메뉴 건너뛰기




Volumn 67, Issue 21, 2007, Pages 10455-10465

Cooperative interactions between androgen receptor (AR) and heat-shock protein 27 facilitate AR transcriptional activity

Author keywords

[No Author keywords available]

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ANDROGEN RECEPTOR; ANTISENSE OLIGONUCLEOTIDE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 90; METRIBOLONE; MITOGEN ACTIVATED PROTEIN KINASE P38; OGX 427; PACLITAXEL; PROSTATE SPECIFIC ANTIGEN; PROTEASOME; PROTEIN MDM2; SERINE; UNCLASSIFIED DRUG;

EID: 35948950583     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-07-2057     Document Type: Article
Times cited : (223)

References (50)
  • 1
    • 0025957233 scopus 로고
    • Transcriptional activation and nuclear targeting signals of the human androgen receptor
    • Simental JA, Sar M, Lane MV, French FS, Wilson EM. Transcriptional activation and nuclear targeting signals of the human androgen receptor. J Biol Chem 1991;266:510-8.
    • (1991) J Biol Chem , vol.266 , pp. 510-518
    • Simental, J.A.1    Sar, M.2    Lane, M.V.3    French, F.S.4    Wilson, E.M.5
  • 2
    • 0027479319 scopus 로고
    • Characterization of two cis-acting DNA elements involved in the androgen regulation of the probasin gene
    • Rennie PS, Bruchovsky N, Leco KJ, et al. Characterization of two cis-acting DNA elements involved in the androgen regulation of the probasin gene. Mol Endocrinol 1993;7:23-36.
    • (1993) Mol Endocrinol , vol.7 , pp. 23-36
    • Rennie, P.S.1    Bruchovsky, N.2    Leco, K.J.3
  • 3
    • 0242290354 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase/Akt pathway by androgen through interaction of p85α, androgen receptor, and Src
    • Sun M, Yang L, Feldman RI, et al. Activation of phosphatidylinositol 3-kinase/Akt pathway by androgen through interaction of p85α, androgen receptor, and Src. J Biol Chem 2003;278:42992-3000.
    • (2003) J Biol Chem , vol.278 , pp. 42992-43000
    • Sun, M.1    Yang, L.2    Feldman, R.I.3
  • 4
    • 0036793098 scopus 로고    scopus 로고
    • The roles of androgen receptors and androgen-binding proteins in nongenomic androgen actions
    • Heinlein CA, Chang C. The roles of androgen receptors and androgen-binding proteins in nongenomic androgen actions. Mol Endocrinol 2002;16:2181-7.
    • (2002) Mol Endocrinol , vol.16 , pp. 2181-2187
    • Heinlein, C.A.1    Chang, C.2
  • 5
    • 0035831020 scopus 로고    scopus 로고
    • Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: Dissociation from transcriptional activity
    • Kousteni S, Bellido T, Plotkin LI, et al. Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: dissociation from transcriptional activity. Cell 2001;104:719-30.
    • (2001) Cell , vol.104 , pp. 719-730
    • Kousteni, S.1    Bellido, T.2    Plotkin, L.I.3
  • 6
    • 0034675994 scopus 로고    scopus 로고
    • Steroid-induced androgen receptor-oestradiol receptor β-Src complex triggers prostate cancer cell proliferation
    • Migliaccio A, Castoria G, Di Domenico M, et al. Steroid-induced androgen receptor-oestradiol receptor β-Src complex triggers prostate cancer cell proliferation. EMBO J 2000;19:5406-17.
    • (2000) EMBO J , vol.19 , pp. 5406-5417
    • Migliaccio, A.1    Castoria, G.2    Di Domenico, M.3
  • 7
    • 0033545848 scopus 로고    scopus 로고
    • From HER2/Neu signal cascade to androgen receptor and its coactivators: A novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells
    • Yeh S, Lin HK, Kang HY, Thin TH, Lin MF, Chang C. From HER2/Neu signal cascade to androgen receptor and its coactivators: a novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells. Proc Natl Acad Sci U S A 1999;96:5458-63.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 5458-5463
    • Yeh, S.1    Lin, H.K.2    Kang, H.Y.3    Thin, T.H.4    Lin, M.F.5    Chang, C.6
  • 8
    • 0034644608 scopus 로고    scopus 로고
    • Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells
    • Haynes MP, Sinha D, Russell KS, et al. Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells. Circ Res 2000;87:677-82.
    • (2000) Circ Res , vol.87 , pp. 677-682
    • Haynes, M.P.1    Sinha, D.2    Russell, K.S.3
  • 9
    • 3543020345 scopus 로고    scopus 로고
    • The role of adapter protein Shc in estrogen nongenomic action
    • Zhang Z, Kumar R, Santen RJ, Song RX. The role of adapter protein Shc in estrogen nongenomic action. Steroids 2004;69:523-9.
    • (2004) Steroids , vol.69 , pp. 523-529
    • Zhang, Z.1    Kumar, R.2    Santen, R.J.3    Song, R.X.4
  • 10
    • 2442528552 scopus 로고    scopus 로고
    • Androgen receptor mediates nongenomic activation of phosphatidylinositol 3-OH kinase in androgen-sensitive epithelial cells
    • Baron S, Manin M, Beaudoin C, et al. Androgen receptor mediates nongenomic activation of phosphatidylinositol 3-OH kinase in androgen-sensitive epithelial cells. J Biol Chem 2004;279:14579-86.
    • (2004) J Biol Chem , vol.279 , pp. 14579-14586
    • Baron, S.1    Manin, M.2    Beaudoin, C.3
  • 11
    • 20444368837 scopus 로고    scopus 로고
    • The androgen receptor and signal-transduction pathways in hormone-refractory prostate cancer. Part 2: Androgen-receptor cofactors and bypass pathways
    • Edwards J, Bartlett JM. The androgen receptor and signal-transduction pathways in hormone-refractory prostate cancer. Part 2: Androgen-receptor cofactors and bypass pathways. BJU Int 2005;95:1327-35.
    • (2005) BJU Int , vol.95 , pp. 1327-1335
    • Edwards, J.1    Bartlett, J.M.2
  • 13
    • 25144436540 scopus 로고    scopus 로고
    • Enhanced radiosensitivity by inhibition of the antiapoptotic gene clusterin using antisense oligodeoxynucleotide in a human bladder cancer model
    • Yamanaka K, Gleave M, Muramaki M, Hara I, Miyake H. Enhanced radiosensitivity by inhibition of the antiapoptotic gene clusterin using antisense oligodeoxynucleotide in a human bladder cancer model. Oncol Rep 2005;13:885-90.
    • (2005) Oncol Rep , vol.13 , pp. 885-890
    • Yamanaka, K.1    Gleave, M.2    Muramaki, M.3    Hara, I.4    Miyake, H.5
  • 16
    • 33751502796 scopus 로고    scopus 로고
    • FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform
    • Yang Z, Wolf IM, Chen H, et al. FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform. Mol Endocrinol 2006;20:2682-94.
    • (2006) Mol Endocrinol , vol.20 , pp. 2682-2694
    • Yang, Z.1    Wolf, I.M.2    Chen, H.3
  • 17
    • 27744519263 scopus 로고    scopus 로고
    • Modulation of estrogen signaling by the novel interaction of heat shock protein 27, a biomarker for atherosclerosis, and estrogen receptor β: Mechanistic insight into the vascular effects of estrogens
    • Miller H, Poon S, Hibbert B, Rayner K, Chen YX, O'Brien ER. Modulation of estrogen signaling by the novel interaction of heat shock protein 27, a biomarker for atherosclerosis, and estrogen receptor β: mechanistic insight into the vascular effects of estrogens. Arterioscler Thromb Vasc Biol 2005;25:e10-4.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25
    • Miller, H.1    Poon, S.2    Hibbert, B.3    Rayner, K.4    Chen, Y.X.5    O'Brien, E.R.6
  • 19
    • 0034963578 scopus 로고    scopus 로고
    • Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c
    • Concannon CG, Orrenius S, Samali A. Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c. Gene Expr 2001;9:195-201.
    • (2001) Gene Expr , vol.9 , pp. 195-201
    • Concannon, C.G.1    Orrenius, S.2    Samali, A.3
  • 20
    • 0043133793 scopus 로고    scopus 로고
    • HSP27 is a ubiquitin-binding protein involved in I-κBβ proteasomal degradation
    • Parcellier A, Schmitt E, Gurbuxani S, et al. HSP27 is a ubiquitin-binding protein involved in I-κBβ proteasomal degradation. Mol Cell Biol 2003;23:5790-802.
    • (2003) Mol Cell Biol , vol.23 , pp. 5790-5802
    • Parcellier, A.1    Schmitt, E.2    Gurbuxani, S.3
  • 21
    • 11144357610 scopus 로고    scopus 로고
    • The bortezomib/proteasome inhibitor PS-341 and triterpenoid CDDO-Im induce synergistic anti-multiple myeloma (MM) activity and overcome bortezomib resistance
    • Chauhan D, Li G, Podar K, et al. The bortezomib/proteasome inhibitor PS-341 and triterpenoid CDDO-Im induce synergistic anti-multiple myeloma (MM) activity and overcome bortezomib resistance. Blood 2004;103:3158-66.
    • (2004) Blood , vol.103 , pp. 3158-3166
    • Chauhan, D.1    Li, G.2    Podar, K.3
  • 22
    • 4644237335 scopus 로고    scopus 로고
    • Heat shock protein 27 increases after androgen ablation and plays a cytoprotective role in hormone-refractory prostate cancer
    • Rocchi P, So A, Kojima S, et al. Heat shock protein 27 increases after androgen ablation and plays a cytoprotective role in hormone-refractory prostate cancer. Cancer Res 2004;64:6595-602.
    • (2004) Cancer Res , vol.64 , pp. 6595-6602
    • Rocchi, P.1    So, A.2    Kojima, S.3
  • 23
    • 28244456529 scopus 로고    scopus 로고
    • Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis
    • Rocchi P, Beraldi E, Ettinger S, et al. Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis. Cancer Res 2005;65:11083-93.
    • (2005) Cancer Res , vol.65 , pp. 11083-11093
    • Rocchi, P.1    Beraldi, E.2    Ettinger, S.3
  • 24
    • 0026348949 scopus 로고
    • The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein
    • Mendelsohn ME, Zhu Y, O'Neill S. The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein. Proc Natl Acad Sci U S A 1991;88:11212-6.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 11212-11216
    • Mendelsohn, M.E.1    Zhu, Y.2    O'Neill, S.3
  • 25
    • 0032729015 scopus 로고    scopus 로고
    • Glucocorticoids regulate the synthesis of HSP27 in rat brain slices
    • Barr CS, Dokas LA. Glucocorticoids regulate the synthesis of HSP27 in rat brain slices. Brain Res 1999;847:9-17.
    • (1999) Brain Res , vol.847 , pp. 9-17
    • Barr, C.S.1    Dokas, L.A.2
  • 26
    • 0026602518 scopus 로고
    • Serum prostate specific antigen levels in mice bearing human prostate LNCaP tumors are determined by tumor volume and endocrine and growth factors
    • Gleave ME, Hsieh JT, Wu HC, von Eschenbach AC, Chung LW. Serum prostate specific antigen levels in mice bearing human prostate LNCaP tumors are determined by tumor volume and endocrine and growth factors. Cancer Res 1992;52:1598-605.
    • (1992) Cancer Res , vol.52 , pp. 1598-1605
    • Gleave, M.E.1    Hsieh, J.T.2    Wu, H.C.3    von Eschenbach, A.C.4    Chung, L.W.5
  • 27
    • 0034667457 scopus 로고    scopus 로고
    • Ligand-independent activation of the androgen receptor by the differentiation agent butyrate in human prostate cancer cells
    • Sadar MD, Gleave ME. Ligand-independent activation of the androgen receptor by the differentiation agent butyrate in human prostate cancer cells. Cancer Res 2000;60:5825-31.
    • (2000) Cancer Res , vol.60 , pp. 5825-5831
    • Sadar, M.D.1    Gleave, M.E.2
  • 28
    • 0036208492 scopus 로고    scopus 로고
    • Formation of the androgen receptor transcription complex
    • Shang Y, Myers M, Brown M. Formation of the androgen receptor transcription complex. Mol Cell 2002;9:601-10.
    • (2002) Mol Cell , vol.9 , pp. 601-610
    • Shang, Y.1    Myers, M.2    Brown, M.3
  • 29
    • 0034486139 scopus 로고    scopus 로고
    • Rapid and quantitative assessment of cancer treatment response using in vivo bioluminescence imaging
    • Rehemtulla A, Stegman LD, Cardozo SJ, et al. Rapid and quantitative assessment of cancer treatment response using in vivo bioluminescence imaging. Neoplasia 2000;2:491-5.
    • (2000) Neoplasia , vol.2 , pp. 491-495
    • Rehemtulla, A.1    Stegman, L.D.2    Cardozo, S.J.3
  • 31
    • 0033119571 scopus 로고    scopus 로고
    • Antiapoptotic signaling in LNCaP prostate cancer cells: A survival signaling pathway independent of phosphatidylinositol 3′-kinase and Akt/protein kinase B
    • Carson JP, Kulik G, Weber MJ. Antiapoptotic signaling in LNCaP prostate cancer cells: a survival signaling pathway independent of phosphatidylinositol 3′-kinase and Akt/protein kinase B. Cancer Res 1999;59:1449-53.
    • (1999) Cancer Res , vol.59 , pp. 1449-1453
    • Carson, J.P.1    Kulik, G.2    Weber, M.J.3
  • 32
    • 0041344614 scopus 로고    scopus 로고
    • Heat shock protein 27 controls apoptosis by regulating Akt activation
    • Rane MJ, Pan Y, Singh S, et al. Heat shock protein 27 controls apoptosis by regulating Akt activation. J Biol Chem 2003;278:27828-35.
    • (2003) J Biol Chem , vol.278 , pp. 27828-27835
    • Rane, M.J.1    Pan, Y.2    Singh, S.3
  • 33
    • 0035793574 scopus 로고    scopus 로고
    • p38 kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • Rane MJ, Coxon PY, Powell DW, et al. p38 kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils. J Biol Chem 2001;276:3517-23.
    • (2001) J Biol Chem , vol.276 , pp. 3517-3523
    • Rane, M.J.1    Coxon, P.Y.2    Powell, D.W.3
  • 34
    • 0142169540 scopus 로고    scopus 로고
    • Isolation and identification of L-dopa decarboxylase as a protein that binds to and enhances transcriptional activity of the androgen receptor using the repressed transactivator yeast two-hybrid system
    • Wafa LA, Cheng H, Rao MA, et al. Isolation and identification of L-dopa decarboxylase as a protein that binds to and enhances transcriptional activity of the androgen receptor using the repressed transactivator yeast two-hybrid system. Biochem J 2003;375:373-83.
    • (2003) Biochem J , vol.375 , pp. 373-383
    • Wafa, L.A.1    Cheng, H.2    Rao, M.A.3
  • 35
    • 0142125911 scopus 로고    scopus 로고
    • Hsp90 as a therapeutic target in prostate cancer
    • Solit DB, Scher HI, Rosen N. Hsp90 as a therapeutic target in prostate cancer. Semin Oncol 2003;30:709-16.
    • (2003) Semin Oncol , vol.30 , pp. 709-716
    • Solit, D.B.1    Scher, H.I.2    Rosen, N.3
  • 36
    • 16844386205 scopus 로고    scopus 로고
    • Emodin down-regulates androgen receptor and inhibits prostate cancer cell growth
    • Cha TL, Qiu L, Chen CT, Wen Y, Hung MC. Emodin down-regulates androgen receptor and inhibits prostate cancer cell growth. Cancer Res 2005;65:2287-95.
    • (2005) Cancer Res , vol.65 , pp. 2287-2295
    • Cha, T.L.1    Qiu, L.2    Chen, C.T.3    Wen, Y.4    Hung, M.C.5
  • 37
    • 13744257306 scopus 로고    scopus 로고
    • Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation
    • Gaughan L, Logan IR, Neal DE, Robson CN. Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation. Nucleic Acids Res 2005;33:13-26.
    • (2005) Nucleic Acids Res , vol.33 , pp. 13-26
    • Gaughan, L.1    Logan, I.R.2    Neal, D.E.3    Robson, C.N.4
  • 39
    • 0031772351 scopus 로고    scopus 로고
    • In vivo evaluation of hsp27 as an inhibitor of actin polymerization: Hsp27 limits actin stress fiber and focal adhesion formation after heat shock
    • Schneider GB, Hamano H, Cooper LF. In vivo evaluation of hsp27 as an inhibitor of actin polymerization: hsp27 limits actin stress fiber and focal adhesion formation after heat shock. J Cell Physiol 1998;177:575-84.
    • (1998) J Cell Physiol , vol.177 , pp. 575-584
    • Schneider, G.B.1    Hamano, H.2    Cooper, L.F.3
  • 40
    • 0034671358 scopus 로고    scopus 로고
    • Heat shock protein expression independently predicts clinical outcome in prostate cancer
    • Cornford PA, Dodson AR, Parsons KF, et al. Heat shock protein expression independently predicts clinical outcome in prostate cancer. Cancer Res 2000;60:7099-105.
    • (2000) Cancer Res , vol.60 , pp. 7099-7105
    • Cornford, P.A.1    Dodson, A.R.2    Parsons, K.F.3
  • 41
    • 0027203545 scopus 로고
    • Differential expression of steroid receptors, hsp27, and pS2 in a series of drug resistant human breast tumor cell lines derived following exposure to antitumor drugs or to fractionated X-irradiation
    • Whelan RD, Hill BT. Differential expression of steroid receptors, hsp27, and pS2 in a series of drug resistant human breast tumor cell lines derived following exposure to antitumor drugs or to fractionated X-irradiation. Breast Cancer Res Treat 1993;26:23-39.
    • (1993) Breast Cancer Res Treat , vol.26 , pp. 23-39
    • Whelan, R.D.1    Hill, B.T.2
  • 42
    • 0029882949 scopus 로고    scopus 로고
    • Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells
    • Richards EH, Hickey E, Weber L, Master JR. Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells. Cancer Res 1996;56:2446-51.
    • (1996) Cancer Res , vol.56 , pp. 2446-2451
    • Richards, E.H.1    Hickey, E.2    Weber, L.3    Master, J.R.4
  • 43
    • 0035671707 scopus 로고    scopus 로고
    • Angiotensin AT(1) receptor stimulates heat shock protein 27 phosphorylation in vitro and in vivo
    • Meier M, King GL, Clermont A, Perez A, Hayashi M, Feener EP. Angiotensin AT(1) receptor stimulates heat shock protein 27 phosphorylation in vitro and in vivo. Hypertension 2001;38:1260-5.
    • (2001) Hypertension , vol.38 , pp. 1260-1265
    • Meier, M.1    King, G.L.2    Clermont, A.3    Perez, A.4    Hayashi, M.5    Feener, E.P.6
  • 44
    • 0028906774 scopus 로고
    • Interleukin (IL)-6 signaling leads to phosphorylation of the small heat shock protein (Hsp)27 through activation of the MAP kinase and MAPKAP kinase 2 pathway in monocytes and monocytic leukemia cells
    • Belka C, Ahlers A, Sott C, Gaestel M, Herrmann F, Brach MA. Interleukin (IL)-6 signaling leads to phosphorylation of the small heat shock protein (Hsp)27 through activation of the MAP kinase and MAPKAP kinase 2 pathway in monocytes and monocytic leukemia cells. Leukemia 1995;9:288-94.
    • (1995) Leukemia , vol.9 , pp. 288-294
    • Belka, C.1    Ahlers, A.2    Sott, C.3    Gaestel, M.4    Herrmann, F.5    Brach, M.A.6
  • 45
    • 0347986522 scopus 로고    scopus 로고
    • Stat3 modulates heat shock 27 kDa protein expression in breast epithelial cells
    • Song H, Ethier SP, Dziubinski ML, Lin J. Stat3 modulates heat shock 27 kDa protein expression in breast epithelial cells. Biochem Biophys Res Commun 2004;314:143-50.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 143-150
    • Song, H.1    Ethier, S.P.2    Dziubinski, M.L.3    Lin, J.4
  • 46
    • 0035955725 scopus 로고    scopus 로고
    • Identification and characterization of hic-5/ARA55 as an hsp27 binding protein
    • Jia Y, Ransom RF, Shibanuma M, Liu C, Welsh MJ, Smoyer WE. Identification and characterization of hic-5/ARA55 as an hsp27 binding protein. J Biol Chem 2001;276:39911-8.
    • (2001) J Biol Chem , vol.276 , pp. 39911-39918
    • Jia, Y.1    Ransom, R.F.2    Shibanuma, M.3    Liu, C.4    Welsh, M.J.5    Smoyer, W.E.6
  • 47
    • 33746472300 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase stimulates estrogen-mediated transcription and proliferation through the phosphorylation and potentiation of the p160 coactivator glucocorticoid receptor-interacting protein 1
    • Frigo DE, Basu A, Nierth-Simpson EN, et al. p38 mitogen-activated protein kinase stimulates estrogen-mediated transcription and proliferation through the phosphorylation and potentiation of the p160 coactivator glucocorticoid receptor-interacting protein 1. Mol Endocrinol 2006;20:971-83.
    • (2006) Mol Endocrinol , vol.20 , pp. 971-983
    • Frigo, D.E.1    Basu, A.2    Nierth-Simpson, E.N.3
  • 48
    • 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
  • 49
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • Neckers L, Schulte TW, Mimnaugh E. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest New Drugs 1999;17:361-73.
    • (1999) Invest New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.