메뉴 건너뛰기




Volumn 3, Issue 12, 2004, Pages 1530-1536

Hsp90 activation and cell cycle regulation

Author keywords

Anticancer drugs; Cancer; Cell cycle; Heat shock protein 90; Selectivity

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; ANSAMYCIN DERIVATIVE; ANTHRACYCLINE DERIVATIVE; ANTINEOPLASTIC AGENT; CISPLATIN; CYCLOPROPANECARBOXYLIC ACID [4 [4 (4 METHYL 1 PIPERAZINYL) 6 (5 METHYL 2H PYRAZOL 3 YLAMINO) 2 PYRIMIDINYLTHIO]PHENYL]AMIDE; DOCETAXEL; GEFITINIB; GELDANAMYCIN; GEMCITABINE; HEAT SHOCK PROTEIN 90; IRINOTECAN; PACLITAXEL; PROTEIN INHIBITOR; TAXANE DERIVATIVE; TRASTUZUMAB;

EID: 17144377442     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.3.12.1277     Document Type: Review
Times cited : (132)

References (78)
  • 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
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Maywood
    • Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 2003; 228:111-33.
    • (2003) Exp Biol Med , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 3
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • Zhang H, Burrows F. Targeting multiple signal transduction pathways through inhibition of Hsp90. J Mol Med 2004; 82:488-99.
    • (2004) J Mol Med , vol.82 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 5
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med 2004; 10:83-90.
    • (2004) Trends Mol Med , vol.10 , pp. 83-90
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 6
    • 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
  • 7
    • 0025640051 scopus 로고
    • Reconstitution of progesterone receptor with heat shock proteins
    • Smith DF, Schowalter DB, Kost SL, Toft DO. Reconstitution of progesterone receptor with heat shock proteins. Mol Endocrinol 1990; 4:1704-11.
    • (1990) Mol Endocrinol , vol.4 , pp. 1704-1711
    • Smith, D.F.1    Schowalter, D.B.2    Kost, S.L.3    Toft, D.O.4
  • 8
    • 0032484127 scopus 로고    scopus 로고
    • The assembly of progesterone receptor-hsp90 complexes using purified proteins
    • Kosano H, Stensgard B, Charlesworth MC, McMahon N, Toft D. The assembly of progesterone receptor-hsp90 complexes using purified proteins. J Biol Chem 1998; 273:32973-9.
    • (1998) J Biol Chem , vol.273 , pp. 32973-32979
    • Kosano, H.1    Stensgard, B.2    Charlesworth, M.C.3    McMahon, N.4    Toft, D.5
  • 12
    • 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
  • 13
    • 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 USA 1994; 91:8324-8.
    • (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
  • 15
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh EG, Chavany C, Neckers L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 1996; 271:22796-801.
    • (1996) J Biol Chem , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0006886916 scopus 로고    scopus 로고
    • PC3 human prostrate xenograft retention of, and oncoprotein modulation by 17-(allylamino)-17-demothoxygeldanamycin(17AAG) in vivo
    • Egorin MJ, Sentz DL, Zuhowski EG, Dobson JM, Schulte TW, Neckers LM, et al. PC3 human prostrate xenograft retention of, and oncoprotein modulation by 17-(allylamino)-17-demothoxygeldanamycin(17AAG) in vivo. Proc Am Assoc Cancer Res 1999; 40:3409.
    • (1999) Proc Am Assoc Cancer Res , vol.40 , pp. 3409
    • Egorin, M.J.1    Sentz, D.L.2    Zuhowski, E.G.3    Dobson, J.M.4    Schulte, T.W.5    Neckers, L.M.6
  • 19
    • 14344254387 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[[(2-dimethylamino) ethyl]amino]geldanamycin (17DMAG, NSC 707545) in C.B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts
    • Eiseman JL, Lan J, Lagattuta TF, Hamburger DR, Joseph E, Covey JM, Egorin MJ. Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[[(2- dimethylamino) ethyl]amino]geldanamycin (17DMAG, NSC 707545) in C.B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts. Cancer Chemother Pharmacol 2004.
    • (2004) Cancer Chemother Pharmacol
    • Eiseman, J.L.1    Lan, J.2    Lagattuta, T.F.3    Hamburger, D.R.4    Joseph, E.5    Covey, J.M.6    Egorin, M.J.7
  • 20
    • 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. 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 2001; 8:289-99.
    • (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
  • 21
    • 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. The benzoquinone ansamycin 17-allylamino-17- demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998; 42:273-9.
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 25
    • 0030218025 scopus 로고    scopus 로고
    • The role of the 90-kDa heat shock protein in cell cycle control and differentiation of the monoblastoid cell line U937
    • Galea-Lauri J, Latchman DS, Katz DR. The role of the 90-kDa heat shock protein in cell cycle control and differentiation of the monoblastoid cell line U937. Exp Cell Res 1996; 226:243-54.
    • (1996) Exp Cell Res , vol.226 , pp. 243-254
    • Galea-Lauri, J.1    Latchman, D.S.2    Katz, D.R.3
  • 26
    • 0035355470 scopus 로고    scopus 로고
    • Cell cycle transition under stress conditions controlled by vertebrate heat shock factors
    • Nakai A, Ishikawa T. Cell cycle transition under stress conditions controlled by vertebrate heat shock factors. EMBO J 2001; 20:2885-95.
    • (2001) EMBO J , vol.20 , pp. 2885-2895
    • Nakai, A.1    Ishikawa, T.2
  • 27
    • 0034653849 scopus 로고    scopus 로고
    • Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates
    • Lange BM, Bachi A, Wilm M, Gonzalez C. Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates. EMBO J 2000; 19:1252-62.
    • (2000) EMBO J , vol.19 , pp. 1252-1262
    • Lange, B.M.1    Bachi, A.2    Wilm, M.3    Gonzalez, C.4
  • 28
    • 0034660892 scopus 로고    scopus 로고
    • The Pezcoller lecture: Cancer cell cycles revisited
    • Sherr CJ. The Pezcoller lecture: Cancer cell cycles revisited. Cancer Res 2000; 60:3689-95.
    • (2000) Cancer Res , vol.60 , pp. 3689-3695
    • Sherr, C.J.1
  • 29
    • 0031019197 scopus 로고    scopus 로고
    • Cyclin D1/Cdk4 regulates retinoblastoma protein-mediated cell cycle arrest by site-specific phosphorylation
    • Connell-Crowley L, Harper JW, Goodrich DW. Cyclin D1/Cdk4 regulates retinoblastoma protein-mediated cell cycle arrest by site-specific phosphorylation. Mol Biol Cell 1997; 8:287-301.
    • (1997) Mol Biol Cell , vol.8 , pp. 287-301
    • Connell-Crowley, L.1    Harper, J.W.2    Goodrich, D.W.3
  • 30
    • 0032491579 scopus 로고    scopus 로고
    • Cyclin D expression is controlled post-transcriprionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway
    • Muise-Helmericks RC, Grimes HL, Bellacosa A, Malstrom SE, Tsichlis PN, Rosen N. Cyclin D expression is controlled post-transcriprionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway. J Biol Chem 1998; 273:29864-72.
    • (1998) J Biol Chem , vol.273 , pp. 29864-29872
    • Muise-Helmericks, R.C.1    Grimes, H.L.2    Bellacosa, A.3    Malstrom, S.E.4    Tsichlis, P.N.5    Rosen, N.6
  • 31
    • 0032705608 scopus 로고    scopus 로고
    • Geldanamycin induces cell cycle arrest in K562 erythroleukemic cells
    • Kim HR, Lee CH, Choi YH, Kang HS, Kim HD. Geldanamycin induces cell cycle arrest in K562 erythroleukemic cells. IUBMB Life 1999; 48:425-8.
    • (1999) IUBMB Life , vol.48 , pp. 425-428
    • Kim, H.R.1    Lee, C.H.2    Choi, Y.H.3    Kang, H.S.4    Kim, H.D.5
  • 32
    • 1642419553 scopus 로고    scopus 로고
    • Geldanamycin, an inhibitor of the chaperone activity of HSP90, induces MAPK-independent cell cycle arrest
    • Bedin M, Gaben AM, Saucier C, Mester J. Geldanamycin, an inhibitor of the chaperone activity of HSP90, induces MAPK-independent cell cycle arrest. Int J Cancer 2004; 109:643-52.
    • (2004) Int J Cancer , vol.109 , pp. 643-652
    • Bedin, M.1    Gaben, A.M.2    Saucier, C.3    Mester, J.4
  • 34
    • 0032485070 scopus 로고    scopus 로고
    • Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells
    • Mahony D, Parry DA, Lees E. Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells. Oncogene 1998; 16:603-11.
    • (1998) Oncogene , vol.16 , pp. 603-611
    • Mahony, D.1    Parry, D.A.2    Lees, E.3
  • 35
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a prorein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova L, Leng X, Parker SB, Harper JW. Mammalian p50Cdc37 is a prorein 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
  • 36
    • 0032996456 scopus 로고    scopus 로고
    • Genetic interactions between Hsp90 and the Cdc2 mitotic machinery in the fission yeast Schizosaccharomyces pombe
    • Munoz MJ, Jimenez J. Genetic interactions between Hsp90 and the Cdc2 mitotic machinery in the fission yeast Schizosaccharomyces pombe. Mol Gen Genet 1999; 261:242-50.
    • (1999) Mol Gen Genet , vol.261 , pp. 242-250
    • Munoz, M.J.1    Jimenez, J.2
  • 38
    • 0028589101 scopus 로고
    • A role for Hsp90 in cell cycle control: Weel tyrosine kinase activity requires interaction with Hsp90
    • Aligue R, Akhavan-Niak H, Russell P. A role for Hsp90 in cell cycle control: Weel tyrosine kinase activity requires interaction with Hsp90. EMBO J 1994; 13:6099-106.
    • (1994) EMBO J , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 39
    • 0035003608 scopus 로고    scopus 로고
    • Hsp90 chaperone complexes are required for the activity and stability of yeast protein kinases Mikl, Weel and Swel
    • Goes FS, Martin J. Hsp90 chaperone complexes are required for the activity and stability of yeast protein kinases Mikl, Weel and Swel. Eur J Biochem 2001; 268:2281-9.
    • (2001) Eur J Biochem , vol.268 , pp. 2281-2289
    • Goes, F.S.1    Martin, J.2
  • 40
    • 0035355510 scopus 로고    scopus 로고
    • Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability
    • de Career G, do Carmo Avides M, Lallena MJ, Glover DM, Gonzalez C. Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability. EMBO J 2001; 20:2878-84.
    • (2001) EMBO J , vol.20 , pp. 2878-2884
    • De Career, G.1    Do Carmo Avides, M.2    Lallena, M.J.3    Glover, D.M.4    Gonzalez, C.5
  • 41
    • 3442890567 scopus 로고    scopus 로고
    • Hear shock prorein 90 regulates the metaphase-anaphase transition in a polo-like kinase-dependent manner
    • de Career G. Hear shock prorein 90 regulates the metaphase-anaphase transition in a polo-like kinase-dependent manner. Cancer Res 2004; 64:5106-12.
    • (2004) Cancer Res , vol.64 , pp. 5106-5112
    • De Career, G.1
  • 43
    • 0037107454 scopus 로고    scopus 로고
    • Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes
    • Lange BM, Rebollo E, Herold A, Gonzalez C. Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes. EMBO J 2002; 21:5364-74.
    • (2002) EMBO J , vol.21 , pp. 5364-5374
    • Lange, B.M.1    Rebollo, E.2    Herold, A.3    Gonzalez, C.4
  • 44
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An WG, Schulte TW, Neckers LM. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ 2000; 11:355-60.
    • (2000) Cell Growth Differ , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 45
    • 0034881367 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart
    • Scholz GM. The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart. Cell Growth Differ 2001; 12:409-17.
    • (2001) Cell Growth Differ , vol.12 , pp. 409-417
    • Scholz, G.M.1
  • 46
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • Blagosklonny MV. Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs. Leukemia 2002; 16:455-62.
    • (2002) Leukemia , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 47
    • 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. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 2002; 21:1159-66.
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 48
    • 0035300564 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function by ansamycins causes the morphological and functional differentiation of breast cancer cells
    • Munster PN, Srethapakdi M, Moasser MM, Rosen N. Inhibition of heat shock protein 90 function by ansamycins causes the morphological and functional differentiation of breast cancer cells. Cancer Res 2001; 61:2945-52.
    • (2001) Cancer Res , vol.61 , pp. 2945-2952
    • Munster, P.N.1    Srethapakdi, M.2    Moasser, M.M.3    Rosen, N.4
  • 50
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylarnino-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-allylarnino-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
  • 51
    • 0027931008 scopus 로고
    • Cell cycle arrests and radiosensitivity of human tumor cell lines: Dependence on wild-type p53 for radiosensitivity
    • McIlwrath AJ, Vasey PA, Ross GM, Brown, R. Cell cycle arrests and radiosensitivity of human tumor cell lines: Dependence on wild-type p53 for radiosensitivity. Cancer Res 1994; 54:3718-22.
    • (1994) Cancer Res , vol.54 , pp. 3718-3722
    • McIlwrath, A.J.1    Vasey, P.A.2    Ross, G.M.3    Brown, R.4
  • 52
    • 0001148491 scopus 로고    scopus 로고
    • Down-regulation of Hsp90 could change cell cycle distribution and increase drug sensitivity of tumor cells
    • Liu XL, Xiao B, Yu ZC, Guo JC, Zhao QC, Xu L, Shi YQ, Fan DM. Down-regulation of Hsp90 could change cell cycle distribution and increase drug sensitivity of tumor cells. World J Gastroenterol 1999; 5:199-208.
    • (1999) World J Gastroenterol , vol.5 , pp. 199-208
    • Liu, X.L.1    Xiao, B.2    Yu, Z.C.3    Guo, J.C.4    Zhao, Q.C.5    Xu, L.6    Shi, Y.Q.7    Fan, D.M.8
  • 53
    • 1642406972 scopus 로고    scopus 로고
    • Synergistic interactions between tamoxifen and trastuzumab (Herceptin)
    • Argiris A, Wang CX, Whalen SG, DiGiovanna MP. Synergistic interactions between tamoxifen and trastuzumab (Herceptin). Clin Cancer Res 2004; 10:1409-20.
    • (2004) Clin Cancer Res , vol.10 , pp. 1409-1420
    • Argiris, A.1    Wang, C.X.2    Whalen, S.G.3    DiGiovanna, M.P.4
  • 54
    • 1642580489 scopus 로고    scopus 로고
    • Inhibition of proliferation and induction of apoptosis in breast cancer cells by the epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor ZD1839 ('Iressa') is independent of EGFR expression level
    • Campiglio M, Locatelli A, Olgiati C, Normanno N, Somenzi G, Vigano L, Fumagalli M, Menard S, Gianni L. Inhibition of proliferation and induction of apoptosis in breast cancer cells by the epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor ZD1839 ('Iressa') is independent of EGFR expression level. J Cell Physiol 2004; 198:259-68.
    • (2004) J Cell Physiol , vol.198 , pp. 259-268
    • Campiglio, M.1    Locatelli, A.2    Olgiati, C.3    Normanno, N.4    Somenzi, G.5    Vigano, L.6    Fumagalli, M.7    Menard, S.8    Gianni, L.9
  • 57
    • 0035902115 scopus 로고    scopus 로고
    • Prolifecation, cell cycle and apoptosis in cancer
    • Evan GI, Vousden KH. Prolifecation, cell cycle and apoptosis in cancer. Nature 2001; 411:342-8.
    • (2001) Nature , vol.411 , pp. 342-348
    • Evan, G.I.1    Vousden, K.H.2
  • 58
    • 0032529464 scopus 로고    scopus 로고
    • Mechanisms of Taxol-induced cell death are concentration dependent
    • Torres K, Horwitz SB. Mechanisms of Taxol-induced cell death are concentration dependent. Cancer Res 1998; 58:3620-6.
    • (1998) Cancer Res , vol.58 , pp. 3620-3626
    • Torres, K.1    Horwitz, S.B.2
  • 59
    • 0036307898 scopus 로고    scopus 로고
    • Limited penetration of anticancer drugs through tumor tissue: A potential cause of resistance of solid tumors to chemotherapy
    • Tannock IF, Lee CM, Tunggal JK, Cowan DS, Egorin MJ. Limited penetration of anticancer drugs through tumor tissue: A potential cause of resistance of solid tumors to chemotherapy. Clin Cancer Res 2002; 8:878-84.
    • (2002) Clin Cancer Res , vol.8 , pp. 878-884
    • Tannock, I.F.1    Lee, C.M.2    Tunggal, J.K.3    Cowan, D.S.4    Egorin, M.J.5
  • 60
  • 61
    • 0034890377 scopus 로고    scopus 로고
    • Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner. See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17- demethoxygeldanamycin: Sequence and tumor biology matters
    • 2155-2158
    • Munster PN, Basso A, Solit D, Norton L, Rosen N. Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner. See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: Sequence and tumor biology matters. Clin Cancer Res 2001; 7:2228-36 (2155-2158).
    • (2001) Clin Cancer Res , vol.7 , pp. 2228-2236
    • Munster, P.N.1    Basso, A.2    Solit, D.3    Norton, L.4    Rosen, N.5
  • 62
    • 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 JH, Tabibi E, Schrump DS. 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 378-9.
    • (2001) Ann Thorac Surg , vol.72 , pp. 371-378
    • Nguyen, D.M.1    Lorang, D.2    Chen, G.A.3    Stewart, J.H.4    Tabibi, E.5    Schrump, D.S.6
  • 63
    • 4143105237 scopus 로고    scopus 로고
    • Geldanamycin enhances cisplatin cytotoxicity through loss of Akt activation in A549 cells
    • McCollum A, Toft DO, Erlichman C. Geldanamycin enhances cisplatin cytotoxicity through loss of Akt activation in A549 cells. Clin Cancer Res 2003; 9:6178s.
    • (2003) Clin Cancer Res , vol.9
    • McCollum, A.1    Toft, D.O.2    Erlichman, C.3
  • 64
    • 0038069088 scopus 로고    scopus 로고
    • Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of Cisplatin in human colon adenocarcinoma cells: Differential caspase activation as a basis for interaction
    • Vasilevskaya IA, Rakitina TV, O'Dwyer PJ. Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of Cisplatin in human colon adenocarcinoma cells: Differential caspase activation as a basis for interaction. Cancer Res 2003; 63:3241-6.
    • (2003) Cancer Res , vol.63 , pp. 3241-3246
    • Vasilevskaya, I.A.1    Rakitina, T.V.2    O'Dwyer, P.J.3
  • 65
    • 0034692430 scopus 로고    scopus 로고
    • Role of the insulin-like growth factor family in cancer development and progression
    • Yu H, Rohan T. Role of the insulin-like growth factor family in cancer development and progression. J Natl Cancer Inst 2000; 92:1472-89.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1472-1489
    • Yu, H.1    Rohan, T.2
  • 66
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta SR, Brunet A, Greenberg ME. Cellular survival: A play in three Akts. Genes Dev 1999; 13:2905-27
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 67
    • 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
  • 68
    • 0031866191 scopus 로고    scopus 로고
    • HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes
    • Ali A, Bharadwaj S, O'Carroll R, Ovsenek N. HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes. Mol Cell Biol 1998; 18:4949-60.
    • (1998) Mol Cell Biol , vol.18 , pp. 4949-4960
    • Ali, A.1    Bharadwaj, S.2    O'Carroll, R.3    Ovsenek, N.4
  • 69
    • 0024442546 scopus 로고
    • Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells
    • Redmond T, Sanchez ER, Bresnick EH, Schlesinger MJ, Toft DO, Pratt WB, Welsh MJ. Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells. Eur J Cell Biol 1989; 50:66-75.
    • (1989) Eur J Cell Biol , vol.50 , pp. 66-75
    • Redmond, T.1    Sanchez, E.R.2    Bresnick, E.H.3    Schlesinger, M.J.4    Toft, D.O.5    Pratt, W.B.6    Welsh, M.J.7
  • 70
    • 0022412314 scopus 로고
    • A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src
    • SSchuh S, Yonemoto W, Brugge J, Bauer VJ, Riehl RM, Sullivan WP, Toft DO. A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src. J Biol Chem 1985; 260:14292-6.
    • (1985) J Biol Chem , vol.260 , pp. 14292-14296
    • Sschuh, S.1    Yonemoto, W.2    Brugge, J.3    Bauer, V.J.4    Riehl, R.M.5    Sullivan, W.P.6    Toft, D.O.7
  • 72
    • 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
  • 73
    • 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
  • 74
    • 0034982174 scopus 로고    scopus 로고
    • Radicicol and geldanamycin prevent neurotoxic effects of anti-cancer drugs on cultured embryonic sensory neurons
    • Sano M. Radicicol and geldanamycin prevent neurotoxic effects of anti-cancer drugs on cultured embryonic sensory neurons. Neuropharmacology 2001; 40:947-53.
    • (2001) Neuropharmacology , vol.40 , pp. 947-953
    • Sano, M.1
  • 75
    • 0035917889 scopus 로고    scopus 로고
    • Cell biology. Do centrosome abnormalities lead to cancer?
    • Marx J. Cell biology. Do centrosome abnormalities lead to cancer? Science 2001; 292:426-9.
    • (2001) Science , vol.292 , pp. 426-429
    • Marx, J.1
  • 76
    • 0038746733 scopus 로고    scopus 로고
    • The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochoremicrotubule attachment and in maintaining the spindle assembly checkpoint
    • Hauf S, Cole RW, LaTerra S, Zimmer C, Schnapp G, Walter R, Heckel A, van Meel J, Rieder CL, Peters JM. The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochoremicrotubule attachment and in maintaining the spindle assembly checkpoint. J Cell Biol 2003; 161:281-94.
    • (2003) J Cell Biol , vol.161 , pp. 281-294
    • Hauf, S.1    Cole, R.W.2    LaTerra, S.3    Zimmer, C.4    Schnapp, G.5    Walter, R.6    Heckel, A.7    Van Meel, J.8    Rieder, C.L.9    Peters, J.M.10
  • 78
    • 0034887884 scopus 로고    scopus 로고
    • Cell cycle-mediated drug resistance: An emerging concept in cancer therapy
    • Shah MA, Schwartz GK. Cell cycle-mediated drug resistance: An emerging concept in cancer therapy. Clin Cancer Res 2001; 7:2168-81.
    • (2001) Clin Cancer Res , vol.7 , pp. 2168-2181
    • Shah, M.A.1    Schwartz, G.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.