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Volumn 7, Issue 6, 2006, Pages 534-541

Heat shock protein-90 inhibitors: A chronicle from geldanamycin to today's agents

Author keywords

Ansamycins; Anticancer therapeutics; Hsp90; PU class Hsp90 inhibitors; Pyrazoles; Radicicol and derivatives

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 17 DIMETHYLLAMINO 17 DEMETHOXYGELDANAMYCIN; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; ANSAMYCIN DERIVATIVE; BENZIMIDAZOLE DERIVATIVE; CNF 1010; COUMARIN DERIVATIVE; CYCLOPROPARADICICOL; FR 901228; G 3130; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HISTONE DEACETYLASE INHIBITOR; KF 55823; KOS 953; LBH 589; MONOCLONAL ANTIBODY; MYCOGRAB; NOVOBIOCIN; POCHONIN D; PU 24 FCI; PURINE DERIVATIVE; PYRAZOLE DERIVATIVE; PYRAZOLOPYRIMIDINE DERIVATIVE; PYRIMIDINE DERIVATIVE; PYRROLOPYRIMIDINE DERIVATIVE; RADICICOL; RESORCINOL DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VER 49009; ZERANOL;

EID: 33745174538     PISSN: 14724472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (91)

References (53)
  • 1
    • 0019404632 scopus 로고
    • Two cellular proteins that immunoprecipitate with the transforming protein of Rous sarcoma virus
    • Oppermann H, Levinson AD, Levintow L, Varmus HE, Bishop JM, Kawai S: Two cellular proteins that immunoprecipitate with the transforming protein of Rous sarcoma virus. Virology (1981) 113(2):736-751.
    • (1981) Virology , vol.113 , Issue.2 , pp. 736-751
    • Oppermann, H.1    Levinson, A.D.2    Levintow, L.3    Varmus, H.E.4    Bishop, J.M.5    Kawai, S.6
  • 2
    • 0027291238 scopus 로고
    • Heat-shock protein Hsp90 governs the activity of pp60v-src kinase
    • Xu Y, Lindquist S: Heat-shock protein Hsp90 governs the activity of pp60v-src kinase. Proc Natl Acad Sci USA (1993) 90(15):7074-7078.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.15 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 3
    • 14344264703 scopus 로고    scopus 로고
    • Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - An update
    • Neckers L, Neckers K: Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - an update. Expert Opin Emerg Drugs (2005) 10(1):137-149.
    • (2005) Expert Opin Emerg Drugs , vol.10 , Issue.1 , pp. 137-149
    • Neckers, L.1    Neckers, K.2
  • 4
    • 1542298267 scopus 로고    scopus 로고
    • Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone
    • Workman P: Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone. Cancer Lett (2004) 206(2):149-157.
    • (2004) Cancer Lett , vol.206 , Issue.2 , pp. 149-157
    • Workman, P.1
  • 5
    • 25844519550 scopus 로고    scopus 로고
    • Hsp90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL: Hsp90 and the chaperoning of cancer. Nat Rev Cancer (2005) 5(10):761-772.
    • (2005) Nat Rev Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 6
    • 33244484848 scopus 로고    scopus 로고
    • Targeting chaperones in transformed systems - A focus on Hsp90 and cancer
    • Chiosis G: Targeting chaperones in transformed systems - a focus on Hsp90 and cancer. Expert Opin Ther Targets (2006) 10(1):37-50.
    • (2006) Expert Opin Ther Targets , vol.10 , Issue.1 , pp. 37-50
    • Chiosis, G.1
  • 8
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • Neckers L, Schulte TW, Mimnaugh E: Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest New Drugs (1999) 17(4):361-373.
    • (1999) Invest New Drugs , vol.17 , Issue.4 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 9
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM: The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol (1998) 42(4):273-279.
    • (1998) Cancer Chemother Pharmacol , vol.42 , Issue.4 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 10
    • 21244466289 scopus 로고    scopus 로고
    • Comparison of 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: Effects on Hsp90 and client proteins in melanoma models
    • Smith V, Sausville EA, Camalier RF, Fiebig HH, Burger AM: Comparison of 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: Effects on Hsp90 and client proteins in melanoma models. Cancer Chemother Pharmacol (2005) 56(2):126-137.
    • (2005) Cancer Chemother Pharmacol , vol.56 , Issue.2 , pp. 126-137
    • Smith, V.1    Sausville, E.A.2    Camalier, R.F.3    Fiebig, H.H.4    Burger, A.M.5
  • 13
    • 18744411808 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of Hsp90 inhibitors based on conformational analysis of radicicol and its analogues
    • Moulin E, Zoete V, Barluenga S, Karplus M, Winssinger N: Design, synthesis, and biological evaluation of Hsp90 inhibitors based on conformational analysis of radicicol and its analogues. J Am Chem Soc (2005) 127(19):6999-7004.
    • (2005) J Am Chem Soc , vol.127 , Issue.19 , pp. 6999-7004
    • Moulin, E.1    Zoete, V.2    Barluenga, S.3    Karplus, M.4    Winssinger, N.5
  • 14
    • 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 MN, Lucas B, Munster PN, Zheng FF, Sepp-Lorenzino L, Rosen N: 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(3):289-299.
    • (2001) Chem Biol , 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
  • 20
    • 0141708701 scopus 로고    scopus 로고
    • Natural product origins of Hsp90 inhibitors
    • Uehara Y: Natural product origins of Hsp90 inhibitors. Curr Cancer Drug Targets (2003) 3(5):325-330.
    • (2003) Curr Cancer Drug Targets , vol.3 , Issue.5 , pp. 325-330
    • Uehara, Y.1
  • 21
    • 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 G Rosen N, Hartl U, Pavletich NP: Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell (1997) 89(2):239-250.
    • (1997) Cell , vol.89 , Issue.2 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, G.3    Rosen, N.4    Hartl, U.5    Pavletich, N.P.6
  • 22
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein tyrosine kinase induced by geldanamycin
    • 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(37):22796-22801.
    • (1996) J Biol Chem , vol.271 , Issue.37 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 23
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM: The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol (1998) 42(4):273-279.
    • (1998) Cancer Chemother Pharmacol , vol.42 , Issue.4 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 25
    • 0142027766 scopus 로고    scopus 로고
    • Angiogenesis impairment in Id-deficient mice cooperates with an Hsp90 inhibitor to completely suppress HER2/neu-dependent breast tumors
    • De Candia P, Solit D, Giri D, Brogi E, Siegel PM, Olshen AB, Muller WJ, Rosen N, Benezra R: Angiogenesis impairment in Id-deficient mice cooperates with an Hsp90 inhibitor to completely suppress HER2/ neu-dependent breast tumors. Proc Natl Acad Sci USA (2003) 100(21):12337-12342.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.21 , pp. 12337-12342
    • De Candia, P.1    Solit, D.2    Giri, D.3    Brogi, E.4    Siegel, P.M.5    Olshen, A.B.6    Muller, W.J.7    Rosen, N.8    Benezra, R.9
  • 26
    • 0141596326 scopus 로고    scopus 로고
    • Clinical development of 17-allylamino, 17-demethoxygeldanamycin
    • Sausville EA, Tomaszewski JE, Ivy P: Clinical development of 17-allylamino, 17-demethoxygeldanamycin. Curr Cancer Drug Targets (2003) 3(5):377-383.
    • (2003) Curr Cancer Drug Targets , vol.3 , Issue.5 , pp. 377-383
    • Sausville, E.A.1    Tomaszewski, J.E.2    Ivy, P.3
  • 28
    • 20944444881 scopus 로고    scopus 로고
    • Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers
    • Ramanathan RK, Trump DL, Eiseman JL, Belani CP, Agarwala SS, Zuhowski EG, Lan J, Potter DM, Ivy SP, Ramalingam S, Brulsky AM et al: Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers. Clin Cancer Res (2005) 11(9):3385-3391.
    • (2005) Clin Cancer Res , vol.11 , Issue.9 , 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    Lan, J.7    Potter, D.M.8    Ivy, S.P.9    Ramalingam, S.10    Brulsky, A.M.11
  • 30
    • 21244466289 scopus 로고    scopus 로고
    • Comparison of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: Effects on Hsp90 and client proteins in melanoma models
    • Smith V, Sausville EA, Camalier RF, Fiebig HH, Burger AM: Comparison of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: Effects on Hsp90 and client proteins in melanoma models. Cancer Chemother Pharmaco (2005) 56(2):126-137.
    • (2005) Cancer Chemother Pharmaco , vol.56 , Issue.2 , pp. 126-137
    • Smith, V.1    Sausville, E.A.2    Camalier, R.F.3    Fiebig, H.H.4    Burger, A.M.5
  • 31
    • 33645471864 scopus 로고    scopus 로고
    • Reaction of geldanamycin and C17-substituted analogues with glutathione: Product identifications and pharmacological implications
    • Cysyk RL, Parker RJ, Barchi JJ Jr, Steeg PS, Hartman NR, Strong JM: Reaction of geldanamycin and C17-substituted analogues with glutathione: Product identifications and pharmacological implications. Chem Res Toxicol (2006) 19(3):376-381.
    • (2006) Chem Res Toxicol , vol.19 , Issue.3 , pp. 376-381
    • Cysyk, R.L.1    Parker, R.J.2    Barchi Jr., J.J.3    Steeg, P.S.4    Hartman, N.R.5    Strong, J.M.6
  • 32
    • 33745137678 scopus 로고    scopus 로고
    • Influence of muldidrug resistance proteins on the antitumor activity of natural and synthetic Hsp90 inhibitors
    • AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics: Discovery, Biology, and Clinical Applications :Abs
    • Zhang H, Neely LS, Yang Y-C, Burrows FJ: Influence of muldidrug resistance proteins on the antitumor activity of natural and synthetic Hsp90 inhibitors. AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics: Discovery, Biology, and Clinical Applications (2005):Abs C39.
    • (2005)
    • Zhang, H.1    Neely, L.S.2    Yang, Y.-C.3    Burrows, F.J.4
  • 33
    • 33244469207 scopus 로고    scopus 로고
    • Development of acquired resistance to 17(allylamino)-17-demethoxygeldanamycin (17-AAG) in hormone refractory breast cancers in vitro
    • Abs LB-267
    • Madden T-A, Pumford S, Barrow D, Dutkowski CM, McClelland R, Nicholson RI: Development of acquired resistance to 17(allylamino)-17-demethoxygeldanamycin (17-AAG) in hormone refractory breast cancers in vitro. Proc Amer Assoc Cancer Res (2005) 96:Abs LB-267.
    • (2005) Proc Amer Assoc Cancer Res , vol.96
    • Madden, T.-A.1    Pumford, S.2    Barrow, D.3    Dutkowski, C.M.4    McClelland, R.5    Nicholson, R.I.6
  • 35
    • 20444465254 scopus 로고    scopus 로고
    • Radester, a novel inhibitor of the Hsp90 protein folding machinery
    • Shen G, Blagg BS: Radester, a novel inhibitor of the Hsp90 protein folding machinery. Org Lett (2005) 7(11):2157-2160.
    • (2005) Org Lett , vol.7 , Issue.11 , pp. 2157-2160
    • Shen, G.1    Blagg, B.S.2
  • 37
    • 17444416142 scopus 로고    scopus 로고
    • Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90
    • Llauger L, He H, Kim J, Aguirre J, Rosen N, Peters U, Davies P, Chiosis G: Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90. J Med Chem (2005) 48(8):2892-2905.
    • (2005) J Med Chem , vol.48 , Issue.8 , pp. 2892-2905
    • Llauger, L.1    He, H.2    Kim, J.3    Aguirre, J.4    Rosen, N.5    Peters, U.6    Davies, P.7    Chiosis, G.8
  • 40
    • 33745149192 scopus 로고    scopus 로고
    • Design and development of purine-scaffold inhibitors of the heat shock protein 90
    • Abs MEDI-206
    • Chiosis G. Design and development of purine-scaffold inhibitors of the heat shock protein 90. ACS (2006) 231:Abs MEDI-206.
    • (2006) ACS , vol.231
    • Chiosis, G.1
  • 41
    • 33745152950 scopus 로고    scopus 로고
    • A phase I dose escalation study of CNF2024 for ZAP-70 positive CLL
    • Kantarjian H. A phase I dose escalation study of CNF2024 for ZAP-70 positive CLL. MD Anderson Leukemia Insights Newsletter (2005) 10 (3). http://www.mdanderson.org/publications/insights/
    • (2005) MD Anderson Leukemia Insights Newsletter , vol.10 , Issue.3
    • Kantarjian, H.1
  • 42
    • 33745164492 scopus 로고    scopus 로고
    • Serenex Inc: Pipeline
    • Serenex Inc: Company World Wide Web Site May 13
    • Serenex Inc: Serenex Inc: Pipeline. Company World Wide Web Site (2005):May 13.
    • (2005)
  • 43
    • 0034594644 scopus 로고    scopus 로고
    • Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins
    • Marcu MG, Schulte TW, Neckers L: Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J Natl Cancer Inst (2000) 92(3):242-248.
    • (2000) J Natl Cancer Inst , vol.92 , Issue.3 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 45
    • 26644473193 scopus 로고    scopus 로고
    • Regulation of the dynamics of Hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone
    • Murphy PJ, Morishima Y, Kovacs JJ, Yao TP, Pratt WB: Regulation of the dynamics of Hsp90 action on the glucocorticoid receptor by acetylation/ deacetylation of the chaperone. J Biol Chem (2005) 280(40):33792-33799.
    • (2005) J Biol Chem , vol.280 , Issue.40 , pp. 33792-33799
    • Murphy, P.J.1    Morishima, Y.2    Kovacs, J.J.3    Yao, T.P.4    Pratt, W.B.5
  • 46
    • 0345734276 scopus 로고    scopus 로고
    • Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin
    • Blank M, Mandel M, Keisari Y, Meruelo D, Lavie G: Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin. Cancer Res (2003) 63(23):8241-8247.
    • (2003) Cancer Res , vol.63 , Issue.23 , pp. 8241-8247
    • Blank, M.1    Mandel, M.2    Keisari, Y.3    Meruelo, D.4    Lavie, G.5
  • 48
    • 27744479712 scopus 로고    scopus 로고
    • Modulating molecular chaperone Hsp90 functions through reversible acetylation
    • Aoyagi S, Archer TK: Modulating molecular chaperone Hsp90 functions through reversible acetylation. Trends Cell Biol (2005) 15(11):565-567.
    • (2005) Trends Cell Biol , vol.15 , Issue.11 , pp. 565-567
    • Aoyagi, S.1    Archer, T.K.2
  • 49
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228
    • Yu X, Guo ZS, Marcu MG, Neckers L, Nguyen DM, Chen GA, Schrump DS: Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. J Natl Cancer Inst (2002) 94(7):504-513.
    • (2002) J Natl Cancer Inst , vol.94 , Issue.7 , pp. 504-513
    • Yu, X.1    Guo, Z.S.2    Marcu, M.G.3    Neckers, L.4    Nguyen, D.M.5    Chen, G.A.6    Schrump, D.S.7
  • 50
    • 18744396967 scopus 로고    scopus 로고
    • Multiple-target drugs: Inhibitors of heat shock protein 90 and of histone deacetylase
    • Budillon A, Bruzzese F, Di Gennaro E, Caraglia M: Multiple-target drugs: Inhibitors of heat shock protein 90 and of histone deacetylase. Curr Drug Targets (2005) 6(3):337-351.
    • (2005) Curr Drug Targets , vol.6 , Issue.3 , pp. 337-351
    • Budillon, A.1    Bruzzese, F.2    Di Gennaro, E.3    Caraglia, M.4
  • 51
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 8 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, Balasis M, Fiskus W, Guo F, Rocha K, Kumaraswamy S, Boyapalle S, Atadja P, Seto E et al: Inhibition of histone deacetylase 8 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem (2005) 280(29):26729-28734.
    • (2005) J Biol Chem , vol.280 , Issue.29 , pp. 26729-28734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11
  • 52
    • 33745131294 scopus 로고    scopus 로고
    • NeuTec Pharma commences patient recruitment in breast cancer clinical trial using its lead drug Mycograb
    • NeuTec Pharma plc: Press Release :September 19
    • NeuTec Pharma plc: NeuTec Pharma commences patient recruitment in breast cancer clinical trial using its lead drug Mycograb. Press Release (2005):September 19.
    • (2005)


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