메뉴 건너뛰기




Volumn 4, Issue 11, 2013, Pages 1042-1047

Analogues of the allosteric heat shock protein 70 (Hsp70) inhibitor, MKT-077, as anti-cancer agents

Author keywords

Breast cancer; Hsp90; mortalin; p53; proteostasis

Indexed keywords

1 ETHYL 2 [[3 ETHYL 5 (3 METHYLBENZOTHIAZOLIN 2 YLIDENE) 4 OXOTHIAZOLIDIN 2 YLIDENE]METHYL]PYRIDINIUM CHLORIDE; HEAT SHOCK PROTEIN 70;

EID: 84887886374     PISSN: None     EISSN: 19485875     Source Type: Journal    
DOI: 10.1021/ml400204n     Document Type: Article
Times cited : (128)

References (28)
  • 1
    • 77953734857 scopus 로고    scopus 로고
    • Heat Shock Protein 70 (Hsp70) as an emerging drug target
    • Evans, C. G.; Chang, L.; Gestwicki, J. E. Heat Shock Protein 70 (Hsp70) as an emerging drug target J. Med. Chem. 2010, 53, 4585-4602
    • (2010) J. Med. Chem. , vol.53 , pp. 4585-4602
    • Evans, C.G.1    Chang, L.2    Gestwicki, J.E.3
  • 2
    • 84865618692 scopus 로고    scopus 로고
    • Inhibition of HSP70: A challenging anti-cancer strategy
    • Goloudina, A. R.; Demidov, O. N.; Garrido, C. Inhibition of HSP70: A challenging anti-cancer strategy Cancer Lett. 2012, 325, 117-124
    • (2012) Cancer Lett. , vol.325 , pp. 117-124
    • Goloudina, A.R.1    Demidov, O.N.2    Garrido, C.3
  • 3
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga, H. H.; Craig, E. A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity Nat. Rev. Mol. Cell Biol. 2010, 11, 579-592
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 4
    • 34447530408 scopus 로고    scopus 로고
    • Molecular chaperones regulate p53 and suppress senescence programs
    • Sherman, M.; Gabai, V.; O'Callaghan, C.; Yaglom, J. Molecular chaperones regulate p53 and suppress senescence programs FEBS Lett. 2007, 581, 3711-3715
    • (2007) FEBS Lett. , vol.581 , pp. 3711-3715
    • Sherman, M.1    Gabai, V.2    O'Callaghan, C.3    Yaglom, J.4
  • 5
    • 18844378888 scopus 로고    scopus 로고
    • Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents
    • Gabai, V. L.; Budagova, K. R.; Sherman, M. Y. Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents Oncogene 2005, 24, 3328-3338
    • (2005) Oncogene , vol.24 , pp. 3328-3338
    • Gabai, V.L.1    Budagova, K.R.2    Sherman, M.Y.3
  • 6
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications
    • Ciocca, D. R.; Calderwood, S. K. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications Cell Stress Chaperones 2005, 10, 86-103
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 7
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis
    • Powers, M. V.; Clarke, P. A.; Workman, P. Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis Cancer Cell 2008, 14, 250-262
    • (2008) Cancer Cell , vol.14 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 8
    • 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.; Pranpat, M.; Fiskus, W.; Boyapalle, S.; Kumaraswamy, S.; Balasis, M.; Greedy, B.; Armitage, E. S. M.; Lawrence, N.; Bhalla, K. 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, 10536-10544
    • (2005) Cancer Res. , vol.65 , pp. 10536-10544
    • Guo, F.1    Rocha, K.2    Bali, P.3    Pranpat, M.4    Fiskus, W.5    Boyapalle, S.6    Kumaraswamy, S.7    Balasis, M.8    Greedy, B.9    Armitage, E.S.M.10    Lawrence, N.11    Bhalla, K.12
  • 9
    • 4644234197 scopus 로고    scopus 로고
    • Induction of heat shock protein 70 (Hsp70) by proteasome inhibitor MG 132 protects articular chondrocytes from cellular death in vitro and in vivo
    • Grossin, L.; Etienne, S.; Gaborit, N.; Pinzano, A.; Cournil-Henrionnet, C.; Gerard, C.; Payan, E.; Netter, P.; Terlain, B.; Gillet, P. Induction of heat shock protein 70 (Hsp70) by proteasome inhibitor MG 132 protects articular chondrocytes from cellular death in vitro and in vivo Biorheology 2004, 41, 521-534
    • (2004) Biorheology , vol.41 , pp. 521-534
    • Grossin, L.1    Etienne, S.2    Gaborit, N.3    Pinzano, A.4    Cournil-Henrionnet, C.5    Gerard, C.6    Payan, E.7    Netter, P.8    Terlain, B.9    Gillet, P.10
  • 10
    • 0031443856 scopus 로고    scopus 로고
    • Induction of PBP74/mortalin/Grp75, a member of the hsp70 family, by low doses of ionizing radiation: A possible role in induced radioresistance
    • Sadekova, S.; Lehnert, S.; Chow, T. Y. K. Induction of PBP74/mortalin/Grp75, a member of the hsp70 family, by low doses of ionizing radiation: a possible role in induced radioresistance Int. J. Radiat. Biol. 1997, 72, 653-660
    • (1997) Int. J. Radiat. Biol. , vol.72 , pp. 653-660
    • Sadekova, S.1    Lehnert, S.2    Chow, T.Y.K.3
  • 11
  • 12
    • 0030064081 scopus 로고    scopus 로고
    • MKT-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation
    • Koya, K.; Li, Y.; Wang, H.; Ukai, T.; Tatsuta, N.; Kawakami, M.; Shishido, T.; Chen, L. B. MKT-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation Cancer Res. 1996, 56, 538-543
    • (1996) Cancer Res. , vol.56 , pp. 538-543
    • Koya, K.1    Li, Y.2    Wang, H.3    Ukai, T.4    Tatsuta, N.5    Kawakami, M.6    Shishido, T.7    Chen, L.B.8
  • 13
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • Wadhwa, R.; Sugihara, T.; Yoshida, A.; Nomura, H.; Reddel, R. R.; Simpson, R.; Maruta, H.; Kaul, S. C. Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function Cancer Res. 2000, 60, 6818-6821
    • (2000) Cancer Res. , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5    Simpson, R.6    Maruta, H.7    Kaul, S.C.8
  • 16
  • 18
    • 0036682377 scopus 로고    scopus 로고
    • Rhodacyanine dye MKT-077 inhibits in vitro telomerase assay but has no detectable effects on telomerase activity in vivo
    • Wadhwa, R.; Colgin, L.; Yaguchi, T.; Taira, K.; Reddel, R. R.; Kaul, S. C. Rhodacyanine dye MKT-077 inhibits in vitro telomerase assay but has no detectable effects on telomerase activity in vivo Cancer Res. 2002, 62, 4434-4438
    • (2002) Cancer Res. , vol.62 , pp. 4434-4438
    • Wadhwa, R.1    Colgin, L.2    Yaguchi, T.3    Taira, K.4    Reddel, R.R.5    Kaul, S.C.6
  • 20
    • 77955661115 scopus 로고    scopus 로고
    • Hsp90 inhibition: Elimination of shock and stress
    • Duerfeldt, A. S.; Blagg, B. S. J. Hsp90 inhibition: elimination of shock and stress Bioorg. Med. Chem. Lett. 2010, 20, 4983-4987
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 4983-4987
    • Duerfeldt, A.S.1    Blagg, B.S.J.2
  • 22
  • 23
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays J. Immunol. Methods 1983, 65, 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 28
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • Bertelsen, E. B.; Chang, L.; Gestwicki, J. E.; Zuiderweg, E. R. P. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 8471-8476
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.