메뉴 건너뛰기




Volumn 12, Issue 9, 2012, Pages 1108-1124

Inhibiting HSP90 to treat cancer: A strategy in evolution

Author keywords

Cancer evolution; Clinical trial; Combination chemotherapy; Drug resistance

Indexed keywords

5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; ALVESPIMYCIN; ANTINEOPLASTIC AGENT; AT 13387; BLLB 021; BORTEZOMIB; BRCA1 PROTEIN; CAPECITABINE; CETUXIMAB; CHECKPOINT KINASE 1; CISPLATIN; CYTARABINE; DOCETAXEL; DS 2248; ERLOTINIB; ETOPOSIDE; GANETESPIB; GELDANAMYCIN; GEMCITABINE; HEAT SHOCK PROTEIN 90 INHIBITOR; IMATINIB; IRINOTECAN; KW 2478; MPC 3100; PU HH71; RETASPIMYCIN; TANESPIMYCIN; TRASTUZUMAB; UNCLASSIFIED DRUG; VORINOSTAT; XL 888;

EID: 84867796642     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/156652412803306657     Document Type: Article
Times cited : (55)

References (152)
  • 1
    • 79955515280 scopus 로고    scopus 로고
    • Resistance to HER2-directed antibodies and tyrosine kinase inhibitors: Mechanisms and clinical implications
    • Garrett JT, Arteaga CL. Resistance to HER2-directed antibodies and tyrosine kinase inhibitors: mechanisms and clinical implications. Cancer Biol Ther 2011; 11: 793-800.
    • (2011) Cancer Biol Ther , vol.11 , pp. 793-800
    • Garrett, J.T.1    Arteaga, C.L.2
  • 2
    • 80054029556 scopus 로고    scopus 로고
    • Recent developments in drug resistance mechanism in chronic myeloid leukemia: A review
    • Vaidya S, Ghosh K, Vundinti BR. Recent developments in drug resistance mechanism in chronic myeloid leukemia: A review. Eur J Haematol 2011; 87: 381-93.
    • (2011) Eur J Haematol , vol.87 , pp. 381-393
    • Vaidya, S.1    Ghosh, K.2    Vundinti, B.R.3
  • 3
    • 73349096261 scopus 로고    scopus 로고
    • Resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer
    • Hammerman PS, Janne PA, Johnson BE. Resistance to epidermal growth factor receptor tyrosine kinase inhibitors in non-small cell lung cancer. Clin Cancer Res 2009; 15: 7502-9.
    • (2009) Clin Cancer Res , vol.15 , pp. 7502-7509
    • Hammerman, P.S.1    Janne, P.A.2    Johnson, B.E.3
  • 4
    • 79953118839 scopus 로고    scopus 로고
    • Genotypic and histological evolution of lung cancers acquiring resistance to EGFR inhibitors
    • Sequist LV, Waltman BA, Dias-Santagata D, et al. Genotypic and histological evolution of lung cancers acquiring resistance to EGFR inhibitors. Sci Transl Med 2011; 3: 75ra26.
    • (2011) Sci Transl Med , vol.3
    • Sequist, L.V.1    Waltman, B.A.2    Dias-Santagata, D.3
  • 6
    • 78149452881 scopus 로고    scopus 로고
    • Protein homeostasis and the phenotypic manifestation of genetic diversity: Principles and mechanisms
    • Jarosz DF, Taipale M, Lindquist S. Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annu Rev Genet 2010; 44: 189-216.
    • (2010) Annu Rev Genet , vol.44 , pp. 189-216
    • Jarosz, D.F.1    Taipale, M.2    Lindquist, S.3
  • 7
    • 0034546905 scopus 로고    scopus 로고
    • From genotype to phenotype: Buffering mechanisms and the storage of genetic information
    • Rutherford SL. From genotype to phenotype: buffering mechanisms and the storage of genetic information. Bioessays 2000; 22: 1095-105.
    • (2000) Bioessays , vol.22 , pp. 1095-1105
    • Rutherford, S.L.1
  • 8
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: Causes, effects and implications of Hsp90-mediated genetic capacitance
    • Sangster TA, Lindquist S, Queitsch C. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays 2004; 26: 348-62.
    • (2004) Bioessays , vol.26 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 9
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 2010; 11: 515-28.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 10
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition
    • Taipale M, Krykbaeva I, Koeva M, et al. Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition. Cell 2012; 150: 987-1001.
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1    Krykbaeva, I.2    Koeva, M.3
  • 11
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • Dutta R, Inouye M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem Sci 2000; 25: 24-8.
    • (2000) Trends Biochem Sci , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 12
    • 35348890981 scopus 로고    scopus 로고
    • Drugging the cancer chaperone HSP90: Combinatorial therapeutic exploitation of oncogene addiction and tumor stress
    • Workman P, Burrows F, Neckers L, Rosen N. Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann N Y Acad Sci 2007; 1113: 202-16.
    • (2007) Ann N Y Acad Sci , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 13
    • 33749335282 scopus 로고    scopus 로고
    • The Connectivity Map: Using gene-expression signatures to connect small molecules, genes, and disease
    • Lamb J, Crawford ED, Peck D, et al. The Connectivity Map: using gene-expression signatures to connect small molecules, genes, and disease. Science 2006; 313: 1929-35.
    • (2006) Science , vol.313 , pp. 1929-1935
    • Lamb, J.1    Crawford, E.D.2    Peck, D.3
  • 14
    • 54249085844 scopus 로고    scopus 로고
    • Chemical biology and the limits of reductionism
    • Peterson RT. Chemical biology and the limits of reductionism. Nat Chem Biol 2008; 4: 635-8.
    • (2008) Nat Chem Biol , vol.4 , pp. 635-638
    • Peterson, R.T.1
  • 15
    • 17844383964 scopus 로고    scopus 로고
    • Perturbational profiling of a cell-line model of tumorigenesis by using metabolic measurements
    • Ramanathan A, Wang C, Schreiber SL. Perturbational profiling of a cell-line model of tumorigenesis by using metabolic measurements. Proc Natl Acad Sci USA 2005; 102: 5992-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5992-5997
    • Ramanathan, A.1    Wang, C.2    Schreiber, S.L.3
  • 16
    • 58849115076 scopus 로고    scopus 로고
    • 90-kDa heat shock protein inhibition abrogates the topoisomerase I poison-induced G2/M checkpoint in p53-null tumor cells by depleting Chk1 and Wee1
    • Tse AN, Sheikh TN, Alan H, Chou TC, Schwartz GK. 90-kDa heat shock protein inhibition abrogates the topoisomerase I poison-induced G2/M checkpoint in p53-null tumor cells by depleting Chk1 and Wee1. Mol Pharmacol 2009; 75: 124-33.
    • (2009) Mol Pharmacol , vol.75 , pp. 124-133
    • Tse, A.N.1    Sheikh, T.N.2    Alan, H.3    Chou, T.C.4    Schwartz, G.K.5
  • 17
    • 58149180924 scopus 로고    scopus 로고
    • A phase 1 doseescalation study of irinotecan in combination with 17- allylamino-17-demethoxygeldanamycin in patients with solid tumors
    • Tse AN, Klimstra DS, Gonen M, et al. A phase 1 doseescalation study of irinotecan in combination with 17- allylamino-17-demethoxygeldanamycin in patients with solid tumors. Clin Cancer Res 2008; 14: 6704-11.
    • (2008) Clin Cancer Res , vol.14 , pp. 6704-6711
    • Tse, A.N.1    Klimstra, D.S.2    Gonen, M.3
  • 18
    • 34547689351 scopus 로고    scopus 로고
    • Inhibition of Hsp90: A multitarget approach to radiosensitization
    • Camphausen K, Tofilon PJ. Inhibition of Hsp90: a multitarget approach to radiosensitization. Clin Cancer Res 2007; 13: 4326-30.
    • (2007) Clin Cancer Res , vol.13 , pp. 4326-4330
    • Camphausen, K.1    Tofilon, P.J.2
  • 19
    • 33644867410 scopus 로고    scopus 로고
    • Inhibition of Hsp90 acts synergistically with topoisomerase II poisons to increase the apoptotic killing of cells due to an increase in topoisomerase II mediated DNA damage
    • Barker CR, McNamara AV, Rackstraw SA, et al. Inhibition of Hsp90 acts synergistically with topoisomerase II poisons to increase the apoptotic killing of cells due to an increase in topoisomerase II mediated DNA damage. Nucleic Acids Res 2006; 34: 1148-57.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1148-1157
    • Barker, C.R.1    McNamara, A.V.2    Rackstraw, S.A.3
  • 20
    • 0036510547 scopus 로고    scopus 로고
    • Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket
    • Soti C, Racz A, Csermely P. A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket. J Biol Chem 2002; 277: 7066-75.
    • (2002) J Biol Chem , vol.277 , pp. 7066-7075
    • Soti, C.1    Racz, A.2    Csermely, P.A.3
  • 21
    • 10344225631 scopus 로고    scopus 로고
    • Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin
    • Bagatell R, Beliakoff J, David CL, Marron MT, Whitesell L. Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin. Int J Cancer 2005; 113: 179-88.
    • (2005) Int J Cancer , vol.113 , pp. 179-188
    • Bagatell, R.1    Beliakoff, J.2    David, C.L.3    Marron, M.T.4    Whitesell, L.5
  • 23
    • 74849095191 scopus 로고    scopus 로고
    • Drugging the heat shock factor 1 pathway: Exploitation of the critical cancer cell dependence on the guardian of the proteome
    • de Billy E, Powers MV, Smith JR, Workman P. Drugging the heat shock factor 1 pathway: exploitation of the critical cancer cell dependence on the guardian of the proteome. Cell Cycle 2009; 8: 3806-8.
    • (2009) Cell Cycle , vol.8 , pp. 3806-3808
    • de Billy, E.1    Powers, M.V.2    Smith, J.R.3    Workman, P.4
  • 24
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis
    • Powers MV, Clarke PA, Workman P. Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis. Cancer Cell 2008; 14: 250-62.
    • (2008) Cancer Cell , vol.14 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 25
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • Leu JI, Pimkina J, Frank A, Murphy ME, George DL. A small molecule inhibitor of inducible heat shock protein 70. Mol Cell 2009; 36: 15-27.
    • (2009) Mol Cell , vol.36 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 26
  • 27
    • 64349121987 scopus 로고    scopus 로고
    • Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design
    • Williamson DS, Borgognoni J, Clay A, et al. Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design. J Med Chem 2009; 52: 1510-3.
    • (2009) J Med Chem , vol.52 , pp. 1510-1513
    • Williamson, D.S.1    Borgognoni, J.2    Clay, A.3
  • 28
    • 53349101499 scopus 로고    scopus 로고
    • Mitotic catastrophe cell death induced by heat shock protein 90 inhibitor in BRCA1-deficient breast cancer cell lines
    • Zajac M, Moneo MV, Carnero A, Benitez J, Martinez-Delgado B. Mitotic catastrophe cell death induced by heat shock protein 90 inhibitor in BRCA1-deficient breast cancer cell lines. Mol Cancer Ther 2008; 7: 2358-66.
    • (2008) Mol Cancer Ther , vol.7 , pp. 2358-2366
    • Zajac, M.1    Moneo, M.V.2    Carnero, A.3    Benitez, J.4    Martinez-Delgado, B.5
  • 29
    • 0034890377 scopus 로고    scopus 로고
    • Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner
    • See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17- demethoxygeldanamycin: sequence and tumor biology matters, Clin. Cancer Res., 7: 2155-2158, 2001
    • Munster PN, Basso A, Solit D, Norton L, Rosen N. Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner. See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17- demethoxygeldanamycin: sequence and tumor biology matters, Clin. Cancer Res., 7: 2155-2158, 2001. Clin Cancer Res 2001; 7: 2228-36.
    • (2001) Clin Cancer Res , vol.7 , pp. 2228-2236
    • Munster, P.N.1    Basso, A.2    Solit, D.3    Norton, L.4    Rosen, N.5
  • 30
    • 0034653849 scopus 로고    scopus 로고
    • Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates
    • Lange BM, Bachi A, Wilm M, Gonzalez C. Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates. EMBO J 2000; 19: 1252-62.
    • (2000) EMBO J , vol.19 , pp. 1252-1262
    • Lange, B.M.1    Bachi, A.2    Wilm, M.3    Gonzalez, C.4
  • 31
    • 59649124272 scopus 로고    scopus 로고
    • Sgt1, a cochaperone of Hsp90 stabilizes Polo and is required for centrosome organization
    • Martins T, Maia AF, Steffensen S, Sunkel CE. Sgt1, a cochaperone of Hsp90 stabilizes Polo and is required for centrosome organization. EMBO J 2009; 28: 234-47.
    • (2009) EMBO J , vol.28 , pp. 234-247
    • Martins, T.1    Maia, A.F.2    Steffensen, S.3    Sunkel, C.E.4
  • 32
    • 33746045662 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, causes kinetochore defects: A novel mechanism by which 17-AAG inhibits cell proliferation
    • Niikura Y, Ohta S, Vandenbeldt KJ, Abdulle R, McEwen BF, Kitagawa K. 17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferation. Oncogene 2006; 25: 4133-46.
    • (2006) Oncogene , vol.25 , pp. 4133-4146
    • Niikura, Y.1    Ohta, S.2    Vandenbeldt, K.J.3    Abdulle, R.4    McEwen, B.F.5    Kitagawa, K.6
  • 33
    • 33748047460 scopus 로고    scopus 로고
    • Taxotere-induced inhibition of human endothelial cell migration is a result of heat shock protein 90 degradation
    • Murtagh J, Lu H, Schwartz EL. Taxotere-induced inhibition of human endothelial cell migration is a result of heat shock protein 90 degradation. Cancer Res 2006; 66: 8192-9.
    • (2006) Cancer Res , vol.66 , pp. 8192-8199
    • Murtagh, J.1    Lu, H.2    Schwartz, E.L.3
  • 34
    • 13944249382 scopus 로고    scopus 로고
    • Coupling apoptosis resistance to the cellular stress response: The IAP-Hsp90 connection in cancer
    • Altieri DC. Coupling apoptosis resistance to the cellular stress response: the IAP-Hsp90 connection in cancer. Cell Cycle 2004; 3: 255-6.
    • (2004) Cell Cycle , vol.3 , pp. 255-256
    • Altieri, D.C.1
  • 35
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 2002; 277: 39858-66.
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 36
    • 77955870224 scopus 로고    scopus 로고
    • 17-DMAG targets the nuclear factor-kappaB family of proteins to induce apoptosis in chronic lymphocytic leukemia: Clinical implications of HSP90 inhibition
    • Hertlein E, Wagner AJ, Jones J, et al. 17-DMAG targets the nuclear factor-kappaB family of proteins to induce apoptosis in chronic lymphocytic leukemia: clinical implications of HSP90 inhibition. Blood 2010; 116: 45-53.
    • (2010) Blood , vol.116 , pp. 45-53
    • Hertlein, E.1    Wagner, A.J.2    Jones, J.3
  • 37
    • 34447498813 scopus 로고    scopus 로고
    • Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer
    • Rodina A, Vilenchik M, Moulick K, et al. Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer. Nat Chem Biol 2007; 3: 498-507.
    • (2007) Nat Chem Biol , vol.3 , pp. 498-507
    • Rodina, A.1    Vilenchik, M.2    Moulick, K.3
  • 38
    • 79951997890 scopus 로고    scopus 로고
    • Loss of phosphatase and tensin homolog or phosphoinositol-3 kinase activation and response to trastuzumab or lapatinib in human epidermal growth factor receptor 2-overexpressing locally advanced breast cancers
    • Dave B, Migliaccio I, Gutierrez MC, et al. Loss of phosphatase and tensin homolog or phosphoinositol-3 kinase activation and response to trastuzumab or lapatinib in human epidermal growth factor receptor 2-overexpressing locally advanced breast cancers. J Clin Oncol 2011; 29: 166-73.
    • (2011) J Clin Oncol , vol.29 , pp. 166-173
    • Dave, B.1    Migliaccio, I.2    Gutierrez, M.C.3
  • 39
    • 79957523828 scopus 로고    scopus 로고
    • KRAS, BRAF, PIK3CA, and PTEN mutations: Implications for targeted therapies in metastatic colorectal cancer
    • De Roock W, De Vriendt V, Normanno N, Ciardiello F, Tejpar S. KRAS, BRAF, PIK3CA, and PTEN mutations: implications for targeted therapies in metastatic colorectal cancer. Lancet Oncol 2011; 12: 594-603.
    • (2011) Lancet Oncol , vol.12 , pp. 594-603
    • de Roock, W.1    de Vriendt, V.2    Normanno, N.3    Ciardiello, F.4    Tejpar, S.5
  • 40
    • 80051705351 scopus 로고    scopus 로고
    • Pharmacokineticpharmacodynamic modeling of biomarker response and tumor growth inhibition to an orally available heat shock protein 90 inhibitor in human tumor xenograft mouse model
    • Yamazaki S, Nguyen L, Vekich S, et al. Pharmacokineticpharmacodynamic modeling of biomarker response and tumor growth inhibition to an orally available heat shock protein 90 inhibitor in human tumor xenograft mouse model. J Pharmacol Exp Ther 2011; 338: 964-73.
    • (2011) J Pharmacol Exp Ther , vol.338 , pp. 964-973
    • Yamazaki, S.1    Nguyen, L.2    Vekich, S.3
  • 41
    • 79952791065 scopus 로고    scopus 로고
    • NCCN Task Force report: Tyrosine kinase inhibitor therapy selection in the management of patients with chronic myelogenous leukemia
    • O'Brien S, Berman E, Moore JO, et al. NCCN Task Force report: tyrosine kinase inhibitor therapy selection in the management of patients with chronic myelogenous leukemia. J Natl Compr Canc Netw 2011; 9 Suppl 2: S1-25.
    • (2011) J Natl Compr Canc Netw , vol.9 , Issue.2 SUPPL.
    • O'Brien, S.1    Berman, E.2    Moore, J.O.3
  • 42
    • 79953141616 scopus 로고    scopus 로고
    • Combining targeted drugs to stop resistant tumors
    • Kaiser J. Combining targeted drugs to stop resistant tumors. Science 2011; 331: 1542-5.
    • (2011) Science , vol.331 , pp. 1542-1545
    • Kaiser, J.1
  • 44
    • 79957958724 scopus 로고    scopus 로고
    • Recent developments in the third generation inhibitors of Bcr-Abl for overriding T315I mutation
    • Lu XY, Cai Q, Ding K. Recent developments in the third generation inhibitors of Bcr-Abl for overriding T315I mutation. Curr Med Chem 2011; 18: 2146-57.
    • (2011) Curr Med Chem , vol.18 , pp. 2146-2157
    • Lu, X.Y.1    Cai, Q.2    Ding, K.3
  • 45
    • 79951961755 scopus 로고    scopus 로고
    • Resistance to BRAF inhibition in melanomas
    • Solit DB, Rosen N. Resistance to BRAF inhibition in melanomas. N Engl J Med 2011; 364: 772-4.
    • (2011) N Engl J Med , vol.364 , pp. 772-774
    • Solit, D.B.1    Rosen, N.2
  • 46
    • 34547137932 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 prolongs survival of mice with BCR-ABL-T315I-induced leukemia and suppresses leukemic stem cells
    • Peng C, Brain J, Hu Y, et al. Inhibition of heat shock protein 90 prolongs survival of mice with BCR-ABL-T315I-induced leukemia and suppresses leukemic stem cells. Blood 2007; 110: 678-85.
    • (2007) Blood , vol.110 , pp. 678-685
    • Peng, C.1    Brain, J.2    Hu, Y.3
  • 47
    • 84857055228 scopus 로고    scopus 로고
    • An openlabel phase II study of the Hsp90 inhibitor ganetespib (STA- 9090) in patients (pts) with metastatic and/or unresectable GIST
    • Demetri GD, Heinrich MC, Chmielowski B, al. e. An openlabel phase II study of the Hsp90 inhibitor ganetespib (STA- 9090) in patients (pts) with metastatic and/or unresectable GIST. J Clin Oncol 2011; 29: 10011.
    • (2011) J Clin Oncol , vol.29 , pp. 10011
    • Demetri, G.D.1    Heinrich, M.C.2    Chmielowski, B.3
  • 48
    • 79951885125 scopus 로고    scopus 로고
    • Activity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer
    • Sequist LV, Gettinger S, Senzer NN, et al. Activity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer. J Clin Oncol 2010; 28: 4953-60.
    • (2010) J Clin Oncol , vol.28 , pp. 4953-4960
    • Sequist, L.V.1    Gettinger, S.2    Senzer, N.N.3
  • 49
    • 79958829892 scopus 로고    scopus 로고
    • Combined effects of novel heat shock protein 90 inhibitor NVP-AUY922 and nilotinib in a random mutagenesis screen
    • Tauchi T, Okabe S, Ashihara E, Kimura S, Maekawa T, Ohyashiki K. Combined effects of novel heat shock protein 90 inhibitor NVP-AUY922 and nilotinib in a random mutagenesis screen. Oncogene 2011; 30: 2789-97.
    • (2011) Oncogene , vol.30 , pp. 2789-2797
    • Tauchi, T.1    Okabe, S.2    Ashihara, E.3    Kimura, S.4    Maekawa, T.5    Ohyashiki, K.6
  • 50
    • 56849131626 scopus 로고    scopus 로고
    • Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
    • Southworth DR, Agard DA. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Mol Cell 2008; 32: 631-40.
    • (2008) Mol Cell , vol.32 , pp. 631-640
    • Southworth, D.R.1    Agard, D.A.2
  • 51
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion
    • Yang Y, Rao R, Shen J, et al. Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion. Cancer Res 2008; 68: 4833-42.
    • (2008) Cancer Res , vol.68 , pp. 4833-4842
    • Yang, Y.1    Rao, R.2    Shen, J.3
  • 52
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • Scroggins BT, Robzyk K, Wang D, et al. An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol Cell 2007; 25: 151-9.
    • (2007) Mol Cell , vol.25 , pp. 151-159
    • Scroggins, B.T.1    Robzyk, K.2    Wang, D.3
  • 53
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs JJ, Murphy PJ, Gaillard S, et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol Cell 2005; 18: 601-7.
    • (2005) Mol Cell , vol.18 , pp. 601-607
    • Kovacs, J.J.1    Murphy, P.J.2    Gaillard, S.3
  • 54
    • 24344473755 scopus 로고    scopus 로고
    • Activity of suberoylanilide hydroxamic Acid against human breast cancer cells with amplification of her-2
    • Bali P, Pranpat M, Swaby R, et al. Activity of suberoylanilide hydroxamic Acid against human breast cancer cells with amplification of her-2. Clin Cancer Res 2005; 11: 6382-9.
    • (2005) Clin Cancer Res , vol.11 , pp. 6382-6389
    • Bali, P.1    Pranpat, M.2    Swaby, R.3
  • 55
    • 77249087051 scopus 로고    scopus 로고
    • Chemical phylogenetics of histone deacetylases
    • Bradner JE, West N, Grachan ML, et al. Chemical phylogenetics of histone deacetylases. Nat Chem Biol 2010; 6: 238-43.
    • (2010) Nat Chem Biol , vol.6 , pp. 238-243
    • Bradner, J.E.1    West, N.2    Grachan, M.L.3
  • 56
    • 52649133274 scopus 로고    scopus 로고
    • HDAC6 inhibition enhances 17-AAG--mediated abrogation of hsp90 chaperone function in human leukemia cells
    • Rao R, Fiskus W, Yang Y, et al. HDAC6 inhibition enhances 17-AAG--mediated abrogation of hsp90 chaperone function in human leukemia cells. Blood 2008; 112: 1886-93.
    • (2008) Blood , vol.112 , pp. 1886-1893
    • Rao, R.1    Fiskus, W.2    Yang, Y.3
  • 57
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan AJ, Scott MD, Frydman J. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 2005; 121: 739-48.
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 58
    • 79960427057 scopus 로고    scopus 로고
    • Selective killing of cancer cells by a small molecule targeting the stress response to ROS
    • Raj L, Ide T, Gurkar AU, et al. Selective killing of cancer cells by a small molecule targeting the stress response to ROS. Nature 2011; 475: 231-4.
    • (2011) Nature , vol.475 , pp. 231-234
    • Raj, L.1    Ide, T.2    Gurkar, A.U.3
  • 59
    • 84863158295 scopus 로고    scopus 로고
    • Using the heatshock response to discover anticancer compounds that target protein homeostasis
    • Santagata S, Xu YM, Wijeratne EM, et al. Using the heatshock response to discover anticancer compounds that target protein homeostasis. ACS Chem Biol 2012; 7: 340-9.
    • (2012) ACS Chem Biol , vol.7 , pp. 340-349
    • Santagata, S.1    Xu, Y.M.2    Wijeratne, E.M.3
  • 60
    • 4444311881 scopus 로고    scopus 로고
    • Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity
    • Mimnaugh EG, Xu W, Vos M, et al. Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity. Mol Cancer Ther 2004; 3: 551-66.
    • (2004) Mol Cancer Ther , vol.3 , pp. 551-566
    • Mimnaugh, E.G.1    Xu, W.2    Vos, M.3
  • 61
    • 33845348883 scopus 로고    scopus 로고
    • Combination mammalian target of rapamycin inhibitor rapamycin and HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin has synergistic activity in multiple myeloma
    • Francis LK, Alsayed Y, Leleu X, et al. Combination mammalian target of rapamycin inhibitor rapamycin and HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin has synergistic activity in multiple myeloma. Clin Cancer Res 2006; 12: 6826-35.
    • (2006) Clin Cancer Res , vol.12 , pp. 6826-6835
    • Francis, L.K.1    Alsayed, Y.2    Leleu, X.3
  • 62
    • 77952219448 scopus 로고    scopus 로고
    • Mechanistic evaluation of the novel HSP90 inhibitor NVP-AUY922 in adult and pediatric glioblastoma
    • Gaspar N, Sharp SY, Eccles SA, et al. Mechanistic evaluation of the novel HSP90 inhibitor NVP-AUY922 in adult and pediatric glioblastoma. Mol Cancer Ther 2010; 9: 1219-33.
    • (2010) Mol Cancer Ther , vol.9 , pp. 1219-1233
    • Gaspar, N.1    Sharp, S.Y.2    Eccles, S.A.3
  • 63
    • 51049093831 scopus 로고    scopus 로고
    • Combination of rapamycin and 17- allylamino-17-demethoxygeldanamycin abrogates Akt activation and potentiates mTOR blockade in breast cancer cells
    • Roforth MM, Tan C. Combination of rapamycin and 17- allylamino-17-demethoxygeldanamycin abrogates Akt activation and potentiates mTOR blockade in breast cancer cells. Anticancer Drugs 2008; 19: 681-8.
    • (2008) Anticancer Drugs , vol.19 , pp. 681-688
    • Roforth, M.M.1    Tan, C.2
  • 64
    • 82955169663 scopus 로고    scopus 로고
    • Evolutionary dynamics in cancer therapy
    • Cunningham J, Gatenby RA, Brown JS. Evolutionary dynamics in cancer therapy. Mol Pharm 2011; 8: 2094-100.
    • (2011) Mol Pharm , vol.8 , pp. 2094-2100
    • Cunningham, J.1    Gatenby, R.A.2    Brown, J.S.3
  • 66
    • 79951689086 scopus 로고    scopus 로고
    • Identification of aneuploidy-selective antiproliferation compounds
    • Tang YC, Williams BR, Siegel JJ, Amon A. Identification of aneuploidy-selective antiproliferation compounds. Cell 2011; 144: 499-512.
    • (2011) Cell , vol.144 , pp. 499-512
    • Tang, Y.C.1    Williams, B.R.2    Siegel, J.J.3    Amon, A.4
  • 67
    • 17444404622 scopus 로고    scopus 로고
    • Hsp90 and environmental impacts on epigenetic states: A model for the trans-generational effects of diethylstibesterol on uterine development and cancer
    • Ruden DM, Xiao L, Garfinkel MD, Lu X. Hsp90 and environmental impacts on epigenetic states: a model for the trans-generational effects of diethylstibesterol on uterine development and cancer. Hum Mol Genet 2005; 14 Spec No 1: R149-55.
    • (2005) Hum Mol Genet , vol.14 , Issue.1
    • Ruden, D.M.1    Xiao, L.2    Garfinkel, M.D.3    Lu, X.4
  • 68
    • 35748931551 scopus 로고    scopus 로고
    • Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levels
    • Sangster TA, Bahrami A, Wilczek A, et al. Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levels. PLoS One 2007; 2: e648.
    • (2007) PLoS One , vol.2
    • Sangster, T.A.1    Bahrami, A.2    Wilczek, A.3
  • 69
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford SL, Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature 1998; 396: 336-42.
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 70
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch C, Sangster TA, Lindquist S. Hsp90 as a capacitor of phenotypic variation. Nature 2002; 417: 618-24.
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 72
    • 35148876623 scopus 로고    scopus 로고
    • The Hsp90 capacitor, developmental remodeling, and evolution: The robustness of gene networks and the curious evolvability of metamorphosis
    • Rutherford S, Hirate Y, Swalla BJ. The Hsp90 capacitor, developmental remodeling, and evolution: the robustness of gene networks and the curious evolvability of metamorphosis. Crit Rev Biochem Mol Biol 2007; 42: 355-72.
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , pp. 355-372
    • Rutherford, S.1    Hirate, Y.2    Swalla, B.J.3
  • 73
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki N, Tawfik DS. Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 2009; 459: 668-73.
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 74
    • 76349117871 scopus 로고    scopus 로고
    • Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons
    • Specchia V, Piacentini L, Tritto P, et al. Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons. Nature 2010; 463: 662-5.
    • (2010) Nature , vol.463 , pp. 662-665
    • Specchia, V.1    Piacentini, L.2    Tritto, P.3
  • 75
    • 79251560849 scopus 로고    scopus 로고
    • Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation
    • Gangaraju VK, Yin H, Weiner MM, Wang J, Huang XA, Lin H. Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation. Nat Genet 2011; 43: 153-8.
    • (2011) Nat Genet , vol.43 , pp. 153-158
    • Gangaraju, V.K.1    Yin, H.2    Weiner, M.M.3    Wang, J.4    Huang, X.A.5    Lin, H.6
  • 76
    • 78650644709 scopus 로고    scopus 로고
    • Hsp90 and environmental stress transform the adaptive value of natural genetic variation
    • Jarosz DF, Lindquist S. Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science 2010; 330: 1820-4.
    • (2010) Science , vol.330 , pp. 1820-1824
    • Jarosz, D.F.1    Lindquist, S.2
  • 77
    • 84862777815 scopus 로고    scopus 로고
    • Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy
    • Chen G, Bradford WD, Seidel CW, Li R. Hsp90 stress potentiates rapid cellular adaptation through induction of aneuploidy. Nature 2012; 482: 246-50.
    • (2012) Nature , vol.482 , pp. 246-250
    • Chen, G.1    Bradford, W.D.2    Seidel, C.W.3    Li, R.4
  • 79
    • 29244469466 scopus 로고    scopus 로고
    • The epigenetic progenitor origin of human cancer
    • Feinberg AP, Ohlsson R, Henikoff S. The epigenetic progenitor origin of human cancer. Nat Rev Genet 2006; 7: 21-33.
    • (2006) Nat Rev Genet , vol.7 , pp. 21-33
    • Feinberg, A.P.1    Ohlsson, R.2    Henikoff, S.3
  • 80
    • 44449177914 scopus 로고    scopus 로고
    • An evolutionary model for initiation, promotion, and progression in carcinogenesis
    • Vincent TL, Gatenby RA. An evolutionary model for initiation, promotion, and progression in carcinogenesis. Int J Oncol 2008; 32: 729-37.
    • (2008) Int J Oncol , vol.32 , pp. 729-737
    • Vincent, T.L.1    Gatenby, R.A.2
  • 81
    • 78049398107 scopus 로고    scopus 로고
    • Distant metastasis occurs late during the genetic evolution of pancreatic cancer
    • Yachida S, Jones S, Bozic I, et al. Distant metastasis occurs late during the genetic evolution of pancreatic cancer. Nature 2010; 467: 1114-7.
    • (2010) Nature , vol.467 , pp. 1114-1117
    • Yachida, S.1    Jones, S.2    Bozic, I.3
  • 82
    • 10344239940 scopus 로고    scopus 로고
    • Hsp90 chaperones wild-type p53 tumor suppressor protein
    • Walerych D, Kudla G, Gutkowska M, et al. Hsp90 chaperones wild-type p53 tumor suppressor protein. J Biol Chem 2004; 279: 48836-45.
    • (2004) J Biol Chem , vol.279 , pp. 48836-48845
    • Walerych, D.1    Kudla, G.2    Gutkowska, M.3
  • 83
    • 0037444766 scopus 로고    scopus 로고
    • Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability
    • Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR. Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability. Biochem J 2003; 370: 849-57.
    • (2003) Biochem J , vol.370 , pp. 849-857
    • Boudeau, J.1    Deak, M.2    Lawlor, M.A.3    Morrice, N.A.4    Alessi, D.R.5
  • 84
    • 45849105629 scopus 로고    scopus 로고
    • Integration of gene dosage and gene expression in non-small cell lung cancer, identification of HSP90 as potential target
    • Gallegos Ruiz MI, Floor K, Roepman P, et al. Integration of gene dosage and gene expression in non-small cell lung cancer, identification of HSP90 as potential target. PLoS One 2008; 3: e0001722.
    • (2008) PLoS One , vol.3
    • Gallegos, R.M.I.1    Floor, K.2    Roepman, P.3
  • 85
    • 37549060720 scopus 로고    scopus 로고
    • Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells
    • Gray PJ, Jr., Stevenson MA, Calderwood SK. Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells. Cancer Res 2007; 67: 11942-50.
    • (2007) Cancer Res , vol.67 , pp. 11942-11950
    • Gray Jr., P.J.1    Stevenson, M.A.2    Calderwood, S.K.3
  • 86
    • 40449089789 scopus 로고    scopus 로고
    • Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin
    • Holmes JL, Sharp SY, Hobbs S, Workman P. Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin. Cancer Res 2008; 68: 1188-97.
    • (2008) Cancer Res , vol.68 , pp. 1188-1197
    • Holmes, J.L.1    Sharp, S.Y.2    Hobbs, S.3    Workman, P.4
  • 87
    • 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: 818-26.
    • (2011) Nat Chem Biol , vol.7 , pp. 818-826
    • Moulick, K.1    Ahn, J.H.2    Zong, H.3
  • 88
    • 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
  • 89
    • 33646725129 scopus 로고    scopus 로고
    • A biochemical rationale for the anticancer effects of Hsp90 inhibitors: Slow, tight binding inhibition by geldanamycin and its analogues
    • Gooljarsingh LT, Fernandes C, Yan K, et al. A biochemical rationale for the anticancer effects of Hsp90 inhibitors: slow, tight binding inhibition by geldanamycin and its analogues. Proc Natl Acad Sci USA 2006; 103: 7625-30.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7625-7630
    • Gooljarsingh, L.T.1    Fernandes, C.2    Yan, K.3
  • 90
    • 84867152376 scopus 로고    scopus 로고
    • Loss of tumor suppressor NF1 activates HSF1 to promote carcinogenesis
    • Epub ahead of print
    • Dai C, Santagata S, Tang Z, et al. Loss of tumor suppressor NF1 activates HSF1 to promote carcinogenesis. J Clin Invest 2012; [Epub ahead of print].
    • (2012) J Clin Invest
    • Dai, C.1    Santagata, S.2    Tang, Z.3
  • 91
    • 67649217159 scopus 로고    scopus 로고
    • Inhibiting the transcription factor HSF1 as an anticancer strategy
    • Whitesell L, Lindquist S. Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin Ther Targets 2009; 13: 469-78.
    • (2009) Expert Opin Ther Targets , vol.13 , pp. 469-478
    • Whitesell, L.1    Lindquist, S.2
  • 92
    • 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
  • 93
    • 84864585171 scopus 로고    scopus 로고
    • HSF1 Drives a Transcriptional Program Distinct from Heat Shock to Support Highly Malignant Human Cancers
    • Mendillo ML, Santagata S, Koeva M, et al. HSF1 Drives a Transcriptional Program Distinct from Heat Shock to Support Highly Malignant Human Cancers. Cell 2012; 150: 549-62.
    • (2012) Cell , vol.150 , pp. 549-562
    • Mendillo, M.L.1    Santagata, S.2    Koeva, M.3
  • 94
    • 81055141345 scopus 로고    scopus 로고
    • High levels of nuclear heatshock factor 1 (HSF1) are associated with poor prognosis in breast cancer
    • Santagata S, Hu R, Lin NU, et al. High levels of nuclear heatshock factor 1 (HSF1) are associated with poor prognosis in breast cancer. Proc Natl Acad Sci USA 2011; 108: 18378-83.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18378-18383
    • Santagata, S.1    Hu, R.2    Lin, N.U.3
  • 95
    • 84857036694 scopus 로고    scopus 로고
    • Use of biomarkers and imaging to evaluate the treatment effect of AUY922, an HSP90 inhibitor, in patients with HER2+ or ER+ metastatic breast cancer
    • Abstract #e11024
    • Schroder CP, Pedersen JV, Chua S, et al. Use of biomarkers and imaging to evaluate the treatment effect of AUY922, an HSP90 inhibitor, in patients with HER2+ or ER+ metastatic breast cancer. J Clin Oncol 2011; 29: Abstract #e11024.
    • (2011) J Clin Oncol , vol.29
    • Schroder, C.P.1    Pedersen, J.V.2    Chua, S.3
  • 96
    • 84858708597 scopus 로고    scopus 로고
    • Heat shock factor 1 promotes invasion and metastasis of hepatocellular carcinoma in vitro and in vivo
    • Fang F, Chang R, Yang L. Heat shock factor 1 promotes invasion and metastasis of hepatocellular carcinoma in vitro and in vivo. Cancer 2012; 118: 1782-94.
    • (2012) Cancer , vol.118 , pp. 1782-1794
    • Fang, F.1    Chang, R.2    Yang, L.3
  • 99
    • 25844530060 scopus 로고    scopus 로고
    • Hsp90 potentiates the rapid evolution of new traits: Drug resistance in diverse fungi
    • Cowen LE, Lindquist S. Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science 2005; 309: 2185-9.
    • (2005) Science , vol.309 , pp. 2185-2189
    • Cowen, L.E.1    Lindquist, S.2
  • 100
    • 62449104891 scopus 로고    scopus 로고
    • Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease
    • Cowen LE, Singh SD, Kohler JR, et al. Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc Natl Acad Sci USA 2009; 106: 2818-23.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2818-2823
    • Cowen, L.E.1    Singh, S.D.2    Kohler, J.R.3
  • 101
    • 39149087719 scopus 로고    scopus 로고
    • The evolution of fungal drug resistance: Modulating the trajectory from genotype to phenotype
    • Cowen LE. The evolution of fungal drug resistance: modulating the trajectory from genotype to phenotype. Nat Rev Microbiol 2008; 6: 187-98.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 187-198
    • Cowen, L.E.1
  • 103
    • 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
  • 104
    • 20044384168 scopus 로고    scopus 로고
    • Phase I trial of 17-allylamino- 17-demethoxygeldanamycin in patients with advanced cancer
    • Goetz MP, Toft D, Reid J, et al. Phase I trial of 17-allylamino- 17-demethoxygeldanamycin in patients with advanced cancer. J Clin Oncol 2005; 23: 1078-87.
    • (2005) J Clin Oncol , vol.23 , pp. 1078-1087
    • Goetz, M.P.1    Toft, D.2    Reid, J.3
  • 105
    • 20944444881 scopus 로고    scopus 로고
    • Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)- 17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers
    • Ramanathan RK, Trump DL, Eiseman JL, et al. Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)- 17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers. Clin Cancer Res 2005; 11: 3385-91.
    • (2005) Clin Cancer Res , vol.11 , pp. 3385-3391
    • Ramanathan, R.K.1    Trump, D.L.2    Eiseman, J.L.3
  • 106
    • 58149340657 scopus 로고    scopus 로고
    • Phase II trial of 17- allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma
    • Solit DB, Osman I, Polsky D, et al. Phase II trial of 17- allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma. Clin Cancer Res 2008; 14: 8302-7.
    • (2008) Clin Cancer Res , vol.14 , pp. 8302-8307
    • Solit, D.B.1    Osman, I.2    Polsky, D.3
  • 107
    • 34250160933 scopus 로고    scopus 로고
    • Phase I and pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with refractory advanced cancers
    • Ramanathan RK, Egorin MJ, Eiseman JL, et al. Phase I and pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with refractory advanced cancers. Clin Cancer Res 2007; 13: 1769-74.
    • (2007) Clin Cancer Res , vol.13 , pp. 1769-1774
    • Ramanathan, R.K.1    Egorin, M.J.2    Eiseman, J.L.3
  • 108
    • 34250197902 scopus 로고    scopus 로고
    • Phase I trial of 17-allylamino- 17-demethoxygeldanamycin in patients with advanced cancer
    • Solit DB, Ivy SP, Kopil C, et al. Phase I trial of 17-allylamino- 17-demethoxygeldanamycin in patients with advanced cancer. Clin Cancer Res 2007; 13: 1775-82.
    • (2007) Clin Cancer Res , vol.13 , pp. 1775-1782
    • Solit, D.B.1    Ivy, S.P.2    Kopil, C.3
  • 109
    • 20144375312 scopus 로고    scopus 로고
    • Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors
    • Grem JL, Morrison G, Guo XD, et al. Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors. J Clin Oncol 2005; 23: 1885-93.
    • (2005) J Clin Oncol , vol.23 , pp. 1885-1893
    • Grem, J.L.1    Morrison, G.2    Guo, X.D.3
  • 110
    • 34250182069 scopus 로고    scopus 로고
    • A phase I study of 17- allylaminogeldanamycin in relapsed/refractory pediatric patients with solid tumors: A Children's Oncology Group study
    • Weigel BJ, Blaney SM, Reid JM, et al. A phase I study of 17- allylaminogeldanamycin in relapsed/refractory pediatric patients with solid tumors: a Children's Oncology Group study. Clin Cancer Res 2007; 13: 1789-93.
    • (2007) Clin Cancer Res , vol.13 , pp. 1789-1793
    • Weigel, B.J.1    Blaney, S.M.2    Reid, J.M.3
  • 111
    • 79960983010 scopus 로고    scopus 로고
    • Why is this effective HSP90 inhibitor not being developed in HER2+ breast cancer?
    • Arteaga CL. Why is this effective HSP90 inhibitor not being developed in HER2+ breast cancer? Clin Cancer Res 2011; 17: 4919-21.
    • (2011) Clin Cancer Res , vol.17 , pp. 4919-4921
    • Arteaga, C.L.1
  • 112
    • 77951907072 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17- dimethylaminoethylamino-17-demethoxygeldanamycin, an inhibitor of heat-shock protein 90, in patients with advanced solid tumors
    • Ramanathan RK, Egorin MJ, Erlichman C, et al. Phase I pharmacokinetic and pharmacodynamic study of 17- dimethylaminoethylamino-17-demethoxygeldanamycin, an inhibitor of heat-shock protein 90, in patients with advanced solid tumors. J Clin Oncol 2010; 28: 1520-6.
    • (2010) J Clin Oncol , vol.28 , pp. 1520-1526
    • Ramanathan, R.K.1    Egorin, M.J.2    Erlichman, C.3
  • 113
    • 79952734485 scopus 로고    scopus 로고
    • A phase I study of the heat shock protein 90 inhibitor alvespimycin (17-DMAG) given intravenously to patients with advanced solid tumors
    • Pacey S, Wilson RH, Walton M, et al. A phase I study of the heat shock protein 90 inhibitor alvespimycin (17-DMAG) given intravenously to patients with advanced solid tumors. Clin Cancer Res 2011; 17: 1561-70.
    • (2011) Clin Cancer Res , vol.17 , pp. 1561-1570
    • Pacey, S.1    Wilson, R.H.2    Walton, M.3
  • 114
    • 72449185268 scopus 로고    scopus 로고
    • Phase I trial of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-D MAG), 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-D MAG), a heat shock protein inhibitor, administered twice weekly in patients with advanced malignancies. Eur J Cancer 2010; 46: 340-7.
    • (2010) Eur J Cancer , vol.46 , pp. 340-347
    • Kummar, S.1    Gutierrez, M.E.2    Gardner, E.R.3
  • 115
    • 77954214309 scopus 로고    scopus 로고
    • Final results from a phase III study of IPI-504 (retaspimycin hydrochloride) versus placebo in patients (pts) with gastrointestinal stromal tumors (GIST) following failure of kinase inhibitor therapies
    • Abstract #64
    • Demetri GD, Le Cesne A, Von Mehren M, et al. Final results from a phase III study of IPI-504 (retaspimycin hydrochloride) versus placebo in patients (pts) with gastrointestinal stromal tumors (GIST) following failure of kinase inhibitor therapies. ASCO GI Cancers Symposium 2010; Abstract #64.
    • (2010) ASCO GI Cancers Symposium
    • Demetri, G.D.1    Le Cesne, A.2    von Mehren, M.3
  • 116
    • 84856032294 scopus 로고    scopus 로고
    • Efficacy and safety of retaspimycin hydrochloride (IPI-504) in combination with trastuzumab in patients (pts) with pretreated, locally advanced or metastatic HER2-positive breast cancer
    • Modi S, Saura C, Henderson CA, et al. Efficacy and safety of retaspimycin hydrochloride (IPI-504) in combination with trastuzumab in patients (pts) with pretreated, locally advanced or metastatic HER2-positive breast cancer. J Clin Oncol 2011; 29: 590.
    • (2011) J Clin Oncol , vol.29 , pp. 590
    • Modi, S.1    Saura, C.2    Henderson, C.A.3
  • 117
    • 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
  • 118
    • 77149153795 scopus 로고    scopus 로고
    • A phase I dose escalation study of AUY922, a novel HSP90 inhibitor, in patients with advanced solid malignancies
    • Sessa C, Sharma SK, Britten CD, et al. A phase I dose escalation study of AUY922, a novel HSP90 inhibitor, in patients with advanced solid malignancies. J Clin Oncol 2009; 27: 3532.
    • (2009) J Clin Oncol , vol.27 , pp. 3532
    • Sessa, C.1    Sharma, S.K.2    Britten, C.D.3
  • 119
    • 51449115938 scopus 로고    scopus 로고
    • A Phase 1 dose-escalation study of the safety and pharmacokinetics (PK) of the oral Hsp90 inhibitor SNX-5422
    • Abstract # 14613
    • Bryson JC, Infante JR, Ramanathan RK, Jones SF, Von Hoff DD, Burris HA, 3rd. A Phase 1 dose-escalation study of the safety and pharmacokinetics (PK) of the oral Hsp90 inhibitor SNX-5422. J Clin Oncol 2008; 26: Abstract # 14613.
    • (2008) J Clin Oncol , vol.26
    • Bryson, J.C.1    Infante, J.R.2    Ramanathan, R.K.3    Jones, S.F.4    von Hoff, D.D.5    Burris III., H.A.6
  • 122
    • 79959956046 scopus 로고    scopus 로고
    • The JAK2/STAT3 signaling pathway is required for growth of CD44CD24 stem cell-like breast cancer cells in human tumors
    • Marotta LL, Almendro V, Marusyk A, et al. The JAK2/STAT3 signaling pathway is required for growth of CD44CD24 stem cell-like breast cancer cells in human tumors. J Clin Invest 2011; 121: 2723-35.
    • (2011) J Clin Invest , vol.121 , pp. 2723-2735
    • Marotta, L.L.1    Almendro, V.2    Marusyk, A.3
  • 123
    • 67449138839 scopus 로고    scopus 로고
    • CUDC-305, a novel synthetic HSP90 inhibitor with unique pharmacologic properties for cancer therapy
    • Bao R, Lai CJ, Qu H, et al. CUDC-305, a novel synthetic HSP90 inhibitor with unique pharmacologic properties for cancer therapy. Clin Cancer Res 2009; 15: 4046-57.
    • (2009) Clin Cancer Res , vol.15 , pp. 4046-4057
    • Bao, R.1    Lai, C.J.2    Qu, H.3
  • 124
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey CA, Kamal A, Lundgren K, et al. The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest 2007; 117: 648-58.
    • (2007) J Clin Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1    Kamal, A.2    Lundgren, K.3
  • 125
    • 78650727347 scopus 로고    scopus 로고
    • A systematic protocol for the characterization of Hsp90 modulators
    • Matts RL, Brandt GE, Lu Y, et al. A systematic protocol for the characterization of Hsp90 modulators. Bioorg Med Chem 2011; 19: 684-92.
    • (2011) Bioorg Med Chem , vol.19 , pp. 684-692
    • Matts, R.L.1    Brandt, G.E.2    Lu, Y.3
  • 126
    • 21144437911 scopus 로고    scopus 로고
    • Rational design of shepherdin, a novel anticancer agent
    • Plescia J, Salz W, Xia F, et al. Rational design of shepherdin, a novel anticancer agent. Cancer Cell 2005; 7: 457-68.
    • (2005) Cancer Cell , vol.7 , pp. 457-468
    • Plescia, J.1    Salz, W.2    Xia, F.3
  • 127
    • 35348887850 scopus 로고    scopus 로고
    • Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network
    • Kang BH, Plescia J, Dohi T, Rosa J, Doxsey SJ, Altieri DC. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network. Cell 2007; 131: 257-70.
    • (2007) Cell , vol.131 , pp. 257-270
    • Kang, B.H.1    Plescia, J.2    Dohi, T.3    Rosa, J.4    Doxsey, S.J.5    Altieri, D.C.6
  • 128
    • 79951673830 scopus 로고    scopus 로고
    • Targeted inhibition of mitochondrial Hsp90 suppresses localised and metastatic prostate cancer growth in a genetic mouse model of disease
    • Kang BH, Tavecchio M, Goel HL, et al. Targeted inhibition of mitochondrial Hsp90 suppresses localised and metastatic prostate cancer growth in a genetic mouse model of disease. Br J Cancer 2011; 104: 629-34.
    • (2011) Br J Cancer , vol.104 , pp. 629-634
    • Kang, B.H.1    Tavecchio, M.2    Goel, H.L.3
  • 129
    • 33646371009 scopus 로고    scopus 로고
    • Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: Evidence that coumarin antibiotics disrupt Hsp90 dimerization
    • Allan RK, Mok D, Ward BK, Ratajczak T. Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization. J Biol Chem 2006; 281: 7161-71.
    • (2006) J Biol Chem , vol.281 , pp. 7161-7171
    • Allan, R.K.1    Mok, D.2    Ward, B.K.3    Ratajczak, T.4
  • 130
    • 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
    • Marcu MG, Chadli A, Bouhouche I, Catelli M, Neckers LM. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J Biol Chem 2000; 275: 37181-6.
    • (2000) J Biol Chem , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 131
    • 79958171071 scopus 로고    scopus 로고
    • Engineering an antibiotic to fight cancer: Optimization of the novobiocin scaffold to produce anti-proliferative agents
    • Zhao H, Donnelly AC, Kusuma BR, et al. Engineering an antibiotic to fight cancer: optimization of the novobiocin scaffold to produce anti-proliferative agents. J Med Chem 2011; 54: 3839-53.
    • (2011) J Med Chem , vol.54 , pp. 3839-3853
    • Zhao, H.1    Donnelly, A.C.2    Kusuma, B.R.3
  • 132
    • 84865000590 scopus 로고    scopus 로고
    • Novel C-Terminal Hsp90 Inhibitor for Head and Neck Squamous Cell Cancer (HNSCC) with in vivo Efficacy and Improved Toxicity Profiles Compared with Standard Agents
    • Cohen SM, Mukerji R, Samadi AK, Zhao H, Blagg BS, Cohen MS. Novel C-Terminal Hsp90 Inhibitor for Head and Neck Squamous Cell Cancer (HNSCC) with in vivo Efficacy and Improved Toxicity Profiles Compared with Standard Agents. Ann Surg Oncol 2012; 19 Suppl 3: 483-90.
    • (2012) Ann Surg Oncol , vol.19 , Issue.3 SUPPL. , pp. 483-490
    • Cohen, S.M.1    Mukerji, R.2    Samadi, A.K.3    Zhao, H.4    Blagg, B.S.5    Cohen, M.S.6
  • 133
    • 82555180241 scopus 로고    scopus 로고
    • An open-label phase II study of the Hsp90 inhibitor ganetespib (STA-9090) as monotherapy in patients with advanced non-small cell lung cancer (NSCLC)
    • Abstract #7500
    • Wong K, Koczywas M, Goldman JW, et al. An open-label phase II study of the Hsp90 inhibitor ganetespib (STA-9090) as monotherapy in patients with advanced non-small cell lung cancer (NSCLC). J Clin Oncol 2011; 29: Abstract #7500.
    • (2011) J Clin Oncol , vol.29
    • Wong, K.1    Koczywas, M.2    Goldman, J.W.3
  • 134
    • 79956318797 scopus 로고    scopus 로고
    • Therapeutic strategies to overcome crizotinib resistance in non-small cell lung cancers harboring the fusion oncogene EML4-ALK
    • Katayama R, Khan TM, Benes C, et al. Therapeutic strategies to overcome crizotinib resistance in non-small cell lung cancers harboring the fusion oncogene EML4-ALK. Proc Natl Acad Sci USA 2011; 108: 7535-40.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 7535-7540
    • Katayama, R.1    Khan, T.M.2    Benes, C.3
  • 135
    • 0036894746 scopus 로고    scopus 로고
    • BRAF and RAS mutations in human lung cancer and melanoma
    • Brose MS, Volpe P, Feldman M, et al. BRAF and RAS mutations in human lung cancer and melanoma. Cancer Res 2002; 62: 6997-7000.
    • (2002) Cancer Res , vol.62 , pp. 6997-7000
    • Brose, M.S.1    Volpe, P.2    Feldman, M.3
  • 136
    • 18444374405 scopus 로고    scopus 로고
    • Mutations of the BRAF gene in human cancer
    • Davies H, Bignell GR, Cox C, et al. Mutations of the BRAF gene in human cancer. Nature 2002; 417: 949-54.
    • (2002) Nature , vol.417 , pp. 949-954
    • Davies, H.1    Bignell, G.R.2    Cox, C.3
  • 137
    • 79953184268 scopus 로고    scopus 로고
    • BRAF V600E mutations are common in pleomorphic xanthoastrocytoma: Diagnostic and therapeutic implications
    • Dias-Santagata D, Lam Q, Vernovsky K, et al. BRAF V600E mutations are common in pleomorphic xanthoastrocytoma: diagnostic and therapeutic implications. PLoS One 2011; 6: e17948.
    • (2011) PLoS One , vol.6
    • Dias-Santagata, D.1    Lam, Q.2    Vernovsky, K.3
  • 138
    • 33747691089 scopus 로고    scopus 로고
    • A phase II trial of 17-(Allylamino)-17-demethoxygeldanamycin in patients with papillary and clear cell renal cell carcinoma
    • Ronnen EA, Kondagunta GV, Ishill N, et al. A phase II trial of 17-(Allylamino)-17-demethoxygeldanamycin in patients with papillary and clear cell renal cell carcinoma. Invest New Drugs 2006; 24: 543-6.
    • (2006) Invest New Drugs , vol.24 , pp. 543-546
    • Ronnen, E.A.1    Kondagunta, G.V.2    Ishill, N.3
  • 139
    • 59449108495 scopus 로고    scopus 로고
    • A phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with hormone-refractory metastatic prostate cancer
    • Heath EI, Hillman DW, Vaishampayan U, et al. A phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with hormone-refractory metastatic prostate cancer. Clin Cancer Res 2008; 14: 7940-6.
    • (2008) Clin Cancer Res , vol.14 , pp. 7940-7946
    • Heath, E.I.1    Hillman, D.W.2    Vaishampayan, U.3
  • 140
    • 36849055007 scopus 로고    scopus 로고
    • Combination of trastuzumab and tanespimycin (17-AAG, KOS-953) is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer: A phase I dose-escalation study
    • Modi S, Stopeck AT, Gordon MS, et al. Combination of trastuzumab and tanespimycin (17-AAG, KOS-953) is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer: a phase I dose-escalation study. J Clin Oncol 2007; 25: 5410-7.
    • (2007) J Clin Oncol , vol.25 , pp. 5410-5417
    • Modi, S.1    Stopeck, A.T.2    Gordon, M.S.3
  • 141
    • 79960985354 scopus 로고    scopus 로고
    • HSP90 Inhibition Is Effective in Breast Cancer: A Phase II Trial of Tanespimycin (17-AAG) Plus Trastuzumab in Patients with HER2-Positive Metastatic Breast Cancer Progressing on Trastuzumab
    • Modi S, Stopeck A, Linden H, et al. HSP90 Inhibition Is Effective in Breast Cancer: A Phase II Trial of Tanespimycin (17-AAG) Plus Trastuzumab in Patients with HER2-Positive Metastatic Breast Cancer Progressing on Trastuzumab. Clin Cancer Res 2011; 17: 5132-9.
    • (2011) Clin Cancer Res , vol.17 , pp. 5132-5139
    • Modi, S.1    Stopeck, A.2    Linden, H.3
  • 142
    • 77949884661 scopus 로고    scopus 로고
    • Randomized study of Lapatinib alone or in combination with trastuzumab in women with ErbB2-positive, trastuzumab-refractory metastatic breast cancer
    • Blackwell KL, Burstein HJ, Storniolo AM, et al. Randomized study of Lapatinib alone or in combination with trastuzumab in women with ErbB2-positive, trastuzumab-refractory metastatic breast cancer. J Clin Oncol 2010; 28: 1124-30.
    • (2010) J Clin Oncol , vol.28 , pp. 1124-1130
    • Blackwell, K.L.1    Burstein, H.J.2    Storniolo, A.M.3
  • 143
    • 77955144862 scopus 로고    scopus 로고
    • Tanespimycin with bortezomib: Activity in relapsed/refractory patients with multiple myeloma
    • Richardson PG, Badros AZ, Jagannath S, et al. Tanespimycin with bortezomib: activity in relapsed/refractory patients with multiple myeloma. Br J Haematol 2010; 150: 428-37.
    • (2010) Br J Haematol , vol.150 , pp. 428-437
    • Richardson, P.G.1    Badros, A.Z.2    Jagannath, S.3
  • 144
    • 79955603500 scopus 로고    scopus 로고
    • Phase I study of 17- allylamino-17 demethoxygeldanamycin, gemcitabine and/or cisplatin in patients with refractory solid tumors
    • Hubbard J, Erlichman C, Toft DO, et al. Phase I study of 17- allylamino-17 demethoxygeldanamycin, gemcitabine and/or cisplatin in patients with refractory solid tumors. Invest New Drugs 2011; 29: 473-80.
    • (2011) Invest New Drugs , vol.29 , pp. 473-480
    • Hubbard, J.1    Erlichman, C.2    Toft, D.O.3
  • 145
    • 80355125870 scopus 로고    scopus 로고
    • Phase I and pharmacological study of cytarabine and tanespimycin in relapsed and refractory acute leukemia
    • Kaufmann SH, Karp JE, Litzow MR, et al. Phase I and pharmacological study of cytarabine and tanespimycin in relapsed and refractory acute leukemia. Haematologica 2011; 96: 1619-26.
    • (2011) Haematologica , vol.96 , pp. 1619-1626
    • Kaufmann, S.H.1    Karp, J.E.2    Litzow, M.R.3
  • 146
    • 0015710782 scopus 로고
    • The use of drugs in combination for the treatment of cancer: Rationale and results
    • DeVita VT, Schein PS. The use of drugs in combination for the treatment of cancer: rationale and results. N Engl J Med 1973; 288: 998-1006.
    • (1973) N Engl J Med , vol.288 , pp. 998-1006
    • Devita, V.T.1    Schein, P.S.2
  • 147
    • 0021857145 scopus 로고
    • Role of mathematical modeling in protocol formulation in cancer chemotherapy
    • Coldman AJ, Goldie JH. Role of mathematical modeling in protocol formulation in cancer chemotherapy. Cancer Treat Rep 1985; 69: 1041-8.
    • (1985) Cancer Treat Rep , vol.69 , pp. 1041-1048
    • Coldman, A.J.1    Goldie, J.H.2
  • 148
  • 151
    • 77951427922 scopus 로고    scopus 로고
    • Can open-source drug R&D repower pharmaceutical innovation?
    • Munos B. Can open-source drug R&D repower pharmaceutical innovation? Clin Pharmacol Ther 2010; 87: 534-6.
    • (2010) Clin Pharmacol Ther , vol.87 , pp. 534-536
    • Munos, B.1
  • 152
    • 79959786193 scopus 로고    scopus 로고
    • How to revive breakthrough innovation in the pharmaceutical industry
    • Munos BH, Chin WW. How to revive breakthrough innovation in the pharmaceutical industry. Sci Transl Med 2011; 3: 89cm16.
    • (2011) Sci Transl Med , vol.3
    • Munos, B.H.1    Chin, W.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.