메뉴 건너뛰기




Volumn 82, Issue 2, 1999, Pages 748-754

Fibroblast growth factor prototype release and fibroblast growth factor receptor signaling

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR; FIBROBLAST GROWTH FACTOR 1; FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR 3; FIBROBLAST GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0032699085     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1615907     Document Type: Conference Paper
Times cited : (92)

References (79)
  • 1
    • 0031661435 scopus 로고    scopus 로고
    • Fibroblast growth factors as multifunctional signaling factors
    • Szebenyi G, Fallon J. Fibroblast growth factors as multifunctional signaling factors. Int Rev Cytol. 1999;185:45-106.
    • (1999) Int Rev Cytol , vol.185 , pp. 45-106
    • Szebenyi, G.1    Fallon, J.2
  • 2
    • 33644973673 scopus 로고    scopus 로고
    • FGF signaling in skeletal development
    • 1998
    • Naski MC, Ornitz D. 1998. FGF Signaling in skeletal development. Frontiers in Bioscience. 1998;3:781-794.
    • (1998) Frontiers in Bioscience , vol.3 , pp. 781-794
    • Naski, M.C.1    Ornitz, D.2
  • 3
    • 0031005778 scopus 로고    scopus 로고
    • Fgfir activation in skeletal disorders: Too much of a good thing
    • 1997
    • Webster MK, Donoghue DJ. 1997. Fgfir activation in skeletal disorders: too much of a good thing. Trends Genet. 1997;13:178-182.
    • (1997) Trends Genet , vol.13 , pp. 178-182
    • Webster, M.K.1    Donoghue, D.J.2
  • 4
    • 0031024921 scopus 로고    scopus 로고
    • Of worms and men: An an evolutionary perspective on the fibroblast growth factor (FGF) and FGF receptor families
    • 1997
    • Coulier F, Pontarotti P, Roubin R, Hartung H, Goldfarb M, Birnbaum D. 1997. Of worms and men: An an evolutionary perspective on the fibroblast growth factor (FGF) and FGF receptor families. J Mol Evol. 1997;44:43-56.
    • (1997) J Mol Evol , vol.44 , pp. 43-56
    • Coulier, F.1    Pontarotti, P.2    Roubin, R.3    Hartung, H.4    Goldfarb, M.5    Birnbaum, D.6
  • 5
    • 0029143960 scopus 로고
    • Molecular mechanisms of angiogenesis: Fibroblast growth factor signal transduction
    • 1995
    • Friesel RE, Maciag T. 1995. Molecular mechanisms of angiogenesis: fibroblast growth factor signal transduction. FASEB J 1995;9:919-925.
    • (1995) FASEB J , vol.9 , pp. 919-925
    • Friesel, R.E.1    Maciag, T.2
  • 6
    • 0027344852 scopus 로고
    • Structural and functional diversity in the FGF receptor multigene family
    • 1993
    • Johnson DEE, Williams LT. 1993. Structural and functional diversity in the FGF receptor multigene family. Adv Cancer Res. 1993;60:1-40.
    • (1993) Adv Cancer Res , vol.60 , pp. 1-40
    • Johnson, D.E.E.1    Williams, L.T.2
  • 7
    • 0024375271 scopus 로고
    • Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor
    • Lee PL, Johnson DE, Cousens LS, Fried VA, Williams LT. Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor. Science. 1989;245:57-60.
    • (1989) Science , vol.245 , pp. 57-60
    • Lee, P.L.1    Johnson, D.E.2    Cousens, L.S.3    Fried, V.A.4    Williams, L.T.5
  • 8
    • 0025893883 scopus 로고
    • Fibroblast growth factor receptors from liver vary in three structural domains
    • Hou JZ, Kan MK, McKeehan K, McBride G, Adams P, McKeehan WL. Fibroblast growth factor receptors from liver vary in three structural domains. Science. 1991;251:665-668.
    • (1991) Science , vol.251 , pp. 665-668
    • Hou, J.Z.1    Kan, M.K.2    McKeehan, K.3    McBride, G.4    Adams, P.5    McKeehan, W.L.6
  • 9
    • 0028239789 scopus 로고
    • Fibroblast growth factor receptor (FGFR) 3: Alternative splicing in immunoglobulin-like domain in creates a receptor highly specific for acidic FGF/FGF-1
    • Chellaiah AT, McEwen DG, Werner S, Xu J, Ornitz DM. Fibroblast growth factor receptor (FGFR) 3: alternative splicing in immunoglobulin-like domain in creates a receptor highly specific for acidic FGF/FGF-1. J .Biol Chem. 1994;269:11620-11627.
    • (1994) J .Biol Chem , vol.269 , pp. 11620-11627
    • Chellaiah, A.T.1    McEwen, D.G.2    Werner, S.3    Xu, J.4    Ornitz, D.M.5
  • 11
    • 0026570847 scopus 로고
    • Determination of ligand-binding specificity by alternative splicing - Two distinct growth factor receptors encoded by a single gene
    • Miki T, Bottaro DP, Fleming TP, Smith CL, Burgess WH, Chan AML, Aaronson SA. Determination of ligand-binding specificity by alternative splicing - two distinct growth factor receptors encoded by a single gene. Proc Natl Acad Sci USA. 1992;89:246-250.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 246-250
    • Miki, T.1    Bottaro, D.P.2    Fleming, T.P.3    Smith, C.L.4    Burgess, W.H.5    Chan, A.M.L.6    Aaronson, S.A.7
  • 13
    • 0025122589 scopus 로고
    • Diverse forms of a receptor for acidic and basic fibroblast growth factors
    • Johnson DE, Lee PL, Lu J, Williams LT. Diverse forms of a receptor for acidic and basic fibroblast growth factors. Mol Cell Biol. 1990;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
  • 14
    • 0028986809 scopus 로고
    • 2-terminal immunoglobulin-like loop I in the ectodomain of the fibroblast growth factor (FGF) receptor-1 lowers affinity for both heparin and FGF-1
    • 2-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. 1995;270:10231-10235.
    • (1995) J Biol Chem , vol.270 , pp. 10231-10235
    • Wang, F.1    Kan, M.2    Yan, G.3    Xu, J.4    McKeehan, W.L.5
  • 15
    • 0027198248 scopus 로고
    • Exon switching and activation of stromal and embryonic fibroblast growth factor receptor genes in prostate epithelial cells accompany stromal independence and malignancy
    • Yan G, Fukabori Y, McBride GS, Nikolaropolous S, McKeehan WL. Exon switching and activation of stromal and embryonic fibroblast growth factor 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    Fukabori, Y.2    McBride, G.S.3    Nikolaropolous, S.4    McKeehan, W.L.5
  • 17
    • 0026344226 scopus 로고
    • Developmental expression of two murine fibroblast growth factor receptors, fig and bek
    • Orr-Urtreger A., Givol D, Yayon A, Yarden Y, Lonai P. Developmental expression of two murine fibroblast growth factor receptors, fig and bek. Development. 1991;113:1419-1434.
    • (1991) Development , vol.113 , pp. 1419-1434
    • Orr-Urtreger, A.1    Givol, D.2    Yayon, A.3    Yarden, Y.4    Lonai, P.5
  • 18
    • 0027409017 scopus 로고
    • Unique expression pattern of the FGF receptor 3 gene during mouse organogenesis
    • Peters K, Ornitz D, Werner S, Williams L. Unique expression pattern of the FGF receptor 3 gene during mouse organogenesis. Dev Biol. 1993;155:423-430.
    • (1993) Dev Biol , vol.155 , pp. 423-430
    • Peters, K.1    Ornitz, D.2    Werner, S.3    Williams, L.4
  • 19
    • 12644265399 scopus 로고    scopus 로고
    • Developmental expression of splicing variants of fibroblast growth factor receptor 3 (fgfr3) in mouse
    • Wuechner C, Nordqvist AC, Winterpacht A, Zabel B, Schalling M. Developmental expression of splicing variants of fibroblast growth factor receptor 3 (fgfr3) in mouse. Int J Dev Biol. 1996;40:1185-1188.
    • (1996) Int J Dev Biol , vol.40 , pp. 1185-1188
    • Wuechner, C.1    Nordqvist, A.C.2    Winterpacht, A.3    Zabel, B.4    Schalling, M.5
  • 20
    • 0026044779 scopus 로고
    • FGFR-4, a new member of the fibroblast growth factor receptor family, expressed in the definitive endoderm and skeletal muscle lineages of the mouse
    • Stark KL, McMahon JA, McMahon AP. FGFR-4, a new member of the fibroblast growth factor receptor family, expressed in the definitive endoderm and skeletal muscle lineages of the mouse. Development. 1991;113:641-651.
    • (1991) Development , vol.113 , pp. 641-651
    • Stark, K.L.1    McMahon, J.A.2    McMahon, A.P.3
  • 21
    • 0028582035 scopus 로고
    • FGFR-1 is required for embryonic growth and mesodermal patterning during mouse gastrulation
    • Yamaguchi TP, Harpal K, Henkemeyer M, Rossant J. FGFR-1 is required for embryonic growth and mesodermal patterning during mouse gastrulation. Genes Dev. 1994;8:3032-3044.
    • (1994) Genes Dev , vol.8 , pp. 3032-3044
    • Yamaguchi, T.P.1    Harpal, K.2    Henkemeyer, M.3    Rossant, J.4
  • 23
    • 0032574824 scopus 로고    scopus 로고
    • Targeted disruption of fibroblast grorwth factor (FGF) receptor 2 suggests a role for fgf signaling in pregastrulation mammalian development
    • Arman E, Haffner-Krausz R, Chen Y, Heath J, Lonai P. Targeted disruption of fibroblast grorwth factor (FGF) receptor 2 suggests a role for FGF signaling in pregastrulation mammalian development. Proc Natl Acad Sci USA. 1998;95:5082-5087.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5082-5087
    • Arman, E.1    Haffner-Krausz, R.2    Chen, Y.3    Heath, J.4    Lonai, P.5
  • 24
    • 0029917507 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 3 is a negative regulator of bone growth
    • Deng C, Wynshaw-Boris A, Zhou F, Kuo A, Leder P. Fibroblast growth factor receptor 3 is a negative regulator of bone growth. Cell. 1996;84:911-921.
    • (1996) Cell , vol.84 , pp. 911-921
    • Deng, C.1    Wynshaw-Boris, A.2    Zhou, F.3    Kuo, A.4    Leder, P.5
  • 25
    • 0029928791 scopus 로고    scopus 로고
    • Skeletal overgrowth and deafness in mice lacking fibroblast growth factor receptor 3
    • Colvin JS, Bohne BA, Harding GW, McEwen DG, Ornitz DM. Skeletal overgrowth and deafness in mice lacking fibroblast growth factor receptor 3. Nature Genet. 1996;12:390-397.
    • (1996) Nature Genet , vol.12 , pp. 390-397
    • Colvin, J.S.1    Bohne, B.A.2    Harding, G.W.3    McEwen, D.G.4    Ornitz, D.M.5
  • 26
    • 0031700905 scopus 로고    scopus 로고
    • FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in the murine lung
    • C.
    • Weinstein M, Xu X, Ohyama K, C. Deng C. FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in the murine lung. Development. 1998;125:3615-3623.
    • (1998) Development , vol.125 , pp. 3615-3623
    • Weinstein, M.1    Xu, X.2    Ohyama, K.3    Deng, C.4
  • 27
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored grb2-binding protein that links FGF-receptor activation to the ras/mapk signaling pathway
    • Kouhara H., Hadari YR, Spivak-Kroizman T, Schilling J, BarSagi D, Lax I, Schlessinger J. 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    Hadari, Y.R.2    Spivak-Kroizman, T.3    Schilling, J.4    BarSagi, D.5    Lax, I.6    Schlessinger, J.7
  • 28
    • 0029764511 scopus 로고    scopus 로고
    • Broadly expressed SNT-like proteins link FGF receptor stimulation to activators of Ras
    • Wang JK, Xu H, Li H-C, Goldfarb M. Broadly expressed SNT-like proteins link FGF receptor stimulation to activators of Ras. Oncogene. 1996;13:721-729.
    • (1996) Oncogene , vol.13 , pp. 721-729
    • Wang, J.K.1    Xu, H.2    Li, H.-C.3    Goldfarb, M.4
  • 29
    • 0025042112 scopus 로고
    • Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase
    • Burgess WH, Dionne CA, Kaplow J, Mudd R, Friesel R, Zilberstein A, Schlessinger J, Jaye M. Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Mol Cell Biol. 1990;10:4770-4777.
    • (1990) Mol Cell Biol , vol.10 , pp. 4770-4777
    • Burgess, W.H.1    Dionne, C.A.2    Kaplow, J.3    Mudd, R.4    Friesel, R.5    Zilberstein, A.6    Schlessinger, J.7    Jaye, M.8
  • 30
    • 0028878979 scopus 로고
    • The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early Xenopus development
    • Tang TL, Freeman RM Jr, O'Reilly AM, Neel BG, Sokol SY. The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early Xenopus development. Cell. 1995;80:473-483.
    • (1995) Cell , vol.80 , pp. 473-483
    • Tang, T.L.1    Freeman R.M., Jr.2    O'Reilly, A.M.3    Neel, B.G.4    Sokol, S.Y.5
  • 31
    • 0031835659 scopus 로고    scopus 로고
    • Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation
    • Hadari YR, Kouhara H, Lax I, Schlessinger J. Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation. Mol Cell Biol. 1998;18:3966-3973.
    • (1998) Mol Cell Biol , vol.18 , pp. 3966-3973
    • Hadari, Y.R.1    Kouhara, H.2    Lax, I.3    Schlessinger, J.4
  • 32
    • 0028817834 scopus 로고
    • She and a novel 89-kDa component couple to the Grb2-Sos complex in fibroblast growth factor-2-stimulated cells
    • Klint P, Kanda S, Claesson-Welsh L. She and a novel 89-kDa component couple to the Grb2-Sos complex in fibroblast growth factor-2-stimulated cells. J Biol Chem. 1995;270:23337-23344.
    • (1995) J Biol Chem , vol.270 , pp. 23337-23344
    • Klint, P.1    Kanda, S.2    Claesson-Welsh, L.3
  • 33
    • 0027955135 scopus 로고
    • Fibroblast growth factor receptors have different signaling and mitogenic potentials
    • Wang JK, Gao G, Goldfarb M. Fibroblast growth factor receptors have different signaling and mitogenic potentials. Mol Cell Biol. 1994;14:181-188.
    • (1994) Mol Cell Biol , vol.14 , pp. 181-188
    • Wang, J.K.1    Gao, G.2    Goldfarb, M.3
  • 34
    • 1842372689 scopus 로고    scopus 로고
    • Signal transduction pathway of human fibroblast growth factor receptor 3
    • Kanai M, Goke M, Tsunekawa S, Podolsky DK. Signal transduction pathway of human fibroblast growth factor receptor 3. J Biol Chem. 1997;272:6621-6628.
    • (1997) J Biol Chem , vol.272 , pp. 6621-6628
    • Kanai, M.1    Goke, M.2    Tsunekawa, S.3    Podolsky, D.K.4
  • 35
    • 0032578009 scopus 로고    scopus 로고
    • Activation of the MAP kinase pathway by FGF-1 correlates with cell proliferation induction while activation of the Src pathway correlates with migration
    • LaVallee TM, Prudovsky IA, McMahon GA, Hu X, Maciag T. Activation of the MAP kinase pathway by FGF-1 correlates with cell proliferation induction while activation of the Src pathway correlates with migration. J Cell Biol. 1998;141:1647-1658.
    • (1998) J Cell Biol , vol.141 , pp. 1647-1658
    • LaVallee, T.M.1    Prudovsky, I.A.2    McMahon, G.A.3    Hu, X.4    Maciag, T.5
  • 36
    • 0030027488 scopus 로고    scopus 로고
    • Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction
    • Mohammadi M., Dikic I, Sorokin A, Burgess WH, Jaye M, Schlessinger J. Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction. Mol Cell Biol. 1996;16:977-989.
    • (1996) Mol Cell Biol , vol.16 , pp. 977-989
    • Mohammadi, M.1    Dikic, I.2    Sorokin, A.3    Burgess, W.H.4    Jaye, M.5    Schlessinger, J.6
  • 37
    • 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, Honegger AM, Rotin D, Fischer R, Bellot F, Li W, Dionne CA, Jaye M, Rubinstein M, Schlessinger J. 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    Honegger, A.M.2    Rotin, D.3    Fischer, R.4    Bellot, F.5    Li, W.6    Dionne, C.A.7    Jaye, M.8    Rubinstein, M.9    Schlessinger, J.10
  • 38
    • 0026641249 scopus 로고
    • Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis
    • M.
    • Mohammadi M, Dionne CA, Li W, Li N, Spivak T, Honegger AM, M. Jaye M, Schlessinger J. Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature. 1992;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
  • 40
    • 0028208902 scopus 로고
    • Direct activation of phospholipase C-gamma by fibroblast growth factor receptor is not required for mesoderm induction in Xenopus animal caps
    • Muslin AJ, Peters KG, Williams LT. Direct activation of phospholipase C-gamma by fibroblast growth factor receptor is not required for mesoderm induction in Xenopus animal caps. Mol Cell Biol. 1994;14:3006-3012.
    • (1994) Mol Cell Biol , vol.14 , pp. 3006-3012
    • Muslin, A.J.1    Peters, K.G.2    Williams, L.T.3
  • 41
    • 0028236448 scopus 로고
    • Point mutation in the fibroblast growth factor receptor eliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells
    • Spivak-Kroizman T, Mohammadi M, Hu P, Jaye M, Schlessinger J, Lax I. Point mutation in the fibroblast growth factor receptor eliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells. J Biol Chem. 1994;269:14419-14423.
    • (1994) J Biol Chem , vol.269 , pp. 14419-14423
    • Spivak-Kroizman, T.1    Mohammadi, M.2    Hu, P.3    Jaye, M.4    Schlessinger, J.5    Lax, I.6
  • 42
    • 0024603003 scopus 로고
    • Heparin-binding growth factor 1 stimulates tyrosine phosphorylation in NIH 3T3 cells
    • Friesel R, Burgess WH, Maciag T. Heparin-binding growth factor 1 stimulates tyrosine phosphorylation in NIH 3T3 cells. Mol Cell Biol. 1989;9:1857-1865.
    • (1989) Mol Cell Biol , vol.9 , pp. 1857-1865
    • Friesel, R.1    Burgess, W.H.2    Maciag, T.3
  • 43
    • 0000816317 scopus 로고    scopus 로고
    • Identification of p90, a prominent tyrosine-phosphorylated protein in fibroblast growth factor-stimulated cells, as 80K-H
    • Goh KC, Lim YP, Ong SH, Siak CB, Cao X, Tan YH, Guy GR. Identification of p90, a prominent tyrosine-phosphorylated protein in fibroblast growth factor-stimulated cells, as 80K-H. J Biol Chem. 1996;271:5832-5838.
    • (1996) J Biol Chem , vol.271 , pp. 5832-5838
    • Goh, K.C.1    Lim, Y.P.2    Ong, S.H.3    Siak, C.B.4    Cao, X.5    Tan, Y.H.6    Guy, G.R.7
  • 44
    • 0032540941 scopus 로고    scopus 로고
    • Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins
    • Xu H, Lee KW, Goldfarb M. Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins. J Biol Chem. 1998;273:17987-17990.
    • (1998) J Biol Chem , vol.273 , pp. 17987-17990
    • Xu, H.1    Lee, K.W.2    Goldfarb, M.3
  • 45
    • 0025931499 scopus 로고
    • Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions
    • Kremer NE, Darcangelo G, Thomas SM, Demarco M, Brugge JS, Halegoua S. Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions. J Cell Biol. 1991;115:809-819.
    • (1991) J Cell Biol , vol.115 , pp. 809-819
    • Kremer, N.E.1    Darcangelo, G.2    Thomas, S.M.3    Demarco, M.4    Brugge, J.S.5    Halegoua, S.6
  • 46
    • 0027286319 scopus 로고
    • Long term growth factor exposure and differential tyrosine phosphorylation are required for DNA synthesis in BALB/c 3T3 cells
    • Zhan X, Hu X, Friesel R, Maciag T. Long term growth factor exposure and differential tyrosine phosphorylation are required for DNA synthesis in BALB/c 3T3 cells. J Biol Chem. 1993;268:9611-9620.
    • (1993) J Biol Chem , vol.268 , pp. 9611-9620
    • Zhan, X.1    Hu, X.2    Friesel, R.3    Maciag, T.4
  • 47
    • 0032572802 scopus 로고    scopus 로고
    • FGF-mediated mesoderm induction involves the Src-family kinase Laloo
    • Weinstein DC, Marden J, Carnevali F, Hemmati-Brivanlou A. FGF-mediated mesoderm induction involves the Src-family kinase Laloo. Nature. 1998;394:904-908.
    • (1998) Nature , vol.394 , pp. 904-908
    • Weinstein, D.C.1    Marden, J.2    Carnevali, F.3    Hemmati-Brivanlou, A.4
  • 48
    • 0032476012 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells
    • Huang C, Liu J, Haudenschild CC, Zhan X. The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells. J Biol Chem. 1998;273:25770-25776.
    • (1998) J Biol Chem , vol.273 , pp. 25770-25776
    • Huang, C.1    Liu, J.2    Haudenschild, C.C.3    Zhan, X.4
  • 49
    • 0028088073 scopus 로고
    • The ins and outs of fibroblast growth factors
    • Mason I.J. The ins and outs of fibroblast growth factors. Cell. 1994;78:547-552.
    • (1994) Cell , vol.78 , pp. 547-552
    • Mason, I.J.1
  • 50
    • 0025582525 scopus 로고
    • Basic fibroblast growth factor (bFGF) and rat C6 glioma cells: Regulation of expression, absence of release, and response to exogenous bFGF
    • Westermann R., Unsicker K. Basic fibroblast growth factor (bFGF) and rat C6 glioma cells: regulation of expression, absence of release, and response to exogenous bFGF. Glia. 1990;3:510-521.
    • (1990) Glia , vol.3 , pp. 510-521
    • Westermann, R.1    Unsicker, K.2
  • 51
    • 0025019946 scopus 로고
    • Subcellular fate of the int-2 oncoprotein is determined by choice of initiation codon
    • Acland P, Dixon M, Peters G, Dickson C. Subcellular fate of the int-2 oncoprotein is determined by choice of initiation codon. Nature. 1990;343:662-665.
    • (1990) Nature , vol.343 , pp. 662-665
    • Acland, P.1    Dixon, M.2    Peters, G.3    Dickson, C.4
  • 52
    • 0028081352 scopus 로고
    • Intact and functional fibroblast growth factor (FGF) receptor-1 traffics near the nucleus in response to FGF-1
    • Prudovsky I, Savion N, Zhan X, Friesel R, Xu J, Hou J, Mckeehan WL, Maciag T. Intact and functional fibroblast growth factor (FGF) receptor-1 traffics near the nucleus in response to FGF-1. J Biol. Chem. 1994;269:31720-31724.
    • (1994) J Biol. Chem. , vol.269 , pp. 31720-31724
    • Prudovsky, I.1    Savion, N.2    Zhan, X.3    Friesel, R.4    Xu, J.5    Hou, J.6    Mckeehan, W.L.7    Maciag, T.8
  • 53
    • 15844396312 scopus 로고    scopus 로고
    • The nuclear trafficking of extracellular FGF-1 correlates with the perinuclear association of the FGFR-1α isoforms but not the FGFR-1β isoforms
    • N. T.M. T. 1996
    • Prudovsky, I., N. Savion N, T.M. LaVallee TM, and T. Maciag T. 1996. The nuclear trafficking of extracellular FGF-1 correlates with the perinuclear association of the FGFR-1α isoforms but not the FGFR-1β isoforms. J .Biol. Chem. 1996;271:14198-14205.
    • (1996) J .Biol. Chem. , vol.271 , pp. 14198-14205
    • Prudovsky, I.1    Savion, N.2    LaVallee, T.M.3    Maciag, T.4
  • 54
    • 0029785143 scopus 로고    scopus 로고
    • Nuclear accumulation of fibroblast growth factor receptors is regulated by multiple signals in adrenal medullary cells
    • Stachowiak MK, Maher PA, Joy A, Mordechai E, Stachowiak EK. Nuclear accumulation of fibroblast growth factor receptors is regulated by multiple signals in adrenal medullary cells. Mol Biol Cell. 1996;7:1299-1317.
    • (1996) Mol Biol Cell , vol.7 , pp. 1299-1317
    • Stachowiak, M.K.1    Maher, P.A.2    Joy, A.3    Mordechai, E.4    Stachowiak, E.K.5
  • 56
    • 0029559922 scopus 로고
    • Fibroblast growth factor receptors (fgfrs) localize in different cellular compartments
    • H.C. J.J. R.C. 1995
    • Johnston, C.L., H.C. Cox HC, J.J. Gomm JJ, and R.C. Coombes RC. 1995. Fibroblast growth factor receptors (fgfrs) localize in different cellular compartments. J .Biol .Chem. 1995;270:30643-30650.
    • (1995) J .Biol .Chem. , vol.270 , pp. 30643-30650
    • Johnston, C.L.1    Cox, H.C.2    Gomm, J.J.3    Coombes, R.C.4
  • 57
    • 0028846512 scopus 로고
    • Constitutive activation of fibroblast growth factor receptor-2 by a point mutation associated with Crouzon syndrome
    • Neilson KM, Friesel RE. Constitutive activation of fibroblast growth factor receptor-2 by a point mutation associated with Crouzon syndrome. J Biol Chem. 1995;270:26037-26040.
    • (1995) J Biol Chem , vol.270 , pp. 26037-26040
    • Neilson, K.M.1    Friesel, R.E.2
  • 58
    • 0029764116 scopus 로고    scopus 로고
    • Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains
    • Neilson KM, Friesel R. Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains. J Biol Chem. 1996;271:25049-25057.
    • (1996) J Biol Chem , vol.271 , pp. 25049-25057
    • Neilson, K.M.1    Friesel, R.2
  • 59
    • 0029935895 scopus 로고    scopus 로고
    • Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia
    • Naski MC, Wang Q, Xu J, Ornitz DM. Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia. Nature Genet. 1996;13:233-237.
    • (1996) Nature Genet , vol.13 , pp. 233-237
    • Naski, M.C.1    Wang, Q.2    Xu, J.3    Ornitz, D.M.4
  • 60
    • 0030896404 scopus 로고    scopus 로고
    • Activation of STAT 1 by mutant fibroblast growth-factor receptor in thanatophoric dysplasia type II dwarfism
    • Su WCS, Kitagawa M, Xue N, Xie B, Garofalo S, Cho J, Deng C, Horton WA, Fu X-Y. Activation of STAT 1 by mutant fibroblast growth-factor receptor in thanatophoric dysplasia type II dwarfism. Nature. 1997;386:288-292.
    • (1997) Nature , vol.386 , pp. 288-292
    • Su, W.C.S.1    Kitagawa, M.2    Xue, N.3    Xie, B.4    Garofalo, S.5    Cho, J.6    Deng, C.7    Horton, W.A.8    Fu, X.-Y.9
  • 62
    • 0028893485 scopus 로고
    • The release of fibroblast growth factor-1 from NIH 3T3 cells in response to temperature involves the function of cysteine residues
    • Jackson A, Tarantini F, Gamble S, Friedman S, Maciag T. The release of fibroblast growth factor-1 from NIH 3T3 cells in response to temperature involves the function of cysteine residues. J Biol Chem. 1995;270:33-36.
    • (1995) J Biol Chem , vol.270 , pp. 33-36
    • Jackson, A.1    Tarantini, F.2    Gamble, S.3    Friedman, S.4    Maciag, T.5
  • 63
    • 0026548976 scopus 로고
    • Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex
    • Mignatti P, Morimoto T, Rifkin DB. Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex. J Cell Physiol. 1992;151:81-93.
    • (1992) J Cell Physiol , vol.151 , pp. 81-93
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 64
    • 0028800457 scopus 로고
    • The cysteine residue responsible for the release of fibroblast growth factor-1 resides in a domain independent of the domain for phosphatidylserine binding
    • Tarantini F, Gamble S, Jackson A, Maciag T. The cysteine residue responsible for the release of fibroblast growth factor-1 resides in a domain independent of the domain for phosphatidylserine binding. J Biol Chem. 1995;270:29039-29042.
    • (1995) J Biol Chem , vol.270 , pp. 29039-29042
    • Tarantini, F.1    Gamble, S.2    Jackson, A.3    Maciag, T.4
  • 65
    • 0031022514 scopus 로고    scopus 로고
    • The carboxy-terminal half of FGF-1 is involved in the regulation of FGF-1 secretion in response to heat shock
    • Shi J, Friedman S, Maciag T. The carboxy-terminal half of FGF-1 is involved in the regulation of FGF-1 secretion in response to heat shock. J Biol Chem. 1997; 272:1142-1147
    • (1997) J Biol Chem , vol.272 , pp. 1142-1147
    • Shi, J.1    Friedman, S.2    Maciag, T.3
  • 66
  • 67
    • 0028168590 scopus 로고
    • Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling
    • 1994
    • Zhang JZ, Davletov BA, Sudhof TC, Anderson RGW. 1994. Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling. Cell. 1994;78:751-760.
    • (1994) Cell , vol.78 , pp. 751-760
    • Zhang, J.Z.1    Davletov, B.A.2    Sudhof, T.C.3    Anderson, R.G.W.4
  • 68
    • 0032575608 scopus 로고    scopus 로고
    • The extravesicular domain of synaptotagmin-1 is released with the latent fibroblast growth factor-1 homodimer in response to heat shock
    • Tarantini F, La Vallee T, Jackson A, Gamble S, Mouta Carreira C, Garfinkel S, Burgess WH, Maciag T. The extravesicular domain of synaptotagmin-1 is released with the latent fibroblast growth factor-1 homodimer in response to heat shock. J Biol Chem. 1998;273:22209-22216.
    • (1998) J Biol Chem , vol.273 , pp. 22209-22216
    • Tarantini, F.1    La Vallee, T.2    Jackson, A.3    Gamble, S.4    Mouta Carreira, C.5    Garfinkel, S.6    Burgess, W.H.7    Maciag, T.8
  • 69
    • 0025270739 scopus 로고
    • Phospholipid-binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin MS, Fried VA, Mignery GA, Jahn R, Sudhof TC. Phospholipid-binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature. 1990;345:260-263.
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Sudhof, T.C.5
  • 70
    • 0029125354 scopus 로고
    • Interaction of partially structured states of acidic fibroblast growth factor with phospholipid membranes
    • Mach H, Middaugh CR. Interaction of partially structured states of acidic fibroblast growth factor with phospholipid membranes. Biochemistry. 1995;34:9913-9920.
    • (1995) Biochemistry , vol.34 , pp. 9913-9920
    • Mach, H.1    Middaugh, C.R.2
  • 71
    • 0032577067 scopus 로고    scopus 로고
    • Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers
    • Chapman ER, Davis AF. Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers. J Biol Chem. 1998;273:13995-14001.
    • (1998) J Biol Chem , vol.273 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 73
    • 0032374094 scopus 로고    scopus 로고
    • The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation
    • Kassam G, Le BH, Choi K, Kang H, Fitzpatrick S, Louie P, Waisman D. The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry. 1998;37:16958-16966.
    • (1998) Biochemistry , vol.37 , pp. 16958-16966
    • Kassam, G.1    Le, B.H.2    Choi, K.3    Kang, H.4    Fitzpatrick, S.5    Louie, P.6    Waisman, D.7
  • 74
    • 0031576550 scopus 로고    scopus 로고
    • Two distinct anti-allergic drugs, amlexanox and cromolyn, bind to the same kinds of calcium-binding proteins, except calmodulin, in bovine lung extract
    • Oyama Y, Shishibori T, Yamashita K, Naya T, Nakagiri S, Maeta H, Kobayashi R. Two distinct anti-allergic drugs, amlexanox and cromolyn, bind to the same kinds of calcium-binding proteins, except calmodulin, in bovine lung extract. Biochem Biophys Res Commun. 1997240:341-347.
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 341-347
    • Oyama, Y.1    Shishibori, T.2    Yamashita, K.3    Naya, T.4    Nakagiri, S.5    Maeta, H.6    Kobayashi, R.7
  • 76
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • PII: S0968-0004
    • Schafer BW, Heizman CW. The S100 family of EF-hand calcium-binding proteins: functions and pathology. TIBS. 1996;21 PII: S0968-0004:134-140.
    • (1996) TIBS , vol.21 , pp. 134-140
    • Schafer, B.W.1    Heizman, C.W.2
  • 77
    • 0030898101 scopus 로고    scopus 로고
    • Myeloid-related protein (mrp) 8 and MRP14, calcium-binding proteins of the s100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway
    • Rammes A., Roth J, Goebeler M, Klempt M, Hartmann M, Sorg C. Myeloid-related protein (mrp) 8 and MRP14, calcium-binding proteins of the s100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway. J Biol Chem. 1997;272:9496-9502.
    • (1997) J Biol Chem , vol.272 , pp. 9496-9502
    • Rammes, A.1    Roth, J.2    Goebeler, M.3    Klempt, M.4    Hartmann, M.5    Sorg, C.6
  • 78
    • 0029788890 scopus 로고    scopus 로고
    • Interaction of the fibrinolyctic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2
    • Hajjar KA, Guevara CA, Lev E, Dowling K, Chacko J. Interaction of the fibrinolyctic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2. J Biol Chem. 1996;271:21652-21659.
    • (1996) J Biol Chem , vol.271 , pp. 21652-21659
    • Hajjar, K.A.1    Guevara, C.A.2    Lev, E.3    Dowling, K.4    Chacko, J.5
  • 79
    • 0032549693 scopus 로고    scopus 로고
    • Level of expression of phospholipid scramblase regulates induced movement of phosphatidylserine to the cell surface
    • Zhao, J, Zhou Q, Wiedmer T, Sims PJ. Level of expression of phospholipid scramblase regulates induced movement of phosphatidylserine to the cell surface. J Biol Chem. 1998;273:6603-6606.
    • (1998) J Biol Chem , vol.273 , pp. 6603-6606
    • Zhao, J.1    Zhou, Q.2    Wiedmer, T.3    Sims, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.