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Volumn 82, Issue 8, 2004, Pages 488-499

Targeting multiple signal transduction pathways through inhibition of Hsp90

Author keywords

17 Allylamino 17 demethoxygeldanamycin; AKT; Her 2; Hsp90; Raf

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 2 (2 CHLORO 4 IODOANILINO) N CYCLOPROPYLMETHOXY 3,4 DIFLUOROBENZAMIDE; 4 [6 METHOXY 7 [3 (1 PIPERIDINYL)PROPOXY] 4 QUINAZOLINYL] 1 PIPERAZINECARBOXYLIC ACID (4 ISOPROPOXYPHENYL)AMIDE; BCR ABL PROTEIN; BENZOQUINONE DERIVATIVE; CEP 701; CISPLATIN; EPIDERMAL GROWTH FACTOR RECEPTOR ANTIBODY; EVEROLIMUS; FLT3 LIGAND; GEFITINIB; HEAT SHOCK PROTEIN 90; HER 2 PROTEIN ANTIBODY; HERBIMYCIN A; IMATINIB; MIDOSTAURIN; NOVOBIOCIN; PACLITAXEL; PROTEIN ANTIBODY; PROTEIN INHIBITOR; PROTEIN KINASE INHIBITOR; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; SEMAXANIB; SORAFENIB; SR 13668; TARGET OF RAPAMYCIN KINASE; TEMSIROLIMUS; TRASTUZUMAB; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 4344674482     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00109-004-0549-9     Document Type: Review
Times cited : (350)

References (87)
  • 1
    • 0141596939 scopus 로고    scopus 로고
    • Structure and functional relationships of Hsp90
    • Prodromou C, Pearl LH (2003) Structure and functional relationships of Hsp90. Curr Cancer Drug Targets 3:301-323
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 301-323
    • Prodromou, C.1    Pearl, L.H.2
  • 3
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney A, Workman P (2002) HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2:3-24
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 4
    • 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, Myers CE, Neckers LM (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 USA 91:8324-8328
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 5
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100:57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 6
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso AD, Solit DB, Munster PN, Rosen N (2002) Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 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
  • 7
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N (2002) Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 277:39858-39866
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 8
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, Neckers L (2001) Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 276:3702-3708
    • (2001) J Biol Chem , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3    Nicchitta, C.4    Marcu, M.5    Yarden, Y.6    Neckers, L.7
  • 9
    • 0027452530 scopus 로고
    • Differential heat stress stability of epidermal growth factor receptor and erbB-2 receptor tyrosine kinase activities
    • Liu SM, Carpenter G (1993) Differential heat stress stability of epidermal growth factor receptor and erbB-2 receptor tyrosine kinase activities. J Cell Physiol 157:237-242
    • (1993) J Cell Physiol , vol.157 , pp. 237-242
    • Liu, S.M.1    Carpenter, G.2
  • 10
    • 0034864813 scopus 로고    scopus 로고
    • HER2 overexpression in various tumor types, focussing on its relationship to the development of invasive breast cancer
    • Menard S, Casalini P, Campiglio M, Pupa S, Agresti R, Tagliabue E (2001) HER2 overexpression in various tumor types, focussing on its relationship to the development of invasive breast cancer. Ann Oncol 12 Suppl 1: S15-19
    • (2001) Ann Oncol , vol.12 , Issue.1 SUPPL.
    • Menard, S.1    Casalini, P.2    Campiglio, M.3    Pupa, S.4    Agresti, R.5    Tagliabue, E.6
  • 11
    • 0030897649 scopus 로고    scopus 로고
    • Growth factor receptors as molecular targets for cancer diagnosis and therapy
    • Zalutsky MR (1997) Growth factor receptors as molecular targets for cancer diagnosis and therapy. Q J Nucl Med 41:71-77
    • (1997) Q J Nucl Med , vol.41 , pp. 71-77
    • Zalutsky, M.R.1
  • 13
    • 0037109014 scopus 로고    scopus 로고
    • ZD1839 (Iressa): An orally active inhibitor of epidermal growth factor signaling with potential for cancer therapy
    • Wakeling AE, Guy SP, Woodburn JR, Ashton SE, Curry BJ, Barker AJ, Gibson KH (2002) ZD1839 (Iressa): an orally active inhibitor of epidermal growth factor signaling with potential for cancer therapy. Cancer Res 62:5749-5754
    • (2002) Cancer Res , vol.62 , pp. 5749-5754
    • Wakeling, A.E.1    Guy, S.P.2    Woodburn, J.R.3    Ashton, S.E.4    Curry, B.J.5    Barker, A.J.6    Gibson, K.H.7
  • 14
    • 0141645488 scopus 로고    scopus 로고
    • Mechanism of action of anti-HER2 monoclonal antibodies: Scientific update on trastuzumab and 2C4
    • Albanell J, Codony J, Rovira A, Mellado B, Gascon P (2003) Mechanism of action of anti-HER2 monoclonal antibodies: scientific update on trastuzumab and 2C4. Adv Exp Med Biol 532:253-268
    • (2003) Adv Exp Med Biol , vol.532 , pp. 253-268
    • Albanell, J.1    Codony, J.2    Rovira, A.3    Mellado, B.4    Gascon, P.5
  • 15
    • 1542751704 scopus 로고    scopus 로고
    • Inhibiting tyrosine kinases: Successes and limitations
    • Arteaga CL (2003) Inhibiting tyrosine kinases: successes and limitations. Cancer Biol Ther 2:S79-S83
    • (2003) Cancer Biol Ther , vol.2
    • Arteaga, C.L.1
  • 17
    • 1942431966 scopus 로고    scopus 로고
    • The Achilles heel of ErbB-2/HER2: Regulation by the Hsp90 chaperone machine and potential for pharmacological intervention
    • Cirri A, Kochupurakkal BS, Yarden Y (2004) The Achilles heel of ErbB-2/HER2: regulation by the Hsp90 chaperone machine and potential for pharmacological intervention. Cell Cycle 3:51-60
    • (2004) Cell Cycle , vol.3 , pp. 51-60
    • Cirri, A.1    Kochupurakkal, B.S.2    Yarden, Y.3
  • 18
    • 0037265586 scopus 로고    scopus 로고
    • Development of small molecule Hsp90 inhibitors: Utilizing both forward and reverse chemical genomics for drug identification
    • Neckers L (2003) Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification. Curr Med Chem 10:733-739
    • (2003) Curr Med Chem , vol.10 , pp. 733-739
    • Neckers, L.1
  • 19
    • 0347132269 scopus 로고    scopus 로고
    • Regulation of the c-Abl and Bcr-abl tyrosine kinases
    • Hantschel O, Superti-Furga G (2004) Regulation of the c-Abl and Bcr-abl tyrosine kinases. Nat Rev Mol Cell Biol 5:33-44
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 33-44
    • Hantschel, O.1    Superti-Furga, G.2
  • 20
    • 0038777142 scopus 로고    scopus 로고
    • Imatinib: A targeted clinical drug development
    • Capdeville R, Silberman S (2003) Imatinib: a targeted clinical drug development. Semin Hematol 40:15-20
    • (2003) Semin Hematol , vol.40 , pp. 15-20
    • Capdeville, R.1    Silberman, S.2
  • 21
    • 0037108879 scopus 로고    scopus 로고
    • Molecular characterization and sensitivity of STI-571 (imatinib mesylate, Gleevec)-resistant, Bcr-abl-positive, human acute leukemia cells to SRC kinase inhibitor PD180970 and 17-allylamino-17-demethoxygeldanamycin
    • Nimmanapalli R, O'Bryan E, Huang M, Bali P, Burnette PK, Loughran T, Tepperberg J, Jove R, Bhalla K (2002) Molecular characterization and sensitivity of STI-571 (imatinib mesylate, Gleevec)-resistant, Bcr-abl-positive, human acute leukemia cells to SRC kinase inhibitor PD180970 and 17-allylamino-17- demethoxygeldanamycin. Cancer Res 62:5761-5769
    • (2002) Cancer Res , vol.62 , pp. 5761-5769
    • Nimmanapalli, R.1    O'Bryan, E.2    Huang, M.3    Bali, P.4    Burnette, P.K.5    Loughran, T.6    Tepperberg, J.7    Jove, R.8    Bhalla, K.9
  • 22
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre ME, Mohammed M, Ellwood K, Hsu N, Paquette R, Rao PN, Sawyers CL (2001) Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification. Science 293:876-880
    • (2001) Science , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3    Hsu, N.4    Paquette, R.5    Rao, P.N.6    Sawyers, C.L.7
  • 23
    • 0035266132 scopus 로고    scopus 로고
    • Geldanamycin and its analogue. 17-allylamino-17-demethoxygeldanamycin lowers Bcr-abl levels and induces apoptosis and differentiation of Bcr-abl-positive human leukemic blasts
    • Nimmanapalli R, O'Bryan E, Bhalla K (2001) Geldanamycin and its analogue. 17-allylamino-17-demethoxygeldanamycin lowers Bcr-abl levels and induces apoptosis and differentiation of Bcr-abl-positive human leukemic blasts. Cancer Res 61:1799-1804
    • (2001) Cancer Res , vol.61 , pp. 1799-1804
    • Nimmanapalli, R.1    O'Bryan, E.2    Bhalla, K.3
  • 24
    • 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 LM, Wortman I, An WG, Schulte TW, Soga S, Murakata C, Tamaoki T, Akinaga S (2000) 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 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    Murakata, C.7    Tamaoki, T.8    Akinaga, S.9
  • 25
    • 0037108448 scopus 로고    scopus 로고
    • BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90
    • Gorre ME, Ellwood-Yen K, Chiosis G, Rosen N, Sawyers CL (2002) BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90. Blood 100:3041-3044
    • (2002) Blood , vol.100 , pp. 3041-3044
    • Gorre, M.E.1    Ellwood-Yen, K.2    Chiosis, G.3    Rosen, N.4    Sawyers, C.L.5
  • 27
    • 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 AR, Hudson WA, Kersey JH (2003) FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases. Clin Cancer Res 9:4483-4493
    • (2003) Clin Cancer Res , 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
  • 30
    • 0141465061 scopus 로고    scopus 로고
    • The role of FLT3 in haematopoietic malignancies
    • Stirewalt DL, Radich JP (2003) The role of FLT3 in haematopoietic malignancies. Nat Rev Cancer 3:650-665
    • (2003) Nat Rev Cancer , vol.3 , pp. 650-665
    • Stirewalt, D.L.1    Radich, J.P.2
  • 31
    • 1542313903 scopus 로고    scopus 로고
    • Mutations in the tyrosine kinase domain of FLT3 define a new molecular mechanism of acquired drug resistance to PTK inhibitors in FLT3-ITD transformed hematopoietic cells
    • Bagrintseva K, Schwab R, Kohl TM, Schnittger S, Eichenlaub S, Ellwart JW, Hiddemann W, Spiekermann K (2004) Mutations in the tyrosine kinase domain of FLT3 define a new molecular mechanism of acquired drug resistance to PTK inhibitors in FLT3-ITD transformed hematopoietic cells. Blood 103:2266-2275
    • (2004) Blood , vol.103 , pp. 2266-2275
    • Bagrintseva, K.1    Schwab, R.2    Kohl, T.M.3    Schnittger, S.4    Eichenlaub, S.5    Ellwart, J.W.6    Hiddemann, W.7    Spiekermann, K.8
  • 33
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco I, Sawyers CL (2002) The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat Rev Cancer 2:489-501
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 34
    • 0041802820 scopus 로고    scopus 로고
    • Targeting mTOR signaling for cancer therapy
    • Huang S, Houghton PJ (2003) Targeting mTOR signaling for cancer therapy. Curr Opin Pharmacol 3:371-377
    • (2003) Curr Opin Pharmacol , vol.3 , pp. 371-377
    • Huang, S.1    Houghton, P.J.2
  • 35
    • 0036735346 scopus 로고    scopus 로고
    • Enhanced sensitivity of multiple myeloma cells containing PTEN mutations to CCI-779
    • Shi Y, Gera J, Hu L, Hsu JH, Bookstein R, Li W, Lichtenstein A (2002) Enhanced sensitivity of multiple myeloma cells containing PTEN mutations to CCI-779. Cancer Res 62:5027-5034
    • (2002) Cancer Res , vol.62 , pp. 5027-5034
    • Shi, Y.1    Gera, J.2    Hu, L.3    Hsu, J.H.4    Bookstein, R.5    Li, W.6    Lichtenstein, A.7
  • 36
    • 0036817880 scopus 로고    scopus 로고
    • Clinical development of mammalian target of rapamycin inhibitors
    • Dancey JE (2002) Clinical development of mammalian target of rapamycin inhibitors. Hematol Oncol Clin North Am 16:1101-1114
    • (2002) Hematol Oncol Clin North Am , vol.16 , pp. 1101-1114
    • Dancey, J.E.1
  • 37
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S, Fujita N, Tsuruo T (2000) Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci USA 97:10832-10837
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 39
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of Hsp90 in signaling and stability of 3-phosphoinositide- dependent kinase-1
    • Fujita N, Sato S, Ishida A, Tsuruo T (2002) Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1. J Biol Chem 277:10346-10353
    • (2002) J Biol Chem , vol.277 , pp. 10346-10353
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 40
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol
    • Solit DB, Basso AD, Olshen AB, Scher HI, Rosen N (2003) Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol. Cancer Res 63:2139-2144
    • (2003) Cancer Res , vol.63 , pp. 2139-2144
    • Solit, D.B.1    Basso, A.D.2    Olshen, A.B.3    Scher, H.I.4    Rosen, N.5
  • 44
    • 0029824710 scopus 로고    scopus 로고
    • Nerve growth factor-mediated activation of the mitogen-activated protein (MAP) kinase cascade involves a signaling complex containing B-Raf and HSP90
    • Jaiswal RK, Weissinger E, Kolch W, Landreth GE (1996) Nerve growth factor-mediated activation of the mitogen-activated protein (MAP) kinase cascade involves a signaling complex containing B-Raf and HSP90. J Biol Chem 271:23626-23629
    • (1996) J Biol Chem , vol.271 , pp. 23626-23629
    • Jaiswal, R.K.1    Weissinger, E.2    Kolch, W.3    Landreth, G.E.4
  • 45
    • 0036401105 scopus 로고    scopus 로고
    • BAY 43-9006: Preclinical data
    • Wilhelm S, Chien DS (2002) BAY 43-9006: preclinical data. Curr Pharm Des 8:2255-2257
    • (2002) Curr Pharm des , vol.8 , pp. 2255-2257
    • Wilhelm, S.1    Chien, D.S.2
  • 48
    • 0141616506 scopus 로고    scopus 로고
    • Activity of the Raf kinase inhibitor BAY 43-9006 in patients with advanced solid tumors
    • Anonymous (2003) Activity of the Raf kinase inhibitor BAY 43-9006 in patients with advanced solid tumors. Clin Colorectal Cancer 3:16-18
    • (2003) Clin Colorectal Cancer , vol.3 , pp. 16-18
  • 51
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • Karin M, Ben-Neriah Y (2000) Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 18:621-663
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 52
    • 0033996762 scopus 로고    scopus 로고
    • The I kappa B kinase (IKK) and NF-kappa B: Key elements of proinflammatory signalling
    • Karin M, Delhase M (2000) The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling. Semin Immunol 12:85-98
    • (2000) Semin Immunol , vol.12 , pp. 85-98
    • Karin, M.1    Delhase, M.2
  • 53
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • Chen G, Cao P, Goeddel DV (2002) TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 9:401-410
    • (2002) Mol Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 55
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • Polakis P (2000) Wnt signaling and cancer. Genes Dev 14:1837-1851
    • (2000) Genes Dev , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 57
    • 0031718204 scopus 로고    scopus 로고
    • Differential molecular interactions of beta-catenin and plakoglobin in adhesion, signaling and cancer
    • Ben-Ze'ev A, Geiger B (1998) Differential molecular interactions of beta-catenin and plakoglobin in adhesion, signaling and cancer. Curr Opin Cell Biol 10:629-639
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 629-639
    • Ben-Ze'ev, A.1    Geiger, B.2
  • 62
    • 0022967572 scopus 로고
    • Phenotypic change from transformed to normal induced by benzoquinonoid ansamycins accompanies inactivation of p60src in rat kidney cells infected with Rous sarcoma virus
    • Uehara Y, Hori M, Takeuchi T, Umezawa H (1986) 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 6:2198-2206
    • (1986) Mol Cell Biol , vol.6 , pp. 2198-2206
    • Uehara, Y.1    Hori, M.2    Takeuchi, T.3    Umezawa, H.4
  • 63
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte TW, Blagosklonny MV, Ingui C, Neckers L (1995) Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem 270:24585-24588
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 64
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90:65-75
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 65
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe SM, Prodromou C, O'Brien R, Ladbury JE, Piper PW, Pearl LH (1999) Structural basis for inhibition of the Hsp90 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
  • 66
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-gel-danamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP (1997) Crystal structure of an Hsp90-gel-danamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 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
  • 67
    • 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 (1998) The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 42:273-279
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 68
    • 0000076189 scopus 로고    scopus 로고
    • Comparison of geldanamycin (NSC-122750) and 17-allylaminogeldanamycin (NSC-330507D) toxicity in rats
    • Page JHJ, Fulton R et al (1997) Comparison of geldanamycin (NSC-122750) and 17-allylaminogeldanamycin (NSC-330507D) toxicity in rats. Proc Am Assoc Cancer Res 38:308
    • (1997) Proc Am Assoc Cancer Res , vol.38 , pp. 308
    • Page, J.H.J.1    Fulton, R.2
  • 71
    • 0026823291 scopus 로고
    • Radicicol, an agent inducing the reversal of transformed phenotypes of src-transformed fibroblasts
    • Kwon HJ, Yoshida M, Abe K, Horinouchi S, Beppu T (1992) Radicicol, an agent inducing the reversal of transformed phenotypes of src-transformed fibroblasts. Biosci Biotechnol Biochem 56:538-539
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 538-539
    • Kwon, H.J.1    Yoshida, M.2    Abe, K.3    Horinouchi, S.4    Beppu, T.5
  • 72
    • 0029085027 scopus 로고
    • Suppression of RAS and MOS transformation by radicicol
    • Zhao JF, Nakano H, Sharma S (1995) Suppression of RAS and MOS transformation by radicicol. Oncogene 11:161-173
    • (1995) Oncogene , vol.11 , pp. 161-173
    • Zhao, J.F.1    Nakano, H.2    Sharma, S.3
  • 73
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte TW, Akinaga S, Soga S, Sullivan W, Stensgard B, Toft D, Neckers LM (1998) Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 3:100-108
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 74
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
    • Sharma SV, Agatsuma T, Nakano H (1998) Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene 16:2639-2645
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 77
    • 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 (2001) 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 8:289-299
    • (2001) Chem Biol , 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    Rosen, N.7
  • 78
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-based novel class of hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis G, Huezo H, Lucas B, Rosen N (2002) Development of a purine-based novel class of hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg Med Chem 10:3555-3564
    • (2002) Bioorg Med Chem , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Huezo, H.2    Lucas, B.3    Rosen, N.4
  • 79
    • 0141454205 scopus 로고    scopus 로고
    • Development of 9-alkyl-8-benzyl-9H-purin-6-ylamines as inhibitors of the Hsp90 family
    • Chiosis G, Shtil A, Lucas B, Huezo H, Rosen N (2001) Development of 9-alkyl-8-benzyl-9H-purin-6-ylamines as inhibitors of the Hsp90 family. Clin Cancer Res 7:474
    • (2001) Clin Cancer Res , vol.7 , pp. 474
    • Chiosis, G.1    Shtil, A.2    Lucas, B.3    Huezo, H.4    Rosen, N.5
  • 81
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • Marcu MG, Chadli A, Bouhouche I, Catelli M, Neckers LM (2000) The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J Biol Chem 275:37181-37186
    • (2000) J Biol Chem , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 82
    • 0033231024 scopus 로고    scopus 로고
    • A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90
    • Itoh H, Ogura M, Komatsuda A, Wakui H, Miura AB, Tashima Y (1999) A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90. Biochem J 343:697-703
    • (1999) Biochem J , vol.343 , pp. 697-703
    • Itoh, H.1    Ogura, M.2    Komatsuda, A.3    Wakui, H.4    Miura, A.B.5    Tashima, Y.6
  • 83
    • 0036510547 scopus 로고    scopus 로고
    • A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket
    • Soti C, Racz A, Csermely P (2002) A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket. J Biol Chem 277:7066-7075
    • (2002) J Biol Chem , vol.277 , pp. 7066-7075
    • Soti, C.1    Racz, A.2    Csermely, P.3
  • 84
    • 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 (2000) Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J Natl Cancer Inst 92:242-248
    • (2000) J Natl Cancer Inst , vol.92 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 85
    • 0036718795 scopus 로고    scopus 로고
    • ATPases as drug targets: Learning from their structure
    • Chene P (2002) ATPases as drug targets: learning from their structure. Nat Rev Drug Discov 1:665-673
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 665-673
    • Chene, P.1
  • 86
    • 4344565621 scopus 로고    scopus 로고
    • Geldanamycin and its 17 allylamino derivative antagonize the action of cis-platin in human colon cancer cells
    • Vasilevskaya I, Rakitina TV, O'Dwyer P (2002) Geldanamycin and its 17 allylamino derivative antagonize the action of cis-platin in human colon cancer cells. Proc Am Assoc Cancer Res 43:342
    • (2002) Proc Am Assoc Cancer Res , vol.43 , pp. 342
    • Vasilevskaya, I.1    Rakitina, T.V.2    O'Dwyer, P.3
  • 87
    • 0034902025 scopus 로고    scopus 로고
    • Enhancement of paclitaxel-mediated cytotoxicity in lung cancer cells by 17-allylamino geldanamycin: In vitro and in vivo analysis
    • Nguyen DM, Lorang D, Chen GA, Stewart JHT, Tabibi E, Schrump DS (2001) Enhancement of paclitaxel-mediated cytotoxicity in lung cancer cells by 17-allylamino geldanamycin: in vitro and in vivo analysis. Ann Thorac Surg 72:371-378
    • (2001) Ann Thorac Surg , vol.72 , pp. 371-378
    • Nguyen, D.M.1    Lorang, D.2    Chen, G.A.3    Stewart, J.H.T.4    Tabibi, E.5    Schrump, D.S.6


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