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Volumn 25, Issue 4, 2015, Pages 221-233

Careless talk costs lives: Fibroblast growth factor receptor signalling and the consequences of pathway malfunction

Author keywords

Cancer; Cell signalling; Fibroblast growth factor; Fibroblast growth factor receptor

Indexed keywords

FIBROBLAST GROWTH FACTOR RECEPTOR; PHOSPHOTRANSFERASE INHIBITOR; FIBROBLAST GROWTH FACTOR;

EID: 84925456768     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2014.11.003     Document Type: Review
Times cited : (128)

References (136)
  • 1
    • 84878942800 scopus 로고    scopus 로고
    • Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology
    • Published online June 1, 2013.
    • Belov, A.A. and Mohammadi, M. (2013) Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology. Cold Spring Harb. Perspect. Biol. 5 Published online June 1, 2013. doi:10.1101/cshperspect.a015958.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5
    • Belov, A.A.1    Mohammadi, M.2
  • 2
    • 84868260259 scopus 로고    scopus 로고
    • Alternative splicing of fibroblast growth factor receptor IgIII loops in cancer
    • Holzmann K., et al. Alternative splicing of fibroblast growth factor receptor IgIII loops in cancer. J. Nucleic Acids 2011, 2012:950508.
    • (2011) J. Nucleic Acids , vol.2012 , pp. 950508
    • Holzmann, K.1
  • 3
    • 0035958277 scopus 로고    scopus 로고
    • Identification of a new fibroblast growth factor receptor, FGFR5
    • Sleeman M., et al. Identification of a new fibroblast growth factor receptor, FGFR5. Gene 2001, 271:171-182.
    • (2001) Gene , vol.271 , pp. 171-182
    • Sleeman, M.1
  • 4
    • 67650323999 scopus 로고    scopus 로고
    • Multiple congenital malformations of Wolf-Hirschhorn syndrome are recapitulated in Fgfrl1 null mice
    • Catela C., et al. Multiple congenital malformations of Wolf-Hirschhorn syndrome are recapitulated in Fgfrl1 null mice. Dis. Model Mech. 2009, 2:283-294.
    • (2009) Dis. Model Mech. , vol.2 , pp. 283-294
    • Catela, C.1
  • 5
    • 84925403522 scopus 로고    scopus 로고
    • Targeted disruption of the intracellular domain of receptor FgfrL1 in mice
    • Bluteau G., et al. Targeted disruption of the intracellular domain of receptor FgfrL1 in mice. PLoS ONE 2014, 9:e105210.
    • (2014) PLoS ONE , vol.9 , pp. e105210
    • Bluteau, G.1
  • 6
    • 84879054546 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor like-1 (FGFRL1) interacts with SHP-1 phosphatase at insulin secretory granules and induces beta-cell ERK1/2 protein activation
    • Silva P.N., et al. Fibroblast growth factor receptor like-1 (FGFRL1) interacts with SHP-1 phosphatase at insulin secretory granules and induces beta-cell ERK1/2 protein activation. J. Biol. Chem. 2013, 288:17859-17870.
    • (2013) J. Biol. Chem. , vol.288 , pp. 17859-17870
    • Silva, P.N.1
  • 7
    • 84875421249 scopus 로고    scopus 로고
    • Exploring mechanisms of FGF signalling through the lens of structural biology
    • Goetz R., Mohammadi M. Exploring mechanisms of FGF signalling through the lens of structural biology. Nat. Rev. Mol. Cell Biol. 2013, 14:166-180.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 166-180
    • Goetz, R.1    Mohammadi, M.2
  • 8
    • 34247565954 scopus 로고    scopus 로고
    • Molecular insights into the klotho-dependent, endocrine mode of action of fibroblast growth factor 19 subfamily members
    • Goetz R., et al. Molecular insights into the klotho-dependent, endocrine mode of action of fibroblast growth factor 19 subfamily members. Mol. Cell. Biol. 2007, 27:3417-3428.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3417-3428
    • Goetz, R.1
  • 9
    • 84865258676 scopus 로고    scopus 로고
    • Conversion of a paracrine fibroblast growth factor into an endocrine fibroblast growth factor
    • Goetz R., et al. Conversion of a paracrine fibroblast growth factor into an endocrine fibroblast growth factor. J. Biol. Chem. 2012, 287:29134-29146.
    • (2012) J. Biol. Chem. , vol.287 , pp. 29134-29146
    • Goetz, R.1
  • 10
    • 84861355961 scopus 로고    scopus 로고
    • Klotho coreceptors inhibit signaling by paracrine fibroblast growth factor 8 subfamily ligands
    • Goetz R., et al. Klotho coreceptors inhibit signaling by paracrine fibroblast growth factor 8 subfamily ligands. Mol. Cell. Biol. 2012, 32:1944-1954.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1944-1954
    • Goetz, R.1
  • 11
    • 77953679934 scopus 로고    scopus 로고
    • The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations
    • Lew E.D., et al. The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations. Sci. Signal. 2009, 2:ra6.
    • (2009) Sci. Signal. , vol.2 , pp. ra6
    • Lew, E.D.1
  • 12
    • 0025941527 scopus 로고
    • A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1
    • Mohammadi M., et al. A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1. Mol. Cell. Biol. 1991, 11:5068-5078.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5068-5078
    • Mohammadi, M.1
  • 13
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • Kouhara H., et al. A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell 1997, 89:693-702.
    • (1997) Cell , vol.89 , pp. 693-702
    • Kouhara, H.1
  • 14
    • 0034612592 scopus 로고    scopus 로고
    • Transformation and Stat activation by derivatives of FGFR1, FGFR3, and FGFR4
    • Hart K.C., et al. Transformation and Stat activation by derivatives of FGFR1, FGFR3, and FGFR4. Oncogene 2000, 19:3309-3320.
    • (2000) Oncogene , vol.19 , pp. 3309-3320
    • Hart, K.C.1
  • 15
    • 0035933094 scopus 로고    scopus 로고
    • Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins
    • Ong S.H., et al. Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:6074-6079.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6074-6079
    • Ong, S.H.1
  • 16
    • 0037076329 scopus 로고    scopus 로고
    • FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl
    • Wong A., et al. FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:6684-6689.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6684-6689
    • Wong, A.1
  • 17
    • 33745870798 scopus 로고    scopus 로고
    • Negative feedback predominates over cross-regulation to control ERK MAPK activity in response to FGF signalling in embryos
    • Smith T.G., et al. Negative feedback predominates over cross-regulation to control ERK MAPK activity in response to FGF signalling in embryos. FEBS Lett. 2006, 580:4242-4245.
    • (2006) FEBS Lett. , vol.580 , pp. 4242-4245
    • Smith, T.G.1
  • 18
    • 0344440845 scopus 로고    scopus 로고
    • Functional analysis of the human Sprouty2 gene promoter
    • Ding W., et al. Functional analysis of the human Sprouty2 gene promoter. Gene 2003, 322:175-185.
    • (2003) Gene , vol.322 , pp. 175-185
    • Ding, W.1
  • 19
    • 0038476592 scopus 로고    scopus 로고
    • Sef inhibits fibroblast growth factor signaling by inhibiting FGFR1 tyrosine phosphorylation and subsequent ERK activation
    • Kovalenko D., et al. Sef inhibits fibroblast growth factor signaling by inhibiting FGFR1 tyrosine phosphorylation and subsequent ERK activation. J. Biol. Chem. 2003, 278:14087-14091.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14087-14091
    • Kovalenko, D.1
  • 20
    • 84874222465 scopus 로고    scopus 로고
    • ERK-mediated phosphorylation of fibroblast growth factor receptor 1 on Ser777 inhibits signaling
    • Zakrzewska M., et al. ERK-mediated phosphorylation of fibroblast growth factor receptor 1 on Ser777 inhibits signaling. Sci. Signal. 2013, 6:ra11.
    • (2013) Sci. Signal. , vol.6 , pp. ra11
    • Zakrzewska, M.1
  • 21
    • 84862669198 scopus 로고    scopus 로고
    • Inhibition of basal FGF receptor signaling by dimeric Grb2
    • Lin C.C., et al. Inhibition of basal FGF receptor signaling by dimeric Grb2. Cell 2012, 149:1514-1524.
    • (2012) Cell , vol.149 , pp. 1514-1524
    • Lin, C.C.1
  • 22
    • 84874368710 scopus 로고    scopus 로고
    • Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity
    • Ahmed Z., et al. Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity. J. Cell Biol. 2013, 200:493-504.
    • (2013) J. Cell Biol. , vol.200 , pp. 493-504
    • Ahmed, Z.1
  • 23
    • 84893769451 scopus 로고    scopus 로고
    • Competition between Grb2 and Plcgamma1 for FGFR2 regulates basal phospholipase activity and invasion
    • Timsah Z., et al. Competition between Grb2 and Plcgamma1 for FGFR2 regulates basal phospholipase activity and invasion. Nat. Struct. Mol. Biol. 2014, 21:180-188.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 180-188
    • Timsah, Z.1
  • 24
    • 84893731921 scopus 로고    scopus 로고
    • Grb-ing receptor activation by the tail
    • Fearon A.E., Grose R.P. Grb-ing receptor activation by the tail. Nat. Struct. Mol. Biol. 2014, 21:113-114.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 113-114
    • Fearon, A.E.1    Grose, R.P.2
  • 25
    • 84884586861 scopus 로고    scopus 로고
    • Functional proteomics defines the molecular switch underlying FGF receptor trafficking and cellular outputs
    • Francavilla C., et al. Functional proteomics defines the molecular switch underlying FGF receptor trafficking and cellular outputs. Mol. Cell 2013, 51:707-722.
    • (2013) Mol. Cell , vol.51 , pp. 707-722
    • Francavilla, C.1
  • 26
    • 73949157671 scopus 로고    scopus 로고
    • Differential interactions of FGFs with heparan sulfate control gradient formation and branching morphogenesis
    • Makarenkova H.P., et al. Differential interactions of FGFs with heparan sulfate control gradient formation and branching morphogenesis. Sci. Signal. 2009, 2:ra55.
    • (2009) Sci. Signal. , vol.2 , pp. ra55
    • Makarenkova, H.P.1
  • 27
    • 84899856088 scopus 로고    scopus 로고
    • The ins and outs of fibroblast growth factor receptor signalling
    • Coleman S.J., et al. The ins and outs of fibroblast growth factor receptor signalling. Clin. Sci. (Lond.) 2014, 127:217-231.
    • (2014) Clin. Sci. (Lond.) , vol.127 , pp. 217-231
    • Coleman, S.J.1
  • 28
    • 84858800071 scopus 로고    scopus 로고
    • Nuclear translocation and functions of growth factor receptors
    • Mills I.G. Nuclear translocation and functions of growth factor receptors. Semin. Cell Dev. Biol. 2011, 23:165-171.
    • (2011) Semin. Cell Dev. Biol. , vol.23 , pp. 165-171
    • Mills, I.G.1
  • 29
    • 84864001533 scopus 로고    scopus 로고
    • FGFR1 cleavage and nuclear translocation regulates breast cancer cell behavior
    • Chioni A.M., Grose R. FGFR1 cleavage and nuclear translocation regulates breast cancer cell behavior. J. Cell Biol. 2012, 197:801-817.
    • (2012) J. Cell Biol. , vol.197 , pp. 801-817
    • Chioni, A.M.1    Grose, R.2
  • 30
    • 84897413643 scopus 로고    scopus 로고
    • Nuclear translocation of FGFR1 and FGF2 in pancreatic stellate cells facilitates pancreatic cancer cell invasion
    • Coleman S.J., et al. Nuclear translocation of FGFR1 and FGF2 in pancreatic stellate cells facilitates pancreatic cancer cell invasion. EMBO Mol. Med. 2014, 6:467-481.
    • (2014) EMBO Mol. Med. , vol.6 , pp. 467-481
    • Coleman, S.J.1
  • 31
    • 84862025583 scopus 로고    scopus 로고
    • A novel nuclear FGF Receptor-1 partnership with retinoid and Nur receptors during developmental gene programming of embryonic stem cells
    • Lee Y.W., et al. A novel nuclear FGF Receptor-1 partnership with retinoid and Nur receptors during developmental gene programming of embryonic stem cells. J. Cell. Biochem. 2012, 113:2920-2936.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 2920-2936
    • Lee, Y.W.1
  • 32
    • 84862003773 scopus 로고    scopus 로고
    • Cooperation of nuclear fibroblast growth factor receptor 1 and Nurr1 offers new interactive mechanism in postmitotic development of mesencephalic dopaminergic neurons
    • Baron O., et al. Cooperation of nuclear fibroblast growth factor receptor 1 and Nurr1 offers new interactive mechanism in postmitotic development of mesencephalic dopaminergic neurons. J. Biol. Chem. 2012, 287:19827-19840.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19827-19840
    • Baron, O.1
  • 33
    • 84879996732 scopus 로고    scopus 로고
    • NGF-induced cell differentiation and gene activation is mediated by integrative nuclear FGFR1 signaling (INFS)
    • Lee Y.W., et al. NGF-induced cell differentiation and gene activation is mediated by integrative nuclear FGFR1 signaling (INFS). PLoS ONE 2013, 8:e68931.
    • (2013) PLoS ONE , vol.8 , pp. e68931
    • Lee, Y.W.1
  • 34
    • 79952452423 scopus 로고    scopus 로고
    • Translocation of exogenous FGF1 into cytosol and nucleus is a periodic event independent of receptor kinase activity
    • Zakrzewska M., et al. Translocation of exogenous FGF1 into cytosol and nucleus is a periodic event independent of receptor kinase activity. Exp. Cell Res. 2011, 317:1005-1015.
    • (2011) Exp. Cell Res. , vol.317 , pp. 1005-1015
    • Zakrzewska, M.1
  • 35
    • 84859603522 scopus 로고    scopus 로고
    • Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnalpha1 and Kpnbeta1
    • Zhen Y., et al. Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnalpha1 and Kpnbeta1. Traffic 2012, 13:650-664.
    • (2012) Traffic , vol.13 , pp. 650-664
    • Zhen, Y.1
  • 36
    • 0029820043 scopus 로고    scopus 로고
    • Fibroblast growth factor (FGF) homologous factors: new members of the FGF family implicated in nervous system development
    • Smallwood P.M., et al. Fibroblast growth factor (FGF) homologous factors: new members of the FGF family implicated in nervous system development. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:9850-9857.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 9850-9857
    • Smallwood, P.M.1
  • 37
    • 0037428518 scopus 로고    scopus 로고
    • Modulation of the cardiac sodium channel Nav1.5 by fibroblast growth factor homologous factor 1B
    • Liu C.J., et al. Modulation of the cardiac sodium channel Nav1.5 by fibroblast growth factor homologous factor 1B. J. Biol. Chem. 2003, 278:1029-1036.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1029-1036
    • Liu, C.J.1
  • 38
    • 84892443614 scopus 로고    scopus 로고
    • FGF14 regulates presynaptic Ca2+ channels and synaptic transmission
    • Yan H., et al. FGF14 regulates presynaptic Ca2+ channels and synaptic transmission. Cell Rep. 2013, 4:66-75.
    • (2013) Cell Rep. , vol.4 , pp. 66-75
    • Yan, H.1
  • 39
    • 84881670624 scopus 로고    scopus 로고
    • Fibroblast growth factor homologous factors modulate cardiac calcium channels
    • Hennessey J.A., et al. Fibroblast growth factor homologous factors modulate cardiac calcium channels. Circ. Res. 2013, 113:381-388.
    • (2013) Circ. Res. , vol.113 , pp. 381-388
    • Hennessey, J.A.1
  • 41
    • 79955002353 scopus 로고    scopus 로고
    • FGF signaling in craniofacial biological control and pathological craniofacial development
    • Hatch N.E. FGF signaling in craniofacial biological control and pathological craniofacial development. Crit. Rev. Eukaryot. Gene Expr. 2010, 20:295-311.
    • (2010) Crit. Rev. Eukaryot. Gene Expr. , vol.20 , pp. 295-311
    • Hatch, N.E.1
  • 42
    • 0034687699 scopus 로고    scopus 로고
    • Loss of fibroblast growth factor receptor 2 ligand-binding specificity in Apert syndrome
    • Yu K., et al. Loss of fibroblast growth factor receptor 2 ligand-binding specificity in Apert syndrome. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:14536-14541.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14536-14541
    • Yu, K.1
  • 43
    • 0029059280 scopus 로고
    • Analysis of phenotypic features and FGFR2 mutations in Apert syndrome
    • Park W.J., et al. Analysis of phenotypic features and FGFR2 mutations in Apert syndrome. Am. J. Hum. Genet. 1995, 57:321-328.
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 321-328
    • Park, W.J.1
  • 44
    • 24344453489 scopus 로고    scopus 로고
    • Abnormalities in cartilage and bone development in the Apert syndrome FGFR2(+/S252W) mouse
    • Wang Y., et al. Abnormalities in cartilage and bone development in the Apert syndrome FGFR2(+/S252W) mouse. Development 2005, 132:3537-3548.
    • (2005) Development , vol.132 , pp. 3537-3548
    • Wang, Y.1
  • 45
    • 84900305191 scopus 로고    scopus 로고
    • A Ser252Trp mutation in fibroblast growth factor receptor 2 (FGFR2) mimicking human Apert syndrome reveals an essential role for FGF signaling in the regulation of endochondral bone formation
    • Chen P., et al. A Ser252Trp mutation in fibroblast growth factor receptor 2 (FGFR2) mimicking human Apert syndrome reveals an essential role for FGF signaling in the regulation of endochondral bone formation. PLoS ONE 2014, 9:e87311.
    • (2014) PLoS ONE , vol.9 , pp. e87311
    • Chen, P.1
  • 46
    • 84903974347 scopus 로고    scopus 로고
    • Therapeutic effect of nanogel-based delivery of soluble FGFR2 with S252W mutation on craniosynostosis
    • Yokota M., et al. Therapeutic effect of nanogel-based delivery of soluble FGFR2 with S252W mutation on craniosynostosis. PLoS ONE 2014, 9:e101693.
    • (2014) PLoS ONE , vol.9 , pp. e101693
    • Yokota, M.1
  • 47
    • 20244366799 scopus 로고    scopus 로고
    • Loss-of-function mutations in FGFR1 cause autosomal dominant Kallmann syndrome
    • Dode C., et al. Loss-of-function mutations in FGFR1 cause autosomal dominant Kallmann syndrome. Nat. Genet. 2003, 33:463-465.
    • (2003) Nat. Genet. , vol.33 , pp. 463-465
    • Dode, C.1
  • 48
    • 84865537839 scopus 로고    scopus 로고
    • Molecular basis for the Kallmann syndrome-linked fibroblast growth factor receptor mutation
    • Thurman R.D., et al. Molecular basis for the Kallmann syndrome-linked fibroblast growth factor receptor mutation. Biochem. Biophys. Res. Commun. 2012, 425:673-678.
    • (2012) Biochem. Biophys. Res. Commun. , vol.425 , pp. 673-678
    • Thurman, R.D.1
  • 49
    • 80053551866 scopus 로고    scopus 로고
    • Novel FGF8 mutations associated with recessive holoprosencephaly, craniofacial defects, and hypothalamo-pituitary dysfunction
    • McCabe M.J., et al. Novel FGF8 mutations associated with recessive holoprosencephaly, craniofacial defects, and hypothalamo-pituitary dysfunction. J. Clin. Endocrinol. Metab. 2011, 96:E1709-E1718.
    • (2011) J. Clin. Endocrinol. Metab. , vol.96 , pp. E1709-E1718
    • McCabe, M.J.1
  • 50
    • 78649513377 scopus 로고    scopus 로고
    • A hypomorphic allele in the FGF8 gene contributes to holoprosencephaly and is allelic to gonadotropin-releasing hormone deficiency in humans
    • Arauz R.F., et al. A hypomorphic allele in the FGF8 gene contributes to holoprosencephaly and is allelic to gonadotropin-releasing hormone deficiency in humans. Mol. Syndromol. 2010, 1:59-66.
    • (2010) Mol. Syndromol. , vol.1 , pp. 59-66
    • Arauz, R.F.1
  • 51
    • 0035253507 scopus 로고    scopus 로고
    • Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM domain of p63
    • McGrath J.A., et al. Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM domain of p63. Hum. Mol. Genet. 2001, 10:221-229.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 221-229
    • McGrath, J.A.1
  • 52
    • 84863229693 scopus 로고    scopus 로고
    • Mutant p63 causes defective expansion of ectodermal progenitor cells and impaired FGF signalling in AEC syndrome
    • Ferone G., et al. Mutant p63 causes defective expansion of ectodermal progenitor cells and impaired FGF signalling in AEC syndrome. EMBO Mol. Med. 2012, 4:192-205.
    • (2012) EMBO Mol. Med. , vol.4 , pp. 192-205
    • Ferone, G.1
  • 53
    • 84889795225 scopus 로고    scopus 로고
    • FGF12 is a candidate Brugada syndrome locus
    • Hennessey J.A., et al. FGF12 is a candidate Brugada syndrome locus. Heart Rhythm 2013, 10:1886-1894.
    • (2013) Heart Rhythm , vol.10 , pp. 1886-1894
    • Hennessey, J.A.1
  • 54
    • 77949690425 scopus 로고    scopus 로고
    • Fibroblast growth factor receptors 1 and 2 in keratinocytes control the epidermal barrier and cutaneous homeostasis
    • Yang J., et al. Fibroblast growth factor receptors 1 and 2 in keratinocytes control the epidermal barrier and cutaneous homeostasis. J. Cell Biol. 2010, 188:935-952.
    • (2010) J. Cell Biol. , vol.188 , pp. 935-952
    • Yang, J.1
  • 55
    • 0037177385 scopus 로고    scopus 로고
    • A role for skin gammadelta T cells in wound repair
    • Jameson J., et al. A role for skin gammadelta T cells in wound repair. Science 2002, 296:747-749.
    • (2002) Science , vol.296 , pp. 747-749
    • Jameson, J.1
  • 56
    • 84880303382 scopus 로고    scopus 로고
    • Fgf9 from dermal gammadelta T cells induces hair follicle neogenesis after wounding
    • Gay D., et al. Fgf9 from dermal gammadelta T cells induces hair follicle neogenesis after wounding. Nat. Med. 2013, 19:916-923.
    • (2013) Nat. Med. , vol.19 , pp. 916-923
    • Gay, D.1
  • 57
    • 0026695949 scopus 로고
    • Large induction of keratinocyte growth factor expression in the dermis during wound healing
    • Werner S., et al. Large induction of keratinocyte growth factor expression in the dermis during wound healing. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:6896-6900.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6896-6900
    • Werner, S.1
  • 58
    • 0028053872 scopus 로고
    • The function of KGF in morphogenesis of epithelium and reepithelialization of wounds
    • Werner S., et al. The function of KGF in morphogenesis of epithelium and reepithelialization of wounds. Science 1994, 266:819-822.
    • (1994) Science , vol.266 , pp. 819-822
    • Werner, S.1
  • 59
    • 84870534441 scopus 로고    scopus 로고
    • FGF receptors 1 and 2 are key regulators of keratinocyte migration in vitro and in wounded skin
    • Meyer M., et al. FGF receptors 1 and 2 are key regulators of keratinocyte migration in vitro and in wounded skin. J. Cell Sci. 2012, 125:5690-5701.
    • (2012) J. Cell Sci. , vol.125 , pp. 5690-5701
    • Meyer, M.1
  • 60
    • 84907215716 scopus 로고    scopus 로고
    • Endothelial cell FGF signaling is required for injury response but not for vascular homeostasis
    • Oladipupo S.S., et al. Endothelial cell FGF signaling is required for injury response but not for vascular homeostasis. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:13379-13384.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 13379-13384
    • Oladipupo, S.S.1
  • 61
    • 5044232017 scopus 로고    scopus 로고
    • Liver regeneration: from myth to mechanism
    • Taub R. Liver regeneration: from myth to mechanism. Nat. Rev. Mol. Cell Biol. 2004, 5:836-847.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 836-847
    • Taub, R.1
  • 62
    • 77956958497 scopus 로고    scopus 로고
    • Regulation of liver regeneration by growth factors and cytokines
    • Bohm F., et al. Regulation of liver regeneration by growth factors and cytokines. EMBO Mol. Med. 2010, 2:294-305.
    • (2010) EMBO Mol. Med. , vol.2 , pp. 294-305
    • Bohm, F.1
  • 63
    • 0042804872 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor signalling is crucial for liver homeostasis and regeneration
    • Steiling H., et al. Fibroblast growth factor receptor signalling is crucial for liver homeostasis and regeneration. Oncogene 2003, 22:4380-4388.
    • (2003) Oncogene , vol.22 , pp. 4380-4388
    • Steiling, H.1
  • 64
    • 77956963188 scopus 로고    scopus 로고
    • FGF receptors 1 and 2 control chemically induced injury and compound detoxification in regenerating livers of mice
    • Bohm F., et al. FGF receptors 1 and 2 control chemically induced injury and compound detoxification in regenerating livers of mice. Gastroenterology 2010, 139:1385-1396.
    • (2010) Gastroenterology , vol.139 , pp. 1385-1396
    • Bohm, F.1
  • 65
    • 0036898019 scopus 로고    scopus 로고
    • Increased carbon tetrachloride-induced liver injury and fibrosis in FGFR4-deficient mice
    • Yu C., et al. Increased carbon tetrachloride-induced liver injury and fibrosis in FGFR4-deficient mice. Am. J. Pathol. 2002, 161:2003-2010.
    • (2002) Am. J. Pathol. , vol.161 , pp. 2003-2010
    • Yu, C.1
  • 66
    • 34848866633 scopus 로고    scopus 로고
    • Liver-specific activities of FGF19 require Klotho beta
    • Lin B.C., et al. Liver-specific activities of FGF19 require Klotho beta. J. Biol. Chem. 2007, 282:27277-27284.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27277-27284
    • Lin, B.C.1
  • 67
    • 84873020006 scopus 로고    scopus 로고
    • FGF7 is a functional niche signal required for stimulation of adult liver progenitor cells that support liver regeneration
    • Takase H.M., et al. FGF7 is a functional niche signal required for stimulation of adult liver progenitor cells that support liver regeneration. Genes Dev. 2013, 27:169-181.
    • (2013) Genes Dev. , vol.27 , pp. 169-181
    • Takase, H.M.1
  • 68
    • 84876934226 scopus 로고    scopus 로고
    • Identification of fibroblast growth factor 15 as a novel mediator of liver regeneration and its application in the prevention of post-resection liver failure in mice
    • Uriarte I., et al. Identification of fibroblast growth factor 15 as a novel mediator of liver regeneration and its application in the prevention of post-resection liver failure in mice. Gut 2013, 62:899-910.
    • (2013) Gut , vol.62 , pp. 899-910
    • Uriarte, I.1
  • 69
    • 84904418941 scopus 로고    scopus 로고
    • Tissue crosstalk in lung development
    • Hines E.A., Sun X. Tissue crosstalk in lung development. J. Cell. Biochem. 2014, 115:1469-1477.
    • (2014) J. Cell. Biochem. , vol.115 , pp. 1469-1477
    • Hines, E.A.1    Sun, X.2
  • 70
    • 80555148937 scopus 로고    scopus 로고
    • Parabronchial smooth muscle constitutes an airway epithelial stem cell niche in the mouse lung after injury
    • Volckaert T., et al. Parabronchial smooth muscle constitutes an airway epithelial stem cell niche in the mouse lung after injury. J. Clin. Invest. 2011, 121:4409-4419.
    • (2011) J. Clin. Invest. , vol.121 , pp. 4409-4419
    • Volckaert, T.1
  • 71
    • 84886779431 scopus 로고    scopus 로고
    • Expression of fibroblast growth factor 9 in normal human lung and idiopathic pulmonary fibrosis
    • Coffey E., et al. Expression of fibroblast growth factor 9 in normal human lung and idiopathic pulmonary fibrosis. J. Histochem. Cytochem. 2013, 61:671-679.
    • (2013) J. Histochem. Cytochem. , vol.61 , pp. 671-679
    • Coffey, E.1
  • 72
    • 84861209036 scopus 로고    scopus 로고
    • Mutant soluble ectodomain of fibroblast growth factor receptor-2 IIIc attenuates bleomycin-induced pulmonary fibrosis in mice
    • Yu Z.H., et al. Mutant soluble ectodomain of fibroblast growth factor receptor-2 IIIc attenuates bleomycin-induced pulmonary fibrosis in mice. Biol. Pharm. Bull. 2012, 35:731-736.
    • (2012) Biol. Pharm. Bull. , vol.35 , pp. 731-736
    • Yu, Z.H.1
  • 73
    • 71049119028 scopus 로고    scopus 로고
    • Bone marrow stem cells expressing keratinocyte growth factor via an inducible lentivirus protects against bleomycin-induced pulmonary fibrosis
    • Aguilar S., et al. Bone marrow stem cells expressing keratinocyte growth factor via an inducible lentivirus protects against bleomycin-induced pulmonary fibrosis. PLoS ONE 2009, 4:e8013.
    • (2009) PLoS ONE , vol.4 , pp. e8013
    • Aguilar, S.1
  • 74
    • 84925403521 scopus 로고    scopus 로고
    • FGF2 is required for epithelial recovery, but not for pulmonary fibrosis, in response to bleomycin
    • Published online July 2, 2014
    • Guzy R.D., et al. FGF2 is required for epithelial recovery, but not for pulmonary fibrosis, in response to bleomycin. Am. J. Respir. Cell Mol. Biol. 2014, Published online July 2, 2014.
    • (2014) Am. J. Respir. Cell Mol. Biol.
    • Guzy, R.D.1
  • 75
    • 75149170979 scopus 로고    scopus 로고
    • Fibroblast growth factor signalling: from development to cancer
    • Turner N., Grose R. Fibroblast growth factor signalling: from development to cancer. Nat. Rev. Cancer 2010, 10:116-129.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 116-129
    • Turner, N.1    Grose, R.2
  • 76
    • 84871803181 scopus 로고    scopus 로고
    • FGFR2 promotes breast tumorigenicity through maintenance of breast tumor-initiating cells
    • Kim S., et al. FGFR2 promotes breast tumorigenicity through maintenance of breast tumor-initiating cells. PLoS ONE 2013, 8:e51671.
    • (2013) PLoS ONE , vol.8 , pp. e51671
    • Kim, S.1
  • 77
    • 84907289340 scopus 로고    scopus 로고
    • Prostate cancer cell-stromal cell crosstalk via FGFR1 mediates antitumor activity of dovitinib in bone metastases
    • 252ra122
    • Wan X., et al. Prostate cancer cell-stromal cell crosstalk via FGFR1 mediates antitumor activity of dovitinib in bone metastases. Sci. Transl. Med. 2014, 6:252ra122.
    • (2014) Sci. Transl. Med. , vol.6
    • Wan, X.1
  • 78
    • 84925440138 scopus 로고    scopus 로고
    • Prognostic value of FGFR gene amplification in patients with different types of cancer: a systematic review and meta-analysis
    • Chang J., et al. Prognostic value of FGFR gene amplification in patients with different types of cancer: a systematic review and meta-analysis. PLoS ONE 2014, 9:e105524.
    • (2014) PLoS ONE , vol.9 , pp. e105524
    • Chang, J.1
  • 79
    • 84925408760 scopus 로고    scopus 로고
    • Phase I/IIa study evaluating the safety, efficacy, pharmacokinetics, and pharmacodynamics of lucitanib in advanced solid tumors
    • 2014
    • Soria J.C., et al. Phase I/IIa study evaluating the safety, efficacy, pharmacokinetics, and pharmacodynamics of lucitanib in advanced solid tumors. Ann. Oncol. 2014, 25:2244-2251. 2014.
    • (2014) Ann. Oncol. , vol.25 , pp. 2244-2251
    • Soria, J.C.1
  • 80
    • 84879859652 scopus 로고    scopus 로고
    • Targeting FGFR with dovitinib (TKI258): preclinical and clinical data in breast cancer
    • Andre F., et al. Targeting FGFR with dovitinib (TKI258): preclinical and clinical data in breast cancer. Clin. Cancer Res. 2013, 19:3693-3702.
    • (2013) Clin. Cancer Res. , vol.19 , pp. 3693-3702
    • Andre, F.1
  • 81
    • 78650451788 scopus 로고    scopus 로고
    • Frequent and focal FGFR1 amplification associates with therapeutically tractable FGFR1 dependency in squamous cell lung cancer
    • Weiss J., et al. Frequent and focal FGFR1 amplification associates with therapeutically tractable FGFR1 dependency in squamous cell lung cancer. Sci. Transl. Med. 2010, 2:62ra93.
    • (2010) Sci. Transl. Med. , vol.2 , pp. 62ra93
    • Weiss, J.1
  • 82
    • 84875189537 scopus 로고    scopus 로고
    • Activating somatic FGFR2 mutations in breast cancer
    • Reintjes N., et al. Activating somatic FGFR2 mutations in breast cancer. PLoS ONE 2013, 8:e60264.
    • (2013) PLoS ONE , vol.8 , pp. e60264
    • Reintjes, N.1
  • 83
    • 84907056979 scopus 로고    scopus 로고
    • Kinase domain activation of FGFR2 yields high-grade lung adenocarcinoma sensitive to a Pan-FGFR inhibitor in a mouse model of NSCLC
    • Tchaicha J.H., et al. Kinase domain activation of FGFR2 yields high-grade lung adenocarcinoma sensitive to a Pan-FGFR inhibitor in a mouse model of NSCLC. Cancer Res. 2014, 74:4676-4684.
    • (2014) Cancer Res. , vol.74 , pp. 4676-4684
    • Tchaicha, J.H.1
  • 84
    • 34250001297 scopus 로고    scopus 로고
    • A genome-wide association study identifies alleles in FGFR2 associated with risk of sporadic postmenopausal breast cancer
    • Hunter D.J., et al. A genome-wide association study identifies alleles in FGFR2 associated with risk of sporadic postmenopausal breast cancer. Nat. Genet. 2007, 39:870-874.
    • (2007) Nat. Genet. , vol.39 , pp. 870-874
    • Hunter, D.J.1
  • 85
    • 34250006413 scopus 로고    scopus 로고
    • Genome-wide association study identifies novel breast cancer susceptibility loci
    • Easton D.F., et al. Genome-wide association study identifies novel breast cancer susceptibility loci. Nature 2007, 447:1087-1093.
    • (2007) Nature , vol.447 , pp. 1087-1093
    • Easton, D.F.1
  • 86
    • 84860404613 scopus 로고    scopus 로고
    • Allele-specific regulation of FGFR2 expression is cell type-dependent and may increase breast cancer risk through a paracrine stimulus involving FGF10
    • Huijts P.E., et al. Allele-specific regulation of FGFR2 expression is cell type-dependent and may increase breast cancer risk through a paracrine stimulus involving FGF10. Breast Cancer Res. 2011, 13:R72.
    • (2011) Breast Cancer Res. , vol.13 , pp. R72
    • Huijts, P.E.1
  • 87
    • 84897550953 scopus 로고    scopus 로고
    • Clinical significance of fibroblast growth factor receptor-3 mutations in bladder cancer: a systematic review and meta-analysis
    • Liu X., et al. Clinical significance of fibroblast growth factor receptor-3 mutations in bladder cancer: a systematic review and meta-analysis. Genet. Mol. Res. 2014, 13:1109-1120.
    • (2014) Genet. Mol. Res. , vol.13 , pp. 1109-1120
    • Liu, X.1
  • 88
    • 84923116560 scopus 로고    scopus 로고
    • FGFR3 overexpression is prognostic of adverse outcome for muscle-invasive bladder carcinoma treated with adjuvant chemotherapy
    • e23-31
    • Sung J.Y., et al. FGFR3 overexpression is prognostic of adverse outcome for muscle-invasive bladder carcinoma treated with adjuvant chemotherapy. Urol. Oncol. 2013, 32:49. e23-31.
    • (2013) Urol. Oncol. , vol.32 , pp. 49
    • Sung, J.Y.1
  • 89
    • 84866499993 scopus 로고    scopus 로고
    • Mutations in FGFR3 and PIK3CA, singly or combined with RAS and AKT1, are associated with AKT but not with MAPK pathway activation in urothelial bladder cancer
    • Juanpere N., et al. Mutations in FGFR3 and PIK3CA, singly or combined with RAS and AKT1, are associated with AKT but not with MAPK pathway activation in urothelial bladder cancer. Hum. Pathol. 2012, 43:1573-1582.
    • (2012) Hum. Pathol. , vol.43 , pp. 1573-1582
    • Juanpere, N.1
  • 90
    • 84900833911 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 3 activation plays a causative role in urothelial cancer pathogenesis in cooperation with Pten loss in mice
    • Foth M., et al. Fibroblast growth factor receptor 3 activation plays a causative role in urothelial cancer pathogenesis in cooperation with Pten loss in mice. J. Pathol. 2014, 233:148-158.
    • (2014) J. Pathol. , vol.233 , pp. 148-158
    • Foth, M.1
  • 91
    • 84871074734 scopus 로고    scopus 로고
    • The t(4;14) translocation and FGFR3 overexpression in multiple myeloma: prognostic implications and current clinical strategies
    • Kalff A., Spencer A. The t(4;14) translocation and FGFR3 overexpression in multiple myeloma: prognostic implications and current clinical strategies. Blood Cancer J. 2012, 2:e89.
    • (2012) Blood Cancer J. , vol.2 , pp. e89
    • Kalff, A.1    Spencer, A.2
  • 92
    • 84896691170 scopus 로고    scopus 로고
    • Comprehensive genomic analysis of rhabdomyosarcoma reveals a landscape of alterations affecting a common genetic axis in fusion-positive and fusion-negative tumors
    • Shern J.F., et al. Comprehensive genomic analysis of rhabdomyosarcoma reveals a landscape of alterations affecting a common genetic axis in fusion-positive and fusion-negative tumors. Cancer Discov. 2014, 4:216-231.
    • (2014) Cancer Discov. , vol.4 , pp. 216-231
    • Shern, J.F.1
  • 93
    • 70449450426 scopus 로고    scopus 로고
    • Identification of FGFR4-activating mutations in human rhabdomyosarcomas that promote metastasis in xenotransplanted models
    • Taylor J.G., et al. Identification of FGFR4-activating mutations in human rhabdomyosarcomas that promote metastasis in xenotransplanted models. J. Clin. Invest. 2009, 119:3395-3407.
    • (2009) J. Clin. Invest. , vol.119 , pp. 3395-3407
    • Taylor, J.G.1
  • 94
    • 84890019316 scopus 로고    scopus 로고
    • Emergence of FGFR family gene fusions as therapeutic targets in a wide spectrum of solid tumours
    • Parker B.C., et al. Emergence of FGFR family gene fusions as therapeutic targets in a wide spectrum of solid tumours. J. Pathol. 2014, 232:4-15.
    • (2014) J. Pathol. , vol.232 , pp. 4-15
    • Parker, B.C.1
  • 95
    • 84873045850 scopus 로고    scopus 로고
    • Oncogenic FGFR3 gene fusions in bladder cancer
    • Williams S.V., et al. Oncogenic FGFR3 gene fusions in bladder cancer. Hum. Mol. Genet. 2012, 22:795-803.
    • (2012) Hum. Mol. Genet. , vol.22 , pp. 795-803
    • Williams, S.V.1
  • 96
    • 84905508021 scopus 로고    scopus 로고
    • FGFR1/3 tyrosine kinase fusions define a unique molecular subtype of non-small cell lung cancer
    • Wang R., et al. FGFR1/3 tyrosine kinase fusions define a unique molecular subtype of non-small cell lung cancer. Clin. Cancer Res. 2014, 20:4107-4114.
    • (2014) Clin. Cancer Res. , vol.20 , pp. 4107-4114
    • Wang, R.1
  • 97
    • 84865805666 scopus 로고    scopus 로고
    • Transforming fusions of FGFR and TACC genes in human glioblastoma
    • Singh D., et al. Transforming fusions of FGFR and TACC genes in human glioblastoma. Science 2012, 337:1231-1235.
    • (2012) Science , vol.337 , pp. 1231-1235
    • Singh, D.1
  • 98
    • 84873347374 scopus 로고    scopus 로고
    • The tumorigenic FGFR3-TACC3 gene fusion escapes miR-99a regulation in glioblastoma
    • Parker B.C., et al. The tumorigenic FGFR3-TACC3 gene fusion escapes miR-99a regulation in glioblastoma. J. Clin. Invest. 2013, 123:855-865.
    • (2013) J. Clin. Invest. , vol.123 , pp. 855-865
    • Parker, B.C.1
  • 99
    • 84896492774 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 2 tyrosine kinase fusions define a unique molecular subtype of cholangiocarcinoma
    • Arai Y., et al. Fibroblast growth factor receptor 2 tyrosine kinase fusions define a unique molecular subtype of cholangiocarcinoma. Hepatology 2013, 59:1427-1434.
    • (2013) Hepatology , vol.59 , pp. 1427-1434
    • Arai, Y.1
  • 100
    • 84878781242 scopus 로고    scopus 로고
    • Identification of targetable FGFR gene fusions in diverse cancers
    • Wu Y.M., et al. Identification of targetable FGFR gene fusions in diverse cancers. Cancer Discov. 2013, 3:636-647.
    • (2013) Cancer Discov. , vol.3 , pp. 636-647
    • Wu, Y.M.1
  • 101
    • 0027198248 scopus 로고
    • Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF)-FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy
    • Yan G., et al. Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF)-FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy. Mol. Cell. Biol. 1993, 13:4513-4522.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4513-4522
    • Yan, G.1
  • 102
    • 79951813692 scopus 로고    scopus 로고
    • TGF-beta regulates isoform switching of FGF receptors and epithelial-mesenchymal transition
    • Shirakihara T., et al. TGF-beta regulates isoform switching of FGF receptors and epithelial-mesenchymal transition. EMBO J. 2011, 30:783-795.
    • (2011) EMBO J. , vol.30 , pp. 783-795
    • Shirakihara, T.1
  • 103
    • 84860255645 scopus 로고    scopus 로고
    • Enhanced expression of fibroblast growth factor receptor 2 IIIc promotes human pancreatic cancer cell proliferation
    • Ishiwata T., et al. Enhanced expression of fibroblast growth factor receptor 2 IIIc promotes human pancreatic cancer cell proliferation. Am. J. Pathol. 2012, 180:1928-1941.
    • (2012) Am. J. Pathol. , vol.180 , pp. 1928-1941
    • Ishiwata, T.1
  • 104
    • 75449096965 scopus 로고    scopus 로고
    • Expression of fibroblast growth factor receptor 2 IIIc in human uterine cervical intraepithelial neoplasia and cervical cancer
    • Kawase R., et al. Expression of fibroblast growth factor receptor 2 IIIc in human uterine cervical intraepithelial neoplasia and cervical cancer. Int. J. Oncol. 2010, 36:331-340.
    • (2010) Int. J. Oncol. , vol.36 , pp. 331-340
    • Kawase, R.1
  • 105
    • 84899545178 scopus 로고    scopus 로고
    • Altered expression of fibroblast growth factor receptor 2 isoform IIIc: relevance to endometrioid adenocarcinoma carcinogenesis and histological differentiation
    • Peng W.X., et al. Altered expression of fibroblast growth factor receptor 2 isoform IIIc: relevance to endometrioid adenocarcinoma carcinogenesis and histological differentiation. Int. J. Clin. Exp. Pathol. 2014, 7:1069-1076.
    • (2014) Int. J. Clin. Exp. Pathol. , vol.7 , pp. 1069-1076
    • Peng, W.X.1
  • 106
    • 79960999875 scopus 로고    scopus 로고
    • Fibroblast growth factor receptors are components of autocrine signaling networks in head and neck squamous cell carcinoma cells
    • Marshall M.E., et al. Fibroblast growth factor receptors are components of autocrine signaling networks in head and neck squamous cell carcinoma cells. Clin. Cancer Res. 2011, 17:5016-5025.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 5016-5025
    • Marshall, M.E.1
  • 107
    • 84895924166 scopus 로고    scopus 로고
    • Pten loss induces autocrine FGF signaling to promote skin tumorigenesis
    • Hertzler-Schaefer K., et al. Pten loss induces autocrine FGF signaling to promote skin tumorigenesis. Cell Rep. 2014, 6:818-826.
    • (2014) Cell Rep. , vol.6 , pp. 818-826
    • Hertzler-Schaefer, K.1
  • 108
    • 84876916275 scopus 로고    scopus 로고
    • Endocrine fibroblast growth factor FGF19 promotes prostate cancer progression
    • Feng S., et al. Endocrine fibroblast growth factor FGF19 promotes prostate cancer progression. Cancer Res. 2013, 73:2551-2562.
    • (2013) Cancer Res. , vol.73 , pp. 2551-2562
    • Feng, S.1
  • 109
    • 84880525684 scopus 로고    scopus 로고
    • A mechanism of resistance to gefitinib mediated by cellular reprogramming and the acquisition of an FGF2-FGFR1 autocrine growth loop
    • Ware K.E., et al. A mechanism of resistance to gefitinib mediated by cellular reprogramming and the acquisition of an FGF2-FGFR1 autocrine growth loop. Oncogenesis 2013, 2:e39.
    • (2013) Oncogenesis , vol.2 , pp. e39
    • Ware, K.E.1
  • 110
    • 84880547779 scopus 로고    scopus 로고
    • Activation of the FGF2-FGFR1 autocrine pathway: a novel mechanism of acquired resistance to gefitinib in NSCLC
    • Terai H., et al. Activation of the FGF2-FGFR1 autocrine pathway: a novel mechanism of acquired resistance to gefitinib in NSCLC. Mol. Cancer Res. 2013, 11:759-767.
    • (2013) Mol. Cancer Res. , vol.11 , pp. 759-767
    • Terai, H.1
  • 111
    • 70350507997 scopus 로고    scopus 로고
    • AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance
    • O'Hare T., et al. AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance. Cancer Cell 2009, 16:401-412.
    • (2009) Cancer Cell , vol.16 , pp. 401-412
    • O'Hare, T.1
  • 112
    • 84859402751 scopus 로고    scopus 로고
    • Ponatinib (AP24534), a multitargeted pan-FGFR inhibitor with activity in multiple FGFR-amplified or mutated cancer models
    • Gozgit J.M., et al. Ponatinib (AP24534), a multitargeted pan-FGFR inhibitor with activity in multiple FGFR-amplified or mutated cancer models. Mol. Cancer Ther. 2012, 11:690-699.
    • (2012) Mol. Cancer Ther. , vol.11 , pp. 690-699
    • Gozgit, J.M.1
  • 113
    • 84892762937 scopus 로고    scopus 로고
    • In brief: ponatinib (Inclusig) returns
    • The Medical Letter Online In brief: ponatinib (Inclusig) returns. Med. Lett. Drugs Ther. 2014, 56:8.
    • (2014) Med. Lett. Drugs Ther. , vol.56 , pp. 8
  • 114
    • 84860120185 scopus 로고    scopus 로고
    • AZD4547: an orally bioavailable, potent, and selective inhibitor of the fibroblast growth factor receptor tyrosine kinase family
    • Gavine P.R., et al. AZD4547: an orally bioavailable, potent, and selective inhibitor of the fibroblast growth factor receptor tyrosine kinase family. Cancer Res. 2012, 72:2045-2056.
    • (2012) Cancer Res. , vol.72 , pp. 2045-2056
    • Gavine, P.R.1
  • 115
    • 80054900437 scopus 로고    scopus 로고
    • Discovery of 3-(2,6-dichloro-3,5-dimethoxy-phenyl)-1-{6-[4-(4-ethyl-piperazin-1-yl)-phenylamin o]-pyrimidin-4-yl}-1-methyl-urea (NVP-BGJ398), a potent and selective inhibitor of the fibroblast growth factor receptor family of receptor tyrosine kinase
    • Guagnano V., et al. Discovery of 3-(2,6-dichloro-3,5-dimethoxy-phenyl)-1-{6-[4-(4-ethyl-piperazin-1-yl)-phenylamin o]-pyrimidin-4-yl}-1-methyl-urea (NVP-BGJ398), a potent and selective inhibitor of the fibroblast growth factor receptor family of receptor tyrosine kinase. J. Med. Chem. 2011, 54:7066-7083.
    • (2011) J. Med. Chem. , vol.54 , pp. 7066-7083
    • Guagnano, V.1
  • 116
    • 81055124246 scopus 로고    scopus 로고
    • A novel, selective inhibitor of fibroblast growth factor receptors that shows a potent broad spectrum of antitumor activity in several tumor xenograft models
    • Zhao G., et al. A novel, selective inhibitor of fibroblast growth factor receptors that shows a potent broad spectrum of antitumor activity in several tumor xenograft models. Mol. Cancer Ther. 2011, 10:2200-2210.
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 2200-2210
    • Zhao, G.1
  • 117
    • 84877679916 scopus 로고    scopus 로고
    • Activity of the fibroblast growth factor receptor inhibitors dovitinib (TKI258) and NVP-BGJ398 in human endometrial cancer cells
    • Konecny G.E., et al. Activity of the fibroblast growth factor receptor inhibitors dovitinib (TKI258) and NVP-BGJ398 in human endometrial cancer cells. Mol. Cancer Ther. 2013, 12:632-642.
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 632-642
    • Konecny, G.E.1
  • 118
    • 84877100340 scopus 로고    scopus 로고
    • FGFR2 gene amplification in gastric cancer predicts sensitivity to the selective FGFR inhibitor AZD4547
    • Xie L., et al. FGFR2 gene amplification in gastric cancer predicts sensitivity to the selective FGFR inhibitor AZD4547. Clin. Cancer Res. 2013, 19:2572-2583.
    • (2013) Clin. Cancer Res. , vol.19 , pp. 2572-2583
    • Xie, L.1
  • 119
    • 84871217393 scopus 로고    scopus 로고
    • Translating the therapeutic potential of AZD4547 in FGFR1-amplified non-small cell lung cancer through the use of patient-derived tumor xenograft models
    • Zhang J., et al. Translating the therapeutic potential of AZD4547 in FGFR1-amplified non-small cell lung cancer through the use of patient-derived tumor xenograft models. Clin. Cancer Res. 2012, 18:6658-6667.
    • (2012) Clin. Cancer Res. , vol.18 , pp. 6658-6667
    • Zhang, J.1
  • 121
    • 84937634093 scopus 로고    scopus 로고
    • First in human study of JNJ-42756493, a potent pan fibroblast growth factor receptor (FGFR) inhibitor in patients with advanced solid tumors [abstract]
    • Dienstmann R., et al. First in human study of JNJ-42756493, a potent pan fibroblast growth factor receptor (FGFR) inhibitor in patients with advanced solid tumors [abstract]. Proceedings of the 105th Annual Meeting of the American Association for Cancer Research 2014.
    • (2014) Proceedings of the 105th Annual Meeting of the American Association for Cancer Research
    • Dienstmann, R.1
  • 122
    • 33947108356 scopus 로고    scopus 로고
    • Monoclonal antibody antagonists of hypothalamic FGFR1 cause potent but reversible hypophagia and weight loss in rodents and monkeys
    • Sun H.D., et al. Monoclonal antibody antagonists of hypothalamic FGFR1 cause potent but reversible hypophagia and weight loss in rodents and monkeys. Am. J. Physiol. Endocrinol. Metab. 2007, 292:E964-E976.
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.292 , pp. E964-E976
    • Sun, H.D.1
  • 123
    • 66349135677 scopus 로고    scopus 로고
    • Antibody-based targeting of FGFR3 in bladder carcinoma and t(4;14)-positive multiple myeloma in mice
    • Qing J., et al. Antibody-based targeting of FGFR3 in bladder carcinoma and t(4;14)-positive multiple myeloma in mice. J. Clin. Invest. 2009, 119:1216-1229.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1216-1229
    • Qing, J.1
  • 124
    • 77957331045 scopus 로고    scopus 로고
    • GP369, an FGFR2-IIIb-specific antibody, exhibits potent antitumor activity against human cancers driven by activated FGFR2 signaling
    • Bai A., et al. GP369, an FGFR2-IIIb-specific antibody, exhibits potent antitumor activity against human cancers driven by activated FGFR2 signaling. Cancer Res. 2010, 70:7630-7639.
    • (2010) Cancer Res. , vol.70 , pp. 7630-7639
    • Bai, A.1
  • 125
    • 84897560527 scopus 로고    scopus 로고
    • Randomized trial of the anti-FGF23 antibody KRN23 in X-linked hypophosphatemia
    • Carpenter T.O., et al. Randomized trial of the anti-FGF23 antibody KRN23 in X-linked hypophosphatemia. J. Clin. Invest. 2014, 124:1587-1597.
    • (2014) J. Clin. Invest. , vol.124 , pp. 1587-1597
    • Carpenter, T.O.1
  • 126
    • 84876103735 scopus 로고    scopus 로고
    • Blockade of nonhormonal fibroblast growth factors by FP-1039 inhibits growth of multiple types of cancer
    • Harding T.C., et al. Blockade of nonhormonal fibroblast growth factors by FP-1039 inhibits growth of multiple types of cancer. Sci. Transl. Med. 2013, 5:ra39.
    • (2013) Sci. Transl. Med. , vol.5 , pp. ra39
    • Harding, T.C.1
  • 127
    • 84884676713 scopus 로고    scopus 로고
    • Postnatal soluble FGFR3 therapy rescues achondroplasia symptoms and restores bone growth in mice
    • 203ra124
    • Garcia S., et al. Postnatal soluble FGFR3 therapy rescues achondroplasia symptoms and restores bone growth in mice. Sci. Transl. Med. 2013, 5:203ra124.
    • (2013) Sci. Transl. Med. , vol.5
    • Garcia, S.1
  • 128
    • 84908571755 scopus 로고    scopus 로고
    • Statin treatment rescues FGFR3 skeletal dysplasia phenotypes
    • Yamashita A., et al. Statin treatment rescues FGFR3 skeletal dysplasia phenotypes. Nature 2014, 513:507-511.
    • (2014) Nature , vol.513 , pp. 507-511
    • Yamashita, A.1
  • 129
    • 84876401041 scopus 로고    scopus 로고
    • Molecular mechanism of SSR 128129E, an extracellularly acting, small-molecule, allosteric inhibitor of FGF receptor signaling
    • Herbert C., et al. Molecular mechanism of SSR 128129E, an extracellularly acting, small-molecule, allosteric inhibitor of FGF receptor signaling. Cancer Cell 2013, 23:489-501.
    • (2013) Cancer Cell , vol.23 , pp. 489-501
    • Herbert, C.1
  • 130
    • 84876355112 scopus 로고    scopus 로고
    • Inhibition of tumor angiogenesis and growth by a small-molecule multi-FGF receptor blocker with allosteric properties
    • Bono F., et al. Inhibition of tumor angiogenesis and growth by a small-molecule multi-FGF receptor blocker with allosteric properties. Cancer Cell 2013, 23:477-488.
    • (2013) Cancer Cell , vol.23 , pp. 477-488
    • Bono, F.1
  • 131
    • 49649123154 scopus 로고    scopus 로고
    • BIBF 1120: triple angiokinase inhibitor with sustained receptor blockade and good antitumor efficacy
    • Hilberg F., et al. BIBF 1120: triple angiokinase inhibitor with sustained receptor blockade and good antitumor efficacy. Cancer Res. 2008, 68:4774-4782.
    • (2008) Cancer Res. , vol.68 , pp. 4774-4782
    • Hilberg, F.1
  • 132
    • 37349105704 scopus 로고    scopus 로고
    • E7080, a novel inhibitor that targets multiple kinases, has potent antitumor activities against stem cell factor producing human small cell lung cancer H146, based on angiogenesis inhibition
    • Matsui J., et al. E7080, a novel inhibitor that targets multiple kinases, has potent antitumor activities against stem cell factor producing human small cell lung cancer H146, based on angiogenesis inhibition. Int. J. Cancer 2008, 122:664-671.
    • (2008) Int. J. Cancer , vol.122 , pp. 664-671
    • Matsui, J.1
  • 133
    • 0033883776 scopus 로고    scopus 로고
    • SU6668 is a potent antiangiogenic and antitumor agent that induces regression of established tumors
    • Laird A.D., et al. SU6668 is a potent antiangiogenic and antitumor agent that induces regression of established tumors. Cancer Res. 2000, 60:4152-4160.
    • (2000) Cancer Res. , vol.60 , pp. 4152-4160
    • Laird, A.D.1
  • 134
    • 78751492146 scopus 로고    scopus 로고
    • ENMD-2076 is an orally active kinase inhibitor with antiangiogenic and antiproliferative mechanisms of action
    • Fletcher G.C., et al. ENMD-2076 is an orally active kinase inhibitor with antiangiogenic and antiproliferative mechanisms of action. Mol. Cancer Ther. 2010, 10:126-137.
    • (2010) Mol. Cancer Ther. , vol.10 , pp. 126-137
    • Fletcher, G.C.1
  • 135
    • 79951826312 scopus 로고    scopus 로고
    • E-3810 is a potent dual inhibitor of VEGFR and FGFR that exerts antitumor activity in multiple preclinical models
    • Bello E., et al. E-3810 is a potent dual inhibitor of VEGFR and FGFR that exerts antitumor activity in multiple preclinical models. Cancer Res. 2011, 71:1396-1405.
    • (2011) Cancer Res. , vol.71 , pp. 1396-1405
    • Bello, E.1
  • 136
    • 15944378835 scopus 로고    scopus 로고
    • CHIR-258, a novel, multitargeted tyrosine kinase inhibitor for the potential treatment of t(4;14) multiple myeloma
    • Trudel S., et al. CHIR-258, a novel, multitargeted tyrosine kinase inhibitor for the potential treatment of t(4;14) multiple myeloma. Blood 2005, 105:2941-2948.
    • (2005) Blood , vol.105 , pp. 2941-2948
    • Trudel, S.1


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