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Volumn 11, Issue 19 I, 2005, Pages 7023-7032

Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; CHAPERONE; CYCLIN DEPENDENT KINASE 4; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; PROTEIN INHIBITOR; RAF PROTEIN; UNCLASSIFIED DRUG;

EID: 26444482073     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: 10.1158/1078-0432.CCR-05-0518     Document Type: Article
Times cited : (164)

References (58)
  • 1
    • 0020491477 scopus 로고
    • Purification of the major mammalian heat shock proteins
    • Welch WJ, Feramisco JR. Purification of the major mammalian heat shock proteins. J Biol Chem 1982; 257:14949-59.
    • (1982) J Biol Chem , vol.257 , pp. 14949-14959
    • Welch, W.J.1    Feramisco, J.R.2
  • 2
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney A, Workman P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2002;2:3-24.
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 3
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs JS, Xu W, Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 2003;3:213-7.
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 5
    • 26444464960 scopus 로고    scopus 로고
    • Picard D. http://www.picard.ch/downloads/ HSP90interactors.pdf.
    • Picard, D.1
  • 6
    • 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, et al. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 2001;276:3702-8.
    • (2001) J Biol Chem , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3
  • 7
    • 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. 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 2001;61:1799-804.
    • (2001) Cancer Res , vol.61 , pp. 1799-1804
    • Nimmanapalli, R.1    O'Bryan, E.2    Bhalla, K.3
  • 9
    • 0029985050 scopus 로고    scopus 로고
    • Hsp90 regulates androgen receptor hormone binding affinity in vivo
    • Fang Y, Fliss AE, Robins DM, Caplan AJ. Hsp90 regulates androgen receptor hormone binding affinity in vivo. J Biol Chem 1996;271:28697-702.
    • (1996) J Biol Chem , vol.271 , pp. 28697-28702
    • Fang, Y.1    Fliss, A.E.2    Robins, D.M.3    Caplan, A.J.4
  • 10
    • 0029813620 scopus 로고    scopus 로고
    • Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway
    • Schulte TW, Blagosklonny MV, Romanova L, et al. Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway. Mol Cell Biol 1996;16:5839-45.
    • (1996) Mol Cell Biol , vol.16 , pp. 5839-5845
    • Schulte, T.W.1    Blagosklonny, M.V.2    Romanova, L.3
  • 11
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova L, Leng X, Parker SB, Harper JW. Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev 1996;10:1491-502.
    • (1996) Genes Dev , vol.10 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.2    Parker, S.B.3    Harper, J.W.4
  • 12
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S, Fujita N, Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci U S A 2000;97:10832-7.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 13
    • 0031909866 scopus 로고    scopus 로고
    • The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
    • Whitesell L, Sutphin PD, Pulcini EJ, Martinez JD, Cook PH. The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 1998;18:1517-24.
    • (1998) Mol Cell Biol , vol.18 , pp. 1517-1524
    • Whitesell, L.1    Sutphin, P.D.2    Pulcini, E.J.3    Martinez, J.D.4    Cook, P.H.5
  • 14
    • 0034650543 scopus 로고    scopus 로고
    • The geldanamycins are potent inhibitors of the hepatocyte growth factor/scatter factor-met-urokinase plasminogen activator-plasmin proteolytic network
    • Webb CP, Hose CD, Koochekpour S, et al. The geldanamycins are potent inhibitors of the hepatocyte growth factor/scatter factor-met-urokinase plasminogen activator-plasmin proteolytic network. Cancer Res 2000;60:342-9.
    • (2000) Cancer Res , vol.60 , pp. 342-349
    • Webb, C.P.1    Hose, C.D.2    Koochekpour, S.3
  • 15
    • 0035844136 scopus 로고    scopus 로고
    • Stable association of hsp90 and p23, but not hsp70, with active human telomerase
    • Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but not hsp70, with active human telomerase. J Biol Chem 2001;276:15571-4.
    • (2001) J Biol Chem , vol.276 , pp. 15571-15574
    • Forsythe, H.L.1    Jarvis, J.L.2    Turner, J.W.3    Elmore, L.W.4    Holt, S.E.5
  • 16
    • 0032749463 scopus 로고    scopus 로고
    • Hypoxia-induced activation of HIF-1: Role of HIF-1α-Hsp90 interaction
    • Minet E, Mottet D, Michel G, et al. Hypoxia-induced activation of HIF-1: role of HIF-1α-Hsp90 interaction. FEBS Lett 1999;460:251-6.
    • (1999) FEBS Lett , vol.460 , pp. 251-256
    • Minet, E.1    Mottet, D.2    Michel, G.3
  • 17
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000;100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 18
    • 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;206:149-57.
    • (2004) Cancer Lett , vol.206 , pp. 149-157
    • Workman, P.1
  • 19
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
    • Grenert JP, Sullivan WP, Fadden P, et al. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J Biol Chem 1997; 272:23843-50.
    • (1997) J Biol Chem , vol.272 , pp. 23843-23850
    • Grenert, J.P.1    Sullivan, W.P.2    Fadden, P.3
  • 20
    • 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. 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 1994;91:8324-8.
    • (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
  • 21
    • 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. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997;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
  • 22
    • 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, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997;89:239-50.
    • (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
  • 23
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte TW, An WG, Neckers LM. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem Biophys Res Commun 1997;239:655-9.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 24
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein I, Robertson D, DiStefano F, Workman P, Clarke PA. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17- demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res 2001;61:4003-9.
    • (2001) Cancer Res , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3    Workman, P.4    Clarke, P.A.5
  • 26
    • 23044441106 scopus 로고    scopus 로고
    • A phase I pharmacokinetic (PK) and pharmacodynamic (PD) study of 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in patients with advanced malignancies
    • Banerji U, O'Donnell A, Scurr M, et al. A phase I pharmacokinetic (PK) and pharmacodynamic (PD) study of 17-allylamino, 17-demethoxygeldanamycin (17-AAG) in patients with advanced malignancies. J Clin Oncol 2005;23:4152-61.
    • (2005) J Clin Oncol , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 27
    • 2142759891 scopus 로고    scopus 로고
    • A Pharmacokinetically (PK)-pharmacodynamically (PD) guided phase I trial of the heat shock protien (Hsp90) inhibitor 17-allylamino, 17- demethoxygeldanamycin (17AAG)
    • Banerji U, O'Donnell A, Scurr M, et al. A Pharmacokinetically (PK)-pharmacodynamically (PD) guided phase I trial of the heat shock protien (Hsp90) inhibitor 17-allylamino, 17-demethoxygeldanamycin (17AAG). Proceedings American Society of Clinical Oncology 2003;22:199-1.
    • (2003) Proceedings American Society of Clinical Oncology , vol.22 , pp. 199-201
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 28
    • 20044384168 scopus 로고    scopus 로고
    • Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer
    • Goetz MP, Toft D, Reid J, et al. Phase I trial of 17-allylamino-17- demethoxygeldanamycin in patients with advanced cancer. J Clin Oncol 2005; 23:1078-87.
    • (2005) J Clin Oncol , vol.23 , pp. 1078-1087
    • Goetz, M.P.1    Toft, D.2    Reid, J.3
  • 29
    • 20144375312 scopus 로고    scopus 로고
    • Phase I and pharmacologic study of 17-(allylamino)-17- demethoxygeldanamycin in adult patients with solid tumors
    • Grem JL, Morrison G, Quo XD, et al. Phase I and pharmacologic study of 17-(allylamino)-17-demethoxygeldanamycin in adult patients with solid tumors. J Clin Oncol 2005;23:1885-93,
    • (2005) J Clin Oncol , vol.23 , pp. 1885-1893
    • Grem, J.L.1    Morrison, G.2    Quo, X.D.3
  • 30
    • 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, 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;11:3385-91.
    • (2005) Clin Cancer Res , vol.11 , pp. 3385-3391
    • Ramanathan, R.K.1    Trump, D.L.2    Eiseman, J.L.3
  • 31
    • 0033523233 scopus 로고    scopus 로고
    • Anticancer agents targeting signaling molecules and cancer cell environment: Challenges for drug development?
    • Gelmon KA, Eisenhauer EA, Harris AL, Ratain MJ, Workman P. Anticancer agents targeting signaling molecules and cancer cell environment: challenges for drug development? J Natl Cancer Inst 1999;91:1281-7.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 1281-1287
    • Gelmon, K.A.1    Eisenhauer, E.A.2    Harris, A.L.3    Ratain, M.J.4    Workman, P.5
  • 32
    • 0038004636 scopus 로고    scopus 로고
    • Clinical biomarkers in drug discovery and development
    • Frank R, Hargreaves R. Clinical biomarkers in drug discovery and development. Nat Rev Drug Discov 2003;2:566-80.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 566-580
    • Frank, R.1    Hargreaves, R.2
  • 33
    • 0033402254 scopus 로고    scopus 로고
    • Discovering novel chemotherapeutic drugs for the third millennium
    • Garrett MD, Workman P. Discovering novel chemotherapeutic drugs for the third millennium. Eur J Cancer 1999;35:2010-30.
    • (1999) Eur J Cancer , vol.35 , pp. 2010-2030
    • Garrett, M.D.1    Workman, P.2
  • 34
    • 0037237884 scopus 로고    scopus 로고
    • How much gets there and what does it do?: The need for better pharmacokinetic and pharmacodynamic endpointsin contemporary drug discovery and development
    • Workman P. How much gets there and what does it do?: the need for better pharmacokinetic and pharmacodynamic endpointsin contemporary drug discovery and development. Curr Pharm Des 2003;9:891-902.
    • (2003) Curr Pharm des , vol.9 , pp. 891-902
    • Workman, P.1
  • 35
    • 0043269344 scopus 로고    scopus 로고
    • Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: Unfolding the relationship between pharmacokinetics and pharmacodynamics
    • Workman P. Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: unfolding the relationship between pharmacokinetics and pharmacodynamics. Mol Cancer Ther 2003;2:131-8.
    • (2003) Mol Cancer Ther , vol.2 , pp. 131-138
    • Workman, P.1
  • 36
    • 3242679103 scopus 로고    scopus 로고
    • Phase I trial design for solid tumor studies of targeted, non-cytotoxic agents: Theory and practice
    • Parulekar WR, Eisenhauer EA. Phase I trial design for solid tumor studies of targeted, non-cytotoxic agents: theory and practice. J Natl Cancer Inst 2004; 96:990-7.
    • (2004) J Natl Cancer Inst , vol.96 , pp. 990-997
    • Parulekar, W.R.1    Eisenhauer, E.A.2
  • 37
    • 0034112079 scopus 로고    scopus 로고
    • Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56μLck
    • Bijlmakers MJ, Marsh M. Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56μLck). Mol Biol Cell 2000;11:1585-95.
    • (2000) Mol Biol Cell , vol.11 , pp. 1585-1595
    • Bijlmakers, M.J.1    Marsh, M.2
  • 38
    • 0141819958 scopus 로고    scopus 로고
    • The stress response: Implications for the clinical development of hsp90 inhibitors
    • Whitesell L, Bagatell R, Falsey R. The stress response: implications for the clinical development of hsp90 inhibitors. Curr Cancer Drug Targets 2003;3:349-58.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 349-358
    • Whitesell, L.1    Bagatell, R.2    Falsey, R.3
  • 39
    • 0141819961 scopus 로고    scopus 로고
    • Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: A mechanistic perspective
    • Maloney A, Clarke PA, Workman P. Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: a mechanistic perspective. Curr Cancer Drug Targets 2003;3:331-41.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 331-341
    • Maloney, A.1    Clarke, P.A.2    Workman, P.3
  • 40
    • 0034710542 scopus 로고    scopus 로고
    • Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone
    • Clarke PA, Hostein I, Banerji U, et al. Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone. Oncogene 2000;19:4125-33.
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1    Hostein, I.2    Banerji, U.3
  • 41
    • 0024563482 scopus 로고
    • Biological properties of ten human ovarian carcinoma cell lines: Calibration in vitro against four platinum complexes
    • Hills CA, Kelland LR, Abel G, Siracky J, Wilson AP, Harrap KR. Biological properties of ten human ovarian carcinoma cell lines: calibration in vitro against four platinum complexes. Br J Cancer 1989;59:527-34.
    • (1989) Br J Cancer , vol.59 , pp. 527-534
    • Hills, C.A.1    Kelland, L.R.2    Abel, G.3    Siracky, J.4    Wilson, A.P.5    Harrap, K.R.6
  • 42
    • 0034469255 scopus 로고    scopus 로고
    • Bioanalytical method validation: A revisit with a decade of progress
    • Shah V, Midha K, Findlay J. Bioanalytical method validation: a revisit with a decade of progress. Pharm Res 2000;12:1551-7.
    • (2000) Pharm Res , vol.12 , pp. 1551-1557
    • Shah, V.1    Midha, K.2    Findlay, J.3
  • 43
    • 0023761465 scopus 로고
    • Testing for the equality of area under the curves when using destructive measurement techniques
    • Bailer A. Testing for the equality of area under the curves when using destructive measurement techniques. J Pharmacokinet Biopharm 1988;16:303-9.
    • (1988) J Pharmacokinet Biopharm , vol.16 , pp. 303-309
    • Bailer, A.1
  • 44
    • 0033579175 scopus 로고    scopus 로고
    • DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland LR, Sharp SY, Rogers PM, Myers TG, Workman P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17- demethoxygeldanamycin, an inhibitor of heat shock protein 90. J Natl Cancer Inst 1999;91:1940-9.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 45
    • 16744368637 scopus 로고    scopus 로고
    • United Kingdom Co-ordinating Committee on Cancer Research guidelines for the welfare of animals in experimental neoplasia
    • 2nd ed.
    • Workman P, Twentyman P, Balkwill F, Balmain A, Chaplin D, Double J. United Kingdom Co-ordinating Committee on Cancer Research guidelines for the welfare of animals in experimental neoplasia. 2nd ed. British Journal of Cancer 1998;77:1-10.
    • (1998) British Journal of Cancer , vol.77 , pp. 1-10
    • Workman, P.1    Twentyman, P.2    Balkwill, F.3    Balmain, A.4    Chaplin, D.5    Double, J.6
  • 46
    • 0030986627 scopus 로고    scopus 로고
    • Phase I and pharmacologic study of the combination paclitaxel and carboplatin as first-line chemotherapy in stage III and IV ovarian cancer
    • Huizing MT, van Warmerdam LJ, Rosing H, et al. Phase I and pharmacologic study of the combination paclitaxel and carboplatin as first-line chemotherapy in stage III and IV ovarian cancer. J Clin Oncol 1997;15:1953-64.
    • (1997) J Clin Oncol , vol.15 , pp. 1953-1964
    • Huizing, M.T.1    Van Warmerdam, L.J.2    Rosing, H.3
  • 47
    • 0026612119 scopus 로고
    • DT-diaphorase and cancer chemotherapy
    • Riley RJ, Workman P. DT-diaphorase and cancer chemotherapy. Biochem Pharmacol 1992;43:1657-69.
    • (1992) Biochem Pharmacol , vol.43 , pp. 1657-1669
    • Riley, R.J.1    Workman, P.2
  • 48
    • 0034743361 scopus 로고    scopus 로고
    • Plasma pharmacokinetics and tissue distribution of 17-(allylamino)-17- demethoxygeldanamycin (NSC 330507) in CD2F1 mice1
    • Egorin MJ, Zuhowski EG, Rosen DM, Sentz DL, Covey JM, Eiseman JL. Plasma pharmacokinetics and tissue distribution of 17-(allylamino)-17- demethoxygeldanamycin (NSC 330507) in CD2F1 mice1. Cancer Chemother Pharmacol 2001;47:291-302.
    • (2001) Cancer Chemother Pharmacol , vol.47 , pp. 291-302
    • Egorin, M.J.1    Zuhowski, E.G.2    Rosen, D.M.3    Sentz, D.L.4    Covey, J.M.5    Eiseman, J.L.6
  • 49
    • 1142273472 scopus 로고    scopus 로고
    • Altered states: Selectively drugging the Hsp90 cancer chaperone
    • Workman P. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol Med 2004;10:47-51.
    • (2004) Trends Mol Med , vol.10 , pp. 47-51
    • Workman, P.1
  • 50
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumor selectivity on Hsp90 inhibitors
    • Kamal A, Thao L, Sensintaffar J, et al. A high-affinity conformation of Hsp90 confers tumor selectivity on Hsp90 inhibitors. Nature 2003;425:407-10.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 52
    • 0036840774 scopus 로고    scopus 로고
    • Challenges of PK/PD measurements in modern drug development
    • Workman P. Challenges of PK/PD measurements in modern drug development. Eur J Cancer 2002;38:2189-93.
    • (2002) Eur J Cancer , vol.38 , pp. 2189-2193
    • Workman, P.1
  • 53
    • 1942485334 scopus 로고    scopus 로고
    • 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models
    • Burger AM, Fiebig HH, Stinson SF, Sausville EA. 17-(Allylamino)-17- demethoxygeldanamycin activity in human melanoma models. Anticancer Drugs 2004; 15:377-87.
    • (2004) Anticancer Drugs , vol.15 , pp. 377-387
    • Burger, A.M.1    Fiebig, H.H.2    Stinson, S.F.3    Sausville, E.A.4
  • 54
    • 0036091221 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts
    • Solit DB, Zheng FF, Drobnjak M, et al. 17-Allylamino-17- demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res 2002;8:986-93.
    • (2002) Clin Cancer Res , vol.8 , pp. 986-993
    • Solit, D.B.1    Zheng, F.F.2    Drobnjak, M.3
  • 55
    • 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. Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol. Cancer Res 2003;63:2139-44.
    • (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
  • 56
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228
    • Yu X, Quo ZS, Marcu MG, et al. Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. J Natl Cancer Inst 2002; 94:504-13.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 504-513
    • Yu, X.1    Quo, Z.S.2    Marcu, M.G.3
  • 57
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C, Morimoto RI. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst 2000;92:1564-72.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 58
    • 22144496224 scopus 로고    scopus 로고
    • A Phase I tiral of 17-allylamino-geldanamycin (17AAG) in patients with advanced cancer
    • Erlichman C, Toft D, Reid J, et al. A Phase I tiral of 17-allylamino-geldanamycin (17AAG) in patients with advanced cancer. Proc American Assoc Clin One 2004;23:202-1.
    • (2004) Proc American Assoc Clin One , vol.23 , pp. 202-211
    • Erlichman, C.1    Toft, D.2    Reid, J.3


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