메뉴 건너뛰기




Volumn 52, Issue 3, 2010, Pages 235-241

Novel compounds increasing chaperone HSP70 expression and their biological activity

Author keywords

Chaperone; Chaperone inducer; Echinochrorne; Shikonin

Indexed keywords

ECHINOCHROME A; HEAT SHOCK PROTEIN 70; HERBACEOUS AGENT; NAPHTHOQUINONE;

EID: 77952038383     PISSN: 00413771     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (9)

References (26)
  • 1
    • 77952014219 scopus 로고    scopus 로고
    • Russian source
  • 2
    • 77952033160 scopus 로고    scopus 로고
    • Russian source
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgramm quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. 1976. A rapid and sensitive method for quantitation of microgramm quantities of protein utilizing the principle of protein-dye binding. Anal. Boichem. 72 : 248-254.
    • (1976) Anal. Boichem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 4
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., Weissman J., Horwich A. 2006. Molecular chaperones and protein quality control. Cell. 125 : 443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 5
    • 70349507340 scopus 로고    scopus 로고
    • The shock of aging: Molecular chaperones and the heat shock response in longevity and aging - A mini-review
    • Calderwood S. K., Murshid A., Prince T. 2009. The shock of aging: molecular chaperones and the heat shock response in longevity and aging - a mini-review. Gerontology. 55 : 550-558.
    • (2009) Gerontology , vol.55 , pp. 550-558
    • Calderwood, S.K.1    Murshid, A.2    Prince, T.3
  • 6
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C. M. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 : 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 11444271010 scopus 로고    scopus 로고
    • Chaperone-assisted folding of newly synthesized proteins in the cytosol
    • Deuerling E., Bukau B. 2004. Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit. Rev. Biochem. Mol. Biol. 39 : 261-277.
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 261-277
    • Deuerling, E.1    Bukau, B.2
  • 8
  • 9
    • 24044487179 scopus 로고    scopus 로고
    • Ectoine alters subcellular localization of inclusions and reduces apoptotic cell death induced by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch
    • Furusho K., Yoshizawa T., Shoji S. 2005. Ectoine alters subcellular localization of inclusions and reduces apoptotic cell death induced by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch. Neurobiol. Dis. 20 : 170-178.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 170-178
    • Furusho, K.1    Yoshizawa, T.2    Shoji, S.3
  • 10
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F. U., Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295 : 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 11
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • Hsu A. L., Murphy C. T., Kenyon C. 2003. Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science. 300 : 1142-1145.
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 12
    • 63449114950 scopus 로고    scopus 로고
    • Activation of the heat shock response in a primary cellular model of motoneuron neurodegeneration-evidence for neuroprotective and neurotoxic effects
    • Kalmar B., Greensmith L. 2009. Activation of the heat shock response in a primary cellular model of motoneuron neurodegeneration-evidence for neuroprotective and neurotoxic effects. Cell Mol. Biol. Lett. 14 : 319-335.
    • (2009) Cell Mol. Biol. Lett. , vol.14 , pp. 319-335
    • Kalmar, B.1    Greensmith, L.2
  • 13
    • 53149114499 scopus 로고    scopus 로고
    • Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS
    • Kalmar B., Novoselov S., Gray A., Cheetham M. E., Margulis B., Greensmith L. 2008. Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS. J. Neurochem. 107 : 339-350.
    • (2008) J. Neurochem , vol.107 , pp. 339-350
    • Kalmar, B.1    Novoselov, S.2    Gray, A.3    Cheetham, M.E.4    Margulis, B.5    Greensmith, L.6
  • 14
    • 58149229542 scopus 로고    scopus 로고
    • Enhanced recovery from contraction-induced damage in skeletal muscles of old mice following treatment with the heat shock protein inducer 17-(allylamino)-17-demethoxygeldanamycin
    • Kayani A. C., Close G. L., Broome C. S., Jackson M. J., McArdle A. 2008. Enhanced recovery from contraction-induced damage in skeletal muscles of old mice following treatment with the heat shock protein inducer 17-(allylamino)-17-demethoxygeldanamycin. Rejuvenation Res. 11 : 1021-1030.
    • (2008) Rejuvenation Res , vol.11 , pp. 1021-1030
    • Kayani, A.C.1    Close, G.L.2    Broome, C.S.3    Jackson, M.J.4    McArdle, A.5
  • 15
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto R. I. 2008. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Develop. 22 : 1427-1438.
    • (2008) Genes Develop , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 16
    • 64949099855 scopus 로고    scopus 로고
    • Protein homeostasis and aging: Taking care of proteins from the cradle to the grave
    • Morimoto R. I., Cuervo A. M. 2009. Protein homeostasis and aging: taking care of proteins from the cradle to the grave. J. Gerontol. Biol. Sci. Med. Sci. 64 : 167-170.
    • (2009) J. Gerontol. Biol. Sci. Med. Sci. , vol.64 , pp. 167-170
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 17
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases. Molecular aspects
    • Perutz M. F. 1999. Glutamine repeats and neurodegenerative diseases. Molecular aspects. Trend Biochem. Sci. 24 : 58-63.
    • (1999) Trend Biochem. Sci , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 18
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira H., Breuer P., Hayer-Hartl M. K., Hartl F. U. 2002. Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Nat. Acad. Sci. USA. 99 : 16 412-16 418.
    • (2002) Proc. Nat. Acad. Sci. USA , vol.99 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 19
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen H. Y., He J. C., Wang Y., Huang Q. Y., Chen J. F. 2005. Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J. Biol. Chem. 280 : 39 962-39 969.
    • (2005) J. Biol. Chem , vol.280 , pp. 39962-39969
    • Shen, H.Y.1    He, J.C.2    Wang, Y.3    Huang, Q.Y.4    Chen, J.F.5
  • 21
    • 0029094250 scopus 로고
    • Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates
    • Wawrzynow A., Zylicz M. 1995. Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J. Biol. Chem. 270 : 19 300-19 306.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19300-19306
    • Wawrzynow, A.1    Zylicz, M.2
  • 23
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide S. D., Morimoto R. I. 2005. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J. Biol. Chem. 280 : 33 097-33 100.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 24
    • 4344674075 scopus 로고    scopus 로고
    • Role of heat shock proteins during polyglutamine neurodegeneration: Mechanisms and hypothesis
    • Wyttenbach A. 2004. Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis. J. Mol. Neurosci. 23 : 69-96.
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 69-96
    • Wyttenbach, A.1
  • 26
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • Zhou H., Li S. H., Li X. J. 2001. Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J. Biol. Chem. 276 : 48 417-48 424.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.H.2    Li, X.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.