg, M.1    Eriksson, I.2    Pikas, D.S.3    Kjellen, L.4
  • 64
    • 0032575517 scopus 로고    scopus 로고
    • The putative heparin-specific N-acetylglucosaminyl N-deacetylase/N-sulfotransferase also occurs in non-heparin-producing cells
    • Toma L, Berninsone P, Hirschberg CB. The putative heparin-specific N-acetylglucosaminyl N-deacetylase/N-sulfotransferase also occurs in non-heparin-producing cells. J Biol Chem 1998;273:22458-22465.
    • (1998) J Biol Chem , vol.273 , pp. 22458-22465
    • Toma, L.1    Berninsone, P.2    Hirschberg, C.B.3
  • 67
    • 0027448951 scopus 로고
    • Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor
    • Maccarana M, Casu B, Lindahl U. Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor. J Biol Chem 1993;268:23898-23905.
    • (1993) J Biol Chem , vol.268 , pp. 23898-23905
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 68
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC. Heparin structure and interactions with basic fibroblast growth factor. Science 1996;271:1116-1120.
    • (1996) Science , vol.271 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, J.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 69
    • 0027428744 scopus 로고
    • Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4
    • Guimond S, Maccarana M, Olwin BB, Lindahl U, Rapraeger AC. Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4. J Biol Chem 1993;268:23906-23914.
    • (1993) J Biol Chem , vol.268 , pp. 23906-23914
    • Guimond, S.1    Maccarana, M.2    Olwin, B.B.3    Lindahl, U.4    Rapraeger, A.C.5
  • 71
    • 0032483520 scopus 로고    scopus 로고
    • Heparan sulfate oligosaccharides require 6-O-sulfation for promotion of basic fibroblast growth factor mitogenic activity
    • Pye DA, Vives RR, Turnbull JE, Hyde P, Gallagher JT. Heparan sulfate oligosaccharides require 6-O-sulfation for promotion of basic fibroblast growth factor mitogenic activity. J Biol Chem 1998;273:22936-22942.
    • (1998) J Biol Chem , vol.273 , pp. 22936-22942
    • Pye, D.A.1    Vives, R.R.2    Turnbull, J.E.3    Hyde, P.4    Gallagher, J.T.5
  • 72
    • 0032515138 scopus 로고    scopus 로고
    • Spatially restricted expression of pipe in the Drosophila egg chamber defines embryonic dorsal-ventral polarity
    • Sen J, Goltz JS, Stevens L, Stein D. Spatially restricted expression of pipe in the Drosophila egg chamber defines embryonic dorsal-ventral polarity. Cell 1998;95:471-481.
    • (1998) Cell , vol.95 , pp. 471-481
    • Sen, J.1    Goltz, J.S.2    Stevens, L.3    Stein, D.4
  • 73
    • 0032526145 scopus 로고    scopus 로고
    • Renal agenesis in mice homozygous for a gene trap mutation in the gene encoding heparan sulfate 2-sulfotransferase
    • Bullock SL, Fletcher JM, Beddington RS, Wilson VA. Renal agenesis in mice homozygous for a gene trap mutation in the gene encoding heparan sulfate 2-sulfotransferase. Genes Dev 1998;12:1894-1906.
    • (1998) Genes Dev , vol.12 , pp. 1894-1906
    • Bullock, S.L.1    Fletcher, J.M.2    Beddington, R.S.3    Wilson, V.A.4
  • 75
    • 0028346380 scopus 로고
    • Interaction of hepatocyte growth factor with heparan sulfate. Elucidation of the major heparan sulfate structural determinants
    • Lyon M, Deakin JA, Mizuno K, Nakamura T, Gallagher JT. Interaction of hepatocyte growth factor with heparan sulfate. Elucidation of the major heparan sulfate structural determinants. J Biol Chem 1994;269:11216-11223.
    • (1994) J Biol Chem , vol.269 , pp. 11216-11223
    • Lyon, M.1    Deakin, J.A.2    Mizuno, K.3    Nakamura, T.4    Gallagher, J.T.5
  • 76
    • 0028784965 scopus 로고
    • Characterization of heparan sulfate oligosaccharides that bind to hepatocyte growth factor
    • Ashikari S, Habuchi H, Kimata K. Characterization of heparan sulfate oligosaccharides that bind to hepatocyte growth factor. J Biol Chem 1995;270:29586-29593.
    • (1995) J Biol Chem , vol.270 , pp. 29586-29593
    • Ashikari, S.1    Habuchi, H.2    Kimata, K.3
  • 77
    • 0030717480 scopus 로고    scopus 로고
    • Amyloid-specific heparan sulfate from human liver and spleen
    • Lindahl B, Lindahl U. Amyloid-specific heparan sulfate from human liver and spleen. J Biol Chem 1997;272:26091-26094.
    • (1997) J Biol Chem , vol.272 , pp. 26091-26094
    • Lindahl, B.1    Lindahl, U.2
  • 78
    • 0031982631 scopus 로고    scopus 로고
    • Heparan sulfate undergoes specific structural changes during the progression from human colon adenoma to carcinoma in vitro
    • Jayson GC, Lyon M, Paraskeva C, Turnbull JE, Deakin JA, Gallagher JT. Heparan sulfate undergoes specific structural changes during the progression from human colon adenoma to carcinoma in vitro. J Biol Chem 1998;273:51-57.
    • (1998) J Biol Chem , vol.273 , pp. 51-57
    • Jayson, G.C.1    Lyon, M.2    Paraskeva, C.3    Turnbull, J.E.4    Deakin, J.A.5    Gallagher, J.T.6
  • 79
    • 0032548932 scopus 로고    scopus 로고
    • Structural modification of fibroblast growth factor-binding heparan sulfate at a determinative stage of neural development
    • Brickman YG, Ford MD, Gallagher JT, Nurcombe V, Bartlett PF, Turnbull JE. Structural modification of fibroblast growth factor-binding heparan sulfate at a determinative stage of neural development. J Biol Chem 1998;273:4350-4359.
    • (1998) J Biol Chem , vol.273 , pp. 4350-4359
    • Brickman, Y.G.1    Ford, M.D.2    Gallagher, J.T.3    Nurcombe, V.4    Bartlett, P.F.5    Turnbull, J.E.6
  • 80
    • 0034723420 scopus 로고    scopus 로고
    • The occurrence of three isoforms of heparan sulfate 6-O-sulfotransferase having different specificities for hexuronic acid adjacent to the targeted N-sulfoglucosamine
    • Habuchi H, Tanaka M, Habuchi O, Yoshida K, Suzuki H, Ban K, Kimata K. The occurrence of three isoforms of heparan sulfate 6-O-sulfotransferase having different specificities for hexuronic acid adjacent to the targeted N-sulfoglucosamine. J Biol Chem 2000;275:2859-2868.
    • (2000) J Biol Chem , vol.275 , pp. 2859-2868
    • Habuchi, H.1    Tanaka, M.2    Habuchi, O.3    Yoshida, K.4    Suzuki, H.5    Ban, K.6    Kimata, K.7
  • 82
    • 0001668795 scopus 로고
    • Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin
    • Lindahl U, Backstrom G, Thunberg L, Leder IG. Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin. Proc Natl Acad Sci USA 1980;77:6551-6555
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6551-6555
    • Lindahl, U.1    Backstrom, G.2    Thunberg, L.3    Leder, I.G.4
  • 83
    • 0022368634 scopus 로고
    • Contribution of monosaccharide residues in heparin binding to antithrombin III
    • Atha DH, Lormeau JC, Petitou M, Rosenberg RD, Choay J. Contribution of monosaccharide residues in heparin binding to antithrombin III. Biochemistry 1985;24:6723-6729.
    • (1985) Biochemistry , vol.24 , pp. 6723-6729
    • Atha, D.H.1    Lormeau, J.C.2    Petitou, M.3    Rosenberg, R.D.4    Choay, J.5
  • 84
    • 0025273939 scopus 로고
    • Biosynthesis of heparin. Availability of glucosaminyl 3-O-sulfation sites
    • Kusche M, Torri G, Casu B, Lindahl U. Biosynthesis of heparin. Availability of glucosaminyl 3-O-sulfation sites. J Biol Chem 1990;265:7292-7300.
    • (1990) J Biol Chem , vol.265 , pp. 7292-7300
    • Kusche, M.1    Torri, G.2    Casu, B.3    Lindahl, U.4
  • 86
    • 0030783519 scopus 로고    scopus 로고
    • Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase
    • Shworak NW, Liu J, Fritze LM, Schwartz JJ, Zhang L, Logeart D, Rosenberg RD. Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J Biol Chem 1997;272:28008-28019.
    • (1997) J Biol Chem , vol.272 , pp. 28008-28019
    • Shworak, N.W.1    Liu, J.2    Fritze, L.M.3    Schwartz, J.J.4    Zhang, L.5    Logeart, D.6    Rosenberg, R.D.7
  • 87
    • 0033605256 scopus 로고    scopus 로고
    • Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells
    • Zhang L, Yoshida K, Liu J, Rosenberg RD. Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells. J Biol Chem 1999;274:5681-5691.
    • (1999) J Biol Chem , vol.274 , pp. 5681-5691
    • Zhang, L.1    Yoshida, K.2    Liu, J.3    Rosenberg, R.D.4
  • 92
    • 0019309810 scopus 로고
    • Macular corneal dystrophy: Failure to synthesize a mature keratan sulfate proteoglycans
    • Hassel JR, Newsome DA, Krachmer JH, Rodrigues MM. Macular corneal dystrophy: Failure to synthesize a mature keratan sulfate proteoglycans. J Biol Chem 1980;77:3705-3709.
    • (1980) J Biol Chem , vol.77 , pp. 3705-3709
    • Hassel, J.R.1    Newsome, D.A.2    Krachmer, J.H.3    Rodrigues, M.M.4
  • 95
    • 0026786473 scopus 로고
    • SV2, a brain synaptic vesicle protein homologous to bacterial transporters
    • Bajjalieh SM, Peterson K, Shinghal R, Scheller RH. SV2, a brain synaptic vesicle protein homologous to bacterial transporters. Science 1992;257:1271-1273.
    • (1992) Science , vol.257 , pp. 1271-1273
    • Bajjalieh, S.M.1    Peterson, K.2    Shinghal, R.3    Scheller, R.H.4
  • 96
    • 0026726318 scopus 로고
    • The synaptic vesicle protein SV2 is a novel type of transmembrane transporter
    • Feany MB, Lee S, Edwards RH, Buckley KM. The synaptic vesicle protein SV2 is a novel type of transmembrane transporter. Cell 1992;70:861-867.
    • (1992) Cell , vol.70 , pp. 861-867
    • Feany, M.B.1    Lee, S.2    Edwards, R.H.3    Buckley, K.M.4
  • 97
    • 0027278599 scopus 로고
    • The SV2 protein of synaptic vesicles is a keratan sulfate proteoglycan
    • Scranton TW, Iwata M, Carlson SS. The SV2 protein of synaptic vesicles is a keratan sulfate proteoglycan. J Neurochem 1993;61:29-44.
    • (1993) J Neurochem , vol.61 , pp. 29-44
    • Scranton, T.W.1    Iwata, M.2    Carlson, S.S.3
  • 100
    • 0031035397 scopus 로고    scopus 로고
    • Pre- and postfusion regulation of transmitter release
    • Rahamimoff R, Fernandez JM. Pre- and postfusion regulation of transmitter release. Neuron 1997;18:17-27.
    • (1997) Neuron , vol.18 , pp. 17-27
    • Rahamimoff, R.1    Fernandez, J.M.2
  • 101
    • 0032832817 scopus 로고    scopus 로고
    • Endothelial ligands for L-selectin
    • Rosen SD. Endothelial ligands for L-selectin. Am J Pathol 1999;155:1013-1020.
    • (1999) Am J Pathol , vol.155 , pp. 1013-1020
    • Rosen, S.D.1
  • 102
    • 0029001510 scopus 로고
    • Selectin-carbohydrate interactions and the initiation of the inflammatory response
    • Lasky LA. Selectin-carbohydrate interactions and the initiation of the inflammatory response. Annu Rev Biochem 1995;64:113-139.
    • (1995) Annu Rev Biochem , vol.64 , pp. 113-139
    • Lasky, L.A.1
  • 103
    • 0029016563 scopus 로고
    • Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin
    • Hemmerich S, Leffler H, Rosen SD. Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin. J Biol Chem 1995;270:12035-12047.
    • (1995) J Biol Chem , vol.270 , pp. 12035-12047
    • Hemmerich, S.1    Leffler, H.2    Rosen, S.D.3
  • 104
    • 0027070306 scopus 로고
    • a epitopes, putative ligands for L-selectin, on peripheral lymph-node high endothelial venules
    • a epitopes, putative ligands for L-selectin, on peripheral lymph-node high endothelial venules. Am J Pathol 1992;141:1259-1264.
    • (1992) Am J Pathol , vol.141 , pp. 1259-1264
    • Paavonen, T.1    Renkonen, R.2
  • 106
    • 0032498546 scopus 로고    scopus 로고
    • L-selectin ligands that are O-glycoprotease resistant and distinct from MECA-79 antigen are sufficient for tethering and rolling of lymphocytes on human high endothelial venules
    • Clark RA, Fuhlbrigge RC, Springer TA. L-selectin ligands that are O-glycoprotease resistant and distinct from MECA-79 antigen are sufficient for tethering and rolling of lymphocytes on human high endothelial venules. J Cell Biol 1998;140:721-731.
    • (1998) J Cell Biol , vol.140 , pp. 721-731
    • Clark, R.A.1    Fuhlbrigge, R.C.2    Springer, T.A.3
  • 107
    • 0035094977 scopus 로고    scopus 로고
    • Chromosomal localization and genomic organization for the galactose/N-acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene family
    • Hemmerich S, Lee JK, Bhakta S, Bistrup A, Ruddle NR, Rosen SD. Chromosomal localization and genomic organization for the galactose/N-acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene family. Glycobiology 2001;11:75-87.
    • (2001) Glycobiology , vol.11 , pp. 75-87
    • Hemmerich, S.1    Lee, J.K.2    Bhakta, S.3    Bistrup, A.4    Ruddle, N.R.5    Rosen, S.D.6
  • 109
    • 0033214388 scopus 로고    scopus 로고
    • Novel oligosaccharide ligands and ligand-processing pathways for the selectins
    • Feizi T, Galustian C. Novel oligosaccharide ligands and ligand-processing pathways for the selectins. Trends Biochem Sci 1999;24:369-372.
    • (1999) Trends Biochem Sci , vol.24 , pp. 369-372
    • Feizi, T.1    Galustian, C.2
  • 110
    • 0030743209 scopus 로고    scopus 로고
    • Reciprocal control of colon-specific sulfomucin and sialosyl-Tn antigen expression in human colorectal neoplasia
    • Yamachika T, Nakanishi H, Inada K, Kitoh K, Kato T, Irimura T, Tatematsu M. Reciprocal control of colon-specific sulfomucin and sialosyl-Tn antigen expression in human colorectal neoplasia. Virchows Arch 1997;431:25-30.
    • (1997) Virchows Arch , vol.431 , pp. 25-30
    • Yamachika, T.1    Nakanishi, H.2    Inada, K.3    Kitoh, K.4    Kato, T.5    Irimura, T.6    Tatematsu, M.7
  • 113
    • 0035968263 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel human β-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans
    • Suzuki A, Hiraoka N, Suzuki M, Angata K, Misra AK, McAuliffe J, Hindsgaul O, Fukuda M. Molecular cloning and expression of a novel human β-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans. J Biol Chem 2001;276:24388-24395.
    • (2001) J Biol Chem , vol.276 , pp. 24388-24395
    • Suzuki, A.1    Hiraoka, N.2    Suzuki, M.3    Angata, K.4    Misra, A.K.5    McAuliffe, J.6    Hindsgaul, O.7    Fukuda, M.8
  • 114
    • 0035920175 scopus 로고    scopus 로고
    • A novel human Gal-3-O-sulfotransferase: Molecular cloning, characterization, and its implications in biosynthesis of (SO(4)-3)Galβ1-4(Fucα1-3)GlcNAc
    • El-Fasakhany FM, Uchimura K, Kannagi R, Muramatsu T. A novel human Gal-3-O-sulfotransferase: Molecular cloning, characterization, and its implications in biosynthesis of (SO(4)-3)Galβ1-4(Fucα1-3)GlcNAc. J Biol Chem 2001;276:26988-26994.
    • (2001) J Biol Chem , vol.276 , pp. 26988-26994
    • El-Fasakhany, F.M.1    Uchimura, K.2    Kannagi, R.3    Muramatsu, T.4
  • 115
    • 0019507223 scopus 로고
    • A differentiation antigen of human NK and K cells identified by a monoclonal antibody (HNK-1)
    • Abo T, Balch CM. A differentiation antigen of human NK and K cells identified by a monoclonal antibody (HNK-1). J Immunol 1981;127:1024-1029.
    • (1981) J Immunol , vol.127 , pp. 1024-1029
    • Abo, T.1    Balch, C.M.2
  • 116
    • 0021062674 scopus 로고
    • Recognition of myelin-associated glycoprotein by monoclonal antibody HNK-1
    • McGarry RC, Helfand SL, Quarles RH, Roder JC. Recognition of myelin-associated glycoprotein by monoclonal antibody HNK-1. Nature 1983;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
  • 117
    • 0021251168 scopus 로고
    • Neural cell adhesion molecules and myelin-associated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1
    • Kruse J, Mailhammer R, Wernecke H, Faissner A, Sommer I, Goridis C, Schachner M. Neural cell adhesion molecules and myelin-associated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1. Nature 1984;311:153-155.
    • (1984) Nature , vol.311 , pp. 153-155
    • Kruse, J.1    Mailhammer, R.2    Wernecke, H.3    Faissner, A.4    Sommer, I.5    Goridis, C.6    Schachner, M.7
  • 118
    • 0023584509 scopus 로고
    • The peripheral myeline glycoprotein PO expresses the L2/HNK-1 and L3 carbohydrate structures shared by neural adhesion molecules
    • Bollensen E, Schachner M. The peripheral myeline glycoprotein PO expresses the L2/HNK-1 and L3 carbohydrate structures shared by neural adhesion molecules. Neurosci Lett 1987;82:77-82.
    • (1987) Neurosci Lett , vol.82 , pp. 77-82
    • Bollensen, E.1    Schachner, M.2
  • 119
    • 0021243658 scopus 로고
    • The monoclonal antibody HNK-1 reacts with a human peripheral nerve ganglioside
    • Ilyas AA, Quarles RH, Brady RO. The monoclonal antibody HNK-1 reacts with a human peripheral nerve ganglioside. Biochem Biophys Res Commun 1984;122:1206-1211.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1206-1211
    • Ilyas, A.A.1    Quarles, R.H.2    Brady, R.O.3
  • 120
    • 0023008691 scopus 로고
    • Strucuture of sulfated glucuronyl glycolipids in the nervous system reacting with HNK-1 antibody and some IgM paraproteins in neuropathy
    • Chou DKH, Ilyas AA, Evans JE, Costello C, Quarles RH, Jungalwara FB. Strucuture of sulfated glucuronyl glycolipids in the nervous system reacting with HNK-1 antibody and some IgM paraproteins in neuropathy. J Biol Chem 1986;261:11717-11725.
    • (1986) J Biol Chem , vol.261 , pp. 11717-11725
    • Chou, D.K.H.1    Ilyas, A.A.2    Evans, J.E.3    Costello, C.4    Quarles, R.H.5    Jungalwara, F.B.6
  • 121
    • 0023103180 scopus 로고
    • Sulfated glucuronic acid-containing glycoconjugates are temporally and spatially regulated antigens in the developing mammalian nervous system
    • Schwarting GA, Jungalwala FB, Chou DK, Boyer AM, Yamamoto M. Sulfated glucuronic acid-containing glycoconjugates are temporally and spatially regulated antigens in the developing mammalian nervous system. Dev Biol 1987;120:65-76.
    • (1987) Dev Biol , vol.120 , pp. 65-76
    • Schwarting, G.A.1    Jungalwala, F.B.2    Chou, D.K.3    Boyer, A.M.4    Yamamoto, M.5
  • 122
    • 0023473072 scopus 로고
    • Perturbation of cranial neural crest migration by the HNK-1 antibody
    • Bronner-Fraser M. Perturbation of cranial neural crest migration by the HNK-1 antibody. Dev Biol 1987;123:321-331.
    • (1987) Dev Biol , vol.123 , pp. 321-331
    • Bronner-Fraser, M.1
  • 123
    • 0022270860 scopus 로고
    • Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies
    • Keilhauer G, Faissner A, Schachner M. Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies. Nature 1985;316:728-730.
    • (1985) Nature , vol.316 , pp. 728-730
    • Keilhauer, G.1    Faissner, A.2    Schachner, M.3
  • 124
    • 0033525021 scopus 로고    scopus 로고
    • Molecular cloning and expression of a second glucuronyltransferase involved in the biosynthesis of the HNK-1 carbohydrate epitope
    • Seiki T, Oka S, Terayama K, Imiya K, Kawasaki T. Molecular cloning and expression of a second glucuronyltransferase involved in the biosynthesis of the HNK-1 carbohydrate epitope. Biochem Biophys Res Commun 1999;255:182-187.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 182-187
    • Seiki, T.1    Oka, S.2    Terayama, K.3    Imiya, K.4    Kawasaki, T.5
  • 125
    • 0033546156 scopus 로고    scopus 로고
    • Cloning and expression of a novel galactoside β1,3-glucuronyltransferase involved in the biosynthesis of HNK-1 epitope
    • Shimoda Y, Tajima Y, Nagase T, Harii K, Osumi N, Sanai Y. Cloning and expression of a novel galactoside β1,3-glucuronyltransferase involved in the biosynthesis of HNK-1 epitope. J Biol Chem 1999;274:17115-17122.
    • (1999) J Biol Chem , vol.274 , pp. 17115-17122
    • Shimoda, Y.1    Tajima, Y.2    Nagase, T.3    Harii, K.4    Osumi, N.5    Sanai, Y.6
  • 126
    • 0032570692 scopus 로고    scopus 로고
    • Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids
    • Ong E, Yeh JC, Ding Y, Hindsgaul O, Fukuda M. Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids. J Biol Chem 1998;273:5190-5195.
    • (1998) J Biol Chem , vol.273 , pp. 5190-5195
    • Ong, E.1    Yeh, J.C.2    Ding, Y.3    Hindsgaul, O.4    Fukuda, M.5
  • 127
  • 128
    • 0034624044 scopus 로고    scopus 로고
    • Molecular cloning and expression of the pituitary glycoprotein hormone N-acetylgalactosamine-4-O-sulfotransferase
    • Xia G, Evers MR, Kang HG, Schachner M, Baenziger JU. Molecular cloning and expression of the pituitary glycoprotein hormone N-acetylgalactosamine-4-O-sulfotransferase. J Biol Chem 2000;275:38402-38409.
    • (2000) J Biol Chem , vol.275 , pp. 38402-38409
    • Xia, G.1    Evers, M.R.2    Kang, H.G.3    Schachner, M.4    Baenziger, J.U.5
  • 129
    • 0034704110 scopus 로고    scopus 로고
    • Molecular cloning and characterization of GalNAc 4-sulfotransferase expressed in human pituitary gland
    • Okuda T, Mita S, Yamauchi S, Fukuta M, Nakano H, Sawada T, Habuchi O. Molecular cloning and characterization of GalNAc 4-sulfotransferase expressed in human pituitary gland. J Biol Chem. 2000;275:40605-40613.
    • (2000) J Biol Chem , vol.275 , pp. 40605-40613
    • Okuda, T.1    Mita, S.2    Yamauchi, S.3    Fukuta, M.4    Nakano, H.5    Sawada, T.6    Habuchi, O.7
  • 130
    • 0035815620 scopus 로고    scopus 로고
    • Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal β1,4-linked N-acetylgalactosamine
    • Kang HG, Evers MR, Xia G, Baenziger JU, Schachner M. Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal β1,4-linked N-acetylgalactosamine. J Biol Chem 2001;276:10861-10869.
    • (2001) J Biol Chem , vol.276 , pp. 10861-10869
    • Kang, H.G.1    Evers, M.R.2    Xia, G.3    Baenziger, J.U.4    Schachner, M.5
  • 131
    • 0034933332 scopus 로고    scopus 로고
    • Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAcβ1-4GlcNAcβ1-R in both N- and O-glycans
    • Hiraoka N, Misra A, Belot F, Hindsgaul O, Fukuda M. Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAcβ1-4GlcNAcβ1-R in both N- and O-glycans. Glycobiology. 2001;11:495-504.
    • (2001) Glycobiology , vol.11 , pp. 495-504
    • Hiraoka, N.1    Misra, A.2    Belot, F.3    Hindsgaul, O.4    Fukuda, M.5
  • 132
    • 0029820671 scopus 로고    scopus 로고
    • From legumes to leukocytes: Biological roles for sulfated carbohydrates
    • Hooper LV, Manzella SM, Baenziger JU. From legumes to leukocytes: Biological roles for sulfated carbohydrates. FASEB J 1996;10:1137-1146.
    • (1996) FASEB J , vol.10 , pp. 1137-1146
    • Hooper, L.V.1    Manzella, S.M.2    Baenziger, J.U.3
  • 134
    • 0031407609 scopus 로고    scopus 로고
    • Chemistry and functional distribution of sulfoglycolipids
    • Ishizuka I. Chemistry and functional distribution of sulfoglycolipids. Prog Lipid Res 1997;36:245-319.
    • (1997) Prog Lipid Res , vol.36 , pp. 245-319
    • Ishizuka, I.1
  • 135
    • 0031040255 scopus 로고    scopus 로고
    • Molecular cloning and expression of cDNA encoding human 3-phosphoadenylylsulfate:galactosylceramide 3-sulfotransferase
    • Honke K, Tsuda M, Hirahara, Y, Ishii A, Makita A, Wada Y. Molecular cloning and expression of cDNA encoding human 3-phosphoadenylylsulfate:galactosylceramide 3-sulfotransferase. J Biol Chem 1997;272:4864-4868.
    • (1997) J Biol Chem , vol.272 , pp. 4864-4868
    • Honke, K.1    Tsuda, M.2    Hirahara, Y.3    Ishii, A.4    Makita, A.5    Wada, Y.6
  • 137
    • 0024532045 scopus 로고
    • Association of elevated sulfatides and sulfotranasferase activities with human renal cell carcinoma
    • Sakakibara N, Gasa S, Kamio K, Makita A, Koyanagi T. Association of elevated sulfatides and sulfotranasferase activities with human renal cell carcinoma. Cancer Res 1989;49:335-339
    • (1989) Cancer Res , vol.49 , pp. 335-339
    • Sakakibara, N.1    Gasa, S.2    Kamio, K.3    Makita, A.4    Koyanagi, T.5
  • 139
    • 0008741309 scopus 로고    scopus 로고
    • Cancer-associated alternative usage of multiple promoters of human GalCer sulfotransferase gene
    • Tsuda M, Egashira M, Niikawa N, Wada Y, Honke K. Cancer-associated alternative usage of multiple promoters of human GalCer sulfotransferase gene. Eur J Biochem 2000;267:2672-2679.
    • (2000) Eur J Biochem , vol.267 , pp. 2672-2679
    • Tsuda, M.1    Egashira, M.2    Niikawa, N.3    Wada, Y.4    Honke, K.5
  • 140
    • 0032170920 scopus 로고    scopus 로고
    • Cancer-associated expression of glycolipid sulfotransferase gene in human renal cell carcinoma cells
    • Honke K, Tsuda M, Hirahara Y, Miyao N, Tsukamoto T, Satoh M, Wada Y. Cancer-associated expression of glycolipid sulfotransferase gene in human renal cell carcinoma cells. Cancer Res 1998;58:3800-3805.
    • (1998) Cancer Res , vol.58 , pp. 3800-3805
    • Honke, K.1    Tsuda, M.2    Hirahara, Y.3    Miyao, N.4    Tsukamoto, T.5    Satoh, M.6    Wada, Y.7
  • 141
    • 0034681139 scopus 로고    scopus 로고
    • The putative tumor supressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate
    • McCormick C, Duncan G, Goutsos KT, Tufaro F. The putative tumor supressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci USA 2000;97:668-673.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 668-673
    • McCormick, C.1    Duncan, G.2    Goutsos, K.T.3    Tufaro, F.4


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