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Volumn 98, Issue 5, 1999, Pages 641-650

Structural basis for FGF receptor dimerization and activation

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR; HEPARIN;

EID: 0033520472     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80051-3     Document Type: Article
Times cited : (527)

References (57)
  • 1
    • 0027255139 scopus 로고
    • A novel form of FGF receptor-3 using an alternative exon in the immunoglobulin domain III
    • Avivi, A., Yayon, A., and Givol, D. (1993). A novel form of FGF receptor-3 using an alternative exon in the immunoglobulin domain III. FEES Lett. 330, 249-252.
    • (1993) FEES Lett. , vol.330 , pp. 249-252
    • Avivi, A.1    Yayon, A.2    Givol, D.3
  • 2
    • 0028803613 scopus 로고
    • Outline structures for the extracellular domains of the fibroblast growth factor receptors
    • Bateman, A., and Chothia, C. (1995). Outline structures for the extracellular domains of the fibroblast growth factor receptors. Nat. Struct. Biol. 2, 1068-1074.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1068-1074
    • Bateman, A.1    Chothia, C.2
  • 4
    • 0025238409 scopus 로고
    • Identification of a cadherin cell adhesion recognition sequence
    • Blaschuk, O.W., Sullivan, Ft., David, S., and Pouliot, Y. (1990). Identification of a cadherin cell adhesion recognition sequence. Dev. Biol. 739, 227-229.
    • (1990) Dev. Biol. , vol.739 , pp. 227-229
    • Blaschuk, O.W.1    Sullivan, Ft.2    David, S.3    Pouliot, Y.4
  • 6
    • 0024339705 scopus 로고
    • The heparin-binding (fibroblast) growth factor family of proteins
    • Burgess, W.H., and Maciag, T. (1989). The heparin-binding (fibroblast) growth factor family of proteins. Annu. Rev. Biochem. 58, 575-606.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 575-606
    • Burgess, W.H.1    Maciag, T.2
  • 7
    • 0028117373 scopus 로고
    • High-affinity binding sites for related fibroblast growth factor ligands reside within different receptor immunoglobulin-like domains
    • Cheon, H.G., LaRochelle, W.J., Bottaro, D.P., Burgess, W.H., and Aaronson, S.A. (1994). High-affinity binding sites for related fibroblast growth factor ligands reside within different receptor immunoglobulin-like domains. Proc. Natl. Acad. Sei. USA 91, 989-993.
    • (1994) Proc. Natl. Acad. Sei. USA , vol.91 , pp. 989-993
    • Cheon, H.G.1    LaRochelle, W.J.2    Bottaro, D.P.3    Burgess, W.H.4    Aaronson, S.A.5
  • 8
    • 0026739404 scopus 로고
    • A novel form of fibroblast growth factor receptor 2. Alternative splicing of the third immunoglobulinlike domain confers ligand binding specificity
    • Dell, K.R., and Williams, L.T. (1992). A novel form of fibroblast growth factor receptor 2. Alternative splicing of the third immunoglobulinlike domain confers ligand binding specificity. J. Biol. Chem. 267, 21225-21229.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21225-21229
    • Dell, K.R.1    Williams, L.T.2
  • 9
    • 0030221511 scopus 로고    scopus 로고
    • CAM-FGF receptor interactions: A model for axonal growth
    • Doherty, P., and Walsh, F.S. (1996). CAM-FGF receptor interactions: a model for axonal growth. Mol. Cell. Neurosci. 8, 99-111.
    • (1996) Mol. Cell. Neurosci. , vol.8 , pp. 99-111
    • Doherty, P.1    Walsh, F.S.2
  • 10
    • 0028817332 scopus 로고
    • A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth
    • Doherty, P., Williams, E., and Walsh, F.S. (1995). A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth. Neuron 14, 57-66.
    • (1995) Neuron , vol.14 , pp. 57-66
    • Doherty, P.1    Williams, E.2    Walsh, F.S.3
  • 12
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • Faham, S., Hileman, R.E., Fromm, U.R., Linhardt, R.J., and Rees, D.C. (1996). Heparin structure and interactions with basic fibroblast growth factor. Science 277, 1116-1120.
    • (1996) Science , vol.277 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, U.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 13
  • 14
    • 0029005663 scopus 로고
    • Heparin can activate a receptor tyrosine kinase
    • Gao, G., and Goldfarb, M. (1995). Heparin can activate a receptor tyrosine kinase. EM BO J. 14, 2183-2190.
    • (1995) EMBO J. , vol.14 , pp. 2183-2190
    • Gao, G.1    Goldfarb, M.2
  • 15
    • 0026800671 scopus 로고
    • X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 Å resolution
    • Holden, H.M., Ito, M., Hartshorne, D.U., and Rayment, I. (1992). X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 Å resolution. J. Mol. Biol. 227, 840-851.
    • (1992) J. Mol. Biol. , vol.227 , pp. 840-851
    • Holden, H.M.1    Ito, M.2    Hartshorne, D.U.3    Rayment, I.4
  • 16
    • 0026649742 scopus 로고
    • Fibroblast growth factor receptor tyrosine kinases: Molecular analysis and signal transduction
    • Jaye, M., Schlessinger, J., and Dionne, C.A. (1992). Fibroblast growth factor receptor tyrosine kinases: molecular analysis and signal transduction. Biochim. Biophys. Acta 7735, 185-199.
    • (1992) Biochim. Biophys. Acta , vol.7735 , pp. 185-199
    • Jaye, M.1    Schlessinger, J.2    Dionne, C.A.3
  • 17
    • 0027344852 scopus 로고
    • Structural and functional diversity in the FGF receptor multigene family
    • Johnson, D.E., and Williams, L.T. (1993). Structural and functional diversity in the FGF receptor multigene family. Adv. Cancer Res. 60, 1-41.
    • (1993) Adv. Cancer Res. , vol.60 , pp. 1-41
    • Johnson, D.E.1    Williams, L.T.2
  • 18
    • 0025122589 scopus 로고
    • Diverse forms of a receptor for acidic and basic fibroblast growth factors
    • Johnson, D.E., Lee, P.L., Lu, J., and Williams, L.T. (1990). Diverse forms of a receptor for acidic and basic fibroblast growth factors. Mol. Cell. Biol. 10, 4728-4736.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4728-4736
    • Johnson, D.E.1    Lee, P.L.2    Lu, J.3    Williams, L.T.4
  • 19
    • 0025912340 scopus 로고
    • The human fibroblast growth factor receptor genes: A common structural arrangement underlies the mechanisms for generating receptorforms that differ in their third immunoglobulin domain
    • Johnson, D.E., Lu, J., Chen, H., Werner, S., and Williams, L.T. (1991). The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptorforms that differ in their third immunoglobulin domain. Mol. Cell. Biol. 77, 4627-4634.
    • (1991) Mol. Cell. Biol. , vol.77 , pp. 4627-4634
    • Johnson, D.E.1    Lu, J.2    Chen, H.3    Werner, S.4    Williams, L.T.5
  • 20
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 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., and McKeehan, W.L. (1993). An essential heparin-binding domain in the fibroblast growth factor receptor kinase. Science 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
    • 0027365931 scopus 로고
    • Aberrant expression of type I fibroblast growth factor receptor in human pancreatic adenocarcinomas
    • Kobrin, M.S., Yamanaka, Y., Friess, H., Lopez, M.E., and Korc, M. (1993). Aberrant expression of type I fibroblast growth factor receptor in human pancreatic adenocarcinomas. Cancer Res. 53, 4741-4744.
    • (1993) Cancer Res. , vol.53 , pp. 4741-4744
    • Kobrin, M.S.1    Yamanaka, Y.2    Friess, H.3    Lopez, M.E.4    Korc, M.5
  • 23
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/M APK signaling pathway
    • Kouhara, H., Hadari, Y.R., Spivak-Kroizman, T., Schilling, J., BarSagi, D., Lax, I., and Schlessinger, J. (1997). A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/M APK signaling pathway. Cell 89, 693-702.
    • (1997) Cell , vol.89 , pp. 693-702
    • Kouhara, H.1    Hadari, Y.R.2    Spivak-Kroizman, T.3    Schilling, J.4    BarSagi, D.5    Lax, I.6    Schlessinger, J.7
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Mac Arthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Mac Arthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon, M.A., and Schlessinger, J. (1994). Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem. Sei. 19, 459-463.
    • (1994) Trends Biochem. Sei. , vol.19 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2
  • 27
    • 0030815133 scopus 로고    scopus 로고
    • RasteiSD: Photorealistic molecular graphics
    • Merrit, E.A., and Bacon, D.U. (1997). RasteiSD: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.U.2
  • 28
    • 0025970826 scopus 로고
    • Expression cDNA cloning of the KGF receptor by creation of a transforming autocrine loop
    • Miki, T., Fleming, T.P., Bottaro, O.P., Rubin, J.S., Ron, D., and Aaronson, S.A. (1991). Expression cDNA cloning of the KGF receptor by creation of a transforming autocrine loop. Science 251, 72-75.
    • (1991) Science , vol.251 , pp. 72-75
    • Miki, T.1    Fleming, T.P.2    Bottaro, O.P.3    Rubin, J.S.4    Ron, D.5    Aaronson, S.A.6
  • 29
    • 0026570847 scopus 로고
    • Determination of ligandbinding specificity by alternative splicing: Two distinct growth factor receptors encoded by a single gene
    • Miki, T., Bottaro, O.P., Fleming, T.P., Smith, C.L., Burgess, W.H., Chan, A.M., and Aaronson, S.A. (1992). Determination of ligandbinding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene. Proc. Natl. Acad. Sei. USA 89, 246-250.
    • (1992) Proc. Natl. Acad. Sei. USA , vol.89 , pp. 246-250
    • Miki, T.1    Bottaro, O.P.2    Fleming, T.P.3    Smith, C.L.4    Burgess, W.H.5    Chan, A.M.6    Aaronson, S.A.7
  • 30
    • 0026641249 scopus 로고
    • Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis
    • Mohammadi, M., Dionne, C.A., Li, W., Li, N., Spivak, T., Honegger, A.M., Jaye, M., and Schlessinger, J. (1992). Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature 358, 681-684.
    • (1992) Nature , vol.358 , pp. 681-684
    • Mohammadi, M.1    Dionne, C.A.2    Li, W.3    Li, N.4    Spivak, T.5    Honegger, A.M.6    Jaye, M.7    Schlessinger, J.8
  • 31
    • 33644973673 scopus 로고    scopus 로고
    • FGF signaling in skeletal development
    • Naski, M.C., and Ornitz, D.M. (1998). FGF signaling in skeletal development. Front Biosci. 3, D781-D794.
    • (1998) Front Biosci. , vol.3
    • Naski, M.C.1    Ornitz, D.M.2
  • 32
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 33
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from interfacial and thermodynamic properties of hydrocarbons
    • Niche-Ms, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Niche-Ms, A.1    Sharp, K.A.2    Honig, B.3
  • 34
    • 0000836705 scopus 로고    scopus 로고
    • Inhibition of adhesion and induction of epithelial cell invasion by HAV-containing E-cadherin-specific peptides
    • Noe, V., Willems, J., Vandekerckhove, J., Roy, F.V., Bruyneel, E., and Mareel, M. (1999). Inhibition of adhesion and induction of epithelial cell invasion by HAV-containing E-cadherin-specific peptides. J. Cell Sei. 772, 127-135.
    • (1999) J. Cell Sei. , vol.772 , pp. 127-135
    • Noe, V.1    Willems, J.2    Vandekerckhove, J.3    Roy, F.V.4    Bruyneel, E.5    Mareel, M.6
  • 35
    • 0026502460 scopus 로고
    • Heparin is required for cell-free binding of bFGF to a soluble receptor and for mitogenesis in whole cells
    • Ornitz, D.M., Yayon, A., Flanagan, J.G., Svahn, C.M., Levi, E., and Leder, P. (1992). Heparin is required for cell-free binding of bFGF to a soluble receptor and for mitogenesis in whole cells. Mol. Cell. Biol. 72, 240-247.
    • (1992) Mol. Cell. Biol. , vol.72 , pp. 240-247
    • Ornitz, D.M.1    Yayon, A.2    Flanagan, J.G.3    Svahn, C.M.4    Levi, E.5    Leder, P.6
  • 37
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L Sawyer, N. Isaacs, and S. Burley, eds. (Daresbury, UK: SERC Daresbury Laboratory)
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend, L Sawyer, N. Isaacs, and S. Burley, eds. (Daresbury, UK: SERC Daresbury Laboratory).
    • (1993) Proceedings of the CCP4 Study Weekend
    • Otwinowski, Z.1
  • 38
    • 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., and Sisk, W.P. (1994). Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization. Biochemistry 33, 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
  • 39
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson, T. (1995). Protein modules and signaling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 41
    • 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., and Moscatelli, D. (1994). Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding. J. Biol. Chem. 269, 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
  • 42
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?
    • Schlessinger, J., Lax, I., and Lemmon, M. (1995). Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors? Cell 83, 357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 44
  • 46
    • 0028986809 scopus 로고
    • Alternately spliced NH2-terminal immunoglobulin-like loop I in the ectodomain of the fibroblast growth factor (FGF) receptor 1 lowers affinity for both heparin and FGF-1
    • Wang, F., Kan, M., Van, G., Xu, J., and McKeehan, W.L (1995). Alternately spliced NH2-terminal immunoglobulin-like loop I in the ectodomain of the fibroblast growth factor (FGF) receptor 1 lowers affinity for both heparin and FGF-1. J. Biol. Chem. 270,10231 -10235.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10231-10235
    • Wang, F.1    Kan, M.2    Van, G.3    Xu, J.4    McKeehan, W.L.5
  • 47
    • 0030843409 scopus 로고    scopus 로고
    • A homeo-interaction sequence in the ectodomain of the fibroblast growth factor receptor
    • Wang, F., Kan, M., McKeehan, K., Jang, J.H., Feng, S., and McKeehan, W.L. (1997). A homeo-interaction sequence in the ectodomain of the fibroblast growth factor receptor. J. Biol. Chem. 272, 23887-23895.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23887-23895
    • Wang, F.1    Kan, M.2    McKeehan, K.3    Jang, J.H.4    Feng, S.5    McKeehan, W.L.6
  • 48
    • 0033524431 scopus 로고    scopus 로고
    • Common and specific determinants for fibroblast growth factors in the ectodomain of the receptor kinase complex
    • Wang, F., Lu, W., McKeehan, K., Mohamedali, K., Gabriel, J.L, Kan, M., and McKeehan, W.L. (1999). Common and specific determinants for fibroblast growth factors in the ectodomain of the receptor kinase complex. Biochemistry 38, 160-171.
    • (1999) Biochemistry , vol.38 , pp. 160-171
    • Wang, F.1    Lu, W.2    McKeehan, K.3    Mohamedali, K.4    Gabriel, J.L.5    Kan, M.6    McKeehan, W.L.7
  • 49
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily-domains for cell surface recognition
    • Williams, A.F., and Barclay, A.N. (1988). The immunoglobulin superfamily-domains for cell surface recognition. Annu. Rev. Immunol. 6, 381-405.
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 50
    • 0028096172 scopus 로고
    • Differential expression of two fibroblast growth factor-receptor genes is associated with malignant progression in human astrocytomas
    • Yamaguchi, F., Saya, H., Bruner, U.M., and Morrison, R.S. (1994). Differential expression of two fibroblast growth factor-receptor genes is associated with malignant progression in human astrocytomas. Proc. Natl. Acad. Sei. USA 91, 484-488.
    • (1994) Proc. Natl. Acad. Sei. USA , vol.91 , pp. 484-488
    • Yamaguchi, F.1    Saya, H.2    Bruner, M.3    Morrison, R.S.4
  • 51
    • 0026607170 scopus 로고
    • A confined variable region confers ligand specificity on fibroblast growth factor receptors: Implications for the origin of the immunoglobulin fold
    • Yayon, A., Zimmer, Y., Shen, G.H., Avivi, A., Yarden, Y., and Givol, D. (1992). A confined variable region confers ligand specificity on fibroblast growth factor receptors: implications for the origin of the immunoglobulin fold. EM BO J. 11, 1885-1890.
    • (1992) EM BO J. , vol.11 , pp. 1885-1890
    • Yayon, A.1    Zimmer, Y.2    Shen, G.H.3    Avivi, A.4    Yarden, Y.5    Givol, D.6
  • 52
  • 53
    • 0026323941 scopus 로고
    • Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta
    • Zhang, J.D., Cousens, L.S., Barr, P.J., and Sprang, S.R. (1991). Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta. Proc. Natl. Acad. Sei. USA 88, 3446-3450.
    • (1991) Proc. Natl. Acad. Sei. USA , vol.88 , pp. 3446-3450
    • Zhang, J.D.1    Cousens, L.S.2    Barr, P.J.3    Sprang, S.R.4
  • 55
    • 0029120338 scopus 로고
    • Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis
    • Zhu, H., Ramnarayan, K., Anchin, J., M iao, W.Y., Sereno, A., M illman, L, Zheng, J., Balaji, V.N., and Wo Iff, M.E. (1995). Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis. J. Biol. Chem. 270, 21869-21874.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21869-21874
    • Zhu, H.1    Ramnarayan, K.2    Anchin, J.3    Miao, W.Y.4    Sereno, A.5    Millman, L.6    Zheng, J.7    Balaji, V.N.8    Woiff, M.E.9
  • 56
    • 0030955506 scopus 로고    scopus 로고
    • Analysis of high-affinity binding determinants in the receptor binding epitope of basic fibroblast growth factor
    • Zhu, H., Anchin, J., Ramnarayan, K., Zheng, J., Kawai, T., Mong, S., and Wolff, M .E. (1997). Analysis of high-affinity binding determinants in the receptor binding epitope of basic fibroblast growth factor. Protein Eng. 10, 417-421.
    • (1997) Protein Eng. , vol.10 , pp. 417-421
    • Zhu, H.1    Anchin, J.2    Ramnarayan, K.3    Zheng, J.4    Kawai, T.5    Mong, S.6    Wolff, M.E.7
  • 57
    • 0031762659 scopus 로고    scopus 로고
    • Identification of two new hydrophobic residues on basic fibroblast growth factor important for fibroblast growth factor receptor binding
    • Zhu, H., Ramnarayan, K., Menzel, P., Miao, Y., Zheng, J., and Mong, S. (1998). Identification of two new hydrophobic residues on basic fibroblast growth factor important for fibroblast growth factor receptor binding. Protein Eng. 11, 937-940.
    • (1998) Protein Eng. , vol.11 , pp. 937-940
    • Zhu, H.1    Ramnarayan, K.2    Menzel, P.3    Miao, Y.4    Zheng, J.5    Mong, S.6


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