메뉴 건너뛰기




Volumn 14, Issue 3, 2009, Pages 273-381

An alphaScreen TM-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction

Author keywords

AlphaScreen ., ; Heat shock protein 90 (Hsp90); High throughput screening (HTS); Hsp organizing protein (HOP); Tetratricopeptide repeat (TPR)

Indexed keywords

HEAT SHOCK PROTEIN 90; PROTEIN INHIBITOR; BIOTIN; CHAPERONE;

EID: 63849342150     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057108330114     Document Type: Article
Times cited : (45)

References (22)
  • 1
    • 34248187981 scopus 로고    scopus 로고
    • Heat shock protein 90: The cancer chaperone
    • Neckers L.: Heat shock protein 90: the cancer chaperone. J Biosci 2007 ; 32: 517-530.
    • (2007) J Biosci , vol.32 , pp. 517-530
    • Neckers, L.1
  • 2
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • Powers MP, Workman P.: Inhibitors of the heat shock response: biology and pharmacology. FEBS Lett 2007 ; 581: 3758-3769.
    • (2007) FEBS Lett , vol.581 , pp. 3758-3769
    • Powers, M.P.1    Workman, P.2
  • 3
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis G., Timaul MN, Lucas B., Munster PN, Zheng, FF, Sepp-Lorenzino L., 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    Munster, P.N.4    Zheng, F.F.5    Sepp-Lorenzino, L.6
  • 4
    • 34147099104 scopus 로고    scopus 로고
    • A duplexed phenotypic screen for the simultaneous detection of inhibitors of the molecular chaperone heat shock protein 90 and modulators of cellular acetylation
    • Hardcastle A., Tomlin P., Norris C., Richards J., Cordwell M., Boxall K., et al. A duplexed phenotypic screen for the simultaneous detection of inhibitors of the molecular chaperone heat shock protein 90 and modulators of cellular acetylation. Mol Cancer Ther 2001 ; 6: 1112-1122.
    • (2001) Mol Cancer Ther , vol.6 , pp. 1112-1122
    • Hardcastle, A.1    Tomlin, P.2    Norris, C.3    Richards, J.4    Cordwell, M.5    Boxall, K.6
  • 5
    • 20044384168 scopus 로고    scopus 로고
    • Phase i trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer
    • Goetz MP, Toft D., Reid J., Ames M., Stensgard B., Safgren S., et al. Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer. J Clin Oncol 2005 ; 23: 1076-1087.
    • (2005) J Clin Oncol , vol.23 , pp. 1076-1087
    • Goetz, M.P.1    Toft, D.2    Reid, J.3    Ames, M.4    Stensgard, B.5    Safgren, S.6
  • 6
    • 34250197902 scopus 로고    scopus 로고
    • Phase i trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer
    • Solit DB, Ivy SP, Kopil C., Sikorski R., Morris MJ, Slovin SF, et al. Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer. Clin Cancer Res 2007 ; 13: 1775-1782.
    • (2007) Clin Cancer Res , vol.13 , pp. 1775-1782
    • Solit, D.B.1    Ivy, S.P.2    Kopil, C.3    Sikorski, R.4    Morris, M.J.5    Slovin, S.F.6
  • 7
    • 34250160933 scopus 로고    scopus 로고
    • Phase i and pharmacodynamic study of 17-(allylamino)-17- demethoxygeldanamycin in adult patients with refractory advanced cancers
    • Ramanathan RK, Egorin MJ, Eiseman JL, Ramalingam S., Friedland D., Agarwala SS, et al. Phase I and pharmacodynamic study of 17-(allylamino)-17- demethoxygeldanamycin in adult patients with refractory advanced cancers. Clin Cancer Res 2007 ; 13: 1769-1774.
    • (2007) Clin Cancer Res , vol.13 , pp. 1769-1774
    • Ramanathan, R.K.1    Egorin, M.J.2    Eiseman, J.L.3    Ramalingam, S.4    Friedland, D.5    Agarwala, S.S.6
  • 8
  • 9
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl LH, Prodromou C., Workman P.: The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J 2008 ; 3: 439-453.
    • (2008) Biochem J , vol.3 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 10
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • Chen S., Smith DF: Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J Biol Chem 1998 ; 273: 35194-35200.
    • (1998) J Biol Chem , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 11
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements of the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Bartunik H., Hartl FU, Moarefi I.: Structure of TPR domain-peptide complexes: critical elements of the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000 ; 101: 199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Bartunik, H.4    Hartl, F.U.5    Moarefi, I.6
  • 12
    • 0037205411 scopus 로고    scopus 로고
    • Ligand discrimination by TPR domains: Relevance and selectivity of EEVD-recognition in Hsp90-HOP-Hsp90 complexes
    • Brinker A., Scheufler C., von der Mulbe F., Fleckenstein B., Herrmann C., Jung G., et al. Ligand discrimination by TPR domains: relevance and selectivity of EEVD-recognition in Hsp90-HOP-Hsp90 complexes. J Biol Chem 2002 ; 277: 19265-19275.
    • (2002) J Biol Chem , vol.277 , pp. 19265-19275
    • Brinker, A.1    Scheufler, C.2    Von Der Mulbe, F.3    Fleckenstein, B.4    Herrmann, C.5    Jung, G.6
  • 13
    • 0029751136 scopus 로고    scopus 로고
    • The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant
    • Chen MS, Silverstein AM, Pratt WB, Chinkers M.: The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant. J Biol Chem 1996 ; 271: 32315-32320.
    • (1996) J Biol Chem , vol.271 , pp. 32315-32320
    • Chen, M.S.1    Silverstein, A.M.2    Pratt, W.B.3    Chinkers, M.4
  • 14
    • 42449136263 scopus 로고    scopus 로고
    • Designed TPR modules as novel anticancer agents
    • Cortajarena AL, Yi F., Regan L.: Designed TPR modules as novel anticancer agents. ACS Chem Biol 2008 ; 3: 161-166.
    • (2008) ACS Chem Biol , vol.3 , pp. 161-166
    • Cortajarena, A.L.1    Yi, F.2    Regan, L.3
  • 15
    • 0028276006 scopus 로고
    • Luminescent oxygen channeling immunoassay: Measurement of particle binding kinetics by chemiluminescence
    • Ullman EF, Kirakossian H., Singh S., Wu ZP, Irvin BR, Pease PS, et al. Luminescent oxygen channeling immunoassay: measurement of particle binding kinetics by chemiluminescence. Proc Natl Acad Sci USA 1994 ; 91: 5426-5430.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5426-5430
    • Ullman, E.F.1    Kirakossian, H.2    Singh, S.3    Wu, Z.P.4    Irvin, B.R.5    Pease, P.S.6
  • 17
    • 33746789921 scopus 로고    scopus 로고
    • Quantitative high-throughput screening: A titration-based approach that efficiently identifies biological activities in large chemical libraries
    • Inglese J., Auld DS, Jadhav A., Johnson RL, Simeonov A., Yasgar A., et al. Quantitative high-throughput screening: a titration-based approach that efficiently identifies biological activities in large chemical libraries. Proc Natl Acad Sci USA 2006 ; 103: 11473-11478.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11473-11478
    • Inglese, J.1    Auld, D.S.2    Jadhav, A.3    Johnson, R.L.4    Simeonov, A.5    Yasgar, A.6
  • 18
    • 33751321865 scopus 로고    scopus 로고
    • A detergent-based assay for the detection of promiscuous inhibitors
    • Feng BY, Shoichet BK: A detergent-based assay for the detection of promiscuous inhibitors. Nat Protocols 2002 ; 1: 550-553.
    • (2002) Nat Protocols , vol.1 , pp. 550-553
    • Feng, B.Y.1    Shoichet, B.K.2
  • 20
    • 63849165949 scopus 로고    scopus 로고
    • A novel class of Hsp90 inhibitors
    • Yi F., Regan L.: A novel class of Hsp90 inhibitors. ACS Chem Biol. In press.
    • ACS Chem Biol
    • Yi, F.1    Regan, L.2
  • 21
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50cdc37
    • Roe SM, Ali MM, Meyer P., Vaughan CK, Panaretou B., Piper PW, et al. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50cdc37. Cell 2004 ; 116: 87-98.
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1    Ali, M.M.2    Meyer, P.3    Vaughan, C.K.4    Panaretou, B.5    Piper, P.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.