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Volumn 3, Issue 6, 2008, Pages 359-372

An integrated-molecule-format multicolor probe for monitoring multiple activities of a bioactive small molecule

Author keywords

[No Author keywords available]

Indexed keywords

ESTROGEN RECEPTOR ALPHA; LIGAND; LUCIFERASE; PROTEIN TYROSINE PHOSPHATASE SHP; LUMINESCENT AGENT; PROTEIN TYROSINE KINASE;

EID: 48049122439     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb800004s     Document Type: Article
Times cited : (45)

References (32)
  • 1
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: A double-edged sword
    • Aggarwal, B. B. (2003) Signalling pathways of the TNF superfamily: a double-edged sword, Nat. Rev. Immunol. 3, 745-756.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 2
    • 34548656928 scopus 로고    scopus 로고
    • Kim, S. B., Kanno, A., Ozawa, T., Tao, H., and Umezawa, Y. (2007) Nongenomic activity of ligands in the association of androgen receptor with Src, ACS Chem. Biol. 2, 484-492.
    • Kim, S. B., Kanno, A., Ozawa, T., Tao, H., and Umezawa, Y. (2007) Nongenomic activity of ligands in the association of androgen receptor with Src, ACS Chem. Biol. 2, 484-492.
  • 3
    • 0037180571 scopus 로고    scopus 로고
    • Noninvasive imaging of protein-protein interactions in living subjects by using reporter protein complementation and reconstitution strategies
    • Paulmurugan, R., Umezawa, Y., and Gambhir, S. S. (2002) Noninvasive imaging of protein-protein interactions in living subjects by using reporter protein complementation and reconstitution strategies, Proc. Natl. Acad. Sci. U.S.A. 99, 15608-15613.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 15608-15613
    • Paulmurugan, R.1    Umezawa, Y.2    Gambhir, S.S.3
  • 4
    • 4143074858 scopus 로고    scopus 로고
    • High-throughput sensing and noninvasive imaging of protein nuclear transport by using reconstitution of split Renilla luciferase
    • Kim, S. B., Ozawa, T., Watanabe, S., and Umezawa, Y. (2004) High-throughput sensing and noninvasive imaging of protein nuclear transport by using reconstitution of split Renilla luciferase, Proc. Natl. Acad. Sci. U. S. A. 101, 11542-11547.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 11542-11547
    • Kim, S.B.1    Ozawa, T.2    Watanabe, S.3    Umezawa, Y.4
  • 5
    • 0036878430 scopus 로고    scopus 로고
    • The influence of Ala243 (Gly247), Arg215 and Thr226 (Asn230) on the bioluminescence spectra and pH-sensitivity of railroad worm, click beetle and firefly luciferases
    • Viviani, V. R., Uchida, A., Viviani, W., and Ohmiya, Y. (2002) The influence of Ala243 (Gly247), Arg215 and Thr226 (Asn230) on the bioluminescence spectra and pH-sensitivity of railroad worm, click beetle and firefly luciferases, Photochem. Photobiol. 76, 538-544.
    • (2002) Photochem. Photobiol , vol.76 , pp. 538-544
    • Viviani, V.R.1    Uchida, A.2    Viviani, W.3    Ohmiya, Y.4
  • 6
    • 33750483267 scopus 로고    scopus 로고
    • An intramolecular folding sensor for imaging estrogen receptor-ligand interactions
    • Paulmurugan, R., and Gambhir, S. S. (2006) An intramolecular folding sensor for imaging estrogen receptor-ligand interactions, Proc. Natl. Acad. Sci. U.S.A. 103, 15883-15888.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 15883-15888
    • Paulmurugan, R.1    Gambhir, S.S.2
  • 7
    • 33746216307 scopus 로고    scopus 로고
    • A fluorescent indicator to visualize activities of the androgen receptor ligands in single living cells
    • Awais, M., Sato, M., Lee, X. F., and Umezawa, Y. (2006) A fluorescent indicator to visualize activities of the androgen receptor ligands in single living cells, Angew. Chem., Int. Ed. 45, 2707-2712.
    • (2006) Angew. Chem., Int. Ed , vol.45 , pp. 2707-2712
    • Awais, M.1    Sato, M.2    Lee, X.F.3    Umezawa, Y.4
  • 9
    • 0034671963 scopus 로고    scopus 로고
    • Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Iα and green fluorescent proteins
    • Sato, M., Hida, N., Ozawa, T., and Umezawa, Y. (2000) Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Iα and green fluorescent proteins, Anal. Chem. 72, 5918-5924.
    • (2000) Anal. Chem , vol.72 , pp. 5918-5924
    • Sato, M.1    Hida, N.2    Ozawa, T.3    Umezawa, Y.4
  • 10
    • 14744281422 scopus 로고    scopus 로고
    • Firefly luciferase enzyme fragment complementation for imaging in cells and living animals
    • Paulmurugan, R., and Gambhir, S. S. (2005) Firefly luciferase enzyme fragment complementation for imaging in cells and living animals, Anal. Chem. 77, 1295-1302.
    • (2005) Anal. Chem , vol.77 , pp. 1295-1302
    • Paulmurugan, R.1    Gambhir, S.S.2
  • 11
    • 34447331719 scopus 로고    scopus 로고
    • Bioluminescent indicator for determining protein-protein interactions using intramolecular complementation of split click beetle luciferase
    • Kim, S. B., Otani, Y., Umezawa, Y., and Tao, H. (2007) Bioluminescent indicator for determining protein-protein interactions using intramolecular complementation of split click beetle luciferase, Anal. Chem. 79, 4820-4826.
    • (2007) Anal. Chem , vol.79 , pp. 4820-4826
    • Kim, S.B.1    Otani, Y.2    Umezawa, Y.3    Tao, H.4
  • 12
    • 33847685881 scopus 로고    scopus 로고
    • Integrated molecule-format bioluminescent probe for visualizing androgenicity of ligands based on the intramolecular association of androgen receptor with its recognition peptide
    • Kim, S. B., Awais, M., Sato, M., Umezawa, Y., and Tao, H. (2007) Integrated molecule-format bioluminescent probe for visualizing androgenicity of ligands based on the intramolecular association of androgen receptor with its recognition peptide, Anal. Chem. 79, 1874-1880.
    • (2007) Anal. Chem , vol.79 , pp. 1874-1880
    • Kim, S.B.1    Awais, M.2    Sato, M.3    Umezawa, Y.4    Tao, H.5
  • 13
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans, R. M. (1988) The steroid and thyroid hormone receptor superfamily, Science 240, 889-895.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 14
    • 15444368857 scopus 로고    scopus 로고
    • Mechanisms of estrogen receptor signaling: Convergence of genomic and nongenomic actions on target genes
    • Bjornstrom, L., and Sjoberg, M. (2005) Mechanisms of estrogen receptor signaling: convergence of genomic and nongenomic actions on target genes, Mol. Endocrinol. 19, 833-842.
    • (2005) Mol. Endocrinol , vol.19 , pp. 833-842
    • Bjornstrom, L.1    Sjoberg, M.2
  • 15
    • 0029563173 scopus 로고
    • Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element
    • Arnold, S. F., Vorojeikina, D. P., and Notides, A. C. (1995) Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element, J. Biol. Chem. 270, 30205-30212.
    • (1995) J. Biol. Chem , vol.270 , pp. 30205-30212
    • Arnold, S.F.1    Vorojeikina, D.P.2    Notides, A.C.3
  • 16
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau, A. K., Barstad, D., Loria, P. M., Cheng, L., Kushner, P. J., Agard, D. A., and Greene, G. L. (1998) The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen, Cell 95, 927-937.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 17
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D. M., Kalkhoven, E., Hoare, S., and Parker, M. G. (1997) A signature motif in transcriptional co-activators mediates binding to nuclear receptors, Nature 387, 733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 18
    • 7944233251 scopus 로고    scopus 로고
    • The interplay between Src and integrins in normal and tumor biology
    • Playford, M. P., and Schaller, M. D. (2004) The interplay between Src and integrins in normal and tumor biology, Oncogene 23, 7928-7946.
    • (2004) Oncogene , vol.23 , pp. 7928-7946
    • Playford, M.P.1    Schaller, M.D.2
  • 19
    • 27544473719 scopus 로고    scopus 로고
    • Quantitative determination of protein nuclear transport induced by phosphorylation or by proteolysis
    • Kim, S. B., Takao, R., Ozawa, T., and Umezawa, Y. (2005) Quantitative determination of protein nuclear transport induced by phosphorylation or by proteolysis, Anal. Chem. 77, 6928-6934.
    • (2005) Anal. Chem , vol.77 , pp. 6928-6934
    • Kim, S.B.1    Takao, R.2    Ozawa, T.3    Umezawa, Y.4
  • 22
    • 0032538434 scopus 로고    scopus 로고
    • A transcriptional coactivator, steroid receptor coactivator-3, selectively augments steroid receptor transcriptional activity
    • Suen, C. S., Berrodin, T. J., Mastroeni, R., Cheskis, B. J., Lyttle, C. R., and Frail, D. E. (1998) A transcriptional coactivator, steroid receptor coactivator-3, selectively augments steroid receptor transcriptional activity, J. Biol. Chem. 273, 27645-27653.
    • (1998) J. Biol. Chem , vol.273 , pp. 27645-27653
    • Suen, C.S.1    Berrodin, T.J.2    Mastroeni, R.3    Cheskis, B.J.4    Lyttle, C.R.5    Frail, D.E.6
  • 23
    • 36749104291 scopus 로고    scopus 로고
    • Quantification of dynamic protein complexes using Renilla luciferase fragment complementation applied to protein kinase A activities in vivo
    • Stefan, E., Aquin, S., Berger, N., Landry, C. R., Nyfeler, B., Bouvier, M., and Michnick, S. W. (2007) Quantification of dynamic protein complexes using Renilla luciferase fragment complementation applied to protein kinase A activities in vivo, Proc. Natl. Acad. Sci. U.S.A. 104, 16916-16921.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 16916-16921
    • Stefan, E.1    Aquin, S.2    Berger, N.3    Landry, C.R.4    Nyfeler, B.5    Bouvier, M.6    Michnick, S.W.7
  • 24
    • 1942454742 scopus 로고    scopus 로고
    • A genetically encoded fluorescent indicator capable of discriminating estrogen agonists from antagonists in living cells
    • Awais, M., Sato, M., Sasaki, K., and Umezawa, Y. (2004) A genetically encoded fluorescent indicator capable of discriminating estrogen agonists from antagonists in living cells, Anal. Chem. 76, 2181-2186.
    • (2004) Anal. Chem , vol.76 , pp. 2181-2186
    • Awais, M.1    Sato, M.2    Sasaki, K.3    Umezawa, Y.4
  • 27
    • 0031036099 scopus 로고    scopus 로고
    • Estradiol-binding mechanism and binding capacity of the human estrogen receptor is regulated by tyrosine phosphorylation
    • Arnold, S. F., Melamed, M., Vorojeikina, D. P., Notides, A. C., and Sasson, S. (1997) Estradiol-binding mechanism and binding capacity of the human estrogen receptor is regulated by tyrosine phosphorylation, Mol. Endocrinol. 11, 48-53.
    • (1997) Mol. Endocrinol , vol.11 , pp. 48-53
    • Arnold, S.F.1    Melamed, M.2    Vorojeikina, D.P.3    Notides, A.C.4    Sasson, S.5
  • 28
    • 0037006978 scopus 로고    scopus 로고
    • Mutations of tyrosine 537 in the human estrogen receptor-alpha selectively alter the receptor's affinity for estradiol and the kinetics of the interaction
    • Zhong, L., and Skafar, D. F. (2002) Mutations of tyrosine 537 in the human estrogen receptor-alpha selectively alter the receptor's affinity for estradiol and the kinetics of the interaction, Biochemistry 41, 4209-4217.
    • (2002) Biochemistry , vol.41 , pp. 4209-4217
    • Zhong, L.1    Skafar, D.F.2
  • 29
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of fire-fly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., Franks, N. P., and Brick, P. (1996) Crystal structure of fire-fly luciferase throws light on a superfamily of adenylate-forming enzymes, Structure 4, 287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 30
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 31
    • 0034465595 scopus 로고    scopus 로고
    • Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells
    • Tyagi, R. K., Lavrovsky, Y., Ahn, S. C., Song, C. S., Chatterjee, B., and Roy, A. K. (2000) Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells, Mol. Endocrinol. 14, 1162-1174.
    • (2000) Mol. Endocrinol , vol.14 , pp. 1162-1174
    • Tyagi, R.K.1    Lavrovsky, Y.2    Ahn, S.C.3    Song, C.S.4    Chatterjee, B.5    Roy, A.K.6
  • 32
    • 0035894271 scopus 로고    scopus 로고
    • Protein splicing-based reconstitution of split green fluorescent protein for monitoring protein-protein interactions in bacteria: Improved sensitivity and reduced screening time
    • Ozawa, T., Takeuchi, T. M., Kaihara, A., Sato, M., and Umezawa, Y. (2001) Protein splicing-based reconstitution of split green fluorescent protein for monitoring protein-protein interactions in bacteria: improved sensitivity and reduced screening time, Anal. Chem. 73, 5866-5874.
    • (2001) Anal. Chem , vol.73 , pp. 5866-5874
    • Ozawa, T.1    Takeuchi, T.M.2    Kaihara, A.3    Sato, M.4    Umezawa, Y.5


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