메뉴 건너뛰기




Volumn 65, Issue , 2012, Pages 471-517

HSP90 Inhibitors for Cancer Therapy and Overcoming Drug Resistance

Author keywords

Biomarkers; Client proteins; Drug resistance; HSP90; Pharmacodynamic assays; Pharmacokinetics

Indexed keywords

5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; 5422; ALVESPIMYCIN; AT 13387; BIIB 021; BIOLOGICAL MARKER; CISPLATIN; CNF 2024; CUDC 305; CYTARABINE; DOCETAXEL; DS 2248; GANETESPIB; GELDANAMYCIN; GEMCITABINE; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HSP 990; IPI 493; IRINOTECAN; KW 2478; MPC 3100; PU H71; PURINE; PURINE DERIVATIVE; RESORCINOL; RETASPIMYCIN; SNX 5422; TANESPIMYCIN; TRASTUZUMAB; UNCLASSIFIED DRUG; VER 52269; XL 888;

EID: 84865839031     PISSN: 10543589     EISSN: 15578925     Source Type: Book Series    
DOI: 10.1016/B978-0-12-397927-8.00015-4     Document Type: Chapter
Times cited : (66)

References (169)
  • 1
    • 77957300462 scopus 로고    scopus 로고
    • Positron emission tomography (PET) with radiolabeled F(ab')2-trastuzumab fragments in patients (pts) with HER2-positive metastatic breast cancer (MBC): initial feasibility results
    • Akhurst T., Morris P., Modi S., Carraquillo J., Solit D., Hudis C., et al. Positron emission tomography (PET) with radiolabeled F(ab')2-trastuzumab fragments in patients (pts) with HER2-positive metastatic breast cancer (MBC): initial feasibility results. Breast Cancer Symposium 2008.
    • (2008) Breast Cancer Symposium
    • Akhurst, T.1    Morris, P.2    Modi, S.3    Carraquillo, J.4    Solit, D.5    Hudis, C.6
  • 2
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006, 440:1013-1017.
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1    Roe, S.M.2    Vaughan, C.K.3    Meyer, P.4    Panaretou, B.5    Piper, P.W.6
  • 6
    • 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 C.L., Marron M.T., Whitesell L. Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin. International Journal of Cancer 2005, 113:179-188.
    • (2005) International Journal of Cancer , vol.113 , pp. 179-188
    • Bagatell, R.1    Beliakoff, J.2    David, C.L.3    Marron, M.T.4    Whitesell, L.5
  • 7
    • 34250162501 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17-N-allylamino-17-demethoxygeldanamycin in pediatric patients with recurrent or refractory solid tumors: a pediatric oncology experimental therapeutics investigators consortium study
    • Bagatell R., Gore L., Egorin M.J., Ho R., Heller G., Boucher N., et al. Phase I pharmacokinetic and pharmacodynamic study of 17-N-allylamino-17-demethoxygeldanamycin in pediatric patients with recurrent or refractory solid tumors: a pediatric oncology experimental therapeutics investigators consortium study. Clinical Cancer Research 2007, 13:1783-1788.
    • (2007) Clinical Cancer Research , vol.13 , pp. 1783-1788
    • Bagatell, R.1    Gore, L.2    Egorin, M.J.3    Ho, R.4    Heller, G.5    Boucher, N.6
  • 8
    • 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., Pacey S., Stapleton S., Asad Y., et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. Journal of Clinical Oncology 2005, 23:4152-4161.
    • (2005) Journal of Clinical Oncology , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3    Pacey, S.4    Stapleton, S.5    Asad, Y.6
  • 9
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso A.D., Solit D.B., Munster P.N., Rosen N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 2002, 21:1159-1166.
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 12
    • 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 K.L., Burstein H.J., Storniolo A.M., Rugo H., Sledge G., Koehler M., et al. Randomized study of Lapatinib alone or in combination with trastuzumab in women with ErbB2-positive, trastuzumab-refractory metastatic breast cancer. Journal of Clinical Oncology 2010, 28:1124-1130.
    • (2010) Journal of Clinical Oncology , vol.28 , pp. 1124-1130
    • Blackwell, K.L.1    Burstein, H.J.2    Storniolo, A.M.3    Rugo, H.4    Sledge, G.5    Koehler, M.6
  • 13
    • 84874018767 scopus 로고    scopus 로고
    • A phase 2 study of the Hsp90 inhibitor ganetespib (STA-9090) as monotherapy in patients with advanced NSCLC, presented at the IASLC 14th World Conference on Lung Cancer.
    • Brahmer, J. K. M., Goldman, J., Paschold, E., Horn, L., Kepros, J., Teofilovici, F., et al. (2011). A phase 2 study of the Hsp90 inhibitor ganetespib (STA-9090) as monotherapy in patients with advanced NSCLC, presented at the IASLC 14th World Conference on Lung Cancer.
    • (2011)
    • Brahmer, J.K.M.1    Goldman, J.2    Paschold, E.3    Horn, L.4    Kepros, J.5    Teofilovici, F.6
  • 16
    • 27144551963 scopus 로고    scopus 로고
    • ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia
    • Castro J.E., Prada C.E., Loria O., Kamal A., Chen L., Burrows F.J., et al. ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia. Blood 2005, 106:2506-2512.
    • (2005) Blood , vol.106 , pp. 2506-2512
    • Castro, J.E.1    Prada, C.E.2    Loria, O.3    Kamal, A.4    Chen, L.5    Burrows, F.J.6
  • 17
    • 71549121697 scopus 로고    scopus 로고
    • A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lymphomas
    • Cerchietti L.C., Lopes E.C., Yang S.N., Hatzi K., Bunting K.L., Tsikitas L.A., et al. A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lymphomas. Nature Medicine 2009, 15:1369-1376.
    • (2009) Nature Medicine , vol.15 , pp. 1369-1376
    • Cerchietti, L.C.1    Lopes, E.C.2    Yang, S.N.3    Hatzi, K.4    Bunting, K.L.5    Tsikitas, L.A.6
  • 18
    • 84875912212 scopus 로고    scopus 로고
    • A comparison of 111In- or 64Cu-DOTA-trastuzumab Fab fragments for imaging subcutaneous HER2-positive tumor xenografts in athymic mice using microSPECT/CT or microPET/CT
    • Chan C., Scollard D.A., McLarty K., Smith S., Reilly R.M. A comparison of 111In- or 64Cu-DOTA-trastuzumab Fab fragments for imaging subcutaneous HER2-positive tumor xenografts in athymic mice using microSPECT/CT or microPET/CT. EJNMMI Research 2011, 1:15.
    • (2011) EJNMMI Research , vol.1 , pp. 15
    • Chan, C.1    Scollard, D.A.2    McLarty, K.3    Smith, S.4    Reilly, R.M.5
  • 19
    • 40749103835 scopus 로고    scopus 로고
    • SNX2112, a synthetic heat shock protein 90 inhibitor, has potent antitumor activity against HER kinase-dependent cancers
    • Chandarlapaty S., Sawai A., Ye Q., Scott A., Silinski M., Huang K., et al. SNX2112, a synthetic heat shock protein 90 inhibitor, has potent antitumor activity against HER kinase-dependent cancers. Clinical Cancer Research 2008, 14:240-248.
    • (2008) Clinical Cancer Research , vol.14 , pp. 240-248
    • Chandarlapaty, S.1    Sawai, A.2    Ye, Q.3    Scott, A.4    Silinski, M.5    Huang, K.6
  • 20
    • 75149123144 scopus 로고    scopus 로고
    • Inhibitors of HSP90 block p95-HER2 signaling in Trastuzumab-resistant tumors and suppress their growth
    • Chandarlapaty S., Scaltriti M., Angelini P., Ye Q., Guzman M., Hudis C.A., et al. Inhibitors of HSP90 block p95-HER2 signaling in Trastuzumab-resistant tumors and suppress their growth. Oncogene 2010, 29:325-334.
    • (2010) Oncogene , vol.29 , pp. 325-334
    • Chandarlapaty, S.1    Scaltriti, M.2    Angelini, P.3    Ye, Q.4    Guzman, M.5    Hudis, C.A.6
  • 22
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis G., Timaul M.N., Lucas B., Munster P.N., Zheng F.F., Sepp-Lorenzino L., et al. A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chemistry & Biology 2001, 8:289-299.
    • (2001) Chemistry & Biology , vol.8 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, P.N.4    Zheng, F.F.5    Sepp-Lorenzino, L.6
  • 23
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis G., Lucas B., Shtil A., Huezo H., Rosen N. Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorganic & Medicinal Chemistry 2002, 10:3555-3564.
    • (2002) Bioorganic & Medicinal Chemistry , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Lucas, B.2    Shtil, A.3    Huezo, H.4    Rosen, N.5
  • 24
    • 84857042166 scopus 로고    scopus 로고
    • A phase I dose-escalation study of the Hsp90 inhibitor ganetespib (STA-9090) administered twice weekly in patients with solid tumors: updated report
    • Abstract 3051
    • Cho D., Heath E.I., Cleary J.M., Kwak E.L., Gandhi L., Lawrence D.P., et al. A phase I dose-escalation study of the Hsp90 inhibitor ganetespib (STA-9090) administered twice weekly in patients with solid tumors: updated report. Journal of Clinical Oncology 2011, 29. Abstract 3051.
    • (2011) Journal of Clinical Oncology , vol.29
    • Cho, D.1    Heath, E.I.2    Cleary, J.M.3    Kwak, E.L.4    Gandhi, L.5    Lawrence, D.P.6
  • 25
    • 12144266330 scopus 로고    scopus 로고
    • Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation
    • Citri A., Gan J., Mosesson Y., Vereb G., Szollosi J., Yarden Y. Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation. EMBO Reports 2004, 5:1165-1170.
    • (2004) EMBO Reports , vol.5 , pp. 1165-1170
    • Citri, A.1    Gan, J.2    Mosesson, Y.3    Vereb, G.4    Szollosi, J.5    Yarden, Y.6
  • 27
    • 25844530060 scopus 로고    scopus 로고
    • Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi
    • Cowen L.E., Lindquist S. Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science 2005, 309:2185-2189.
    • (2005) Science , vol.309 , pp. 2185-2189
    • Cowen, L.E.1    Lindquist, S.2
  • 30
    • 75749122202 scopus 로고    scopus 로고
    • An investigation into the potential use of serum Hsp70 as a novel tumour biomarker for Hsp90 inhibitors
    • Dakappagari N., Neely L., Tangri S., Lundgren K., Hipolito L., Estrellado A., et al. An investigation into the potential use of serum Hsp70 as a novel tumour biomarker for Hsp90 inhibitors. Biomarkers 2010, 15:31-38.
    • (2010) Biomarkers , vol.15 , pp. 31-38
    • Dakappagari, N.1    Neely, L.2    Tangri, S.3    Lundgren, K.4    Hipolito, L.5    Estrellado, A.6
  • 31
    • 77956429649 scopus 로고    scopus 로고
    • Inhibition of Hsp90 with resorcylic acid macrolactones: synthesis and binding studies
    • Day J.E., Sharp S.Y., Rowlands M.G., Aherne W., Lewis W., Roe S.M., et al. Inhibition of Hsp90 with resorcylic acid macrolactones: synthesis and binding studies. Chemistry 2010, 16:10366-10372.
    • (2010) Chemistry , vol.16 , pp. 10366-10372
    • Day, J.E.1    Sharp, S.Y.2    Rowlands, M.G.3    Aherne, W.4    Lewis, W.5    Roe, S.M.6
  • 33
    • 37649018967 scopus 로고    scopus 로고
    • Inhibition of the Heat Shock Protein 90 (Hsp90) chaperone with the novel agent IPI-504 to overcome resistance to tyrosine kinase inhibitors (TKIs) in metastatic GIST: updated results of a phase I trial
    • Demetri G., Sledge G., Morgan J.A., Wagner A., Quigley M.T., Polson K., et al. Inhibition of the Heat Shock Protein 90 (Hsp90) chaperone with the novel agent IPI-504 to overcome resistance to tyrosine kinase inhibitors (TKIs) in metastatic GIST: updated results of a phase I trial. Journal of Clinical Oncology, ASCO Annual Meetings Proceedings Part I 2007, 25(18S):10024.
    • (2007) Journal of Clinical Oncology, ASCO Annual Meetings Proceedings Part I , vol.25 , Issue.18 S , pp. 10024
    • Demetri, G.1    Sledge, G.2    Morgan, J.A.3    Wagner, A.4    Quigley, M.T.5    Polson, K.6
  • 34
    • 61649098007 scopus 로고    scopus 로고
    • Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket
    • Donnelly A., Blagg B.S. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. Current Medicinal Chemistry 2008, 15:2702-2717.
    • (2008) Current Medicinal Chemistry , vol.15 , pp. 2702-2717
    • Donnelly, A.1    Blagg, B.S.2
  • 35
    • 34247499347 scopus 로고    scopus 로고
    • Evaluation of plasma insulin-like growth factor binding protein 2 and Her-2 extracellular domain as biomarkers for 17-allylamino-17-demethoxygeldanamycin treatment of adult patients with advanced solid tumors
    • Eiseman J.L., Guo J., Ramanathan R.K., Belani C.P., Solit D.B., Scher H.I., et al. Evaluation of plasma insulin-like growth factor binding protein 2 and Her-2 extracellular domain as biomarkers for 17-allylamino-17-demethoxygeldanamycin treatment of adult patients with advanced solid tumors. Clinical Cancer Research 2007, 13:2121-2127.
    • (2007) Clinical Cancer Research , vol.13 , pp. 2121-2127
    • Eiseman, J.L.1    Guo, J.2    Ramanathan, R.K.3    Belani, C.P.4    Solit, D.B.5    Scher, H.I.6
  • 37
    • 34249075147 scopus 로고    scopus 로고
    • MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling
    • Engelman J.A., Zejnullahu K., Mitsudomi T., Song Y., Hyland C., Park J.O., et al. MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling. Science 2007, 316:1039-1043.
    • (2007) Science , vol.316 , pp. 1039-1043
    • Engelman, J.A.1    Zejnullahu, K.2    Mitsudomi, T.3    Song, Y.4    Hyland, C.5    Park, J.O.6
  • 39
    • 33644823855 scopus 로고    scopus 로고
    • Presence of MLH1 protein aggravates the potential of the HSP90 inhibitor radicicol to sensitize tumor cells to cisplatin
    • Fedier A., Stuedli A., Fink D. Presence of MLH1 protein aggravates the potential of the HSP90 inhibitor radicicol to sensitize tumor cells to cisplatin. International Journal of Oncology 2005, 27:1697-1705.
    • (2005) International Journal of Oncology , vol.27 , pp. 1697-1705
    • Fedier, A.1    Stuedli, A.2    Fink, D.3
  • 41
    • 67649327341 scopus 로고    scopus 로고
    • Phase 1, pharmacokinetic (PK) and pharmacodynamic (PD) study of oral alvespimycin (A; KOS-1022; 17-DMAG): two different schedules in patients with advanced malignancies
    • Flaherty K., Gore L., Avadhani A., Leong S., Harlacker K., Zhong Z. Phase 1, pharmacokinetic (PK) and pharmacodynamic (PD) study of oral alvespimycin (A; KOS-1022; 17-DMAG): two different schedules in patients with advanced malignancies. Journal of Clinical Oncology 2007, 25.
    • (2007) Journal of Clinical Oncology , vol.25
    • Flaherty, K.1    Gore, L.2    Avadhani, A.3    Leong, S.4    Harlacker, K.5    Zhong, Z.6
  • 43
    • 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 L.K., Alsayed Y., Leleu X., Jia X., Singha U.K., Anderson J., et al. Combination mammalian target of rapamycin inhibitor rapamycin and HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin has synergistic activity in multiple myeloma. Clinical Cancer Research 2006, 12:6826-6835.
    • (2006) Clinical Cancer Research , vol.12 , pp. 6826-6835
    • Francis, L.K.1    Alsayed, Y.2    Leleu, X.3    Jia, X.4    Singha, U.K.5    Anderson, J.6
  • 44
    • 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 M.I., Floor K., Roepman P., Rodriguez J.A., Meijer G.A., Mooi W.J., 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 Ruiz, M.I.1    Floor, K.2    Roepman, P.3    Rodriguez, J.A.4    Meijer, G.A.5    Mooi, W.J.6
  • 45
    • 62449226171 scopus 로고    scopus 로고
    • Acquired resistance to 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) in glioblastoma cells
    • Gaspar N., Sharp S.Y., Pacey S., Jones C., Walton M., Vassal G., et al. Acquired resistance to 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin) in glioblastoma cells. Cancer Research 2009, 69:1966-1975.
    • (2009) Cancer Research , vol.69 , pp. 1966-1975
    • Gaspar, N.1    Sharp, S.Y.2    Pacey, S.3    Jones, C.4    Walton, M.5    Vassal, G.6
  • 46
    • 31544454764 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function by 17-allylamino-17-demethoxy-geldanamycin in Hodgkin's lymphoma cells down-regulates Akt kinase, dephosphorylates extracellular signal-regulated kinase, and induces cell cycle arrest and cell death
    • Georgakis G.V., Li Y., Rassidakis G.Z., Martinez-Valdez H., Medeiros L.J., Younes A. Inhibition of heat shock protein 90 function by 17-allylamino-17-demethoxy-geldanamycin in Hodgkin's lymphoma cells down-regulates Akt kinase, dephosphorylates extracellular signal-regulated kinase, and induces cell cycle arrest and cell death. Clinical Cancer Research 2006, 12:584-590.
    • (2006) Clinical Cancer Research , vol.12 , pp. 584-590
    • Georgakis, G.V.1    Li, Y.2    Rassidakis, G.Z.3    Martinez-Valdez, H.4    Medeiros, L.J.5    Younes, A.6
  • 47
    • 2442695516 scopus 로고    scopus 로고
    • Cotreatment with 17-allylamino-demethoxygeldanamycin and FLT-3 kinase inhibitor PKC412 is highly effective against human acute myelogenous leukemia cells with mutant FLT-3
    • George P., Bali P., Cohen P., Tao J., Guo F., Sigua C., et al. Cotreatment with 17-allylamino-demethoxygeldanamycin and FLT-3 kinase inhibitor PKC412 is highly effective against human acute myelogenous leukemia cells with mutant FLT-3. Cancer Research 2004, 64:3645-3652.
    • (2004) Cancer Research , vol.64 , pp. 3645-3652
    • George, P.1    Bali, P.2    Cohen, P.3    Tao, J.4    Guo, F.5    Sigua, C.6
  • 48
    • 20844444898 scopus 로고    scopus 로고
    • Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3
    • George P., Bali P., Annavarapu S., Scuto A., Fiskus W., Guo F., et al. Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3. Blood 2005, 105:1768-1776.
    • (2005) Blood , vol.105 , pp. 1768-1776
    • George, P.1    Bali, P.2    Annavarapu, S.3    Scuto, A.4    Fiskus, W.5    Guo, F.6
  • 49
    • 20044384168 scopus 로고    scopus 로고
    • Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer
    • Goetz M.P., Toft D., Reid J., Ames M., Stensgard B., Safgren S., et al. Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer. Journal of Clinical Oncology 2005, 23:1078-1087.
    • (2005) Journal of Clinical Oncology , vol.23 , pp. 1078-1087
    • Goetz, M.P.1    Toft, D.2    Reid, J.3    Ames, M.4    Stensgard, B.5    Safgren, S.6
  • 50
    • 20144375312 scopus 로고    scopus 로고
    • Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors
    • Grem J.L., Morrison G., Guo X.D., Agnew E., Takimoto C.H., Thomas R., et al. Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors. Journal of Clinical Oncology 2005, 23:1885-1893.
    • (2005) Journal of Clinical Oncology , vol.23 , pp. 1885-1893
    • Grem, J.L.1    Morrison, G.2    Guo, X.D.3    Agnew, E.4    Takimoto, C.H.5    Thomas, R.6
  • 51
    • 68249119157 scopus 로고    scopus 로고
    • Heat shock protein 27 as a new therapeutic target for radiation sensitization of head and neck squamous cell carcinoma
    • Hadchity E., Aloy M.T., Paulin C., Armandy E., Watkin E., Rousson R., et al. Heat shock protein 27 as a new therapeutic target for radiation sensitization of head and neck squamous cell carcinoma. Molecular Therapy 2009, 17:1387-1394.
    • (2009) Molecular Therapy , vol.17 , pp. 1387-1394
    • Hadchity, E.1    Aloy, M.T.2    Paulin, C.3    Armandy, E.4    Watkin, E.5    Rousson, R.6
  • 52
    • 59449108495 scopus 로고    scopus 로고
    • A phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with hormone-refractory metastatic prostate cancer
    • Heath E.I., Hillman D.W., Vaishampayan U., Sheng S., Sarkar F., Harper F., et al. A phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with hormone-refractory metastatic prostate cancer. Clinical Cancer Research 2008, 14:7940-7946.
    • (2008) Clinical Cancer Research , vol.14 , pp. 7940-7946
    • Heath, E.I.1    Hillman, D.W.2    Vaishampayan, U.3    Sheng, S.4    Sarkar, F.5    Harper, F.6
  • 54
    • 77749309983 scopus 로고    scopus 로고
    • Measuring the pharmacodynamic effects of a novel Hsp90 inhibitor on HER2/neu expression in mice using Zr-DFO-trastuzumab
    • Holland J.P., Caldas-Lopes E., Divilov V., Longo V.A., Taldone T., Zatorska D., et al. Measuring the pharmacodynamic effects of a novel Hsp90 inhibitor on HER2/neu expression in mice using Zr-DFO-trastuzumab. PLoS One 2010, 5:e8859.
    • (2010) PLoS One , vol.5
    • Holland, J.P.1    Caldas-Lopes, E.2    Divilov, V.3    Longo, V.A.4    Taldone, T.5    Zatorska, D.6
  • 55
    • 21244462689 scopus 로고    scopus 로고
    • In vivo antitumor efficacy of 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin hydrochloride), a water-soluble geldanamycin derivative
    • Hollingshead M., Alley M., Burger A.M., Borgel S., Pacula-Cox C., Fiebig H.H., et al. In vivo antitumor efficacy of 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin hydrochloride), a water-soluble geldanamycin derivative. Cancer Chemotherapy and Pharmacology 2005, 56:115-125.
    • (2005) Cancer Chemotherapy and Pharmacology , vol.56 , pp. 115-125
    • Hollingshead, M.1    Alley, M.2    Burger, A.M.3    Borgel, S.4    Pacula-Cox, C.5    Fiebig, H.H.6
  • 56
    • 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 D.O., Qin R., Stensgard B.A., Felten S., et al. Phase I study of 17-allylamino-17 demethoxygeldanamycin, gemcitabine and/or cisplatin in patients with refractory solid tumors. Investigational New Drugs 2011, 29:473-480.
    • (2011) Investigational New Drugs , vol.29 , pp. 473-480
    • Hubbard, J.1    Erlichman, C.2    Toft, D.O.3    Qin, R.4    Stensgard, B.A.5    Felten, S.6
  • 57
    • 84874021147 scopus 로고    scopus 로고
    • Infinity. A phase 1 dose escalation study of IPI-493. Available from Updated June 10, [cited; Available from .
    • Infinity. A phase 1 dose escalation study of IPI-493. Available from Updated June 10, 2011 [cited; Available from http://clinicaltrials.gov/ct2/show/NCT00724425%3fterm%3dIPI-493%26rank%3d1.
    • (2011)
  • 58
    • 77952544010 scopus 로고    scopus 로고
    • ATPase inhibitors of heat-shock protein 90, second season
    • Janin Y.L. ATPase inhibitors of heat-shock protein 90, second season. Drug Discovery Today 2010, 15:342-353.
    • (2010) Drug Discovery Today , vol.15 , pp. 342-353
    • Janin, Y.L.1
  • 59
    • 78650644709 scopus 로고    scopus 로고
    • Hsp90 and environmental stress transform the adaptive value of natural genetic variation
    • Jarosz D.F., Lindquist S. Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science 2010, 330:1820-1824.
    • (2010) Science , vol.330 , pp. 1820-1824
    • Jarosz, D.F.1    Lindquist, S.2
  • 60
    • 78149452881 scopus 로고    scopus 로고
    • Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms
    • Jarosz D.F., Taipale M., Lindquist S. Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annual Review of Genetics 2010, 44:189-216.
    • (2010) Annual Review of Genetics , vol.44 , pp. 189-216
    • Jarosz, D.F.1    Taipale, M.2    Lindquist, S.3
  • 61
    • 84874019216 scopus 로고    scopus 로고
    • A phase II trial of ganetespib: efficacy and safety in patients (pts) with metastatic breast cancer (MBC), presented at the 34th San Antonio Breast Cancer Conference in December, 2011.
    • Jhaveri, K. C. S., Lake, D., Gilewski, T., Robson, M., Goldfarb, S., Drullinsky, P., et al. (2011). A phase II trial of ganetespib: efficacy and safety in patients (pts) with metastatic breast cancer (MBC), presented at the 34th San Antonio Breast Cancer Conference in December, 2011.
    • (2011)
    • Jhaveri, K.C.S.1    Lake, D.2    Gilewski, T.3    Robson, M.4    Goldfarb, S.5    Drullinsky, P.6
  • 62
    • 84857039457 scopus 로고    scopus 로고
    • Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers
    • Jhaveri K., Taldone T., Modi S., Chiosis G. Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers. Biochimica et Biophysica Acta 2012, 1823:742-755.
    • (2012) Biochimica et Biophysica Acta , vol.1823 , pp. 742-755
    • Jhaveri, K.1    Taldone, T.2    Modi, S.3    Chiosis, G.4
  • 63
    • 84874022236 scopus 로고    scopus 로고
    • Infinity Halts RING trial in advanced gastrointestinal stromal tumors. Available from .
    • Johnston, A., Allaire, M. (2009). Infinity Halts RING trial in advanced gastrointestinal stromal tumors. Available from http://investoripicom/releasedetailcfm%3fReleaseID%3d377328.
    • (2009)
    • Johnston, A.1    Allaire, M.2
  • 64
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A., Thao L., Sensintaffar J., Zhang L., Boehm M.F., Fritz L.C., et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003, 425:407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6
  • 65
    • 80355125870 scopus 로고    scopus 로고
    • Phase I and pharmacological study of cytarabine and tanespimycin in relapsed and refractory acute leukemia
    • Kaufmann S.H., Karp J.E., Litzow M.R., Mesa R.A., Hogan W., Steensma D.P., et al. Phase I and pharmacological study of cytarabine and tanespimycin in relapsed and refractory acute leukemia. Haematologica 2011, 96:1619-1626.
    • (2011) Haematologica , vol.96 , pp. 1619-1626
    • Kaufmann, S.H.1    Karp, J.E.2    Litzow, M.R.3    Mesa, R.A.4    Hogan, W.5    Steensma, D.P.6
  • 66
    • 33750302365 scopus 로고    scopus 로고
    • Analysis of epidermal growth factor receptor gene mutation in patients with non-small cell lung cancer and acquired resistance to gefitinib
    • Kosaka T., Yatabe Y., Endoh H., Yoshida K., Hida T., Tsuboi M., et al. Analysis of epidermal growth factor receptor gene mutation in patients with non-small cell lung cancer and acquired resistance to gefitinib. Clinical Cancer Research 2006, 12:5764-5769.
    • (2006) Clinical Cancer Research , vol.12 , pp. 5764-5769
    • Kosaka, T.1    Yatabe, Y.2    Endoh, H.3    Yoshida, K.4    Hida, T.5    Tsuboi, M.6
  • 67
    • 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 M.E., Gardner E.R., Chen X., Figg W.D., Zajac-Kaye M., 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. European Journal of Cancer 2010, 46:340-347.
    • (2010) European Journal of Cancer , vol.46 , pp. 340-347
    • Kummar, S.1    Gutierrez, M.E.2    Gardner, E.R.3    Chen, X.4    Figg, W.D.5    Zajac-Kaye, M.6
  • 68
    • 33749335282 scopus 로고    scopus 로고
    • The connectivity map: using gene-expression signatures to connect small molecules, genes, and disease
    • Lamb J., Crawford E.D., Peck D., Modell J.W., Blat I.C., Wrobel M.J., et al. The connectivity map: using gene-expression signatures to connect small molecules, genes, and disease. Science 2006, 313:1929-1935.
    • (2006) Science , vol.313 , pp. 1929-1935
    • Lamb, J.1    Crawford, E.D.2    Peck, D.3    Modell, J.W.4    Blat, I.C.5    Wrobel, M.J.6
  • 69
    • 85006484740 scopus 로고    scopus 로고
    • A phase I/II trial of the potent Hsp90 inhibitor STA-9090 administered once weekly in patients with advanced hematologic malignancies
    • Abstract 3294
    • Lancet J., Smith D., Bradley R., Komrokji R.S., Teofilovici F., Rizzieri D. A phase I/II trial of the potent Hsp90 inhibitor STA-9090 administered once weekly in patients with advanced hematologic malignancies. Blood (ASH Annual Meeting Abstracts) 2010, 116. Abstract 3294.
    • (2010) Blood (ASH Annual Meeting Abstracts) , vol.116
    • Lancet, J.1    Smith, D.2    Bradley, R.3    Komrokji, R.S.4    Teofilovici, F.5    Rizzieri, D.6
  • 70
    • 77950929054 scopus 로고    scopus 로고
    • Phase I study of the heat shock protein 90 inhibitor alvespimycin (KOS-1022, 17-DMAG) administered intravenously twice weekly to patients with acute myeloid leukemia
    • Lancet J.E., Gojo I., Burton M., Quinn M., Tighe S.M., Kersey K., et al. Phase I study of the heat shock protein 90 inhibitor alvespimycin (KOS-1022, 17-DMAG) administered intravenously twice weekly to patients with acute myeloid leukemia. Leukemia 2010, 24:699-705.
    • (2010) Leukemia , vol.24 , pp. 699-705
    • Lancet, J.E.1    Gojo, I.2    Burton, M.3    Quinn, M.4    Tighe, S.M.5    Kersey, K.6
  • 71
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane A.A., Chabner B.A. Histone deacetylase inhibitors in cancer therapy. Journal of Clinical Oncology 2009, 27:5459-5468.
    • (2009) Journal of Clinical Oncology , vol.27 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 72
    • 0042337311 scopus 로고    scopus 로고
    • Synergistic effects of geldanamycin and antitumor drugs
    • Liao Z.Y., Zhang S.H., Zhen Y.S. Synergistic effects of geldanamycin and antitumor drugs. Yao xue xue bao 2001, 36:569-575.
    • (2001) Yao xue xue bao , vol.36 , pp. 569-575
    • Liao, Z.Y.1    Zhang, S.H.2    Zhen, Y.S.3
  • 73
    • 84865844011 scopus 로고    scopus 로고
    • Hsp90 inhibitors and drug resistance in cancer: the potential benefits of combination therapies of Hsp90 inhibitors and other anti-cancer drugs
    • Lu X., Xiao L., Wang L., Ruden D.M. Hsp90 inhibitors and drug resistance in cancer: the potential benefits of combination therapies of Hsp90 inhibitors and other anti-cancer drugs. Biochemical Pharmacology 2011.
    • (2011) Biochemical Pharmacology
    • Lu, X.1    Xiao, L.2    Wang, L.3    Ruden, D.M.4
  • 74
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib
    • Lynch T.J., Bell D.W., Sordella R., Gurubhagavatula S., Okimoto R.A., Brannigan B.W., et al. Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. The New England Journal of Medicine 2004, 350:2129-2139.
    • (2004) The New England Journal of Medicine , vol.350 , pp. 2129-2139
    • Lynch, T.J.1    Bell, D.W.2    Sordella, R.3    Gurubhagavatula, S.4    Okimoto, R.A.5    Brannigan, B.W.6
  • 76
    • 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 S.B., Vielhauer G.A., Manthe C.A., Chaguturu V.K., Szabla K., Matts R.L., et al. Characterization of a novel novobiocin analogue as a putative C-terminal inhibitor of heat shock protein 90 in prostate cancer cells. The Prostate 2010, 70:27-36.
    • (2010) The Prostate , vol.70 , pp. 27-36
    • Matthews, S.B.1    Vielhauer, G.A.2    Manthe, C.A.3    Chaguturu, V.K.4    Szabla, K.5    Matts, R.L.6
  • 77
    • 33845301225 scopus 로고    scopus 로고
    • Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism
    • McCollum A.K., Teneyck C.J., Sauer B.M., Toft D.O., Erlichman C. Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism. Cancer Research 2006, 66:10967-10975.
    • (2006) Cancer Research , vol.66 , pp. 10967-10975
    • McCollum, A.K.1    Teneyck, C.J.2    Sauer, B.M.3    Toft, D.O.4    Erlichman, C.5
  • 80
    • 22044437522 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibition sensitizes acute myelogenous leukemia cells to cytarabine
    • Mesa R.A., Loegering D., Powell H.L., Flatten K., Arlander S.J., Dai N.T., et al. Heat shock protein 90 inhibition sensitizes acute myelogenous leukemia cells to cytarabine. Blood 2005, 106:318-327.
    • (2005) Blood , vol.106 , pp. 318-327
    • Mesa, R.A.1    Loegering, D.2    Powell, H.L.3    Flatten, K.4    Arlander, S.J.5    Dai, N.T.6
  • 82
    • 79955668058 scopus 로고    scopus 로고
    • Biogen Idec restructures, sharpens neurology focus
    • Mitchell P. Biogen Idec restructures, sharpens neurology focus. Nature Biotechnology 2011, 29(1):7-8.
    • (2011) Nature Biotechnology , vol.29 , Issue.1 , pp. 7-8
    • Mitchell, P.1
  • 85
    • 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 A.T., Gordon M.S., Mendelson D., Solit D.B., Bagatell R., 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. Journal of Clinical Oncology 2007, 25:5410-5417.
    • (2007) Journal of Clinical Oncology , vol.25 , pp. 5410-5417
    • Modi, S.1    Stopeck, A.T.2    Gordon, M.S.3    Mendelson, D.4    Solit, D.B.5    Bagatell, R.6
  • 87
    • 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
    • abstract 590
    • Modi S., Saura C., Henderson C.A., Lin N.U., Mahtani R.L., Goddard J., 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. Journal of Clinical Oncology 2011, 29. abstract 590.
    • (2011) Journal of Clinical Oncology , vol.29
    • Modi, S.1    Saura, C.2    Henderson, C.A.3    Lin, N.U.4    Mahtani, R.L.5    Goddard, J.6
  • 88
    • 79960985354 scopus 로고    scopus 로고
    • HSP90 inhibition is effective in breast cancer: a phase 2 trial of tanespimycin (17AAG) plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab
    • Modi S., Stopeck A.T., Linden H.M., Solit D.B., Chandarlapaty S., Rosen N., et al. HSP90 inhibition is effective in breast cancer: a phase 2 trial of tanespimycin (17AAG) plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab. Clinical Cancer Research 2011.
    • (2011) Clinical Cancer Research
    • Modi, S.1    Stopeck, A.T.2    Linden, H.M.3    Solit, D.B.4    Chandarlapaty, S.5    Rosen, N.6
  • 89
    • 84865835171 scopus 로고    scopus 로고
    • A small molecule Hsp90 inhibitor provides a global overview of proteome alterations in cancer
    • Moulick K., Ahn J., Zong H., Rodina A., Chiosis G. A small molecule Hsp90 inhibitor provides a global overview of proteome alterations in cancer. Nature Chemical Biology 2011.
    • (2011) Nature Chemical Biology
    • Moulick, K.1    Ahn, J.2    Zong, H.3    Rodina, A.4    Chiosis, G.5
  • 91
    • 33751344602 scopus 로고    scopus 로고
    • HER2 therapy: molecular mechanisms of trastuzumab resistance
    • Nahta R., Esteva F.J. HER2 therapy: molecular mechanisms of trastuzumab resistance. Breast Cancer Research: BCR 2006, 8:215.
    • (2006) Breast Cancer Research: BCR , vol.8 , pp. 215
    • Nahta, R.1    Esteva, F.J.2
  • 92
    • 0034902025 scopus 로고    scopus 로고
    • Enhancement of paclitaxel-mediated cytotoxicity in lung cancer cells by 17-allylamino geldanamycin: in vitro and in vivo analysis
    • discussion 8-9
    • Nguyen D.M., Lorang D., Chen G.A., Stewart JHt, Tabibi E., Schrump D.S. Enhancement of paclitaxel-mediated cytotoxicity in lung cancer cells by 17-allylamino geldanamycin: in vitro and in vivo analysis. The Annals of Thoracic Surgery 2001, 72:371-378. discussion 8-9.
    • (2001) The Annals of Thoracic Surgery , vol.72 , pp. 371-378
    • Nguyen, D.M.1    Lorang, D.2    Chen, G.A.3    Stewart, J.4    Tabibi, E.5    Schrump, D.S.6
  • 94
    • 68949197399 scopus 로고    scopus 로고
    • Monitoring therapeutic response of human ovarian cancer to 17-DMAG by noninvasive PET imaging with (64)Cu-DOTA-trastuzumab
    • Niu G., Li Z., Cao Q., Chen X. Monitoring therapeutic response of human ovarian cancer to 17-DMAG by noninvasive PET imaging with (64)Cu-DOTA-trastuzumab. European Journal of Nuclear Medicine and Molecular Imaging 2009, 36:1510-1519.
    • (2009) European Journal of Nuclear Medicine and Molecular Imaging , vol.36 , pp. 1510-1519
    • Niu, G.1    Li, Z.2    Cao, Q.3    Chen, X.4
  • 95
    • 79957896979 scopus 로고    scopus 로고
    • The Hsp90 inhibitor IPI-504 rapidly lowers EML4-ALK levels and induces tumor regression in ALK-driven NSCLC models
    • Normant E., Paez G., West K.A., Lim A.R., Slocum K.L., Tunkey C., et al. The Hsp90 inhibitor IPI-504 rapidly lowers EML4-ALK levels and induces tumor regression in ALK-driven NSCLC models. Oncogene 2011, 30:2581-2586.
    • (2011) Oncogene , vol.30 , pp. 2581-2586
    • Normant, E.1    Paez, G.2    West, K.A.3    Lim, A.R.4    Slocum, K.L.5    Tunkey, C.6
  • 98
    • 68849125093 scopus 로고    scopus 로고
    • A single arm phase II trial of IPI-504 in patients with castration resistant prostate cancer (CRPC)
    • Abstract 219
    • Oh W., Stadler W.M., Srinivas S., Chu F., Bubley G., Quigley M., et al. A single arm phase II trial of IPI-504 in patients with castration resistant prostate cancer (CRPC). Genitourinary Cancers Symposium 2009, Abstract 219.
    • (2009) Genitourinary Cancers Symposium
    • Oh, W.1    Stadler, W.M.2    Srinivas, S.3    Chu, F.4    Bubley, G.5    Quigley, M.6
  • 100
    • 80052437758 scopus 로고    scopus 로고
    • New strategies in overcoming acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in lung cancer
    • Oxnard G.R., Arcila M.E., Chmielecki J., Ladanyi M., Miller V.A., Pao W. New strategies in overcoming acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in lung cancer. Clinical Cancer Research 2011, 17:5530-5537.
    • (2011) Clinical Cancer Research , vol.17 , pp. 5530-5537
    • Oxnard, G.R.1    Arcila, M.E.2    Chmielecki, J.3    Ladanyi, M.4    Miller, V.A.5    Pao, W.6
  • 101
    • 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 R.H., Walton M., Eatock M.M., Hardcastle A., Zetterlund A., et al. A phase I study of the heat shock protein 90 inhibitor alvespimycin (17-DMAG) given intravenously to patients with advanced solid tumors. Clinical Cancer Research 2011, 17:1561-1570.
    • (2011) Clinical Cancer Research , vol.17 , pp. 1561-1570
    • Pacey, S.1    Wilson, R.H.2    Walton, M.3    Eatock, M.M.4    Hardcastle, A.5    Zetterlund, A.6
  • 102
    • 33646488373 scopus 로고    scopus 로고
    • Targeting Hsp90 by 17-AAG in leukemia cells: mechanisms for synergistic and antagonistic drug combinations with arsenic trioxide and Ara-C
    • Pelicano H., Carew J.S., McQueen T.J., Andreeff M., Plunkett W., Keating M.J., et al. Targeting Hsp90 by 17-AAG in leukemia cells: mechanisms for synergistic and antagonistic drug combinations with arsenic trioxide and Ara-C. Leukemia 2006, 20:610-619.
    • (2006) Leukemia , vol.20 , pp. 610-619
    • Pelicano, H.1    Carew, J.S.2    McQueen, T.J.3    Andreeff, M.4    Plunkett, W.5    Keating, M.J.6
  • 103
    • 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., Goodrich A., Kong L., Grayzel D., 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, 110:678-685.
    • (2007) Blood , vol.110 , pp. 678-685
    • Peng, C.1    Brain, J.2    Hu, Y.3    Goodrich, A.4    Kong, L.5    Grayzel, D.6
  • 104
    • 35148813851 scopus 로고    scopus 로고
    • Heat shock protein 90: a potential therapeutic target in leukemic progenitor and stem cells harboring mutant BCR-ABL resistant to kinase inhibitors
    • Peng C., Li D., Li S. Heat shock protein 90: a potential therapeutic target in leukemic progenitor and stem cells harboring mutant BCR-ABL resistant to kinase inhibitors. Cell Cycle 2007, 6:2227-2231.
    • (2007) Cell Cycle , vol.6 , pp. 2227-2231
    • Peng, C.1    Li, D.2    Li, S.3
  • 105
    • 84874018549 scopus 로고    scopus 로고
    • Pfizer. Pfizer annual report. Available from [cited; Available from .
    • Pfizer. Pfizer annual report. Available from 2008. [cited; Available from http://www.pfizer.com/files/annualreport/2008/financial/financial_highlights2008.pdf.
    • (2008)
  • 106
    • 34248195608 scopus 로고    scopus 로고
    • High HSP90 expression is associated with decreased survival in breast cancer
    • Pick E., Kluger Y., Giltnane J.M., Moeder C., Camp R.L., Rimm D.L., et al. High HSP90 expression is associated with decreased survival in breast cancer. Cancer Research 2007, 67:2932-2937.
    • (2007) Cancer Research , vol.67 , pp. 2932-2937
    • Pick, E.1    Kluger, Y.2    Giltnane, J.M.3    Moeder, C.4    Camp, R.L.5    Rimm, D.L.6
  • 107
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: biology and pharmacology
    • Powers M.V., Workman P. Inhibitors of the heat shock response: biology and pharmacology. FEBS Letters 2007, 581:3758-3769.
    • (2007) FEBS Letters , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 108
    • 77953576838 scopus 로고    scopus 로고
    • Targeting HSP70: the second potentially druggable heat shock protein and molecular chaperone?
    • Powers M.V., Jones K., Barillari C., Westwood I., van Montfort R.L., Workman P. Targeting HSP70: the second potentially druggable heat shock protein and molecular chaperone?. Cell Cycle 2010, 9:1542-1550.
    • (2010) Cell Cycle , vol.9 , pp. 1542-1550
    • Powers, M.V.1    Jones, K.2    Barillari, C.3    Westwood, I.4    van Montfort, R.L.5    Workman, P.6
  • 109
    • 84874018776 scopus 로고    scopus 로고
    • Press Release. F. Kosan announces senior management changes and clinical portfolio priorities. Available from. [cited; Available from .
    • Press Release. F. Kosan announces senior management changes and clinical portfolio priorities. Available from 2008. [cited; Available from http://phx.corporate-ir.net/phoenix.zhtml%3fc%3d121014%26p%3dirol-newsArticle%26ID%3d1113760%26highlight%3d.
    • (2008)
  • 110
    • 84874020881 scopus 로고    scopus 로고
    • PressRelease. Bristol-Myers Squibb Halts development of tanespimycin. Available from. [cited; Available from .
    • PressRelease. Bristol-Myers Squibb Halts development of tanespimycin. Available from 2008. [cited; Available from http://www.myelomabeacon.com/news/2010/07/22/tanespimycin-development-halted/.
    • (2008)
  • 111
    • 0141596939 scopus 로고    scopus 로고
    • Structure and functional relationships of Hsp90
    • Prodromou C., Pearl L.H. Structure and functional relationships of Hsp90. Current Cancer Drug Targets 2003, 3:301-323.
    • (2003) Current Cancer Drug Targets , vol.3 , pp. 301-323
    • Prodromou, C.1    Pearl, L.H.2
  • 113
    • 0345734267 scopus 로고    scopus 로고
    • Coadministration of the heat shock protein 90 antagonist 17-allylamino- 17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells
    • Rahmani M., Yu C., Dai Y., Reese E., Ahmed W., Dent P., et al. Coadministration of the heat shock protein 90 antagonist 17-allylamino- 17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells. Cancer Research 2003, 63:8420-8427.
    • (2003) Cancer Research , vol.63 , pp. 8420-8427
    • Rahmani, M.1    Yu, C.2    Dai, Y.3    Reese, E.4    Ahmed, W.5    Dent, P.6
  • 114
    • 80455162319 scopus 로고    scopus 로고
    • A phase I study of PF-04929113 (SNX-5422), an orally bioavailable heat shock protein 90 inhibitor, in patients with refractory solid tumor malignancies and lymphomas
    • Rajan A., Kelly R.J., Trepel J.B., Kim Y.S., Alarcon S.V., Kummar S., et al. A phase I study of PF-04929113 (SNX-5422), an orally bioavailable heat shock protein 90 inhibitor, in patients with refractory solid tumor malignancies and lymphomas. Clinical Cancer Research 2011, 17:6831-6839.
    • (2011) Clinical Cancer Research , vol.17 , pp. 6831-6839
    • Rajan, A.1    Kelly, R.J.2    Trepel, J.B.3    Kim, Y.S.4    Alarcon, S.V.5    Kummar, S.6
  • 115
    • 50349093362 scopus 로고    scopus 로고
    • A phase I study of 17-allylamino-17-demethoxygeldanamycin combined with paclitaxel in patients with advanced solid malignancies
    • Ramalingam S.S., Egorin M.J., Ramanathan R.K., Remick S.C., Sikorski R.P., Lagattuta T.F., et al. A phase I study of 17-allylamino-17-demethoxygeldanamycin combined with paclitaxel in patients with advanced solid malignancies. Clinical Cancer Research 2008, 14:3456-3461.
    • (2008) Clinical Cancer Research , vol.14 , pp. 3456-3461
    • Ramalingam, S.S.1    Egorin, M.J.2    Ramanathan, R.K.3    Remick, S.C.4    Sikorski, R.P.5    Lagattuta, T.F.6
  • 116
    • 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 R.K., Trump D.L., Eiseman J.L., Belani C.P., Agarwala S.S., Zuhowski E.G., 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. Clinical Cancer Research 2005, 11:3385-3391.
    • (2005) Clinical Cancer Research , vol.11 , pp. 3385-3391
    • Ramanathan, R.K.1    Trump, D.L.2    Eiseman, J.L.3    Belani, C.P.4    Agarwala, S.S.5    Zuhowski, E.G.6
  • 117
    • 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 R.K., Egorin M.J., Erlichman C., Remick S.C., Ramalingam S.S., Naret 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. Journal of Clinical Oncology 2010, 28:1520-1526.
    • (2010) Journal of Clinical Oncology , vol.28 , pp. 1520-1526
    • Ramanathan, R.K.1    Egorin, M.J.2    Erlichman, C.3    Remick, S.C.4    Ramalingam, S.S.5    Naret, C.6
  • 119
    • 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., Aguirre J., Kim J., Chiang A., et al. Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer. Nature Chemical Biology 2007, 3:498-507.
    • (2007) Nature Chemical Biology , vol.3 , pp. 498-507
    • Rodina, A.1    Vilenchik, M.2    Moulick, K.3    Aguirre, J.4    Kim, J.5    Chiang, A.6
  • 120
    • 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 M.M., Tan C. Combination of rapamycin and 17-allylamino-17-demethoxygeldanamycin abrogates Akt activation and potentiates mTOR blockade in breast cancer cells. Anticancer Drugs 2008, 19:681-688.
    • (2008) Anticancer Drugs , vol.19 , pp. 681-688
    • Roforth, M.M.1    Tan, C.2
  • 121
    • 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 E., Kondagunta G., Ishill N., Sweeney S., DeLuca J., Schwartz L., et al. A phase II trial of 17-(Allylamino)-17-demethoxygeldanamycin in patients with papillary and clear cell renal cell carcinoma. Investigational New Drugs 2006, 24:543-546.
    • (2006) Investigational New Drugs , vol.24 , pp. 543-546
    • Ronnen, E.1    Kondagunta, G.2    Ishill, N.3    Sweeney, S.4    DeLuca, J.5    Schwartz, L.6
  • 122
    • 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 B.J. The Hsp90 capacitor, developmental remodeling, and evolution: the robustness of gene networks and the curious evolvability of metamorphosis. Critical Reviews in Biochemistry and Molecular Biology 2007, 42:355-372.
    • (2007) Critical Reviews in Biochemistry and Molecular Biology , vol.42 , pp. 355-372
    • Rutherford, S.1    Hirate, Y.2    Swalla, B.J.3
  • 123
    • 79960983822 scopus 로고    scopus 로고
    • AUY922, a novel HSP90 inhibitor: final results of a first-in-human study in patients with advanced solid malignancies
    • Abstract 2528
    • Samuel T., Sessa C., Britten C., Milligan K.S., Mita M.M., Banerji U., et al. AUY922, a novel HSP90 inhibitor: final results of a first-in-human study in patients with advanced solid malignancies. Journal of Clinical Oncology 2010, 28. Abstract 2528.
    • (2010) Journal of Clinical Oncology , vol.28
    • Samuel, T.1    Sessa, C.2    Britten, C.3    Milligan, K.S.4    Mita, M.M.5    Banerji, U.6
  • 124
    • 0034982174 scopus 로고    scopus 로고
    • Radicicol and geldanamycin prevent neurotoxic effects of anti-cancer drugs on cultured embryonic sensory neurons
    • Sano M. Radicicol and geldanamycin prevent neurotoxic effects of anti-cancer drugs on cultured embryonic sensory neurons. Neuropharmacology 2001, 40:947-953.
    • (2001) Neuropharmacology , vol.40 , pp. 947-953
    • Sano, M.1
  • 125
  • 126
    • 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
    • Schroder C., Pederson J.V., Chua S., Swanton C., Akimov M., Ide 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. Journal of Clinical Oncology 2011, 29.
    • (2011) Journal of Clinical Oncology , pp. 29
    • Schroder, C.1    Pederson, J.V.2    Chua, S.3    Swanton, C.4    Akimov, M.5    Ide, S.6
  • 127
  • 128
    • 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 L.V., Gettinger S., Senzer N.N., Martins R.G., Jänne P.A., Lilenbaum R., et al. Activity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer. Journal of Clinical Oncology 2010, 28:4953-4960.
    • (2010) Journal of Clinical Oncology , vol.28 , pp. 4953-4960
    • Sequist, L.V.1    Gettinger, S.2    Senzer, N.N.3    Martins, R.G.4    Jänne, P.A.5    Lilenbaum, R.6
  • 129
    • 73149102557 scopus 로고    scopus 로고
    • KU135, a novel novobiocin-derived C-terminal inhibitor of the 90-kDa heat shock protein, exerts potent antiproliferative effects in human leukemic cells
    • Shelton S.N., Shawgo M.E., Matthews S.B., Lu Y., Donnelly A.C., Szabla K., et al. KU135, a novel novobiocin-derived C-terminal inhibitor of the 90-kDa heat shock protein, exerts potent antiproliferative effects in human leukemic cells. Molecular Pharmacology 2009, 76:1314-1322.
    • (2009) Molecular Pharmacology , vol.76 , pp. 1314-1322
    • Shelton, S.N.1    Shawgo, M.E.2    Matthews, S.B.3    Lu, Y.4    Donnelly, A.C.5    Szabla, K.6
  • 130
    • 44649083135 scopus 로고    scopus 로고
    • Hsp90 inhibition suppresses mutant EGFR-T790M signaling and overcomes kinase inhibitor resistance
    • Shimamura T., Li D., Ji H., Haringsma H.J., Liniker E., Borgman C.L., et al. Hsp90 inhibition suppresses mutant EGFR-T790M signaling and overcomes kinase inhibitor resistance. Cancer Research 2008, 68:5827-5838.
    • (2008) Cancer Research , vol.68 , pp. 5827-5838
    • Shimamura, T.1    Li, D.2    Ji, H.3    Haringsma, H.J.4    Liniker, E.5    Borgman, C.L.6
  • 131
    • 0034665760 scopus 로고    scopus 로고
    • Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex
    • Shiotsu Y., Neckers L.M., Wortman I., An W.G., Schulte T.W., Soga S., et al. Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex. Blood 2000, 96:2284-2291.
    • (2000) Blood , vol.96 , pp. 2284-2291
    • Shiotsu, Y.1    Neckers, L.M.2    Wortman, I.3    An, W.G.4    Schulte, T.W.5    Soga, S.6
  • 132
    • 58249137998 scopus 로고    scopus 로고
    • 17-AAG sensitized malignant glioma cells to death-receptor mediated apoptosis
    • Siegelin M.D., Habel A., Gaiser T. 17-AAG sensitized malignant glioma cells to death-receptor mediated apoptosis. Neurobiology of Disease 2009, 33:243-249.
    • (2009) Neurobiology of Disease , vol.33 , pp. 243-249
    • Siegelin, M.D.1    Habel, A.2    Gaiser, T.3
  • 136
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to taxol
    • Solit D.B., Basso A.D., Olshen A.B., Scher H.I., Rosen N. Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to taxol. Cancer Research 2003, 63:2139-2144.
    • (2003) Cancer Research , vol.63 , pp. 2139-2144
    • Solit, D.B.1    Basso, A.D.2    Olshen, A.B.3    Scher, H.I.4    Rosen, N.5
  • 138
    • 58149340657 scopus 로고    scopus 로고
    • Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma
    • Solit D., Osman I., Polsky D., Panageas K., Daud A., Goydos J., et al. Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma. Clinical Cancer Research 2008, 14:8302-8307.
    • (2008) Clinical Cancer Research , vol.14 , pp. 8302-8307
    • Solit, D.1    Osman, I.2    Polsky, D.3    Panageas, K.4    Daud, A.5    Goydos, J.6
  • 139
    • 0023681189 scopus 로고
    • Mechanism of cis-diamminedichloroplatinum(II)-induced cytotoxicity: role of G2 arrest and DNA double-strand breaks
    • Sorenson C.M., Eastman A. Mechanism of cis-diamminedichloroplatinum(II)-induced cytotoxicity: role of G2 arrest and DNA double-strand breaks. Cancer Research 1988, 48:4484-4488.
    • (1988) Cancer Research , vol.48 , pp. 4484-4488
    • Sorenson, C.M.1    Eastman, A.2
  • 140
    • 70349921403 scopus 로고    scopus 로고
    • Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol
    • Sreeramulu S., Gande S.L., Gobel M., Schwalbe H. Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol. Angewandte Chemie International Edition 2009, 48:5853-5855.
    • (2009) Angewandte Chemie International Edition , vol.48 , pp. 5853-5855
    • Sreeramulu, S.1    Gande, S.L.2    Gobel, M.3    Schwalbe, H.4
  • 141
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
    • Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997, 89:239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 142
    • 62149135294 scopus 로고    scopus 로고
    • Discovery and development of heat shock protein 90 inhibitors
    • Taldone T., Sun W., Chiosis G. Discovery and development of heat shock protein 90 inhibitors. Bioorganic & Medicinal Chemistry 2009, 17:2225-2235.
    • (2009) Bioorganic & Medicinal Chemistry , vol.17 , pp. 2225-2235
    • Taldone, T.1    Sun, W.2    Chiosis, G.3
  • 143
    • 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, 30:2789-2797.
    • (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
  • 144
    • 58149180924 scopus 로고    scopus 로고
    • A phase 1 dose-escalation study of irinotecan in combination with 17-allylamino-17-demethoxygeldanamycin in patients with solid tumors
    • Tse A.N., Klimstra D.S., Gonen M., Shah M., Sheikh T., Sikorski R., et al. A phase 1 dose-escalation study of irinotecan in combination with 17-allylamino-17-demethoxygeldanamycin in patients with solid tumors. Clinical Cancer Research 2008, 14:6704-6711.
    • (2008) Clinical Cancer Research , vol.14 , pp. 6704-6711
    • Tse, A.N.1    Klimstra, D.S.2    Gonen, M.3    Shah, M.4    Sheikh, T.5    Sikorski, R.6
  • 146
    • 0038069088 scopus 로고    scopus 로고
    • Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of Cisplatin in human colon adenocarcinoma cells: differential caspase activation as a basis for interaction
    • Vasilevskaya I.A., Rakitina T.V., O'Dwyer P.J. Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of Cisplatin in human colon adenocarcinoma cells: differential caspase activation as a basis for interaction. Cancer Research 2003, 63:3241-3246.
    • (2003) Cancer Research , vol.63 , pp. 3241-3246
    • Vasilevskaya, I.A.1    Rakitina, T.V.2    O'Dwyer, P.J.3
  • 147
    • 1642576969 scopus 로고    scopus 로고
    • Quantitative effects on c-Jun N-terminal protein kinase signaling determine synergistic interaction of cisplatin and 17-allylamino-17-demethoxygeldanamycin in colon cancer cell lines
    • Vasilevskaya I.A., Rakitina T.V., O'Dwyer P.J. Quantitative effects on c-Jun N-terminal protein kinase signaling determine synergistic interaction of cisplatin and 17-allylamino-17-demethoxygeldanamycin in colon cancer cell lines. Molecular Pharmacology 2004, 65:235-243.
    • (2004) Molecular Pharmacology , vol.65 , pp. 235-243
    • Vasilevskaya, I.A.1    Rakitina, T.V.2    O'Dwyer, P.J.3
  • 148
    • 3042553538 scopus 로고    scopus 로고
    • Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90
    • Vilenchik M., Solit D., Basso A., Huezo H., Lucas B., He H., et al. Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90. Chemistry & Biology 2004, 11:787-797.
    • (2004) Chemistry & Biology , vol.11 , pp. 787-797
    • Vilenchik, M.1    Solit, D.2    Basso, A.3    Huezo, H.4    Lucas, B.5    He, H.6
  • 149
    • 44449177914 scopus 로고    scopus 로고
    • An evolutionary model for initiation, promotion, and progression in carcinogenesis
    • Vincent T.L., Gatenby R.A. An evolutionary model for initiation, promotion, and progression in carcinogenesis. International Journal of Oncology 2008, 32:729-737.
    • (2008) International Journal of Oncology , vol.32 , pp. 729-737
    • Vincent, T.L.1    Gatenby, R.A.2
  • 150
    • 14044278635 scopus 로고    scopus 로고
    • Tumor therapeutics by design: targeting and activation of death receptors
    • Wajant H., Gerspach J., Pfizenmaier K. Tumor therapeutics by design: targeting and activation of death receptors. Cytokine & Growth Factor Reviews 2005, 16:55-76.
    • (2005) Cytokine & Growth Factor Reviews , vol.16 , pp. 55-76
    • Wajant, H.1    Gerspach, J.2    Pfizenmaier, K.3
  • 151
    • 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 B.J., Blaney S.M., Reid J.M., Safgren S.L., Bagatell R., Kersey J., et al. A phase I study of 17-allylaminogeldanamycin in relapsed/refractory pediatric patients with solid tumors: a children's oncology group study. Clinical Cancer Research 2007, 13:1789-1793.
    • (2007) Clinical Cancer Research , vol.13 , pp. 1789-1793
    • Weigel, B.J.1    Blaney, S.M.2    Reid, J.M.3    Safgren, S.L.4    Bagatell, R.5    Kersey, J.6
  • 153
    • 84857050136 scopus 로고    scopus 로고
    • HSP90 as a platform for the assembly of more effective cancer chemotherapy
    • Whitesell L., Lin N.U. HSP90 as a platform for the assembly of more effective cancer chemotherapy. Biochimica et Biophysica Acta 2012, 1823:756-766.
    • (2012) Biochimica et Biophysica Acta , vol.1823 , pp. 756-766
    • Whitesell, L.1    Lin, N.U.2
  • 156
    • 34548490977 scopus 로고    scopus 로고
    • Intratumor injection of the Hsp90 inhibitor 17AAG decreases tumor growth and induces apoptosis in a prostate cancer xenograft model
    • Williams C.R., Tabios R., Linehan W.M., Neckers L. Intratumor injection of the Hsp90 inhibitor 17AAG decreases tumor growth and induces apoptosis in a prostate cancer xenograft model. Journal of Urology 2007, 178:1528-1532.
    • (2007) Journal of Urology , vol.178 , pp. 1528-1532
    • Williams, C.R.1    Tabios, R.2    Linehan, W.M.3    Neckers, L.4
  • 157
    • 72249088988 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors: new mode of therapy to overcome endocrine resistance
    • Wong C., Chen S. Heat shock protein 90 inhibitors: new mode of therapy to overcome endocrine resistance. Cancer Research 2009, 69:8670-8677.
    • (2009) Cancer Research , vol.69 , pp. 8670-8677
    • Wong, C.1    Chen, S.2
  • 158
    • 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. Annals of the New York Academy of Sciences 2007, 1113:202-216.
    • (2007) Annals of the New York Academy of Sciences , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 159
    • 33746899628 scopus 로고    scopus 로고
    • Association with HSP90 inhibits Cbl-mediated down-regulation of mutant epidermal growth factor receptors
    • Yang S., Qu S., Perez-Tores M., Sawai A., Rosen N., Solit D.B., et al. Association with HSP90 inhibits Cbl-mediated down-regulation of mutant epidermal growth factor receptors. Cancer Research 2006, 66:6990-6997.
    • (2006) Cancer Research , vol.66 , pp. 6990-6997
    • Yang, S.1    Qu, S.2    Perez-Tores, M.3    Sawai, A.4    Rosen, N.5    Solit, D.B.6
  • 161
    • 0141925960 scopus 로고    scopus 로고
    • FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases
    • Yao Q., Nishiuchi R., Li Q., Kumar A.R., Hudson W.A., Kersey J.H. FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases. Clinical Cancer Research 2003, 9:4483-4493.
    • (2003) Clinical Cancer Research , vol.9 , pp. 4483-4493
    • Yao, Q.1    Nishiuchi, R.2    Li, Q.3    Kumar, A.R.4    Hudson, W.A.5    Kersey, J.H.6
  • 163
    • 74049091229 scopus 로고    scopus 로고
    • BIIB021, a novel Hsp90 inhibitor, sensitizes head and neck squamous cell carcinoma to radiotherapy
    • Yin X., Zhang H., Lundgren K., Wilson L., Burrows F., Shores C.G. BIIB021, a novel Hsp90 inhibitor, sensitizes head and neck squamous cell carcinoma to radiotherapy. International Journal of Cancer 2010, 126:1216-1225.
    • (2010) International Journal of Cancer , vol.126 , pp. 1216-1225
    • Yin, X.1    Zhang, H.2    Lundgren, K.3    Wilson, L.4    Burrows, F.5    Shores, C.G.6
  • 164
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • Zhang H., Burrows F. Targeting multiple signal transduction pathways through inhibition of Hsp90. Journal of Molecular Medicine (Berlin) 2004, 82:488-499.
    • (2004) Journal of Molecular Medicine (Berlin) , vol.82 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 166
    • 38349153572 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells
    • Zhang T., Hamza A., Cao X., Wang B., Yu S., Zhan C.G., et al. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Molecular Cancer Therapeutics 2008, 7:162-170.
    • (2008) Molecular Cancer Therapeutics , vol.7 , pp. 162-170
    • Zhang, T.1    Hamza, A.2    Cao, X.3    Wang, B.4    Yu, S.5    Zhan, C.G.6
  • 167
    • 77955138765 scopus 로고    scopus 로고
    • Prevention and treatment of bortezemib-induced peripheral neuropathy by the Hsp90 inhibitor tanespimycin (KOS-953) in the rat
    • Zhong Z., Simmons J., Timmermans P. Prevention and treatment of bortezemib-induced peripheral neuropathy by the Hsp90 inhibitor tanespimycin (KOS-953) in the rat. European Journal of Cancer Supplements 2008, 6:23.
    • (2008) European Journal of Cancer Supplements , vol.6 , pp. 23
    • Zhong, Z.1    Simmons, J.2    Timmermans, P.3
  • 168
    • 35948950583 scopus 로고    scopus 로고
    • Cooperative interactions between androgen receptor (AR) and heat-shock protein 27 facilitate AR transcriptional activity
    • Zoubeidi A., Zardan A., Beraldi E., Fazli L., Sowery R., Rennie P., et al. Cooperative interactions between androgen receptor (AR) and heat-shock protein 27 facilitate AR transcriptional activity. Cancer Research 2007, 67:10455-10465.
    • (2007) Cancer Research , vol.67 , pp. 10455-10465
    • Zoubeidi, A.1    Zardan, A.2    Beraldi, E.3    Fazli, L.4    Sowery, R.5    Rennie, P.6
  • 169
    • 75149177573 scopus 로고    scopus 로고
    • Hsp90 and co-chaperones twist the functions of diverse client proteins
    • Zuehlke A., Johnson J.L. Hsp90 and co-chaperones twist the functions of diverse client proteins. Biopolymers 2010, 93:211-217.
    • (2010) Biopolymers , vol.93 , pp. 211-217
    • Zuehlke, A.1    Johnson, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.