메뉴 건너뛰기




Volumn 4, Issue 4, 2012, Pages 211-218

Heat shock protein 90 inhibition: Rationale and clinical potential

Author keywords

clinical trial; heat shock protein 90; pharmacological inhibition

Indexed keywords

5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; ALVESPIMYCIN; AT 13387; BORTEZOMIB; DOCETAXEL; EVEROLIMUS; GANETESPIB; GELDANAMYCIN; HEAT SHOCK PROTEIN 90 INHIBITOR; IMATINIB; KW 2478; PROTEASOME; RETASPIMYCIN; RITUXIMAB; TANESPIMYCIN; TRASTUZUMAB; UNCLASSIFIED DRUG;

EID: 84866549191     PISSN: 17588340     EISSN: 17588359     Source Type: Journal    
DOI: 10.1177/1758834012445574     Document Type: Review
Times cited : (47)

References (54)
  • 1
    • 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. (2005) Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 23: 4152–4161.
    • (2005) J Clin Oncol , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3    Pacey, S.4    Stapleton, S.5    Asad, Y.6
  • 2
    • 67449138839 scopus 로고    scopus 로고
    • CUDC-305, a novel synthetic HSP 90 inhibitor with unique pharmacologic properties for cancer therapy
    • Bao R. Lai C.J. Qu H. Wang D. Yin L. Zifcak B. et al. (2009) CUDC-305, a novel synthetic HSP 90 inhibitor with unique pharmacologic properties for cancer therapy. Clin Cancer Res 15: 4046–4057.
    • (2009) Clin Cancer Res , vol.15 , pp. 4046-4057
    • Bao, R.1    Lai, C.J.2    Qu, H.3    Wang, D.4    Yin, L.5    Zifcak, B.6
  • 3
    • 46749131522 scopus 로고    scopus 로고
    • Divergent synthesis of a pochonin library targeting HSP 90 and in vivo efficacy of an identified inhibitor
    • Barluenga S. Wang C. Fontaine J.G. Aouadi K. Beebe K. Tsutsumi S. et al. (2008) Divergent synthesis of a pochonin library targeting HSP 90 and in vivo efficacy of an identified inhibitor. Angew Chem Int Ed Engl 47: 4432–4435.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 4432-4435
    • Barluenga, S.1    Wang, C.2    Fontaine, J.G.3    Aouadi, K.4    Beebe, K.5    Tsutsumi, S.6
  • 4
    • 0035819537 scopus 로고    scopus 로고
    • Re: Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Blagosklonny M.V. (2001) Re: Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst 93: 239–240.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 239-240
    • Blagosklonny, M.V.1
  • 5
    • 0036494113 scopus 로고    scopus 로고
    • Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK), a novel Hsp90-client tyrosine kinase: down-regulation of NPM-ALK expression and tyrosine phosphorylation in ALK(+) CD30(+) lymphoma cells by the Hsp 90 antagonist 17-allylamino,17-demethoxygeldanamycin
    • Bonvini P. Gastaldi T. Falini B. Rosolen A. (2002) Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK), a novel Hsp90-client tyrosine kinase: down-regulation of NPM-ALK expression and tyrosine phosphorylation in ALK(+) CD30(+) lymphoma cells by the Hsp 90 antagonist 17-allylamino,17-demethoxygeldanamycin. Cancer Res 62: 1559–1566.
    • (2002) Cancer Res , vol.62 , pp. 1559-1566
    • Bonvini, P.1    Gastaldi, T.2    Falini, B.3    Rosolen, A.4
  • 6
    • 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 Hsp 90 molecular chaperone
    • Brough P.A. Barril X. Borgognoni J. Chene P. Davies N.G. Davis B. et al. (2009) Combining hit identification strategies: fragment-based and in silico approaches to orally active 2-aminothieno[2,3-d]pyrimidine inhibitors of the Hsp 90 molecular chaperone. J Med Chem 52: 4794–4809.
    • (2009) J Med Chem , vol.52 , pp. 4794-4809
    • Brough, P.A.1    Barril, X.2    Borgognoni, J.3    Chene, P.4    Davies, N.G.5    Davis, B.6
  • 7
    • 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. (2008) SNX2112, a synthetic heat shock protein 90 inhibitor, has potent antitumor activity against HER kinase-dependent cancers. Clin Cancer Res 14: 240–248.
    • (2008) Clin Cancer Res , vol.14 , pp. 240-248
    • Chandarlapaty, S.1    Sawai, A.2    Ye, Q.3    Scott, A.4    Silinski, M.5    Huang, K.6
  • 8
    • 0029011834 scopus 로고
    • Analysis of heat-shock protein expression in myeloid leukaemia cells by flow cytometry
    • Chant I.D. Rose P.E. Morris A.G. (1995) Analysis of heat-shock protein expression in myeloid leukaemia cells by flow cytometry. Br J Haematol 90: 163–168.
    • (1995) Br J Haematol , vol.90 , pp. 163-168
    • Chant, I.D.1    Rose, P.E.2    Morris, A.G.3
  • 9
    • 0027503365 scopus 로고
    • Heat shock protein hsp 70 in patients with axillary lymph node-negative breast cancer: prognostic implications
    • Ciocca D.R. Clark G.M. Tandon A.K. Fuqua S.A. Welch W.J. McGuire W.L. (1993) Heat shock protein hsp 70 in patients with axillary lymph node-negative breast cancer: prognostic implications. J Natl Cancer Inst 85: 570–574.
    • (1993) J Natl Cancer Inst , vol.85 , pp. 570-574
    • Ciocca, D.R.1    Clark, G.M.2    Tandon, A.K.3    Fuqua, S.A.4    Welch, W.J.5    McGuire, W.L.6
  • 10
    • 33645471864 scopus 로고    scopus 로고
    • Reaction of geldanamycin and C17-substituted analogues with glutathione: product identifications and pharmacological implications
    • Cysyk R.L. Parker R.J. Barchi J.J. Jr Steeg P.S. Hartman N.R. Strong J.M. (2006) Reaction of geldanamycin and C17-substituted analogues with glutathione: product identifications and pharmacological implications. Chem Res Toxicol 19: 376–381.
    • (2006) Chem Res Toxicol , vol.19 , pp. 376-381
    • Cysyk, R.L.1    Parker, R.J.2    Barchi, J.J.3    Steeg, P.S.4    Hartman, N.R.5    Strong, J.M.6
  • 11
    • 73149098932 scopus 로고    scopus 로고
    • The antiproliferative activity of the heat shock protein 90 inhibitor IPI-504 is not dependent on NAD(P) H:quinone oxidoreductase 1 activity in vivo
    • Douglas M. Lim A.R. Porter J.R. West K. Pink M.M. Ge J. et al. (2009) The antiproliferative activity of the heat shock protein 90 inhibitor IPI-504 is not dependent on NAD(P)H:quinone oxidoreductase 1 activity in vivo. Mol Cancer Ther 8: 3369–3378.
    • (2009) Mol Cancer Ther , vol.8 , pp. 3369-3378
    • Douglas, M.1    Lim, A.R.2    Porter, J.R.3    West, K.4    Pink, M.M.5    Ge, J.6
  • 12
    • 0032101569 scopus 로고    scopus 로고
    • Metabolism of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations
    • Egorin M.J. Rosen D.M. Wolff J.H. Callery P.S. Musser S.M. Eiseman J.L. (1998) Metabolism of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations. Cancer Res 58: 2385–2396.
    • (1998) Cancer Res , vol.58 , pp. 2385-2396
    • Egorin, M.J.1    Rosen, D.M.2    Wolff, J.H.3    Callery, P.S.4    Musser, S.M.5    Eiseman, J.L.6
  • 13
    • 80052440676 scopus 로고    scopus 로고
    • The novel HSP 90 inhibitor, IPI-493, is highly effective in human gastrointestinal stromal tumor xenografts carrying heterogeneous KIT mutations
    • Floris G. Sciot R. Wozniak A. van Looy T. Wellens J. Faa G. et al. (2011) The novel HSP 90 inhibitor, IPI-493, is highly effective in human gastrointestinal stromal tumor xenografts carrying heterogeneous KIT mutations. Clin Cancer Res 17: 5604–5614.
    • (2011) Clin Cancer Res , vol.17 , pp. 5604-5614
    • Floris, G.1    Sciot, R.2    Wozniak, A.3    van Looy, T.4    Wellens, J.5    Faa, G.6
  • 14
    • 33746662241 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90
    • Ge J. Normant E. Porter J.R. Ali J.A. Dembski M.S. Gao Y. et al. (2006) Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90. J Med Chem 49: 4606–4615.
    • (2006) J Med Chem , vol.49 , pp. 4606-4615
    • Ge, J.1    Normant, E.2    Porter, J.R.3    Ali, J.A.4    Dembski, M.S.5    Gao, Y.6
  • 15
    • 26444462561 scopus 로고    scopus 로고
    • Preclinical toxicity of a geldanamycin analog, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG)
    • in rats and dogs potential clinical relevance
    • Glaze E.R. Lambert A.L. Smith A.C. Page J.G. Johnson W.D. McCormick D.L. et al. (2005) Preclinical toxicity of a geldanamycin analog, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), in rats and dogs: potential clinical relevance. Cancer Chemother Pharmacol 56: 637–647.
    • (2005) Cancer Chemother Pharmacol , vol.56 , pp. 637-647
    • Glaze, E.R.1    Lambert, A.L.2    Smith, A.C.3    Page, J.G.4    Johnson, W.D.5    McCormick, D.L.6
  • 16
    • 0042885973 scopus 로고    scopus 로고
    • The Hsp 90 chaperone complex as a novel target for cancer therapy
    • Goetz M.P. Toft D.O. Ames M.M. Erlichman C. (2003) The Hsp 90 chaperone complex as a novel target for cancer therapy. Ann Oncol 14: 1169–1176.
    • (2003) Ann Oncol , vol.14 , pp. 1169-1176
    • Goetz, M.P.1    Toft, D.O.2    Ames, M.M.3    Erlichman, C.4
  • 17
    • 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. (2005) Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors. J Clin Oncol 23: 1885–1893.
    • (2005) J Clin Oncol , 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
  • 18
    • 27544446054 scopus 로고    scopus 로고
    • Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P) H:quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition
    • Guo W. Reigan P. Siegel D. Zirrolli J. Gustafson D. Ross D. (2005) Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res 65: 10006–10015.
    • (2005) Cancer Res , vol.65 , pp. 10006-10015
    • Guo, W.1    Reigan, P.2    Siegel, D.3    Zirrolli, J.4    Gustafson, D.5    Ross, D.6
  • 19
    • 77749309983 scopus 로고    scopus 로고
    • Measuring the pharmacodynamic effects of a novel Hsp 90 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. (2010) Measuring the pharmacodynamic effects of a novel Hsp 90 inhibitor on HER2/neu expression in mice using Zr-DFO-trastuzumab. PloS ONE 5: e8859.
    • (2010) PloS ONE , vol.5 , pp. e8859
    • Holland, J.P.1    Caldas-Lopes, E.2    Divilov, V.3    Longo, V.A.4    Taldone, T.5    Zatorska, D.6
  • 20
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs J.S. Xu W. Neckers L. (2003) Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3: 213–217.
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 22
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp 90 confers tumour selectivity on Hsp 90 inhibitors
    • Kamal A. Thao L. Sensintaffar J. Zhang L. Boehm M.F. Fritz L.C. et al. (2003) A high-affinity conformation of Hsp 90 confers tumour selectivity on Hsp 90 inhibitors. Nature 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
  • 23
    • 0029642276 scopus 로고
    • Differential expression of 70-kDa heat shock-protein in human oral tumorigenesis
    • Kaur J. Ralhan R. (1995) Differential expression of 70-kDa heat shock-protein in human oral tumorigenesis. Int J Cancer 63: 774–779.
    • (1995) Int J Cancer , vol.63 , pp. 774-779
    • Kaur, J.1    Ralhan, R.2
  • 25
    • 34548181032 scopus 로고    scopus 로고
    • FLT 3 inhibition in acute myeloid leukaemia
    • Knapper S. (2007) FLT 3 inhibition in acute myeloid leukaemia. Br J Haematol 138: 687–699.
    • (2007) Br J Haematol , vol.138 , pp. 687-699
    • Knapper, S.1
  • 26
    • 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. (2010) Phase I trial of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein inhibitor, administered twice weekly in patients with advanced malignancies. Eur J Cancer 46: 340–347.
    • (2010) Eur J 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
  • 27
    • 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. (2010) 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 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
  • 28
    • 52049125709 scopus 로고    scopus 로고
    • The novel HSP 90 inhibitor STA-9090 exhibits activity against Kit-dependent and -independent malignant mast cell tumors
    • Lin T.Y. Bear M. Du Z. Foley K.P. Ying W. Barsoum J. et al. (2008) The novel HSP 90 inhibitor STA-9090 exhibits activity against Kit-dependent and -independent malignant mast cell tumors. Exp Hematol 36: 1266–1277.
    • (2008) Exp Hematol , vol.36 , pp. 1266-1277
    • Lin, T.Y.1    Bear, M.2    Du, Z.3    Foley, K.P.4    Ying, W.5    Barsoum, J.6
  • 30
    • 64349108515 scopus 로고    scopus 로고
    • Potent non-benzoquinone ansamycin heat shock protein 90 inhibitors from genetic engineering of Streptomyces hygroscopicus
    • Menzella H.G. Tran T.T. Carney J.R. Lau-Wee J. Galazzo J. Reeves C.D. et al. (2009) Potent non-benzoquinone ansamycin heat shock protein 90 inhibitors from genetic engineering of Streptomyces hygroscopicus. J Med Chem 52: 1518–1521.
    • (2009) J Med Chem , vol.52 , pp. 1518-1521
    • Menzella, H.G.1    Tran, T.T.2    Carney, J.R.3    Lau-Wee, J.4    Galazzo, J.5    Reeves, C.D.6
  • 31
    • 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. (2007) Combination of trastuzumab and tanespimycin (17-AAG, KOS-953) is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer:a phase I dose-escalation study. J Clin Oncol 25: 5410–5417.
    • (2007) J Clin Oncol , 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
  • 32
    • 0031297298 scopus 로고    scopus 로고
    • The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones
    • Morimoto R.I. Kline M.P. Bimston D.N. Cotto J.J. (1997) The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem 32: 17–29.
    • (1997) Essays Biochem , vol.32 , pp. 17-29
    • Morimoto, R.I.1    Kline, M.P.2    Bimston, D.N.3    Cotto, J.J.4
  • 34
    • 34248187981 scopus 로고    scopus 로고
    • Heat shock protein 90: the cancer chaperone
    • Neckers L. (2007) Heat shock protein 90: the cancer chaperone. J Biosci 32: 517–530.
    • (2007) J Biosci , vol.32 , pp. 517-530
    • Neckers, L.1
  • 35
    • 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. (2007) Heat shock protein 90: a potential therapeutic target in leukemic progenitor and stem cells harboring mutant BCR-ABL resistant to kinase inhibitors. Cell Cycle 6: 2227–2231.
    • (2007) Cell Cycle , vol.6 , pp. 2227-2231
    • Peng, C.1    Li, D.2    Li, S.3
  • 36
    • 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. (2011) 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. Clin Cancer Res 17: 6831–6839.
    • (2011) Clin Cancer Res , 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
  • 37
    • 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. (2010) Phase I pharmacokinetic and pharmacodynamic study of 17-dimethylaminoethylamino-17-demethoxygeldanamycin, an inhibitor of heat-shock protein 90, in patients with advanced solid tumors. J Clin Oncol 28: 1520–1526.
    • (2010) J Clin Oncol , 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
  • 38
    • 78851472038 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 (HSP90) as a therapeutic strategy for the treatment of myeloma and other cancers
    • Richardson P.G. Mitsiades C.S. Laubach J.P. Lonial S. Chanan-Khan A.A. Anderson K.C. (2011) Inhibition of heat shock protein 90 (HSP90) as a therapeutic strategy for the treatment of myeloma and other cancers. Br J Haematol 152: 367–379.
    • (2011) Br J Haematol , vol.152 , pp. 367-379
    • Richardson, P.G.1    Mitsiades, C.S.2    Laubach, J.P.3    Lonial, S.4    Chanan-Khan, A.A.5    Anderson, K.C.6
  • 39
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F. (1996) Discovery of the heat shock response. Cell Stress Chaperones 1: 97–98.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 40
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp 90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe S.M. Prodromou C. O'Brien R. Ladbury J.E. Piper P.W. Pearl L.H. (1999) Structural basis for inhibition of the Hsp 90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42: 260–266.
    • (1999) J Med Chem , vol.42 , 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
  • 41
    • 0029008487 scopus 로고
    • Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases
    • Sepp-Lorenzino L. Ma Z. Lebwohl D.E. Vinitsky A. Rosen N. (1995) Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases. J Biol Chem 270: 16580–16587.
    • (1995) J Biol Chem , vol.270 , pp. 16580-16587
    • Sepp-Lorenzino, L.1    Ma, Z.2    Lebwohl, D.E.3    Vinitsky, A.4    Rosen, N.5
  • 42
    • 22244485706 scopus 로고    scopus 로고
    • Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins
    • Shimamura T. Lowell A.M. Engelman J.A. Shapiro G.I. (2005) Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins. Cancer Res 65: 6401–6408.
    • (2005) Cancer Res , vol.65 , pp. 6401-6408
    • Shimamura, T.1    Lowell, A.M.2    Engelman, J.A.3    Shapiro, G.I.4
  • 43
    • 33745574028 scopus 로고    scopus 로고
    • Early tumor response to Hsp 90 therapy using HER 2 PET: comparison with 18F-FDG PET
    • Smith-Jones P.M. Solit D. Afroze F. Rosen N. Larson S.M. (2006) Early tumor response to Hsp 90 therapy using HER 2 PET: comparison with 18F-FDG PET. J Nucl Med 47: 793–796.
    • (2006) J Nucl Med , vol.47 , pp. 793-796
    • Smith-Jones, P.M.1    Solit, D.2    Afroze, F.3    Rosen, N.4    Larson, S.M.5
  • 44
    • 33751258297 scopus 로고    scopus 로고
    • Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti- cancer agent directed against Hsp90
    • Sydor J.R. Normant E. Pien C.S. Porter J.R. Ge J. Grenier L. et al. (2006) Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti- cancer agent directed against Hsp90. Proc Natl Acad Sci U S A 103: 17408–17413.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17408-17413
    • Sydor, J.R.1    Normant, E.2    Pien, C.S.3    Porter, J.R.4    Ge, J.5    Grenier, L.6
  • 46
    • 0141708701 scopus 로고    scopus 로고
    • Natural product origins of Hsp 90 inhibitors
    • Uehara Y. (2003) Natural product origins of Hsp 90 inhibitors. Curr Cancer Drug Targets 3: 325–330.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 325-330
    • Uehara, Y.1
  • 47
    • 25844519550 scopus 로고    scopus 로고
    • HSP 90 and the chaperoning of cancer
    • Whitesell L. Lindquist S.L. (2005) HSP 90 and the chaperoning of cancer. Nat Rev Cancer 5: 761–772.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 48
    • 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 E.G. de Costa B. Myers C.E. Neckers L.M. (1994) 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 U S A 91: 8324–8328.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    de Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 49
    • 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. (2007) Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann N Y Acad Sci 1113: 202–216.
    • (2007) Ann N Y Acad Sci , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 50
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb 2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • J Biol Chem
    • Xu W. Mimnaugh E. Rosser M.F. Nicchitta C. Marcu M. Yarden Y. et al. (2001) Sensitivity of mature Erbb 2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 276: 3702–3708.
    • (2001) , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3    Nicchitta, C.4    Marcu, M.5    Yarden, Y.6
  • 51
    • 3042685847 scopus 로고    scopus 로고
    • New efficient synthesis of resorcinylic macrolides via ynolides: establishment of cycloproparadicicol as synthetically feasible preclinical anticancer agent based on Hsp 90 as the target
    • Yang Z.Q. Geng X. Solit D. Pratilas C.A. Rosen N. Danishefsky S.J. (2004) New efficient synthesis of resorcinylic macrolides via ynolides: establishment of cycloproparadicicol as synthetically feasible preclinical anticancer agent based on Hsp 90 as the target. J Am Chem Soc 126: 7881–7889.
    • (2004) J Am Chem Soc , vol.126 , pp. 7881-7889
    • Yang, Z.Q.1    Geng, X.2    Solit, D.3    Pratilas, C.A.4    Rosen, N.5    Danishefsky, S.J.6
  • 52
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells
    • Yufu Y. Nishimura J. Nawata H. (1992) High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells. Leuk Res 16: 597–605.
    • (1992) Leuk Res , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 53
    • 52449110026 scopus 로고    scopus 로고
    • Optimizing natural products by biosynthetic engineering: discovery of nonquinone Hsp 90 inhibitors
    • Zhang M.Q. Gaisser S. Nur E.A.M. Sheehan L.S. Vousden W.A. Gaitatzis N. et al. (2008) Optimizing natural products by biosynthetic engineering: discovery of nonquinone Hsp 90 inhibitors. J Med Chem 51: 5494–5497.
    • (2008) J Med Chem , vol.51 , pp. 5494-5497
    • Zhang, M.Q.1    Gaisser, S.2    Nur, E.A.M.3    Sheehan, L.S.4    Vousden, W.A.5    Gaitatzis, N.6
  • 54
    • 72149125851 scopus 로고    scopus 로고
    • Characterization of celastrol to inhibit hsp 90 and cdc 37 interaction
    • Zhang T. Li Y. Yu Y. Zou P. Jiang Y. Sun D. (2009) Characterization of celastrol to inhibit hsp 90 and cdc 37 interaction. J Biol Chem 284: 35381–35389.
    • (2009) J Biol Chem , vol.284 , pp. 35381-35389
    • Zhang, T.1    Li, Y.2    Yu, Y.3    Zou, P.4    Jiang, Y.5    Sun, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.