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Volumn 6, Issue 4, 2007, Pages 1198-1211

Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 3,4 DIARYLPYRAZOLE RESORCINOL; ADENOSINE TRIPHOSPHATASE; AMIDE; B RAF KINASE; CCT 018159; CT 018159; GLYCOPROTEIN P; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 72; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; ISOXAZOLE DERIVATIVE; PROTEIN ARGININE METHYLTRANSFERASE; PYRAZOLE DERIVATIVE; RADICICOL; RAF PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); RESORCINOL DERIVATIVE; SURVIVIN; UNCLASSIFIED DRUG; VER 49009; VER 50589;

EID: 34248166042     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-07-0149     Document Type: Article
Times cited : (143)

References (60)
  • 1
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney A, Workman P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2002;2:3-24.
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 2
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005;5:761-72.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 3
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000;100: 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 4
    • 1542298267 scopus 로고    scopus 로고
    • Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone
    • Workman P. Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone. Cancer Lett 2004;206: 149-57.
    • (2004) Cancer Lett , vol.206 , pp. 149-157
    • Workman, P.1
  • 5
    • 28244444919 scopus 로고    scopus 로고
    • Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino-17-demethoxygeldanamycin
    • da Rocha DS, Friedlos F, Light Y, et al. Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino-17-demethoxygeldanamycin. Cancer Res 2005;65:10686-91.
    • (2005) Cancer Res , vol.65 , pp. 10686-10691
    • da Rocha, D.S.1    Friedlos, F.2    Light, Y.3
  • 6
    • 30444441778 scopus 로고    scopus 로고
    • V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors
    • Grbovic OM, Basso AD, Sawai A, et al. V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors. Proc Natl Acad Sci U S A 2006;103:57-62.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 57-62
    • Grbovic, O.M.1    Basso, A.D.2    Sawai, A.3
  • 7
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A, Thao L, Sensintaffar J, et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003;425: 407-10.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 9
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B, Prodromou C, Roe SM, et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J 1998;17:4829-36.
    • (1998) EMBO J , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3
  • 10
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte TW, An WG, Neckers LM. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem Biophys Res Commun 1997;239:655-9.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 11
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell P, Ballinger CA, Jiang J, et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol 2001;3:93-6.
    • (2001) Nat Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3
  • 13
    • 0036836678 scopus 로고    scopus 로고
    • Halohydrin and oxime derivatives of radicicol: Synthesis and antitumor activities
    • Agatsuma T, Ogawa H, Akasaka K, et al. Halohydrin and oxime derivatives of radicicol: synthesis and antitumor activities. Bioorg Med Chem 2002;10:3445-54.
    • (2002) Bioorg Med Chem , vol.10 , pp. 3445-3454
    • Agatsuma, T.1    Ogawa, H.2    Akasaka, K.3
  • 14
    • 0036139023 scopus 로고    scopus 로고
    • Pharmacokinetics, tissue distribution, and metabolism of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (NSC 707545) in CD2F1 mice and Fischer 344 rats
    • Egorin MJ, Lagattuta TF, Hamburger DR, et al. Pharmacokinetics, tissue distribution, and metabolism of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (NSC 707545) in CD2F1 mice and Fischer 344 rats. Cancer Chemother Pharmacol 2002;49:7-19.
    • (2002) Cancer Chemother Pharmacol , vol.49 , pp. 7-19
    • Egorin, M.J.1    Lagattuta, T.F.2    Hamburger, D.R.3
  • 15
    • 0033579175 scopus 로고    scopus 로고
    • DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland LR, Sharp SY, Rogers PM, Myers TG, Workman P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J Natl Cancer Inst 1999;91:1940-9.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 16
    • 27544446054 scopus 로고    scopus 로고
    • Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: Role of 17-AAG hydroquinone in heat shock protein 90 inhibition
    • Guo W, Reigan P, Siegel D, et al. Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res 2005;65:10006-15.
    • (2005) Cancer Res , vol.65 , pp. 10006-10015
    • Guo, W.1    Reigan, P.2    Siegel, D.3
  • 18
    • 33751258297 scopus 로고    scopus 로고
    • Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90
    • Sydor JR, Normant E, Pien CS, et al. Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90. Proc Natl Acad Sci U S A 2006;103:17408-13.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17408-17413
    • Sydor, J.R.1    Normant, E.2    Pien, C.S.3
  • 20
    • 33746191768 scopus 로고    scopus 로고
    • Inhibitors of the HSP90 molecular chaperone: Current status
    • Sharp S, Workman P. Inhibitors of the HSP90 molecular chaperone: current status. Adv Cancer Res 2006;95:323-48.
    • (2006) Adv Cancer Res , vol.95 , pp. 323-348
    • Sharp, S.1    Workman, P.2
  • 21
    • 28144440479 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors. A text book example of medicinal chemistry?
    • Janin YL. Heat shock protein 90 inhibitors. A text book example of medicinal chemistry? J Med Chem 2005;48:7503-12.
    • (2005) J Med Chem , vol.48 , pp. 7503-7512
    • Janin, Y.L.1
  • 23
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe SM, Prodromou C, O'Brien R, et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 1999;42:260-6.
    • (1999) J Med Chem , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3
  • 24
    • 33746365169 scopus 로고    scopus 로고
    • Discovery and development of purine-scaffold Hsp90 inhibitors
    • Chiosis G. Discovery and development of purine-scaffold Hsp90 inhibitors. Curr Top Med Chem 2006;6:1183-91.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1183-1191
    • Chiosis, G.1
  • 25
    • 33745174538 scopus 로고    scopus 로고
    • Heat shock protein-90 inhibitors: A chronicle from geldanamycin to today's agents
    • Chiosis G, Caldas LE, Solit D. Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today's agents. Curr Opin Investig Drugs 2006;7:534-41.
    • (2006) Curr Opin Investig Drugs , vol.7 , pp. 534-541
    • Chiosis, G.1    Caldas, L.E.2    Solit, D.3
  • 26
    • 20644448390 scopus 로고    scopus 로고
    • The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors
    • Cheung KM, Matthews TP, James K, et al. The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg Med Chem Lett 2005;15:3338-43.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 3338-3343
    • Cheung, K.M.1    Matthews, T.P.2    James, K.3
  • 27
    • 33947210121 scopus 로고    scopus 로고
    • In vitro biological characterization of a novel, synthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors
    • Sharp SY, Boxall K, Rowlands M, et al. In vitro biological characterization of a novel, synthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors. Cancer Res 2007;67: 2206-16.
    • (2007) Cancer Res , vol.67 , pp. 2206-2216
    • Sharp, S.Y.1    Boxall, K.2    Rowlands, M.3
  • 28
    • 33746040516 scopus 로고    scopus 로고
    • Preclinical pharmacokinetics and metabolism of a novel diaryl pyrazole resorcinol series of heat shock protein 90 inhibitors
    • Smith NF, Hayes A, James K, et al. Preclinical pharmacokinetics and metabolism of a novel diaryl pyrazole resorcinol series of heat shock protein 90 inhibitors. Mol Cancer Ther 2006;6:1628-37.
    • (2006) Mol Cancer Ther , vol.6 , pp. 1628-1637
    • Smith, N.F.1    Hayes, A.2    James, K.3
  • 29
    • 21244505104 scopus 로고    scopus 로고
    • Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design
    • Dymock BW, Barril X, Brough PA, et al. Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design. J Med Chem 2005;48:4212-5.
    • (2005) J Med Chem , vol.48 , pp. 4212-4215
    • Dymock, B.W.1    Barril, X.2    Brough, P.A.3
  • 30
    • 80053302479 scopus 로고    scopus 로고
    • Isoxazole compounds as inhibitors of heat shock proteins.
    • Eur. Pat. Off. No. WO 2004/ 072051 A1
    • Drysdale M, Dymock B, Finch H, et al. Isoxazole compounds as inhibitors of heat shock proteins. 2004; pp. 1-180. [Eur. Pat. Off. No. WO 2004/ 072051 A1].
    • (2004) , pp. 1-180
    • Drysdale, M.1    Dymock, B.2    Finch, H.3
  • 31
    • 3042637928 scopus 로고    scopus 로고
    • Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms
    • Wright L, Barril X, Dymock B, et al. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem Biol 2004;11: 775-85.
    • (2004) Chem Biol , vol.11 , pp. 775-785
    • Wright, L.1    Barril, X.2    Dymock, B.3
  • 32
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1
    • Panaretou B, Siligardi G, Meyer P, et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 2002;10:1307-18.
    • (2002) Mol Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1    Siligardi, G.2    Meyer, P.3
  • 33
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
    • Rowlands MG, Newbatt YM, Prodromou C, et al. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem 2004;327:176-83.
    • (2004) Anal Biochem , vol.327 , pp. 176-183
    • Rowlands, M.G.1    Newbatt, Y.M.2    Prodromou, C.3
  • 34
    • 33644665083 scopus 로고    scopus 로고
    • A fluorescence polarization assay for inhibitors of Hsp90
    • Howes R, Barril X, Dymock BW, et al. A fluorescence polarization assay for inhibitors of Hsp90. Anal Biochem 2006;350:202-13.
    • (2006) Anal Biochem , vol.350 , pp. 202-213
    • Howes, R.1    Barril, X.2    Dymock, B.W.3
  • 35
    • 33645470397 scopus 로고    scopus 로고
    • Benzoquinone ansamycin heat shock protein 90 inhibitors modulate multiple functions required for tumor angiogenesis
    • Sanderson S, Valenti M, Gowan S, et al. Benzoquinone ansamycin heat shock protein 90 inhibitors modulate multiple functions required for tumor angiogenesis. Mol Cancer Ther 2006;5:522-32.
    • (2006) Mol Cancer Ther , vol.5 , pp. 522-532
    • Sanderson, S.1    Valenti, M.2    Gowan, S.3
  • 36
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein I, Robertson D, DiStefano F, Workman P, Clarke PA. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res 2001;61: 4003-9.
    • (2001) Cancer Res , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3    Workman, P.4    Clarke, P.A.5
  • 37
    • 16744368637 scopus 로고    scopus 로고
    • United Kingdom Co-ordinating Committee on Cancer Research guidelines for the welfare of animals in experimental neoplasia
    • 2nd ed
    • Workman P, Twentyman P, Balkwill F, et al. United Kingdom Co-ordinating Committee on Cancer Research guidelines for the welfare of animals in experimental neoplasia. 2nd ed. Br J Cancer 1998;77:1-10.
    • (1998) Br J Cancer , vol.77 , pp. 1-10
    • Workman, P.1    Twentyman, P.2    Balkwill, F.3
  • 38
    • 27644591251 scopus 로고    scopus 로고
    • In vitro and in vivo pharmacokinetic-pharmacodynamic relationships for the trisubstituted aminopurine cyclin-dependent kinase inhibitors olomoucine, bohemine and CYC202
    • Raynaud FI, Whittaker SR, Fischer PM, et al. In vitro and in vivo pharmacokinetic-pharmacodynamic relationships for the trisubstituted aminopurine cyclin-dependent kinase inhibitors olomoucine, bohemine and CYC202. Clin Cancer Res 2005;11:4875-87.
    • (2005) Clin Cancer Res , vol.11 , pp. 4875-4887
    • Raynaud, F.I.1    Whittaker, S.R.2    Fischer, P.M.3
  • 39
    • 0027942213 scopus 로고
    • Regression of established breast carcinoma xenografts with antibody-directed enzyme prodrug therapy against c-erbB2 p185
    • Eccles SA, Court WJ, Box GA, et al. Regression of established breast carcinoma xenografts with antibody-directed enzyme prodrug therapy against c-erbB2 p185. Cancer Res 1994;54:5171-7.
    • (1994) Cancer Res , vol.54 , pp. 5171-5177
    • Eccles, S.A.1    Court, W.J.2    Box, G.A.3
  • 40
    • 0141482154 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: Implications for ascites formation
    • Belotti D, Paganoni P, Manenti L, et al. Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation. Cancer Res 2003;63:5224-9.
    • (2003) Cancer Res , vol.63 , pp. 5224-5229
    • Belotti, D.1    Paganoni, P.2    Manenti, L.3
  • 41
    • 23144445834 scopus 로고    scopus 로고
    • Solid-phase immunoassays in mechanism-based drug discovery: Their application in the development of inhibitors of the molecular chaperone heat-shock protein 90
    • Hardcastle A, Boxall K, Richards J, et al. Solid-phase immunoassays in mechanism-based drug discovery: their application in the development of inhibitors of the molecular chaperone heat-shock protein 90. Assay Drug Dev Technol 2005;3:273-85.
    • (2005) Assay Drug Dev Technol , vol.3 , pp. 273-285
    • Hardcastle, A.1    Boxall, K.2    Richards, J.3
  • 42
    • 0022474105 scopus 로고
    • Studies on the in vivo disposition of Adriamycin in human tumours which exhibit different responses to the drug
    • Cummings J, McArdle CS. Studies on the in vivo disposition of Adriamycin in human tumours which exhibit different responses to the drug. Br J Cancer 1986;53:835-8.
    • (1986) Br J Cancer , vol.53 , pp. 835-838
    • Cummings, J.1    McArdle, C.S.2
  • 43
    • 0033785989 scopus 로고    scopus 로고
    • Establishment of an isogenic human colon tumor model for NQ01 gene expression: Application to investigate the role of DT-diaphorase in bioreductive drug activation in vitro and in vivo
    • Sharp SY, Kelland LR, Valenti MR, et al. Establishment of an isogenic human colon tumor model for NQ01 gene expression: application to investigate the role of DT-diaphorase in bioreductive drug activation in vitro and in vivo. Mol Pharmacol 2000;58:1146-55.
    • (2000) Mol Pharmacol , vol.58 , pp. 1146-1155
    • Sharp, S.Y.1    Kelland, L.R.2    Valenti, M.R.3
  • 44
    • 0028001292 scopus 로고
    • Effects of a new antioestrogen, idoxifene, on cisplatin- and doxorubicin-sensitive and - resistant human ovarian carcinoma cell lines
    • Sharp SY, Rowlands MG, Jarman M, Kelland LR. Effects of a new antioestrogen, idoxifene, on cisplatin- and doxorubicin-sensitive and - resistant human ovarian carcinoma cell lines. Br J Cancer 1994;70:409-14.
    • (1994) Br J Cancer , vol.70 , pp. 409-414
    • Sharp, S.Y.1    Rowlands, M.G.2    Jarman, M.3    Kelland, L.R.4
  • 45
    • 0036849436 scopus 로고    scopus 로고
    • Retention of activity by the new generation platinum agent AMD0473 in four human tumour cell lines possessing acquired resistance to oxaliplatin
    • Sharp SY, O'Neill CF, Rogers P, Boxall FE, Kelland LR. Retention of activity by the new generation platinum agent AMD0473 in four human tumour cell lines possessing acquired resistance to oxaliplatin. Eur J Cancer 2002;38:2309-15.
    • (2002) Eur J Cancer , vol.38 , pp. 2309-2315
    • Sharp, S.Y.1    O'Neill, C.F.2    Rogers, P.3    Boxall, F.E.4    Kelland, L.R.5
  • 46
    • 23044441106 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies
    • Banerji U, O'Donnell A, Scurr M, et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 2005;23:4152-61.
    • (2005) J Clin Oncol , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 48
    • 0034886833 scopus 로고    scopus 로고
    • Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: Sequence and tumor biology matters
    • See
    • See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters. Clin Cancer Res 2001;7:2155-8, 2228-36.
    • (2001) Clin Cancer Res , vol.7
    • Sausville, E.A.1
  • 49
    • 0023057847 scopus 로고
    • Sequence and organization of genes encoding the human 27 kDa heat shock protein
    • Hickey E, Brandon SE, Potter R, et al. Sequence and organization of genes encoding the human 27 kDa heat shock protein. Nucleic Acids Res 1986;14:4127-45.
    • (1986) Nucleic Acids Res , vol.14 , pp. 4127-4145
    • Hickey, E.1    Brandon, S.E.2    Potter, R.3
  • 50
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C, Morimoto RI. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst 2000;92: 1564-72.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 51
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S, Fujita N, Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci U S A 2000;97:10832-7.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 52
    • 31144453233 scopus 로고    scopus 로고
    • BRAF mutation predicts sensitivity to MEK inhibition
    • Solit DB, Garraway LA, Pratilas CA, et al. BRAF mutation predicts sensitivity to MEK inhibition. Nature 2006;439:358-62.
    • (2006) Nature , vol.439 , pp. 358-362
    • Solit, D.B.1    Garraway, L.A.2    Pratilas, C.A.3
  • 53
    • 34147150867 scopus 로고    scopus 로고
    • Gene and protein expression profiling of human ovarian cancer cells treated with the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG)
    • Maloney A, Clarke P, Naaby-Hansen S, et al. Gene and protein expression profiling of human ovarian cancer cells treated with the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG). Cancer Res 2007;67:3239-53.
    • (2007) Cancer Res , vol.67 , pp. 3239-3253
    • Maloney, A.1    Clarke, P.2    Naaby-Hansen, S.3
  • 54
    • 0032585545 scopus 로고    scopus 로고
    • Evaluation of dynamic polar molecular surface area as predictor of drug absorption: Comparison with other computational and experimental predictors
    • Palm K, Luthman K, Ungell AL, et al. Evaluation of dynamic polar molecular surface area as predictor of drug absorption: comparison with other computational and experimental predictors. J Med Chem 1998;41: 5382-92.
    • (1998) J Med Chem , vol.41 , pp. 5382-5392
    • Palm, K.1    Luthman, K.2    Ungell, A.L.3
  • 55
    • 34248166884 scopus 로고    scopus 로고
    • Phase I trial of KOS-953, a heat shock protein 90 inhibitor, and trastuzumab (T)
    • Modi S, Stopeck A, Gordon MS, et al. Phase I trial of KOS-953, a heat shock protein 90 inhibitor, and trastuzumab (T). J Clin Oncol (Meeting Abstracts) 2006;24:501.
    • (2006) J Clin Oncol (Meeting Abstracts) , vol.24 , pp. 501
    • Modi, S.1    Stopeck, A.2    Gordon, M.S.3
  • 56
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998; 42:273-9.
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 57
    • 0033890818 scopus 로고    scopus 로고
    • Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents
    • Bagatell R, Paine-Murrieta GD, Taylor CW, et al. Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents. Clin Cancer Res 2000;6:3312-8.
    • (2000) Clin Cancer Res , vol.6 , pp. 3312-3318
    • Bagatell, R.1    Paine-Murrieta, G.D.2    Taylor, C.W.3
  • 59
    • 33644871349 scopus 로고    scopus 로고
    • Silencing of survivin gene by small interfering RNAs produces supra-additive growth suppression in combination with 17-allylamino-17-demethoxygeldanamycin in human prostate cancer cells
    • Paduano F, Villa R, Pennati M, et al. Silencing of survivin gene by small interfering RNAs produces supra-additive growth suppression in combination with 17-allylamino-17-demethoxygeldanamycin in human prostate cancer cells. Mol Cancer Ther 2006;5:179-86.
    • (2006) Mol Cancer Ther , vol.5 , pp. 179-186
    • Paduano, F.1    Villa, R.2    Pennati, M.3
  • 60
    • 6344222803 scopus 로고    scopus 로고
    • Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S. Human SWI/ SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol 2004;24:9630-45.
    • Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S. Human SWI/ SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol 2004;24:9630-45.


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