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Volumn 281, Issue 5, 1998, Pages 899-915

Solution structure of acidic fibroblast growth factor bound to 1,3,6-naphthalenetrisulfonate: A minimal model for the anti-tumoral action of suramins and suradistas

Author keywords

Angiogenesis inhibitors; Anti angiogenic tumour therapy; Fibroblast growth factors; Suradistas; Suramin

Indexed keywords

ACIDIC FIBROBLAST GROWTH FACTOR; HEPARIN; NAPHTHALENESULFONIC ACID DERIVATIVE; SURADISTA; SURAMIN; UNCLASSIFIED DRUG;

EID: 0032483474     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1977     Document Type: Article
Times cited : (53)

References (71)
  • 1
    • 0006393051 scopus 로고
    • Two-dimensional spectroscopy. Application to nuclear magnetic resonance
    • Aue W.P., Bartholdi E., Ernst R.R. Two-dimensional spectroscopy. Application to nuclear magnetic resonance. J. Chem. Phys. 64:1976;2229-2246
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bartholdi, E.2    Ernst, R.R.3
  • 3
    • 5144233105 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax A., Davies D. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 65:1985;355-360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davies, D.2
  • 4
    • 0001625717 scopus 로고
    • New heterocyclic analogs of suramin with bFGF inhibiting activity. Synthesis, SAR and possible mode of action
    • Biasoli G., Botta M., Ciomei M., Corelli F., Grandi M., Manetti F., Mongelli N., Paio A. New heterocyclic analogs of suramin with bFGF inhibiting activity. Synthesis, SAR and possible mode of action. Med. Chem. Res. 4:1993;202-210
    • (1993) Med. Chem. Res. , vol.4 , pp. 202-210
    • Biasoli, G.1    Botta, M.2    Ciomei, M.3    Corelli, F.4    Grandi, M.5    Manetti, F.6    Mongelli, N.7    Paio, A.8
  • 5
    • 0028345444 scopus 로고
    • A structure-activity analysis of antagonism of the growthfactor and angiogenic activity of basic fibroblast growth factorby suramin and related polyanions
    • Braddock P.S., Hu D.-E., Fan T.-P.D., Stratford I.J., Harris A.L., Bicknell R. A structure-activity analysis of antagonism of the growthfactor and angiogenic activity of basic fibroblast growth factorby suramin and related polyanions. Brit. J. Cancer. 69:1994;890-898
    • (1994) Brit. J. Cancer. , vol.69 , pp. 890-898
    • Braddock, P.S.1    Hu, D.-E.2    Fan, T.-P.D.3    Stratford, I.J.4    Harris, A.L.5    Bicknell, R.6
  • 6
    • 0024339705 scopus 로고
    • The heparin-binding (fibroblast) growth factor family of proteins
    • Burgess W.H., Maciag T. The heparin-binding (fibroblast) growth factor family of proteins. Annu. Rev. Biochem. 58:1989;575-606
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 575-606
    • Burgess, W.H.1    MacIag, T.2
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 10
    • 0031024921 scopus 로고    scopus 로고
    • Of worms and men: An evolutionary perspective on the fibroblast growth factor (FGF) and FGF receptor families
    • Coulier F., Pontarotti P., Roubin R., Hartung H., Goldfarb M., Birnbaum D. Of worms and men an evolutionary perspective on the fibroblast growth factor (FGF) and FGF receptor families. J. Mol. Evol. 44:1997;43-56
    • (1997) J. Mol. Evol. , vol.44 , pp. 43-56
    • Coulier, F.1    Pontarotti, P.2    Roubin, R.3    Hartung, H.4    Goldfarb, M.5    Birnbaum, D.6
  • 11
    • 0030498734 scopus 로고    scopus 로고
    • Angiogenesis and metastasis
    • Ellis L.M., Fidler I.J. Angiogenesis and metastasis. Eur. J. Cancer. 32A:1996;2451-2460
    • (1996) Eur. J. Cancer , vol.32 , pp. 2451-2460
    • Ellis, L.M.1    Fidler, I.J.2
  • 13
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • Faham S., Hileman R.E., Fromm J.R., Linhardt R.J., Rees D.C. Heparin structure and interactions with basic fibroblast growth factor. Science. 271:1996;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
    • 85013312416 scopus 로고
    • Tumor angiogenesis: Therapeutic implications
    • Folkman J. Tumor angiogenesis therapeutic implications. New Engl. J. Med. 285:1971;1182-1186
    • (1971) New Engl. J. Med. , vol.285 , pp. 1182-1186
    • Folkman, J.1
  • 15
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman J. Angiogenesis in cancer, vascular, rheumatoid and other disease. Nature Med. 1:1995;27-31
    • (1995) Nature Med. , vol.1 , pp. 27-31
    • Folkman, J.1
  • 16
    • 0023157363 scopus 로고
    • Angiogenic factors
    • Folkman J., Klagsbrun M. Angiogenic factors. Science. 235:1987;442-447
    • (1987) Science , vol.235 , pp. 442-447
    • Folkman, J.1    Klagsbrun, M.2
  • 17
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana A., Fassina G., Vita C., Dalzoppo D., Moreno Z., Zambonin M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry. 25:1986;1847-1851
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Moreno, Z.5    Zambonin, M.6
  • 18
    • 0031572867 scopus 로고    scopus 로고
    • Interaction of fibroblast growth factor-1 and related peptides with heparan sulfate and its oligosaccharides
    • Fromm J.R., Hileman R.E., Weiler J.M., Linhardt R.J. Interaction of fibroblast growth factor-1 and related peptides with heparan sulfate and its oligosaccharides. Arch. Biochem. Biophys. 346:1997;252-262
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 252-262
    • Fromm, J.R.1    Hileman, R.E.2    Weiler, J.M.3    Linhardt, R.J.4
  • 19
    • 0026799316 scopus 로고
    • Inhibition of angiogenesis by suramin
    • Gagliardi A., Hadd H., Collins D.C. Inhibition of angiogenesis by suramin. Cancer Res. 52:1992;5073-5075
    • (1992) Cancer Res. , vol.52 , pp. 5073-5075
    • Gagliardi, A.1    Hadd, H.2    Collins, D.C.3
  • 21
    • 0028939826 scopus 로고
    • Clinical importance of the determination of tumor angiogenesis in breast carcinoma: Much more than a new prognostic tool
    • Gasparini G., Harris A.L. Clinical importance of the determination of tumor angiogenesis in breast carcinoma much more than a new prognostic tool. J. Clin. Oncol. 13:1995;765-782
    • (1995) J. Clin. Oncol. , vol.13 , pp. 765-782
    • Gasparini, G.1    Harris, A.L.2
  • 22
    • 0028486240 scopus 로고
    • Fibroblast growth factor, a protein with a broad spectrum of biological activities
    • Giménez-Gallego G., Cuevas P. Fibroblast growth factor, a protein with a broad spectrum of biological activities. Neurolog. Res. 16:1994;313-316
    • (1994) Neurolog. Res. , vol.16 , pp. 313-316
    • Giménez-Gallego, G.1    Cuevas, P.2
  • 23
    • 0022452713 scopus 로고
    • Human brain-derived acidic and basic fibroblast growth factors: Amino terminal sequences and specific mitogenic activities
    • Giménez-Gallego G., Con G., Hatcher V.B., Thomas K.A. Human brain-derived acidic and basic fibroblast growth factors amino terminal sequences and specific mitogenic activities. Biochem. Biophys. Res. Commun. 135:1986;541-548
    • (1986) Biochem. Biophys. Res. Commun. , vol.135 , pp. 541-548
    • Giménez-Gallego, G.1    Con, G.2    Hatcher, V.B.3    Thomas, K.A.4
  • 24
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • Güntert P., Wüthrich K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J. Biomol. NMR. 1:1991;447-456
    • (1991) J. Biomol. NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 25
    • 0026089657 scopus 로고
    • Efficient computation of the three-dimensional protein structures from NMR using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert P., Braun W., Wüthrich K. Efficient computation of the three-dimensional protein structures from NMR using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217:1991;517-530
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 26
    • 0030708525 scopus 로고    scopus 로고
    • Discovering high affinity ligands for proteins
    • Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high affinity ligands for proteins. Science. 278:1997;497-499
    • (1997) Science , vol.278 , pp. 497-499
    • Hajduk, P.J.1    Meadows, R.P.2    Fesik, S.W.3
  • 28
    • 0026319891 scopus 로고
    • Suppression of solid tumor growth by immunoneutralizing monoclonal antibody aganist human basic fibroblast growth factor
    • Hori A., Sasada R., Matsutani E., Naito K., Sakura Y., Fujita T., Kozai Y. Suppression of solid tumor growth by immunoneutralizing monoclonal antibody aganist human basic fibroblast growth factor. Cancer Res. 51:1991;6180-6184
    • (1991) Cancer Res. , vol.51 , pp. 6180-6184
    • Hori, A.1    Sasada, R.2    Matsutani, E.3    Naito, K.4    Sakura, Y.5    Fujita, T.6    Kozai, Y.7
  • 29
    • 0026649742 scopus 로고
    • Fibroblast growth factor receptor tyrosine kinases: Molecular analysis and signal transduction
    • Jaye M., Schlessinger J., Dionne C.A. Fibroblast growth factor receptor tyrosine kinases molecular analysis and signal transduction. Biochim. Biophys. Acta. 1135:1992;185-199
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 185-199
    • Jaye, M.1    Schlessinger, J.2    Dionne, C.A.3
  • 30
    • 0030767269 scopus 로고    scopus 로고
    • Cell release of bioactive fibroblast growth factor 2 by exon 6-encoded sequence of vascular endothelial growth factor
    • Jonca F., Ortega N., Gleizes P.E., Bertrand N., Plouet J. Cell release of bioactive fibroblast growth factor 2 by exon 6-encoded sequence of vascular endothelial growth factor. J. Biol. Chem. 272:1997;24203-24209
    • (1997) J. Biol. Chem. , vol.272 , pp. 24203-24209
    • Jonca, F.1    Ortega, N.2    Gleizes, P.E.3    Bertrand, N.4    Plouet, J.5
  • 31
    • 0027995683 scopus 로고
    • Detection, delineation, measurement ad display of cavities in macromolecular structures
    • Kleywegt G., Jones A. Detection, delineation, measurement ad display of cavities in macromolecular structures. Acta Crystallog. sect. D. 50:1994;178-185
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.1    Jones, A.2
  • 32
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R.R., Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 33
    • 0030738390 scopus 로고    scopus 로고
    • Destabilization, oligomerization and inhibition of the mitogenic activity of acidic fibroblast growth factor by aurintricarboxylic acid
    • Lozano R.M., Rivas G., Giménez-Gallego G. Destabilization, oligomerization and inhibition of the mitogenic activity of acidic fibroblast growth factor by aurintricarboxylic acid. Eur. J. Biochem. 248:1997;30-36
    • (1997) Eur. J. Biochem. , vol.248 , pp. 30-36
    • Lozano, R.M.1    Rivas, G.2    Giménez-Gallego, G.3
  • 34
    • 0030848490 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-induced in vitro angiogenesis and plasminogen activator expression are dependent on endogenous basic fibroblast growth factor
    • Mandriota S.J., Pepper M.S. Vascular endothelial growth factor-induced in vitro angiogenesis and plasminogen activator expression are dependent on endogenous basic fibroblast growth factor. J. Cell Sci. 110:1997;2293-2302
    • (1997) J. Cell Sci. , vol.110 , pp. 2293-2302
    • Mandriota, S.J.1    Pepper, M.S.2
  • 36
    • 0021114895 scopus 로고
    • Application of phase-sensitive two-dimensional correlated spectroscopy (COSY) for measurement of proton-proton spin-spin coupling constants
    • Marion D., Wüthrich K. Application of phase-sensitive two-dimensional correlated spectroscopy (COSY) for measurement of proton-proton spin-spin coupling constants. Biochem. Biophys. Res. Commun. 113:1983;967-974
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 39
    • 0026556882 scopus 로고
    • β-Trefoil fold. Patters of structure and sequence in the Kunitz inhibitors, interleukins-1β and 1α and fibroblast growth factors
    • Murzin A.G., Lesk A.M., Chothia C. β-Trefoil fold. Patters of structure and sequence in the Kunitz inhibitors, interleukins-1β and 1α and fibroblast growth factors. J. Mol. Biol. 233:1992;531-543
    • (1992) J. Mol. Biol. , vol.233 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 41
    • 0026502460 scopus 로고
    • Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells
    • Ornitz D.M., Yayon A., Flanagan J.G., Svahn C.M., Levi E., Leder P. Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells. Mol. Cell. Biol. 12:1992;240-247
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 240-247
    • Ornitz, D.M.1    Yayon, A.2    Flanagan, J.G.3    Svahn, C.M.4    Levi, E.5    Leder, P.6
  • 42
    • 0027989479 scopus 로고
    • Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization
    • Pantoliano M.W., Horlick R.A., Springer B.A., Van Dyk D.E., Tobery T., Wetmore D.R., Lear J.D., Nahapetian A.T., Bradley J.D., Sisk W.P. Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization. Biochemistry. 33:1994;10229-10248
    • (1994) Biochemistry , vol.33 , pp. 10229-10248
    • Pantoliano, M.W.1    Horlick, R.A.2    Springer, B.A.3    Van Dyk, D.E.4    Tobery, T.5    Wetmore, D.R.6    Lear, J.D.7    Nahapetian, A.T.8    Bradley, J.D.9    Sisk, W.P.10
  • 43
    • 0026729378 scopus 로고
    • Suramin prevents neovascularisation and tumour growth through blocking of basic fibroblast growth factor activity
    • Pesenti E., Sola F., Mongelli N., Grandi M., Spreafico F. Suramin prevents neovascularisation and tumour growth through blocking of basic fibroblast growth factor activity. Brit. J. Cancer. 66:1992;367-372
    • (1992) Brit. J. Cancer , vol.66 , pp. 367-372
    • Pesenti, E.1    Sola, F.2    Mongelli, N.3    Grandi, M.4    Spreafico, F.5
  • 46
    • 0030598354 scopus 로고    scopus 로고
    • Three-dimensional structure of the acidic fibroblast growth factor in solution: Effects of binding to a heparin funcional analogue
    • Pineda-Lucena A., Jiménez M.A., Lozano R.M., Nieto J.L., Santoro J., Rico M., Giménez-Gallego G. Three-dimensional structure of the acidic fibroblast growth factor in solution effects of binding to a heparin funcional analogue. J. Mol. Biol. 264:1996;162-178
    • (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    Giménez-Gallego, G.7
  • 48
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 6:1992;661-665
    • (1992) J. Biomol. NMR , vol.6 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 50
    • 0025835670 scopus 로고
    • Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
    • Rapraeger A.C., Krufka A., Olwin B.B. Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation. Science. 252:1991;1705-1708
    • (1991) Science , vol.252 , pp. 1705-1708
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 51
    • 0031038068 scopus 로고    scopus 로고
    • Expression of the angiogenic factors vascular endothelial cell growth factor, acidic and basic fibroblast growth factor, tumor growth factor beta-1, platelet-derived endothelial cell growth factor, placenta growth factor, and pleiotropin in human primary breast cancer and its relation to angiogenesis
    • Relf M., LeJeune S., Scott P.A.E., Fox S., Smith K., Leek R., Moghaddam A., Whitehouse R., Bicknell R., Harris A.L. Expression of the angiogenic factors vascular endothelial cell growth factor, acidic and basic fibroblast growth factor, tumor growth factor beta-1, platelet-derived endothelial cell growth factor, placenta growth factor, and pleiotropin in human primary breast cancer and its relation to angiogenesis. Cancer Res. 57:1997;963-969
    • (1997) Cancer Res. , vol.57 , pp. 963-969
    • Relf, M.1    Lejeune, S.2    Scott, P.A.E.3    Fox, S.4    Smith, K.5    Leek, R.6    Moghaddam, A.7    Whitehouse, R.8    Bicknell, R.9    Harris, A.L.10
  • 52
    • 0028023801 scopus 로고
    • Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding
    • Roghani M., Mansukhani A., Dell'Era P., Bellosta P., Basilico C., Rifkin D.B., Moscatelli D. Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding. J. Biol. Chem. 269:1994;3976-3984
    • (1994) J. Biol. Chem. , vol.269 , pp. 3976-3984
    • Roghani, M.1    Mansukhani, A.2    Dell'Era, P.3    Bellosta, P.4    Basilico, C.5    Rifkin, D.B.6    Moscatelli, D.7
  • 53
    • 0029858290 scopus 로고    scopus 로고
    • X-ray analysis structure of native full length human fibroblast growth factor at 0.25 nm resolution
    • Romero A., Pineda-Lucena A., Giménez-Gallego G. X-ray analysis structure of native full length human fibroblast growth factor at 0.25 nm resolution. Eur. J. Biochem. 241:1996;453-461
    • (1996) Eur. J. Biochem. , vol.241 , pp. 453-461
    • Romero, A.1    Pineda-Lucena, A.2    Giménez-Gallego, G.3
  • 54
    • 0024505467 scopus 로고
    • Parmacokinetics and distribution of heparin-binding growth factor I (endothelial cell growth factor) in the rat
    • Rosengart T.K., Kuperschmid J.P., Maciag T., Clark R. Parmacokinetics and distribution of heparin-binding growth factor I (endothelial cell growth factor) in the rat. Circ. Res. 64:1989;227-234
    • (1989) Circ. Res. , vol.64 , pp. 227-234
    • Rosengart, T.K.1    Kuperschmid, J.P.2    MacIag, T.3    Clark, R.4
  • 55
    • 0031035987 scopus 로고    scopus 로고
    • Angiogenesis in colorectal cancer
    • Saclarides T.J. Angiogenesis in colorectal cancer. Surg. Clin. North America. 77:1997;253-260
    • (1997) Surg. Clin. North America , vol.77 , pp. 253-260
    • Saclarides, T.J.1
  • 59
    • 0027298410 scopus 로고
    • Suramin: A novel antineoplasic agent with multiple potential mechanisms of action
    • Stein C.A. Suramin a novel antineoplasic agent with multiple potential mechanisms of action. Cancer Res. 53:1993;2239-2248
    • (1993) Cancer Res. , vol.53 , pp. 2239-2248
    • Stein, C.A.1
  • 60
    • 0028318791 scopus 로고
    • Suramin, an anticancer and angiosuppressive agent, inhibits endothelial cell binding of basic fibroblast growth factor, migration, proliferation, and induction of urokinase-type plasminogen activator
    • Takano S., Gately S., Neville M.E., Herblin W.F., Gross J.L., Engelhard H., Perricone M., Eidsvoog K., Brem S. Suramin, an anticancer and angiosuppressive agent, inhibits endothelial cell binding of basic fibroblast growth factor, migration, proliferation, and induction of urokinase-type plasminogen activator. Cancer Res. 54:1994;2654-2660
    • (1994) Cancer Res. , vol.54 , pp. 2654-2660
    • Takano, S.1    Gately, S.2    Neville, M.E.3    Herblin, W.F.4    Gross, J.L.5    Engelhard, H.6    Perricone, M.7    Eidsvoog, K.8    Brem, S.9
  • 61
    • 0011293081 scopus 로고
    • Pure brain-derived acidic fibroblast growth factor is a potent angiogenic vascular endothelial cell mitogen with sequence homology to interleukin 1
    • Thomas K.A., Rios-Candelore M., Giménez-Gallego G., DiSalvo J., Bennett C., Rodkey J., Fitzpatrick S. Pure brain-derived acidic fibroblast growth factor is a potent angiogenic vascular endothelial cell mitogen with sequence homology to interleukin 1. Proc. Natl. Acd. Sci. USA. 82:1985;6409-6413
    • (1985) Proc. Natl. Acd. Sci. USA , vol.82 , pp. 6409-6413
    • Thomas, K.A.1    Rios-Candelore, M.2    Giménez-Gallego, G.3    Disalvo, J.4    Bennett, C.5    Rodkey, J.6    Fitzpatrick, S.7
  • 62
    • 0028218987 scopus 로고
    • Energetic characterization of the basic fibroblast growth factor heparin interaction: Identification of the heparin binding domain
    • Thompson L.D., Pantoliano M.W., Springer B.A. Energetic characterization of the basic fibroblast growth factor heparin interaction identification of the heparin binding domain. Biochemistry. 33:1994;3831-3840
    • (1994) Biochemistry , vol.33 , pp. 3831-3840
    • Thompson, L.D.1    Pantoliano, M.W.2    Springer, B.A.3
  • 63
    • 0029912061 scopus 로고    scopus 로고
    • Inhibitors of angiogenesis in a clinical perpective
    • Voest E.E. Inhibitors of angiogenesis in a clinical perpective. Anti-Cancer Drugs. 7:1996;723-727
    • (1996) Anti-Cancer Drugs , vol.7 , pp. 723-727
    • Voest, E.E.1
  • 65
    • 0030855812 scopus 로고    scopus 로고
    • Antisense targeting of basic fibroblast growth factor and fibroblast growth factor receptor-1 in human melanomas blocks intratumoral angiogenesis and tumor growth
    • Wang Y., Becker D. Antisense targeting of basic fibroblast growth factor and fibroblast growth factor receptor-1 in human melanomas blocks intratumoral angiogenesis and tumor growth. Nat. Med. 3:1997;887-893
    • (1997) Nat. Med. , vol.3 , pp. 887-893
    • Wang, Y.1    Becker, D.2
  • 67
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wüthrich K., Billeter M., Braun W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J. Mol. Biol. 180:1984;715-740
    • (1984) J. Mol. Biol. , vol.180 , pp. 715-740
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 68
    • 0025090695 scopus 로고
    • Autocrine transformation by chimeric signal peptide-basic fibroblast growth factor: Reversal by suramin
    • Yayon A., Klagsbrun M. Autocrine transformation by chimeric signal peptide-basic fibroblast growth factor reversal by suramin. Proc. Natl Acad. Sci. USA. 87:1990;5346-5350
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5346-5350
    • Yayon, A.1    Klagsbrun, M.2
  • 69
    • 0025976838 scopus 로고
    • Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
    • Yayon A., Klagsbrun M., Esko J.D., Leder P., Ornitz D.M. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell. 64:1991;841-848
    • (1991) Cell , vol.64 , pp. 841-848
    • Yayon, A.1    Klagsbrun, M.2    Esko, J.D.3    Leder, P.4    Ornitz, D.M.5
  • 70
    • 0002053270 scopus 로고    scopus 로고
    • Antiangiogenic naptalene sulfonic distamycin-A derivatives tightly interact with basic fibroblast growth factor
    • Zamai M., Parola A.H., Grandi M., Mongelli N., Caiolfa V.R. Antiangiogenic naptalene sulfonic distamycin-A derivatives tightly interact with basic fibroblast growth factor. Med. Chem. Res. 7:1997;36-44
    • (1997) Med. Chem. Res. , vol.7 , pp. 36-44
    • Zamai, M.1    Parola, A.H.2    Grandi, M.3    Mongelli, N.4    Caiolfa, V.R.5
  • 71
    • 0026577745 scopus 로고
    • High-level synthesis in Escherichia coli of shortened and full-length human acidic fibroblast growth factor and purification in a form stable in aqueous solutions
    • Zazo M., Lozano R.M., Ortega S., Varela J., Díaz-Orejas R., Ramírez J.M., Giménez-Gallego G. High-level synthesis in Escherichia coli of shortened and full-length human acidic fibroblast growth factor and purification in a form stable in aqueous solutions. Gene. 113:1992;231-238
    • (1992) Gene , vol.113 , pp. 231-238
    • Zazo, M.1    Lozano, R.M.2    Ortega, S.3    Varela, J.4    Díaz-Orejas, R.5    Ramírez, J.M.6    Giménez-Gallego, G.7


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