메뉴 건너뛰기




Volumn 55, Issue 2, 2006, Pages 74-78

The toxic aggregation of proteins: a kind of "molecular delinquency" actively fought in the cell by molecular chaperones and proteases;L'agrégation toxique des protéines : une forme de « délinquance moléculaire » activement combattue dans la cellule par les chaperones moléculaires et les protéases

Author keywords

Aggresome; Amyloids; Apoptosis; Heat shock proteins; Hsp 27; Hsp 70; Hsp 90; Inflammation; Proteasome

Indexed keywords

AMYLOID; CHAPERONE; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 33646490134     PISSN: 00033928     EISSN: 17683181     Source Type: Journal    
DOI: 10.1016/j.ancard.2006.02.002     Document Type: Article
Times cited : (1)

References (27)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1999) 329-332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 3
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski P.J., and Wacker J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6 (2005) 11-22
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 5
    • 0037147221 scopus 로고    scopus 로고
    • Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones
    • Ben-Zvi A.P., and Goloubinoff P. Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones. J. Biol. Chem. 277 (2002) 49422-49427
    • (2002) J. Biol. Chem. , vol.277 , pp. 49422-49427
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 6
  • 8
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26 (2001) 597-604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 9
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu T., Mogk A., Langen H., Goloubinoff P., and Bukau B. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol. Microbiol. 40 (2001) 397-413
    • (2001) Mol. Microbiol. , vol.40 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 10
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide S.D., and Morimoto R.I. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J. Biol. Chem. 280 (2005) 33097-33100
    • (2005) J. Biol. Chem. , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 11
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P., Mogk A., Ben-Zvi A.P., Tomoyasu T., and Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96 (1999) 13732-13737
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Ben-Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 12
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10 (2000) 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 14
    • 26944499091 scopus 로고    scopus 로고
    • Heat shock pretreatment inhibited the release of Smac/DIABLO from mitochondria and apoptosis induced by hydrogen peroxide in cardiomyocytes and C2C12 myogenic cells
    • Jiang B., Xiao W., Shi Y., Liu M., and Xiao X. Heat shock pretreatment inhibited the release of Smac/DIABLO from mitochondria and apoptosis induced by hydrogen peroxide in cardiomyocytes and C2C12 myogenic cells. Cell Stress Chaperones 10 (2005) 252-262
    • (2005) Cell Stress Chaperones , vol.10 , pp. 252-262
    • Jiang, B.1    Xiao, W.2    Shi, Y.3    Liu, M.4    Xiao, X.5
  • 16
    • 8444221224 scopus 로고    scopus 로고
    • The genetic basis of singlet oxygen-induced stress responses of Arabidopsis thaliana
    • Wagner D., Przybyla D., Op den Camp R., Kim C., Landgraf F., Lee K.P., et al. The genetic basis of singlet oxygen-induced stress responses of Arabidopsis thaliana. Science 306 (2004) 1183-1185
    • (2004) Science , vol.306 , pp. 1183-1185
    • Wagner, D.1    Przybyla, D.2    Op den Camp, R.3    Kim, C.4    Landgraf, F.5    Lee, K.P.6
  • 17
    • 0036738485 scopus 로고    scopus 로고
    • Adenoviral transfer of Hsp70 into pulmonary epithelium ameliorates experimental acute respiratory distress syndrome
    • Weiss Y.G., Maloyan A., Tazelaar J., Raj N., and Deutschman C.S. Adenoviral transfer of Hsp70 into pulmonary epithelium ameliorates experimental acute respiratory distress syndrome. J. Clin. Invest. 110 (2002) 801-806
    • (2002) J. Clin. Invest. , vol.110 , pp. 801-806
    • Weiss, Y.G.1    Maloyan, A.2    Tazelaar, J.3    Raj, N.4    Deutschman, C.S.5
  • 18
    • 0030453530 scopus 로고    scopus 로고
    • Differential protection of primary rat cardiocytes by transfection of specific heat stress proteins
    • Cumming D.V., Heads R.J., Watson A., Latchman D.S., and Yellon D.M. Differential protection of primary rat cardiocytes by transfection of specific heat stress proteins. J. Mol. Cell. Cardiol. 28 (1996) 2343-2349
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 2343-2349
    • Cumming, D.V.1    Heads, R.J.2    Watson, A.3    Latchman, D.S.4    Yellon, D.M.5
  • 19
    • 0032990851 scopus 로고    scopus 로고
    • Heat shock proteins delivered with a virus vector can protect cardiac cells against apoptosis as well as against thermal or hypoxic stress
    • Brar B.K., Stephanou A., Wagstaff M.J., Coffin R.S., Marber M.S., Engelmann G., et al. Heat shock proteins delivered with a virus vector can protect cardiac cells against apoptosis as well as against thermal or hypoxic stress. J. Mol. Cell. Cardiol. 31 (1999) 135-146
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 135-146
    • Brar, B.K.1    Stephanou, A.2    Wagstaff, M.J.3    Coffin, R.S.4    Marber, M.S.5    Engelmann, G.6
  • 20
    • 0034862016 scopus 로고    scopus 로고
    • Heat shock proteins and cardiac protection
    • Latchman D.S. Heat shock proteins and cardiac protection. Cardiovasc. Res. 51 (2001) 637-646
    • (2001) Cardiovasc. Res. , vol.51 , pp. 637-646
    • Latchman, D.S.1
  • 21
    • 0028905823 scopus 로고
    • Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery
    • Plumier J.C., Ross B.M., Currie R.W., Angelidis C.E., Kazlaris H., Kollias G., et al. Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery. J. Clin. Invest. 95 (1995) 1854-1860
    • (1995) J. Clin. Invest. , vol.95 , pp. 1854-1860
    • Plumier, J.C.1    Ross, B.M.2    Currie, R.W.3    Angelidis, C.E.4    Kazlaris, H.5    Kollias, G.6
  • 22
    • 27644515982 scopus 로고    scopus 로고
    • Controlled expression of recombinant proteins in physcomitrella patens by a conditional heat-shock promoter: a tool for plant research and biotechnology
    • Saidi Y., Finka A., Chakhporanian M., Zryd J.P., Schaefer D.G., and Goloubinoff P. Controlled expression of recombinant proteins in physcomitrella patens by a conditional heat-shock promoter: a tool for plant research and biotechnology. Plant Mol. Biol. 59 (2005) 697-711
    • (2005) Plant Mol. Biol. , vol.59 , pp. 697-711
    • Saidi, Y.1    Finka, A.2    Chakhporanian, M.3    Zryd, J.P.4    Schaefer, D.G.5    Goloubinoff, P.6
  • 23
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich D.A., Sistonen L., Kroes R.A., and Morimoto R.I. Effect of sodium salicylate on the human heat shock response. Science 255 (1992) 1243-1245
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.A.1    Sistonen, L.2    Kroes, R.A.3    Morimoto, R.I.4
  • 24
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a conducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D., Kalmar B., Dick J.R., Riddoch-Contreras J., Burnstock G., and Greensmith L. Treatment with arimoclomol, a conducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med. 10 (2004) 402-405
    • (2004) Nat. Med. , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 25
    • 20344378481 scopus 로고    scopus 로고
    • Resveratrol: preventing properties against vascular alterations and ageing
    • Delmas D., Jannin B., and Latruffe N. Resveratrol: preventing properties against vascular alterations and ageing. Mol. Nutr. Food Res. 49 (2005) 377-395
    • (2005) Mol. Nutr. Food Res. , vol.49 , pp. 377-395
    • Delmas, D.1    Jannin, B.2    Latruffe, N.3
  • 27
    • 0035834026 scopus 로고    scopus 로고
    • Single oral dose of geranylgeranylacetone induces heat-shock protein 72 and renders protection against ischemia-reperfusion injury in rat heart
    • Ooie T., Takahashi N., Saikawa T., Nawata T., Arikawa M., Yamanaka K., et al. Single oral dose of geranylgeranylacetone induces heat-shock protein 72 and renders protection against ischemia-reperfusion injury in rat heart. Circulation 104 (2001) 1837-1843
    • (2001) Circulation , vol.104 , pp. 1837-1843
    • Ooie, T.1    Takahashi, N.2    Saikawa, T.3    Nawata, T.4    Arikawa, M.5    Yamanaka, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.