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Volumn 46, Issue 12, 2003, Pages 2325-2333

Introduction of a chemical constraint in a short peptide derived from human acidic fibroblast growth factor elicits mitogenic structural determinants

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINYLLYSYLLYSYLHISTIDYLCYSTEINYLGLUTAMINYLLYSYLASPARAGINYLTRYPTOP HYLPHENYLALANINAMIDE; ACIDIC FIBROBLAST GROWTH FACTOR; PEPTIDE; SERYLLYSYLLYSYLHISTIDYLALANYLGLUTAMINYLLYSYLASPARAGINYLTRYPTOPHYLPHENYLALAN INAMIDE; UNCLASSIFIED DRUG;

EID: 0038101402     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm020543e     Document Type: Article
Times cited : (19)

References (67)
  • 1
    • 0033662360 scopus 로고    scopus 로고
    • Fibroblast growth factors and their inhibitors
    • Manetti, F.; Corelli, F.; Botta, M. Fibroblast growth factors and their inhibitors. Curr. Pharm. Des. 2000, 6, 1897-1924.
    • (2000) Curr. Pharm. Des. , vol.6 , pp. 1897-1924
    • Manetti, F.1    Corelli, F.2    Botta, M.3
  • 2
    • 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. 1989, 58, 575-606.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 575-606
    • Burgess, W.H.1    Maciag, T.2
  • 3
    • 0025738048 scopus 로고
    • The fibroblast growth factor family
    • Baird, A.; Klagsbrun, M. The fibroblast growth factor family. Cancer Cells 1990, 3, 239-243.
    • (1990) Cancer Cells , vol.3 , pp. 239-243
    • Baird, A.1    Klagsbrun, M.2
  • 4
    • 0023157363 scopus 로고
    • Angiogenic factors
    • Folkman, J.; Klagsbrun, M. Angiogenic factors. Science 1987, 235, 442-447.
    • (1987) Science , vol.235 , pp. 442-447
    • Folkman, J.1    Klagsbrun, M.2
  • 5
    • 0026649742 scopus 로고
    • Fibroblast growth factor receptor tyrosine kninases: Molecular analysis and signal transduction
    • Jaye, M.; Schlessinger, J.; Dionne, C. A. Fibroblast growth factor receptor tyrosine kninases: molecular analysis and signal transduction. Biochim. Biophys. Acta 1992, 1135, 185-199.
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 185-199
    • Jaye, M.1    Schlessinger, J.2    Dionne, C.A.3
  • 6
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ulrich, A.; Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990, 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ulrich, A.1    Schlessinger, J.2
  • 7
    • 0031600117 scopus 로고    scopus 로고
    • The heparan sulfatefibroblast growth factor family: Diversity of structure and function
    • McKeehan, W. L.; Wang, F.; Kan, M. The heparan sulfatefibroblast growth factor family: diversity of structure and function. Prog. Nucleic Acid Res. Mol. Biol. 1998, 59, 135-173.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.59 , pp. 135-173
    • McKeehan, W.L.1    Wang, F.2    Kan, M.3
  • 8
    • 0023831047 scopus 로고
    • A heparin-binding angiogenic protein - Basic fibroblast growth factor - Is stored within basement-membrane
    • Folkman, J.; Klagsbrun, M.; Sasse, J.; Wadzinski, M.; Ingber, D.; Vlodavsky, I. A heparin-binding angiogenic protein - basic fibroblast growth factor - is stored within basement-membrane. Am. J. Pathol. 1988, 130, 393-400.
    • (1988) Am. J. Pathol. , vol.130 , pp. 393-400
    • Folkman, J.1    Klagsbrun, M.2    Sasse, J.3    Wadzinski, M.4    Ingber, D.5    Vlodavsky, I.6
  • 9
    • 0025812425 scopus 로고
    • Extracellular sequestration and release of fibroblast growth factor: A regulatory mechanism?
    • Vlodavsky, I. Extracellular sequestration and release of fibroblast growth factor: a regulatory mechanism? Trends Biochem. Sci. 1991, 16, 268-271.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 268-271
    • Vlodavsky, I.1
  • 10
    • 0022477372 scopus 로고
    • Heparin protects basic and acidic fibroblast growth factors from inactivation
    • Gospodarowicz, D.; Cheng, J. Heparin protects basic and acidic fibroblast growth factors from inactivation. J. Cell. Physiol. 1986, 128, 475-484.
    • (1986) J. Cell. Physiol. , vol.128 , pp. 475-484
    • Gospodarowicz, D.1    Cheng, J.2
  • 11
    • 0024579448 scopus 로고
    • Interaction of heparin with human basic fibroblast growth factor: Protection of the angiogenic protein from proteolytic degradation by glucosaminoglycan
    • Sommer, A.; Rifkin, D. B. Interaction of heparin with human basic fibroblast growth factor: protection of the angiogenic protein from proteolytic degradation by glucosaminoglycan. J. Cell. Physiol. 1989, 138, 215-220.
    • (1989) J. Cell. Physiol. , vol.138 , pp. 215-220
    • Sommer, A.1    Rifkin, D.B.2
  • 12
    • 0029024317 scopus 로고
    • FGF binding and FGF receptor activation by synthetic heparan-derived di- and tri-saccharides
    • Ornitz, D. M.; Herr, H. B.; Nilsson, M.; Westman, J.; Svahn, C. M.; Waksman, G. FGF binding and FGF receptor activation by synthetic heparan-derived di- and tri-saccharides. Science 1995, 268, 432-436.
    • (1995) Science , vol.268 , pp. 432-436
    • Ornitz, D.M.1    Herr, H.B.2    Nilsson, M.3    Westman, J.4    Svahn, C.M.5    Waksman, G.6
  • 14
    • 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.; Sysk, 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 1994, 33, 10229-19248.
    • (1994) Biochemistry , vol.33 , pp. 10229-19248
    • 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    Sysk, W.P.10
  • 16
    • 12444334153 scopus 로고    scopus 로고
    • Molecular modeling as a powerful tool for the mapping of fibroblast growth factor receptor-1 ligand binding determinants
    • Oyama, S., Jr.; Miranda, M. T. M.; Kiyota, S.; Gambarini, A. G. Molecular modeling as a powerful tool for the mapping of fibroblast growth factor receptor-1 ligand binding determinants. J. Mol. Model. 1999, 5, 90-96.
    • (1999) J. Mol. Model. , vol.5 , pp. 90-96
    • Oyama S., Jr.1    Miranda, M.T.M.2    Kiyota, S.3    Gambarini, A.G.4
  • 18
    • 0033616671 scopus 로고    scopus 로고
    • Molecular characteristics of fibroblast growth factor-fibroblast growth factor receptor-heparin-like glycosaminoglycan complex
    • Ventakaran, 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. U.S.A. 1999, 96, 3658-3663.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3658-3663
    • Ventakaran, G.1    Raman, R.2    Sasisekharan, V.3    Sasisekharan, R.4
  • 19
    • 0033152903 scopus 로고    scopus 로고
    • A dimeric ternary complex of FGFR1, heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding
    • Huhtala, M. T.; Penkainen, O.; Johnson, M. S. A dimeric ternary complex of FGFR1, heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding. Structure 1999, 7, 699-709.
    • (1999) Structure , vol.7 , pp. 699-709
    • Huhtala, M.T.1    Penkainen, O.2    Johnson, M.S.3
  • 21
    • 0027192075 scopus 로고
    • An essential heparin-binding domain in the fibroblast growth factor receptor kinase
    • Kan, M.; Wang, F.; Xu, J.; Crabb, J. W.; Hou, J.; McKeehan, W. L. An essential heparin-binding domain in the fibroblast growth factor receptor kinase. Science 1993, 259, 1918-1921.
    • (1993) Science , vol.259 , pp. 1918-1921
    • Kan, M.1    Wang, F.2    Xu, J.3    Crabb, J.W.4    Hou, J.5    McKeehan, W.L.6
  • 22
    • 0030031438 scopus 로고    scopus 로고
    • X-ray crystal structure of human acidic fibroblast growth factor
    • Blaber, M.; DiSalvo, J.; Thomas, K. A. X-ray crystal structure of human acidic fibroblast growth factor. Biochemistry 1996, 35, 2086-2094.
    • (1996) Biochemistry , vol.35 , pp. 2086-2094
    • Blaber, M.1    DiSalvo, J.2    Thomas, K.A.3
  • 24
    • 0029610777 scopus 로고
    • Chimeric molecules between keratinocyte growth factor and basic fibroblast growth factor define domains that confer receptor binding specificity
    • Reich-Slottky, R.; Shaoul, E.; Berman, B.; Graziani, G.; Ron, D. Chimeric molecules between keratinocyte growth factor and basic fibroblast growth factor define domains that confer receptor binding specificity. J. Biol. Chem. 1995, 270, 29813-29818.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29813-29818
    • Reich-Slottky, R.1    Shaoul, E.2    Berman, B.3    Graziani, G.4    Ron, D.5
  • 25
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini, L.; Burke, D. F.; von Delft, F.; Mulloy, B.; Blundell, T. L. 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
  • 26
    • 9544230725 scopus 로고    scopus 로고
    • Mitogenic activity of peptides related to the sequence of human fibroblast growth factor-1
    • Oyama, S., Jr.; Miranda, M. T. M.; Toma, I. N.; Viviani, W.; Gambarinin, A. Mitogenic activity of peptides related to the sequence of human fibroblast growth factor-1. Biochem. Mol. Biol. Int. 1996, 39, 1237-1244.
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 1237-1244
    • Oyama S., Jr.1    Miranda, M.T.M.2    Toma, I.N.3    Viviani, W.4    Gambarinin, A.5
  • 27
    • 0035187229 scopus 로고    scopus 로고
    • Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a b-trefoil
    • Brych, S. R.; Blaber, S. I.; Logan, T. M.; Blaber, M. Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a b-trefoil. Protein Sci. 2001, 10, 2587-2599.
    • (2001) Protein Sci. , vol.10 , pp. 2587-2599
    • Brych, S.R.1    Blaber, S.I.2    Logan, T.M.3    Blaber, M.4
  • 29
    • 0029831680 scopus 로고    scopus 로고
    • An automated approach for clustering an ensemble of NMR-derived structures into conformationally related subfamilies
    • Kelly, L. A.; Gardner, S. P.; Sutcliffe, M. J. An automated approach for clustering an ensemble of NMR-derived structures into conformationally related subfamilies. Protein Eng. 1996, 9, 1063-1065.
    • (1996) Protein Eng. , vol.9 , pp. 1063-1065
    • Kelly, L.A.1    Gardner, S.P.2    Sutcliffe, M.J.3
  • 31
    • 0037065676 scopus 로고    scopus 로고
    • Hints of nonhierarchical folding of acidic fibroblast growth factor
    • Sanz, J. M.; Jiménez, M. A.; Giméenez-Gallego, G. Hints of nonhierarchical folding of acidic fibroblast growth factor. Biochemistry 2002, 41, 1923-1933.
    • (2002) Biochemistry , vol.41 , pp. 1923-1933
    • Sanz, J.M.1    Jiménez, M.A.2    Giméenez-Gallego, G.3
  • 32
    • 0037133525 scopus 로고    scopus 로고
    • NMR structure of the second intracellular loop of the α2A-adrenergic receptor: Evidence for a novel cytoplasmic helix
    • Chung, D. A.; Zuiderweg, E. R. P.; Fowler, C. B.; Soyer, O. S.; Mosberg, H. I.; Neubig, R. R. NMR structure of the second intracellular loop of the α2A-adrenergic receptor: evidence for a novel cytoplasmic helix. Biochemistry 2002, 41, 3596-3604.
    • (2002) Biochemistry , vol.41 , pp. 3596-3604
    • Chung, D.A.1    Zuiderweg, E.R.P.2    Fowler, C.B.3    Soyer, O.S.4    Mosberg, H.I.5    Neubig, R.R.6
  • 33
    • 0035745660 scopus 로고    scopus 로고
    • Peptide fragments as models to study the structure of a G-protein coupled receptor: The alfa-factor receptor of Sacharomices cerevisiae
    • Naider, F.; Arshava, B.; Ding, F-X.; Arevalo, E.; Becker, J. M. Peptide fragments as models to study the structure of a G-protein coupled receptor: the alfa-factor receptor of Sacharomices cerevisiae. Biopolymers 2001, 60, 334-350.
    • (2001) Biopolymers , vol.60 , pp. 334-350
    • Naider, F.1    Arshava, B.2    Ding, F.-X.3    Arevalo, E.4    Becker, J.M.5
  • 36
    • 0028903022 scopus 로고
    • 100 Years lock-and-key concept: Are peptide keys shaped and guided to their receptors by target cell membrane?
    • Schwyzer, R. 100 years lock-and-key concept: are peptide keys shaped and guided to their receptors by target cell membrane? Biopolymers 1995, 37, 5-16.
    • (1995) Biopolymers , vol.37 , pp. 5-16
    • Schwyzer, R.1
  • 37
    • 0035830401 scopus 로고    scopus 로고
    • Solution structure of the second extracellular loop of human thromboxane A2 receptor
    • Ruan, K.-H.; So, S.-P.; Wu, J.; Huang, A.; Kung, J. Solution structure of the second extracellular loop of human thromboxane A2 receptor. Biochemistry 2001, 40, 275-280.
    • (2001) Biochemistry , vol.40 , pp. 275-280
    • Ruan, K.-H.1    So, S.-P.2    Wu, J.3    Huang, A.4    Kung, J.5
  • 38
    • 0037589024 scopus 로고    scopus 로고
    • Conformational features of a synthetic model of the first extracellular loop of the angiotensin II AT1A receptor
    • in press
    • Nicastro, G.; Peri, F.; Franzoni, L.; de Chiara, C.; Sartor, G.; Spisni, A. Conformational Features of a Synthetic Model of the First Extracellular Loop of the Angiotensin II AT1A Receptor. J. Pept. Sci., in press.
    • J. Pept. Sci.
    • Nicastro, G.1    Peri, F.2    Franzoni, L.3    De Chiara, C.4    Sartor, G.5    Spisni, A.6
  • 39
    • 0027230745 scopus 로고
    • A keratinocyte growth factor receptor-derived peptide antagonist identifies part of the ligand binding site
    • Bottaro, D. P.; Fortney, E.; Rubin, J. S.; Aaronson, S. A. A keratinocyte growth factor receptor-derived peptide antagonist identifies part of the ligand binding site. J. Biol. Chem. 1993, 268, 9180-9183.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9180-9183
    • Bottaro, D.P.1    Fortney, E.2    Rubin, J.S.3    Aaronson, S.A.4
  • 42
    • 0031572867 scopus 로고    scopus 로고
    • Interaction of fibroblast growth factor-1 and related peptides with heparan sulfate and its oligosaccharides
    • Fromm, J. R.; Hileman, H. 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. 1997, 346, 252-262.
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 252-262
    • Fromm, J.R.1    Hileman, H.E.2    Weiler, J.M.3    Linhardt, R.J.4
  • 43
    • 12444342414 scopus 로고    scopus 로고
    • New synthetic peptides derived from human fibroblast growth factor-1: Search for agonists and inhibitors
    • Proceedings of the 15th American Peptide Symposium, Nashville, TN, June 14-19, 1999; Tam, J. P., Kaumaya, P. T. P., Eds.; ESCOM/Kluwer: Dordrecht, The Netherlands
    • Kiyota, S.; Gambarini, A. G.; Viviani, W.; Oyama, S., Jr.; Toma, I. N.; Sykes, B. D.; Miranda, M. T. M. New synthetic peptides derived from human fibroblast growth factor-1: search for agonists and inhibitors. In Peptides: Frontiers of Peptide Science; Proceedings of the 15th American Peptide Symposium, Nashville, TN, June 14-19, 1999; Tam, J. P., Kaumaya, P. T. P., Eds.; ESCOM/Kluwer: Dordrecht, The Netherlands, 1999; pp 641-642.
    • (1999) Peptides: Frontiers of Peptide Science , pp. 641-642
    • Kiyota, S.1    Gambarini, A.G.2    Viviani, W.3    Oyama S., Jr.4    Toma, I.N.5    Sykes, B.D.6    Miranda, M.T.M.7
  • 44
    • 0025001394 scopus 로고
    • Heparin and heparan sulfate increase the radius of diffusion and action of basic fibroblast growth factor
    • Flaumenhaft, R.; Moscatelli, D.; Rifkin, D. B. Heparin and heparan sulfate increase the radius of diffusion and action of basic fibroblast growth factor. J. Cell. Biol. 1990, 111, 1651-1659.
    • (1990) J. Cell. Biol. , vol.111 , pp. 1651-1659
    • Flaumenhaft, R.1    Moscatelli, D.2    Rifkin, D.B.3
  • 45
    • 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 1994, 33, 3831-3840.
    • (1994) Biochemistry , vol.33 , pp. 3831-3840
    • Thompson, L.D.1    Pantoliano, M.W.2    Springer, B.A.3
  • 47
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano, W. L.; Ultsch, M. H.; de Vos, A. M.; Wells, J. A. Convergent solutions to binding at a protein-protein interface. Science 2000, 287, 1279-1282.
    • (2000) Science , vol.287 , pp. 1279-1282
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 48
  • 50
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov, A. N.; Schlessinger, J.; Hubbard, S. R.; Mohammadi, M. Structural basis for FGF receptor dimerization and activation. Cell 1999, 98, 641-650.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 51
    • 0026556882 scopus 로고
    • b-Trefoil fold-patterns of structures and sequence in the Kunitz inhibitors, intrleukins-1b and 1a and fibroblast growth factors
    • Murzin, A. G.; Lesk, A. M.; Chothia, C. b-Trefoil fold-patterns of structures and sequence in the Kunitz inhibitors, intrleukins-1b and 1a and fibroblast growth factors. J. Mol. Biol. 1992, 233, 531-543.
    • (1992) J. Mol. Biol. , vol.233 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 52
    • 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 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
  • 53
    • 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, M. A.; Lozano, R. M.; Nielo, J. L.; Santoro, J.; Rico, M.; Giménez-Gallego, G. Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog. J. Mol. Biol. 1996, 264, 162-178.
    • (1996) J. Mol. Biol. , vol.264 , pp. 162-178
    • Pineda-Lucena, A.1    Jiménez, M.A.2    Lozano, R.M.3    Nielo, J.L.4    Santoro, J.5    Rico, M.6    Giménez-Gallego, G.7
  • 54
    • 0030743067 scopus 로고    scopus 로고
    • Solid-phase peptide synthesis at elevated temperatures: A search for an optimized synthesis condition of unsulfated cholecystokinin-12
    • Varanda, L. M.; Miranda, M. T. M. Solid-phase peptide synthesis at elevated temperatures: a search for an optimized synthesis condition of unsulfated cholecystokinin-12. J. Pept. Res. 1997, 50, 102-108.
    • (1997) J. Pept. Res. , vol.50 , pp. 102-108
    • Varanda, L.M.1    Miranda, M.T.M.2
  • 55
    • 0013579630 scopus 로고
    • Optimization of disulfide bond formation
    • Misicka, A.; Hruby, V. J. Optimization of disulfide bond formation. Pol. J. Chem. 1994, 68, 893-99.
    • (1994) Pol. J. Chem. , vol.68 , pp. 893-899
    • Misicka, A.1    Hruby, V.J.2
  • 56
    • 0027336612 scopus 로고
    • Synthesis of human CCK 26-33 and CCK-33 related analogs on 2,4-DMBHA and TMBHA
    • Miranda, M. T. M.; Liddle, R. A.; Rivier, J. E. Synthesis of human CCK 26-33 and CCK-33 related analogs on 2,4-DMBHA and TMBHA. J. Med. Chem. 1993, 36, 1681-1688.
    • (1993) J. Med. Chem. , vol.36 , pp. 1681-1688
    • Miranda, M.T.M.1    Liddle, R.A.2    Rivier, J.E.3
  • 57
    • 0015897954 scopus 로고
    • Pituitary extracts and steroid hormones in the control of 3T3 cell growth
    • Armelin, H. A. Pituitary extracts and steroid hormones in the control of 3T3 cell growth. Proc. Natl. Acad. Sci. U.S.A. 1973, 70, 2702-2706.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 2702-2706
    • Armelin, H.A.1
  • 58
    • 0021359304 scopus 로고
    • Heparin-affinity: Purification of a tumor derived capillary endothelial cell growth factor
    • Shing, Y.; Folkman, J.; Sullivan; R.; Butterfield, C.; Murray, J.; Klagsbrun, M. Heparin-affinity: purification of a tumor derived capillary endothelial cell growth factor. Science 1984, 223, 1296-1298.
    • (1984) Science , vol.223 , pp. 1296-1298
    • Shing, Y.1    Folkman, J.2    Sullivan, R.3    Butterfield, C.4    Murray, J.5    Klagsbrun, M.6
  • 59
    • 0026043349 scopus 로고
    • Identification and assay of fibroblast growth factor receptors
    • Kan, M.; Shi, E. G.; Mckeehan, W. L. Identification and assay of fibroblast growth factor receptors. Methods Enzymol. 1991, 198, 159-171.
    • (1991) Methods Enzymol. , vol.198 , pp. 159-171
    • Kan, M.1    Shi, E.G.2    Mckeehan, W.L.3
  • 61
    • 33845378943 scopus 로고
    • Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • Davis, D. G.; Bax, A. Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 1985, 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 62
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax, A.; Davis, D. G. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 1985, 63, 207-213.
    • (1985) J. Magn. Reson. , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 63
    • 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. 1980, 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 64
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D. J.; Haberkorn, R. A.; Ruben, D. J. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Res. 1982, 48, 286-292.
    • (1982) J. Magn. Res. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 65
    • 45249128810 scopus 로고
    • Measurement of vicinal couplings from cross peaks in COSY spectra
    • Kim, Y.; Prestegard, J. H. Measurement of vicinal couplings from cross peaks in COSY spectra. J. Magn. Res. 1989, 84, 9-13.
    • (1989) J. Magn. Res. , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegard, J.H.2
  • 67
    • 0023732144 scopus 로고    scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • Nilges, M.; Clore, G. M.; Gronenborn, A. Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Lett. 1998, 239, 129-136.
    • (1998) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.3


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