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Volumn 65, Issue 22, 2005, Pages 10536-10544

Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; ANTILEUKEMIC AGENT; BCR ABL PROTEIN; BENZYLIDENE DERIVATIVE; CYTARABINE; ETOPOSIDE; HEAT SHOCK PROTEIN 70; KNK 437; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN BAX; PROTEIN C RAF; PROTEIN KINASE B; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 28544433004     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-1799     Document Type: Article
Times cited : (205)

References (62)
  • 1
    • 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
  • 2
    • 4143095430 scopus 로고    scopus 로고
    • Altered Hsp90 function in cancer: A unique therapeutic opportunity
    • Bagatell R, Whitesell L. Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol Cancer Ther 2004;3:1021-30.
    • (2004) Mol Cancer Ther , vol.3 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 3
    • 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
  • 5
    • 0037265586 scopus 로고    scopus 로고
    • Development of small molecule Hsp90 inhibitors: Utilizing both forward and reverse chemical genomics for drug identification
    • Neckers L. Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification. Curr Med Chem 2003; 10:733-9.
    • (2003) Curr Med Chem , vol.10 , pp. 733-739
    • Neckers, L.1
  • 6
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med 2003;228:111-33.
    • (2003) Exp Biol Med , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 7
    • 19944433616 scopus 로고    scopus 로고
    • Mechanistic role of heat shock protein 70 in Bcr-Abl-mediated resistance to apoptosis in human acute leukemia cells
    • Guo F, Sigua C, Bali P, et al. Mechanistic role of heat shock protein 70 in Bcr-Abl-mediated resistance to apoptosis in human acute leukemia cells. Blood 2005; 105:1246-55.
    • (2005) Blood , vol.105 , pp. 1246-1255
    • Guo, F.1    Sigua, C.2    Bali, P.3
  • 8
    • 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
  • 9
    • 0033944777 scopus 로고    scopus 로고
    • Heat shock proteins: Modulators of apoptosis in tumour cells
    • Creagh EM, Sheehan D, Cotter TG. Heat shock proteins: modulators of apoptosis in tumour cells. Leukemia 2000;14:1161-73.
    • (2000) Leukemia , vol.14 , pp. 1161-1173
    • Creagh, E.M.1    Sheehan, D.2    Cotter, T.G.3
  • 10
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • Rohde M, Daugaard M, Jensen MH, Helin K, Nylandsted J, Jaattela M. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 2005;19:570-82.
    • (2005) Genes Dev , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5    Jaattela, M.6
  • 11
    • 0033578065 scopus 로고    scopus 로고
    • Oncogenic potential of Hsp72
    • Volloch VZ, Sherman MY. Oncogenic potential of Hsp72. Oncogene 1999;18:3648-51.
    • (1999) Oncogene , vol.18 , pp. 3648-3651
    • Volloch, V.Z.1    Sherman, M.Y.2
  • 12
    • 0030054050 scopus 로고    scopus 로고
    • T cell lymphoma in transgenic mice expressing the human Hsp70 gene
    • Seo JS, Park YM, Kim JI, et al. T cell lymphoma in transgenic mice expressing the human Hsp70 gene. Biochem Biophys Res Commun 1996;218:582-7.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 582-587
    • Seo, J.S.1    Park, Y.M.2    Kim, J.I.3
  • 13
    • 3242879188 scopus 로고    scopus 로고
    • "The stress of dying": The role of heat shock proteins in the regulation of apoptosis
    • Beere HM. "The stress of dying": the role of heat shock proteins in the regulation of apoptosis. J Cell Sci 2004;117:2641-51.
    • (2004) J Cell Sci , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 14
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama S, Reed JC, Homma S. Heat-shock proteins as regulators of apoptosis. Oncogene 2003;22:9041-7.
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 16
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM, Wolf BB, Cain K, et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2000;2:469-75.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3
  • 17
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jaattela M, Wissing D, Kokholm K, Kallunki T, Egeblad M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J 1998; 17:6124-34.
    • (1998) EMBO J , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 18
    • 17944366977 scopus 로고    scopus 로고
    • Heat-shock protein 70 antagonizes apoptosis-inducing factor
    • Ravagnan L, Gurbuxani S, Susin SA, et al. Heat-shock protein 70 antagonizes apoptosis-inducing factor. Nat Cell Biol 2001;3:839-43.
    • (2001) Nat Cell Biol , vol.3 , pp. 839-843
    • Ravagnan, L.1    Gurbuxani, S.2    Susin, S.A.3
  • 19
    • 0242606282 scopus 로고    scopus 로고
    • Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor
    • Gurbuxani S, Schmitt E, Cande C, et al. Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor. Oncogene 2003;22:6669-78.
    • (2003) Oncogene , vol.22 , pp. 6669-6678
    • Gurbuxani, S.1    Schmitt, E.2    Cande, C.3
  • 20
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted J, Rohde M, Brand K, Bastholm L, Elling F, Jaattela M. Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc Natl Acad Sci U S A 2000;97:7871-6.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jaattela, M.6
  • 21
    • 0037115547 scopus 로고    scopus 로고
    • Eradication of glioblastoma, and breast and colon carcinoma xenografts by Hsp70 depletion
    • Nylandsted J, Wick W, Hirt UA, et al. Eradication of glioblastoma, and breast and colon carcinoma xenografts by Hsp70 depletion. Cancer Res 2002;62:7139-42.
    • (2002) Cancer Res , vol.62 , pp. 7139-7142
    • Nylandsted, J.1    Wick, W.2    Hirt, U.A.3
  • 22
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 1998;94:471-80.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 23
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 1998;12:3788-96.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 24
    • 0034212740 scopus 로고    scopus 로고
    • Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells
    • Yokota S, Kitahara M, Nagata K. Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells. Cancer Res 2000;60:2942-8.
    • (2000) Cancer Res , vol.60 , pp. 2942-2948
    • Yokota, S.1    Kitahara, M.2    Nagata, K.3
  • 25
    • 0035138956 scopus 로고    scopus 로고
    • The effects of KNK437, a novel inhibitor of heat shock protein synthesis, on the acquisition of thermotolerance in a murine transplantable tumor in vivo
    • Koishi M, Yokota S, Mae T, et al. The effects of KNK437, a novel inhibitor of heat shock protein synthesis, on the acquisition of thermotolerance in a murine transplantable tumor in vivo. Clin Cancer Res 2001;7:215-9.
    • (2001) Clin Cancer Res , vol.7 , pp. 215-219
    • Koishi, M.1    Yokota, S.2    Mae, T.3
  • 26
    • 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
  • 27
    • 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, et al. 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 2002;62:5761-9.
    • (2002) Cancer Res , vol.62 , pp. 5761-5769
    • Nimmanapalli, R.1    O'Bryan, E.2    Huang, M.3
  • 28
    • 0043016178 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive orrefractory chronic myelogenous leukemia-blast crisis cells
    • Nimmanapalli R, Fuino L, Bali P, et al. Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive orrefractory chronic myelogenous leukemia-blast crisis cells. Cancer Res 2003;63:5126-35.
    • (2003) Cancer Res , vol.63 , pp. 5126-5135
    • Nimmanapalli, R.1    Fuino, L.2    Bali, P.3
  • 29
    • 0034665903 scopus 로고    scopus 로고
    • CGP57148 (STI-571) induces differentiation and apoptosis and sensitizes Bcr-Abl positive human leukemia cells to apoptosis due to antileukemic drugs
    • Fang G, Kim C, Perkins C, et al. CGP57148 (STI-571) induces differentiation and apoptosis and sensitizes Bcr-Abl positive human leukemia cells to apoptosis due to antileukemic drugs. Blood 2000;96:2246-56.
    • (2000) Blood , vol.96 , pp. 2246-2256
    • Fang, G.1    Kim, C.2    Perkins, C.3
  • 30
    • 0033830374 scopus 로고    scopus 로고
    • The chaperone function of hsp70 is required for protection against stress-induced apoptosis
    • Mosser DD, Caron AW, Bourget L, et al. The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol Cell Biol 2000;20:7146-59.
    • (2000) Mol Cell Biol , vol.20 , pp. 7146-7159
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3
  • 31
    • 11144358387 scopus 로고    scopus 로고
    • Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells
    • Guo F, Sigua C, Tao J, et al. Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells. Cancer Res 2004;64:2580-9.
    • (2004) Cancer Res , vol.64 , pp. 2580-2589
    • Guo, F.1    Sigua, C.2    Tao, J.3
  • 32
    • 20244362748 scopus 로고    scopus 로고
    • Flavopiridol downregulates antiapoptotic proteins and sensitizes human breast cancer cells to epothilone B-induced apoptosis
    • Wittmann S, Bali P, Donapaty S, et al. Flavopiridol downregulates antiapoptotic proteins and sensitizes human breast cancer cells to epothilone B-induced apoptosis. Cancer Res 2003;63:93-9.
    • (2003) Cancer Res , vol.63 , pp. 93-99
    • Wittmann, S.1    Bali, P.2    Donapaty, S.3
  • 33
    • 0037380884 scopus 로고    scopus 로고
    • Bax plays a pivotal role in thapsigargin-induced apoptosis of human colon cancer cells by controlling Smac/Diablo and Omi/HtrA2 release from mitochondria
    • Yamaguchi H, Bhalla K, Wang HG. Bax plays a pivotal role in thapsigargin-induced apoptosis of human colon cancer cells by controlling Smac/Diablo and Omi/HtrA2 release from mitochondria. Cancer Res 2003;63:1483-9.
    • (2003) Cancer Res , vol.63 , pp. 1483-1489
    • Yamaguchi, H.1    Bhalla, K.2    Wang, H.G.3
  • 34
    • 1642490813 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 down-regulates Her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine, and epothilone B
    • Fuino L, Bali P, Wittmann S, et al. Histone deacetylase inhibitor LAQ824 down-regulates Her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine, and epothilone B. Mol Cancer Ther 2003;2:971-84.
    • (2003) Mol Cancer Ther , vol.2 , pp. 971-984
    • Fuino, L.1    Bali, P.2    Wittmann, S.3
  • 35
    • 0345707575 scopus 로고    scopus 로고
    • The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells
    • Xu W, Yuan X, Jung YJ, et al. The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells. Cancer Res 2003;63:7777-84.
    • (2003) Cancer Res , vol.63 , pp. 7777-7784
    • Xu, W.1    Yuan, X.2    Jung, Y.J.3
  • 36
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: Roles in cell survival and oncogenesis
    • Cory S, Huang DC, Adams J. The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 2003;22:8590-607.
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.3
  • 37
    • 0037081329 scopus 로고    scopus 로고
    • Epothilone B analogue (BMS247550)-mediated cytotoxicity through induction of Bax conformational change in human breast cancer cells
    • Yamaguchi H, Paranawithana S, Lee M, Huang Z, Bhalla K, Wang HG. Epothilone B analogue (BMS247550)-mediated cytotoxicity through induction of Bax conformational change in human breast cancer cells. Cancer Res 2002;62:466-71.
    • (2002) Cancer Res , vol.62 , pp. 466-471
    • Yamaguchi, H.1    Paranawithana, S.2    Lee, M.3    Huang, Z.4    Bhalla, K.5    Wang, H.G.6
  • 38
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev 2001;15:2922-33.
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 39
    • 1842843854 scopus 로고    scopus 로고
    • Hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
    • Gotoh T, Terada K, Oyadomari S, Mori M. hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ 2004;11:390-402.
    • (2004) Cell Death Differ , vol.11 , pp. 390-402
    • Gotoh, T.1    Terada, K.2    Oyadomari, S.3    Mori, M.4
  • 40
    • 4344651318 scopus 로고    scopus 로고
    • Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization
    • Nylandsted J, Gyrd-Hansen M, Danielewicz A, et al. Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization. J Exp Med 2004;200:425-35.
    • (2004) J Exp Med , vol.200 , pp. 425-435
    • Nylandsted, J.1    Gyrd-Hansen, M.2    Danielewicz, A.3
  • 41
    • 0347356337 scopus 로고    scopus 로고
    • Genomic instability and enhanced radiosensitivity in Hsp70.1- and Hsp70.3-deflcient mice
    • Hunt CR, Dix DJ, Sharma GG, et al. Genomic instability and enhanced radiosensitivity in Hsp70.1- and Hsp70.3-deflcient mice. Mol Cell Biol 2004;24:899-911.
    • (2004) Mol Cell Biol , vol.24 , pp. 899-911
    • Hunt, C.R.1    Dix, D.J.2    Sharma, G.G.3
  • 42
    • 12344307185 scopus 로고    scopus 로고
    • Mechanism of hsp70i gene bookmarking
    • Xing H, Wilkerson DC, Mayhew CN, et al. Mechanism of hsp70i gene bookmarking. Science 2005;307:421-3.
    • (2005) Science , vol.307 , pp. 421-423
    • Xing, H.1    Wilkerson, D.C.2    Mayhew, C.N.3
  • 44
    • 0141953270 scopus 로고    scopus 로고
    • A JNK-dependent pathway is required for TNFα-induced apoptosis
    • Deng Y, Ren X, Yang L, Lin Y, Wu X. A JNK-dependent pathway is required for TNFα-induced apoptosis. Cell 2003;115:61-70.
    • (2003) Cell , vol.115 , pp. 61-70
    • Deng, Y.1    Ren, X.2    Yang, L.3    Lin, Y.4    Wu, X.5
  • 45
    • 0036234472 scopus 로고    scopus 로고
    • Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis
    • Gabai VL, Mabuchi K, Mosser DD, Sherman MY. Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis. Mol Cell Biol 2002;22:3415-24.
    • (2002) Mol Cell Biol , vol.22 , pp. 3415-3424
    • Gabai, V.L.1    Mabuchi, K.2    Mosser, D.D.3    Sherman, M.Y.4
  • 46
    • 0035254227 scopus 로고    scopus 로고
    • Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase
    • Park HS, Lee JS, Huh SH, Seo JS, Choi EJ. Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J 2001;20:446-56.
    • (2001) EMBO J , vol.20 , pp. 446-456
    • Park, H.S.1    Lee, J.S.2    Huh, S.H.3    Seo, J.S.4    Choi, E.J.5
  • 47
    • 0033830374 scopus 로고    scopus 로고
    • The chaperone function of hsp70 is required for protection against stress-induced apoptosis
    • Mosser DD, Caron AW, Bourget L, et al. The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol Cell Biol 2000;20:7146-59.
    • (2000) Mol Cell Biol , vol.20 , pp. 7146-7159
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3
  • 48
    • 0034714355 scopus 로고    scopus 로고
    • Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation
    • Hatai T, Matsuzawa A, Inoshita S, et al. Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria- dependent caspase activation. J Biol Chem 2000;275:26576-81.
    • (2000) J Biol Chem , vol.275 , pp. 26576-26581
    • Hatai, T.1    Matsuzawa, A.2    Inoshita, S.3
  • 49
    • 0036840931 scopus 로고    scopus 로고
    • Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1
    • Park HS, Cho SG, Kim CK, et al. Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1. Mol Cell Biol 2002;22:7721-30.
    • (2002) Mol Cell Biol , vol.22 , pp. 7721-7730
    • Park, H.S.1    Cho, S.G.2    Kim, C.K.3
  • 50
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A, Thao L, Sensintaffar J, et al. A high-affinity conformation of Hsp90 confers tumour 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
  • 51
    • 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, Guo 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    Guo, X.D.3
  • 52
    • 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
  • 53
    • 27544492938 scopus 로고    scopus 로고
    • Anti-tumor activity of a novel, water soluble Hsp90 inhibitor IPI-504 in multiple myeloma
    • Sydor JR, Pien CS, Zhange Y, et al. Anti-tumor activity of a novel, water soluble Hsp90 inhibitor IPI-504 in multiple myeloma [abstract]. Proc Am Assoc Cancer Res 2005;45:6160.
    • (2005) Proc Am Assoc Cancer Res , vol.45 , pp. 6160
    • Sydor, J.R.1    Pien, C.S.2    Zhange, Y.3
  • 54
    • 21244462689 scopus 로고    scopus 로고
    • In vivo antitumor efficacy of 17-DMAG (17-dimethylaminoethylamino-17- demethoxygeldanamycin hydrochloride), a water-soluble geldanamycin derivative
    • Hollingshead M, Alley M, Burger AM, et al. In vivo antitumor efficacy of 17-DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin hydrochloride), a water-soluble geldanamycin derivative. Cancer Chemother Pharmacol 2005;56:115-25.
    • (2005) Cancer Chemother Pharmacol , vol.56 , pp. 115-125
    • Hollingshead, M.1    Alley, M.2    Burger, A.M.3
  • 56
    • 28544450490 scopus 로고    scopus 로고
    • The two faces of Hsp90: Dissecting the cytotoxic and cytoprotective responses with selective Hsp90 modulators
    • Zhang H, Yang Y-C, Le D, Tsurumoto S, Win V, Burrows F. The two faces of Hsp90: dissecting the cytotoxic and cytoprotective responses with selective Hsp90 modulators [abstract]. Proc Am Assoc Cancer Res 2005;46:1527.
    • (2005) Proc Am Assoc Cancer Res , vol.46 , pp. 1527
    • Zhang, H.1    Yang, Y.-C.2    Le, D.3    Tsurumoto, S.4    Win, V.5    Burrows, F.6
  • 57
    • 0026755773 scopus 로고
    • Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoids
    • Hosokawa N, Hirayoshi K, Kudo H, et al. Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoids. Mol Cell Biol 1992; 12:3490-8.
    • (1992) Mol Cell Biol , vol.12 , pp. 3490-3498
    • Hosokawa, N.1    Hirayoshi, K.2    Kudo, H.3
  • 58
    • 4344592639 scopus 로고    scopus 로고
    • Distinct stimulus-specific histone modifications at hsp70 chromatin targeted by the transcription factor heat shock factor-1
    • Thomson S, Hollis A, Hazzalin CA, Mahadevan LC. Distinct stimulus-specific histone modifications at hsp70 chromatin targeted by the transcription factor heat shock factor-1. Mol Cell 2004;15:585-94.
    • (2004) Mol Cell , vol.15 , pp. 585-594
    • Thomson, S.1    Hollis, A.2    Hazzalin, C.A.3    Mahadevan, L.C.4
  • 59
    • 0034674061 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity
    • Dai R, Frejtag W, He B, Zhang Y, Mivechi NF. c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity. J Biol Chem 2000;275:18210-8.
    • (2000) J Biol Chem , vol.275 , pp. 18210-18218
    • Dai, R.1    Frejtag, W.2    He, B.3    Zhang, Y.4    Mivechi, N.F.5
  • 60
    • 16844366162 scopus 로고    scopus 로고
    • Polo-like kinase 1 phosphorylates heat shock transcription factor 1 and mediates its nuclear translocation during heat stress
    • Kim SA, Yoon JH, Lee SH, Ahn SG. Polo-like kinase 1 phosphorylates heat shock transcription factor 1 and mediates its nuclear translocation during heat stress. J Biol Chem 2005;280:12653-7.
    • (2005) J Biol Chem , vol.280 , pp. 12653-12657
    • Kim, S.A.1    Yoon, J.H.2    Lee, S.H.3    Ahn, S.G.4
  • 61
    • 2442695516 scopus 로고    scopus 로고
    • Co-treatment with 17-allylamino-demethoxygeldanamycin (17-AAG) and FLT-3 kinase inhibitor PKC412 is highly effective against human AML cells with mutant FLT-3
    • George P, Bali P, Cohen P, et al. Co-treatment with 17-allylamino- demethoxygeldanamycin (17-AAG) and FLT-3 kinase inhibitor PKC412 is highly effective against human AML cells with mutant FLT-3. Cancer Res 2004;64:3645-52.
    • (2004) Cancer Res , vol.64 , pp. 3645-3652
    • George, P.1    Bali, P.2    Cohen, P.3
  • 62
    • 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. 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 2002;100:3041-4.
    • (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


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