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Volumn 20, Issue 9, 2009, Pages 2401-2412

Fibroblast growth factor receptor-1 (FGFR1) nuclear dynamics reveal a novel mechanism in transcription control

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR 1; S6 KINASE;

EID: 65649127721     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-06-0600     Document Type: Article
Times cited : (65)

References (42)
  • 1
    • 0029741379 scopus 로고    scopus 로고
    • 5 quaternary structure of cholera toxin
    • Bastiaens, P.I.H., Majoul, I. V., Verveer, P. J., Soling, H. D., and Jovin, T. M. (1996). Imaging the intracellular trafficking and state of the AB(5) quaternary structure of cholera toxin. EMBO J. 15 , 4246-4253. (Pubitemid 26278707)
    • (1996) EMBO Journal , vol.15 , Issue.16 , pp. 4246-4253
    • Bastiaens, P.I.H.1    Majoul, I.V.2    Verveer, P.J.3    Soling, H.-D.4    Jovin, T.M.5
  • 2
    • 0013537360 scopus 로고    scopus 로고
    • Dynamic behavior of transcription factors on a natural promoter in living cells
    • DOI 10.1093/embo-reports/kvf244
    • Becker, M., Baumann, C., John, S., Walker, D. A., Vigneron, M., McNally, J. G., and Hager, G. L. (2002). Dynamic behavior of transcription factors on a natural promoter in living cells. EMBO Rep. 3 , 1188-1194. (Pubitemid 36105009)
    • (2002) EMBO Reports , vol.3 , Issue.12 , pp. 1188-1194
    • Becker, M.1    Baumann, C.2    John, S.3    Walker, D.A.4    Vigneron, M.5    McNally, J.G.6    Hager, G.L.7
  • 3
    • 0347927629 scopus 로고    scopus 로고
    • Differential intranuclear localization of fibroblast growth factor-2 isoforms and specific interaction with the survival of motoneuron protein
    • DOI 10.1074/jbc.M206056200
    • Claus, P., Doring, F., Gringel, S., Muller-Ostermeyer, F., Fuhlrott, J., Kraft, T., and Grothe, C. (2003). Differential intranuclear localization of fibroblast growth factor-2 isoforms and specific interaction with the survival of motoneuron protein. J. Biol. Chem. 278 , 479-485. (Pubitemid 36043599)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 479-485
    • Claus, P.1    Doring, F.2    Gringel, S.3    Muller-Ostermeyer, F.4    Fuhlrott, J.5    Kraft, T.6    Grothe, C.7
  • 4
    • 0036261563 scopus 로고    scopus 로고
    • Proteasomal inhibition enhances glucocorticoid receptor transactivation and alters its subnuclear trafficking
    • DOI 10.1128/MCB.22.12.4113-4123.2002
    • Deroo, B. J., Rentsch, C., Sampath, S., Young, J., DeFranco, D. B., and Archer, T. K. (2002). Proteasomal inhibition enhances glucocorticoid receptor transactivation and alters its subnuclear trafficking. Mol. Cell. Biol. 22 , 4113-4123. (Pubitemid 34556582)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.12 , pp. 4113-4123
    • Deroo, B.J.1    Rentsch, C.2    Sampath, S.3    Young, J.4    DeFranco, D.B.5    Archer, T.K.6
  • 5
    • 0028242341 scopus 로고
    • Inhibitors of transcription such as 5,6-dichloro-1-β-D- ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7") promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit
    • Dubois, M. F., Nguyen, V. T., Bellier, S., and Bensaude, O. (1994). Inhibitors of transcription such as 5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7) promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit. J. Biol. Chem. 269 , 13331-13336. (Pubitemid 24978619)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.18 , pp. 13331-13336
    • Dubois, M.-F.1    Nguyen, V.T.2    Bellier, S.3    Bensaude, O.4
  • 6
    • 2242433534 scopus 로고    scopus 로고
    • A kinetic framework for a mammalian RNA polymerase in vivo
    • DOI 10.1126/science.1076164
    • Dundr, M., Hoffmann-Rohrer, U., Hu, Q., Grummt, I., Rothblum, L. I., Phair, R. D., and Misteli, T. (2002). A kinetic framework for a mammalian RNA polymerase in vivo. Science 298 , 1623-1626. (Pubitemid 35387201)
    • (2002) Science , vol.298 , Issue.5598 , pp. 1623-1626
    • Dundr, M.1    Hoffmann-Rohrer, U.2    Hu, Q.3    Grummt, I.4    Rothblum, L.I.5    Phair, R.D.6    Misteli, T.7
  • 7
    • 33745761634 scopus 로고    scopus 로고
    • Factors controlling fibroblast growth factor receptor-1's cytoplasmic trafficking and its regulation as revealed by FRAP analysis
    • DOI 10.1091/mbc.E05-08-0749
    • Dunham-Ems, S. M., Pudavar, H. E., Myers, J. M., Maher, P. A., Prasad, P. N., and Stachowiak, M. K. (2006). Factors controlling fibroblast growth factor receptor-1's cytoplasmic trafficking and its regulation as revealed by FRAP analysis. Mol. Biol. Cell 17 , 2223-2235. (Pubitemid 44011738)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2223-2235
    • Dunham-Ems, S.M.1    Pudavar, H.E.2    Myers, J.M.3    Maher, P.A.4    Prasad, P.N.5    Stachowiak, M.K.6
  • 8
    • 3442876959 scopus 로고    scopus 로고
    • Cellular signaling and protein-protein interactions studied using fluorescence recovery after photobleaching
    • Dunham, S. M., Pudavar, H. E., Prasad, P. N., and Stachowiak, M. K. (2004). Cellular signaling and protein-protein interactions studied using fluorescence recovery after photobleaching. J. Phys. Chem. B 108 , 10540-10546.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 10540-10546
    • Dunham, S.M.1    Pudavar, H.E.2    Prasad, P.N.3    Stachowiak, M.K.4
  • 9
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases Link Ubiquitylation of Histone H2B to Methylation of Histone H3
    • DOI 10.1016/S1097-2765(04)00026-7
    • Ezhkova, E., and Tansey, W. P. (2004). Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol. Cell 13 , 435-442. (Pubitemid 38229815)
    • (2004) Molecular Cell , vol.13 , Issue.3 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 10
    • 23344445129 scopus 로고    scopus 로고
    • Control of CREB-binding protein signaling by nuclear fibroblast growth factor receptor-1: A novel mechanism of gene regulation
    • DOI 10.1074/jbc.M504400200
    • Fang, X., Stachowiak, E. K., Dunham-Ems, S. M., Klejbor, I., and Stachowiak, M. K. (2005). Control of CREB-binding protein signaling by nuclear fibroblast growth factor receptor-1, a novel mechanism of gene regulation. J. Biol. Chem. 280 , 28451-28462. (Pubitemid 41105744)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28451-28462
    • Fang, X.1    Stachowiak, E.K.2    Dunham-Ems, S.M.3    Klejbor, I.4    Stachowiak, M.K.5
  • 13
    • 0028956761 scopus 로고
    • High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells-implications for the modulation of FGF-2
    • Hanneken, A., Maher, P., and Baird, A. (1995). High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells-implications for the modulation of FGF-2. J. Cell Biol. 128 , 1221-1228.
    • (1995) J. Cell Biol. , vol.128 , pp. 1221-1228
    • Hanneken, A.1    Maher, P.2    Baird, A.3
  • 14
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • He, D. C., Nickerson, J. A., and Penman, S. (1990). Core filaments of the nuclear matrix. J. Cell Biol. 110 , 569-580. (Pubitemid 20088925)
    • (1990) Journal of Cell Biology , vol.110 , Issue.3 , pp. 569-580
    • He, D.1    Nickerson, J.A.2    Penman, S.3
  • 15
    • 3142669265 scopus 로고    scopus 로고
    • 90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): Role in FGFR1 signaling
    • DOI 10.1074/jbc.M311144200
    • Hu, Y., Fang, X., Dunham, S. M., Prada, C., Stachowiak, E. K., and Stachowiak, M. K. (2004). 90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling. J. Biol. Chem. 279 , 29325-29335. (Pubitemid 38915810)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.28 , pp. 29325-29335
    • Hu, Y.1    Fang, X.2    Dunham, S.M.3    Prada, C.4    Stachowiak, E.K.5    Stachowiak, M.K.6
  • 16
    • 10044250938 scopus 로고    scopus 로고
    • Dynamic interactions of a transcription factor with DNA are accelerated by a chromatin remodeller
    • DOI 10.1038/sj.embor.7400281
    • Karpova, T. S., Chen, T. Y., Sprague, B. L., and McNally, J. G. (2004). Dynamic interactions of a transcription factor with DNA are accelerated by a chromatin remodeller. EMBO Rep. 5 , 1064-1070. (Pubitemid 39600205)
    • (2004) EMBO Reports , vol.5 , Issue.11 , pp. 1064-1070
    • Karpova, T.S.1    Chen, C.Y.2    Sprague, B.L.3    McNally, J.G.4
  • 17
    • 0037049641 scopus 로고    scopus 로고
    • The transcription cycle of RNA polymerase II in living cells
    • DOI 10.1083/jcb.200206019
    • Kimura, H., Sugaya, K., and Cook, P. R. (2002). The transcription cycle of RNA polymerase II in living cells. J. Cell Biol. 159 , 777-782. (Pubitemid 36008360)
    • (2002) Journal of Cell Biology , vol.159 , Issue.5 , pp. 777-782
    • Kimura, H.1    Sugaya, K.2    Cook, P.R.3
  • 18
    • 7244260747 scopus 로고    scopus 로고
    • Induction of cyclin-dependent kinase 5 and its activator p35 through the extracellular-signal-regulated kinase and protein kinase a pathways during retinoic-acid mediated neuronal differentiation in human neuroblastoma SK-N-BE(2)C cells
    • DOI 10.1111/j.1471-4159.2004.02770.x
    • Lee, J. H., and Kim, K. T. (2004). Induction of cyclin-dependent kinase 5 and its activator p35 through the extracellular-signal-regulated kinase and protein kinase A pathways during retinoic-acid mediated neuronal differentiation in human neuroblastoma SK-N-BE(2)C cells. J. Neurochem. 91 , 634-647. (Pubitemid 39431158)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.3 , pp. 634-647
    • Lee, J.-H.1    Kim, K.-T.2
  • 19
    • 0029954235 scopus 로고    scopus 로고
    • Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2
    • DOI 10.1083/jcb.134.2.529
    • Maher, P. A. (1996). Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2. J. Cell Biol. 134 , 529-536. (Pubitemid 26250718)
    • (1996) Journal of Cell Biology , vol.134 , Issue.2 , pp. 529-536
    • Maher, P.A.1
  • 20
    • 0026854973 scopus 로고
    • Kinetics of formation reactions of two- and trinuclear complexes of silver in radiophotoluminescent glasses
    • Marshall, N. F., and Price, D. H. (1992). Control of formation of two distinct classes of RNA polymerase II elongation complexes. Mol. Cell. Biol. 12 , 2078-2090. (Pubitemid 23632012)
    • (1992) Fizika i Khimiya Stekla , vol.18 , Issue.3 , pp. 66-76
    • Syutkin, V.M.1    Dmitryuk, A.V.2    Tolkachev, V.A.3
  • 21
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • DOI 10.1126/science.287.5456.1262
    • McNally, J. G., Muller, W. G., Walker, D., Wolford, R., and Hager, G. L. (2000). The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science 287 , 1262-1265. (Pubitemid 30112147)
    • (2000) Science , vol.287 , Issue.5456 , pp. 1262-1265
    • McNally, J.C.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 22
  • 23
    • 0000631273 scopus 로고    scopus 로고
    • The signal-dependent coactivator CBP is a nuclear target for pp90(RSK)
    • DOI 10.1016/S0092-8674(00)80119-1
    • Nakajima, T., Fukamizu, A., Takahashi, J., Gage, F. H., Fisher, T., Blenis, J., and Montminy, M. R. (1996). The signal-dependent coactivator CBP is a nuclear target for pp90RSK. Cell 86 , 465-474. (Pubitemid 26272086)
    • (1996) Cell , vol.86 , Issue.3 , pp. 465-474
    • Nakajima, T.1    Fukamizu, A.2    Takahashi, J.3    Gage, F.H.4    Fisher, T.5    Blenis, J.6    Montminy, M.R.7
  • 25
    • 0031807917 scopus 로고    scopus 로고
    • Immunofluorescent localization of actin in relation to transcription sites in mouse pronuclei
    • DOI 10.1002/(SICI)1098-2795(199807)50:3<263::AID-MRD2>3.0.CO;2-H
    • Nguyen, E., Besombes, D., and Debey, P. (1998). Immunofluorescent localization of actin in relation to transcription sites in mouse pronuclei. Mol. Reprod. Dev. 50 , 263-272. (Pubitemid 28268465)
    • (1998) Molecular Reproduction and Development , vol.50 , Issue.3 , pp. 263-272
    • Nguyen, E.1    Besombes, D.2    Debey, P.3
  • 27
    • 0035384692 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy: A mini review
    • Periasamy, A. (2001). Fluorescence resonance energy transfer microscopy: a mini review. J. Biomed. Optics 6 , 287-291.
    • (2001) J. Biomed. Optics , vol.6 , pp. 287-291
    • Periasamy, A.1
  • 28
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • DOI 10.1038/35007077
    • Phair, R. D., and Misteli, T. (2000). High mobility of proteins in the mammalian cell nucleus. Nature 404 , 604-609. (Pubitemid 30205058)
    • (2000) Nature , vol.404 , Issue.6778 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 29
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: Three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • DOI 10.1128/MCB.24.14.6393-6402.2004
    • Phair, R. D., Scaffidi, P., Elbi, C., Vecerova, J., Dey, A., Ozato, K., Brown, D. T., Hager, G., Bustin, M., and Misteli, T. (2004). Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins. Mol. Cell. Biol. 24 , 6393-6402. (Pubitemid 38891138)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.14 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerova, J.4    Dey, A.5    Ozato, K.6    Brown, D.T.7    Hager, G.8    Bustin, M.9    Misteli, T.10
  • 30
    • 0035911965 scopus 로고    scopus 로고
    • Importin β-mediated nuclear import of fibroblast growth factor receptor: Role in cell proliferation
    • DOI 10.1083/jcb.152.6.1307
    • Reilly, J. F., and Maher, P. A. (2001). Importin beta-mediated nuclear import of fibroblast growth factor receptor: role in cell proliferation. J. Cell Biol. 152 , 1307-1312. (Pubitemid 34280187)
    • (2001) Journal of Cell Biology , vol.152 , Issue.6 , pp. 1307-1312
    • Reilly, J.F.1    Maher, P.A.2
  • 31
    • 27144492957 scopus 로고    scopus 로고
    • Direct regulation of rRNA transcription by fibroblast growth factor 2
    • DOI 10.1128/MCB.25.21.9419-9426.2005
    • Sheng, Z., Liang, Y., Lin, C. Y., Comai, L., and Chirico, W. J. (2005). Direct regulation of rRNA transcription by fibroblast growth factor 2. Mol. Cell. Biol. 25 , 9419-9426. (Pubitemid 41507842)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.21 , pp. 9419-9426
    • Sheng, Z.1    Liang, Y.2    Lin, C.-Y.3    Comai, L.4    Chirico, W.J.5
  • 32
    • 0142202822 scopus 로고    scopus 로고
    • Nuclear Matrix Bound Fibroblast Growth Factor Receptor Is Associated With Splicing Factor Rich and Transcriptionally Active Nuclear Speckles
    • DOI 10.1002/jcb.10672
    • Somanathan, S., Stachowiak, E. K., Siegel, A. J., Stachowiak, M. K., and Berezney, R. (2003). Nuclear matrix bound fibroblast growth factor receptor is associated with splicing factor rich and transcriptionally active nuclear speckles. J. Cell. Biochem. 90 , 856-869. (Pubitemid 37406628)
    • (2003) Journal of Cellular Biochemistry , vol.90 , Issue.4 , pp. 856-869
    • Somanathan, S.1    Stachowiak, E.K.2    Siegel, A.J.3    Stachowiak, M.K.4    Berezney, R.5
  • 33
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • DOI 10.1529/biophysj.103.026765
    • Sprague, B. L., Pego, R. L., Stavreva, D. A., and McNally, J. G. (2004). Analysis of binding reactions by fluorescence recovery after photobleaching. Biophys. J. 86 , 3473-3495. (Pubitemid 38780231)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 34
    • 0037347399 scopus 로고    scopus 로고
    • cAMP-induced differentiation of human neuronal progenitor cells is mediated by nuclear fibroblast growth factor receptor-1 (FGFR1)
    • DOI 10.1046/j.1471-4159.2003.01624.x
    • Stachowiak, E. K., Fang, X., Myers, J., Dunham, S., and Stachowiak, M. K. (2003a). cAMP-induced differentiation of human neuronal progenitor cells is mediated by nuclear fibroblast growth factor receptor-1 (FGFR1). J. Neurochem. 84 , 1296-1312. (Pubitemid 36343596)
    • (2003) Journal of Neurochemistry , vol.84 , Issue.6 , pp. 1296-1312
    • Stachowiak, E.K.1    Fang, X.2    Myers, J.3    Dunham, S.4    Stachowiak, M.K.5
  • 35
    • 0242443214 scopus 로고    scopus 로고
    • Integrative Nuclear FGFR1 Signaling (INFS) as a Part of a Universal "Feed-Forward-And-Gate" Signaling Module That Controls Cell Growth and Differentiation
    • DOI 10.1002/jcb.10606
    • Stachowiak, M. K., Fang, X., Myers, J. M., Dunham, S. M., Berezney, R., Maher, P. A., and Stachowiak, E. K. (2003b). Integrative nuclear FGFR1 signaling (INFS) as a part of a universal "feed-forward-and-gate" signaling module that controls cell growth and differentiation. J. Cell. Biochem. 90 , 662-691. (Pubitemid 37392460)
    • (2003) Journal of Cellular Biochemistry , vol.90 , Issue.4 , pp. 662-691
    • Stachowiak, M.K.1    Fang, X.2    Myers, J.M.3    Dunham, S.M.4    Berezney, R.5    Maher, P.A.6    Stachowiak, E.K.7
  • 36
    • 0029785143 scopus 로고    scopus 로고
    • Nuclear accumulation of fibroblast growth factor receptors is regulated by multiple signals in adrenal medullary cells
    • Stachowiak, M. K., Maher, P. A., Joy, A., Mordechai, E., and Stachowiak, E. K. (1996a). Nuclear accumulation of fibroblast growth factor receptors is regulated by multiple signals in adrenal medullary cells. Mol. Biol. Cell 7 , 1299-1317. (Pubitemid 26262065)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.8 , pp. 1299-1317
    • Stachowiak, M.K.1    Maher, P.A.2    Joy, A.3    Mordechai, E.4    Stachowiak, E.K.5
  • 37
    • 0029997013 scopus 로고    scopus 로고
    • Nuclear localization of functional FGF receptor 1 in human astrocytes suggests a novel mechanism for growth factor action
    • DOI 10.1016/0169-328X(96)00010-1
    • Stachowiak, M. K., Maher, P. A., Joy, A., Mordechai, E., and Stachowiak, E. K. (1996b). Nuclear localization of functional FGF receptor 1 in human astrocytes suggests a novel mechanism for growth factor action. Brain Res. 38 , 161-165. (Pubitemid 26159205)
    • (1996) Molecular Brain Research , vol.38 , Issue.1 , pp. 161-165
    • Stachowiak, M.K.1    Maher, P.A.2    Joy, A.3    Mordechai, E.4    Stachowiak, E.K.5
  • 38
    • 37249065138 scopus 로고    scopus 로고
    • Integrative nuclear signaling in cell development - A role for FGF receptor-1
    • DOI 10.1089/dna.2007.0664
    • Stachowiak, M. K., Maher, P. A., and Stachowiak, E. K. (2007). Integrative nuclear signaling in cell development-a role for FGF Receptor-1. DNA Cell Biol. 26 , 811-826. (Pubitemid 350274413)
    • (2007) DNA and Cell Biology , vol.26 , Issue.12 , pp. 811-826
    • Stachowiak, M.K.1    Maher, P.A.2    Stachowiak, E.K.3
  • 39
    • 12144290835 scopus 로고    scopus 로고
    • Rapid Glucocorticoid Receptor Exchange at a Promoter Is Coupled to Transcription and Regulated by Chaperones and Proteasomes
    • DOI 10.1128/MCB.24.7.2682-2697.2004
    • Stavreva, D. A., Muller, W. G., Hager, G. L., Smith, C. L., and McNally, J. G. (2004). Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes. Mol. Cell. Biol. 24 , 2682-2697. (Pubitemid 38381261)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.7 , pp. 2682-2697
    • Stavreva, D.A.1    Muller, W.G.2    Hager, G.L.3    Smith, C.L.4    McNally, J.G.5
  • 42
    • 0035141041 scopus 로고    scopus 로고
    • FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent
    • DOI 10.1038/35050515
    • Stenoien, D. L., Patel, K., Mancini, M. G., Dutertre, M., Smith, C. L., O'Malley, B. W., and Mancini, M. A. (2001b). FRAP reveals that mobility of oestrogen receptor-alpha is ligand-and proteasome-dependent. Nat. Cell Biol. 3 , 15-23. (Pubitemid 32114827)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 15-23
    • Stenoien, D.L.1    Patel, K.2    Mancini, M.G.3    Dutertre, M.4    Smith, C.L.5    O'Malley, B.W.6    Mancini, M.A.7


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