메뉴 건너뛰기




Volumn 6, Issue 5, 2011, Pages 559-587

Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment

Author keywords

cancer; chaperone; heat shock protein 90; targeted therapy

Indexed keywords

3 (5 CHLORO 2,4 DIHYDROXYPHENYL) N ETHYL 4 (4 METHOXYPHENYL) 5 PYRAZOLECARBOXAMIDE; 4 [4 (1,4 BENZODIOXAN 6 YL) 5 METHYL 1H PYRAZOL 3 YL] 6 ETHYLRESORCINOL; 5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; ADENOSINE TRIPHOSPHATASE; ALVESPIMYCIN; ANSAMYCIN DERIVATIVE; AT 13387; BIBB 021; BULGARIALACTONE B; CISPLATIN; CNF 2024; CUDC 305; CYCLOPROPARADICICOL; EPIGALLOCATECHIN GALLATE; G 3129; G 3130; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HERBIMYCIN B; KF 25706; KW 2478; MACBECIN I; NVP BEP800; PU 24FCL; PU 3; PU H 71; RADICICOL; RETASPIMYCIN; TANESPIMYCIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 79955432735     PISSN: 17460441     EISSN: None     Source Type: Journal    
DOI: 10.1517/17460441.2011.563296     Document Type: Review
Times cited : (78)

References (119)
  • 1
    • 77954945333 scopus 로고    scopus 로고
    • Targeting the dynamic HSP90 complex in cancer
    • Trepel J, Mollapour M, Giaccone G, et al. Targeting the dynamic HSP90 complex in cancer. Nat Rev Cancer 2010;10:537-49
    • (2010) Nat Rev Cancer , vol.10 , pp. 537-49
    • Trepel, J.1    Mollapour, M.2    Giaccone, G.3
  • 2
    • 77952551024 scopus 로고    scopus 로고
    • Discovery and development of Hsp90 inhibitors: A promising pathway for cancer therapy
    • Porter JR, Fritz CC, Depew KM. Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy. Curr Opin Chem Biol 2010;14:412-20
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 412-20
    • Porter, J.R.1    Fritz, C.C.2    Depew, K.M.3
  • 3
    • 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. 515-28
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 4
    • 61949349758 scopus 로고    scopus 로고
    • Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
    • Hessling M, Richter K, Buchner J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat Struct Mol Biol 2009;16:287-93
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 287-93
    • Hessling, M.1    Richter, K.2    Buchner, J.3
  • 5
    • 61949212626 scopus 로고    scopus 로고
    • The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
    • Mickler M, Hessling M, Ratzke C, et al. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat Struct Mol Biol 2009;16:281-6
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 281-6
    • Mickler, M.1    Hessling, M.2    Ratzke, C.3
  • 6
    • 42949147146 scopus 로고    scopus 로고
    • Multiple conformations of E. coli Hsp90 in solution: Insights into the conformational dynamics of Hsp90
    • DOI 10.1016/j.str.2008.01.021, PII S096921260800110X
    • Krukenberg KA, Forster F, Rice LM, et al. Multiple conformations of E. coli Hsp90 in solution: Insights into the conformational dynamics of Hsp90. Structure 2008;16:755-65 (Pubitemid 351615019)
    • (2008) Structure , vol.16 , Issue.5 , pp. 755-765
    • Krukenberg, K.A.1    Forster, F.2    Rice, L.M.3    Sali, A.4    Agard, D.A.5
  • 7
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • Mayer MP. Gymnastics of molecular chaperones. Mol Cell 2010;39:321-31
    • (2010) Mol Cell , vol.39 , pp. 321-31
    • Mayer, M.P.1
  • 8
    • 33746705661 scopus 로고    scopus 로고
    • Chaperoning steroid hormone action
    • DOI 10.1016/j.tem.2006.06.003, PII S1043276006001007
    • Picard D. Chaperoning steroid hormone action. Trends Endocrinol Metab 2006;17:229-35 (Pubitemid 44164280)
    • (2006) Trends in Endocrinology and Metabolism , vol.17 , Issue.6 , pp. 229-235
    • Picard, D.1
  • 9
    • 49649113716 scopus 로고    scopus 로고
    • Conserved conformational changes in the ATPase cycle of human hsp90
    • Richter K, Soroka J, Skalniak L, et al. Conserved conformational changes in the ATPase cycle of human hsp90. J Biol Chem 2008;283:17757-65
    • (2008) J Biol Chem , vol.283 , pp. 17757-65
    • Richter, K.1    Soroka, J.2    Skalniak, L.3
  • 10
    • 0035839576 scopus 로고    scopus 로고
    • Stoichiometry, abundance, and functional significance of the Hsp90/Hsp70-based multiprotein chaperone machinery in reticulocyte lysate
    • Murphy PJ, Kanelakis KC, Galigniana MD, et al. Stoichiometry, abundance, and functional significance of the Hsp90/Hsp70-based multiprotein chaperone machinery in reticulocyte lysate. J Biol Chem 2001;276:30092-8
    • (2001) J Biol Chem , vol.276 , pp. 30092-8
    • Murphy, P.J.1    Kanelakis, K.C.2    Galigniana, M.D.3
  • 12
    • 33750008686 scopus 로고    scopus 로고
    • Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • DOI 10.1016/j.cell.2006.09.027, PII S009286740601275X
    • Shiau AK, Harris SF, Southworth DR, et al. Structural analysis of E. coli Hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006;127:329-40 (Pubitemid 44572381)
    • (2006) Cell , vol.127 , Issue.2 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 13
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali MMU, Roe SM, Vaughan CK, et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006;440:1013-17
    • (2006) Nature , vol.440 , pp. 1013-17
    • Mmu, A.1    Roe, S.M.2    Vaughan, C.K.3
  • 14
    • 34948893963 scopus 로고    scopus 로고
    • Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones
    • DOI 10.1016/j.molcel.2007.08.024, PII S1097276507005941
    • Dollins DE, Warren JJ, Immormino RM, et al. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the Hsp90 chaperones. Mol Cell 2007;28:41-56 (Pubitemid 47531972)
    • (2007) Molecular Cell , vol.28 , Issue.1 , pp. 41-56
    • Dollins, D.E.1    Warren, J.J.2    Immormino, R.M.3    Gewirth, D.T.4
  • 15
  • 18
    • 0035823582 scopus 로고    scopus 로고
    • Coordinated ATP hydrolysis by the Hsp90 dimer
    • Richter K, Muschler P, Hainzl O, et al. Coordinated ATP Hydrolysis by the Hsp90 Dimer. J Biol Chem 2001;276:33689-96
    • (2001) J Biol Chem , vol.276 , pp. 33689-96
    • Richter, K.1    Muschler, P.2    Hainzl, O.3
  • 21
    • 44349097402 scopus 로고    scopus 로고
    • Structural studies on the co-chaperone Hop and its complexes with Hsp90
    • Onuoha SC, Coulstock ET, Grossmann JG, et al. Structural studies on the co-chaperone Hop and its complexes with Hsp90. J Mol Biol 2008;379:732-44
    • (2008) J Mol Biol , vol.379 , pp. 732-44
    • Onuoha, S.C.1    Coulstock, E.T.2    Grossmann, J.G.3
  • 22
    • 75949106173 scopus 로고    scopus 로고
    • Asymmetric activation of the Hsp90 dimer by its cochaperone aha1
    • Retzlaff M, Hagn F, Mitschke L, et al. Asymmetric activation of the Hsp90 dimer by its cochaperone aha1. Mol Cell 2010 37:344-54
    • Mol Cell , vol.2010 , Issue.37 , pp. 344-54
    • Retzlaff, M.1    Hagn, F.2    Mitschke, L.3
  • 23
    • 33747878717 scopus 로고    scopus 로고
    • Structure of an Hsp90-Cdc37-Cdk4 complex
    • Vaughan CK, Gohlke U, Sobott F, et al. Structure of an Hsp90-Cdc37-Cdk4 complex. Mol Cell 2006;23:697-707
    • (2006) Mol Cell , vol.23 , pp. 697-707
    • Vaughan, C.K.1    Gohlke, U.2    Sobott, F.3
  • 24
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37 - A chaperone cancer conspiracy
    • DOI 10.1016/j.gde.2004.12.011, PII S0959437X04001972, Oncogenes and Cell Proliferation
    • Pearl LH. Hsp90 and Cdc37-a chaperone cancer conspiracy. Curr Opin Genet Dev 2005;15:55-61 (Pubitemid 40127632)
    • (2005) Current Opinion in Genetics and Development , vol.15 , Issue.1 , pp. 55-61
    • Pearl, L.H.1
  • 25
    • 74249085361 scopus 로고    scopus 로고
    • Update on Hsp90 inhibitors in clinical trial
    • Kim YS, Alarcon SV, Lee S, et al. Update on Hsp90 inhibitors in clinical trial. Curr Top Med Chem 2009;9:1479-92
    • (2009) Curr Top Med Chem , vol.9 , pp. 1479-92
    • Kim, Y.S.1    Alarcon, S.V.2    Lee, S.3
  • 28
    • 61649098007 scopus 로고    scopus 로고
    • Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket
    • Donnelly A, Blagg BSJ. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. Curr Med Chem 2008;15:2702-17
    • (2008) Curr Med Chem , vol.15 , pp. 2702-17
    • Donnelly, A.1    Bsj, B.2
  • 29
    • 0022967572 scopus 로고
    • Phenotypic change from transformed to normal induced by benzoquinonoid ansamycins accompanies inactivation of p60(src) in rat kidney cells infected with Rous sarcoma virus
    • Uehara Y, Hori M, Takeuchi T, et al. Phenotypic change from transformed to normal induced by benzoquinonoid ansamycins accompanies inactivation of p60src in rat kidney cells infected with Rous sarcoma virus. Mol Cell Biol 1986;6:2198-206 (Pubitemid 17189579)
    • (1986) Molecular and Cellular Biology , vol.6 , Issue.6 , pp. 2198-2206
    • Uehara, Y.1    Hori, M.2    Takeuchi, T.3    Umezawa, H.4
  • 30
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De Costa B, et al. Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 1994;91:8324-8
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3
  • 31
    • 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. Bioorg Med Chem 2009;17:2225-35
    • (2009) Bioorg Med Chem , vol.17 , pp. 2225-35
    • Taldone, T.1    Sun, W.2    Chiosis, G.3
  • 33
    • 77749270556 scopus 로고    scopus 로고
    • Hsp90 inhibitors: Clinical development and future opportunities in oncology therapy
    • Gao Z, Garcia-Echeverria C, Jensen MR. Hsp90 inhibitors: clinical development and future opportunities in oncology therapy. Curr Opin Drug Discovery Dev 2010;13:193-202
    • (2010) Curr Opin Drug Discovery Dev , vol.13 , pp. 193-202
    • Gao, Z.1    Garcia-Echeverria, C.2    Jensen, M.R.3
  • 34
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • DOI 10.1021/jm980403y
    • Roe SM, Prodromou C, OBrien R, et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 1999;42:260-6 (Pubitemid 29069861)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.2 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 35
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, et al. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997;89:239-50 (Pubitemid 27199896)
    • (1997) Cell , vol.89 , Issue.2 , 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
  • 36
    • 33645975518 scopus 로고    scopus 로고
    • Chaperoning oncogenes: Hsp90 as a target of geldanamycin
    • Neckers L. Chaperoning oncogenes: Hsp90 as a target of geldanamycin. Handb Exp Pharmacol 2006;172:259-77
    • (2006) Handb Exp Pharmacol , vol.172 , pp. 259-77
    • Neckers, L.1
  • 37
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185(c-erbB-2) receptor protein-tyrosine kinase induced by geldanamycin
    • DOI 10.1074/jbc.271.37.22796
    • Mimnaugh EG, Chavany C, Neckers L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 1996;271:22796-801 (Pubitemid 26304727)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 38
    • 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
    • DOI 10.1016/S1074-5521(01)00015-1, PII S1074552101000151
    • Chiosis G, Timaul MN, Lucas B, 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. Chem Biol 2001;8:289-99 (Pubitemid 32296118)
    • (2001) Chemistry and Biology , vol.8 , Issue.3 , 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    Rosen, N.7
  • 39
    • 74249105371 scopus 로고    scopus 로고
    • Purine-scaffold Hsp90 inhibitors
    • Taldone T, Chiosis G. Purine-scaffold Hsp90 inhibitors. Curr Top Med Chem 2009;9:1436-46
    • (2009) Curr Top Med Chem , vol.9 , pp. 1436-46
    • Taldone, T.1    Chiosis, G.2
  • 41
    • 67651160909 scopus 로고    scopus 로고
    • Targeting heat shock protein 90 with non-quinone inhibitors: A novel chemotherapeutic approach in human hepatocellular carcinoma
    • Breinig M, Caldas-Lopes E, Goeppert B, et al. Targeting heat shock protein 90 with non-quinone inhibitors: a novel chemotherapeutic approach in human hepatocellular carcinoma. Hepatology 2009;50:102-12
    • (2009) Hepatology , vol.50 , pp. 102-12
    • Breinig, M.1    Caldas-Lopes, E.2    Goeppert, B.3
  • 42
    • 66249138886 scopus 로고    scopus 로고
    • Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models
    • Caldas-Lopes E, Cerchietti L, Ahn JH, et al. Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models. Proc Natl Acad Sci USA 2009;106:8368-73
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8368-73
    • Caldas-Lopes, E.1    Cerchietti, L.2    Ahn, J.H.3
  • 43
    • 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 LC, Lopes EC, Yang SN, et al. A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lymphomas. Nat Med 2009;15:1369-76
    • (2009) Nat Med , vol.15 , pp. 1369-76
    • Cerchietti, L.C.1    Lopes, E.C.2    Yang, S.N.3
  • 44
    • 77957854088 scopus 로고    scopus 로고
    • HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans
    • Marubayashi S, Koppikar P, Taldone T, et al. HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans. J Clin Invest 2010;120:3578-93
    • (2010) J Clin Invest , vol.120 , pp. 3578-93
    • Marubayashi, S.1    Koppikar, P.2    Taldone, T.3
  • 46
    • 67449138839 scopus 로고    scopus 로고
    • CUDC- 305, a novel synthetic HSP90 inhibitor with unique pharmacologic properties for cancer therapy
    • Bao R, Lai C-J, 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. 4046-57
    • Bao, R.1    Lai, C.-J.2    Qu, H.3
  • 47
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
    • Rowlands MG, Newbatt YM, Prodromou C, et al. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem 2004;327:176
    • (2004) Anal Biochem , vol.327 , pp. 176
    • Rowlands, M.G.1    Newbatt, Y.M.2    Prodromou, C.3
  • 49
    • 77952383375 scopus 로고    scopus 로고
    • New molecular and biological mechanism of antitumor activities of KW-2478, a novel nonansamycin heat shock protein 90 inhibitor, in multiple myeloma cells
    • Nakashima T, Ishii T, Tagaya H, et al. New molecular and biological mechanism of antitumor activities of KW-2478, a novel nonansamycin heat shock protein 90 inhibitor, in multiple myeloma cells. Clin Cancer Res 2010;16:2792-802
    • (2010) Clin Cancer Res , vol.16 , pp. 2792-802
    • Nakashima, T.1    Ishii, T.2    Tagaya, H.3
  • 50
    • 3242722132 scopus 로고    scopus 로고
    • A time-resolved fluorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors
    • DOI 10.1016/j.ab.2004.04.011, PII S000326970400329X
    • Zhou V, Han S, Brinker A, et al. A time-resolved fluorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors. Anal Biochem 2004;331:349-57 (Pubitemid 38953086)
    • (2004) Analytical Biochemistry , vol.331 , Issue.2 , pp. 349-357
    • Zhou, V.1    Han, S.2    Brinker, A.3    Klock, H.4    Caldwell, J.5    Gu, X.-J.6
  • 51
    • 55749083540 scopus 로고    scopus 로고
    • Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone
    • Kung P-P, Funk L, Meng J, et al. Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone. Bioorg Med Chem Lett 2008;18:6273-8
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 6273-8
    • Kung, P.-P.1    Funk, L.2    Meng, J.3
  • 52
    • 74849125314 scopus 로고    scopus 로고
    • Dihydroxyphenylisoindoline amides as orally bioavailable inhibitors of the heat shock protein 90 (Hsp90) molecular chaperone
    • Kung P-P, Huang B, Zhang G, et al. Dihydroxyphenylisoindoline amides as orally bioavailable inhibitors of the heat shock protein 90 (Hsp90) molecular chaperone. J Med Chem 2010;53:499-503
    • (2010) J Med Chem , vol.53 , pp. 499-503
    • Kung, P.-P.1    Huang, B.2    Zhang, G.3
  • 54
    • 67650468165 scopus 로고    scopus 로고
    • Potent triazolothione inhibitor of heat-shock protein-90
    • Feldman RI, Mintzer B, Zhu D, et al. Potent triazolothione inhibitor of heat-shock protein-90. Chem Biol Drug Des 2009;74:43-50
    • (2009) Chem Biol Drug des , vol.74 , pp. 43-50
    • Feldman, R.I.1    Mintzer, B.2    Zhu, D.3
  • 56
    • 47349092634 scopus 로고    scopus 로고
    • Discovery of aminoquinolines as a new class of potent inhibitors of heat shock protein 90 (Hsp90): Synthesis, biology, and molecular modeling
    • Ganesh T, Min J, Thepchatri P, et al. Discovery of aminoquinolines as a new class of potent inhibitors of heat shock protein 90 (Hsp90): synthesis, biology, and molecular modeling. Bioorg Med Chem 2008;16:6903-10
    • (2008) Bioorg Med Chem , vol.16 , pp. 6903-10
    • Ganesh, T.1    Min, J.2    Thepchatri, P.3
  • 57
    • 77955444211 scopus 로고    scopus 로고
    • Application of chemoproteomics to drug discovery: Identification of a clinical candidate targeting Hsp90
    • Fadden P, Huang KH, Veal JM, et al. Application of chemoproteomics to drug discovery: identification of a clinical candidate targeting Hsp90. Chem Biol 2010;17:686-94
    • (2010) Chem Biol , vol.17 , pp. 686-94
    • Fadden, P.1    Huang, K.H.2    Veal, J.M.3
  • 58
    • 67650741952 scopus 로고    scopus 로고
    • Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents
    • Huang KH, Veal JM, Fadden RP, et al. Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents. J Med Chem 2009;52:4288-305
    • (2009) J Med Chem , vol.52 , pp. 4288-305
    • Huang, K.H.1    Veal, J.M.2    Fadden, R.P.3
  • 59
    • 0029118437 scopus 로고
    • Novel bioactive azaphilones from fruit bodies and mycelial cultures of the ascomycete bulgaria inquinans
    • Stadler M, Anke H, Dekermendjian K, et al. Novel bioactive azaphilones from fruit bodies and mycelial cultures of the ascomycete bulgaria inquinans. Nat Prod Lett 1995;7:7-14
    • (1995) Nat Prod Lett , vol.7 , pp. 7-14
    • Stadler, M.1    Anke, H.2    Dekermendjian, K.3
  • 60
    • 77955469426 scopus 로고    scopus 로고
    • Natural and semisynthetic azaphilones as a new scaffold for Hsp90 inhibitors
    • Musso L, Dallavalle S, Merlini L, et al. Natural and semisynthetic azaphilones as a new scaffold for Hsp90 inhibitors. Bioorg Med Chem 2010;18:6031-43
    • (2010) Bioorg Med Chem , vol.18 , pp. 6031-43
    • Musso, L.1    Dallavalle, S.2    Merlini, L.3
  • 62
    • 35148840116 scopus 로고    scopus 로고
    • A novel class of Hsp90 inhibitors isolated by structure-based virtual screening
    • DOI 10.1016/j.bmcl.2007.08.069, PII S0960894X07010268
    • Park H, Kim Y-J, Hahn J-S. A novel class of Hsp90 inhibitors isolated by structure-based virtual screening. Biorg Med Chem Lett 2007;17:6345-9 (Pubitemid 47552807)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.22 , pp. 6345-6349
    • Park, H.1    Kim, Y.-J.2    Hahn, J.-S.3
  • 63
    • 67651108949 scopus 로고    scopus 로고
    • Identification of new Hsp90 inhibitors by structure-based virtual screening
    • Hong T-J, Park H, Kim Y-J, et al. Identification of new Hsp90 inhibitors by structure-based virtual screening. Bioorg Med Chem Lett 2009;19:4839-42
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 4839-42
    • Hong, T.-J.1    Park, H.2    Kim, Y.-J.3
  • 64
    • 77955863827 scopus 로고    scopus 로고
    • Fragment-based drug discovery applied to Hsp90. Discovery of two lead series with high ligand efficiency
    • Murray CW, Carr MG, Callaghan O, et al. Fragment-based drug discovery applied to Hsp90. Discovery of two lead series with high ligand efficiency. J Med Chem 2010;53:5942-55
    • (2010) J Med Chem , vol.53 , pp. 5942-55
    • Murray, C.W.1    Carr, M.G.2    Callaghan, O.3
  • 65
    • 77955873344 scopus 로고    scopus 로고
    • Discovery of (2,4-dihydroxy-5- isopropylphenyl)-[5-(4-methylpiperazin- 1-ylmethyl)-1,3-dihydroisoindol-2-yl] methanone (AT13387), a novel inhibitor of the molecular chaperone Hsp90 by fragment based drug design
    • Woodhead AJ, Angove H, Carr MG, et al. Discovery of (2,4-dihydroxy-5- isopropylphenyl)-[5-(4-methylpiperazin- 1-ylmethyl)-1,3-dihydroisoindol-2-yl] methanone (AT13387), a novel inhibitor of the molecular chaperone Hsp90 by fragment based drug design. J Med Chem 2010;53:5956-69
    • (2010) J Med Chem , vol.53 , pp. 5956-69
    • Woodhead, A.J.1    Angove, H.2    Carr, M.G.3
  • 66
    • 79955405506 scopus 로고    scopus 로고
    • Significance of the long term pharmacodynamic actions of Hsp90 inhibitor AT13387
    • Curry J, Angove H, Graham B, et al. Significance of the long term pharmacodynamic actions of Hsp90 inhibitor AT13387. AACR abstract 2009
    • (2009) AACR Abstract
    • Curry, J.1    Angove, H.2    Graham, B.3
  • 67
    • 68549115383 scopus 로고    scopus 로고
    • Combining hit identification strategies: Fragment-based and in silico approaches to orally active 2-aminothieno [2,3-d]pyrimidine inhibitors of the Hsp90 molecular chaperone
    • Brough PA, Barril X, Borgognoni J, et al. Combining hit identification strategies: Fragment-based and in silico approaches to orally active 2-aminothieno [2,3-d]pyrimidine inhibitors of the Hsp90 molecular chaperone. J Med Chem 2009;52:4794-809
    • (2009) J Med Chem , vol.52 , pp. 4794-809
    • Brough, P.A.1    Barril, X.2    Borgognoni, J.3
  • 69
    • 67049133236 scopus 로고    scopus 로고
    • Fragment-based identification of Hsp90 inhibitors
    • Barker JJ, Barker O, Boggio R, et al. Fragment-based identification of Hsp90 inhibitors. ChemMedChem 2009;4:963-6
    • (2009) ChemMedChem , vol.4 , pp. 963-6
    • Barker, J.J.1    Barker, O.2    Boggio, R.3
  • 71
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • DOI 10.1016/j.str.2004.03.020, PII S0969212604001261
    • Harris SF, Shiau AK, Agard DA. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 2004;12:1087-97 (Pubitemid 38748780)
    • (2004) Structure , vol.12 , Issue.6 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 72
    • 74249108175 scopus 로고    scopus 로고
    • Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases
    • Brandt GEL, Blagg BSJ. Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases. Curr Top Med Chem 2009;9:1447-61
    • (2009) Curr Top Med Chem , vol.9 , pp. 1447-61
    • Gel, B.1    Bsj, B.2
  • 74
    • 16344364163 scopus 로고    scopus 로고
    • Epigallocatechin gallate inhibits aryl hydrocarbon receptor gene transcription through an indirect mechanism involving binding to a 90 kDa heat shock protein
    • DOI 10.1021/bi047433p
    • Palermo CM, Westlake CA, Gasiewicz TA. Epigallocatechin gallate inhibits aryl hydrocarbon receptor gene transcription through an indirect mechanism involving binding to a 90 KDa heat shock protein. Biochemistry 2005;44:5041-52 (Pubitemid 40471220)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5041-5052
    • Palermo, C.M.1    Westlake, C.A.2    Gasiewicz, T.A.3
  • 75
    • 71549153791 scopus 로고    scopus 로고
    • Withaferin A targets heat shock protein 90 in pancreatic cancer cells
    • Yu Y, Hamza A, Zhang T, et al. Withaferin A targets heat shock protein 90 in pancreatic cancer cells. Biochem Pharmacol 2010;79:542-51
    • (2010) Biochem Pharmacol , vol.79 , pp. 542-51
    • Yu, Y.1    Hamza, A.2    Zhang, T.3
  • 77
    • 58249112898 scopus 로고    scopus 로고
    • Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors
    • Smith JR, Clarke PA, de Billy E, et al. Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors. Oncogene 2009;28:157-69
    • (2009) Oncogene , vol.28 , pp. 157-69
    • Smith, J.R.1    Clarke, P.A.2    De Billy, E.3
  • 79
    • 38349153572 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells
    • Zhang T, Hamza A, Cao X, et al. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol Cancer Ther 2008;7:162-70
    • (2008) Mol Cancer Ther , vol.7 , pp. 162-70
    • Zhang, T.1    Hamza, A.2    Cao, X.3
  • 80
    • 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 SL, Gobel M, et al. Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol. Angew Chem Int Ed 2009;48:5853-5
    • (2009) Angew Chem Int Ed , vol.48 , pp. 5853-5
    • Sreeramulu, S.1    Gande, S.L.2    Gobel, M.3
  • 81
    • 33646406554 scopus 로고    scopus 로고
    • Celastrol a triterpene extracted from the Chinese "thunder of God Vine," is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice
    • Yang H, Chen D, Cui QC, et al. Celastrol, a triterpene extracted from the Chinese Thunder of God Vine, is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res 2006;66:4758-65
    • (2006) Cancer Res , vol.66 , pp. 4758-65
    • Yang, H.1    Chen, D.2    Cui, Q.C.3
  • 82
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • DOI 10.1016/S0092-8674(00)80830-2
    • Scheufler C, Brinker A, Bourenkov G, et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000;101:199-210 (Pubitemid 32004747)
    • (2000) Cell , vol.101 , Issue.2 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl F.Ulrich7    Moarefi, I.8
  • 83
    • 42449136263 scopus 로고    scopus 로고
    • Designed TPR modules as novel anticancer agents
    • Cortajarena AL, Yi F, Regan L. Designed TPR modules as novel anticancer agents. ACS Chem Biol 2008;3:161-6
    • (2008) ACS Chem Biol , vol.3 , pp. 161-6
    • Cortajarena, A.L.1    Yi, F.2    Regan, L.3
  • 84
    • 63849342150 scopus 로고    scopus 로고
    • An AlphaScreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction
    • Yi F, Zhu P, Southall N, et al. An AlphaScreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction. J Biomol Screen 2009;14:273-81
    • (2009) J Biomol Screen , vol.14 , pp. 273-81
    • Yi, F.1    Zhu, P.2    Southall, N.3
  • 85
    • 58149144382 scopus 로고    scopus 로고
    • A novel class of small molecule inhibitors of Hsp90
    • Yi F, Regan L. A novel class of small molecule inhibitors of Hsp90. ACS Chem Biol 2008;3:645-54
    • (2008) ACS Chem Biol , vol.3 , pp. 645-54
    • Yi, F.1    Regan, L.2
  • 87
    • 11144357391 scopus 로고    scopus 로고
    • Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
    • Meyer P, Prodromou C, Liao C, et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 2004;23:1402-10
    • (2004) EMBO J , vol.23 , pp. 1402-10
    • Meyer, P.1    Prodromou, C.2    Liao, C.3
  • 88
    • 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
    • DOI 10.1158/0008-5472.CAN-07-3268
    • Holmes JL, Sharp SY, Hobbs S, et al. 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;68:1187-96 (Pubitemid 351272238)
    • (2008) Cancer Research , vol.68 , Issue.4 , pp. 1187-1196
    • Holmes, J.L.1    Sharp, S.Y.2    Hobbs, S.3    Workman, P.4
  • 91
    • 0036786205 scopus 로고    scopus 로고
    • Mechanism of antiandrogen action: Key role of Hsp90 in conformational change and transcriptional activity of the androgen receptor
    • Georget V, Terouanne B, Nicolas J-C, et al. Mechanism of antiandrogen action: Key role of Hsp90 in conformational change and transcriptional activity of the androgen receptor. Biochemistry 2002;41:11824-31
    • (2002) Biochemistry , vol.41 , pp. 11824-31
    • Georget, V.1    Terouanne, B.2    Nicolas, J.-C.3
  • 92
    • 77950187693 scopus 로고    scopus 로고
    • Camptothecin disrupts androgen receptor signaling and suppresses prostate cancer cell growth
    • Liu S, Yuan Y, Okumura Y, et al. Camptothecin disrupts androgen receptor signaling and suppresses prostate cancer cell growth. Biochem Biophys Res Commun 2010;394:297-302
    • (2010) Biochem Biophys Res Commun , vol.394 , pp. 297-302
    • Liu, S.1    Yuan, Y.2    Okumura, Y.3
  • 95
    • 70449710842 scopus 로고    scopus 로고
    • Hsp90 is regulated by a switch point in the C-terminal domain
    • Retzlaff M, Stahl M, Eberl HC, et al. Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep 2009;10:1147-53
    • (2009) EMBO Rep , vol.10 , pp. 1147-53
    • Retzlaff, M.1    Stahl, M.2    Eberl, H.C.3
  • 96
    • 31444454302 scopus 로고    scopus 로고
    • The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
    • DOI 10.1038/sj.emboj.7600930, PII 7600930
    • Wandinger SK, Suhre MH, Wegele H, et al. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J 2006;25:367-76 (Pubitemid 43152857)
    • (2006) EMBO Journal , vol.25 , Issue.2 , pp. 367-376
    • Wandinger, S.K.1    Suhre, M.H.2    Wegele, H.3    Buchner, J.4
  • 98
    • 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. 4833-42
    • Yang, Y.1    Rao, R.2    Shen, J.3
  • 100
    • 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. 1886-93
    • Rao, R.1    Fiskus, W.2    Yang, Y.3
  • 101
    • 43049173740 scopus 로고    scopus 로고
    • MS-275, a novel histone deacetylase inhibitor with selectivity against HDAC1, induces degradation of FLT3 via inhibition of chaperone function of heat shock protein 90 in AML cells
    • Nishioka C, Ikezoe T, Yang J, et al. MS-275, a novel histone deacetylase inhibitor with selectivity against HDAC1, induces degradation of FLT3 via inhibition of chaperone function of heat shock protein 90 in AML cells. Leuk Res 2008;32:1382-92
    • (2008) Leuk Res , vol.32 , pp. 1382-92
    • Nishioka, C.1    Ikezoe, T.2    Yang, J.3
  • 102
    • 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
    • DOI 10.1182/blood-2004-09-3413
    • George P, Bali P, Annavarapu S, 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;105:1768-76 (Pubitemid 40223701)
    • (2005) Blood , vol.105 , Issue.4 , pp. 1768-1776
    • George, P.1    Bali, P.2    Annavarapu, S.3    Scuto, A.4    Fiskus, W.5    Guo, F.6    Sigua, C.7    Sondarva, G.8    Moscinski, L.9    Atadja, P.10    Bhalla, K.11
  • 103
    • 63549104682 scopus 로고    scopus 로고
    • Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer
    • Morra G, Verkhivker G, Colombo G. Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer. PLoS Comput Biol 2009;5:e1000323
    • (2009) PLoS Comput Biol , vol.5
    • Morra, G.1    Verkhivker, G.2    Colombo, G.3
  • 104
    • 0035980061 scopus 로고    scopus 로고
    • Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein
    • Zhao YG, Gilmore R, Leone G, et al. Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein. J Biol Chem 2001;276:32822-7
    • (2001) J Biol Chem , vol.276 , pp. 32822-7
    • Zhao, Y.G.1    Gilmore, R.2    Leone, G.3
  • 105
    • 0028806464 scopus 로고
    • Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the Hsp90 stress protein and the pp60v-src tyrosine kinase
    • Mimnaugh EG, Worland PJ, Whitesell L, et al. Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the Hsp90 stress protein and the pp60v-src tyrosine kinase. J Biol Chem 1995;270:28654-9
    • (1995) J Biol Chem , vol.270 , pp. 28654-9
    • Mimnaugh, E.G.1    Worland, P.J.2    Whitesell, L.3
  • 106
    • 70349326246 scopus 로고    scopus 로고
    • CK2: The kinase controlling the Hsp90 chaperone machinery
    • Miyata Y. CK2: the kinase controlling the Hsp90 chaperone machinery. Cell Mol Life Sci 2009;66:1840-9
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1840-9
    • Miyata, Y.1
  • 107
    • 75949112264 scopus 로고    scopus 로고
    • Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function
    • Mollapour M, Tsutsumi S, Donnelly AC, et al. Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. Mol Cell 2010;37:333-43
    • (2010) Mol Cell , vol.37 , pp. 333-43
    • Mollapour, M.1    Tsutsumi, S.2    Donnelly, A.C.3
  • 108
    • 4243105077 scopus 로고    scopus 로고
    • IC101 induces apoptosis by Akt dephosphorylation via an inhibition of heat shock protein 90-ATP binding activity accompanied by preventing the interaction with Akt in L1210 cells
    • DOI 10.1124/jpet.104.065979
    • Fujiwara H, Yamakuni T, Ueno M, et al. IC101 induces apoptosis by Akt dephosphorylation via an inhibition of heat shock protein 90-ATP binding activity accompanied by preventing the interaction with Akt in L1210 cells. J Pharmacol Exp Ther 2004;310:1288-95 (Pubitemid 39108952)
    • (2004) Journal of Pharmacology and Experimental Therapeutics , vol.310 , Issue.3 , pp. 1288-1295
    • Fujiwara, H.1    Yamakuni, T.2    Ueno, M.3    Ishizuka, M.4    Shinkawa, T.5    Isobe, T.6    Ohizumi, Y.7
  • 110
    • 0035898534 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR
    • DOI 10.1093/emboj/20.14.3771
    • Donze O, Abbas-Terki T, Picard D. The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J 2001;20:3771-80 (Pubitemid 32691788)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3771-3780
    • Donze, O.1    Abbas-Terki, T.2    Picard, D.3
  • 111
    • 55749096409 scopus 로고    scopus 로고
    • Inhibition of Hsp90 activates osteoclast c-Src signaling and promotes growth of prostate carcinoma cells in bone
    • Yano A, Tsutsumi S, Soga S, et al. Inhibition of Hsp90 activates osteoclast c-Src signaling and promotes growth of prostate carcinoma cells in bone. Proc Natl Acad Sci USA 2008;105:15541-6
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15541-6
    • Yano, A.1    Tsutsumi, S.2    Soga, S.3
  • 113
    • 54749126264 scopus 로고    scopus 로고
    • P-Glycoprotein-mediated resistance to Hsp90-directed therapy is eclipsed by the heat shock response
    • McCollum AK, TenEyck CJ, Stensgard B, et al. P-Glycoprotein-mediated resistance to Hsp90-directed therapy is eclipsed by the heat shock response. Cancer Res 2008;68:7419-27
    • (2008) Cancer Res , vol.68 , pp. 7419-27
    • McCollum, A.K.1    Teneyck, C.J.2    Stensgard, B.3
  • 114
    • 11244337455 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[[(2- dimethylamino)ethyl]amino]geldanamycin (17DMAG, NSC 707545) in C.B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts
    • DOI 10.1007/s00280-004-0865-3
    • Eiseman JL, Lan J, Lagattuta TF, et al. Pharmacokinetics and pharmacodynamics of 17-demethoxy-17-[[(2-dimethylamino) ethyl]amino]geldanamycin (17DMAG, NSC 707545) in C.B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts. Cancer Chemother Pharmacol 2005;55:21-32 (Pubitemid 40064492)
    • (2005) Cancer Chemotherapy and Pharmacology , vol.55 , Issue.1 , pp. 21-32
    • Eiseman, J.L.1    Lan, J.2    Lagattuta, T.F.3    Hamburger, D.R.4    Joseph, E.5    Covey, J.M.6    Egorin, M.J.7
  • 115
    • 68849084042 scopus 로고    scopus 로고
    • Antitumor efficacy of IPI-504, a selective heat shock protein 90 inhibitor against human epidermal growth factor receptor 2-positive human xenograft models as a single agent and in combination with trastuzumab or lapatinib
    • Leow CC, Chesebrough J, Coffman KT, et al. Antitumor efficacy of IPI-504, a selective heat shock protein 90 inhibitor against human epidermal growth factor receptor 2-positive human xenograft models as a single agent and in combination with trastuzumab or lapatinib. Mol Cancer Ther 2009;8:2131-41
    • (2009) Mol Cancer Ther , vol.8 , pp. 2131-41
    • Leow, C.C.1    Chesebrough, J.2    Coffman, K.T.3
  • 116
    • 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 JP, Caldas-Lopes E, Divilov V, 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
  • 117
    • 66449094961 scopus 로고    scopus 로고
    • BIIB021, an orally available, fully synthetic small-molecule inhibitor of the heat shock protein Hsp90
    • Lundgren K, Zhang H, Brekken J, et al. BIIB021, an orally available, fully synthetic small-molecule inhibitor of the heat shock protein Hsp90. Mol Cancer Ther 2009;8:921-9
    • (2009) Mol Cancer Ther , vol.8 , pp. 921-9
    • Lundgren, K.1    Zhang, H.2    Brekken, J.3
  • 118
    • 48949119477 scopus 로고    scopus 로고
    • NVP-AUY922: A small molecule HSP90 inhibitor with potent antitumor activity in preclinical breast cancer models
    • Jensen MR, Schoepfer J, Radimerski T, et al. NVP-AUY922: a small molecule HSP90 inhibitor with potent antitumor activity in preclinical breast cancer models. Breast Cancer Res 2008;10:R33
    • (2008) Breast Cancer Res , vol.10
    • Jensen, M.R.1    Schoepfer, J.2    Radimerski, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.