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Volumn , Issue , 2009, Pages 83-97

Assay Development for Heat Shock Proteins

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EID: 77749326874     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420070514-10     Document Type: Chapter
Times cited : (2)

References (29)
  • 1
    • 0036836678 scopus 로고    scopus 로고
    • Halohydrin and oxime derivatives of radicicol: Synthesis and antitumor activities
    • Agatsuma, T. et al. 2002. Halohydrin and oxime derivatives of radicicol: synthesis and antitumor activities. Bioorg. Med. Chem. 10, 3445-3454.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3445-3454
    • Agatsuma, T.1
  • 2
    • 0032555184 scopus 로고    scopus 로고
    • Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli
    • Brune, M. et al. 1998. Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli. Biochemistry 37, 10370-10380.
    • (1998) Biochemistry , vol.37 , pp. 10370-10380
    • Brune, M.1
  • 3
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG: Low target binding affinity and potent cell activity: Finding an explanation
    • Chiosis, G., Huezo, H. et al. 2003. 17AAG: low target binding affinity and potent cell activity: finding an explanation. Mol. Cancer Ther. 2, 123-129.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 123-129
    • Chiosis, G.1    Huezo, H.2
  • 4
    • 0141485327 scopus 로고    scopus 로고
    • Development of purine-scaffold small molecule inhibitors of Hsp90
    • Chiosis, G., Lucas, B. et al. 2003. Development of purine-scaffold small molecule inhibitors of Hsp90. Curr. Cancer Drug Targets 3, 371-376.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 371-376
    • Chiosis, G.1    Lucas, B.2
  • 5
    • 35148849219 scopus 로고    scopus 로고
    • High-throughput screening fluorescence polarization assay for tumor-specific Hsp90
    • Du, Y. et al. 2007. High-throughput screening fluorescence polarization assay for tumor-specific Hsp90. J. Biomol. Screen. 12, 915-924.
    • (2007) J. Biomol. Screen. , vol.12 , pp. 915-924
    • Du, Y.1
  • 6
    • 0344270928 scopus 로고    scopus 로고
    • Regulation of survivin function by Hsp90
    • Fortugno, P. et al. 2003. Regulation of survivin function by Hsp90. Proc. Natl. Acad. Sci. USA 100, 13791-13796.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13791-13796
    • Fortugno, P.1
  • 7
    • 0042885973 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex as a novel target for cancer therapy
    • Goetz, M.P. et al. 2003. The Hsp90 chaperone complex as a novel target for cancer therapy. Ann. Oncol. 14, 1169-1176.
    • (2003) Ann. Oncol. , vol.14 , pp. 1169-1176
    • Goetz, M.P.1
  • 8
    • 33644665083 scopus 로고    scopus 로고
    • A fluorescence polarization assay for inhibitors of Hsp90
    • Howes, R. et al. 2006. A fluorescence polarization assay for inhibitors of Hsp90. Anal. Biochem. 350, 202-213.
    • (2006) Anal. Biochem. , vol.350 , pp. 202-213
    • Howes, R.1
  • 9
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • Kamal, A., M.F. Boehm, and F.J. Burrows. 2004. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol. Med. 10, 283-290.
    • (2004) Trends Mol. Med. , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 10
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal, A. et al. 2003. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425, 407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 11
    • 16644376293 scopus 로고    scopus 로고
    • Development of a fluorescence polarization assay for the molecular chaperone Hsp90
    • Kim, J. et al. 2004. Development of a fluorescence polarization assay for the molecular chaperone Hsp90. J. Biomol. Screen. 9, 375-381.
    • (2004) J. Biomol. Screen. , vol.9 , pp. 375-381
    • Kim, J.1
  • 12
    • 0027081145 scopus 로고
    • Potent and specific inhibition of p60v-src protein kinase both in vivo and in vitro by radicicol
    • Kwon, H.J. et al. 1992. Potent and specific inhibition of p60v-src protein kinase both in vivo and in vitro by radicicol. Cancer Res. 52, 6926-6930.
    • (1992) Cancer Res. , vol.52 , pp. 6926-6930
    • Kwon, H.J.1
  • 13
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • Marcu, M.G. et al. 2000. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 275, 37181-37186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1
  • 14
    • 33646345860 scopus 로고    scopus 로고
    • Dihydroquinone ansamycins: Toward resolving the conflict between low in vitro affinity and high cellular potency of geldanamycin derivatives
    • Maroney, A.C. et al. 2006. Dihydroquinone ansamycins: toward resolving the conflict between low in vitro affinity and high cellular potency of geldanamycin derivatives. Biochemistry 45, 5678-5685.
    • (2006) Biochemistry , vol.45 , pp. 5678-5685
    • Maroney, A.C.1
  • 15
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human hsp90 by a client protein
    • McLaughlin, S.H., H.W. Smith, and S.E. Jackson. 2002. Stimulation of the weak ATPase activity of human hsp90 by a client protein. J. Mol. Biol. 315, 787-798.
    • (2002) J. Mol. Biol. , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 16
    • 0036510722 scopus 로고    scopus 로고
    • Regulation of heat shock protein 90 ATPase activity by sequences in the carboxyl terminus
    • Owen, B.A. et al. 2002. Regulation of heat shock protein 90 ATPase activity by sequences in the carboxyl terminus. J. Biol. Chem. 277, 7086-7091.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7086-7091
    • Owen, B.A.1
  • 17
    • 85099486499 scopus 로고    scopus 로고
    • Hsp90 inhibitors in the clinic
    • Pacey, S. et al. 2006. Hsp90 inhibitors in the clinic. Handb. Exp. Pharmacol. 172, 331-358.
    • (2006) Handb. Exp. Pharmacol. , vol.172 , pp. 331-358
    • Pacey, S.1
  • 18
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATPase activity of hsp90 by the stress-regulated co-chaperone aha1
    • Panaretou, B. et al. 2002. Activation of the ATPase activity of hsp90 by the stress-regulated co-chaperone aha1. Mol. Cell 10, 1307-1318.
    • (2002) Mol. Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1
  • 19
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37: A chaperone cancer conspiracy
    • Pearl, L.H. 2005. Hsp90 and Cdc37: a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 15, 55-61.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 20
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W.B. and D.O. Toft. 2003. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. 228, 111-133.
    • (2003) Exp. Biol. Med. , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 21
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
    • Rowlands, M.G. et al. 2004. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal. Biochem. 327, 176-183.
    • (2004) Anal. Biochem. , vol.327 , pp. 176-183
    • Rowlands, M.G.1
  • 22
    • 0141596326 scopus 로고    scopus 로고
    • Clinical development of 17-allylamino, 17-demethoxygeldanamycin
    • Sausville, E.A., J.E. Tomaszewski, and P. Ivy. 2003. Clinical development of 17-allylamino, 17-demethoxygeldanamycin. Curr. Cancer Drug Targets 3, 377-383.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 377-383
    • Sausville, E.A.1    Tomaszewski, J.E.2    Ivy, P.3
  • 23
    • 0348111450 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of GRP94: Basis for ligand specificity and regulation
    • Soldano, K.L. et al. 2003. Structure of the N-terminal domain of GRP94: basis for ligand specificity and regulation. J. Biol. Chem. 278, 48330-48338.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48330-48338
    • Soldano, K.L.1
  • 24
    • 1642268986 scopus 로고    scopus 로고
    • Hsp90 isoforms: Functions, expression and clinical importance
    • Sreedhar, A.S. et al. 2004. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 562, 11-15.
    • (2004) FEBS Lett. , vol.562 , pp. 11-15
    • Sreedhar, A.S.1
  • 25
    • 2342516893 scopus 로고    scopus 로고
    • Survivin: Apoptosis inhibitor and its regulation by Hsp90
    • Suriawinata, A. 2004. Survivin: apoptosis inhibitor and its regulation by Hsp90. Lab. Invest. 84, 395-403.
    • (2004) Lab. Invest. , vol.84 , pp. 395-403
    • Suriawinata, A.1
  • 26
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein 90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L. et al. 1994. Inhibition of heat shock protein 90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91, 8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1
  • 27
    • 1142273472 scopus 로고    scopus 로고
    • Altered states: Selectively drugging the Hsp90 cancer chaperone
    • Workman, P. 2004. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol. Med. 10, 47-51.
    • (2004) Trends Mol. Med. , vol.10 , pp. 47-51
    • Workman, P.1
  • 28
    • 35348890981 scopus 로고    scopus 로고
    • Drugging the cancer chaperone HSP90: Combinatorial therapeutic exploitation of oncogene addiction and tumor stress
    • Workman, P. et al. 2007. Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann. NY Acad. Sci. 1113, 202-216.
    • (2007) Ann. NY Acad. Sci. , vol.1113 , pp. 202-216
    • Workman, P.1
  • 29
    • 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. et al. 2004. 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. 331, 349-357.
    • (2004) Anal. Biochem. , vol.331 , pp. 349-357
    • Zhou, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.