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Volumn 11, Issue 8, 2013, Pages 478-488

Development of a high-throughput screening cancer cell-based luciferase refolding assay for identifying Hsp90 inhibitors

Author keywords

ABC; ATP binding cassette; counts per second; cps; FBS; fetal bovine serum; heat shock protein 90; heat shock response; Hsp90; HSR; HTS, highthroughput; rabbit reticulocyte lysate; RRL; S N; screening; signal to noise ratio; SRB; sulforhodamine B

Indexed keywords

BIPERIDEN; CHAPERONE; ETHOXYQUIN; HEAT SHOCK PROTEIN 90 INHIBITOR; LUCIFERASE; NOVOBIOCIN; ONCOPROTEIN; ANTINEOPLASTIC AGENT; COLORING AGENT; ENZYME INHIBITOR; HEAT SHOCK PROTEIN 90; LISSAMINE RHODAMINE B; MOLECULAR LIBRARY; RHODAMINE;

EID: 84886405298     PISSN: 1540658X     EISSN: 15578127     Source Type: Journal    
DOI: 10.1089/adt.2012.498     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG: Low target binding affinity and potent cell activity-finding an explanation
    • Chiosis G, Huezo H, Rosen N, et al.: 17AAG: low target binding affinity and potent cell activity-finding an explanation. Mol Cancer Ther 2003;2:123-129.
    • (2003) Mol Cancer Ther , vol.2 , pp. 123-129
    • Chiosis, G.1    Huezo, H.2    Rosen, N.3
  • 2
    • 84857994615 scopus 로고    scopus 로고
    • HSP90 inhibition: Two-pronged exploitation of cancer dependencies
    • Travers J, Sharp S, Workman P: HSP90 inhibition: two-pronged exploitation of cancer dependencies. Drug Discov Today 2012;17:242-252.
    • (2012) Drug Discov Today , vol.17 , pp. 242-252
    • Travers, J.1    Sharp, S.2    Workman, P.3
  • 3
    • 84855457952 scopus 로고    scopus 로고
    • Hsp90 molecular chaperone inhibitors: Are we there yet
    • Neckers L, Workman P: Hsp90 molecular chaperone inhibitors: are we there yet Clin Cancer Res 2012;18:64-76.
    • (2012) Clin Cancer Res , vol.18 , pp. 64-76
    • Neckers, L.1    Workman, P.2
  • 4
    • 72449185268 scopus 로고    scopus 로고
    • Phase i trial of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein inhibitor, administered twice weekly in patients with advanced malignancies
    • Kummar S, Gutierrez ME, Gardner ER, et al.: Phase I trial of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein inhibitor, administered twice weekly in patients with advanced malignancies. Eur J Cancer 2010;46:340-347.
    • (2010) Eur J Cancer , vol.46 , pp. 340-347
    • Kummar, S.1    Gutierrez, M.E.2    Gardner, E.R.3
  • 5
    • 74249085361 scopus 로고    scopus 로고
    • Update on Hsp90 inhibitors in clinical trial
    • Kim YS, Alarcon SV, Lee S, et al.: Update on Hsp90 inhibitors in clinical trial. Curr Top Med Chem 2009;9:1479-1492.
    • (2009) Curr Top Med Chem , vol.9 , pp. 1479-1492
    • Kim, Y.S.1    Alarcon, S.V.2    Lee, S.3
  • 7
    • 33750357639 scopus 로고    scopus 로고
    • Synthesis and evaluation of coumermycin A1 analogues that inhibit the Hsp90 protein folding machinery
    • DOI 10.1021/ol061918j
    • Burlison JA, Blagg BS: Synthesis and evaluation of coumermycin A1 analogues that inhibit the Hsp90 protein folding machinery. Org Lett 2006;8:4855-4858. (Pubitemid 44629477)
    • (2006) Organic Letters , vol.8 , Issue.21 , pp. 4855-4858
    • Burlison, J.A.1    Blagg, B.S.J.2
  • 8
    • 56449125983 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of coumarin ring derivatives of the novobiocin scaffold that exhibit antiproliferative activity
    • Donnelly AC, Mays JR, Burlison JA, et al.: The design, synthesis, and evaluation of coumarin ring derivatives of the novobiocin scaffold that exhibit antiproliferative activity. J Org Chem 2008;73:8901-8920.
    • (2008) J Org Chem , vol.73 , pp. 8901-8920
    • Donnelly, A.C.1    Mays, J.R.2    Burlison, J.A.3
  • 9
    • 80054995372 scopus 로고    scopus 로고
    • Development and characterization of a novel C-terminal inhibitor of Hsp90 in androgen dependent and independent prostate cancer cells
    • Eskew JD, Sadikot T, Morales P, et al.: Development and characterization of a novel C-terminal inhibitor of Hsp90 in androgen dependent and independent prostate cancer cells. BMC Cancer 2011;11:468-484.
    • (2011) BMC Cancer , vol.11 , pp. 468-484
    • Eskew, J.D.1    Sadikot, T.2    Morales, P.3
  • 12
    • 80255138632 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of arylated novobiocin analogs as Hsp90 inhibitors
    • Kusuma BR, Duerfeldt AS, Blagg BS: Synthesis and biological evaluation of arylated novobiocin analogs as Hsp90 inhibitors. Bioorg Med Chem Lett 2011;21:7170-7174.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 7170-7174
    • Kusuma, B.R.1    Duerfeldt, A.S.2    Blagg, B.S.3
  • 13
    • 80052801777 scopus 로고    scopus 로고
    • Targeting the heat shock protein 90 dimer with dimeric inhibitors
    • Kusuma BR, Peterson LB, Zhao H, et al.: Targeting the heat shock protein 90 dimer with dimeric inhibitors. J Med Chem 2011;54:6234-6253.
    • (2011) J Med Chem , vol.54 , pp. 6234-6253
    • Kusuma, B.R.1    Peterson, L.B.2    Zhao, H.3
  • 14
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • DOI 10.1074/jbc.M003701200
    • Marcu MG, Chadli A, Bouhouche I, Catelli M, Neckers LM: The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATPbinding domain in the carboxyl terminus of the chaperone. J Biol Chem 2000;275:37181-37186. (Pubitemid 32002137)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 15
    • 72849119781 scopus 로고    scopus 로고
    • Characterization of a novel novobiocin analogue as a putative C-terminal inhibitor of heat shock protein 90 in prostate cancer cells
    • Matthews SB, Vielhauer GA, Manthe CA, et al.: Characterization of a novel novobiocin analogue as a putative C-terminal inhibitor of heat shock protein 90 in prostate cancer cells. Prostate 2010;70:27-36.
    • (2010) Prostate , vol.70 , pp. 27-36
    • Matthews, S.B.1    Vielhauer, G.A.2    Manthe, C.A.3
  • 16
    • 74249114114 scopus 로고    scopus 로고
    • Assays for identification of Hsp90 inhibitors and biochemical methods for discriminating their mechanism of action
    • Matts RL, Manjarrez JR: Assays for identification of Hsp90 inhibitors and biochemical methods for discriminating their mechanism of action. Curr Top Med Chem 2009;9:1462-1478.
    • (2009) Curr Top Med Chem , vol.9 , pp. 1462-1478
    • Matts, R.L.1    Manjarrez, J.R.2
  • 17
    • 0024361230 scopus 로고
    • Protein denaturation during heat shock and related stress. Escherichia coli β-galactosidase and Photinus pyralis luciferase inactivation in mouse cells
    • Nguyen VT, Morange M, Bensaude O: Protein denaturation during heat shock and related stress. Escherichia coli beta-galactosidase and Photinus pyralis luciferase inactivation in mouse cells. J Biol Chem 1989;264:10487-10492. (Pubitemid 19161613)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.18 , pp. 10487-10492
    • Nguyen, V.T.1    Morange, M.2    Bensaude, O.3
  • 18
    • 0025740514 scopus 로고
    • Denaturation of proteins during heat shock - In vivo recovery of solubility and activity of reporter enzymes
    • Pinto M, Morange M, Bensaude O: Denaturation of proteins during heat shock. In vivo recovery of solubility and activity of reporter enzymes. J Biol Chem 1991;266:13941-13946. (Pubitemid 21907444)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.21 , pp. 13941-13946
    • Pinto, M.1    Morange, M.2    Bensaude, O.3
  • 19
    • 0025883203 scopus 로고
    • Heat-shock-induced denaturation of proteins: Characterization of the insolubilization of the interferon-induced p68 kinase
    • Dubois MF, Hovanessian AG, Bensaude O: Heat-shock-induced denaturation of proteins. Characterization of the insolubilization of the interferon-induced p68 kinase. J Biol Chem 1991;266:9707-9711. (Pubitemid 21906714)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.15 , pp. 9707-9711
    • Dubois, M.F.1    Hovanessian, A.G.2    Bensaude, O.3
  • 21
    • 0031432208 scopus 로고    scopus 로고
    • Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo
    • DOI 10.1105/tpc.9.12.2171
    • Forreiter C, Kirschner M, Nover L: Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo. Plant Cell 1997;9:2171-2181. (Pubitemid 28174054)
    • (1997) Plant Cell , vol.9 , Issue.12 , pp. 2171-2181
    • Forreiter, C.1    Kirschner, M.2    Nover, L.3
  • 22
    • 0033618871 scopus 로고    scopus 로고
    • The effect of temperature and protein synthesis on the renaturation of firefly luciferase in intact H9c2 cells
    • DOI 10.1007/s000180050386
    • Souren JE, Wiegant FA, van Hof P, van Aken JM, van Wijk R: The effect of temperature and protein synthesis on the renaturation of firefly luciferase in intact H9c2 cells. Cell Mol Life Sci 1999;55:1473-1481. (Pubitemid 29427946)
    • (1999) Cellular and Molecular Life Sciences , vol.55 , Issue.11 , pp. 1473-1481
    • Souren, J.E.M.1    Wiegant, F.A.C.2    Van Hof, P.3    Van Aken, J.M.4    Van Wijk, R.5
  • 23
    • 0033061601 scopus 로고    scopus 로고
    • The role of hsp70 in protection and repair of luciferase activity in vivo experimental data and mathematical modelling
    • DOI 10.1007/s000180050333
    • Souren JE, Wiegant FA, Van Wijk R: The role of hsp70 in protection and repair of luciferase activity in vivo; experimental data and mathematical modelling. Cell Mol Life Sci 1999;55:799-811. (Pubitemid 29257628)
    • (1999) Cellular and Molecular Life Sciences , vol.55 , Issue.5 , pp. 799-811
    • Souren, J.E.M.1    Wiegant, F.A.C.2    Van Wijk, R.3
  • 24
    • 33846666927 scopus 로고    scopus 로고
    • High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase
    • DOI 10.1016/j.bmc.2007.01.004, PII S0968089607000065
    • Galam L, Hadden MK, Ma Z, et al.: High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase. Bioorg Med Chem 2007;15:1939-1946. (Pubitemid 46188404)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.5 , pp. 1939-1946
    • Galam, L.1    Hadden, M.K.2    Ma, Z.3    Ye, Q.-Z.4    Yun, B.-G.5    Blagg, B.S.J.6    Matts, R.L.7
  • 25
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • DOI 10.1038/nature01913
    • Kamal A, Thao L, Sensintaffar J, et al.: A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003;425: 407-410. (Pubitemid 37187270)
    • (2003) Nature , vol.425 , Issue.6956 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6    Burrows, F.J.7
  • 26
    • 80054851888 scopus 로고    scopus 로고
    • Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90
    • Moulick K, Ahn JH, Zong H, et al.: Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90. Nat Chem Biol 2011; 7:818-826.
    • (2011) Nat Chem Biol , vol.7 , pp. 818-826
    • Moulick, K.1    Ahn, J.H.2    Zong, H.3
  • 29
    • 66449094961 scopus 로고    scopus 로고
    • BIIB021, an orally available, fully synthetic small-molecule inhibitor of the heat shock protein Hsp90
    • Lundgren K, Zhang H, Brekken J, et al.: BIIB021, an orally available, fully synthetic small-molecule inhibitor of the heat shock protein Hsp90. Mol Can Ther 2009;8:921-929.
    • (2009) Mol Can Ther , vol.8 , pp. 921-929
    • Lundgren, K.1    Zhang, H.2    Brekken, J.3
  • 32
    • 80053997701 scopus 로고    scopus 로고
    • A novel C-terminal HSP90 inhibitor KU135 induces apoptosis and cell cycle arrest in melanoma cells
    • Samadi AK, Zhang X, Mukerji R, et al.: A novel C-terminal HSP90 inhibitor KU135 induces apoptosis and cell cycle arrest in melanoma cells. Cancer Lett 2011;312:158-167.
    • (2011) Cancer Lett , vol.312 , pp. 158-167
    • Samadi, A.K.1    Zhang, X.2    Mukerji, R.3
  • 34
    • 41649098631 scopus 로고    scopus 로고
    • Dicoumarol down-regulates human PTTG1/Securin mRNA expression through inhibition of Hsp90
    • DOI 10.1158/1535-7163.MCT-07-0457
    • Hernandez A, Lopez-Lluch G, Bernal JA, Navas P, Pintor-Toro JA: Dicoumarol down-regulates human PTTG1/Securin mRNA expression through inhibition of Hsp90. Mol Can Ther 2008;7:474-482. (Pubitemid 351482130)
    • (2008) Molecular Cancer Therapeutics , vol.7 , Issue.3 , pp. 474-482
    • Hernandez, A.1    Lopez-Lluch, G.2    Bernal, J.A.3    Navas, P.4    Pintor-Toro, J.A.5
  • 36
    • 0035002490 scopus 로고    scopus 로고
    • Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding
    • DOI 10.1046/j.1432-1327.2001.02145.x
    • Minami M, Nakamura M, Emori Y, Minami Y: Both the N-and C-terminal chaperone sites of Hsp90 participate in protein refolding. Eur J Biochem 2001;268:2520-2524. (Pubitemid 32417781)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.8 , pp. 2520-2524
    • Minami, M.1    Nakamura, M.2    Emori, Y.3    Minami, Y.4
  • 37
    • 80053371954 scopus 로고    scopus 로고
    • Firefly luciferase mutants as sensors of proteome stress
    • Gupta R, Kasturi P, Bracher A, et al.: Firefly luciferase mutants as sensors of proteome stress. Nat Methods 2011;8:879-884.
    • (2011) Nat Methods , vol.8 , pp. 879-884
    • Gupta, R.1    Kasturi, P.2    Bracher, A.3


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