메뉴 건너뛰기




Volumn , Issue , 2008, Pages 305-335

HSP90 inhibitors: Targeting the cancer chaperone for combinatorial blockade of oncogenic pathways

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84882527526     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012369448-5.50016-1     Document Type: Chapter
Times cited : (3)

References (192)
  • 1
    • 0036836678 scopus 로고    scopus 로고
    • Halohydrin and oxime derivatives of radicicol: synthesis and anti-tumor activities
    • Agatsuma T., Ogawa H., Akasaka K., et al. Halohydrin and oxime derivatives of radicicol: synthesis and anti-tumor activities. Bioorg. Med. Chem. 2002, 10:3445-3454.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3445-3454
    • Agatsuma, T.1    Ogawa, H.2    Akasaka, K.3
  • 2
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali M.M., Roe S.M., Vaughan C.K., et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006, 440:1013-1017.
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1    Roe, S.M.2    Vaughan, C.K.3
  • 3
    • 33646371009 scopus 로고    scopus 로고
    • Modulation of chaperone function and co-chaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization
    • Allan R.K., Mok D., Ward B.K., Ratajczak T Modulation of chaperone function and co-chaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization. J. Biol. Chem. 2006, 281:7161-7171.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7161-7171
    • Allan, R.K.1    Mok, D.2    Ward, B.K.3    Ratajczak, T.4
  • 4
    • 0032735232 scopus 로고    scopus 로고
    • Survivin apoptosis: an interloper between cell death and cell proliferation in cancer
    • Altieri D.C., Marchisio P.C. Survivin apoptosis: an interloper between cell death and cell proliferation in cancer. Lab. Invest. 1999, 79:1327-1333.
    • (1999) Lab. Invest. , vol.79 , pp. 1327-1333
    • Altieri, D.C.1    Marchisio, P.C.2
  • 5
    • 0142121760 scopus 로고    scopus 로고
    • Total synthesis of (+)-geldanamycin and (-)-o-quinogeldanamycin: asymmetric glycolate aldol reactions and biological evaluation
    • Andrus M.B., Meredith E.L., Hicken E.J., et al. Total synthesis of (+)-geldanamycin and (-)-o-quinogeldanamycin: asymmetric glycolate aldol reactions and biological evaluation. J. Org. Chem. 2003, 68:8162-8169.
    • (2003) J. Org. Chem. , vol.68 , pp. 8162-8169
    • Andrus, M.B.1    Meredith, E.L.2    Hicken, E.J.3
  • 6
    • 27744479712 scopus 로고    scopus 로고
    • Modulating molecular chaperone Hsp90 functions through reversible acetylation
    • Aoyagi S., Archer T.K. Modulating molecular chaperone Hsp90 functions through reversible acetylation. Trends Cell Biol. 2005, 15:565-567.
    • (2005) Trends Cell Biol. , vol.15 , pp. 565-567
    • Aoyagi, S.1    Archer, T.K.2
  • 7
    • 0033210210 scopus 로고    scopus 로고
    • GRP94, an ER chaperone with protein and peptide binding properties
    • Argon Y., Simen B.B. GRP94, an ER chaperone with protein and peptide binding properties. Semin. Cell Dev. Biol. 1999, 10:495-505.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 495-505
    • Argon, Y.1    Simen, B.B.2
  • 8
    • 33344475514 scopus 로고    scopus 로고
    • Development of synthetic routes to macrocyclic compounds based on the HSP90 inhibitor radicicol
    • Atrash B., Cooper T.S., et al. Development of synthetic routes to macrocyclic compounds based on the HSP90 inhibitor radicicol. Tetrahedron Lett. 2006, 47:2237-2240.
    • (2006) Tetrahedron Lett. , vol.47 , pp. 2237-2240
    • Atrash, B.1    Cooper, T.S.2
  • 9
    • 0033890818 scopus 로고    scopus 로고
    • Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90binding agents
    • Bagatell R., Paine-Murrieta G.D., Taylor C.W., et al. Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90binding agents. Clin. Cancer Res. 2000, 6:3312-3318.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 3312-3318
    • Bagatell, R.1    Paine-Murrieta, G.D.2    Taylor, C.W.3
  • 10
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P., Pranpat M., Bradner J., et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. 2005, 280:26,729-26,734.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3
  • 11
    • 23044441106 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies
    • Banerji U., O'Donnell A., Scurr M., et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J. Clin. Oncol. 2005, 23:4152-4161.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 12
    • 26444482073 scopus 로고    scopus 로고
    • Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models
    • Banerji U., Walton M., Raynaud F., et al. Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models. Clin. Cancer Res. 2005, 11:7023-7032.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 7023-7032
    • Banerji, U.1    Walton, M.2    Raynaud, F.3
  • 13
    • 0035194748 scopus 로고    scopus 로고
    • Expression of inducible Hsp70 enhances the proliferation of MCF-7 breast cancer cells and protects against the cytotoxic effects of hyperthermia
    • Barnes J.A., Dix D.J., Collins B.W., et al. Expression of inducible Hsp70 enhances the proliferation of MCF-7 breast cancer cells and protects against the cytotoxic effects of hyperthermia. Cell Stress Chaperones. 2001, 6:316-325.
    • (2001) Cell Stress Chaperones. , vol.6 , pp. 316-325
    • Barnes, J.A.1    Dix, D.J.2    Collins, B.W.3
  • 14
    • 26844524967 scopus 로고    scopus 로고
    • Structure-based discovery of a new class of Hsp90 inhibitors
    • Barril X., Brough P., Drysdale M., et al. Structure-based discovery of a new class of Hsp90 inhibitors. Bioorg. Med. Chem. Lett. 2005, 15:5187-5191.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 5187-5191
    • Barril, X.1    Brough, P.2    Drysdale, M.3
  • 15
    • 33645002986 scopus 로고    scopus 로고
    • 4-Amino derivatives of the Hsp90 inhibitor CCT018159
    • Barril X., Beswick M.C., Collier A., et al. 4-Amino derivatives of the Hsp90 inhibitor CCT018159. Bioorg. Med. Chem. Lett. 2006, 16:2543-2548.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 2543-2548
    • Barril, X.1    Beswick, M.C.2    Collier, A.3
  • 16
    • 33746247080 scopus 로고    scopus 로고
    • IPI504, a novel HSP90 inhibitor, causes inhibition and degradation of KIT in imatinib-resistant GIST: Rationale for therapeutic targeting in GIST
    • Bauer S., Yu L., Read M., et al. IPI504, a novel HSP90 inhibitor, causes inhibition and degradation of KIT in imatinib-resistant GIST: Rationale for therapeutic targeting in GIST. Clin. Cancer Res. 2005, 11(24 Suppl.):S9111.
    • (2005) Clin. Cancer Res. , vol.11 , Issue.24 SUPPL.
    • Bauer, S.1    Yu, L.2    Read, M.3
  • 17
    • 0034253533 scopus 로고    scopus 로고
    • Heatshock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere H.M., Wolf B.B., Cain K., et al. Heatshock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat. Cell Biol. 2000, 2:469-475.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3
  • 18
    • 31544433450 scopus 로고    scopus 로고
    • Orally active purine-based inhibitors of the heat shock protein 90
    • Biamonte M.A., Shi J., Hong K., et al. Orally active purine-based inhibitors of the heat shock protein 90. J. Med. Chem. 2006, 49:817-828.
    • (2006) J. Med. Chem. , vol.49 , pp. 817-828
    • Biamonte, M.A.1    Shi, J.2    Hong, K.3
  • 19
    • 0345734276 scopus 로고    scopus 로고
    • Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin
    • Blank M., Mandel M., Keisari Y., et al. Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin. Cancer Res. 2003, 63:8241-8247.
    • (2003) Cancer Res. , vol.63 , pp. 8241-8247
    • Blank, M.1    Mandel, M.2    Keisari, Y.3
  • 20
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • Bukau B., Deuerling E., Pfund C., Craig E.A. Getting newly synthesized proteins into shape. Cell 2000, 101:119-122.
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 21
    • 1942485334 scopus 로고    scopus 로고
    • 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models
    • Burger A.M., Fiebig H.H., Stinson S.F., Sausville E.A. 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models. Anticancer Drugs 2004, 15:377-387.
    • (2004) Anticancer Drugs , vol.15 , pp. 377-387
    • Burger, A.M.1    Fiebig, H.H.2    Stinson, S.F.3    Sausville, E.A.4
  • 22
    • 33845306864 scopus 로고    scopus 로고
    • Novobiocin: redesigning a DNA gyrase inhibitor for selective inhibition of hsp90
    • Burlison J.A., Neckers L., Smith A.B., et al. Novobiocin: redesigning a DNA gyrase inhibitor for selective inhibition of hsp90. J. Am. Chem. Soc. 2006, 128:15529-15536.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15529-15536
    • Burlison, J.A.1    Neckers, L.2    Smith, A.B.3
  • 23
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Caplan A.J., Mandal A.K., Theodoraki M.A. Molecular chaperones and protein kinase quality control. Trends Cell Biol. 2006, 17:87-92.
    • (2006) Trends Cell Biol. , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 24
    • 33748938280 scopus 로고    scopus 로고
    • Phase 1 clinical trial of KOS-953 + bortezomib (BZ) in relapsed refractory multiple myeloma (MM)
    • Chanan-Khan A., Richardson P., Alsina M., et al. Phase 1 clinical trial of KOS-953 + bortezomib (BZ) in relapsed refractory multiple myeloma (MM). J. Clin. Oncol. (Meeting Abstracts) 2006, 24:3066.
    • (2006) J. Clin. Oncol. (Meeting Abstracts) , vol.24 , pp. 3066
    • Chanan-Khan, A.1    Richardson, P.2    Alsina, M.3
  • 25
    • 0029011834 scopus 로고
    • Analysis of heat-shock protein expression in myeloid leukemia cells by fl ow cytometry
    • Chant I.D., Rose P.E., Morris A.G. Analysis of heat-shock protein expression in myeloid leukemia cells by fl ow cytometry. Br. J. Haematol. 1995, 90:163-168.
    • (1995) Br. J. Haematol. , vol.90 , pp. 163-168
    • Chant, I.D.1    Rose, P.E.2    Morris, A.G.3
  • 26
    • 28644443855 scopus 로고    scopus 로고
    • The HSP90 family of genes in the human genome: Insights into their divergence and evolution
    • Chen B., Piel W.H., Gui L., et al. The HSP90 family of genes in the human genome: Insights into their divergence and evolution. Genomics 2005, 86:627-637.
    • (2005) Genomics , vol.86 , pp. 627-637
    • Chen, B.1    Piel, W.H.2    Gui, L.3
  • 27
    • 0036718795 scopus 로고    scopus 로고
    • ATPases as drug targets: learning from their structure
    • Chene P ATPases as drug targets: learning from their structure. Nat. Rev. Drug Discov. 2002, 1:665-673.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 665-673
    • Chene, P.1
  • 28
    • 20644448390 scopus 로고    scopus 로고
    • The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors
    • Cheung K.M., Matthews T.P., et al. The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg. Med. Chem. Lett. 2005, 15:3338-3343.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 3338-3343
    • Cheung, K.M.1    Matthews, T.P.2
  • 29
    • 33244484848 scopus 로고    scopus 로고
    • Targeting chaperones in transformed systems - a focus on Hsp90 and cancer
    • Chiosis G Targeting chaperones in transformed systems - a focus on Hsp90 and cancer. Expert Opin. Ther. Targets 2006, 10:37-50.
    • (2006) Expert Opin. Ther. Targets , vol.10 , pp. 37-50
    • Chiosis, G.1
  • 30
    • 33746365169 scopus 로고    scopus 로고
    • Discovery and development of purine-scaffold hsp90 inhibitors
    • Chiosis G Discovery and development of purine-scaffold hsp90 inhibitors. Curr. Top. Med. Chem. 2006, 6:1183.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1183
    • Chiosis, G.1
  • 31
    • 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 M.N., Lucas B., et al. 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, 8:289-299.
    • (2001) Chem. Biol. , vol.8 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3
  • 32
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis G., Lucas B., Shtil A., et al. Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg. Med. Chem. 2002, 10:3555-3564.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Lucas, B.2    Shtil, A.3
  • 33
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG: low target binding affinity and potent cell activity - finding an explanation
    • Chiosis G., Huezo H., Rosen N., et al. 17AAG: low target binding affinity and potent cell activity - finding an explanation. Mol. Cancer Ther. 2003, 2:123-129.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 123-129
    • Chiosis, G.1    Huezo, H.2    Rosen, N.3
  • 34
    • 33745174538 scopus 로고    scopus 로고
    • Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today's agents
    • Chiosis G., Caldas L.E., Solit D Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today's agents. Curr. Opin. Invest. Drugs 2006, 7:534-541.
    • (2006) Curr. Opin. Invest. Drugs , vol.7 , pp. 534-541
    • Chiosis, G.1    Caldas, L.E.2    Solit, D.3
  • 35
    • 0344393470 scopus 로고    scopus 로고
    • Magnetic resonance spectroscopic pharmacodynamic markers of the heat shock protein 90 inhibitor 17-allylamino,17-demethoxygeldanamycin (17AAG) in human colon cancer models
    • Chung Y.L., Troy H., Banerji U., et al. Magnetic resonance spectroscopic pharmacodynamic markers of the heat shock protein 90 inhibitor 17-allylamino,17-demethoxygeldanamycin (17AAG) in human colon cancer models. J. Natl Cancer Inst. 2003, 95:1624-1633.
    • (2003) J. Natl Cancer Inst. , vol.95 , pp. 1624-1633
    • Chung, Y.L.1    Troy, H.2    Banerji, U.3
  • 36
    • 0027503365 scopus 로고
    • Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications
    • Ciocca D.R., Clark G.M., Tandon A.K., et al. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications. J. Natl Cancer Inst. 1993, 85:570-574.
    • (1993) J. Natl Cancer Inst. , vol.85 , pp. 570-574
    • Ciocca, D.R.1    Clark, G.M.2    Tandon, A.K.3
  • 37
    • 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 P.A., 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, 19:4125-4133.
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1    Hostein, I.2    Banerji, U.3
  • 38
    • 33751106653 scopus 로고    scopus 로고
    • New approaches to molecular cancer therapeutics
    • Collins I., Workman P New approaches to molecular cancer therapeutics. Nat. Chem. Biol. 2006, 2:689-700.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 689-700
    • Collins, I.1    Workman, P.2
  • 39
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell P., Ballinger C.A., Jiang J., et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 2001, 3:93-96.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3
  • 40
    • 0032058966 scopus 로고    scopus 로고
    • Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients
    • Conroy S.E., Sasieni P.D., Fentiman I., Latchman D.S. Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients. Eur. J. Cancer 1998, 34:942-943.
    • (1998) Eur. J. Cancer , vol.34 , pp. 942-943
    • Conroy, S.E.1    Sasieni, P.D.2    Fentiman, I.3    Latchman, D.S.4
  • 41
    • 33344477290 scopus 로고    scopus 로고
    • Synthesis of resorcinylic macrocycles related to radicicol via ring-closing metathesis
    • Cooper T.S., Atrash B., Sheldrake P., et al. Synthesis of resorcinylic macrocycles related to radicicol via ring-closing metathesis. Tetrahedron Lett. 2006, 47:2241-2243.
    • (2006) Tetrahedron Lett. , vol.47 , pp. 2241-2243
    • Cooper, T.S.1    Atrash, B.2    Sheldrake, P.3
  • 42
    • 0033944777 scopus 로고    scopus 로고
    • Heat shock proteins - modulators of apoptosis in tumor cells
    • Creagh E.M., Sheehan D., Cotter T.G. Heat shock proteins - modulators of apoptosis in tumor cells. Leukemia 2000, 14:1161-1173.
    • (2000) Leukemia , vol.14 , pp. 1161-1173
    • Creagh, E.M.1    Sheehan, D.2    Cotter, T.G.3
  • 43
    • 28244444919 scopus 로고    scopus 로고
    • Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino17-demethoxygeldanamycin
    • da Rocha Dias D.S., Friedlos F., Light Y., et al. Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino17-demethoxygeldanamycin. Cancer Res. 2005, 65:10686-10691.
    • (2005) Cancer Res. , vol.65 , pp. 10686-10691
    • da Rocha Dias, D.S.1    Friedlos, F.2    Light, Y.3
  • 45
    • 0001251439 scopus 로고
    • A new antifungal substance of fungal origin
    • Delmotte P., Delmotteplaquee J A new antifungal substance of fungal origin. Nature 1953, 171:344.
    • (1953) Nature , vol.171 , pp. 344
    • Delmotte, P.1    Delmotteplaquee, J.2
  • 46
    • 33747041690 scopus 로고    scopus 로고
    • Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection
    • Demidenko Z.N., Vivo C., Halicka H.D., et al. Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection. Cell Death Diff. 2006, 13:1434-1441.
    • (2006) Cell Death Diff. , vol.13 , pp. 1434-1441
    • Demidenko, Z.N.1    Vivo, C.2    Halicka, H.D.3
  • 47
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 1999, 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 50
    • 21244505104 scopus 로고    scopus 로고
    • Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design
    • Dymock B.W., Barril X., Brough P.A., et al. Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design. J. Med. Chem. 2005, 48:4212-4215.
    • (2005) J. Med. Chem. , vol.48 , pp. 4212-4215
    • Dymock, B.W.1    Barril, X.2    Brough, P.A.3
  • 52
    • 0034743361 scopus 로고    scopus 로고
    • Plasma pharmacokinetics and tissue distribution of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) in CD2F1 mice1
    • Egorin M.J., Zuhowski E.G., Rosen D.M., 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
  • 53
    • 33750107199 scopus 로고    scopus 로고
    • Enzyme specific activation of benzoquinone ansamycin prodrugs using HuCC49DeltaCH2-beta-galactosidase conjugates
    • Fang L., Battisti R.F., Cheng H., et al. Enzyme specific activation of benzoquinone ansamycin prodrugs using HuCC49DeltaCH2-beta-galactosidase conjugates. J. Med. Chem. 2006, 49:6290-6297.
    • (2006) J. Med. Chem. , vol.49 , pp. 6290-6297
    • Fang, L.1    Battisti, R.F.2    Cheng, H.3
  • 54
    • 0034603178 scopus 로고    scopus 로고
    • The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties
    • Felts S.J., Owen B.A., Nguyen P., et al. The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 2000, 275:3305-3312.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3305-3312
    • Felts, S.J.1    Owen, B.A.2    Nguyen, P.3
  • 55
    • 10944263745 scopus 로고    scopus 로고
    • Small molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity
    • Fewell S.W., Smith C.M., Lyon M.A., et al. Small molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity. J. Biol. Chem. 2004, 279:51,131-51,140.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51131-51140
    • Fewell, S.W.1    Smith, C.M.2    Lyon, M.A.3
  • 57
    • 1642490813 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 down-regulates Her2 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 Her2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine, and epothilone B. Mol. Cancer Ther. 2003, 2:971-984.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 971-984
    • Fuino, L.1    Bali, P.2    Wittmann, S.3
  • 58
    • 1242315877 scopus 로고    scopus 로고
    • HSP27 and HSP70: potentially oncogenic apoptosis inhibitors
    • Garrido C., Schmitt E., Cande C., et al. HSP27 and HSP70: potentially oncogenic apoptosis inhibitors. Cell Cycle 2003, 2:579-584.
    • (2003) Cell Cycle , vol.2 , pp. 579-584
    • Garrido, C.1    Schmitt, E.2    Cande, C.3
  • 59
    • 20844444898 scopus 로고    scopus 로고
    • Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3
    • George P., Bali P., Annavarapu S., et al. Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3. Blood 2005, 105:1768-1776.
    • (2005) Blood , vol.105 , pp. 1768-1776
    • George, P.1    Bali, P.2    Annavarapu, S.3
  • 60
    • 0037040975 scopus 로고    scopus 로고
    • The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation
    • Grammatikakis N., Vultur A., Ramana C.V., et al. The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation. J. Biol. Chem. 2002, 277:8312-8320.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8312-8320
    • Grammatikakis, N.1    Vultur, A.2    Ramana, C.V.3
  • 61
    • 30444441778 scopus 로고    scopus 로고
    • V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors
    • Grbovic O.M., Basso A.D., Sawai A., et al. V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors. Proc. Natl Acad. Sci. USA 2006, 103:57-62.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 57-62
    • Grbovic, O.M.1    Basso, A.D.2    Sawai, A.3
  • 62
    • 27544446054 scopus 로고    scopus 로고
    • Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition
    • Guo W., Reigan P., Siegel D., et al. Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res. 2005, 65:10,006-10,015.
    • (2005) Cancer Res. , vol.65 , pp. 10006-10015
    • Guo, W.1    Reigan, P.2    Siegel, D.3
  • 63
    • 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. 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, 65:10,536-10,544.
    • (2005) Cancer Res. , vol.65 , pp. 10536-10544
    • Guo, F.1    Rocha, K.2    Bali, P.3
  • 64
    • 33747140819 scopus 로고    scopus 로고
    • Antileukemic activity of shepherdin and molecular diversity of hsp90 inhibitors
    • Gyurkocza B., Plescia J., Raskett C.M., et al. Antileukemic activity of shepherdin and molecular diversity of hsp90 inhibitors. J. Natl Cancer Inst. 2006, 98:1068-1077.
    • (2006) J. Natl Cancer Inst. , vol.98 , pp. 1068-1077
    • Gyurkocza, B.1    Plescia, J.2    Raskett, C.M.3
  • 65
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., Weinberg R.A. The hallmarks of cancer. Cell 2000, 100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 67
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex
    • Hernandez M.P., Sullivan W.P., Toft D.O. The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J. Biol. Chem. 2002, 277:38,294-38,304.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 68
    • 0024364170 scopus 로고
    • Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein
    • Hickey E., Brandon S.E., Smale G., et al. Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol. Cell Biol. 1989, 9:2615-2626.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 2615-2626
    • Hickey, E.1    Brandon, S.E.2    Smale, G.3
  • 69
    • 33749433916 scopus 로고    scopus 로고
    • Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators
    • Hieronymus H., Lamb J., Ross K.N., et al. Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators. Cancer Cell 2006, 10:321-330.
    • (2006) Cancer Cell , vol.10 , pp. 321-330
    • Hieronymus, H.1    Lamb, J.2    Ross, K.N.3
  • 70
    • 33751573305 scopus 로고    scopus 로고
    • Identification of novel keratinocyte differentiation modulating compounds by high-throughput screening
    • Honma M., Stubbs M., Collins I., et al. Identification of novel keratinocyte differentiation modulating compounds by high-throughput screening. J. Biomol. Screen 2006, 11:977-984.
    • (2006) J. Biomol. Screen , vol.11 , pp. 977-984
    • Honma, M.1    Stubbs, M.2    Collins, I.3
  • 71
    • 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., et al. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res. 2001, 61:4003-4009.
    • (2001) Cancer Res. , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3
  • 72
    • 33644665083 scopus 로고    scopus 로고
    • A fl uorescence polarization assay for inhibitors of Hsp90
    • Howes R., Barril X., Dymock B.W., et al. A fl uorescence polarization assay for inhibitors of Hsp90. Analyt. Biochem. 2006, 350:202-213.
    • (2006) Analyt. Biochem. , vol.350 , pp. 202-213
    • Howes, R.1    Barril, X.2    Dymock, B.W.3
  • 73
    • 0033231024 scopus 로고    scopus 로고
    • A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90
    • Itoh H., Ogura M., Komatsuda A., et al. A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90. Biochem. J. 1999, 343(Pt 3):697-703.
    • (1999) Biochem. J. , vol.343 , Issue.PART 3 , pp. 697-703
    • Itoh, H.1    Ogura, M.2    Komatsuda, A.3
  • 75
    • 0025875566 scopus 로고
    • Heat shock inhibits the cytotoxic action of TNF-alpha in tumor cells but does not alter its noncytotoxic actions in endothelial and adrenal cells
    • Jaattela M., Pinola M., Saksela E Heat shock inhibits the cytotoxic action of TNF-alpha in tumor cells but does not alter its noncytotoxic actions in endothelial and adrenal cells. Lymphokine Cytokine Res. 1991, 10:119-125.
    • (1991) Lymphokine Cytokine Res. , vol.10 , pp. 119-125
    • Jaattela, M.1    Pinola, M.2    Saksela, E.3
  • 76
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jaattela M., Wissing D., Kokholm K., et al. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J, 1998, 17:6124-6134.
    • (1998) EMBO J, , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3
  • 78
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes
    • Johnson J., Corbisier R., Stensgard B., Toft D The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes. J. Steroid Biochem. Mol. Biol. 1996, 56:31-37.
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.56 , pp. 31-37
    • Johnson, J.1    Corbisier, R.2    Stensgard, B.3    Toft, D.4
  • 79
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C., Morimoto R.I. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl Cancer Inst. 2000, 92:1564-1572.
    • (2000) J. Natl Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 80
    • 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, 425:407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 81
    • 0035400270 scopus 로고    scopus 로고
    • Mechanisms of resistance to cisplatin
    • Kartalou M., Essigmann J.M. Mechanisms of resistance to cisplatin. Mutat. Res. 2001, 478:23-43.
    • (2001) Mutat. Res. , vol.478 , pp. 23-43
    • Kartalou, M.1    Essigmann, J.M.2
  • 82
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi Y., Kovacs J.J., McLaurin A., et al. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 2003, 115:727-738.
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3
  • 83
    • 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 L.R., Sharp S.Y., Rogers P.M., et al. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J. Natl Cancer Inst. 1999, 91:1940-1949.
    • (1999) J. Natl Cancer Inst. , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3
  • 84
    • 0033636957 scopus 로고    scopus 로고
    • Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteins
    • Kimmins S., MacRae T.H. Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteins. Cell Stress Chaperones 2000, 5:76-86.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 76-86
    • Kimmins, S.1    MacRae, T.H.2
  • 85
    • 0027251913 scopus 로고
    • Correlation of the survival of ovarian cancer patients with mRNA expression of the 60-kD heatshock protein HSP-60
    • Kimura E., Enns R.E., Alcaraz J., et al. Correlation of the survival of ovarian cancer patients with mRNA expression of the 60-kD heatshock protein HSP-60. J. Clin. Oncol. 1993, 11:891-898.
    • (1993) J. Clin. Oncol. , vol.11 , pp. 891-898
    • Kimura, E.1    Enns, R.E.2    Alcaraz, J.3
  • 86
    • 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, 7:215-219.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 215-219
    • Koishi, M.1    Yokota, S.2    Mae, T.3
  • 87
    • 13944270580 scopus 로고    scopus 로고
    • Crystal structures of human HSP90alpha-complexed with dihydroxyphenylpyrazoles
    • Kreusch A., Han S., Brinker A., et al. Crystal structures of human HSP90alpha-complexed with dihydroxyphenylpyrazoles. Bioorg. Med. Chem. Lett. 2005, 15:1475-1478.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 1475-1478
    • Kreusch, A.1    Han, S.2    Brinker, A.3
  • 88
    • 34248663408 scopus 로고    scopus 로고
    • Effects of the histone deacetylase inhibitor (HDACi) LAQ824 on histone acetylation, Hsp70 and c-Raf in peripheral blood lymphocytes from patients with advanced solid tumors enrolled in a Phase I clinical trial
    • Kristeleit R., Tandy D., Atadja P., et al. Effects of the histone deacetylase inhibitor (HDACi) LAQ824 on histone acetylation, Hsp70 and c-Raf in peripheral blood lymphocytes from patients with advanced solid tumors enrolled in a Phase I clinical trial. Proc. Am. Assoc. Clin. Oncol. 2004, 22:3032.
    • (2004) Proc. Am. Assoc. Clin. Oncol. , vol.22 , pp. 3032
    • Kristeleit, R.1    Tandy, D.2    Atadja, P.3
  • 89
    • 0027081145 scopus 로고
    • Potent and specific inhibition of p60v-src protein kinase both in vivo and in vitro by radicicol
    • Kwon H.J., Yoshida M., Fukui Y., et al. Potent and specific inhibition of p60v-src protein kinase both in vivo and in vitro by radicicol. Cancer Res. 1992, 52:6926-6930.
    • (1992) Cancer Res. , vol.52 , pp. 6926-6930
    • Kwon, H.J.1    Yoshida, M.2    Fukui, Y.3
  • 90
    • 0036377797 scopus 로고    scopus 로고
    • Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90 (hsp90) is necessary for its autophosphorylation
    • Langer T., Schlatter H., Fasold H Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90 (hsp90) is necessary for its autophosphorylation. Cell Biol. Intl 2002, 26:653-657.
    • (2002) Cell Biol. Intl , vol.26 , pp. 653-657
    • Langer, T.1    Schlatter, H.2    Fasold, H.3
  • 91
    • 3142545683 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of a new class of geldanamycin derivatives as potent inhibitors of Hsp90
    • le Brazidec J.Y., Kamal A., Busch D., et al. Synthesis and biological evaluation of a new class of geldanamycin derivatives as potent inhibitors of Hsp90. J. Med. Chem. 2004, 47:3865-3873.
    • (2004) J. Med. Chem. , vol.47 , pp. 3865-3873
    • le Brazidec, J.Y.1    Kamal, A.2    Busch, D.3
  • 92
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation
    • Li C.Y., Lee J.S., Ko Y.G., et al. Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J. Biol. Chem. 2000, 275:25,665-25,671.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25665-25671
    • Li, C.Y.1    Lee, J.S.2    Ko, Y.G.3
  • 93
    • 14544267242 scopus 로고    scopus 로고
    • New aminocoumarin antibiotics from genetically engineered Streptomyces strains
    • Li S.M., Heide L New aminocoumarin antibiotics from genetically engineered Streptomyces strains. Curr. Med. Chem. 2005, 12:419-427.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 419-427
    • Li, S.M.1    Heide, L.2
  • 95
    • 17444416142 scopus 로고    scopus 로고
    • Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90
    • Llauger L., He H., Kim J., et al. Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90. J. Med. Chem. 2005, 48:2892-2905.
    • (2005) J. Med. Chem. , vol.48 , pp. 2892-2905
    • Llauger, L.1    He, H.2    Kim, J.3
  • 96
    • 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
  • 97
    • 34147150867 scopus 로고    scopus 로고
    • Gene and protein expression profiling of human ovarian cancer cells treated with the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG)
    • Maloney A., Clarke P., Naaby-Hansen S., et al. Gene and protein expression profiling of human ovarian cancer cells treated with the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17AAG). Cancer Res. 2007, 67:3239-3253.
    • (2007) Cancer Res. , vol.67 , pp. 3239-3253
    • Maloney, A.1    Clarke, P.2    Naaby-Hansen, S.3
  • 98
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATPbinding domain in the carboxyl terminus of the chaperone
    • Marcu M.G., Chadli A., Bouhouche I., et al. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATPbinding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 2000, 275:37,181-37,186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3
  • 99
    • 0034594644 scopus 로고    scopus 로고
    • Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins
    • Marcu M.G., Schulte T.W., Neckers L Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J. Natl Cancer Inst. 2000, 92:242-248.
    • (2000) J. Natl Cancer Inst. , vol.92 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 100
    • 20844444338 scopus 로고    scopus 로고
    • S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities
    • Martinez-Ruiz A., Villanueva L., de Gonzalez O.C., et al. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc. Natl Acad. Sci. USA 2005, 102:8525-8530.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8525-8530
    • Martinez-Ruiz, A.1    Villanueva, L.2    de Gonzalez, O.C.3
  • 101
    • 0842281502 scopus 로고    scopus 로고
    • Recombinant antibodies: a natural partner in combinatorial antifungal therapy
    • Matthews R.C., Burnie J.P. Recombinant antibodies: a natural partner in combinatorial antifungal therapy. Vaccine 2004, 22:865-871.
    • (2004) Vaccine , vol.22 , pp. 865-871
    • Matthews, R.C.1    Burnie, J.P.2
  • 102
    • 0037636527 scopus 로고    scopus 로고
    • Preclinical assessment of the efficacy of mycograb, a human recombinant antibody against fungal HSP90
    • Matthews R.C., Rigg G., Hodgetts S., et al. Preclinical assessment of the efficacy of mycograb, a human recombinant antibody against fungal HSP90. Antimicrob. Agents Chemother. 2003, 47:2208-2216.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2208-2216
    • Matthews, R.C.1    Rigg, G.2    Hodgetts, S.3
  • 103
    • 14844353677 scopus 로고    scopus 로고
    • Genetic approaches to polyketide antibiotics
    • McDaniel R., Welch M., Hutchinson C.R. Genetic approaches to polyketide antibiotics. 1. Chem. Rev. 2005, 105:543-558.
    • (2005) 1. Chem. Rev. , vol.105 , pp. 543-558
    • McDaniel, R.1    Welch, M.2    Hutchinson, C.R.3
  • 104
    • 33746341544 scopus 로고    scopus 로고
    • Discovery and development of pyrazole-scaffold hsp90 inhibitors
    • McDonald E., Jones K., Brough P.A., et al. Discovery and development of pyrazole-scaffold hsp90 inhibitors. Curr. Top. Med. Chem. 2006, 6:1193-1203.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1193-1203
    • McDonald, E.1    Jones, K.2    Brough, P.A.3
  • 105
    • 33746377987 scopus 로고    scopus 로고
    • Inhibitors of the HSP90 molecular chaperone: attacking the master regulator in cancer
    • McDonald E., Workman P., Jones K Inhibitors of the HSP90 molecular chaperone: attacking the master regulator in cancer. Curr. Top. Med. Chem. 2006, 6:1091-1107.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1091-1107
    • McDonald, E.1    Workman, P.2    Jones, K.3
  • 106
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heatinducible apoptosis
    • McMillan D.R., Xiao X., Shao L., et al. Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heatinducible apoptosis. J. Biol. Chem. 1998, 273:7523-7528.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.2    Shao, L.3
  • 107
    • 33845915755 scopus 로고    scopus 로고
    • Smallmolecule targeting of heat shock protein 90 chaperone function: rational identification of a new anticancer lead
    • Meli M., Pennati M., Curto M., et al. Smallmolecule targeting of heat shock protein 90 chaperone function: rational identification of a new anticancer lead. J. Med. Chem. 2006, 49:7721-7730.
    • (2006) J. Med. Chem. , vol.49 , pp. 7721-7730
    • Meli, M.1    Pennati, M.2    Curto, M.3
  • 108
    • 4444311881 scopus 로고    scopus 로고
    • Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity
    • Mimnaugh E.G., Xu W., Vos M., et al. Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity. Mol. Cancer Ther. 2004, 3:551-566.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 551-566
    • Mimnaugh, E.G.1    Xu, W.2    Vos, M.3
  • 109
    • 34248166884 scopus 로고    scopus 로고
    • Phase I trial of KOS-953, a heat shock protein 90 inhibitor, and trastuzumab (T)
    • Modi S., Stopeck A., Gordon M.S., et al. Phase I trial of KOS-953, a heat shock protein 90 inhibitor, and trastuzumab (T). J. Clin. Oncol. (Meeting Abstracts) 2006, 24:501.
    • (2006) J. Clin. Oncol. (Meeting Abstracts) , vol.24 , pp. 501
    • Modi, S.1    Stopeck, A.2    Gordon, M.S.3
  • 110
    • 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 R.I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 1998, 12:3788-3796.
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 111
    • 18744411808 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of HSP90 inhibitors based on conformational analysis of radicicol and its analogs
    • Moulin E., Zoete V., Barluenga S., et al. Design, synthesis, and biological evaluation of HSP90 inhibitors based on conformational analysis of radicicol and its analogs. J Am. Chem. Soc. 2005, 127:6999-7004.
    • (2005) J Am. Chem. Soc. , vol.127 , pp. 6999-7004
    • Moulin, E.1    Zoete, V.2    Barluenga, S.3
  • 112
    • 0034890377 scopus 로고    scopus 로고
    • Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapyinduced apoptosis in an RB- and schedule-dependent manner
    • See also: E.A. Sausville (2001); 2228-2236.
    • Munster P.N., Basso A., Solit D., et al. Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapyinduced apoptosis in an RB- and schedule-dependent manner 2001, See also: E.A. Sausville (2001). Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters. Clin. Cancer Res. 7, 2155-2158; 2228-2236.
    • (2001) Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters. Clin. Cancer Res. , vol.7 , pp. 2155-2158
    • Munster, P.N.1    Basso, A.2    Solit, D.3
  • 113
    • 26644473193 scopus 로고    scopus 로고
    • Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone
    • Murphy P.J., Morishima Y., Kovacs J.J., et al. Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone. J. Biol. Chem. 2005, 280:33,792-33,799.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33792-33799
    • Murphy, P.J.1    Morishima, Y.2    Kovacs, J.J.3
  • 115
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1
    • Panaretou B., Siligardi G., Meyer P., et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol. Cell 2002, 10:1307-1318.
    • (2002) Mol. Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1    Siligardi, G.2    Meyer, P.3
  • 116
    • 10644292744 scopus 로고    scopus 로고
    • Engineered biosynthesis of geldanamycin analogs for Hsp90 inhibition
    • Patel K., Piagentini M., Rascher A., et al. Engineered biosynthesis of geldanamycin analogs for Hsp90 inhibition. Chem. Biol. 2004, 11:1625-1633.
    • (2004) Chem. Biol. , vol.11 , pp. 1625-1633
    • Patel, K.1    Piagentini, M.2    Rascher, A.3
  • 117
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the hsp90 molecular chaperone machinery
    • Pearl L.H., Prodromou C Structure and mechanism of the hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75:271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 118
    • 33746705661 scopus 로고    scopus 로고
    • Chaperoning steroid hormone action
    • Picard D Chaperoning steroid hormone action. Trends Endocrinol. Metab. 2006, 17:229-235.
    • (2006) Trends Endocrinol. Metab. , vol.17 , pp. 229-235
    • Picard, D.1
  • 119
    • 21144437911 scopus 로고    scopus 로고
    • Rational design of shepherdin, a novel anticancer agent
    • Plescia J., Salz W., Xia F., et al. Rational design of shepherdin, a novel anticancer agent. Cancer Cell 2005, 7:457-468.
    • (2005) Cancer Cell , vol.7 , pp. 457-468
    • Plescia, J.1    Salz, W.2    Xia, F.3
  • 120
    • 0029947822 scopus 로고    scopus 로고
    • Mitochondria are selective targets for the protective effects of heat shock against oxidative injury
    • Polla B.S., Kantengwa S., Francois D., et al. Mitochondria are selective targets for the protective effects of heat shock against oxidative injury. Proc. Natl Acad. Sci. USA 1996, 93:6458-6463.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6458-6463
    • Polla, B.S.1    Kantengwa, S.2    Francois, D.3
  • 121
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt W.B., Toft D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exper. Biol. Med. (Maywood) 2003, 228:111-133.
    • (2003) Exper. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 122
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C., Roe S.M., O'Brien R., et al. 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
  • 123
    • 0034663806 scopus 로고    scopus 로고
    • The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains
    • Prodromou C., Panaretou B., Chohan S., et al. The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J. 2000, 19:4383-4392.
    • (2000) EMBO J. , vol.19 , pp. 4383-4392
    • Prodromou, C.1    Panaretou, B.2    Chohan, S.3
  • 124
    • 33750986790 scopus 로고    scopus 로고
    • Inhibition of hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol
    • Proisy N., Sharp S.Y., Boxall K., et al. Inhibition of hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol. Chem. Biol. 2006, 13:1203-1215.
    • (2006) Chem. Biol. , vol.13 , pp. 1203-1215
    • Proisy, N.1    Sharp, S.Y.2    Boxall, K.3
  • 125
    • 0034383950 scopus 로고    scopus 로고
    • Protein folding: progress made and promises ahead
    • Radford S.E. Protein folding: progress made and promises ahead. Trends Biochem. Sci. 2000, 25:611-618.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 611-618
    • Radford, S.E.1
  • 126
    • 0028970484 scopus 로고
    • Differential expression of Mr 70,000 heat shock protein in normal, premalignant, and malignant human uterine cervix
    • Ralhan R., Kaur J Differential expression of Mr 70,000 heat shock protein in normal, premalignant, and malignant human uterine cervix. Clin. Cancer Res. 1995, 1:1217-1222.
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1217-1222
    • Ralhan, R.1    Kaur, J.2
  • 127
    • 25844516563 scopus 로고    scopus 로고
    • Structurebased design of 7-carbamate analogs of geldanamycin
    • Rastelli G., Tian Z.Q., Wang Z., et al. Structurebased design of 7-carbamate analogs of geldanamycin. Bioorg. Med. Chem. Lett. 2005, 15:5016-5021.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 5016-5021
    • Rastelli, G.1    Tian, Z.Q.2    Wang, Z.3
  • 128
    • 33749983958 scopus 로고    scopus 로고
    • Hsp90: twist and fold
    • Richter K., Buchner J hsp90: twist and fold. Cell 2006, 127:251-253.
    • (2006) Cell , vol.127 , pp. 251-253
    • Richter, K.1    Buchner, J.2
  • 129
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa F A new puffing pattern induced by temperature shock and DNP in Drosophila. Experienta 1962, 18:571-573.
    • (1962) Experienta , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 130
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe S.M., Prodromou C., O'Brien R., et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 1999, 42:260-266.
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3
  • 131
    • 10744220096 scopus 로고    scopus 로고
    • The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation
    • Rosenhagen M.C., Soti C., Schmidt U., et al. The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation. Mol. Endocrinol. 2003, 17:1991-2001.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1991-2001
    • Rosenhagen, M.C.1    Soti, C.2    Schmidt, U.3
  • 132
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
    • Rowlands M.G., Newbatt Y.M., Prodromou C., et al. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Analyt. Biochem. 2004, 327:176-183.
    • (2004) Analyt. Biochem. , vol.327 , pp. 176-183
    • Rowlands, M.G.1    Newbatt, Y.M.2    Prodromou, C.3
  • 133
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford S.L., Lindquist S Hsp90 as a capacitor for morphological evolution. Nature 1998, 396:336-342.
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 134
    • 33745071182 scopus 로고    scopus 로고
    • Potentiation of paclitaxel activity by the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin in human ovarian carcinoma cell lines with high levels of activated AKT
    • Sain N., Krishnan B., Ormerod M.G., et al. Potentiation of paclitaxel activity by the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin in human ovarian carcinoma cell lines with high levels of activated AKT. Mol. Cancer Ther. 2006, 5:1197-1208.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1197-1208
    • Sain, N.1    Krishnan, B.2    Ormerod, M.G.3
  • 135
    • 0034253474 scopus 로고    scopus 로고
    • Negative regulation of the Apaf-1 apoptosome by Hsp70
    • Saleh A., Srinivasula S.M., Balkir L., et al. Negative regulation of the Apaf-1 apoptosome by Hsp70. Nat. Cell Biol. 2000, 2:476-483.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 476-483
    • Saleh, A.1    Srinivasula, S.M.2    Balkir, L.3
  • 136
    • 32844470038 scopus 로고    scopus 로고
    • AEG3482 is an antiapoptotic compound that inhibits Jun kinase activity and cell death through induced expression of heat shock protein 70
    • Salehi A.H., Morris S.J., Ho W.C., et al. AEG3482 is an antiapoptotic compound that inhibits Jun kinase activity and cell death through induced expression of heat shock protein 70. Chem. Biol. 2006, 13:213-223.
    • (2006) Chem. Biol. , vol.13 , pp. 213-223
    • Salehi, A.H.1    Morris, S.J.2    Ho, W.C.3
  • 137
    • 33645470397 scopus 로고    scopus 로고
    • Benzoquinone ansamycin heat shock protein 90 inhibitors modulate multiple functions required for tumor angiogenesis
    • Sanderson S., Valenti M., Gowan S., et al. Benzoquinone ansamycin heat shock protein 90 inhibitors modulate multiple functions required for tumor angiogenesis. Mol. Cancer Ther. 2006, 5:522-532.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 522-532
    • Sanderson, S.1    Valenti, M.2    Gowan, S.3
  • 139
    • 0029123128 scopus 로고
    • ErbB-2 oncogene inhibition by geldanamycin derivatives: synthesis, mechanism of action, and structure-activity relationships
    • Schnur R.C., Corman M.L., Gallaschun R.J., et al. erbB-2 oncogene inhibition by geldanamycin derivatives: synthesis, mechanism of action, and structure-activity relationships. J. Med. Chem. 1995, 38:3813-3820.
    • (1995) J. Med. Chem. , vol.38 , pp. 3813-3820
    • Schnur, R.C.1    Corman, M.L.2    Gallaschun, R.J.3
  • 140
    • 0029122080 scopus 로고
    • Inhibition of the oncogene product p185erbB-2 in vitro and in vivo by geldanamycin and dihydrogeldanamycin derivatives
    • Schnur R.C., Corman M.L., Gallaschun R.J., et al. Inhibition of the oncogene product p185erbB-2 in vitro and in vivo by geldanamycin and dihydrogeldanamycin derivatives. J. Med. Chem. 1995, 38:3806-3812.
    • (1995) J. Med. Chem. , vol.38 , pp. 3806-3812
    • Schnur, R.C.1    Corman, M.L.2    Gallaschun, R.J.3
  • 141
    • 0035903129 scopus 로고    scopus 로고
    • Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37
    • Scholz G.M., Cartledge K., Hall N.E. Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37. J. Biol. Chem. 2001, 276:30,971-30,979.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30971-30979
    • Scholz, G.M.1    Cartledge, K.2    Hall, N.E.3
  • 142
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte T.W., Neckers L.M. The benzoquinone ansamycin 17-allylamino17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. 1998, 42:273-279.
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 143
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte T.W., An W.G., Neckers L.M. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem. Biophys. Res. Commun. 1997, 239:655-659.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 144
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte T.W., Akinaga S., Soga S., et al. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 1998, 3:100-108.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3
  • 145
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • Scroggins B.T., Robzyk K., Wang D., et al. An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol. Cell 2007, 25:151-159.
    • (2007) Mol. Cell , vol.25 , pp. 151-159
    • Scroggins, B.T.1    Robzyk, K.2    Wang, D.3
  • 146
    • 33947210121 scopus 로고    scopus 로고
    • In vitro biological characterization of a novel, synthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors
    • Sharp S.Y., Boxall K., Rowlands M., et al. In vitro biological characterization of a novel, synthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors. Cancer Res. 2007, 67:2206-2216.
    • (2007) Cancer Res. , vol.67 , pp. 2206-2216
    • Sharp, S.Y.1    Boxall, K.2    Rowlands, M.3
  • 147
    • 20444465254 scopus 로고    scopus 로고
    • Radester, a novel inhibitor of the Hsp90 protein folding machinery
    • Shen G., Blagg B.S. Radester, a novel inhibitor of the Hsp90 protein folding machinery. Org. Lett. 2005, 7:2157-2160.
    • (2005) Org. Lett. , vol.7 , pp. 2157-2160
    • Shen, G.1    Blagg, B.S.2
  • 148
    • 7044269372 scopus 로고    scopus 로고
    • Syntheses of photolabile novobiocin analogues
    • Shen G., Yu X.M., Blagg B.S. Syntheses of photolabile novobiocin analogues. Bioorg. Med. Chem. Lett. 2004, 14:5903-5906.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 5903-5906
    • Shen, G.1    Yu, X.M.2    Blagg, B.S.3
  • 149
    • 0036233939 scopus 로고    scopus 로고
    • Heat shock protein 90-antagonist destabilizes Bcr-Abl/HSP90 chaperone complex
    • Shiotsu Y., Soga S., Akinaga S Heat shock protein 90-antagonist destabilizes Bcr-Abl/HSP90 chaperone complex. Leukemia Lymphoma 2002, 43:961-968.
    • (2002) Leukemia Lymphoma , vol.43 , pp. 961-968
    • Shiotsu, Y.1    Soga, S.2    Akinaga, S.3
  • 150
    • 33749993417 scopus 로고    scopus 로고
    • The consensus coding sequences of human breast and colorectal cancers
    • Sjoblom T., Jones S., Wood L.D., et al. The consensus coding sequences of human breast and colorectal cancers. Science 2006, 314:268-274.
    • (2006) Science , vol.314 , pp. 268-274
    • Sjoblom, T.1    Jones, S.2    Wood, L.D.3
  • 151
    • 33746040516 scopus 로고    scopus 로고
    • Preclinical pharmacokinetics and metabolism of a novel diaryl pyrazole resorcinol series of heat shock protein 90 inhibitors
    • Smith N., Hayes A., James K., et al. Preclinical pharmacokinetics and metabolism of a novel diaryl pyrazole resorcinol series of heat shock protein 90 inhibitors. Mol. Cancer Ther. 2006, 5:1628-1637.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1628-1637
    • Smith, N.1    Hayes, A.2    James, K.3
  • 152
    • 33847405771 scopus 로고    scopus 로고
    • The application of cassette dosing for pharmacokinetic screening in small-molecule cancer drug discovery
    • Smith N., Raynaud F., Workman P The application of cassette dosing for pharmacokinetic screening in small-molecule cancer drug discovery. Mol. Cancer Ther. 2007, 6:428-440.
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 428-440
    • Smith, N.1    Raynaud, F.2    Workman, P.3
  • 153
    • 21244466289 scopus 로고    scopus 로고
    • Comparison of 17-dimethylaminoethylamino17-demethoxy-geldanamycin (17DMAG) and 17allylamino-17-demethoxygeldanamycin (17AAG) in vitro: effects on Hsp90 and client proteins in melanoma models
    • Smith V., Sausville E.A., Camalier R.F., et al. Comparison of 17-dimethylaminoethylamino17-demethoxy-geldanamycin (17DMAG) and 17allylamino-17-demethoxygeldanamycin (17AAG) in vitro: effects on Hsp90 and client proteins in melanoma models. Cancer Chemother. Pharmacol. 2005, 56:126-137.
    • (2005) Cancer Chemother. Pharmacol. , vol.56 , pp. 126-137
    • Smith, V.1    Sausville, E.A.2    Camalier, R.F.3
  • 154
    • 2542643923 scopus 로고    scopus 로고
    • Imaging the pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors
    • Smith-Jones P.M., Solit D.B., Akhurst T., et al. Imaging the pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors. Nat. Biotechnol. 2004, 22:701-706.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 701-706
    • Smith-Jones, P.M.1    Solit, D.B.2    Akhurst, T.3
  • 156
    • 0348111450 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of GRP94: basis for ligand specificity and regulation
    • Soldano K.L., Jivan A., Nicchitta C.V., Gewirth D.T. Structure of the N-terminal domain of GRP94: basis for ligand specificity and regulation. J. Biol. Chem. 2003, 48:48,330-48,338.
    • (2003) J. Biol. Chem. , vol.48 , pp. 48330-48338
    • Soldano, K.L.1    Jivan, A.2    Nicchitta, C.V.3    Gewirth, D.T.4
  • 157
    • 33746417580 scopus 로고    scopus 로고
    • Hsp90: a novel target for cancer therapy
    • Solit D.B., Rosen N Hsp90: a novel target for cancer therapy. Curr. Top. Med. Chem. 2006, 6:1205-1214.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1205-1214
    • Solit, D.B.1    Rosen, N.2
  • 158
    • 0036091221 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER2/neu and inhibits the growth of prostate cancer xenografts
    • Solit D.B., Zheng F.F., Drobnjak M., et al. 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER2/neu and inhibits the growth of prostate cancer xenografts. Clin. Cancer Res. 2002, 8:986-993.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 986-993
    • Solit, D.B.1    Zheng, F.F.2    Drobnjak, M.3
  • 159
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function downregulates Akt kinase and sensitizes tumors to Taxol
    • Solit D.B., Basso A.D., Olshen A.B., et al. Inhibition of heat shock protein 90 function downregulates Akt kinase and sensitizes tumors to Taxol. Cancer Res. 2003, 63:2139-2144.
    • (2003) Cancer Res. , vol.63 , pp. 2139-2144
    • Solit, D.B.1    Basso, A.D.2    Olshen, A.B.3
  • 161
    • 33244474580 scopus 로고    scopus 로고
    • Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation
    • Stankiewicz A.R., Lachapelle G., Foo C.P., et al. Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation. J. Biol. Chem. 2005, 280:38,729-38,739.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38729-38739
    • Stankiewicz, A.R.1    Lachapelle, G.2    Foo, C.P.3
  • 163
    • 33751258297 scopus 로고    scopus 로고
    • Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anticancer agent directed against Hsp90
    • Sydor J.R., Normant E., Pien C.S., et al. Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anticancer agent directed against Hsp90. Proc. Natl Acad. Sci. USA 2006, 103:17,408-17,413.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 17408-17413
    • Sydor, J.R.1    Normant, E.2    Pien, C.S.3
  • 164
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • Takayama S., Reed J.C. Molecular chaperone targeting and regulation by BAG family proteins. Nat. Cell Biol. 2001, 3:E237-E241.
    • (2001) Nat. Cell Biol. , vol.3
    • Takayama, S.1    Reed, J.C.2
  • 165
    • 0033670274 scopus 로고    scopus 로고
    • Effect of deoxyspergualin on the long-term outcome of renal transplantation
    • Tanabe K., Tokumoto T., Ishikawa N., et al. Effect of deoxyspergualin on the long-term outcome of renal transplantation. Transplant Proc. 2000, 32:1745-1746.
    • (2000) Transplant Proc. , vol.32 , pp. 1745-1746
    • Tanabe, K.1    Tokumoto, T.2    Ishikawa, N.3
  • 166
    • 0141708701 scopus 로고    scopus 로고
    • Natural product origins of Hsp90 inhibitors
    • Uehara Y Natural product origins of Hsp90 inhibitors. Curr. Cancer Drug Targets 2003, 3:325-330.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 325-330
    • Uehara, Y.1
  • 167
    • 34547192041 scopus 로고    scopus 로고
    • HSP-90 inhibitors promise to complement cancer therapies
    • Vastag B HSP-90 inhibitors promise to complement cancer therapies. Nat. Biotechnol. 2006, 24:1307.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1307
    • Vastag, B.1
  • 168
    • 33747878717 scopus 로고    scopus 로고
    • Structure of an Hsp90-Cdc37-Cdk4 complex
    • Vaughan C.K., Gohlke U., Sobott F., et al. Structure of an Hsp90-Cdc37-Cdk4 complex. Mol. Cell 2006, 23:697-707.
    • (2006) Mol. Cell , vol.23 , pp. 697-707
    • Vaughan, C.K.1    Gohlke, U.2    Sobott, F.3
  • 169
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: versatile regulators
    • Verdin E., Dequiedt F., Kasler H.G. Class II histone deacetylases: versatile regulators. Trends Genet. 2003, 19:286-293.
    • (2003) Trends Genet. , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 170
    • 3042553538 scopus 로고    scopus 로고
    • Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90
    • Vilenchik M., Solit D., Basso A., et al. Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90. Chem. Biol. 2004, 11:787-797.
    • (2004) Chem. Biol. , vol.11 , pp. 787-797
    • Vilenchik, M.1    Solit, D.2    Basso, A.3
  • 171
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fi brosis
    • Wang X., Venable J., LaPointe P., et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fi brosis. Cell 2006, 127:803-815.
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    LaPointe, P.3
  • 172
    • 33746961739 scopus 로고    scopus 로고
    • Mechanisms of disease: Oncogene addiction - a rationale for molecular targeting in cancer therapy
    • Weinstein I.B., Joe A.K. Mechanisms of disease: Oncogene addiction - a rationale for molecular targeting in cancer therapy. Nat. Clin. Pract. Oncol. 2006, 3:448-457.
    • (2006) Nat. Clin. Pract. Oncol. , vol.3 , pp. 448-457
    • Weinstein, I.B.1    Joe, A.K.2
  • 173
    • 33646900838 scopus 로고    scopus 로고
    • Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death
    • Westerheide S.D., Kawahara T.L., Orton K., Morimoto R.I Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death. J. Biol. Chem. 2006, 281:9616-9622.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9616-9622
    • Westerheide, S.D.1    Kawahara, T.L.2    Orton, K.3    Morimoto, R.I.4
  • 174
  • 175
    • 0026735864 scopus 로고
    • Benzoquinonoid ansamycins possess selective tumoricidal activity unrelated to src kinase inhibition
    • Whitesell L., Shifrin S.D., Schwab G., Neckers L.M. Benzoquinonoid ansamycins possess selective tumoricidal activity unrelated to src kinase inhibition. Cancer Res. 1992, 52:1721-1728.
    • (1992) Cancer Res. , vol.52 , pp. 1721-1728
    • Whitesell, L.1    Shifrin, S.D.2    Schwab, G.3    Neckers, L.M.4
  • 176
    • 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 E.G., de Costa B., et al. 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, 91:8324-8328.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    de Costa, B.3
  • 177
    • 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, 2:131-138.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 131-138
    • Workman, P.1
  • 178
    • 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
  • 179
    • 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, 206:149-157.
    • (2004) Cancer Lett. , vol.206 , pp. 149-157
    • Workman, P.1
  • 180
    • 33646457229 scopus 로고    scopus 로고
    • Minimally invasive pharmacokinetic and pharmacodynamic technologies in hypothesis-testing clinical trials of innovative therapies
    • Workman P., Aboagye E.O., Chung Y.L., et al. Minimally invasive pharmacokinetic and pharmacodynamic technologies in hypothesis-testing clinical trials of innovative therapies. J. Natl Cancer Inst. 2006, 98:580-598.
    • (2006) J. Natl Cancer Inst. , vol.98 , pp. 580-598
    • Workman, P.1    Aboagye, E.O.2    Chung, Y.L.3
  • 181
    • 3042637928 scopus 로고    scopus 로고
    • Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms
    • Wright L., Barril X., Dymock B., et al. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem. Biol. 2004, 11:775-785.
    • (2004) Chem. Biol. , vol.11 , pp. 775-785
    • Wright, L.1    Barril, X.2    Dymock, B.3
  • 182
    • 0037451452 scopus 로고    scopus 로고
    • Total synthesis as a resource in the discovery of potentially valuable antitumor agents: cycloproparadicicol
    • Yamamoto K., Garbaccio R.M., Stachel S.J., et al. Total synthesis as a resource in the discovery of potentially valuable antitumor agents: cycloproparadicicol. Angew. Chem. Intl Ed Engl. 2003, 42:1280-1284.
    • (2003) Angew. Chem. Intl Ed Engl. , vol.42 , pp. 1280-1284
    • Yamamoto, K.1    Garbaccio, R.M.2    Stachel, S.J.3
  • 183
    • 33646406554 scopus 로고    scopus 로고
    • Celastrol, a triterpene extracted from the Chinese "Thunder of God Vine," is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice
    • Yang H., Chen D., Cui Q.C., et al. Celastrol, a triterpene extracted from the Chinese "Thunder of God Vine," is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res. 2006, 66:4758-4765.
    • (2006) Cancer Res. , vol.66 , pp. 4758-4765
    • Yang, H.1    Chen, D.2    Cui, Q.C.3
  • 184
    • 18844396087 scopus 로고    scopus 로고
    • Potent activity of a novel dimeric heat shock protein 90 inhibitor against head and neck squamous cell carcinoma in vitro and in vivo
    • Yin X., Zhang H., Burrows F., et al. Potent activity of a novel dimeric heat shock protein 90 inhibitor against head and neck squamous cell carcinoma in vitro and in vivo. Clin. Cancer Res. 2005, 11:3889-3896.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 3889-3896
    • Yin, X.1    Zhang, H.2    Burrows, F.3
  • 185
    • 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, 60:2942-2948.
    • (2000) Cancer Res. , vol.60 , pp. 2942-2948
    • Yokota, S.1    Kitahara, M.2    Nagata, K.3
  • 187
    • 25144435448 scopus 로고    scopus 로고
    • Hsp90 inhibitors identified from a library of novobiocin analogues
    • Yu X.M., Shen G., Neckers L., et al. Hsp90 inhibitors identified from a library of novobiocin analogues. J. Am. Chem. Soc. 2005, 127:12,778-12,779.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12778-12779
    • Yu, X.M.1    Shen, G.2    Neckers, L.3
  • 188
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells
    • Yufu Y., Nishimura J., Nawata H High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells. Leukemia Res. 1992, 16:597-605.
    • (1992) Leukemia Res. , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 189
    • 33745086222 scopus 로고    scopus 로고
    • Identification of new biomarkers for clinical trials of Hsp90 inhibitors
    • Zhang H., Chung D., Yang Y.C., et al. Identification of new biomarkers for clinical trials of Hsp90 inhibitors. Mol. Cancer Ther. 2006, 5:1256-1264.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1256-1264
    • Zhang, H.1    Chung, D.2    Yang, Y.C.3
  • 190
    • 0029085027 scopus 로고
    • Suppression of RAS and MOS transformation by radicicol
    • Zhao J.F., Nakano H., Sharma S Suppression of RAS and MOS transformation by radicicol. Oncogene 1995, 11:161-173.
    • (1995) Oncogene , vol.11 , pp. 161-173
    • Zhao, J.F.1    Nakano, H.2    Sharma, S.3
  • 191
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • Zhao R., Davey M., Hsu Y.C., et al. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 2005, 120:715-727.
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1    Davey, M.2    Hsu, Y.C.3
  • 192
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stresssensitive complex with HSF1
    • Zou J., Guo Y., Guettouche T., et al. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stresssensitive complex with HSF1. Cell 1998, 94:471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.