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Volumn 12, Issue 20 PART 1, 2006, Pages 6087-6093

A phase I trial of twice-weekly 17-allylamino-demethoxy-geldanamycin in patients with advanced cancer

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINODEMETHOXY GELDANAMYCIN; CHAPERONE; CYCLIN DEPENDENT KINASE 4; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FOCAL ADHESION KINASE; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTEGRIN LINKED KINASE; PROTEIN KINASE B; PROTEIN P53; PROTEIN TYROSINE KINASE; RAF PROTEIN; SOMATOMEDIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 33750711384     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: 10.1158/1078-0432.CCR-06-1015     Document Type: Article
Times cited : (107)

References (35)
  • 1
    • 0031297298 scopus 로고    scopus 로고
    • The heat-shock response: Regulation and function of heat-shock proteins and molecular chaperones
    • Morimoto RI, Kline MP, Bimston DN, Cotto JJ. The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem 1997;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
  • 2
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002;295:1852-8.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 3
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young JC, Moarefi I, Hartl FU. Hsp90: a specialized but essential protein-folding tool. J Cell Biol 2001;154:267-73.
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 4
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt WB, Toft DO. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 1997;18:306-60.
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 5
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: Chaperoning signal transduction
    • Richter K, Buchner J. Hsp90: Chaperoning signal transduction. J Cell Physiol 2001;188:281-90.
    • (2001) J Cell Physiol , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 6
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-60v-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 HSP90-60v-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
  • 7
    • 0042885973 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex as a novel target for cancer therapy
    • Goetz MP, Toft DO, Ames MM, Erlichman C. The Hsp90 chaperone complex as a novel target for cancer therapy. Ann Oncol 2003;14:1169-76.
    • (2003) Ann Oncol , vol.14 , pp. 1169-1176
    • Goetz, M.P.1    Toft, D.O.2    Ames, M.M.3    Erlichman, C.4
  • 8
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 2002;8:555-61.
    • (2002) Trends Mol Med , vol.8 , pp. 555-561
    • Neckers, L.1
  • 9
    • 0141596941 scopus 로고    scopus 로고
    • Overview: Translating Hsp90 biology into Hsp90 drugs
    • Workman P. Overview: translating Hsp90 biology into Hsp90 drugs. Curr Cancer Drug Targets 2003;3:297-300.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 297-300
    • Workman, P.1
  • 10
    • 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
  • 11
    • 0033890818 scopus 로고    scopus 로고
    • Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents
    • Bagatell R, Paine-Murrieta GD, Taylor CW, et al. Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents. Clin Cancer Res 2000;6:3312-8.
    • (2000) Clin Cancer Res , vol.6 , pp. 3312-3318
    • Bagatell, R.1    Paine-Murrieta, G.D.2    Taylor, C.W.3
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0034777916 scopus 로고    scopus 로고
    • Destabilization of steroid receptors by heat shock protein 90-binding drugs: A ligand-independent approach to hormonal therapy of breast cancer
    • Bagatell R, Khan O, Paine-Murrieta G, et al. Destabilization of steroid receptors by heat shock protein 90-binding drugs: a ligand-independent approach to hormonal therapy of breast cancer. Clin Cancer Res 2001;7:2076-84.
    • (2001) Clin Cancer Res , vol.7 , pp. 2076-2084
    • Bagatell, R.1    Khan, O.2    Paine-Murrieta, G.3
  • 16
    • 0034902025 scopus 로고    scopus 로고
    • Enhancement of paclitaxel-mediated cytotoxicity in lung cancer cells by 17-allylamino geldanamycin: In vitro and in vivo analysis
    • discussion 78-9
    • Nguyen DM, Lorang D, Chen GA, et al. Enhancement of paclitaxel-mediated cytotoxicity in lung cancer cells by 17-allylamino geldanamycin: in vitro and in vivo analysis. Ann Thorac Surg 2001;72:371-8; discussion 78-9.
    • (2001) Ann Thorac Surg , vol.72 , pp. 371-378
    • Nguyen, D.M.1    Lorang, D.2    Chen, G.A.3
  • 17
    • 0035872396 scopus 로고    scopus 로고
    • Disruption of the EF-2 kinase/Hsp90 protein complex: A possible mechanism to inhibit glioblastoma by geldanamycin
    • Yang J, Yang JM, Iannone M, et al. Disruption of the EF-2 kinase/Hsp90 protein complex: a possible mechanism to inhibit glioblastoma by geldanamycin. Cancer Res 2001;61:4010-6.
    • (2001) Cancer Res , vol.61 , pp. 4010-4016
    • Yang, J.1    Yang, J.M.2    Iannone, M.3
  • 18
    • 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, et al. 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
  • 19
    • 0032101569 scopus 로고    scopus 로고
    • Metabolism of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations
    • Egorin MJ, Rosen DM, Wolff JH, et al. Metabolism of 17-(allylamino)-17- demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations. Cancer Res 1998;58:2385-96.
    • (1998) Cancer Res , vol.58 , pp. 2385-2396
    • Egorin, M.J.1    Rosen, D.M.2    Wolff, J.H.3
  • 20
    • 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
  • 22
    • 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
  • 23
    • 0030749549 scopus 로고    scopus 로고
    • Accelerated titration designs for phase I clinical trials in oncology
    • Simon R, Freidlin B, Rubinstein L, et al. Accelerated titration designs for phase I clinical trials in oncology. J Natl Cancer Inst 1997;89:1138-47.
    • (1997) J Natl Cancer Inst , vol.89 , pp. 1138-1147
    • Simon, R.1    Freidlin, B.2    Rubinstein, L.3
  • 24
    • 0029075280 scopus 로고
    • Binding of p23 and hsp90 during assembly with the progesterone receptor
    • Johnson JL, Toft DO. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol Endocrinol 1995;9:670-8.
    • (1995) Mol Endocrinol , vol.9 , pp. 670-678
    • Johnson, J.L.1    Toft, D.O.2
  • 25
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith PK, Krohn RI, Hermanson GT, et al. Measurement of protein using bicinchoninic acid. Anal Biochem 1985;150:76-85.
    • (1985) Anal Biochem , vol.150 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 26
    • 0035884184 scopus 로고    scopus 로고
    • Reutilization of immunoblots after chemiluminescent detection
    • Kaufmann SH. Reutilization of immunoblots after chemiluminescent detection. Anal Biochem 2001;296:283-6.
    • (2001) Anal Biochem , vol.296 , pp. 283-286
    • Kaufmann, S.H.1
  • 28
  • 29
    • 29144473795 scopus 로고    scopus 로고
    • How do cells respond to their thermal environment?
    • Lepock JR. How do cells respond to their thermal environment? Int J Hyperthermia 2005;21:681-7.
    • (2005) Int J Hyperthermia , vol.21 , pp. 681-687
    • Lepock, J.R.1
  • 30
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala L, Nykanen P, Sistonen L. Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J 2001;15:1118-31.
    • (2001) FASEB J , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 31
    • 28544433004 scopus 로고    scopus 로고
    • Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin
    • Guo F, Rocha K, Bali P, et al. Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin. Cancer Res 2005;65:10536-44.
    • (2005) Cancer Res , vol.65 , pp. 10536-10544
    • Guo, F.1    Rocha, K.2    Bali, P.3
  • 32
    • 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, et al. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 2002;277:39858-66.
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3
  • 33
    • 33646371494 scopus 로고    scopus 로고
    • Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
    • Arlander SJ, Felts SJ, Wagner JM, et al. Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones. J Biol Chem 2006;281:2989-98.
    • (2006) J Biol Chem , vol.281 , pp. 2989-2998
    • Arlander, S.J.1    Felts, S.J.2    Wagner, J.M.3
  • 34
    • 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
  • 35
    • 22044437522 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibition sensitizes acute myelogenous leukemia cells to cytarabine
    • Mesa RA, Loegering D, Powell HL, et al. Heat shock protein 90 inhibition sensitizes acute myelogenous leukemia cells to cytarabine. Blood 2005;106:318-27.
    • (2005) Blood , vol.106 , pp. 318-327
    • Mesa, R.A.1    Loegering, D.2    Powell, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.