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Volumn 51, Issue 3, 2008, Pages 373-375

Discovery of benzisoxazoles as potent inhibitors of chaperone heat shock protein 90

Author keywords

[No Author keywords available]

Indexed keywords

BENZISOXAZOLE DERIVATIVE; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; ISOXAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 39149136212     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm701385c     Document Type: Article
Times cited : (83)

References (22)
  • 1
    • 33745155113 scopus 로고    scopus 로고
    • Multiple targeted tyrosine kinase inhibition in the clinic: All for one or one for all?
    • de Jonge, M. J.; Verweij, J. Multiple targeted tyrosine kinase inhibition in the clinic: all for one or one for all? Eur. J. Cancer 2006, 42 (10), 1351-1356.
    • (2006) Eur. J. Cancer , vol.42 , Issue.10 , pp. 1351-1356
    • de Jonge, M.J.1    Verweij, J.2
  • 3
    • 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 (11), 1205-1214.
    • (2006) Curr. Top. Med. Chem , vol.6 , Issue.11 , pp. 1205-1214
    • Solit, D.B.1    Rosen, N.2
  • 4
    • 33645975518 scopus 로고    scopus 로고
    • Chaperoning oncogenes: Hsp90 as a target of geldanamycin
    • Neckers, L. Chaperoning oncogenes: Hsp90 as a target of geldanamycin. Handb. Exp. Pharmacol. 2006, (172), 259-277.
    • (2006) Handb. Exp. Pharmacol , vol.172 , pp. 259-277
    • Neckers, L.1
  • 5
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 2001, 70, 603-647.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 6
    • 0037007283 scopus 로고    scopus 로고
    • Molecular chaperones - cellular machines for protein folding
    • Walter, S.; Buchner, J. Molecular chaperones - cellular machines for protein folding. Angew. Chem., Int. Ed. 2002, 41 (7), 1098-1113.
    • (2002) Angew. Chem., Int. Ed , vol.41 , Issue.7 , pp. 1098-1113
    • Walter, S.1    Buchner, J.2
  • 7
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B.; Weissman, J.; Horwich, A. Molecular chaperones and protein quality control. Cell 2006, 125 (3), 443-451.
    • (2006) Cell , vol.125 , Issue.3 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 8
    • 33746705661 scopus 로고    scopus 로고
    • Chaperoning steroid hormone action
    • Picard, D. Chaperoning steroid hormone action. Trends Endocrinol. Metab. 2006, 17 (6), 229-235.
    • (2006) Trends Endocrinol. Metab , vol.17 , Issue.6 , pp. 229-235
    • Picard, D.1
  • 9
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard, D. Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 2002, 59 (10), 1640-1648.
    • (2002) Cell. Mol. Life Sci , vol.59 , Issue.10 , pp. 1640-1648
    • Picard, D.1
  • 10
    • 0141596939 scopus 로고    scopus 로고
    • Structure and functional relationships of Hsp90
    • Prodromou, C.; Pearl, L. H. Structure and functional relationships of Hsp90. Curr. Cancer Drug Targets 2003, 3 (5), 301-323.
    • (2003) Curr. Cancer Drug Targets , vol.3 , Issue.5 , pp. 301-323
    • Prodromou, C.1    Pearl, L.H.2
  • 11
    • 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
  • 12
    • 39149126263 scopus 로고    scopus 로고
    • is provided at the D. Picard lab Web site
    • A comprehensive listing is provided at the D. Picard lab Web site: http://www.picard.ch/downloads/downloads.htm.
    • A comprehensive listing
  • 13
    • 33749507014 scopus 로고    scopus 로고
    • Effectiveness of Hsp90 inhibitors as anti-cancer drugs
    • (a) Xiao, L; Lu, X; Ruden, D. M. Effectiveness of Hsp90 inhibitors as anti-cancer drugs. Mini-Rev. Med. Chem. 2006, 6, 1137-1143.
    • (2006) Mini-Rev. Med. Chem , vol.6 , pp. 1137-1143
    • Xiao, L.1    Lu, X.2    Ruden, D.M.3
  • 14
    • 33746365169 scopus 로고    scopus 로고
    • Discovery and development of purine-scaffold Hsp90 inhibitors
    • (b) Chiosis, G. Discovery and development of purine-scaffold Hsp90 inhibitors. Curr. Top. Med. Chem. 2006, 6, 1183-1191.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1183-1191
    • Chiosis, G.1
  • 15
    • 33746381708 scopus 로고    scopus 로고
    • Geldanamycin, radicicol, and chimeric inhibitors of the Hsp90 N-terminal ATP binding site
    • (c) Hadden, M. K.; Lubbers, D. J.; Blagg, B. S. J. Geldanamycin, radicicol, and chimeric inhibitors of the Hsp90 N-terminal ATP binding site. Curr. Top. Med. Chem. 2006, 6, 1173-1182.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1173-1182
    • Hadden, M.K.1    Lubbers, D.J.2    Blagg, B.S.J.3
  • 17
    • 21244505104 scopus 로고    scopus 로고
    • Dymock, B. W.; Barril, X; Brough, P. A.; Cansfleld, J. E.; Massey, A.; McDonald, E; Hubbard, R. E.; Surgenor, A; Roughley, S. D.; Webb, P; Workman, P; Wright, L; Drysdale, M. J. Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design. J. Med. Chem. 2005, 48, 4212-4215.
    • (e) Dymock, B. W.; Barril, X; Brough, P. A.; Cansfleld, J. E.; Massey, A.; McDonald, E; Hubbard, R. E.; Surgenor, A; Roughley, S. D.; Webb, P; Workman, P; Wright, L; Drysdale, M. J. Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design. J. Med. Chem. 2005, 48, 4212-4215.
  • 19
    • 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. Screening 2004, 9 (5), 375-381.
    • (2004) J. Biomol. Screening , vol.9 , Issue.5 , pp. 375-381
    • Kim, J.1    Felts, S.2    Llauger, L.3    He, H.4    Huezo, H.5    Rosen, N.6    Chiosis, G.7
  • 20
    • 39149132041 scopus 로고    scopus 로고
    • PDB code for 6: 3BM9. PDB code for 13: 3BMY.
    • PDB code for 6: 3BM9. PDB code for 13: 3BMY.
  • 21
    • 4744376265 scopus 로고    scopus 로고
    • Malamas, M. S.; Manas, E. S.; McDevitt, R. E.; Gunawan, I; Xu, Z. B.; Collini, M. D.; Miller, C. P.; Dinh, T; Henderson, R. A.; Keith, J. C., Jr.; Harris, H. A. Design and synthesis of aryl diphenolic azoles as potent and selective estrogen receptor-β ligands. J. Med. Chem. 2004, 47, 5021-5040.
    • Malamas, M. S.; Manas, E. S.; McDevitt, R. E.; Gunawan, I; Xu, Z. B.; Collini, M. D.; Miller, C. P.; Dinh, T; Henderson, R. A.; Keith, J. C., Jr.; Harris, H. A. Design and synthesis of aryl diphenolic azoles as potent and selective estrogen receptor-β ligands. J. Med. Chem. 2004, 47, 5021-5040.
  • 22
    • 39149109535 scopus 로고    scopus 로고
    • The values represent an average of at least three independent determinations unless otherwise mentioned
    • The values represent an average of at least three independent determinations unless otherwise mentioned.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.