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Volumn 43, Issue 5, 2011, Pages 768-774

Heat shock protein 104 inhibited the fibrillization of prion peptide 106-126 and disassembled prion peptide 106-126 fibrils in vitro

Author keywords

Cytotoxicity; Fibril; Hsp104; Prion disease; PrP106 126

Indexed keywords

HEAT SHOCK PROTEIN 104; PRION PROTEIN; PRION PROTEIN 106-126; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 79953214343     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2011.01.022     Document Type: Article
Times cited : (34)

References (30)
  • 2
    • 20744456278 scopus 로고    scopus 로고
    • Amidation and structure relaxation abolish the neurotoxicity of the prion peptide PrP106-126 in vivo and in vitro
    • DOI 10.1074/jbc.M500210200
    • A.L. Bergström, H. Cordes, N. Zsurger, P.M. Heegaard, H. Laursen, and J. Chabry Amidation and structure relaxation abolish the neurotoxicity of the prion peptide PrP106-126 in vivo and in vitro J Biol Chem 280 2005 23114 23121 (Pubitemid 40853222)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.24 , pp. 23114-23121
    • Bergstrom, A.-L.1    Cordes, H.2    Zsurger, N.3    Heegaard, P.M.H.4    Laursen, H.5    Chabry, J.6
  • 3
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: reparating the responsible protein aggregates from the innocent bystanders Annu Rev Neurosci 26 2003 267 298 (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 5
    • 34548258322 scopus 로고    scopus 로고
    • Enhancing the fibrillization and deposition of the amyloid-b peptide reduces its negative impact on behavior and synaptic activity-dependent proteins
    • I.H. Cheng, K. Scearce-Levie, J. Legleiter, J.J. Palop, H. Gerstein, and N. Bien-Ly Enhancing the fibrillization and deposition of the amyloid-b peptide reduces its negative impact on behavior and synaptic activity-dependent proteins J Biol Chem 282 2007 23818 23828
    • (2007) J Biol Chem , vol.282 , pp. 23818-23828
    • Cheng, I.H.1    Scearce-Levie, K.2    Legleiter, J.3    Palop, J.J.4    Gerstein, H.5    Bien-Ly, N.6
  • 6
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [P SI+]
    • Y.O. Chernoff, S.L. Lindquist, B. Ono, S.G. Inge-Vechtomov, and S.W. Liebman Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [P SI+] Science 268 1995 880 884
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 8
    • 33747040086 scopus 로고    scopus 로고
    • Infection by ME7 prion is not modified in transgenic mice expressing the yeast chaperone Hsp104 in neurons
    • DOI 10.1016/j.neulet.2006.05.066, PII S0304394006005532
    • F. Dandoy-Dron, A. Bogdanova, V. Beringue, Y. Bailly, M.G. Tovey, and H. Laude Infection by ME7 prion is not modified in transgenic mice expressing the yeast chaperone Hsp104 in neurons Neurosci Lett 405 2006 181 185 (Pubitemid 44209305)
    • (2006) Neuroscience Letters , vol.405 , Issue.3 , pp. 181-185
    • Dandoy-Dron, F.1    Bogdanova, A.2    Beringue, V.3    Bailly, Y.4    Tovey, M.G.5    Laude, H.6    Dron, M.7
  • 9
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: Protein disaggregating machines
    • S.M. Doyle, and S. Wickner Hsp104 and ClpB: protein disaggregating machines Trends Biochem Sci 34 2009 40 48
    • (2009) Trends Biochem Sci , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 12
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • DOI 10.1016/S0092-8674(00)81223-4
    • J.R. Glover, and S. Lindquist Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins Cell 94 1998 73 82 (Pubitemid 28347471)
    • (1998) Cell , vol.94 , Issue.1 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 13
    • 34247868930 scopus 로고    scopus 로고
    • The toxicity of the PrP106-126 prion peptide on cultured photoreceptors correlates with the prion protein distribution in the mammalian and human retina
    • DOI 10.2353/ajpath.2007.060340
    • J. Gong, A. Jellali, V. Forster, J. Mutterer, E. Dubus, and W.D. Altrock The toxicity of the PrP106-126 prion peptide on cultured photoreceptors correlates with the prion protein distribution in the mammalian and human retina Am J Pathol 170 2007 1314 1324 (Pubitemid 47339338)
    • (2007) American Journal of Pathology , vol.170 , Issue.4 , pp. 1314-1324
    • Gong, J.1    Jellali, A.2    Forster, V.3    Mutterer, J.4    Dubus, E.5    Altrock, W.D.6    Sahel, J.A.7    Rendon, A.8    Picaud, S.9
  • 14
    • 74949142621 scopus 로고    scopus 로고
    • Oligomers of the prion protein fragment 106-126 are likely assembled from β-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation
    • M. Grabenauer, C. Wu, P. Soto, J.E. Shea, and M.T. Bowers Oligomers of the prion protein fragment 106-126 are likely assembled from β-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation J Am Chem Soc 132 2010 532 539
    • (2010) J Am Chem Soc , vol.132 , pp. 532-539
    • Grabenauer, M.1    Wu, C.2    Soto, P.3    Shea, J.E.4    Bowers, M.T.5
  • 17
    • 63449110324 scopus 로고    scopus 로고
    • Life cycle of yeast prions: Propagation mediated by amyloid fibrils
    • Y. Inoue Life cycle of yeast prions: propagation mediated by amyloid fibrils Protein Pept Lett 16 2009 271 276
    • (2009) Protein Pept Lett , vol.16 , pp. 271-276
    • Inoue, Y.1
  • 18
    • 0034623960 scopus 로고    scopus 로고
    • The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome
    • DOI 10.1074/jbc.M005543200
    • T. Jin, Y. Gu, G. Zanusso, M. Sy, A. Kumar, and M. Cohen N. Singh The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome J Biol Chem 275 2000 38699 38704 (Pubitemid 32009203)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38699-38704
    • Jin, T.1    Gu, Y.2    Zanusso, G.3    Sy, M.4    Kumar, A.5    Cohen, M.6    Gambetti, P.7    Singh, N.8
  • 19
    • 51349150684 scopus 로고    scopus 로고
    • Hsp104 antagonizes α-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease
    • C. Lo Bianco, J. Shorter, E. Régulier, H. Lashuel, T. Iwatsubo, and S. Lindquist Hsp104 antagonizes α-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease J Clin Invest 118 2008 3087 3097
    • (2008) J Clin Invest , vol.118 , pp. 3087-3097
    • Lo Bianco, C.1    Shorter, J.2    Régulier, E.3    Lashuel, H.4    Iwatsubo, T.5    Lindquist, S.6
  • 21
    • 0034462603 scopus 로고    scopus 로고
    • [URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • DOI 10.1128/MCB.20.23.8916-8922.2000
    • H. Moriyama, H.K. Edskes, and R.B. Wickner [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p Mol Cell Biol 20 2000 8916 8922 (Pubitemid 32245922)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.23 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 22
    • 0037014426 scopus 로고    scopus 로고
    • Protein Misfolding, Amyloid Formation, and Neurodegeneration
    • P.J. Muchowski Protein Misfolding, Amyloid Formation, and Neurodegeneration Neuron 35 2002 9 12
    • (2002) Neuron , vol.35 , pp. 9-12
    • Muchowski, P.J.1
  • 24
    • 37349102454 scopus 로고    scopus 로고
    • Hsp104: A weapon to combat diverse neurodegenerative disorders
    • DOI 10.1159/000109760
    • J. Shorter Hsp104: a weapon to combat diverse neurodegenerative disorders Neurosignals 16 2008 63 74 (Pubitemid 350308322)
    • (2008) NeuroSignals , vol.16 , Issue.1 , pp. 63-74
    • Shorter, J.1
  • 25
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • DOI 10.1126/science.1098007
    • J. Shorter, and S. Lindquist Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers Science 304 2004 1793 1797 (Pubitemid 38787894)
    • (2004) Science , vol.304 , Issue.5678 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 26
    • 33746405081 scopus 로고    scopus 로고
    • Destruction or Potentiation of Different Prions Catalyzed by Similar Hsp104 Remodeling Activities
    • DOI 10.1016/j.molcel.2006.05.042, PII S1097276506003868
    • J. Shorter, and S. Lindquist Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities Mol Cell 23 2006 425 438 (Pubitemid 44128844)
    • (2006) Molecular Cell , vol.23 , Issue.3 , pp. 425-438
    • Shorter, J.1    Lindquist, S.2
  • 27
    • 77957919566 scopus 로고    scopus 로고
    • Structural polymorphism of amyloid oligomers and fibrils underlies different fibrillization pathways: Immunogenicity and cytotoxicity
    • M. Stefani Structural polymorphism of amyloid oligomers and fibrils underlies different fibrillization pathways: immunogenicity and cytotoxicity Curr Protein Pept Sci 11 2010 343 354
    • (2010) Curr Protein Pept Sci , vol.11 , pp. 343-354
    • Stefani, M.1
  • 28
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie prion protein
    • J. Tatzelt, S.B. Prusiner, and W.J. Welch Chemical chaperones interfere with the formation of scrapie prion protein EMBO J 15 1996 6363 6373 (Pubitemid 26413769)
    • (1996) EMBO Journal , vol.15 , Issue.23 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 29
    • 67649573991 scopus 로고    scopus 로고
    • Morphology and secondary structure of stable beta-oligomers formed by amyloid peptide PrP(106-126)
    • P. Walsh, J. Yau, K. Simonetti, and S. Sharpe Morphology and secondary structure of stable beta-oligomers formed by amyloid peptide PrP(106-126) Biochemistry 48 2009 5779 5781
    • (2009) Biochemistry , vol.48 , pp. 5779-5781
    • Walsh, P.1    Yau, J.2    Simonetti, K.3    Sharpe, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.