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Volumn 29, Issue 17, 2009, Pages 4663-4678

Homodimerization controls the fibroblast growth factor 9 subfamily's receptor binding and heparan sulfate-dependent diffusion in the extracellular matrix

(13)  Kalinina, Juliya a   Byron, Sara A b   Makarenkova, Helen P c,d   Olsen, Shaun K a,h   Eliseenkova, Anna V a   Larochelle, William J e,i   Dhanabal, Mohanraj e,j   Blais, Steven a   Ornitz, David M g   Day, Loren A f   Neubert, Thomas A a   Pollock, Pamela M b   Mohammadi, Moosa a  


Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR; FIBROBLAST GROWTH FACTOR 20; FIBROBLAST GROWTH FACTOR 9; HEPARAN SULFATE; UNCLASSIFIED DRUG;

EID: 68849110534     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01780-08     Document Type: Article
Times cited : (37)

References (71)
  • 2
    • 45849139021 scopus 로고    scopus 로고
    • Velafermin (rhFGF-20) reduces the severity and duration of hamster cheek pouch mucositis induced by fractionated radiation
    • Ara, G., B. A. Watkins, H. Zhong, T. R. Hawthorne, C. E. Karkaria, S. T. Sonis, and W. J. Larochelle. 2008. Velafermin (rhFGF-20) reduces the severity and duration of hamster cheek pouch mucositis induced by fractionated radiation. Int. J. Radiat. Biol. 84:401-412.
    • (2008) Int. J. Radiat. Biol , vol.84 , pp. 401-412
    • Ara, G.1    Watkins, B.A.2    Zhong, H.3    Hawthorne, T.R.4    Karkaria, C.E.5    Sonis, S.T.6    Larochelle, W.J.7
  • 3
    • 13444263240 scopus 로고    scopus 로고
    • Fibroblast growth factor signaling during early vertebrate development
    • Bottcher, R. T., and C. Niehrs. 2005. Fibroblast growth factor signaling during early vertebrate development. Endocr. Rev. 26:63-77.
    • (2005) Endocr. Rev , vol.26 , pp. 63-77
    • Bottcher, R.T.1    Niehrs, C.2
  • 5
    • 34548250374 scopus 로고    scopus 로고
    • A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases
    • Chen, H., J. Ma, W. Li, A. V. Eliseenkova, C. Xu, T. A. Neubert, W. T. Miller, and M. Mohammadi. 2007. A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases. Mol. Cell 27:717-730.
    • (2007) Mol. Cell , vol.27 , pp. 717-730
    • Chen, H.1    Ma, J.2    Li, W.3    Eliseenkova, A.V.4    Xu, C.5    Neubert, T.A.6    Miller, W.T.7    Mohammadi, M.8
  • 6
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho, H. S., and D. J. Leahy. 2002. Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297:1330-1333.
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 7
    • 0034956610 scopus 로고    scopus 로고
    • Lung hypoplasia and neonatal death in Fgf9-null mice identify this gene as an essential regulator of lung mesenchyme
    • Colvin, J. S., A. C. White, S. J. Pratt, and D. M. Ornitz. 2001. Lung hypoplasia and neonatal death in Fgf9-null mice identify this gene as an essential regulator of lung mesenchyme. Development 128:2095-2106.
    • (2001) Development , vol.128 , pp. 2095-2106
    • Colvin, J.S.1    White, A.C.2    Pratt, S.J.3    Ornitz, D.M.4
  • 9
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K. A. 1985. Theory for the folding and stability of globular proteins. Biochemistry 24:1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 11
    • 0031733974 scopus 로고    scopus 로고
    • Diversity does make a difference: Fibroblast growth factor-heparin interactions
    • Faham, S., R. J. Linhardt, and D. C. Rees. 1998. Diversity does make a difference: fibroblast growth factor-heparin interactions. Curr. Opin. Struct. Biol. 8:578-586.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 578-586
    • Faham, S.1    Linhardt, R.J.2    Rees, D.C.3
  • 12
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson, K. M., M. B. Berger, J. M. Mendrola, H. S. Cho, D. J. Leahy, and M. A. Lemmon. 2003. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol. Cell 11:507-517.
    • (2003) Mol. Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 14
    • 52249096620 scopus 로고    scopus 로고
    • Fgf9 signaling regulates small intestinal elongation and mesenchymal development
    • Geske, M. J., X. Zhang, K. K. Patel, D. M. Ornitz, and T. S. Stappenbeck. 2008. Fgf9 signaling regulates small intestinal elongation and mesenchymal development. Development 135:2959-2968.
    • (2008) Development , vol.135 , pp. 2959-2968
    • Geske, M.J.1    Zhang, X.2    Patel, K.K.3    Ornitz, D.M.4    Stappenbeck, T.S.5
  • 16
    • 18144413583 scopus 로고    scopus 로고
    • Fibroblast growth factor signaling in tumorigenesis
    • Grose, R., and C. Dickson. 2005. Fibroblast growth factor signaling in tumorigenesis. Cytokine Growth Factor Rev. 16:179-186.
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 179-186
    • Grose, R.1    Dickson, C.2
  • 18
    • 33745474608 scopus 로고    scopus 로고
    • Insights into the role of heparan sulphate in fibroblast growth factor signalling
    • Harmer, N. J. 2006. Insights into the role of heparan sulphate in fibroblast growth factor signalling. Biochem. Soc. Trans. 34:442-445.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 442-445
    • Harmer, N.J.1
  • 19
    • 0031693463 scopus 로고    scopus 로고
    • Epithelial/mesenchymal interactions and branching morphogenesis of the lung
    • Hogan, B. L., and J. M. Yingling. 1998. Epithelial/mesenchymal interactions and branching morphogenesis of the lung. Curr. Opin. Genet. Dev. 8:481-486.
    • (1998) Curr. Opin. Genet. Dev , vol.8 , pp. 481-486
    • Hogan, B.L.1    Yingling, J.M.2
  • 20
    • 0026738953 scopus 로고
    • Substitution of putative half-cystine residues in heparin-binding fibroblast growth factor receptors. Loss of binding activity in both two and three loop isoforms
    • Hou, J., M. Kan, F. Wang, J. M. Xu, M. Nakahara, G. McBride, K. McKeehan, and W. L. McKeehan. 1992. Substitution of putative half-cystine residues in heparin-binding fibroblast growth factor receptors. Loss of binding activity in both two and three loop isoforms. J. Biol. Chem. 267:17804-17808.
    • (1992) J. Biol. Chem , vol.267 , pp. 17804-17808
    • Hou, J.1    Kan, M.2    Wang, F.3    Xu, J.M.4    Nakahara, M.5    McBride, G.6    McKeehan, K.7    McKeehan, W.L.8
  • 21
    • 2942594298 scopus 로고    scopus 로고
    • Juxtamembrane autoinhibition in receptor tyrosine kinases
    • Hubbard, S. R. 2004. Juxtamembrane autoinhibition in receptor tyrosine kinases. Nat. Rev. Mol. Cell Biol. 5:464-471.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 464-471
    • Hubbard, S.R.1
  • 22
    • 5444250989 scopus 로고    scopus 로고
    • Biochemical analysis of pathogenic ligand-dependent FGFR2 mutations suggests distinct pathophysiological mechanisms for craniofacial and limb abnormalities
    • Ibrahimi, O. A., F. Zhang, A. V. Eliseenkova, N. Itoh, R. J. Linhardt, and M. Mohammadi. 2004. Biochemical analysis of pathogenic ligand-dependent FGFR2 mutations suggests distinct pathophysiological mechanisms for craniofacial and limb abnormalities. Hum. Mol. Genet. 13:2313-2324.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 2313-2324
    • Ibrahimi, O.A.1    Zhang, F.2    Eliseenkova, A.V.3    Itoh, N.4    Linhardt, R.J.5    Mohammadi, M.6
  • 24
    • 0030833319 scopus 로고    scopus 로고
    • Fgfr2 and osteopontin domains in the developing skull vault are mutually exclusive and can be altered by locally applied FGF2
    • Iseki, S., A. O. Wilkie, J. K. Heath, T. Ishimaru, K. Eto, and G. M. Morriss-Kay. 1997. Fgfr2 and osteopontin domains in the developing skull vault are mutually exclusive and can be altered by locally applied FGF2. Development 124:3375-3384.
    • (1997) Development , vol.124 , pp. 3375-3384
    • Iseki, S.1    Wilkie, A.O.2    Heath, J.K.3    Ishimaru, T.4    Eto, K.5    Morriss-Kay, G.M.6
  • 25
    • 3042826804 scopus 로고    scopus 로고
    • Directionally specific paracrine communication mediated by epithelial FGF9 to stromal FGFR3 in two-compartment premalignant prostate tumors
    • Jin, C., F. Wang, X. Wu, C. Yu, Y. Luo, and W. L. McKeehan. 2004. Directionally specific paracrine communication mediated by epithelial FGF9 to stromal FGFR3 in two-compartment premalignant prostate tumors. Cancer Res. 64:4555-4562.
    • (2004) Cancer Res , vol.64 , pp. 4555-4562
    • Jin, C.1    Wang, F.2    Wu, X.3    Yu, C.4    Luo, Y.5    McKeehan, W.L.6
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building 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
  • 28
    • 49649118142 scopus 로고    scopus 로고
    • Endocrine FGFs and klothos: Emerging concepts
    • Kuro-o, M. 2008. Endocrine FGFs and klothos: emerging concepts. Trends Endocrinol. Metab. 19:239-245.
    • (2008) Trends Endocrinol. Metab , vol.19 , pp. 239-245
    • Kuro-o, M.1
  • 29
    • 33847382417 scopus 로고    scopus 로고
    • The mouse seminal vesicle shape mutation is allelic with Fgfr2
    • Kuslak, S. L., J. L. Thielen, and P. C. Marker. 2007. The mouse seminal vesicle shape mutation is allelic with Fgfr2. Development 134:557-565.
    • (2007) Development , vol.134 , pp. 557-565
    • Kuslak, S.L.1    Thielen, J.L.2    Marker, P.C.3
  • 31
    • 33745129425 scopus 로고    scopus 로고
    • Fibroblast growth factor signals regulate a wave of Hedgehog activation that is essential for coronary vascular development
    • Lavine, K. J., A. C. White, C. Park, C. S. Smith, K. Choi, F. Long, C. C. Hui, and D. M. Ornitz. 2006. Fibroblast growth factor signals regulate a wave of Hedgehog activation that is essential for coronary vascular development. Genes Dev. 20:1651-1666.
    • (2006) Genes Dev , vol.20 , pp. 1651-1666
    • Lavine, K.J.1    White, A.C.2    Park, C.3    Smith, C.S.4    Choi, K.5    Long, F.6    Hui, C.C.7    Ornitz, D.M.8
  • 32
    • 11244306331 scopus 로고    scopus 로고
    • Endocardial and epicardial derived FGF signals regulate myocardial proliferation and differentiation in vivo
    • Lavine, K. J., K. Yu, A. C. White, X. Zhang, C. Smith, J. Partanen, and D. M. Ornitz. 2005. Endocardial and epicardial derived FGF signals regulate myocardial proliferation and differentiation in vivo. Dev. Cell 8:85-95.
    • (2005) Dev. Cell , vol.8 , pp. 85-95
    • Lavine, K.J.1    Yu, K.2    White, A.C.3    Zhang, X.4    Smith, C.5    Partanen, J.6    Ornitz, D.M.7
  • 33
    • 0027772959 scopus 로고
    • Shape complementarity at protein/ protein interfaces
    • Lawrence, M. C., and P. M. Colman. 1993. Shape complementarity at protein/ protein interfaces. J. Mol. Biol. 234:946-950.
    • (1993) J. Mol. Biol , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 37
    • 25844440918 scopus 로고    scopus 로고
    • A protein canyon in the FGF-FGF receptor dimer selects from an a la carte menu of heparan sulfate motifs
    • Mohammadi, M., S. K. Olsen, and R. Goetz. 2005. A protein canyon in the FGF-FGF receptor dimer selects from an a la carte menu of heparan sulfate motifs. Curr. Opin. Struct. Biol. 15:506-516.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 506-516
    • Mohammadi, M.1    Olsen, S.K.2    Goetz, R.3
  • 38
    • 18144423534 scopus 로고    scopus 로고
    • Structural basis for fibroblast growth factor receptor activation
    • Mohammadi, M., S. K. Olsen, and O. A. Ibrahimi. 2005. Structural basis for fibroblast growth factor receptor activation. Cytokine Growth Factor Rev. 16:107-137.
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 107-137
    • Mohammadi, M.1    Olsen, S.K.2    Ibrahimi, O.A.3
  • 39
    • 0026556882 scopus 로고
    • beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors
    • Murzin, A. G., A. M. Lesk, and C. Chothia. 1992. beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors. J. Mol. Biol. 223:531-543.
    • (1992) J. Mol. Biol , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 40
    • 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
  • 42
    • 0037447999 scopus 로고    scopus 로고
    • Preferential neurotrophic activity of fibroblast growth factor-20 for dopaminergic neurons through fibroblast growth factor receptor-1c
    • Ohmachi, S., T. Mikami, M. Konishi, A. Miyake, and N. Itoh. 2003. Preferential neurotrophic activity of fibroblast growth factor-20 for dopaminergic neurons through fibroblast growth factor receptor-1c. J. Neurosci. Res. 72: 436-443.
    • (2003) J. Neurosci. Res , vol.72 , pp. 436-443
    • Ohmachi, S.1    Mikami, T.2    Konishi, M.3    Miyake, A.4    Itoh, N.5
  • 43
    • 0034703621 scopus 로고    scopus 로고
    • FGF-20, a novel neurotrophic factor, preferentially expressed in the substantia nigra pars compacta of rat brain
    • Ohmachi, S., Y. Watanabe, T. Mikami, N. Kusu, T. Ibi, A. Akaike, and N. Itoh. 2000. FGF-20, a novel neurotrophic factor, preferentially expressed in the substantia nigra pars compacta of rat brain. Biochem. Biophys. Res. Commun. 277:355-360.
    • (2000) Biochem. Biophys. Res. Commun , vol.277 , pp. 355-360
    • Ohmachi, S.1    Watanabe, Y.2    Mikami, T.3    Kusu, N.4    Ibi, T.5    Akaike, A.6    Itoh, N.7
  • 45
    • 0035081241 scopus 로고    scopus 로고
    • Ornitz, D. M., and N. Itoh. 2001. Fibroblast growth factors. Genome Biol. 2:REVIEWS3005.
    • Ornitz, D. M., and N. Itoh. 2001. Fibroblast growth factors. Genome Biol. 2:REVIEWS3005.
  • 47
    • 0027199056 scopus 로고
    • Developmental localization of the splicing alternatives of fibroblast growth factor receptor-2 (FGFR2)
    • Orr-Urtreger, A., M. T. Bedford, T. Burakova, E. Arman, Y. Zimmer, A. Yayon, D. Givol, and P. Lonai. 1993. Developmental localization of the splicing alternatives of fibroblast growth factor receptor-2 (FGFR2). Dev. Biol. 158:475-486.
    • (1993) Dev. Biol , vol.158 , pp. 475-486
    • Orr-Urtreger, A.1    Bedford, M.T.2    Burakova, T.3    Arman, E.4    Zimmer, Y.5    Yayon, A.6    Givol, D.7    Lonai, P.8
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 4344684497 scopus 로고    scopus 로고
    • Fgf9 signaling regulates inner ear morphogenesis through epithelial-mesenchymal interactions
    • Pirvola, U., X. Zhang, J. Mantela, D. M. Ornitz, and J. Ylikoski. 2004. Fgf9 signaling regulates inner ear morphogenesis through epithelial-mesenchymal interactions. Dev. Biol. 273:350-360.
    • (2004) Dev. Biol , vol.273 , pp. 350-360
    • Pirvola, U.1    Zhang, X.2    Mantela, J.3    Ornitz, D.M.4    Ylikoski, J.5
  • 51
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov, A. N., S. R. Hubbard, J. Schlessinger, and M. Mohammadi. 2000. Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Cell 101:413-424.
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 52
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov, A. N., J. Schlessinger, S. R. Hubbard, and M. Mohammadi. 1999. Structural basis for FGF receptor dimerization and activation. Cell 98:641-650.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 53
    • 0025835670 scopus 로고
    • Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
    • Rapraeger, A. C., A. Krufka, and B. B. Olwin. 1991. Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation. Science 252:1705-1708.
    • (1991) Science , vol.252 , pp. 1705-1708
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 54
    • 49449109011 scopus 로고    scopus 로고
    • Parthenogenetic dopamine neurons from primate embryonic stem cells restore function in experimental Parkinson's disease
    • Sanchez-Pernaute, R., H. Lee, M. Patterson, C. Reske-Nielsen, T. Yoshizaki, K. C. Sonntag, L. Studer, and O. Isacson. 2008. Parthenogenetic dopamine neurons from primate embryonic stem cells restore function in experimental Parkinson's disease. Brain 131:2127-2139.
    • (2008) Brain , vol.131 , pp. 2127-2139
    • Sanchez-Pernaute, R.1    Lee, H.2    Patterson, M.3    Reske-Nielsen, C.4    Yoshizaki, T.5    Sonntag, K.C.6    Studer, L.7    Isacson, O.8
  • 56
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck, P. 2003. On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal. Biochem. 320:104-124.
    • (2003) Anal. Biochem , vol.320 , pp. 104-124
    • Schuck, P.1
  • 58
    • 0034602719 scopus 로고    scopus 로고
    • Structural interactions of fibroblast growth factor receptor with its ligands
    • Stauber, D. J., A. D. DiGabriele, and W. A. Hendrickson. 2000. Structural interactions of fibroblast growth factor receptor with its ligands. Proc. Natl. Acad. Sci. USA 97:49-54.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 49-54
    • Stauber, D.J.1    DiGabriele, A.D.2    Hendrickson, W.A.3
  • 59
    • 17244378089 scopus 로고    scopus 로고
    • FGFR2b signaling regulates ex vivo submandibular gland epithelial cell proliferation and branching morphogenesis
    • Steinberg, Z., C. Myers, V. M. Heim, C. A. Lathrop, I. T. Rebustini, J. S. Stewart, M. Larsen, and M. P. Hoffman. 2005. FGFR2b signaling regulates ex vivo submandibular gland epithelial cell proliferation and branching morphogenesis. Development 132:1223-1234.
    • (2005) Development , vol.132 , pp. 1223-1234
    • Steinberg, Z.1    Myers, C.2    Heim, V.M.3    Lathrop, C.A.4    Rebustini, I.T.5    Stewart, J.S.6    Larsen, M.7    Hoffman, M.P.8
  • 60
    • 38449096256 scopus 로고    scopus 로고
    • FGF signaling: Its role in bone development and human skeleton diseases
    • Su, N., X. Du, and L. Chen. 2008. FGF signaling: its role in bone development and human skeleton diseases. Front. Biosci. 13:2842-2865.
    • (2008) Front. Biosci , vol.13 , pp. 2842-2865
    • Su, N.1    Du, X.2    Chen, L.3
  • 62
    • 27744534898 scopus 로고    scopus 로고
    • Functions and regulations of fibroblast growth factor signaling during embryonic development
    • Thisse, B., and C. Thisse. 2005. Functions and regulations of fibroblast growth factor signaling during embryonic development. Dev. Biol. 287:390-402.
    • (2005) Dev. Biol , vol.287 , pp. 390-402
    • Thisse, B.1    Thisse, C.2
  • 63
    • 37549010298 scopus 로고    scopus 로고
    • The fibroblast growth factor system is downregulated following social defeat
    • Turner, C. A., N. Calvo, D. O. Frost, H. Akil, and S. J. Watson. 2008. The fibroblast growth factor system is downregulated following social defeat. Neurosci. Lett. 430:147-150.
    • (2008) Neurosci. Lett , vol.430 , pp. 147-150
    • Turner, C.A.1    Calvo, N.2    Frost, D.O.3    Akil, H.4    Watson, S.J.5
  • 65
    • 33646705916 scopus 로고    scopus 로고
    • FGF9 and SHH signaling coordinate lung growth and development through regulation of distinct mesenchymal domains
    • White, A. C., J. Xu, Y. Yin, C. Smith, G. Schmid, and D. M. Ornitz. 2006. FGF9 and SHH signaling coordinate lung growth and development through regulation of distinct mesenchymal domains. Development 133:1507-1517.
    • (2006) Development , vol.133 , pp. 1507-1517
    • White, A.C.1    Xu, J.2    Yin, Y.3    Smith, C.4    Schmid, G.5    Ornitz, D.M.6
  • 66
    • 29344463583 scopus 로고    scopus 로고
    • fgf20 is essential for initiating zebrafish fin regeneration
    • Whitehead, G. G., S. Makino, C. L. Lien, and M. T. Keating. 2005. fgf20 is essential for initiating zebrafish fin regeneration. Science 310:1957-1960.
    • (2005) Science , vol.310 , pp. 1957-1960
    • Whitehead, G.G.1    Makino, S.2    Lien, C.L.3    Keating, M.T.4
  • 67
    • 17844402791 scopus 로고    scopus 로고
    • Bad bones, absent smell, selfish testes: The pleiotropic consequences of human FGF receptor mutations
    • Wilkie, A. O. 2005. Bad bones, absent smell, selfish testes: the pleiotropic consequences of human FGF receptor mutations. Cytokine Growth Factor Rev. 16:187-203.
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 187-203
    • Wilkie, A.O.1
  • 68
    • 0031885801 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation loop between FGF8 and FGF10 is essential for limb induction
    • Xu, X., M. Weinstein, C. Li, M. Naski, R. I. Cohen, D. M. Ornitz, P. Leder, and C. Deng. 1998. Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation loop between FGF8 and FGF10 is essential for limb induction. Development 125:753-765.
    • (1998) Development , vol.125 , pp. 753-765
    • Xu, X.1    Weinstein, M.2    Li, C.3    Naski, M.4    Cohen, R.I.5    Ornitz, D.M.6    Leder, P.7    Deng, C.8
  • 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., M. Klagsbrun, J. D. Esko, P. Leder, and D. M. Ornitz. 1991. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 64:841-848.
    • (1991) Cell , vol.64 , pp. 841-848
    • Yayon, A.1    Klagsbrun, M.2    Esko, J.D.3    Leder, P.4    Ornitz, D.M.5
  • 71


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