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Volumn 9, Issue 15, 2009, Pages 1419-1435

Hsp90 inhibition with resorcylic acid lactones (RALs)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTINEOPLASTIC AGENT; GELDANAMYCIN; HEAT SHOCK PROTEIN 90 INHIBITOR; POCHONIN A; POCHONIN B; POCHONIN C; POCHONIN D; POCHONIN E; POCHONIN G; POCHONIN I; POCHONIN J; POCHONIN L; POCHONIN N; POCHONIN O; POCHONIN P; PROCAINE PENICILLIN ALUMINIUM MONOSTEARATE; RADICICOL; RESORCYCLIC ACID LACTONE; TANESPIMYCIN; TETRAHYDROMONORDEN; UNCLASSIFIED DRUG; ZEARALENONE; ADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 90; MACROLIDE;

EID: 74249106421     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802609789895665     Document Type: Review
Times cited : (52)

References (100)
  • 1
    • 0001251439 scopus 로고
    • A new antifungal substance of fungal origin
    • Delmotte, P.; Delmotte-Plaquee, J. A new antifungal substance of fungal origin. Nature 1953, 171, 344.
    • (1953) Nature , vol.171 , pp. 344
    • Delmotte, P.1    Delmotte-Plaquee, J.2
  • 2
    • 33845481603 scopus 로고    scopus 로고
    • Chemistry and biology of resorcylic acid lactones
    • Winssinger, N.; Barluenga, S. Chemistry and biology of resorcylic acid lactones. Chem. Commun. 2007, 22-36.
    • (2007) Chem. Commun , pp. 22-36
    • Winssinger, N.1    Barluenga, S.2
  • 3
    • 57049163500 scopus 로고    scopus 로고
    • Resorcylic acid lactones: A pluripotent scaffold with therapeutic potential
    • Barluenga, S.; Dakas, P.; Boulifa, M.; Moulin, E.; Winssinger, N.; Resorcylic acid lactones: A pluripotent scaffold with therapeutic potential. C. R. Chem. 2008, 11, 1306-1317.
    • (2008) C. R. Chem , vol.11 , pp. 1306-1317
    • Barluenga, S.1    Dakas, P.2    Boulifa, M.3    Moulin, E.4    Winssinger, N.5
  • 4
    • 57149127991 scopus 로고    scopus 로고
    • Resorcylic acid lactones as new lead structures for kinase inhibition
    • Hofmann, T.; Altmann, K.-H. Resorcylic acid lactones as new lead structures for kinase inhibition. C. R. Chim. 2008, 11, 1318-1335.
    • (2008) C. R. Chim , vol.11 , pp. 1318-1335
    • Hofmann, T.1    Altmann, K.-H.2
  • 5
    • 33644920385 scopus 로고    scopus 로고
    • Search for Hsp90 inhibitors with potential anticancer activity: Isolation and SAR studies of radicicol and monocillin I from two plant-associated fungi of the Sonoran desert
    • Turbyville, T. J.; Wijeratne, E. M.; Liu, M. X.; Burns, A. M.; Seliga, C. J.; Luevano, L. A.; David, C. L.; Faeth, S. H.; Whitesell, L.; Gunatilaka, A. A. Search for Hsp90 inhibitors with potential anticancer activity: isolation and SAR studies of radicicol and monocillin I from two plant-associated fungi of the Sonoran desert. J. Nat. Prod. 2006, 69, 178-184.
    • (2006) J. Nat. Prod , vol.69 , pp. 178-184
    • Turbyville, T.J.1    Wijeratne, E.M.2    Liu, M.X.3    Burns, A.M.4    Seliga, C.J.5    Luevano, L.A.6    David, C.L.7    Faeth, S.H.8    Whitesell, L.9    Gunatilaka, A.A.10
  • 6
    • 0037040681 scopus 로고    scopus 로고
    • Aigialomycins A-E, new resorcylic macrolides from the marine mangrove fungus Aigialus parvus
    • Isaka, M.; Suyarnsestakorn, C.; Tanticharoen, M.; Kongsaeree, P.; Thebtaranonth, Y. Aigialomycins A-E, new resorcylic macrolides from the marine mangrove fungus Aigialus parvus. J. Org. Chem. 2002, 67, 1561-1566.
    • (2002) J. Org. Chem , vol.67 , pp. 1561-1566
    • Isaka, M.1    Suyarnsestakorn, C.2    Tanticharoen, M.3    Kongsaeree, P.4    Thebtaranonth, Y.5
  • 8
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J.; Yang, P. L.; Gray, N. S. Targeting cancer with small molecule kinase inhibitors. Nat. Rev. Cancer 2009, 9, 28-39.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 9
    • 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.; Ladbury, J. E.; Piper, P. W.; Pearl, L. H. 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    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 11
    • 18744411808 scopus 로고    scopus 로고
    • Synthesis, and Biological Evaluation of HSP90 Inhibitors Based on Conformational Analysis of Radicicol and Its Analogues
    • Moulin, E.; Zoete, V.; Barluenga, S.; Karplus, M.; Winssinger, N. Design, Synthesis, and Biological Evaluation of HSP90 Inhibitors Based on Conformational Analysis of Radicicol and Its Analogues. 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    Karplus, M.4    Winssinger5    Design, N.6
  • 12
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from Archaea with implications for meiotic recombination
    • Bergerat, A.; de Massy, B.; Gadelle, D.; Varoutas, P. C.; Nicolas, A.; Forterre, P. An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 1997, 386, 414-417.
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1    de Massy, B.2    Gadelle, D.3    Varoutas, P.C.4    Nicolas, A.5    Forterre, P.6
  • 13
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • Dutta, R.; Inouye, M. GHKL, an emergent ATPase/kinase superfamily .Trends Biochem. Sci. 2000, 25, 24-28.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 14
    • 0036073440 scopus 로고    scopus 로고
    • Inhibition of branched-chain alpha-keto acid dehydrogenase kinase and Sln1 yeast histidine kinase by the antifungal antibiotic radicicol
    • Besant, P. G.; Lasker, M. V.; Bui, C. D.; Turck, C. W. Inhibition of branched-chain alpha-keto acid dehydrogenase kinase and Sln1 yeast histidine kinase by the antifungal antibiotic radicicol. Mol. Pharmacol. 2002, 62, 289-296.
    • (2002) Mol. Pharmacol , vol.62 , pp. 289-296
    • Besant, P.G.1    Lasker, M.V.2    Bui, C.D.3    Turck, C.W.4
  • 15
    • 17644388495 scopus 로고    scopus 로고
    • Inhibition of archaeal growth and DNA topoisomerase VI activities by the Hsp90 inhibitor radicicol
    • Gadelle, D.; Bocs, C.; Graille, M.; Forterre, P. Inhibition of archaeal growth and DNA topoisomerase VI activities by the Hsp90 inhibitor radicicol. Nucleic Acids Res. 2005, 33, 2310-2317.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2310-2317
    • Gadelle, D.1    Bocs, C.2    Graille, M.3    Forterre, P.4
  • 16
    • 42749090538 scopus 로고    scopus 로고
    • The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ
    • Guarnieri, M. T.; Zhang, L.; Shen, J.; Zhao, R. The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ. J. Mol. Biol. 2008, 379, 82-93.
    • (2008) J. Mol. Biol , vol.379 , pp. 82-93
    • Guarnieri, M.T.1    Zhang, L.2    Shen, J.3    Zhao, R.4
  • 18
    • 35348890981 scopus 로고    scopus 로고
    • Drugging the cancer chaperone HSP90: Combinatorial therapeutic exploitation of oncogene addiction and tumor stress
    • Workman, P.; Burrows, F.; Neckers, L.; Rosen, N. Drugging the cancer chaperone HSP90: Combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann. N.Y. Acad. Sci. 2007, 1113, 202-216.
    • (2007) Ann. N.Y. Acad. Sci , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 19
    • 14344264703 scopus 로고    scopus 로고
    • Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - an update
    • Neckers, L.; Neckers, K. Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - an update. Expert Opin. Emerg. Drugs 2005, 10, 137-149.
    • (2005) Expert Opin. Emerg. Drugs , vol.10 , pp. 137-149
    • Neckers, L.1    Neckers, K.2
  • 20
    • 62149135294 scopus 로고    scopus 로고
    • Discovery and development of heat shock protein 90 inhibitors
    • Taldone, T.; Sun, W.; Chiosis, G. Discovery and development of heat shock protein 90 inhibitors. Bioorg. Med. Chem. Lett. 2009, 17, 2225-2235.
    • (2009) Bioorg. Med. Chem. Lett , vol.17 , pp. 2225-2235
    • Taldone, T.1    Sun, W.2    Chiosis, G.3
  • 21
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell, L.; Lindquist, S. L. HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 2005, 5, 761-772.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 22
    • 51449093764 scopus 로고    scopus 로고
    • Targeting Hsp90: Small-molecule inhibitors and their clinical development
    • Taldone, T.; Gozman, A.; Maharaj, R.; Chiosis, G. Targeting Hsp90: small-molecule inhibitors and their clinical development. Curr. Opin. Pharmacol. 2008, 8, 370-374.
    • (2008) Curr. Opin. Pharmacol , vol.8 , pp. 370-374
    • Taldone, T.1    Gozman, A.2    Maharaj, R.3    Chiosis, G.4
  • 23
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler, A.; Lurz, R.; Lueder, G.; Priller, J.; Lehrach, H.; Hayer-Hartl, M. K.; Hartl, F. U.; Wanker, E. E. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 2001, 10, 1307-1315.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Lehrach, H.5    Hayer-Hartl, M.K.6    Hartl, F.U.7    Wanker, E.E.8
  • 26
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila
    • Auluck, P. K.; Bonini, N. M. Pharmacological prevention of Parkinson disease in Drosophila. Nat. Med. 2002, 8, 1185-1186.
    • (2002) Nat. Med , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 27
    • 57449113371 scopus 로고    scopus 로고
    • Heat shock protein 90: Translation from cancer to Alzheimer's disease treatment?
    • Luo, W.; Rodina, A.; Chiosis, G. Heat shock protein 90: translation from cancer to Alzheimer's disease treatment? BMC Neurosci. 2008, 9, (Suppl 2), S7.
    • (2008) BMC Neurosci , vol.9 , Issue.SUPPL. 2
    • Luo, W.1    Rodina, A.2    Chiosis, G.3
  • 28
    • 33846471075 scopus 로고    scopus 로고
    • Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    • Geller, R.; Vignuzzi, M.; Andino, R.; Frydman, J. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 2007, 21, 195-205.
    • (2007) Genes Dev , vol.21 , pp. 195-205
    • Geller, R.1    Vignuzzi, M.2    Andino, R.3    Frydman, J.4
  • 30
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
    • Sharma, S. V.; Agatsuma, T.; Nakano, H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene 1998, 16, 2639-2645.
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 31
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the Nterminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte, T. W.; Akinaga, S.; Soga, S.; Sullivan, W.; Stensgard, B.; Toft, D.; Neckers, L. M. Antibiotic radicicol binds to the Nterminal 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    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 32
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • Neckers, L.; Schulte, T. W.; Mimnaugh, E. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest. New Drugs 1999, 17, 361-373.
    • (1999) Invest. New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 33
    • 28144440479 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors. A text book example of medicinal chemistry
    • Janin, Y. L. Heat shock protein 90 inhibitors. A text book example of medicinal chemistry. J. Med. Chem. 2005, 48, 7503-7512.
    • (2005) J. Med. Chem , vol.48 , pp. 7503-7512
    • Janin, Y.L.1
  • 34
    • 84882527526 scopus 로고    scopus 로고
    • Sharp, S. Y.; Jones, K.; Workman, P. HSP90 inhibitors: targeting the cancer chaperone for combinatorial blockade of oncogenic pathways. Cancer Drug Des. Disc. 2008, 305-335.
    • Sharp, S. Y.; Jones, K.; Workman, P. HSP90 inhibitors: targeting the cancer chaperone for combinatorial blockade of oncogenic pathways. Cancer Drug Des. Disc. 2008, 305-335.
  • 35
    • 38849117688 scopus 로고    scopus 로고
    • Discovery and development of purine-scaffold Hsp90 inhibitors
    • Chiosis, G.; Kang, Y.; Sun, W. Discovery and development of purine-scaffold Hsp90 inhibitors. Expert Opin. Drug Discov. 2008, 3, 99-114.
    • (2008) Expert Opin. Drug Discov , vol.3 , pp. 99-114
    • Chiosis, G.1    Kang, Y.2    Sun, W.3
  • 36
    • 34248166042 scopus 로고    scopus 로고
    • Sharp, S. Y.; Prodromou, C.; Boxall, K.; Powers, M. V.; Holmes, J. L.; Box, G.; Matthews, T. P.; Cheung, K.-M. J.; Kalusa, A.; James, K.; Hayes, A.; Hardcastle, A.; Dymock, B.; Brough, P. A.; Barril, X.; Cansfield, J. E.; Wright, L.; Surgenor, A.; Foloppe, N.; Hubbard, R. E.; Aherne, W.; Pearl, L.; Jones, K.; McDonald, E.; Raynaud, F.; Eccles, S.; Drysdale, M.; Workman, P. Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic potent resorcinylic pyrazole/isoxazole amide analogues. Mol. Cancer Ther. 2007, 6, 1198-1211.
    • Sharp, S. Y.; Prodromou, C.; Boxall, K.; Powers, M. V.; Holmes, J. L.; Box, G.; Matthews, T. P.; Cheung, K.-M. J.; Kalusa, A.; James, K.; Hayes, A.; Hardcastle, A.; Dymock, B.; Brough, P. A.; Barril, X.; Cansfield, J. E.; Wright, L.; Surgenor, A.; Foloppe, N.; Hubbard, R. E.; Aherne, W.; Pearl, L.; Jones, K.; McDonald, E.; Raynaud, F.; Eccles, S.; Drysdale, M.; Workman, P. Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic potent resorcinylic pyrazole/isoxazole amide analogues. Mol. Cancer Ther. 2007, 6, 1198-1211.
  • 38
    • 42349084306 scopus 로고    scopus 로고
    • Eccles, S. A.; Massey, A.; Raynaud, F. I.; Sharp, S. Y.; Box, G.; Valenti, M.; Patterson, L.; de Haven Brandon, A.; Gowan, S.; Boxall, F.; Aherne, W.; Rowlands, M.; Hayes, A.; Martins, V.; Urban, F.; Boxall, K.; Prodromou, C.; Pearl, L.; James, K.; Matthews, T. P.; Cheung, K.-M.; Kalusa, A.; Jones, K.; McDonald, E.; Barril, X.; Brough, P. A.; Cansfield, J. E.; Dymock, B.; Drysdale, M. J.; Finch, H.; Howes, R.; Hubbard, R. E.; Surgenor, A.; Webb, P.; Wood, M.; Wright, L.; Workman, P. NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis. Cancer Res. 2008, 68, 2850-2860.
    • Eccles, S. A.; Massey, A.; Raynaud, F. I.; Sharp, S. Y.; Box, G.; Valenti, M.; Patterson, L.; de Haven Brandon, A.; Gowan, S.; Boxall, F.; Aherne, W.; Rowlands, M.; Hayes, A.; Martins, V.; Urban, F.; Boxall, K.; Prodromou, C.; Pearl, L.; James, K.; Matthews, T. P.; Cheung, K.-M.; Kalusa, A.; Jones, K.; McDonald, E.; Barril, X.; Brough, P. A.; Cansfield, J. E.; Dymock, B.; Drysdale, M. J.; Finch, H.; Howes, R.; Hubbard, R. E.; Surgenor, A.; Webb, P.; Wood, M.; Wright, L.; Workman, P. NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis. Cancer Res. 2008, 68, 2850-2860.
  • 39
    • 67650741952 scopus 로고    scopus 로고
    • Huang, K. H.; Veal, J. M.; Fadden, R. P.; Rice, J. W.; Eaves, J.; Strachan, J. P.; Barabasz, A. F.; Foley, B. E.; Barta, T. E.; Ma, W.; Silinski, M. A.; Hu, M.; Partridge, J. M.; Scott, A.; DuBois, L. G.; Freed, T.; Steed, P. M.; Ommen, A. J.; Smith, E. D.; Hughes, P. F.; Woodward, A. R.; Hanson, G. J.; McCall, W. S.; Markworth, C. J.; Hinkley, L.; Jenks, M.; Geng, L.; Lewis, M.; Otto, J.; Pronk, B.; Verleysen, K.; Hall, S. E. Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents. J. Med. Chem. 2009, 52, 4288-4305.
    • Huang, K. H.; Veal, J. M.; Fadden, R. P.; Rice, J. W.; Eaves, J.; Strachan, J. P.; Barabasz, A. F.; Foley, B. E.; Barta, T. E.; Ma, W.; Silinski, M. A.; Hu, M.; Partridge, J. M.; Scott, A.; DuBois, L. G.; Freed, T.; Steed, P. M.; Ommen, A. J.; Smith, E. D.; Hughes, P. F.; Woodward, A. R.; Hanson, G. J.; McCall, W. S.; Markworth, C. J.; Hinkley, L.; Jenks, M.; Geng, L.; Lewis, M.; Otto, J.; Pronk, B.; Verleysen, K.; Hall, S. E. Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents. J. Med. Chem. 2009, 52, 4288-4305.
  • 40
    • 3242722132 scopus 로고    scopus 로고
    • A time-resolved fluorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors
    • Zhou, V.; Han, S.; Brinker, A.; Klock, H.; Caldwell, J.; Gu, X. J. A time-resolved fluorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors. Anal. Biochem. 2004, 331, 349-357.
    • (2004) Anal. Biochem , vol.331 , pp. 349-357
    • Zhou, V.1    Han, S.2    Brinker, A.3    Klock, H.4    Caldwell, J.5    Gu, X.J.6
  • 42
    • 16644376293 scopus 로고    scopus 로고
    • Development of a fluorescence polarization assay for the molecular chaperone Hsp90
    • Kim, J.; Felts, S.; Llauger, L.; He, H.; Huezo, H.; Rosen, N.; Chiosis, G. Development of a fluorescence polarization assay for the molecular chaperone Hsp90. J. Biomol. Screen. 2004, 9, 375-381.
    • (2004) J. Biomol. Screen , vol.9 , pp. 375-381
    • Kim, J.1    Felts, S.2    Llauger, L.3    He, H.4    Huezo, H.5    Rosen, N.6    Chiosis, G.7
  • 43
    • 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.; Pearl, L. H.; Workman, P.; Aherne, W. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal. Biochem. 2004, 327, 176-183.
    • (2004) Anal. Biochem , vol.327 , pp. 176-183
    • Rowlands, M.G.1    Newbatt, Y.M.2    Prodromou, C.3    Pearl, L.H.4    Workman, P.5    Aherne, W.6
  • 44
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • Xu, W.; Mimnaugh, E.; Rosser, M. F.; Nicchitta, C.; Marcu, M.; Yarden, Y.; Neckers, L. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 2001, 276, 3702-3708.
    • (2001) J. Biol. Chem , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3    Nicchitta, C.4    Marcu, M.5    Yarden, Y.6    Neckers, L.7
  • 45
    • 34250790717 scopus 로고    scopus 로고
    • Polyketides, proteins and genes in fungi: Programmed nano-machines begin to reveal their secrets
    • Cox, R. J. Polyketides, proteins and genes in fungi: programmed nano-machines begin to reveal their secrets. Org. Biomol. Chem. 2007, 5, 2010-2026.
    • (2007) Org. Biomol. Chem , vol.5 , pp. 2010-2026
    • Cox, R.J.1
  • 46
    • 44049091848 scopus 로고    scopus 로고
    • A polyketide macrolactone synthase from the filamentous fungus Gibberella zeae
    • Zhou, H.; Zhan, J.; Watanabe, K.; Xie, X.; Tang, Y. A polyketide macrolactone synthase from the filamentous fungus Gibberella zeae. Proc. Natl. Acad. Sci. USA 2008, 105, 6249-6254.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6249-6254
    • Zhou, H.1    Zhan, J.2    Watanabe, K.3    Xie, X.4    Tang, Y.5
  • 47
    • 57649230837 scopus 로고    scopus 로고
    • Functional characterization of the biosynthesis of radicicol, an Hsp90 inhibitor resorcylic acid lactone from chaetomium chiversii
    • Wang, S.; Xu, Y.; Maine, E. A.; Wijeratne, E. M. K.; Espinosa-Artiles, P.; Gunatilaka, A. A. L.; Molnar, I. Functional characterization of the biosynthesis of radicicol, an Hsp90 inhibitor resorcylic acid lactone from chaetomium chiversii. Chem. Biol. 2008, 15, 1328-1338.
    • (2008) Chem. Biol , vol.15 , pp. 1328-1338
    • Wang, S.1    Xu, Y.2    Maine, E.A.3    Wijeratne, E.M.K.4    Espinosa-Artiles, P.5    Gunatilaka, A.A.L.6    Molnar, I.7
  • 48
    • 48749109006 scopus 로고    scopus 로고
    • Biomimetic synthesis of resorcylate natural products utilizing late stage aromatization: Concise total syntheses of the marine antifungal agents 15G256iota and 15G256beta
    • Navarro, I.; Basset, J. F.; Hebbe, S.; Major, S. M.; Werner, T.; Howsham, C.; Brackow, J.; Barrett, A. G. Biomimetic synthesis of resorcylate natural products utilizing late stage aromatization: concise total syntheses of the marine antifungal agents 15G256iota and 15G256beta. J. Am. Chem. Soc. 2008, 130, 10293-10298.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 10293-10298
    • Navarro, I.1    Basset, J.F.2    Hebbe, S.3    Major, S.M.4    Werner, T.5    Howsham, C.6    Brackow, J.7    Barrett, A.G.8
  • 49
    • 56949084988 scopus 로고    scopus 로고
    • The search for a hair-growth stimulant: New radicicol analogues as WNT-5A expression inhibitors from Pochonia chlamydosporia var. chlamydosporia
    • Shinonaga, H.; Kawamura, Y.; Ikeda, A.; Aoki, M.; Sakai, N.; Fujimoto, N.; Kawashima, A. The search for a hair-growth stimulant: new radicicol analogues as WNT-5A expression inhibitors from Pochonia chlamydosporia var. chlamydosporia. Tetrahedron Lett. 2009, 50, 108-110.
    • (2009) Tetrahedron Lett , vol.50 , pp. 108-110
    • Shinonaga, H.1    Kawamura, Y.2    Ikeda, A.3    Aoki, M.4    Sakai, N.5    Fujimoto, N.6    Kawashima, A.7
  • 50
    • 62549124118 scopus 로고    scopus 로고
    • New radicicol analogs from Pochonia chlamydosporia var. chlamydosporia and their WNT-5A expression inhibitory activities
    • Shinonaga, H.; Kawamura, Y.; Ikeda, A.; Aoki, M.; Sakai, N.; Fujimoto, N.; Kawashima, A. Pochonins K-P: New radicicol analogs from Pochonia chlamydosporia var. chlamydosporia and their WNT-5A expression inhibitory activities. Tetrahedron 2009, 65, 3446-3453.
    • (2009) Tetrahedron , vol.65 , pp. 3446-3453
    • Shinonaga, H.1    Kawamura, Y.2    Ikeda, A.3    Aoki, M.4    Sakai, N.5    Fujimoto, N.6    Kawashima, A.7    Pochonins, K.-P.8
  • 52
    • 34547910622 scopus 로고    scopus 로고
    • Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells
    • Schumacher, J. A.; Crockett, D. K.; Elenitoba-Johnson, K. S.; Lim, M. S. Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells. Proteomics 2007, 7, 2603-2616.
    • (2007) Proteomics , vol.7 , pp. 2603-2616
    • Schumacher, J.A.1    Crockett, D.K.2    Elenitoba-Johnson, K.S.3    Lim, M.S.4
  • 53
    • 0026513918 scopus 로고
    • Convergent stereospecific total synthesis of monocillin I and monorden (or radicicol)
    • Lampilas, M.; Lett, R. Convergent stereospecific total synthesis of monocillin I and monorden (or radicicol). Tetrahedron Lett. 1992, 33, 777-780.
    • (1992) Tetrahedron Lett , vol.33 , pp. 777-780
    • Lampilas, M.1    Lett, R.2
  • 54
    • 0037182281 scopus 로고    scopus 로고
    • Improvements of the total synthesis of monocillin I and radicicol via Miyaura-Suzuki couplings
    • Tichkowsky, I.; Lett, R. Improvements of the total synthesis of monocillin I and radicicol via Miyaura-Suzuki couplings. Tetrahedron Lett. 2002, 43, 4003-4007.
    • (2002) Tetrahedron Lett , vol.43 , pp. 4003-4007
    • Tichkowsky, I.1    Lett, R.2
  • 56
    • 24344442417 scopus 로고    scopus 로고
    • Solution- and solid-phase synthesis of radicicol (monorden) and pochonin C
    • Barluenga, S.; Moulin, E.; Lopez, P.; Winssinger, N. Solution- and solid-phase synthesis of radicicol (monorden) and pochonin C. Chem. Eur. J. 2005, 11, 4935-4952.
    • (2005) Chem. Eur. J , vol.11 , pp. 4935-4952
    • Barluenga, S.1    Moulin, E.2    Lopez, P.3    Winssinger, N.4
  • 58
    • 29444460171 scopus 로고    scopus 로고
    • Concise Synthesis of Pochonin A, an HSP90 Inhibitor
    • Moulin, E.; Barluenga, S.; Winssinger, N. Concise Synthesis of Pochonin A, an HSP90 Inhibitor. Org. Lett. 2005, 7, 5637-5639.
    • (2005) Org. Lett , vol.7 , pp. 5637-5639
    • Moulin, E.1    Barluenga, S.2    Winssinger, N.3
  • 61
    • 3042685847 scopus 로고    scopus 로고
    • New efficient synthesis of resorcinylic macrolides via ynolides: Establishment of cycloproparadicicol as synthetically feasible preclinical anticancer agent based on Hsp90 as the target
    • Yang, Z.-Q.; Geng, X.; Solit, D.; Pratilas, C. A.; Rosen, N.; Danishefsky, S. J. New efficient synthesis of resorcinylic macrolides via ynolides: establishment of cycloproparadicicol as synthetically feasible preclinical anticancer agent based on Hsp90 as the target. J. Am. Chem. Soc. 2004, 126, 7881-7889.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 7881-7889
    • Yang, Z.-Q.1    Geng, X.2    Solit, D.3    Pratilas, C.A.4    Rosen, N.5    Danishefsky, S.J.6
  • 64
    • 53849085500 scopus 로고    scopus 로고
    • Efficient synthesis of a novel resorcyclide as anticancer agent based on Hsp90 inhibition
    • Lei, X.; Danishefsky, S. J. Efficient synthesis of a novel resorcyclide as anticancer agent based on Hsp90 inhibition. Adv. Synth. Catal. 2008, 350, 1677-1681.
    • (2008) Adv. Synth. Catal , vol.350 , pp. 1677-1681
    • Lei, X.1    Danishefsky, S.J.2
  • 65
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H. C.; Finn, M. G.; Sharpless, K. B. Click chemistry: diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. Engl. 2001, 40, 2004-2021.
    • (2001) Angew. Chem. Int. Ed. Engl , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 66
    • 33846060714 scopus 로고    scopus 로고
    • Synthesis of a benzolactone collection using click chemistry
    • Ritschel, J.; Sasse, F.; Maier, M. Synthesis of a benzolactone collection using click chemistry. Eur. J. Org. Chem. 2007, 78-87.
    • (2007) Eur. J. Org. Chem , pp. 78-87
    • Ritschel, J.1    Sasse, F.2    Maier, M.3
  • 67
    • 67649380752 scopus 로고    scopus 로고
    • An improved synthesis of resorcylic acid macrolactone inhibitors of Hsp90
    • Day, J. E. H.; Blake, A. J.; Moody, C. J. An improved synthesis of resorcylic acid macrolactone inhibitors of Hsp90. Synlett 2009, 1567-1570.
    • (2009) Synlett , pp. 1567-1570
    • Day, J.E.H.1    Blake, A.J.2    Moody, C.J.3
  • 70
    • 33845302853 scopus 로고    scopus 로고
    • Chiosis, G.; Neckers, L. Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive. ACS Chem. Biol. 2006, 1, 279-284.
    • Chiosis, G.; Neckers, L. Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive. ACS Chem. Biol. 2006, 1, 279-284.
  • 73
    • 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.; Connelly, S.; Roe, S. M.; Prodromou, C.; Slawin, A. M.; Pearl, L. H.; Workman, P.; Moody, C. J. 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    Connelly, S.4    Roe, S.M.5    Prodromou, C.6    Slawin, A.M.7    Pearl, L.H.8    Workman, P.9    Moody, C.J.10
  • 74
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso, A. D.; Solit, D. B.; Munster, P. N.; Rosen, N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 2002, 21, 1159-1166.
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 77
    • 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, 278, 48330-48338.
    • (2003) J. Biol. Chem , vol.278 , pp. 48330-48338
    • Soldano, K.L.1    Jivan, A.2    Nicchitta, C.V.3    Gewirth, D.T.4
  • 78
    • 67349273712 scopus 로고    scopus 로고
    • The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts
    • Spichty, M.; Taly, A., Hagn, F.; Kessler, H.; Barluenga, S.; Winssinger, N.; Karplus, M. The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts. Biophys. Chem. 2009, 143, 111-123.
    • (2009) Biophys. Chem , vol.143 , pp. 111-123
    • Spichty, M.1    Taly, A.2    Hagn, F.3    Kessler, H.4    Barluenga, S.5    Winssinger, N.6    Karplus, M.7
  • 79
    • 74249099855 scopus 로고    scopus 로고
    • personal communication
    • Hagn, F.; Kessler, H. personal communication 2008.
    • (2008)
    • Hagn, F.1    Kessler, H.2
  • 81
    • 33644979098 scopus 로고    scopus 로고
    • Wang, M.; Shen, G.; Blagg, B. S. Radanamycin, a macrocyclic chimera of radicicol and geldanamycin. Bioorg. Med. Chem. Lett. 2006, 16, 2459-2462.
    • Wang, M.; Shen, G.; Blagg, B. S. Radanamycin, a macrocyclic chimera of radicicol and geldanamycin. Bioorg. Med. Chem. Lett. 2006, 16, 2459-2462.
  • 82
    • 33749132153 scopus 로고    scopus 로고
    • Design, synthesis, and structure--activity relationships for chimeric inhibitors of Hsp90
    • Shen, G.; Wang, M.; Welch, T. R.; Blagg, B. S. Design, synthesis, and structure--activity relationships for chimeric inhibitors of Hsp90. J. Org. Chem. 2006, 71, 7618-7631.
    • (2006) J. Org. Chem , vol.71 , pp. 7618-7631
    • Shen, G.1    Wang, M.2    Welch, T.R.3    Blagg, B.S.4
  • 83
    • 20444465254 scopus 로고    scopus 로고
    • Shen, G.; Blagg, B. S. Radester, a novel inhibitor of the Hsp90 protein folding machinery, Org. Lett. 2005, 7, 2157-2160.
    • Shen, G.; Blagg, B. S. Radester, a novel inhibitor of the Hsp90 protein folding machinery, Org. Lett. 2005, 7, 2157-2160.
  • 84
    • 10044237881 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide
    • Clevenger, R. C.; Blagg, B. S. Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide. Org. Lett. 2004, 6, 4459-4462.
    • (2004) Org. Lett , vol.6 , pp. 4459-4462
    • Clevenger, R.C.1    Blagg, B.S.2
  • 85
    • 67649586399 scopus 로고    scopus 로고
    • Hadden, M. K.; Blagg, B. S. J. Synthesis and evaluation of radamide analogues, a chimera of radicicol and geldanamycin. J. Org. Chem. 2009, 74, 4697-4704.
    • Hadden, M. K.; Blagg, B. S. J. Synthesis and evaluation of radamide analogues, a chimera of radicicol and geldanamycin. J. Org. Chem. 2009, 74, 4697-4704.
  • 86
    • 67349154388 scopus 로고    scopus 로고
    • Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: Implications for paralog-specific drug design
    • Immormino, R. M.; Metzger, L. E.; Reardon, P. N.; Dollins, D. E.; Blagg, B. S. J.; Gewirth, D. T. Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. J. Mol. Biol. 2009, 388, 1033-1042.
    • (2009) J. Mol. Biol , vol.388 , pp. 1033-1042
    • Immormino, R.M.1    Metzger, L.E.2    Reardon, P.N.3    Dollins, D.E.4    Blagg, B.S.J.5    Gewirth, D.T.6
  • 89
    • 0037108448 scopus 로고    scopus 로고
    • BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90
    • Gorre, M. E.; Ellwood-Yen, K.; Chiosis, G.; Rosen, N.; Sawyers, C. L. BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90. Blood 2002, 100, 3041-3044.
    • (2002) Blood , vol.100 , pp. 3041-3044
    • Gorre, M.E.1    Ellwood-Yen, K.2    Chiosis, G.3    Rosen, N.4    Sawyers, C.L.5
  • 90
    • 34547137932 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 prolongs survival of mice with BCR-ABL-T315I-induced leukemia and suppresses leukemic stem cells
    • Peng, C.; Brain, J.; Hu, Y.; Goodrich, A.; Kong, L.; Grayzel, D.; Pak, R.; Read, M.; Li, S. Inhibition of heat shock protein 90 prolongs survival of mice with BCR-ABL-T315I-induced leukemia and suppresses leukemic stem cells. Blood 2007, 110, 678-685.
    • (2007) Blood , vol.110 , pp. 678-685
    • Peng, C.1    Brain, J.2    Hu, Y.3    Goodrich, A.4    Kong, L.5    Grayzel, D.6    Pak, R.7    Read, M.8    Li, S.9
  • 91
    • 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
  • 92
    • 34250162144 scopus 로고    scopus 로고
    • Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells
    • Xu, W.; Neckers, L. Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells. Clin. Cancer Res. 2007, 13, 1625-1629.
    • (2007) Clin. Cancer Res , vol.13 , pp. 1625-1629
    • Xu, W.1    Neckers, L.2
  • 93
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol
    • Solit, D. B.; Basso, A. D.; Olshen, A. B.; Scher, H. I.; Rosen, N. Inhibition of heat shock protein 90 function down-regulates 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    Scher, H.I.4    Rosen, N.5
  • 95
    • 70350548428 scopus 로고    scopus 로고
    • 17 AAG for HSP90 inhibition in cancer - from bench to bedside
    • Usmani, S. Z.; Bona, R.; Li, Z. 17 AAG for HSP90 inhibition in cancer - from bench to bedside. Curr. Mol. Med. 2009, 9, 654-664.
    • (2009) Curr. Mol. Med , vol.9 , pp. 654-664
    • Usmani, S.Z.1    Bona, R.2    Li, Z.3
  • 96
    • 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.; Myers, T. G.; Workman, P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J. Natl. Cancer Inst. 1999, 91, 1940-1949.
    • (1999) J. Natl. Cancer Inst , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 97
    • 62449226171 scopus 로고    scopus 로고
    • Acquired resistance to 17-allylamino-17- demethoxygeldanamycin (17-AAG, tanespimycin) in glioblastoma cells
    • Gaspar, N.; Sharp, S. Y.; Pacey, S.; Jones, C.; Walton, M.; Vassal, G.; Eccles, S.; Pearson, A.; Workman, P. Acquired resistance to 17-allylamino-17- demethoxygeldanamycin (17-AAG, tanespimycin) in glioblastoma cells. Cancer Res. 2009, 69, 1966-1975.
    • (2009) Cancer Res , vol.69 , pp. 1966-1975
    • Gaspar, N.1    Sharp, S.Y.2    Pacey, S.3    Jones, C.4    Walton, M.5    Vassal, G.6    Eccles, S.7    Pearson, A.8    Workman, P.9
  • 98
    • 65649143827 scopus 로고    scopus 로고
    • Prodromou, C.; Nuttall, J. M.; Millson, S. H.; Roe, S. M.; Sim, T.-S.; Tan, D.; Workman, P.; Pearl, L. H.; Piper, P. W. Structural Basis of the Radicicol Resistance Displayed by a Fungal Hsp90. ACS Chem. Biol. 2009, 4, 289-297.
    • Prodromou, C.; Nuttall, J. M.; Millson, S. H.; Roe, S. M.; Sim, T.-S.; Tan, D.; Workman, P.; Pearl, L. H.; Piper, P. W. Structural Basis of the Radicicol Resistance Displayed by a Fungal Hsp90. ACS Chem. Biol. 2009, 4, 289-297.
  • 100
    • 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
    • Munster, P. N.; 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. Clin. Cancer Res. 2001, 7, 2228-2236.
    • (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


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