메뉴 건너뛰기




Volumn 35, Issue , 2014, Pages 60-72

Heparan sulfate 3-O-sulfation: A rare modification in search of a function

Author keywords

3 O Sulfotransferases; Antithrombin; Growth factors; Heparan sulfate; Sulfation

Indexed keywords

ANTITHROMBIN; CYCLOPHILIN B; FIBROBLAST GROWTH FACTOR; GLYCOPROTEIN D; HEPARAN SULFATE; SULFOTRANSFERASE; VIRUS GLYCOPROTEIN; CYCLOPHILIN; GLYCOPROTEIN D, HUMAN HERPESVIRUS 1; OLIGOSACCHARIDE; SULFATE; URONIC ACID; VIRUS ENVELOPE PROTEIN;

EID: 84901404021     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2013.12.001     Document Type: Article
Times cited : (172)

References (149)
  • 1
    • 0037022615 scopus 로고    scopus 로고
    • Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix
    • Allain F., Vanpouille C., Carpentier M., Slomianny M.C., Durieux S., Spik G. Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:2714-2719.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2714-2719
    • Allain, F.1    Vanpouille, C.2    Carpentier, M.3    Slomianny, M.C.4    Durieux, S.5    Spik, G.6
  • 3
    • 0022368634 scopus 로고
    • Contribution of monosaccharide residues in heparin binding to antithrombin III
    • Atha D.H., Lormeau J.C., Petitou M., Rosenberg R.D., 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
  • 4
    • 0023646713 scopus 로고
    • Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III
    • Atha D.H., Lormeau J.C., Petitou M., Rosenberg R.D., Choay J. Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III. Biochemistry 1987, 26:6454-6461.
    • (1987) Biochemistry , vol.26 , pp. 6454-6461
    • Atha, D.H.1    Lormeau, J.C.2    Petitou, M.3    Rosenberg, R.D.4    Choay, J.5
  • 5
    • 84859173127 scopus 로고    scopus 로고
    • Genetic variations in genes involved in heparan sulphate biosynthesis are associated with Plasmodium falciparum parasitaemia: a familial study in Burkina Faso
    • Atkinson A., Garnier S., Afridi S., Fumoux F., Rihet P. Genetic variations in genes involved in heparan sulphate biosynthesis are associated with Plasmodium falciparum parasitaemia: a familial study in Burkina Faso. Malar. J. 2012, 11:108.
    • (2012) Malar. J. , vol.11 , pp. 108
    • Atkinson, A.1    Garnier, S.2    Afridi, S.3    Fumoux, F.4    Rihet, P.5
  • 6
    • 84860374004 scopus 로고    scopus 로고
    • Direct visualization of specifically modified extracellular glycans in living animals
    • Attreed M., Desbois M., van Kuppevelt T.H., Bulow H.E. Direct visualization of specifically modified extracellular glycans in living animals. Nat. Methods 2012, 9:477-479.
    • (2012) Nat. Methods , vol.9 , pp. 477-479
    • Attreed, M.1    Desbois, M.2    van Kuppevelt, T.H.3    Bulow, H.E.4
  • 7
    • 0021913331 scopus 로고
    • Structural characterization of the oligosaccharides formed by depolymerization of heparin with nitrous acid
    • Bienkowski M.J., Conrad H.E. Structural characterization of the oligosaccharides formed by depolymerization of heparin with nitrous acid. J Biol Chem. 1985, 260:356-365.
    • (1985) J Biol Chem. , vol.260 , pp. 356-365
    • Bienkowski, M.J.1    Conrad, H.E.2
  • 8
    • 34247610845 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans fine-tune mammalian physiology
    • Bishop J.R., Schuksz M., Esko J.D. Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 2007, 446:1030-1037.
    • (2007) Nature , vol.446 , pp. 1030-1037
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 9
    • 0038521258 scopus 로고    scopus 로고
    • Diurnal pineal 3-O-sulphotransferase 2 expression controlled by beta-adrenergic repression
    • Borjigin J., Deng J., Sun X., De Jesus M., Liu T., Wang M.M. Diurnal pineal 3-O-sulphotransferase 2 expression controlled by beta-adrenergic repression. J. Biol. Chem. 2003, 278:16315-16319.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16315-16319
    • Borjigin, J.1    Deng, J.2    Sun, X.3    De Jesus, M.4    Liu, T.5    Wang, M.M.6
  • 11
    • 76149086192 scopus 로고    scopus 로고
    • Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells
    • Bui C., Ouzzine M., Talhaoui I., Sharp S., Prydz K., Coughtrie M.W., Fournel-Gigleux S. Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells. Faseb J. 2010, 24:436-450.
    • (2010) Faseb J. , vol.24 , pp. 436-450
    • Bui, C.1    Ouzzine, M.2    Talhaoui, I.3    Sharp, S.4    Prydz, K.5    Coughtrie, M.W.6    Fournel-Gigleux, S.7
  • 12
    • 33845368187 scopus 로고    scopus 로고
    • Combinatorial expression patterns of heparan sulfate sulfotransferases in zebrafish: I. The 3-O-sulfotransferase family
    • Cadwallader A.B., Yost H.J. Combinatorial expression patterns of heparan sulfate sulfotransferases in zebrafish: I. The 3-O-sulfotransferase family. Dev. Dyn. 2006, 235:3423-3431.
    • (2006) Dev. Dyn. , vol.235 , pp. 3423-3431
    • Cadwallader, A.B.1    Yost, H.J.2
  • 14
    • 0019801543 scopus 로고
    • The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence. Chemical and 13C nuclear-magnetic-resonance studies
    • Casu B., Oreste P., Torri G., Zoppetti G., Choay J., Lormeau J.C., Petitou M., Sinay P. The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence. Chemical and 13C nuclear-magnetic-resonance studies. Biochem J. 1981, 197:599-609.
    • (1981) Biochem J. , vol.197 , pp. 599-609
    • Casu, B.1    Oreste, P.2    Torri, G.3    Zoppetti, G.4    Choay, J.5    Lormeau, J.C.6    Petitou, M.7    Sinay, P.8
  • 15
    • 24344435938 scopus 로고    scopus 로고
    • Characterization of the structure of antithrombin-binding heparan sulfate generated by heparan sulfate 3-O-sulfotransferase 5
    • Chen J., Liu J. Characterization of the structure of antithrombin-binding heparan sulfate generated by heparan sulfate 3-O-sulfotransferase 5. Biochim. Biophys. Acta 2005, 1725:190-200.
    • (2005) Biochim. Biophys. Acta , vol.1725 , pp. 190-200
    • Chen, J.1    Liu, J.2
  • 16
    • 0242693270 scopus 로고    scopus 로고
    • Biosynthesis of 3-O-sulfated heparan sulfate: unique substrate specificity of heparan sulfate 3-O-sulfotransferase isoform 5
    • Chen J., Duncan M.B., Carrick K., Pope R.M., Liu J. Biosynthesis of 3-O-sulfated heparan sulfate: unique substrate specificity of heparan sulfate 3-O-sulfotransferase isoform 5. Glycobiology 2003, 13:785-794.
    • (2003) Glycobiology , vol.13 , pp. 785-794
    • Chen, J.1    Duncan, M.B.2    Carrick, K.3    Pope, R.M.4    Liu, J.5
  • 17
    • 34548615858 scopus 로고    scopus 로고
    • Using an enzymatic combinatorial approach to identify anticoagulant heparan sulfate structures
    • Chen J., Jones C.L., Liu J. Using an enzymatic combinatorial approach to identify anticoagulant heparan sulfate structures. Chem. Biol. 2007, 14:986-993.
    • (2007) Chem. Biol. , vol.14 , pp. 986-993
    • Chen, J.1    Jones, C.L.2    Liu, J.3
  • 18
    • 0021061174 scopus 로고
    • Structure-activity relationship in heparin: a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
    • Choay J., Petitou M., Lormeau J.C., Sinay P., Casu B., Gatti G. Structure-activity relationship in heparin: a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity. Biochem. Biophys. Res. Commun. 1983, 116:492-499.
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 492-499
    • Choay, J.1    Petitou, M.2    Lormeau, J.C.3    Sinay, P.4    Casu, B.5    Gatti, G.6
  • 20
    • 0025051257 scopus 로고
    • Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: antithrombin binding on cultured endothelial cells and perfused rat aorta
    • de Agostini A., Watkins S.C., Slayter H.S., Youssoufian H., Rosenberg R.D. Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: antithrombin binding on cultured endothelial cells and perfused rat aorta. J. Cell Biol. 1990, 111:1293-1304.
    • (1990) J. Cell Biol. , vol.111 , pp. 1293-1304
    • de Agostini, A.1    Watkins, S.C.2    Slayter, H.S.3    Youssoufian, H.4    Rosenberg, R.D.5
  • 22
    • 76249111617 scopus 로고    scopus 로고
    • Synthesis of heparan sulfate with cyclophilin B-binding properties is determined by cell type-specific expression of sulfotransferases
    • Deligny A., Denys A., Marcant A., Melchior A., Mazurier J., van Kuppevelt T.H., Allain F. Synthesis of heparan sulfate with cyclophilin B-binding properties is determined by cell type-specific expression of sulfotransferases. J. Biol. Chem. 2010, 285:1701-1715.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1701-1715
    • Deligny, A.1    Denys, A.2    Marcant, A.3    Melchior, A.4    Mazurier, J.5    van Kuppevelt, T.H.6    Allain, F.7
  • 23
    • 0027169806 scopus 로고
    • Oligosaccharide composition of heparin and low-molecular-weight heparins by capillary electrophoresis
    • Desai U.R., Wang H., Ampofo S.A., Linhardt R.J. Oligosaccharide composition of heparin and low-molecular-weight heparins by capillary electrophoresis. Anal. Biochem. 1993, 213:120-127.
    • (1993) Anal. Biochem. , vol.213 , pp. 120-127
    • Desai, U.R.1    Wang, H.2    Ampofo, S.A.3    Linhardt, R.J.4
  • 25
    • 1542298280 scopus 로고    scopus 로고
    • The biosynthesis of anticoagulant heparan sulfate by the heparan sulfate 3-O-sulfotransferase isoform 5
    • Duncan M.B., Chen J., Krise J.P., Liu J. The biosynthesis of anticoagulant heparan sulfate by the heparan sulfate 3-O-sulfotransferase isoform 5. Biochim. Biophys. Acta 2004, 1671:34-43.
    • (2004) Biochim. Biophys. Acta , vol.1671 , pp. 34-43
    • Duncan, M.B.1    Chen, J.2    Krise, J.P.3    Liu, J.4
  • 26
    • 2942561980 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of heparan sulfate 3-O-sulfotransferase isoform 1
    • Edavettal S.C., Lee K.A., Negishi M., Linhardt R.J., Liu J., Pedersen L.C. Crystal structure and mutational analysis of heparan sulfate 3-O-sulfotransferase isoform 1. J. Biol. Chem. 2004, 279:25789-25797.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25789-25797
    • Edavettal, S.C.1    Lee, K.A.2    Negishi, M.3    Linhardt, R.J.4    Liu, J.5    Pedersen, L.C.6
  • 27
    • 0025182924 scopus 로고
    • Characterization of novel sequences containing 3-O-sulfated glucosamine in glomerular basement membrane heparan sulfate and localization of sulfated disaccharides to a peripheral domain
    • Edge A.S., Spiro R.G. Characterization of novel sequences containing 3-O-sulfated glucosamine in glomerular basement membrane heparan sulfate and localization of sulfated disaccharides to a peripheral domain. J. Biol. Chem. 1990, 265:15874-15881.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15874-15881
    • Edge, A.S.1    Spiro, R.G.2
  • 28
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: assembly of ligand binding sites in heparan sulfate
    • Esko J.D., Selleck S.B. Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu. Rev. Biochem. 2002, 71:435-471.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 29
    • 17244366458 scopus 로고    scopus 로고
    • Kupffer's vesicle is a ciliated organ of asymmetry in the zebrafish embryo that initiates left-right development of the brain, heart and gut
    • Essner J.J., Amack J.D., Nyholm M.K., Harris E.B., Yost H.J. Kupffer's vesicle is a ciliated organ of asymmetry in the zebrafish embryo that initiates left-right development of the brain, heart and gut. Development 2005, 132:1247-1260.
    • (2005) Development , vol.132 , pp. 1247-1260
    • Essner, J.J.1    Amack, J.D.2    Nyholm, M.K.3    Harris, E.B.4    Yost, H.J.5
  • 31
    • 27844520213 scopus 로고    scopus 로고
    • Synthesis of anticoagulantly active heparan sulfate proteoglycans by glomerular epithelial cells involves multiple 3-O-sulfotransferase isoforms and a limiting precursor pool
    • Girardin E.P., Hajmohammadi S., Birmele B., Helisch A., Shworak N.W., de Agostini A.I. Synthesis of anticoagulantly active heparan sulfate proteoglycans by glomerular epithelial cells involves multiple 3-O-sulfotransferase isoforms and a limiting precursor pool. J. Biol. Chem. 2005, 280:38059-38070.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38059-38070
    • Girardin, E.P.1    Hajmohammadi, S.2    Birmele, B.3    Helisch, A.4    Shworak, N.W.5    de Agostini, A.I.6
  • 32
    • 33750030783 scopus 로고    scopus 로고
    • Conformational transitions induced in heparin octasaccharides by binding with antithrombin III
    • Guerrini M., Guglieri S., Beccati D., Torri G., Viskov C., Mourier P. Conformational transitions induced in heparin octasaccharides by binding with antithrombin III. Biochem J. 2006, 399:191-198.
    • (2006) Biochem J. , vol.399 , pp. 191-198
    • Guerrini, M.1    Guglieri, S.2    Beccati, D.3    Torri, G.4    Viskov, C.5    Mourier, P.6
  • 33
    • 55549136766 scopus 로고    scopus 로고
    • Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction. Evidence for very high affinity induced by an unusual glucuronic acid residue
    • Guerrini M., Guglieri S., Casu B., Torri G., Mourier P., Boudier C., Viskov C. Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction. Evidence for very high affinity induced by an unusual glucuronic acid residue. J. Biol. Chem. 2008, 283:26662-26675.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26662-26675
    • Guerrini, M.1    Guglieri, S.2    Casu, B.3    Torri, G.4    Mourier, P.5    Boudier, C.6    Viskov, C.7
  • 34
    • 84871422681 scopus 로고    scopus 로고
    • An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence
    • Guerrini M., Elli S., Mourier P., Rudd T.R., Gaudesi D., Casu B., Boudier C., Torri G., Viskov C. An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence. Biochem. J. 2013, 449:343-351.
    • (2013) Biochem. J. , vol.449 , pp. 343-351
    • Guerrini, M.1    Elli, S.2    Mourier, P.3    Rudd, T.R.4    Gaudesi, D.5    Casu, B.6    Boudier, C.7    Torri, G.8    Viskov, C.9
  • 36
    • 58149279328 scopus 로고    scopus 로고
    • Visualizing mechanosensory endings of TrkC-expressing neurons in HS3ST-2-hPLAP mice
    • Hasegawa H., Wang F. Visualizing mechanosensory endings of TrkC-expressing neurons in HS3ST-2-hPLAP mice. J. Comp. Neurol. 2008, 511:543-556.
    • (2008) J. Comp. Neurol. , vol.511 , pp. 543-556
    • Hasegawa, H.1    Wang, F.2
  • 37
    • 84865087900 scopus 로고    scopus 로고
    • 3-O-Sulfated heparan sulfate recognized by the antibody HS4C3 contribute to the differentiation of mouse embryonic stem cells via Fas signaling
    • Hirano K., Sasaki N., Ichimiya T., Miura T., Van Kuppevelt T.H., Nishihara S. 3-O-Sulfated heparan sulfate recognized by the antibody HS4C3 contribute to the differentiation of mouse embryonic stem cells via Fas signaling. PLoS ONE 2012, 7:e43440.
    • (2012) PLoS ONE , vol.7
    • Hirano, K.1    Sasaki, N.2    Ichimiya, T.3    Miura, T.4    Van Kuppevelt, T.H.5    Nishihara, S.6
  • 38
    • 0017074450 scopus 로고
    • Anticoagulant activity of heparin: separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin
    • Höök M., Bjork I., Hopwood J., Lindahl U. Anticoagulant activity of heparin: separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin. FEBS Lett. 1976, 66:90-93.
    • (1976) FEBS Lett. , vol.66 , pp. 90-93
    • Höök, M.1    Bjork, I.2    Hopwood, J.3    Lindahl, U.4
  • 39
    • 0017177632 scopus 로고
    • Anticoagulant activity of heparin: isolation of antithrombin-binding sites
    • Hopwood J., Höök M., Linker A., Lindahl U. Anticoagulant activity of heparin: isolation of antithrombin-binding sites. FEBS Lett. 1976, 69:51-54.
    • (1976) FEBS Lett. , vol.69 , pp. 51-54
    • Hopwood, J.1    Höök, M.2    Linker, A.3    Lindahl, U.4
  • 40
    • 0025320371 scopus 로고
    • Rat heparan sulphates. A study of the antithrombin-binding properties of heparan sulphate chains from rat adipose tissue, brain, carcase, heart, intestine, kidneys, liver, lungs, skin and spleen
    • Horner A.A. Rat heparan sulphates. A study of the antithrombin-binding properties of heparan sulphate chains from rat adipose tissue, brain, carcase, heart, intestine, kidneys, liver, lungs, skin and spleen. Biochem. J. 1990, 266:553-559.
    • (1990) Biochem. J. , vol.266 , pp. 553-559
    • Horner, A.A.1
  • 41
    • 79959589596 scopus 로고    scopus 로고
    • Synthesis of 3-O-sulfonated heparan sulfate octasaccharides that inhibit the herpes simplex virus type 1 host-cell interaction
    • Hu Y.P., Lin S.Y., Huang C.Y., Zulueta M.M., Liu J.Y., Chang W., Hung S.C. Synthesis of 3-O-sulfonated heparan sulfate octasaccharides that inhibit the herpes simplex virus type 1 host-cell interaction. Nat. Chem. 2011, 3:557-563.
    • (2011) Nat. Chem. , vol.3 , pp. 557-563
    • Hu, Y.P.1    Lin, S.Y.2    Huang, C.Y.3    Zulueta, M.M.4    Liu, J.Y.5    Chang, W.6    Hung, S.C.7
  • 42
    • 0029897204 scopus 로고    scopus 로고
    • Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding
    • Huntington J.A., Olson S.T., Fan B.Q., Gettins P.G.W. Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding. Biochemistry 1996, 35:8495-8503.
    • (1996) Biochemistry , vol.35 , pp. 8495-8503
    • Huntington, J.A.1    Olson, S.T.2    Fan, B.Q.3    Gettins, P.G.W.4
  • 43
    • 0042661060 scopus 로고    scopus 로고
    • Heparan sulfate is required for bone morphogenetic protein-7 signaling
    • Irie A., Habuchi H., Kimata K., Sanai Y. Heparan sulfate is required for bone morphogenetic protein-7 signaling. Biochem. Biophys. Res. Commun. 2003, 308:858-865.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 858-865
    • Irie, A.1    Habuchi, H.2    Kimata, K.3    Sanai, Y.4
  • 47
    • 84875997500 scopus 로고    scopus 로고
    • Structurally informative tandem mass spectrometry of highly sulfated natural and chemoenzymatically synthesized heparin and heparan sulfate glycosaminoglycans
    • Kailemia M.J., Li L., Xu Y., Liu J., Linhardt R.J., Amster I.J. Structurally informative tandem mass spectrometry of highly sulfated natural and chemoenzymatically synthesized heparin and heparan sulfate glycosaminoglycans. Mol. Cell. Proteomics 2013, 12:979-990.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 979-990
    • Kailemia, M.J.1    Li, L.2    Xu, Y.3    Liu, J.4    Linhardt, R.J.5    Amster, I.J.6
  • 48
    • 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 L.C. 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
  • 49
    • 0242416911 scopus 로고    scopus 로고
    • Heparan sulphate N-sulphotransferase activity: reaction mechanism and substrate recognition
    • Kakuta Y., Li L., Pedersen L.C., Pedersen L.G., Negishi M. Heparan sulphate N-sulphotransferase activity: reaction mechanism and substrate recognition. Biochem. Soc. Trans. 2003, 31:331-334.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 331-334
    • Kakuta, Y.1    Li, L.2    Pedersen, L.C.3    Pedersen, L.G.4    Negishi, M.5
  • 51
    • 0021362049 scopus 로고
    • Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability
    • Koide T., Odani S., Takahashi K., Ono T., Sakuragawa N. Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Proc. Natl. Acad. Sci. U. S. A. 1984, 81:289-293.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 289-293
    • Koide, T.1    Odani, S.2    Takahashi, K.3    Ono, T.4    Sakuragawa, N.5
  • 52
    • 0026722468 scopus 로고
    • Isolation and characterization of heparan sulfate proteoglycans produced by cloned rat microvascular endothelial cells
    • Kojima T., Leone C.W., Marchildon G.A., Marcum J.A., Rosenberg R.D. Isolation and characterization of heparan sulfate proteoglycans produced by cloned rat microvascular endothelial cells. J. Biol. Chem. 1992, 267:4859-4869.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4859-4869
    • Kojima, T.1    Leone, C.W.2    Marchildon, G.A.3    Marcum, J.A.4    Rosenberg, R.D.5
  • 55
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins: the concept of specificity
    • Kreuger J., Spillmann D., Li J.P., Lindahl U. Interactions between heparan sulfate and proteins: the concept of specificity. J. Cell Biol. 2006, 174:323-327.
    • (2006) J. Cell Biol. , vol.174 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.P.3    Lindahl, U.4
  • 56
    • 0242385433 scopus 로고    scopus 로고
    • Enzymatic synthesis of antithrombin III-binding heparan sulfate pentasaccharide
    • Kuberan B., Lech M.Z., Beeler D.L., Wu Z.L., Rosenberg R.D. Enzymatic synthesis of antithrombin III-binding heparan sulfate pentasaccharide. Nat Biotechnol. 2003, 21:1343-1346.
    • (2003) Nat Biotechnol. , vol.21 , pp. 1343-1346
    • Kuberan, B.1    Lech, M.Z.2    Beeler, D.L.3    Wu, Z.L.4    Rosenberg, R.D.5
  • 57
    • 1242339713 scopus 로고    scopus 로고
    • Light-induced 3-O-sulfotransferase expression alters pineal heparan sulfate fine structure. A surprising link to circadian rhythm
    • Kuberan B., Lech M., Borjigin J., Rosenberg R.D. Light-induced 3-O-sulfotransferase expression alters pineal heparan sulfate fine structure. A surprising link to circadian rhythm. J. Biol. Chem. 2004, 279:5053-5054.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5053-5054
    • Kuberan, B.1    Lech, M.2    Borjigin, J.3    Rosenberg, R.D.4
  • 60
    • 0030037196 scopus 로고    scopus 로고
    • Molecular genetics of antithrombin deficiency
    • Lane D.A., Kunz G., Olds R.J., Thein S.L. Molecular genetics of antithrombin deficiency. Blood Rev. 1996, 10:59-74.
    • (1996) Blood Rev. , vol.10 , pp. 59-74
    • Lane, D.A.1    Kunz, G.2    Olds, R.J.3    Thein, S.L.4
  • 61
    • 84864419337 scopus 로고    scopus 로고
    • Sulfamate proton solvent exchange in heparin oligosaccharides: evidence for a persistent hydrogen bond in the antithrombin-binding pentasaccharide Arixtra
    • Langeslay D.J., Young R.P., Beni S., Beecher C.N., Mueller L.J., Larive C.K. Sulfamate proton solvent exchange in heparin oligosaccharides: evidence for a persistent hydrogen bond in the antithrombin-binding pentasaccharide Arixtra. Glycobiology 2012, 22:1173-1182.
    • (2012) Glycobiology , vol.22 , pp. 1173-1182
    • Langeslay, D.J.1    Young, R.P.2    Beni, S.3    Beecher, C.N.4    Mueller, L.J.5    Larive, C.K.6
  • 63
    • 41449101025 scopus 로고    scopus 로고
    • Disaccharide structure code for the easy representation of constituent oligosaccharides from glycosaminoglycans
    • Lawrence R., Lu H., Rosenberg R.D., Esko J.D., Zhang L. Disaccharide structure code for the easy representation of constituent oligosaccharides from glycosaminoglycans. Nat. Methods 2008, 5:291-292.
    • (2008) Nat. Methods , vol.5 , pp. 291-292
    • Lawrence, R.1    Lu, H.2    Rosenberg, R.D.3    Esko, J.D.4    Zhang, L.5
  • 64
    • 0019314486 scopus 로고
    • A novel 3-O sulfatase from human urine acting on methyl-2-deoxy-2-sulfamino-alphs-d-glucopyranoside 3-sulfate
    • Leder I.G. A novel 3-O sulfatase from human urine acting on methyl-2-deoxy-2-sulfamino-alphs-d-glucopyranoside 3-sulfate. Biochem. Biophys. Res. Commun. 1980, 94:1183-1189.
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 1183-1189
    • Leder, I.G.1
  • 65
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin
    • Li W., Johnson D.J., Esmon C.T., Huntington J.A. Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. Nat. Struct. Mol. Biol. 2004, 11:857-862.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 857-862
    • Li, W.1    Johnson, D.J.2    Esmon, C.T.3    Huntington, J.A.4
  • 67
    • 70149088868 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins-design and functional implications
    • Lindahl U., Li J.P. Interactions between heparan sulfate and proteins-design and functional implications. Int. Rev. Cell Mol. Biol. 2009, 276:105-159.
    • (2009) Int. Rev. Cell Mol. Biol. , vol.276 , pp. 105-159
    • Lindahl, U.1    Li, J.P.2
  • 69
    • 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 I.G. Evidence for a 3-O-sulfated d-glucosamine residue in the antithrombin-binding sequence of heparin. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:6551-6555.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6551-6555
    • Lindahl, U.1    Backstrom, G.2    Thunberg, L.3    Leder, I.G.4
  • 70
    • 0020544564 scopus 로고
    • The antithrombin-binding sequence in heparin. Identification of an essential 6-O-sulfate group
    • Lindahl U., Backstrom G., Thunberg L. The antithrombin-binding sequence in heparin. Identification of an essential 6-O-sulfate group. J. Biol. Chem. 1983, 258:9826-9830.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9826-9830
    • Lindahl, U.1    Backstrom, G.2    Thunberg, L.3
  • 71
    • 33846850636 scopus 로고    scopus 로고
    • Anticoagulant heparan sulfate: structural specificity and biosynthesis
    • Liu J., Pedersen L.C. Anticoagulant heparan sulfate: structural specificity and biosynthesis. Appl. Microbiol. Biotechnol. 2007, 74:263-272.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 263-272
    • Liu, J.1    Pedersen, L.C.2
  • 73
    • 0033582432 scopus 로고    scopus 로고
    • Expression of heparan sulfate d-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities
    • Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L., Fritze L.M., Rosenberg R.D. Expression of heparan sulfate d-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J. Biol. Chem. 1999, 274:5185-5192.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5185-5192
    • Liu, J.1    Shworak, N.W.2    Sinay, P.3    Schwartz, J.J.4    Zhang, L.5    Fritze, L.M.6    Rosenberg, R.D.7
  • 74
    • 0033621488 scopus 로고    scopus 로고
    • Heparan sulfate d-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues
    • Liu J.A., Shriver Z., Blaiklock P., Yoshida K., Sasisekharan R., Rosenberg R.D. Heparan sulfate d-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues. J. Biol. Chem. 1999, 274:38155-38162.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38155-38162
    • Liu, J.A.1    Shriver, Z.2    Blaiklock, P.3    Yoshida, K.4    Sasisekharan, R.5    Rosenberg, R.D.6
  • 77
    • 33645664882 scopus 로고    scopus 로고
    • Structural specificity in a FGF7-affinity purified heparin octasaccharide required for formation of a complex with FGF7 and FGFR2IIIb
    • Luo Y., Ye S., Kan M., McKeehan W.L. Structural specificity in a FGF7-affinity purified heparin octasaccharide required for formation of a complex with FGF7 and FGFR2IIIb. J. Cell. Biochem. 2006, 97:1241-1258.
    • (2006) J. Cell. Biochem. , vol.97 , pp. 1241-1258
    • Luo, Y.1    Ye, S.2    Kan, M.3    McKeehan, W.L.4
  • 79
    • 0022004194 scopus 로고
    • Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells
    • Marcum J.A., Rosenberg R.D. Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells. Biochem. Biophys. Res. Commun. 1985, 126:365-372.
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 365-372
    • Marcum, J.A.1    Rosenberg, R.D.2
  • 81
    • 0022892749 scopus 로고
    • Cloned bovine aortic endothelial cells synthesize anticoagulantly active heparan sulfate proteoglycan
    • Marcum J.A., Atha D.H., Fritze L.M., Nawroth P., Stern D., Rosenberg R.D. Cloned bovine aortic endothelial cells synthesize anticoagulantly active heparan sulfate proteoglycan. J. Biol. Chem. 1986, 261:7507-7517.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7507-7517
    • Marcum, J.A.1    Atha, D.H.2    Fritze, L.M.3    Nawroth, P.4    Stern, D.5    Rosenberg, R.D.6
  • 82
    • 0022453540 scopus 로고
    • Anticoagulantly active heparin-like molecules from cultured fibroblasts
    • Marcum J.A., Conway E.M., Youssoufian H., Rosenberg R.D. Anticoagulantly active heparin-like molecules from cultured fibroblasts. Exp. Cell Res. 1986, 166:253-258.
    • (1986) Exp. Cell Res. , vol.166 , pp. 253-258
    • Marcum, J.A.1    Conway, E.M.2    Youssoufian, H.3    Rosenberg, R.D.4
  • 84
    • 0033618340 scopus 로고    scopus 로고
    • Requirement for anticoagulant heparan sulfate in the fibroblast growth factor receptor complex
    • McKeehan W.L., Wu X.C., Kan M. Requirement for anticoagulant heparan sulfate in the fibroblast growth factor receptor complex. J. Biol. Chem. 1999, 274:21511-21514.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21511-21514
    • McKeehan, W.L.1    Wu, X.C.2    Kan, M.3
  • 85
    • 0034718216 scopus 로고    scopus 로고
    • Distribution of sulfated glycosaminoglycans in the animal kingdom: widespread occurrence of heparin-like compounds in invertebrates
    • Medeiros G.F., Mendes A., Castro R.A.B., Baú E.C., Nader H.B., Dietrich C.P. Distribution of sulfated glycosaminoglycans in the animal kingdom: widespread occurrence of heparin-like compounds in invertebrates. Biochim. Biophys. Acta Gen. Subj. 2000, 1475:287-294.
    • (2000) Biochim. Biophys. Acta Gen. Subj. , vol.1475 , pp. 287-294
    • Medeiros, G.F.1    Mendes, A.2    Castro, R.A.B.3    Baú, E.C.4    Nader, H.B.5    Dietrich, C.P.6
  • 86
    • 62149152738 scopus 로고    scopus 로고
    • Differentiation of 3-O-sulfated heparin disaccharide isomers: identification of structural aspects of the heparin CCL2 binding motif
    • Meissen J.K., Sweeney M.D., Girardi M., Lawrence R., Esko J.D., Leary J.A. Differentiation of 3-O-sulfated heparin disaccharide isomers: identification of structural aspects of the heparin CCL2 binding motif. J. Am. Soc. Mass Spectrom. 2009, 20:652-657.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 652-657
    • Meissen, J.K.1    Sweeney, M.D.2    Girardi, M.3    Lawrence, R.4    Esko, J.D.5    Leary, J.A.6
  • 87
    • 0026733347 scopus 로고
    • Cell surface heparan sulfate proteoglycans from human vascular endothelial cells. Core protein characterization and antithrombin III binding properties
    • Mertens G., Cassiman J.J., Van den Berghe H., Vermylen J., David G. Cell surface heparan sulfate proteoglycans from human vascular endothelial cells. Core protein characterization and antithrombin III binding properties. J. Biol. Chem. 1992, 267:20435-20443.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20435-20443
    • Mertens, G.1    Cassiman, J.J.2    Van den Berghe, H.3    Vermylen, J.4    David, G.5
  • 88
    • 0019880301 scopus 로고
    • The antithrombin-binding sequence of heparin studied by n.m.r. spectroscopy
    • Meyer B., Thunberg L., Lindahl U., Larm O., Leder I.G. The antithrombin-binding sequence of heparin studied by n.m.r. spectroscopy. Carbohydr. Res. 1981, 88:C1-C4.
    • (1981) Carbohydr. Res. , vol.88
    • Meyer, B.1    Thunberg, L.2    Lindahl, U.3    Larm, O.4    Leder, I.G.5
  • 90
    • 0037448688 scopus 로고    scopus 로고
    • Methylation-associated silencing of heparan sulfate d-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers
    • Miyamoto K., Asada K., Fukutomi T., Okochi E., Yagi Y., Hasegawa T., Asahara T., Sugimura T., Ushijima T. Methylation-associated silencing of heparan sulfate d-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers. Oncogene 2003, 22:274-280.
    • (2003) Oncogene , vol.22 , pp. 274-280
    • Miyamoto, K.1    Asada, K.2    Fukutomi, T.3    Okochi, E.4    Yagi, Y.5    Hasegawa, T.6    Asahara, T.7    Sugimura, T.8    Ushijima, T.9
  • 92
    • 57649221151 scopus 로고    scopus 로고
    • Tetrasulfated disaccharide unit in heparan sulfate: enzymatic formation and tissue distribution
    • Mochizuki H., Yoshida K., Shibata Y., Kimata K. Tetrasulfated disaccharide unit in heparan sulfate: enzymatic formation and tissue distribution. J. Biol. Chem. 2008, 283:31237-31245.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31237-31245
    • Mochizuki, H.1    Yoshida, K.2    Shibata, Y.3    Kimata, K.4
  • 93
    • 7244223316 scopus 로고    scopus 로고
    • Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1
    • Moon A.F., Edavettal S.C., Krahn J.M., Munoz E.M., Negishi M., Linhardt R.J., Liu J., Pedersen L.C. Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1. J. Biol. Chem. 2004, 279:45185-45193.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45185-45193
    • Moon, A.F.1    Edavettal, S.C.2    Krahn, J.M.3    Munoz, E.M.4    Negishi, M.5    Linhardt, R.J.6    Liu, J.7    Pedersen, L.C.8
  • 96
    • 84855646812 scopus 로고    scopus 로고
    • A synthetic heparan sulfate oligosaccharide library reveals the novel enzymatic action of d-glucosaminyl 3-O-sulfotransferase-3a
    • Nguyen T.K., Arungundram S., Tran V.M., Raman K., Al-Mafraji K., Venot A., Boons G.J., Kuberan B. A synthetic heparan sulfate oligosaccharide library reveals the novel enzymatic action of d-glucosaminyl 3-O-sulfotransferase-3a. Mol. Biosyst. 2012, 8:609-614.
    • (2012) Mol. Biosyst. , vol.8 , pp. 609-614
    • Nguyen, T.K.1    Arungundram, S.2    Tran, V.M.3    Raman, K.4    Al-Mafraji, K.5    Venot, A.6    Boons, G.J.7    Kuberan, B.8
  • 97
    • 0018164321 scopus 로고
    • The binding of low-affinity and high-affinity heparin to antithrombin. Fluorescence studies
    • Nordenman B., Danielsson A., Bjork I. The binding of low-affinity and high-affinity heparin to antithrombin. Fluorescence studies. Eur. J. Biochem. 1978, 90:1-6.
    • (1978) Eur. J. Biochem. , vol.90 , pp. 1-6
    • Nordenman, B.1    Danielsson, A.2    Bjork, I.3
  • 98
    • 33644816869 scopus 로고    scopus 로고
    • A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread
    • O'Donnell C.D., Tiwari V., Oh M.J., Shukla D. A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread. Virology 2006, 346:452-459.
    • (2006) Virology , vol.346 , pp. 452-459
    • O'Donnell, C.D.1    Tiwari, V.2    Oh, M.J.3    Shukla, D.4
  • 99
    • 0033578910 scopus 로고    scopus 로고
    • Antiangiogenic activity of the cleaved conformation of the serpin antithrombin
    • O'Reilly M.S., Pirie-Shepherd S., Lane W.S., Folkman J. Antiangiogenic activity of the cleaved conformation of the serpin antithrombin. Science 1999, 285:1926-1928.
    • (1999) Science , vol.285 , pp. 1926-1928
    • O'Reilly, M.S.1    Pirie-Shepherd, S.2    Lane, W.S.3    Folkman, J.4
  • 100
    • 42649106868 scopus 로고    scopus 로고
    • The heparanome and regulation of cell function: structures, functions and challenges
    • Ori A., Wilkinson M.C., Fernig D.G. The heparanome and regulation of cell function: structures, functions and challenges. Front. Biosci. 2008, 13:4309-4338.
    • (2008) Front. Biosci. , vol.13 , pp. 4309-4338
    • Ori, A.1    Wilkinson, M.C.2    Fernig, D.G.3
  • 101
    • 0020164869 scopus 로고
    • Structure and biological activity of finback-whale (Balaenoptera physalus L.) heparin octasaccharide. Chemical, carbon-13 nuclear-magnetic-resonance, enzymic and biological studies
    • Ototani N., Kikuchi M., Yosizawa Z. Structure and biological activity of finback-whale (Balaenoptera physalus L.) heparin octasaccharide. Chemical, carbon-13 nuclear-magnetic-resonance, enzymic and biological studies. Biochem J. 1982, 205:23-30.
    • (1982) Biochem J. , vol.205 , pp. 23-30
    • Ototani, N.1    Kikuchi, M.2    Yosizawa, Z.3
  • 102
    • 0023664894 scopus 로고
    • Structure and antithrombin-binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela mactroides
    • Pejler G., Danielsson I., Björk U., Lindahl H.B.Nader, Dietrich C.P. Structure and antithrombin-binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela mactroides. J. Biol. Chem. 1987, 262:11413-11421.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11413-11421
    • Pejler, G.1    Danielsson, I.2    Björk, U.3    Lindahl, H.B.N.4    Dietrich, C.P.5
  • 103
    • 0023219699 scopus 로고
    • Structure and affinity for antithrombin of heparan sulfate chains derived from basement membrane proteoglycans
    • Pejler G., Bäckström G., Lindahl U., Paulsson M., Dziadek M., Fujiwara S., Timpl R. Structure and affinity for antithrombin of heparan sulfate chains derived from basement membrane proteoglycans. J. Biol. Chem. 1987, 262:5036-5043.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5036-5043
    • Pejler, G.1    Bäckström, G.2    Lindahl, U.3    Paulsson, M.4    Dziadek, M.5    Fujiwara, S.6    Timpl, R.7
  • 104
    • 84862285980 scopus 로고    scopus 로고
    • Probing structural selectivity of synthetic heparin binding to stabilin protein receptors
    • Pempe E.H., Xu Y., Gopalakrishnan S., Liu J., Harris E.N. Probing structural selectivity of synthetic heparin binding to stabilin protein receptors. J. Biol. Chem. 2012, 287:20774-20783.
    • (2012) J. Biol. Chem. , vol.287 , pp. 20774-20783
    • Pempe, E.H.1    Xu, Y.2    Gopalakrishnan, S.3    Liu, J.4    Harris, E.N.5
  • 105
    • 0034996148 scopus 로고    scopus 로고
    • Anticoagulant heparan sulfate proteoglycans expression in the rat ovary peaks in preovulatory granulosa cells
    • Princivalle M., Hasan S., Hosseini G., de Agostini A.I. Anticoagulant heparan sulfate proteoglycans expression in the rat ovary peaks in preovulatory granulosa cells. Glycobiology 2001, 11:183-194.
    • (2001) Glycobiology , vol.11 , pp. 183-194
    • Princivalle, M.1    Hasan, S.2    Hosseini, G.3    de Agostini, A.I.4
  • 106
    • 0029011878 scopus 로고
    • Biosynthesis of heparin/heparan sulfate. The d-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides
    • Razi N., Lindahl U. Biosynthesis of heparin/heparan sulfate. The d-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides. J. Biol. Chem. 1995, 270:11267-11275.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11267-11275
    • Razi, N.1    Lindahl, U.2
  • 107
    • 70350442571 scopus 로고    scopus 로고
    • The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation
    • Richard B., Swanson R., Olson S.T. The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation. J. Biol. Chem. 2009, 284:27054-27064.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27054-27064
    • Richard, B.1    Swanson, R.2    Olson, S.T.3
  • 108
    • 0019862158 scopus 로고
    • The antithrombin-binding sequence of heparin. Location of essential N-sulfate groups
    • Riesenfeld J., Thunberg L., Höök M., Lindahl U. The antithrombin-binding sequence of heparin. Location of essential N-sulfate groups. J. Biol. Chem. 1981, 256:2389-2394.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2389-2394
    • Riesenfeld, J.1    Thunberg, L.2    Höök, M.3    Lindahl, U.4
  • 109
    • 0015821564 scopus 로고
    • The purification and mechanism of action of human antithrombin-heparin cofactor
    • Rosenberg R.D., Damus P.S. The purification and mechanism of action of human antithrombin-heparin cofactor. J. Biol. Chem. 1973, 248:6490-6505.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6490-6505
    • Rosenberg, R.D.1    Damus, P.S.2
  • 111
    • 58149151221 scopus 로고    scopus 로고
    • Antiangiogenic forms of antithrombin specifically bind to the anticoagulant heparin sequence
    • Schedin-Weiss S., Richard B., Hjelm R., Olson S.T. Antiangiogenic forms of antithrombin specifically bind to the anticoagulant heparin sequence. Biochemistry 2008, 47:13610-13619.
    • (2008) Biochemistry , vol.47 , pp. 13610-13619
    • Schedin-Weiss, S.1    Richard, B.2    Hjelm, R.3    Olson, S.T.4
  • 112
    • 0024268182 scopus 로고
    • Heparan sulphate with no affinity for antithrombin III and the control of haemostasis
    • Scully M.F., Ellis V., Kakkar V.V. Heparan sulphate with no affinity for antithrombin III and the control of haemostasis. FEBS Lett. 1988, 241:11-14.
    • (1988) FEBS Lett. , vol.241 , pp. 11-14
    • Scully, M.F.1    Ellis, V.2    Kakkar, V.V.3
  • 114
    • 0017189425 scopus 로고
    • Formation of anhydrosugars in the chemical depolymerization of heparin
    • Shively J.E., Conrad H.E. Formation of anhydrosugars in the chemical depolymerization of heparin. Biochemistry 1976, 15:3932-3942.
    • (1976) Biochemistry , vol.15 , pp. 3932-3942
    • Shively, J.E.1    Conrad, H.E.2
  • 115
    • 0034641723 scopus 로고    scopus 로고
    • Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin
    • Shriver Z., Sundaram M., Venkataraman G., Fareed A., Linhardt R., Biemann K., Sasisekharan R. Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:10365-10370.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10365-10370
    • Shriver, Z.1    Sundaram, M.2    Venkataraman, G.3    Fareed, A.4    Linhardt, R.5    Biemann, K.6    Sasisekharan, R.7
  • 117
    • 0030783519 scopus 로고    scopus 로고
    • Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate d-glucosaminyl 3-O-sulfotransferase
    • Shworak N.W., Liu J., Fritze L.M.S., Schwartz J.J., Zhang L.J., Logeart D., Rosenberg R.D. 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.S.3    Schwartz, J.J.4    Zhang, L.J.5    Logeart, D.6    Rosenberg, R.D.7
  • 118
    • 0033582505 scopus 로고    scopus 로고
    • Multiple isoforms of heparan sulfate d-glucosaminyl 3-O-sulfotransferase-isolation, characterization, and expression of human cDNAs and identification of distinct genomic loci
    • Shworak N.W., Liu J.A., Petros L.M., Zhang L.J., Kobayashi M., Copeland N.G., Jenkins N.A., Rosenberg R.D. Multiple isoforms of heparan sulfate d-glucosaminyl 3-O-sulfotransferase-isolation, characterization, and expression of human cDNAs and identification of distinct genomic loci. J. Biol. Chem. 1999, 274:5170-5184.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5170-5184
    • Shworak, N.W.1    Liu, J.A.2    Petros, L.M.3    Zhang, L.J.4    Kobayashi, M.5    Copeland, N.G.6    Jenkins, N.A.7    Rosenberg, R.D.8
  • 120
    • 0028898786 scopus 로고
    • Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Role of the antithrombin binding pentasaccharide in heparin rate enhancement
    • Streusand V.J., Bjork I., Gettins P.G., Petitou M., Olson S.T. Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Role of the antithrombin binding pentasaccharide in heparin rate enhancement. J. Biol. Chem. 1995, 270:9043-9051.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9043-9051
    • Streusand, V.J.1    Bjork, I.2    Gettins, P.G.3    Petitou, M.4    Olson, S.T.5
  • 121
    • 77952247819 scopus 로고    scopus 로고
    • Direct effects of IL-4/IL-13 and the nematode Nippostrongylus brasiliensis on intestinal epithelial cells in vitro
    • Takeda K., Hashimoto K., Uchikawa R., Tegoshi T., Yamada M., Arizono N. Direct effects of IL-4/IL-13 and the nematode Nippostrongylus brasiliensis on intestinal epithelial cells in vitro. Parasite Immunol. 2010, 32:420-429.
    • (2010) Parasite Immunol. , vol.32 , pp. 420-429
    • Takeda, K.1    Hashimoto, K.2    Uchikawa, R.3    Tegoshi, T.4    Yamada, M.5    Arizono, N.6
  • 122
    • 84883234314 scopus 로고    scopus 로고
    • Distinct 3-O-sulfated heparan sulfate modification patterns are required for kal-1-dependent neurite branching in a context-dependent manner in Caenorhabditis elegans
    • Tecle E., Diaz-Balzac C.A., Bulow H.E. Distinct 3-O-sulfated heparan sulfate modification patterns are required for kal-1-dependent neurite branching in a context-dependent manner in Caenorhabditis elegans. G3 (Bethesda) 2013, 3:541-552.
    • (2013) G3 (Bethesda) , vol.3 , pp. 541-552
    • Tecle, E.1    Diaz-Balzac, C.A.2    Bulow, H.E.3
  • 124
    • 0020108082 scopus 로고
    • Further characterization of the antithrombin-binding sequence in heparin
    • Thunberg L., Bäckström G., Lindahl U. Further characterization of the antithrombin-binding sequence in heparin. Carbohydr. Res. 1982, 100:393-410.
    • (1982) Carbohydr. Res. , vol.100 , pp. 393-410
    • Thunberg, L.1    Bäckström, G.2    Lindahl, U.3
  • 126
    • 33748502316 scopus 로고    scopus 로고
    • Role for 3-O-sulfated heparan sulfate as the receptor for herpes simplex virus type 1 entry into primary human corneal fibroblasts
    • Tiwari V., Clement C., Xu D., Valyi-Nagy T., Yue B.Y., Liu J., Shukla D. Role for 3-O-sulfated heparan sulfate as the receptor for herpes simplex virus type 1 entry into primary human corneal fibroblasts. J. Virol. 2006, 80:8970-8980.
    • (2006) J. Virol. , vol.80 , pp. 8970-8980
    • Tiwari, V.1    Clement, C.2    Xu, D.3    Valyi-Nagy, T.4    Yue, B.Y.5    Liu, J.6    Shukla, D.7
  • 127
    • 0029916871 scopus 로고    scopus 로고
    • Structures of five sulfated hexasaccharides prepared from porcine intestinal heparin using bacterial heparinase - Structural variants with apparent biosynthetic precursor-product relationships for the antithrombin III-binding site
    • Tsuda H., Yamada S.H., Yamane Y., Yoshida K., Hopwood J.J., Sugahara K. Structures of five sulfated hexasaccharides prepared from porcine intestinal heparin using bacterial heparinase - Structural variants with apparent biosynthetic precursor-product relationships for the antithrombin III-binding site. J Biol Chem. 1996, 271:10495-10502.
    • (1996) J Biol Chem. , vol.271 , pp. 10495-10502
    • Tsuda, H.1    Yamada, S.H.2    Yamane, Y.3    Yoshida, K.4    Hopwood, J.J.5    Sugahara, K.6
  • 129
    • 84883679862 scopus 로고    scopus 로고
    • Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties
    • Viskov C., Elli S., Urso E., Gaudesi D., Mourier P., Herman F., Boudier C., Casu B., Torri G., Guerrini M. Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties. J Biol Chem. 2013, 288:25895-25907.
    • (2013) J Biol Chem. , vol.288 , pp. 25895-25907
    • Viskov, C.1    Elli, S.2    Urso, E.3    Gaudesi, D.4    Mourier, P.5    Herman, F.6    Boudier, C.7    Casu, B.8    Torri, G.9    Guerrini, M.10
  • 130
    • 0036037343 scopus 로고    scopus 로고
    • The anti-inflammatory actions of antithrombin-a review
    • Wiedermann Ch J., Romisch J. The anti-inflammatory actions of antithrombin-a review. Acta Med. Austriaca 2002, 29:89-92.
    • (2002) Acta Med. Austriaca , vol.29 , pp. 89-92
    • Wiedermann Ch, J.1    Romisch, J.2
  • 131
    • 79251513584 scopus 로고    scopus 로고
    • Autocrine effects of interleukin-6 mediate acute-phase proinflammatory and tissue-reparative transcriptional responses of canine bladder mucosa
    • Wood M.W., Breitschwerdt E.B., Gookin J.L. Autocrine effects of interleukin-6 mediate acute-phase proinflammatory and tissue-reparative transcriptional responses of canine bladder mucosa. Infect. Immun. 2011, 79:708-715.
    • (2011) Infect. Immun. , vol.79 , pp. 708-715
    • Wood, M.W.1    Breitschwerdt, E.B.2    Gookin, J.L.3
  • 132
    • 0345826115 scopus 로고    scopus 로고
    • Determining heparan sulfate structure in the vicinity of specific sulfotransferase recognition sites by mass spectrometry
    • Wu Z.L., Lech M., Beeler D.L., Rosenberg R.D. Determining heparan sulfate structure in the vicinity of specific sulfotransferase recognition sites by mass spectrometry. J. Biol. Chem. 2004, 279:1861-1866.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1861-1866
    • Wu, Z.L.1    Lech, M.2    Beeler, D.L.3    Rosenberg, R.D.4
  • 133
    • 0037020248 scopus 로고    scopus 로고
    • Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1
    • Xia G.Q., Chen J.H., Tiwari V., Ju W.J., Li J.P., Malmström A., Shukla D., Liu J. Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1. J. Biol. Chem. 2002, 277:37912-37919.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37912-37919
    • Xia, G.Q.1    Chen, J.H.2    Tiwari, V.3    Ju, W.J.4    Li, J.P.5    Malmström, A.6    Shukla, D.7    Liu, J.8
  • 134
    • 84902215812 scopus 로고    scopus 로고
    • Demystifying heparan sulfate-binding proteins
    • (in press)
    • Xu D., Esko J.D. Demystifying heparan sulfate-binding proteins. Annu. Rev. Biochem. Vol. 2014, (83). (in press).
    • (2014) Annu. Rev. Biochem. Vol. , Issue.83
    • Xu, D.1    Esko, J.D.2
  • 135
    • 12844267473 scopus 로고    scopus 로고
    • Characterization of heparan sulphate 3-O-sulphotransferase isoform 6 and its role in assisting the entry of herpes simplex virus type 1
    • Xu D., Tiwari V., Xia G., Clement C., Shukla D., Liu J. Characterization of heparan sulphate 3-O-sulphotransferase isoform 6 and its role in assisting the entry of herpes simplex virus type 1. Biochem. J. 2005, 385:451-459.
    • (2005) Biochem. J. , vol.385 , pp. 451-459
    • Xu, D.1    Tiwari, V.2    Xia, G.3    Clement, C.4    Shukla, D.5    Liu, J.6
  • 136
  • 138
    • 84865235998 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of heparin oligosaccharides with both anti-factor Xa and anti-factor IIa activities
    • Xu Y., Pempe E.H., Liu J. Chemoenzymatic synthesis of heparin oligosaccharides with both anti-factor Xa and anti-factor IIa activities. J. Biol. Chem. 2012, 287:29054-29061.
    • (2012) J. Biol. Chem. , vol.287 , pp. 29054-29061
    • Xu, Y.1    Pempe, E.H.2    Liu, J.3
  • 139
    • 27244453272 scopus 로고    scopus 로고
    • Developmental and regional expression of heparan sulfate sulfotransferase genes in the mouse brain
    • Yabe T., Hata T., He J., Maeda N. Developmental and regional expression of heparan sulfate sulfotransferase genes in the mouse brain. Glycobiology 2005, 15:982-993.
    • (2005) Glycobiology , vol.15 , pp. 982-993
    • Yabe, T.1    Hata, T.2    He, J.3    Maeda, N.4
  • 140
    • 0027513987 scopus 로고
    • Structural studies on the bacterial lyase-resistant tetrasaccharides derived from the antithrombin III-binding of porcine intestinal heparin
    • Yamada S., Yoshida K., Sugiura M., Sugahara K., Khoo K.H., Morris H.R., Dell A. Structural studies on the bacterial lyase-resistant tetrasaccharides derived from the antithrombin III-binding of porcine intestinal heparin. J. Biol. Chem. 1993, 268:4780-4787.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4780-4787
    • Yamada, S.1    Yoshida, K.2    Sugiura, M.3    Sugahara, K.4    Khoo, K.H.5    Morris, H.R.6    Dell, A.7
  • 142
    • 0042389659 scopus 로고    scopus 로고
    • Mutations in the N termini of herpes simplex virus type 1 and 2 gDs alter functional interactions with the entry/fusion receptors HVEM, Nectin-2, and 3-O-sulfated heparan sulfate but not with Nectin-1
    • Yoon M., Zago A., Shukla D., Spear P.G. Mutations in the N termini of herpes simplex virus type 1 and 2 gDs alter functional interactions with the entry/fusion receptors HVEM, Nectin-2, and 3-O-sulfated heparan sulfate but not with Nectin-1. J. Virol. 2003, 77:9221-9231.
    • (2003) J. Virol. , vol.77 , pp. 9221-9231
    • Yoon, M.1    Zago, A.2    Shukla, D.3    Spear, P.G.4
  • 143
    • 0032561364 scopus 로고    scopus 로고
    • The retinoic acid and cAMP-dependent up-regulation of 3-O-sulfotransferase-1 leads to a dramatic augmentation of anticoagulantly active heparan sulfate biosynthesis in F9 embryonal carcinoma cells
    • Zhang L.J., Schwartz J.J., Miller J., Liu J., Fritze L.M.S., Shworak N.W., Rosenberg R.D. The retinoic acid and cAMP-dependent up-regulation of 3-O-sulfotransferase-1 leads to a dramatic augmentation of anticoagulantly active heparan sulfate biosynthesis in F9 embryonal carcinoma cells. J. Biol. Chem. 1998, 273:27998-28003.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27998-28003
    • Zhang, L.J.1    Schwartz, J.J.2    Miller, J.3    Liu, J.4    Fritze, L.M.S.5    Shworak, N.W.6    Rosenberg, R.D.7
  • 144
    • 0033605256 scopus 로고    scopus 로고
    • Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells
    • Zhang L.J., Yoshida K., Liu J., Rosenberg R.D. 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.J.1    Yoshida, K.2    Liu, J.3    Rosenberg, R.D.4
  • 146
    • 0035800749 scopus 로고    scopus 로고
    • The effect of precursor structures on the action of glucosaminyl 3-O-sulfotransferase-1 and the biosynthesis of anticoagulant heparan sulfate
    • Zhang L.J., Lawrence R., Schwartz J.J., Bai X.M., Wei G., Esko J.D., Rosenberg R.D. The effect of precursor structures on the action of glucosaminyl 3-O-sulfotransferase-1 and the biosynthesis of anticoagulant heparan sulfate. J. Biol. Chem. 2001, 276:28806-28813.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28806-28813
    • Zhang, L.J.1    Lawrence, R.2    Schwartz, J.J.3    Bai, X.M.4    Wei, G.5    Esko, J.D.6    Rosenberg, R.D.7
  • 147
    • 23944454401 scopus 로고    scopus 로고
    • The heparin-binding site of antithrombin is crucial for antiangiogenic activity
    • Zhang W., Swanson R., Izaguirre G., Xiong Y., Lau L.F., Olson S.T. The heparin-binding site of antithrombin is crucial for antiangiogenic activity. Blood 2005, 106:1621-1628.
    • (2005) Blood , vol.106 , pp. 1621-1628
    • Zhang, W.1    Swanson, R.2    Izaguirre, G.3    Xiong, Y.4    Lau, L.F.5    Olson, S.T.6
  • 149
    • 79960903117 scopus 로고    scopus 로고
    • Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfoglucosamine residue
    • Zhao W., Garron M.L., Yang B., Xiao Z., Esko J.D., Cygler M., Linhardt R.J. Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfoglucosamine residue. FEBS Lett. 2011, 585:2461-2466.
    • (2011) FEBS Lett. , vol.585 , pp. 2461-2466
    • Zhao, W.1    Garron, M.L.2    Yang, B.3    Xiao, Z.4    Esko, J.D.5    Cygler, M.6    Linhardt, R.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.