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Volumn 288, Issue 33, 2013, Pages 23633-23638

Heat shock response activation exacerbates inclusion body formation in a cellular model of huntington disease

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR MODEL; HEAT SHOCK RESPONSE; HEAT-SHOCK; HUNTINGTON DISEASE; INCLUSION BODIES; MUTANT HUNTINGTIN; THERAPEUTIC STRATEGY;

EID: 84882386037     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C113.481945     Document Type: Article
Times cited : (44)

References (22)
  • 1
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A., and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease. Nat. Med. 10, (suppl.) S10-S17
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., and Aronin, N. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 5
    • 84874832163 scopus 로고    scopus 로고
    • Protein homeostasis as a therapeutic target for diseases of protein conformation
    • Calamini, B., and Morimoto, R. I. (2012) Protein homeostasis as a therapeutic target for diseases of protein conformation. Curr. Top. Med. Chem. 12, 2623-2640
    • (2012) Curr. Top. Med. Chem. , vol.12 , pp. 2623-2640
    • Calamini, B.1    Morimoto, R.I.2
  • 6
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: Systems biology of proteotoxic stress in aging and disease
    • Morimoto, R. I. (2011) The heat shock response: systems biology of proteotoxic stress in aging and disease. Cold Spring Harbor Symp. Quant. Biol. 76, 91-99
    • (2011) Cold Spring Harbor Symp. Quant. Biol. , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 8
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • Trinklein, N. D., Murray, J. I., Hartman, S. J., Botstein, D., and Myers, R. M. (2004) The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol. Biol. Cell 15, 1254-1261
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 9
    • 77949884097 scopus 로고    scopus 로고
    • Induction of molecular chaperones as a therapeutic strategy for the polyglutamine diseases
    • Nagai, Y., Fujikake, N., Popiel, H. A., and Wada, K. (2010) Induction of molecular chaperones as a therapeutic strategy for the polyglutamine diseases. Curr. Pharm. Biotechnol. 11, 188-197
    • (2010) Curr. Pharm. Biotechnol. , vol.11 , pp. 188-197
    • Nagai, Y.1    Fujikake, N.2    Popiel, H.A.3    Wada, K.4
  • 10
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler, A., Lurz, R., Lueder, G., Priller, J., Lehrach, H., Hayer-Hartl, M. K., Hartl, F. U., and Wanker, E. E. (2001) Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 10, 1307-1315
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Lehrach, H.5    Hayer-Hartl, M.K.6    Hartl, F.U.7    Wanker, E.E.8
  • 15
    • 84861369587 scopus 로고    scopus 로고
    • Impaired heat shock response in cells expressing full-length polyglutamine-expanded huntingtin
    • Chafekar, S. M., and Duennwald, M. L. (2012) Impaired heat shock response in cells expressing full-length polyglutamine-expanded huntingtin. PLoS One 7, e37929
    • (2012) PLoS One , vol.7
    • Chafekar, S.M.1    Duennwald, M.L.2
  • 16
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay, D. G., Sathasivam, K., Tobaben, S., Stahl, B., Marber, M., Mestril, R., Mahal, A., Smith, D. L., Woodman, B., and Bates, G. P. (2004) Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet. 13, 1389-1405
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 18
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells
    • Mosser, D. D., Theodorakis, N. G., and Morimoto, R. I. (1988) Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells. Mol. Cell. Biol. 8, 4736-4744
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 20
    • 79551609332 scopus 로고    scopus 로고
    • BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins
    • Gamerdinger, M., Kaya, A. M., Wolfrum, U., Clement, A. M., and Behl, C. (2011) BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep. 12, 149-156
    • (2011) EMBO Rep. , vol.12 , pp. 149-156
    • Gamerdinger, M.1    Kaya, A.M.2    Wolfrum, U.3    Clement, A.M.4    Behl, C.5
  • 22
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., and Finkbeiner, S. (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.