메뉴 건너뛰기




Volumn 13, Issue 20, 2007, Pages 2045-2056

Interaction of heparins with fibroblast growth factors: Conformational aspects

Author keywords

FGF; Heparin; NMR spectroscopy; Oligosaccharide conformation; Protein carbohydrate interaction

Indexed keywords

ANGIOGENESIS INHIBITOR; BINDING PROTEIN; FIBROBLAST GROWTH FACTOR; FIBROBLAST GROWTH FACTOR RECEPTOR; GLYCOSAMINOGLYCAN; HEPARIN; IDURONIC ACID; OLIGOSACCHARIDE; POLYSACCHARIDE; TETRASACCHARIDE;

EID: 34447265278     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161207781039733     Document Type: Review
Times cited : (32)

References (64)
  • 2
    • 0033616671 scopus 로고    scopus 로고
    • Molecular characteristics of fibroblast growth factor-fibroblast growth factor receptor-heparin-like glycosaminoglycan complex
    • Venkataraman G, Raman R, Sasisekharan V, Sasisekharan R. Molecular characteristics of fibroblast growth factor-fibroblast growth factor receptor-heparin-like glycosaminoglycan complex. Proc Natl Acad Sci USA 1999; 96: 3658-63.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3658-3663
    • Venkataraman, G.1    Raman, R.2    Sasisekharan, V.3    Sasisekharan, R.4
  • 3
    • 0030045640 scopus 로고    scopus 로고
    • Preferential self-association of basic fibroblast growth factor is stabilized by heparin during receptor dimerization and activation
    • Venkataraman G, Sasisekharan, V, Herr AB, Ornitz DM, Waksman G, Cooney CL, et al. Preferential self-association of basic fibroblast growth factor is stabilized by heparin during receptor dimerization and activation. Proc Natl Acad Sci USA 1996; 93: 845-50.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 845-850
    • Venkataraman, G.1    Sasisekharan, V.2    Herr, A.B.3    Ornitz, D.M.4    Waksman, G.5    Cooney, C.L.6
  • 4
    • 0035443744 scopus 로고    scopus 로고
    • Role of heparan sulfate in fibroblast growth factor signaling: A structural view
    • Pellegrini L. Role of heparan sulfate in fibroblast growth factor signaling: a structural view. Curr Opin Struct Biol 2001; 11: 629-34.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 629-634
    • Pellegrini, L.1
  • 5
    • 0027448951 scopus 로고
    • Minimal sequence in heparin-heparan sulfate required for binding of basic fibroblast growth factor
    • Maccarana M, Casu B, Lindahl U. Minimal sequence in heparin-heparan sulfate required for binding of basic fibroblast growth factor. J Biol Chem 1993; 268: 23898-905.
    • (1993) J Biol Chem , vol.268 , pp. 23898-23905
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 6
    • 1842530198 scopus 로고    scopus 로고
    • Characterization of growth factor-binding structures in heparin/heparan sulphate using an octasaccharide library
    • Ashikari-Hada S, Habuchi H, Kariya Y, Itoh N, Reddi AH, Kimata K. Characterization of growth factor-binding structures in heparin/heparan sulphate using an octasaccharide library. J Biol Chem 2004; 279: 12346-54.
    • (2004) J Biol Chem , vol.279 , pp. 12346-12354
    • Ashikari-Hada, S.1    Habuchi, H.2    Kariya, Y.3    Itoh, N.4    Reddi, A.H.5    Kimata, K.6
  • 8
    • 17744401668 scopus 로고
    • Conformer populations of L-iduronic acid residues in glycosaminoglycan sequences
    • Ferro DR, Provasoli A, Ragazzi M, Casu B, Torri G, Bossennec V, et al. Conformer populations of L-iduronic acid residues in glycosaminoglycan sequences. Carbohydr Res 1990; 195: 157-67.
    • (1990) Carbohydr Res , vol.195 , pp. 157-167
    • Ferro, D.R.1    Provasoli, A.2    Ragazzi, M.3    Casu, B.4    Torri, G.5    Bossennec, V.6
  • 9
    • 84988141308 scopus 로고
    • A force-field study of the conformational characteristics of the iduronate ring
    • Ragazzi M, Ferro DR, Provasoli A. A force-field study of the conformational characteristics of the iduronate ring. J Comput Chem 1986; 7: 105-12.
    • (1986) J Comput Chem , vol.7 , pp. 105-112
    • Ragazzi, M.1    Ferro, D.R.2    Provasoli, A.3
  • 10
    • 0022443619 scopus 로고
    • Evidence for conformational equilibrium of the sulfated L-iduronate residue in heparin and in synthetic mono- and oligosaccharides
    • Ferro DR, Provasoli A, Ragazzi M, Torri G, Casu B, Gatti G, et al. Evidence for conformational equilibrium of the sulfated L-iduronate residue in heparin and in synthetic mono- and oligosaccharides. J Am Chem Soc 1986; 108: 6773-8.
    • (1986) J Am Chem Soc , vol.108 , pp. 6773-6778
    • Ferro, D.R.1    Provasoli, A.2    Ragazzi, M.3    Torri, G.4    Casu, B.5    Gatti, G.6
  • 11
    • 0033135544 scopus 로고    scopus 로고
    • Structure of heparin-derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts
    • Hricovíni M, Guerrini M, Bisio A. Structure of heparin-derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts. Eur J Biochem 1999; 261: 789-801.
    • (1999) Eur J Biochem , vol.261 , pp. 789-801
    • Hricovíni, M.1    Guerrini, M.2    Bisio, A.3
  • 12
    • 0025855259 scopus 로고
    • The 1st total synthesis of the antithrombin-III binding-site of porcine mucosa heparin
    • Petitou M, Jaurand G, Derrion M, Duchaussoy P, Choay J. The 1st total synthesis of the antithrombin-III binding-site of porcine mucosa heparin. Bioorg Med Chem Lett 1991; 1: 95-8.
    • (1991) Bioorg Med Chem Lett , vol.1 , pp. 95-98
    • Petitou, M.1    Jaurand, G.2    Derrion, M.3    Duchaussoy, P.4    Choay, J.5
  • 14
    • 84882561010 scopus 로고    scopus 로고
    • Casu B. Structure, active domains of heparin. In: Garg HG, Linhardt RJ, Hales CA Eds, Chemistry and biology of heparin and heparan sulfate. Elsevier 2005; 461.
    • Casu B. Structure, active domains of heparin. In: Garg HG, Linhardt RJ, Hales CA Eds, Chemistry and biology of heparin and heparan sulfate. Elsevier 2005; 461.
  • 15
    • 0033650826 scopus 로고    scopus 로고
    • Conformation and dynamics of heparin and heparan sulfate
    • Mulloy B, Forster M.J. Conformation and dynamics of heparin and heparan sulfate. Glycobiology 2000; 10: 1147-56.
    • (2000) Glycobiology , vol.10 , pp. 1147-1156
    • Mulloy, B.1    Forster, M.J.2
  • 17
    • 0025707188 scopus 로고
    • Conformation of the pentasaccharide corresponding to the binding-site of heparin for antithrombin
    • Ragazzi M, Ferro DR, Perly B, Sinay P, Petitou M, Choay JM. Conformation of the pentasaccharide corresponding to the binding-site of heparin for antithrombin. Carbohydr Res 1990; 195: 169-85.
    • (1990) Carbohydr Res , vol.195 , pp. 169-185
    • Ragazzi, M.1    Ferro, D.R.2    Perly, B.3    Sinay, P.4    Petitou, M.5    Choay, J.M.6
  • 19
    • 0030691889 scopus 로고    scopus 로고
    • NMR solution conformation of heparin-derived hexasaccharide
    • Mikhailov D, Linhardt RJ, Mayo KH. NMR solution conformation of heparin-derived hexasaccharide Biochem J 1997; 328: 51-61.
    • (1997) Biochem J , vol.328 , pp. 51-61
    • Mikhailov, D.1    Linhardt, R.J.2    Mayo, K.H.3
  • 20
    • 0027164634 scopus 로고
    • m.r. and molecular-modelling studies of the solution conformation of heparin
    • Mulloy B, Forster MJ, Jones C, Davies DB. N.m.r. and molecular-modelling studies of the solution conformation of heparin. Biochem J 1993; 293: 849-58.
    • (1993) Biochem J , vol.293 , pp. 849-858
    • Mulloy, B.1    Forster, M.J.2    Jones, C.3    Davies, D.N.4
  • 22
    • 0028957865 scopus 로고
    • Dynamics in aqueous solutions of the pentasaccharide corresponding to the binding site of heparin for antithrombin III studied by NMR relaxation measurements
    • Hricovíni M, Torri G. Dynamics in aqueous solutions of the pentasaccharide corresponding to the binding site of heparin for antithrombin III studied by NMR relaxation measurements. Carbohydr Res 1995; 268: 159-75.
    • (1995) Carbohydr Res , vol.268 , pp. 159-175
    • Hricovíni, M.1    Torri, G.2
  • 23
    • 27244432426 scopus 로고    scopus 로고
    • Dynamic properties of biologically active synthetic heparin-like hexasaccharides
    • Angulo J, Hricovíni M, Gairi M, Guerrini M, de Paz JL, Ojeda R, et al. Dynamic properties of biologically active synthetic heparin-like hexasaccharides. Glycobiology 2005; 15: 1008-15.
    • (2005) Glycobiology , vol.15 , pp. 1008-1015
    • Angulo, J.1    Hricovíni, M.2    Gairi, M.3    Guerrini, M.4    de Paz, J.L.5    Ojeda, R.6
  • 24
    • 0342684436 scopus 로고    scopus 로고
    • Motional properties of E. coli polysaccharide K5 in aqueous solution analyzed by NMR relaxation measurements
    • Hricovíni M, Guerrini M, Torri G, Casu B. Motional properties of E. coli polysaccharide K5 in aqueous solution analyzed by NMR relaxation measurements. Carbohydr Res 1997; 300: 69-76.
    • (1997) Carbohydr Res , vol.300 , pp. 69-76
    • Hricovíni, M.1    Guerrini, M.2    Torri, G.3    Casu, B.4
  • 25
    • 10744225880 scopus 로고    scopus 로고
    • Undersulfated and glycol-split heparins endowed with antiangiogenic activity
    • Casu B, Guerrini M, Guglieri S, Naggi A, Perez M, Torri G, et al. Undersulfated and glycol-split heparins endowed with antiangiogenic activity. J Med Chem 2004; 47: 838-48.
    • (2004) J Med Chem , vol.47 , pp. 838-848
    • Casu, B.1    Guerrini, M.2    Guglieri, S.3    Naggi, A.4    Perez, M.5    Torri, G.6
  • 28
    • 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: 1116-20.
    • (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
  • 29
    • 15744403559 scopus 로고    scopus 로고
    • Structural insights into biological roles of protein-glycosaminoglycan interactions
    • Raman R, Sasisekharan V, Sasisekharan R. Structural insights into biological roles of protein-glycosaminoglycan interactions. Chem Biol 2005; 12: 267-77.
    • (2005) Chem Biol , vol.12 , pp. 267-277
    • Raman, R.1    Sasisekharan, V.2    Sasisekharan, R.3
  • 30
    • 0035707396 scopus 로고    scopus 로고
    • Structure and biological interactions of heparin and heparan sulfate
    • Casu B, Lindahl U. Structure and biological interactions of heparin and heparan sulfate. Adv Carbohydr Chem Biochem 2001; 57: 159-206.
    • (2001) Adv Carbohydr Chem Biochem , vol.57 , pp. 159-206
    • Casu, B.1    Lindahl, U.2
  • 32
    • 2442549670 scopus 로고    scopus 로고
    • Interactions of heparin/ heparan sulfate with proteins: Appraisal of structural factors and experimental approaches
    • Powel AK, Yates EA, Fernig DG, Turnbull JE. Interactions of heparin/ heparan sulfate with proteins: Appraisal of structural factors and experimental approaches. Glycobiology 2004; 14: 17R-30R.
    • (2004) Glycobiology , vol.14
    • Powel, A.K.1    Yates, E.A.2    Fernig, D.G.3    Turnbull, J.E.4
  • 33
    • 0032566048 scopus 로고    scopus 로고
    • Structure of a heparin-linked biologically active dimer of fibroblast growth factor
    • DiGabriele AD, Lax I, Chen DI, Svahn CM, Jae M, Schlessinger J, et al. Structure of a heparin-linked biologically active dimer of fibroblast growth factor. Nature 1998; 393: 812-7.
    • (1998) Nature , vol.393 , pp. 812-817
    • DiGabriele, A.D.1    Lax, I.2    Chen, D.I.3    Svahn, C.M.4    Jae, M.5    Schlessinger, J.6
  • 34
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov AN, Schlessinger J, Hubbard SH, Mohammadi M. Structural basis for FGF receptor dimerization and activation. Cell 1999; 98: 641-50.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.H.3    Mohammadi, M.4
  • 35
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov AN, Hubbard SH, Schlessinger J, Mohammadi M. Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Cell 2000; 101: 413-24.
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.H.2    Schlessinger, J.3    Mohammadi, M.4
  • 36
    • 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: 1029-34
    • (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
  • 37
    • 0033058869 scopus 로고    scopus 로고
    • Solution structure of human acidic fibroblast growth factor and interaction with heparin-derived hexasaccharide
    • Ogura K, Nagata K, Hatanaka H, Habuchi H, Kimata K, Tate S, et al. Solution structure of human acidic fibroblast growth factor and interaction with heparin-derived hexasaccharide. J Biomol NMR 1999; 13: 11-24.
    • (1999) J Biomol NMR , vol.13 , pp. 11-24
    • Ogura, K.1    Nagata, K.2    Hatanaka, H.3    Habuchi, H.4    Kimata, K.5    Tate, S.6
  • 38
    • 0030890997 scopus 로고    scopus 로고
    • Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor
    • Moy FJ, Safran M, Seddon AP, Kitche D, Böhlen, P, Aviezer D, et al. Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor. Biochemistry 1997; 36: 4782-91.
    • (1997) Biochemistry , vol.36 , pp. 4782-4791
    • Moy, F.J.1    Safran, M.2    Seddon, A.P.3    Kitche, D.4    Böhlen, P.5    Aviezer, D.6
  • 39
    • 0031807320 scopus 로고    scopus 로고
    • Molecular modelling studies on binding of bFGF to heparin and its receptor FGFR1
    • Lam K, Rao VSR, Qasba PK. Molecular modelling studies on binding of bFGF to heparin and its receptor FGFR1. J Biomol Struct Dyn 1998; 15: 1009-27.
    • (1998) J Biomol Struct Dyn , vol.15 , pp. 1009-1027
    • Lam, K.1    Rao, V.S.R.2    Qasba, P.K.3
  • 40
    • 31544445500 scopus 로고    scopus 로고
    • Multimers of the fibroblast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin
    • Harmer NJ, Robinson CJ, Adam LE, Ilag LL, Robinson CV, Gallagher JT, et al. Multimers of the fibroblast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin. Biochem J 2006; 393: 741-8.
    • (2006) Biochem J , vol.393 , pp. 741-748
    • Harmer, N.J.1    Robinson, C.J.2    Adam, L.E.3    Ilag, L.L.4    Robinson, C.V.5    Gallagher, J.T.6
  • 41
    • 0030598354 scopus 로고    scopus 로고
    • Three-dimensional structure of acidic fibroblast growth factor in solution: Effects of binding to a heparin functional analog
    • Pineda-Lucena A, Jiménez MA, Lozano RM, Nieto JL, Santoro J, Rico M, et al. Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog. J Mol Biol 1996; 264: 162-78.
    • (1996) J Mol Biol , vol.264 , pp. 162-178
    • Pineda-Lucena, A.1    Jiménez, M.A.2    Lozano, R.M.3    Nieto, J.L.4    Santoro, J.5    Rico, M.6
  • 42
    • 0026011735 scopus 로고
    • Three-dimensional structures of acidic and basic fibroblast growth factors
    • Zhu X, Komiya H, Chirino A, Faham S, Fox GM, Arakawa T, et al. Three-dimensional structures of acidic and basic fibroblast growth factors. Science 1991; 251: 90-3.
    • (1991) Science , vol.251 , pp. 90-93
    • Zhu, X.1    Komiya, H.2    Chirino, A.3    Faham, S.4    Fox, G.M.5    Arakawa, T.6
  • 43
    • 0033658646 scopus 로고    scopus 로고
    • Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dipendent on specific structural features: Differential requirements for the modulation of FGF1 and FGF-2
    • Pey DA, Vives RR, Hyde P, Gallagher JT. Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dipendent on specific structural features: differential requirements for the modulation of FGF1 and FGF-2. Glycobiology 2000; 10: 1183.
    • (2000) Glycobiology , vol.10 , pp. 1183
    • Pey, D.A.1    Vives, R.R.2    Hyde, P.3    Gallagher, J.T.4
  • 44
    • 0347087449 scopus 로고    scopus 로고
    • The activation of fibroblast growth factors (FGFs) by glycosaminoglycans: Influence of the sulfation pattern on the biological activity of FGF-1
    • Angulo J, Ojeda R, Paz JL, Lucas R, Nieto PM, Lozano R, et al. The activation of fibroblast growth factors (FGFs) by glycosaminoglycans: influence of the sulfation pattern on the biological activity of FGF-1. Chembiochem 2004; 5: 55-61.
    • (2004) Chembiochem , vol.5 , pp. 55-61
    • Angulo, J.1    Ojeda, R.2    Paz, J.L.3    Lucas, R.4    Nieto, P.M.5    Lozano, R.6
  • 45
    • 20244368809 scopus 로고    scopus 로고
    • 0 conformations of a bioactive heparin-like hexasaccharide J Am Chem Soc 2005; 127: 5778-9.
    • 0 conformations of a bioactive heparin-like hexasaccharide J Am Chem Soc 2005; 127: 5778-9.
  • 46
    • 0034946994 scopus 로고    scopus 로고
    • A rational approach to heparin-related fragments 2 synthesis of differently sulfated tetrasaccharides as potential ligands for Fibroblast Growth Factors
    • Poletti L, Lay L, Fleischer M, Vogel C, Guerrini M, Torri G, et al. A rational approach to heparin-related fragments 2 synthesis of differently sulfated tetrasaccharides as potential ligands for Fibroblast Growth Factors. Eur J Org Chem 2001; 14: 2727-34.
    • (2001) Eur J Org Chem , vol.14 , pp. 2727-2734
    • Poletti, L.1    Lay, L.2    Fleischer, M.3    Vogel, C.4    Guerrini, M.5    Torri, G.6
  • 48
    • 0028068096 scopus 로고
    • Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble FGF receptor-1
    • Rusnati M, Coltrini D, Caccia P, Dell'Era P, Zoppetti G, Oreste P, et al. Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble FGF receptor-1. Biochem Biophys Res Commun 1994; 203: 450-8.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 450-458
    • Rusnati, M.1    Coltrini, D.2    Caccia, P.3    Dell'Era, P.4    Zoppetti, G.5    Oreste, P.6
  • 49
    • 0032483520 scopus 로고    scopus 로고
    • Heparan sulphate oligosaccharides require 6-O-sulfation for promotion of basic fibroblast growth factor mitogenic activity
    • Pye DA, Vives RR, Turnbull JE, Hyde P, Gallagher JT. Heparan sulphate oligosaccharides require 6-O-sulfation for promotion of basic fibroblast growth factor mitogenic activity. J Biol Chem 1998; 273: 22936-42.
    • (1998) J Biol Chem , vol.273 , pp. 22936-22942
    • Pye, D.A.1    Vives, R.R.2    Turnbull, J.E.3    Hyde, P.4    Gallagher, J.T.5
  • 50
    • 0032790340 scopus 로고    scopus 로고
    • A synthetic heparan sulfate pentasaccharide, exclusively containing L-Iduronic acid, displays higher affinity for FGF-2 its D-Glucuronic acid-containing isomers
    • Kovensky J, Duchaussoy P, Bono F, Salmivirta M, Sizun P, Herbert JM, et al. A synthetic heparan sulfate pentasaccharide, exclusively containing L-Iduronic acid, displays higher affinity for FGF-2 its D-Glucuronic acid-containing isomers. Bioorg Med Chem 1999; 7: 1567-80.
    • (1999) Bioorg Med Chem , vol.7 , pp. 1567-1580
    • Kovensky, J.1    Duchaussoy, P.2    Bono, F.3    Salmivirta, M.4    Sizun, P.5    Herbert, J.M.6
  • 51
    • 0037103725 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 binds to small heparin-derived oligosaccharides and stimulates a sustained phosphorylation of p42/44 mitogen-activated protein kinase and proliferation of rat mammary fibroblasts
    • Delehedde M, Lyon M, Gallagher JT, Rudland PS, Fernig DG. Fibroblast growth factor-2 binds to small heparin-derived oligosaccharides and stimulates a sustained phosphorylation of p42/44 mitogen-activated protein kinase and proliferation of rat mammary fibroblasts. Biochem J 2002; 366: 235-44.
    • (2002) Biochem J , vol.366 , pp. 235-244
    • Delehedde, M.1    Lyon, M.2    Gallagher, J.T.3    Rudland, P.S.4    Fernig, D.G.5
  • 52
    • 0033635299 scopus 로고    scopus 로고
    • Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization
    • Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, et al. Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. Molecular Cell 2000; 6: 743-50.
    • (2000) Molecular Cell , vol.6 , pp. 743-750
    • Schlessinger, J.1    Plotnikov, A.N.2    Ibrahimi, O.A.3    Eliseenkova, A.V.4    Yeh, B.K.5    Yayon, A.6
  • 53
    • 0029024317 scopus 로고
    • FGF binding and FGF receptor activation by synthetic heparan derived di- and tetrasaccharides
    • Ornitz MD, Herr AB, Nilsson M, Westman J, Svhan CM, Waksman G. FGF binding and FGF receptor activation by synthetic heparan derived di- and tetrasaccharides. Science 1995; 268: 432-6.
    • (1995) Science , vol.268 , pp. 432-436
    • Ornitz, M.D.1    Herr, A.B.2    Nilsson, M.3    Westman, J.4    Svhan, C.M.5    Waksman, G.6
  • 55
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signalling via EGF and FGF receptors
    • Schlessinger J. Common and distinct elements in cellular signalling via EGF and FGF receptors. Science 2004; 306: 1506-7.
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 56
    • 33748688639 scopus 로고    scopus 로고
    • Naggi A. Glycol-splitting as a device for modulating inhibition of growth factors and heparanase by heparin and heparin derivatives. In: Garg HG, Linhardt RJ, Hales CA Eds, Chemistry and biology of heparin and heparan sulfate. Elsevier 2005; 461.
    • Naggi A. Glycol-splitting as a device for modulating inhibition of growth factors and heparanase by heparin and heparin derivatives. In: Garg HG, Linhardt RJ, Hales CA Eds, Chemistry and biology of heparin and heparan sulfate. Elsevier 2005; 461.
  • 57
    • 18544372310 scopus 로고    scopus 로고
    • Short heparin sequences spaced by glycol-split uronate residues are antagonists of fibroblast growth factor 2 and angiogenesis inhibitors
    • Casu B, Guerrini M, Guglieri S, Naggi A, Perez M, Torri G, et al. Short heparin sequences spaced by glycol-split uronate residues are antagonists of fibroblast growth factor 2 and angiogenesis inhibitors. Biochem 2002; 41: 10519-28.
    • (2002) Biochem , vol.41 , pp. 10519-10528
    • Casu, B.1    Guerrini, M.2    Guglieri, S.3    Naggi, A.4    Perez, M.5    Torri, G.6
  • 58
    • 34447258097 scopus 로고    scopus 로고
    • Dynamics of heparin and heparin derivative spaced by glycol-split urinate residues analyzed by NMR relaxation measurements
    • Manuscript in preparation
    • Hricovíni M, Guerrini M, Naggi A, Torri G, Casu B. Dynamics of heparin and heparin derivative spaced by glycol-split urinate residues analyzed by NMR relaxation measurements. (Manuscript in preparation).
    • Hricovíni, M.1    Guerrini, M.2    Naggi, A.3    Torri, G.4    Casu, B.5
  • 59
    • 0029377157 scopus 로고
    • Complete relaxation and conformational exchange matrix (CORCEMA) analysis of NOESY spectra of interacting systems; two-dimensional transferred NOESY
    • Moseley HNB, Curto EV, Krishna NR. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of NOESY spectra of interacting systems; two-dimensional transferred NOESY. J Magn Reson 1995; B108: 243-61.
    • (1995) J Magn Reson , vol.B108 , pp. 243-261
    • Moseley, H.N.B.1    Curto, E.V.2    Krishna, N.R.3
  • 60
    • 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: 578-86.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 578-586
    • Faham, S.1    Linhardt, R.J.2    Rees, D.C.3
  • 61
    • 33748886858 scopus 로고    scopus 로고
    • B3LYP/6-311++G** study of structure and spin-spin coupling constant in methyl 2-O-sulfo-α-L-iduronate
    • Hricovini M. B3LYP/6-311++G** study of structure and spin-spin coupling constant in methyl 2-O-sulfo-α-L-iduronate. Carbohydr Res 2006; 341: 2575-80.
    • (2006) Carbohydr Res , vol.341 , pp. 2575-2580
    • Hricovini, M.1
  • 62
    • 27844537859 scopus 로고    scopus 로고
    • Molecular mechanisms of and possible treatment strategies for idiopathic pulmonary fibrosis
    • Gharaee-Kermani M, Phan SH. Molecular mechanisms of and possible treatment strategies for idiopathic pulmonary fibrosis. Curr Pharm Des 2005; 11(30): 3943-71.
    • (2005) Curr Pharm Des , vol.11 , Issue.30 , pp. 3943-3971
    • Gharaee-Kermani, M.1    Phan, S.H.2
  • 63
    • 21044433780 scopus 로고    scopus 로고
    • Biotechnological engineering of heparin/heparan sulphate: A novel area of multi-target drug discovery
    • Rusnati M, Oreste P, Zoppetti G, Presta M. Biotechnological engineering of heparin/heparan sulphate: a novel area of multi-target drug discovery. Curr Pharm Des 2005; 11(19): 2489-99.
    • (2005) Curr Pharm Des , vol.11 , Issue.19 , pp. 2489-2499
    • Rusnati, M.1    Oreste, P.2    Zoppetti, G.3    Presta, M.4
  • 64
    • 33750538244 scopus 로고    scopus 로고
    • Protein NMR-based screening in drug discovery
    • Zartler ER, Shapiro MJ. Protein NMR-based screening in drug discovery. Curr Pharm Des 2006; 12(31): 3963-72.
    • (2006) Curr Pharm Des , vol.12 , Issue.31 , pp. 3963-3972
    • Zartler, E.R.1    Shapiro, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.