메뉴 건너뛰기




Volumn 24, Issue 9, 2004, Pages 1549-1557

Heparin-binding domains in vascular biology

Author keywords

Antithrombin; Basic amino acids; Consensus sequence; Glycosaminoglycan; Heparin binding domains

Indexed keywords

AMINO ACID; ANTITHROMBIN; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; HEPARIN BINDING PROTEIN;

EID: 4444342956     PISSN: 10795642     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.ATV.0000137189.22999.3f     Document Type: Short Survey
Times cited : (187)

References (107)
  • 1
    • 0000493337 scopus 로고
    • The inhibition of blood clotting: An unidentified substance which acts in conjunction with heparin to prevent the conversion of prothrombin into thrombin
    • Brinkhous KM, Smith HP, Warner ED, Seegers WH. The inhibition of blood clotting: an unidentified substance which acts in conjunction with heparin to prevent the conversion of prothrombin into thrombin. Am J Physiol. 1939;125:683-687.
    • (1939) Am J Physiol , vol.125 , pp. 683-687
    • Brinkhous, K.M.1    Smith, H.P.2    Warner, E.D.3    Seegers, W.H.4
  • 2
    • 0001627642 scopus 로고
    • Inherited antithrombin deficiency causing thrombophilia
    • Egeberg O. Inherited antithrombin deficiency causing thrombophilia. Thromb Diath Haemorrh. 1965;13:516-530.
    • (1965) Thromb Diath Haemorrh , vol.13 , pp. 516-530
    • Egeberg, O.1
  • 3
    • 0015821564 scopus 로고
    • The purification and mechanism of action of human antithrombin-heparin cofactor
    • Rosenberg RD, Damus PS. 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
  • 4
    • 0029059972 scopus 로고
    • Therapeutic uses of heparin beyond its traditional role as an anticoagulant
    • Tyrrell DJ, Kilfeather S, Page CP. Therapeutic uses of heparin beyond its traditional role as an anticoagulant. Trends Pharmacol Sci. 1995;16: 198-204.
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 198-204
    • Tyrrell, D.J.1    Kilfeather, S.2    Page, C.P.3
  • 6
    • 0038792320 scopus 로고    scopus 로고
    • 2003 Claude S. Hudson Award address in carbohydrate chemistry. Heparin: Structure and activity
    • Linhardt RJ. 2003 Claude S. Hudson Award address in carbohydrate chemistry. Heparin: structure and activity. J Med Chem. 2003;46: 2551-2564.
    • (2003) J Med Chem , vol.46 , pp. 2551-2564
    • Linhardt, R.J.1
  • 9
    • 0032573127 scopus 로고    scopus 로고
    • Thermodynamic analysis of the heparin interaction with a basic cyclic peptide using isothermal titration calorimetry
    • Hileman RE, Jennings RN, Linhardt RJ. Thermodynamic analysis of the heparin interaction with a basic cyclic peptide using isothermal titration calorimetry. Biochemistry. 1998;37:15231-15237.
    • (1998) Biochemistry , vol.37 , pp. 15231-15237
    • Hileman, R.E.1    Jennings, R.N.2    Linhardt, R.J.3
  • 11
    • 0037507303 scopus 로고    scopus 로고
    • Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation
    • Jairajpuri MA, Lu A, Desai U, Olson ST, Bjork I, Bock SC. Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation. J Biol Chem. 2003;278: 15941-15950.
    • (2003) J Biol Chem , vol.278 , pp. 15941-15950
    • Jairajpuri, M.A.1    Lu, A.2    Desai, U.3    Olson, S.T.4    Bjork, I.5    Bock, S.C.6
  • 12
    • 0037837506 scopus 로고    scopus 로고
    • 1976-1983, A critical period in the history of heparin: The discovery of the antithrombin binding site
    • Petitou M, Casu B, Lindahl U. 1976-1983, a critical period in the history of heparin: the discovery of the antithrombin binding site. Biochimie. 2003;85:83-89.
    • (2003) Biochimie , vol.85 , pp. 83-89
    • Petitou, M.1    Casu, B.2    Lindahl, U.3
  • 13
    • 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
  • 14
    • 0031733974 scopus 로고    scopus 로고
    • Diversity does make a difference: Fibroblast growth factor-heparin interactions
    • Faham S, Linhardt RJ, Rees DC. Diversity does make a difference: fibroblast growth factor-heparin interactions. Curr Opin Struct Biol. 1998;8:578-586.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 578-586
    • Faham, S.1    Linhardt, R.J.2    Rees, D.C.3
  • 16
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature. 2000;407:1029-1034.
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 20
    • 0035927442 scopus 로고    scopus 로고
    • Probing the interaction of dengue virus envelope protein with heparin: Assessment of glycosaminoglycan-derived inhibitors
    • Marks RM, Lu H, Sundaresan R, Toida T, Suzuki A, Imanari T, Hernaiz MJ, Linhardt RJ. Probing the interaction of dengue virus envelope protein with heparin: assessment of glycosaminoglycan-derived inhibitors. J Med Chem. 2001;44:2178-2187.
    • (2001) J Med Chem , vol.44 , pp. 2178-2187
    • Marks, R.M.1    Lu, H.2    Sundaresan, R.3    Toida, T.4    Suzuki, A.5    Imanari, T.6    Hernaiz, M.J.7    Linhardt, R.J.8
  • 22
    • 0032006909 scopus 로고    scopus 로고
    • Glycosaminoglycan-protein interactions: Definition of consensus sites in glycosaminoglycan binding proteins
    • Hileman RE, Fromm JR, Weiler JM, Linhardt RJ. Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins. BioEssays. 1998;20:156-167.
    • (1998) BioEssays , vol.20 , pp. 156-167
    • Hileman, R.E.1    Fromm, J.R.2    Weiler, J.M.3    Linhardt, R.J.4
  • 23
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin AD, Weintraub HJ. Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis. 1989;9:21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 24
    • 0027327277 scopus 로고
    • Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues
    • Margalit H, Fischer N, Ben-Sasson SA. Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J Biol Chem. 1993;268:19228-19231.
    • (1993) J Biol Chem , vol.268 , pp. 19228-19231
    • Margalit, H.1    Fischer, N.2    Ben-Sasson, S.A.3
  • 26
    • 0028832566 scopus 로고
    • Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor
    • Fromm JR, Hileman RE, Caldwell EEO, Weiler JM, Linhardt RJ. Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor. Arch Biochem Biophys. 1995;323:279-287.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 279-287
    • Fromm, J.R.1    Hileman, R.E.2    Caldwell, E.E.O.3    Weiler, J.M.4    Linhardt, R.J.5
  • 27
    • 0345114077 scopus 로고
    • Hard and soft acids and bases
    • Pearson RG. Hard and soft acids and bases. J Am Chem Soc. 1963;85: 3533-3539.
    • (1963) J Am Chem Soc , vol.85 , pp. 3533-3539
    • Pearson, R.G.1
  • 30
    • 0035443891 scopus 로고    scopus 로고
    • Order out of complexity-protein structures that interact with heparin
    • Mulloy B, Linhardt RJ. Order out of complexity-protein structures that interact with heparin. Curr Opin Struct Biol. 2001;11:623-628.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 623-628
    • Mulloy, B.1    Linhardt, R.J.2
  • 31
    • 0029914095 scopus 로고    scopus 로고
    • High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy
    • Moy FJ, Seddon AP, Bohlen P, Powers R. High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy. Biochemistry. 1996;35:13552-13561.
    • (1996) Biochemistry , vol.35 , pp. 13552-13561
    • Moy, F.J.1    Seddon, A.P.2    Bohlen, P.3    Powers, R.4
  • 33
    • 0033520448 scopus 로고    scopus 로고
    • Heparin dodecasaccharide-binding to platelet factor-4 and growth-related protein-introduction of a partially folded state and implications for heparin-induced thrombocytopenia
    • Mikhailov D, Young HC, Linhardt RJ, Mayo KH. Heparin dodecasaccharide- binding to platelet factor-4 and growth-related protein-introduction of a partially folded state and implications for heparin-induced thrombocytopenia. J Biol Chem. 1999;274:25317-25329.
    • (1999) J Biol Chem , vol.274 , pp. 25317-25329
    • Mikhailov, D.1    Young, H.C.2    Linhardt, R.J.3    Mayo, K.H.4
  • 34
    • 1842477451 scopus 로고    scopus 로고
    • Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin
    • Peterson FC, Elgin ES, Nelson TJ, Zhang F, Hoeger TJ, Linhardt RJ, Volkman BF. Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin. J Biol Chem. 2004;279:12598-12604.
    • (2004) J Biol Chem , vol.279 , pp. 12598-12604
    • Peterson, F.C.1    Elgin, E.S.2    Nelson, T.J.3    Zhang, F.4    Hoeger, T.J.5    Linhardt, R.J.6    Volkman, B.F.7
  • 35
    • 0027071813 scopus 로고
    • Heparin binding site, conformational change, and activation of antithrombin
    • Evans DL, Marshall CJ, Christey PB, Carrell RW. Heparin binding site, conformational change, and activation of antithrombin. Biochemistry. 1992:31:12629-12642.
    • (1992) Biochemistry , vol.31 , pp. 12629-12642
    • Evans, D.L.1    Marshall, C.J.2    Christey, P.B.3    Carrell, R.W.4
  • 36
    • 0028218987 scopus 로고
    • Energetic characterization of the basic fibroblast growth factor-heparin interaction: Identification of the heparin binding domain
    • Thompson LD, Pantoliano MW, Springer BA. Energetic characterization of the basic fibroblast growth factor-heparin interaction: identification of the heparin binding domain. Biochemistry. 1994;33: 3831-3840.
    • (1994) Biochemistry , vol.33 , pp. 3831-3840
    • Thompson, L.D.1    Pantoliano, M.W.2    Springer, B.A.3
  • 37
    • 0028961396 scopus 로고
    • Mapping the heparin-binding site of mucus proteinase inhibitor
    • Mellet P, Ermolieff J, Bieth JG. Mapping the heparin-binding site of mucus proteinase inhibitor. Biochemistry. 1995;34:2645-2652.
    • (1995) Biochemistry , vol.34 , pp. 2645-2652
    • Mellet, P.1    Ermolieff, J.2    Bieth, J.G.3
  • 38
    • 0030062092 scopus 로고    scopus 로고
    • Heparinase I from Flavobacterium heparinum. Mapping and characterization of the heparin binding domain
    • Sasisekharan R, Venkataraman G, Godavarti R, Ernst S, Cooney CL, Langer R. Heparinase I from Flavobacterium heparinum. Mapping and characterization of the heparin binding domain. J Biol Chem. 1996;271: 3124-3131.
    • (1996) J Biol Chem , vol.271 , pp. 3124-3131
    • Sasisekharan, R.1    Venkataraman, G.2    Godavarti, R.3    Ernst, S.4    Cooney, C.L.5    Langer, R.6
  • 39
    • 0029936796 scopus 로고    scopus 로고
    • Interaction of heparin with fibrinogen using surface plasmon resonance technology: Investigation of heparin binding site on fibrinogen
    • Raut S, Gaffney PJ. Interaction of heparin with fibrinogen using surface plasmon resonance technology: investigation of heparin binding site on fibrinogen. Thromb Res. 1996;81:503-509.
    • (1996) Thromb Res , vol.81 , pp. 503-509
    • Raut, S.1    Gaffney, P.J.2
  • 40
    • 0029800333 scopus 로고    scopus 로고
    • Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin
    • Meagher JL, Huntington JA, Fan B, Gettins PGW. Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin. J Biol Chem. 1996;271:29353-29358.
    • (1996) J Biol Chem , vol.271 , pp. 29353-29358
    • Meagher, J.L.1    Huntington, J.A.2    Fan, B.3    Gettins, P.G.W.4
  • 41
    • 0030853308 scopus 로고    scopus 로고
    • Identification of the antithrombin III heparin binding site
    • Ersdal-Badju E, Lu A, Zuo Y, Picard V, Bock SC. Identification of the antithrombin III heparin binding site. J Biol Chem. 1997;272: 19393-19400.
    • (1997) J Biol Chem , vol.272 , pp. 19393-19400
    • Ersdal-Badju, E.1    Lu, A.2    Zuo, Y.3    Picard, V.4    Bock, S.C.5
  • 43
    • 0032553436 scopus 로고    scopus 로고
    • Characterization of a heparin binding site on the heavy chain of factor XI
    • Zhao M, Abdel-Razek T, Sun M-F, Gailani D. Characterization of a heparin binding site on the heavy chain of factor XI. J Biol Chem. 1998;273:31153-31159.
    • (1998) J Biol Chem , vol.273 , pp. 31153-31159
    • Zhao, M.1    Abdel-Razek, T.2    Sun, M.-F.3    Gailani, D.4
  • 44
    • 0033531628 scopus 로고    scopus 로고
    • Docking of glycosaminoglycans to heparin-binding proteins: Validation for aFGF, bFGF, and antithrombin and application to IL-8
    • Bitomsky W, Wade RC. Docking of glycosaminoglycans to heparin-binding proteins: validation for aFGF, bFGF, and antithrombin and application to IL-8. J Am Chem Soc. 1999;121:3004-3013.
    • (1999) J Am Chem Soc , vol.121 , pp. 3004-3013
    • Bitomsky, W.1    Wade, R.C.2
  • 46
    • 0033587477 scopus 로고    scopus 로고
    • Site-directed mutagenesis and molecular modeling identify a crucial amino acid in specifying the heparin affinity of FGF-1
    • Patrie KM, Botelho MJ, Franklin K, Chiu I-M. Site-directed mutagenesis and molecular modeling identify a crucial amino acid in specifying the heparin affinity of FGF-1. Biochemistry. 1999;38: 9264-9272.
    • (1999) Biochemistry , vol.38 , pp. 9264-9272
    • Patrie, K.M.1    Botelho, M.J.2    Franklin, K.3    Chiu, I.-M.4
  • 48
    • 0034602993 scopus 로고    scopus 로고
    • Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding
    • Rezaie AR, Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding, J Biol Chem. 2000;275:3320-3327.
    • (2000) J Biol Chem , vol.275 , pp. 3320-3327
    • Rezaie, A.R.1
  • 49
    • 0035954370 scopus 로고    scopus 로고
    • Localization of a Heparin Binding Site in the Catalytic Domain of Factor XIa
    • Badellino KO, Walsh PN, Localization of a Heparin Binding Site in the Catalytic Domain of Factor XIa, Biochemistry. 2001;40;7569-7580.
    • (2001) Biochemistry , vol.40 , pp. 7569-7580
    • Badellino, K.O.1    Walsh, P.N.2
  • 50
    • 0035968239 scopus 로고    scopus 로고
    • Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C
    • Friedrich U, Blom AM, Dahlback B, Villoutreix BO. Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C. J Biol Chem. 2001;276:24122-24128.
    • (2001) J Biol Chem , vol.276 , pp. 24122-24128
    • Friedrich, U.1    Blom, A.M.2    Dahlback, B.3    Villoutreix, B.O.4
  • 51
    • 0034898556 scopus 로고    scopus 로고
    • Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis
    • Bellosta P, Iwahori A, Plotnikov AN, Eliseenkova AV, Basilico C, Mohammadi M. Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis. Mol Cell Biol. 2001;21:5946-5957,
    • (2001) Mol Cell Biol , vol.21 , pp. 5946-5957
    • Bellosta, P.1    Iwahori, A.2    Plotnikov, A.N.3    Eliseenkova, A.V.4    Basilico, C.5    Mohammadi, M.6
  • 52
    • 0038608022 scopus 로고    scopus 로고
    • CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10)
    • Campanella GSV, Lee EMJ, Sun J, Luster AD. CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10). J Biol Chem. 2003; 278:17066-17074.
    • (2003) J Biol Chem , vol.278 , pp. 17066-17074
    • Campanella, G.S.V.1    Lee, E.M.J.2    Sun, J.3    Luster, A.D.4
  • 53
    • 0036021104 scopus 로고    scopus 로고
    • Identification of critical molecular interactions mediating heparin activation of antithrombin implications for the design of improved heparin anticoagulants
    • Olson ST, Bjork I, Bock SC. Identification of critical molecular interactions mediating heparin activation of antithrombin implications for the design of improved heparin anticoagulants. Trends Cardiovasc Med. 2002;12:198-205.
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 198-205
    • Olson, S.T.1    Bjork, I.2    Bock, S.C.3
  • 54
    • 0019821957 scopus 로고
    • Binding of high-affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction
    • Olson ST, Srinivasan KR, Bjoerk I, Shore JD. Binding of high-affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction. J Biol Chem. 1981;256:11073-11079.
    • (1981) J Biol Chem , vol.256 , pp. 11073-11079
    • Olson, S.T.1    Srinivasan, K.R.2    Bjoerk, I.3    Shore, J.D.4
  • 55
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson ST, Bjork I, Sheffer R, Craig PA, Shore JD, Choay J. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J Biol Chem. 1992;267:12528-12538.
    • (1992) J Biol Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 56
    • 0018642625 scopus 로고
    • Evidence by chemical modification for the involvement of one or more tryptophanyl residues of bovine antithrombin in the binding of high-affinity heparin
    • Bjoerk I, Nordling K. Evidence by chemical modification for the involvement of one or more tryptophanyl residues of bovine antithrombin in the binding of high-affinity heparin. Eur J Biochem. 1979; 102:497-502.
    • (1979) Eur J Biochem , vol.102 , pp. 497-502
    • Bjoerk, I.1    Nordling, K.2
  • 57
    • 0019153944 scopus 로고
    • The heparin binding site of antithrombin III. Evidence for a critical tryptophan residue
    • Blackburn MN, Sibley CC. The heparin binding site of antithrombin III. Evidence for a critical tryptophan residue. J Biol Chem. 1980;255: 824-826.
    • (1980) J Biol Chem , vol.255 , pp. 824-826
    • Blackburn, M.N.1    Sibley, C.C.2
  • 58
    • 0021343234 scopus 로고
    • The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence
    • Blackburn MN, Smith RL, Carson J, Sibley CC. The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence. J Biol Chem. 1984;259:939-941.
    • (1984) J Biol Chem , vol.259 , pp. 939-941
    • Blackburn, M.N.1    Smith, R.L.2    Carson, J.3    Sibley, C.C.4
  • 59
    • 0023620674 scopus 로고
    • The heparin binding site of human antithrombin III. Selective chemical modification at Lys114, Lys125, and Lys287 impairs its heparin cofactor activity
    • Liu CS, Chang JY. The heparin binding site of human antithrombin III. Selective chemical modification at Lys114, Lys125, and Lys287 impairs its heparin cofactor activity. J Biol Chem. 1987;262:17356-17361.
    • (1987) J Biol Chem , vol.262 , pp. 17356-17361
    • Liu, C.S.1    Chang, J.Y.2
  • 60
    • 0023262814 scopus 로고
    • Identification of a lysyl residue in antithrombin which is essential for heparin binding
    • Peterson CB, Noyes CM, Pecon JM, Church FC, Blackburn MN. Identification of a lysyl residue in antithrombin which is essential for heparin binding. J Biol Chem. 1987;262:8061-8065.
    • (1987) J Biol Chem , vol.262 , pp. 8061-8065
    • Peterson, C.B.1    Noyes, C.M.2    Pecon, J.M.3    Church, F.C.4    Blackburn, M.N.5
  • 61
    • 0024513414 scopus 로고
    • Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III
    • Chang JY. Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. J Biol Chem. 1989;264:3111-3115.
    • (1989) J Biol Chem , vol.264 , pp. 3111-3115
    • Chang, J.Y.1
  • 63
    • 0025228798 scopus 로고
    • Influence of chemical modification of tryptophan residues on the properties of human antithrombin III
    • Shah N, Scully MF, Ellis V, Kakkar VV. Influence of chemical modification of tryptophan residues on the properties of human antithrombin III. Thromb Res. 1990;57:343-352.
    • (1990) Thromb Res , vol.57 , pp. 343-352
    • Shah, N.1    Scully, M.F.2    Ellis, V.3    Kakkar, V.V.4
  • 64
    • 0025033915 scopus 로고
    • Evidence that arginine-129 and arginine-145 are located within the heparin binding site of human antithrombin III
    • Sun XJ, Chang JY. Evidence that arginine-129 and arginine-145 are located within the heparin binding site of human antithrombin III. Biochemistry. 1990;29:8957-8962.
    • (1990) Biochemistry , vol.29 , pp. 8957-8962
    • Sun, X.J.1    Chang, J.Y.2
  • 66
    • 0034713836 scopus 로고    scopus 로고
    • The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139
    • Arocas V, Turk B, Bock SC, Olson ST, Bjork I. The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139. Biochemistry. 2000;39:8512-8518.
    • (2000) Biochemistry , vol.39 , pp. 8512-8518
    • Arocas, V.1    Turk, B.2    Bock, S.C.3    Olson, S.T.4    Bjork, I.5
  • 67
    • 0031588685 scopus 로고    scopus 로고
    • The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site
    • Skinner R, Abrahams JP, Whisstock JC, Lesk AM, Carrell RW, Wardell MR. The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site. J Mol Biol. 1997;266:601-609.
    • (1997) J Mol Biol , vol.266 , pp. 601-609
    • Skinner, R.1    Abrahams, J.P.2    Whisstock, J.C.3    Lesk, A.M.4    Carrell, R.W.5    Wardell, M.R.6
  • 68
    • 0029897204 scopus 로고    scopus 로고
    • Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding
    • Huntington JA, Olson ST, Fan B, Gettins PG. 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.3    Gettins, P.G.4
  • 69
    • 0034685780 scopus 로고    scopus 로고
    • The conformational activation of antithrombin, A 2.85 Å structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions
    • Huntington JA, McCoy A, Belzar KJ, Pei XY, Gettins PG, Carrell RW. The conformational activation of antithrombin, A 2.85 Å structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions. J Biol Chem. 2000;275:15377-15383.
    • (2000) J Biol Chem , vol.275 , pp. 15377-15383
    • Huntington, J.A.1    McCoy, A.2    Belzar, K.J.3    Pei, X.Y.4    Gettins, P.G.5    Carrell, R.W.6
  • 70
    • 0035805579 scopus 로고    scopus 로고
    • Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin
    • Chuang YJ, Swanson R, Raja SM, Olson ST. Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin. J Biol Chem. 2001;276:14961-14971.
    • (2001) J Biol Chem , vol.276 , pp. 14961-14971
    • Chuang, Y.J.1    Swanson, R.2    Raja, S.M.3    Olson, S.T.4
  • 71
    • 0034705489 scopus 로고    scopus 로고
    • Role of arginine 129 in heparin binding and activation of antithrombin
    • Desai U, Swanson R, Bock SC, Bjork I, Olson ST. Role of arginine 129 in heparin binding and activation of antithrombin. J Biol Chem. 2000; 275:18976-18984.
    • (2000) J Biol Chem , vol.275 , pp. 18976-18984
    • Desai, U.1    Swanson, R.2    Bock, S.C.3    Bjork, I.4    Olson, S.T.5
  • 72
    • 0035941340 scopus 로고    scopus 로고
    • Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding
    • Arocas V, Bock SC, Raja S, Olson ST, Bjork I, Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding. J Biol Chem. 2001;276:43809-43817.
    • (2001) J Biol Chem , vol.276 , pp. 43809-43817
    • Arocas, V.1    Bock, S.C.2    Raja, S.3    Olson, S.T.4    Bjork, I.5
  • 73
    • 0037108171 scopus 로고    scopus 로고
    • Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding
    • Schedin-Weiss S, Arocas V, Bock SC, Olson ST, Bjoerk I. Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding. Biochemistry. 2002;41:12369-12376.
    • (2002) Biochemistry , vol.41 , pp. 12369-12376
    • Schedin-Weiss, S.1    Arocas, V.2    Bock, S.C.3    Olson, S.T.4    Bjoerk, I.5
  • 74
    • 0033520102 scopus 로고    scopus 로고
    • The role of Arg46 and Arg47 of antithrombin in heparin binding
    • Arocas V, Bock SC, Olson ST, Bjork I. The role of Arg46 and Arg47 of antithrombin in heparin binding. Biochemistry. 1999;38:10196-10204.
    • (1999) Biochemistry , vol.38 , pp. 10196-10204
    • Arocas, V.1    Bock, S.C.2    Olson, S.T.3    Bjork, I.4
  • 75
    • 1642453874 scopus 로고    scopus 로고
    • Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change
    • Schedin-Weiss S, Desai UR, Bock SC, Olson ST, Bjoerk I. Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change. Biochemistry. 2004;43:675-683.
    • (2004) Biochemistry , vol.43 , pp. 675-683
    • Schedin-Weiss, S.1    Desai, U.R.2    Bock, S.C.3    Olson, S.T.4    Bjoerk, I.5
  • 77
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects
    • Olson ST, Bjork I. Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects. J Biol Chem. 1991; 266:6353-6364.
    • (1991) J Biol Chem , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Bjork, I.2
  • 78
    • 0030917184 scopus 로고    scopus 로고
    • The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change
    • Turk B, Brieditis I, Bock SC, Olson ST, Bjork I. The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Biochemistry. 1997;36: 6682-6691.
    • (1997) Biochemistry , vol.36 , pp. 6682-6691
    • Turk, B.1    Brieditis, I.2    Bock, S.C.3    Olson, S.T.4    Bjork, I.5
  • 81
    • 0035887033 scopus 로고    scopus 로고
    • Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor
    • Lietha D, Chirgadze DY, Mulloy B, Blundell TL, Gherardi E. Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor. EMBO J. 2001;20:5543-5555.
    • (2001) EMBO J , vol.20 , pp. 5543-5555
    • Lietha, D.1    Chirgadze, D.Y.2    Mulloy, B.3    Blundell, T.L.4    Gherardi, E.5
  • 82
    • 2942561980 scopus 로고    scopus 로고
    • Structural analysis of the sulfotransferase (3-OST-3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1
    • Moon AF, Edavettal SC, Krahn JM, Munoz EM, Negishi M, Linhardt RJ, Liu J, Pedersen LC. Structural analysis of the sulfotransferase (3-OST-3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1. J Biol Chem. 2004;279:25789-25797.
    • (2004) J Biol Chem , vol.279 , pp. 25789-25797
    • 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
  • 85
    • 0040735688 scopus 로고    scopus 로고
    • Heparin-binding growth-associated molecule contains two heparin-binding β-sheet domains that are homologous to the thrombospondin type I repeat
    • Kilpeläinen I. Kaksonen M, Kinnunen T, Avikainen H, Linhardt RJ, Fath M, Raulo E, Rauvala H. Heparin-binding growth-associated molecule contains two heparin-binding β-sheet domains that are homologous to the thrombospondin type I repeat. J Biol Chem. 2000; 275:13564-13570.
    • (2000) J Biol Chem , vol.275 , pp. 13564-13570
    • Kilpeläinen, I.1    Kaksonen, M.2    Kinnunen, T.3    Avikainen, H.4    Linhardt, R.J.5    Fath, M.6    Raulo, E.7    Rauvala, H.8
  • 86
    • 0022443619 scopus 로고
    • Evidence for conformational equilibrium of the sulfated L-iduronate residue in heparin and in synthetic heparin mono- and oligosaccharides: NMR and force-field studies
    • Ferro DR, Choay J. Evidence for conformational equilibrium of the sulfated L-iduronate residue in heparin and in synthetic heparin mono- and oligosaccharides: NMR and force-field studies. J Am Chem Soc. 1986;108:6773-6778.
    • (1986) J Am Chem Soc , vol.108 , pp. 6773-6778
    • Ferro, D.R.1    Choay, J.2
  • 87
    • 0033650826 scopus 로고    scopus 로고
    • Conformation and dynamics of heparin and heparan sulfate
    • Mulloy B, Forster MJ. Conformation and dynamics of heparin and heparan sulfate. Glycobiology. 2000;10:1147-1156.
    • (2000) Glycobiology , vol.10 , pp. 1147-1156
    • Mulloy, B.1    Forster, M.J.2
  • 89
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • Esko JD, Selleck SB. 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
  • 91
    • 0022004194 scopus 로고
    • Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells
    • Marcum JA, Rosenberg RD. 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
  • 94
    • 0037382806 scopus 로고    scopus 로고
    • Heparan sulfate: Antithrombotic or not?
    • Weitz JI. Heparan sulfate: antithrombotic or not? J Clin Invest. 2003; 111:952-954.
    • (2003) J Clin Invest , vol.111 , pp. 952-954
    • Weitz, J.I.1
  • 95
    • 0028875752 scopus 로고
    • Blood coagulation. The thrombin paradox
    • Griffin JH. Blood coagulation. The thrombin paradox. Nature. 1995; 378:337-338.
    • (1995) Nature , vol.378 , pp. 337-338
    • Griffin, J.H.1
  • 96
    • 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 AI, Watkins SC, Slayter HS, Youssoufian H, Rosenberg RD. 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.I.1    Watkins, S.C.2    Slayter, H.S.3    Youssoufian, H.4    Rosenberg, R.D.5
  • 97
    • 0022620718 scopus 로고
    • On the interaction of rabbit antithrombin III with the luminal surface of the normal and deendothelialized rabbit thoracic aorta in vitro
    • Hatton MWC, Moar SL, Richardson M. On the interaction of rabbit antithrombin III with the luminal surface of the normal and deendothelialized rabbit thoracic aorta in vitro. Blood. 1986;67:878-886.
    • (1986) Blood , vol.67 , pp. 878-886
    • Hatton, M.W.C.1    Moar, S.L.2    Richardson, M.3
  • 98
    • 0023818186 scopus 로고
    • Evidence that rabbit 1251-antithrombin III binds to proteoheparan sulfate at the subendothelium of the rabbit aorta in vitro
    • Hatton MWC, Moar SL, Richardson M. Evidence that rabbit 1251-antithrombin III binds to proteoheparan sulfate at the subendothelium of the rabbit aorta in vitro. Blood Vessels. 1988;25:12-27.
    • (1988) Blood Vessels , vol.25 , pp. 12-27
    • Hatton, M.W.C.1    Moar, S.L.2    Richardson, M.3
  • 99
    • 0037391906 scopus 로고    scopus 로고
    • Molecular and cellular modulation of fibrinolysis
    • Kolev K, Machovich R. Molecular and cellular modulation of fibrinolysis. Thromb Haemost. 2003;89:610-621.
    • (2003) Thromb Haemost , vol.89 , pp. 610-621
    • Kolev, K.1    Machovich, R.2
  • 100
    • 0036820449 scopus 로고    scopus 로고
    • Angiogenic gene therapy strategies for the treatment of cardiovascular disease
    • Rasmussen HS, Rasmussen CS, Macko J, Yonehiro G. Angiogenic gene therapy strategies for the treatment of cardiovascular disease. Curr Opin Mol Ther. 2002;4:476-481.
    • (2002) Curr Opin Mol Ther , vol.4 , pp. 476-481
    • Rasmussen, H.S.1    Rasmussen, C.S.2    Macko, J.3    Yonehiro, G.4
  • 101
    • 0028930591 scopus 로고
    • Dermatan sulfate as a potential therapeutic agent
    • Linhardt RT, Hileman RE. Dermatan sulfate as a potential therapeutic agent. Gen Pharmacol. 1995;26:443-451.
    • (1995) Gen Pharmacol , vol.26 , pp. 443-451
    • Linhardt, R.T.1    Hileman, R.E.2
  • 102
    • 0037143655 scopus 로고    scopus 로고
    • Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
    • Baglin TP, Carrell RW, Church FC, Esmon CT, Huntington JA. Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc Natl Acad Sci U S A. 2002;99: 11079-11084.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11079-11084
    • Baglin, T.P.1    Carrell, R.W.2    Church, F.C.3    Esmon, C.T.4    Huntington, J.A.5
  • 104
    • 0042768015 scopus 로고    scopus 로고
    • Migration of specific leukocyte subsets in response to cytokine or chemokine application in vivo
    • Perretti M, Getting SJ. Migration of specific leukocyte subsets in response to cytokine or chemokine application in vivo. Methods Mol Biol. 2003;225:139-146.
    • (2003) Methods Mol Biol , vol.225 , pp. 139-146
    • Perretti, M.1    Getting, S.J.2
  • 105
    • 0036080430 scopus 로고    scopus 로고
    • Do morphogen gradients arise by diffusion?
    • Lander AD, Nie Q, Wan FYM. Do morphogen gradients arise by diffusion? Dev Cell. 2002;2:785-796.
    • (2002) Dev Cell , vol.2 , pp. 785-796
    • Lander, A.D.1    Nie, Q.2    Wan, F.Y.M.3
  • 106
    • 3242702218 scopus 로고    scopus 로고
    • Role of glycosaminoglycans in cellular communication
    • Linhardt RJ, Toida T. Role of glycosaminoglycans in cellular communication. Acc Chem Res. 2004;37:431-438.
    • (2004) Acc Chem Res , vol.37 , pp. 431-438
    • Linhardt, R.J.1    Toida, T.2
  • 107
    • 0036200993 scopus 로고    scopus 로고
    • Neutrophil priming in host defense: Role of oxidants as priming agents
    • Swain SD, Rohn TT, Quinn MT. Neutrophil priming in host defense: role of oxidants as priming agents. Antioxid Redox Signal. 2002;4: 69-83.
    • (2002) Antioxid Redox Signal , vol.4 , pp. 69-83
    • Swain, S.D.1    Rohn, T.T.2    Quinn, M.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.