메뉴 건너뛰기




Volumn 51, Issue 46, 2012, Pages 9270-9276

Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME ACTIVITY; GLYCOPROTEINS; NEURODEGENERATIVE DISEASES; PEPTIDES;

EID: 84869392249     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301277k     Document Type: Article
Times cited : (73)

References (37)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F. and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75, 333-366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis Nature 475, 324-332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 10
    • 1642528843 scopus 로고    scopus 로고
    • Small Heat-shock Proteins and Clusterin: Intra- and Extracellular Molecular Chaperones with a Common Mechanism of Action and Function?
    • DOI 10.1080/15216540310001640498
    • Carver, J. A., Rekas, A., Thorn, D. C., and Wilson, M. R. (2003) Small heat-shock proteins and clusterin: Intra-and extracellular molecular chaperones with a common mechanism of action and function? IUBMB Life 55, 661-668 (Pubitemid 38116418)
    • (2003) IUBMB Life , vol.55 , Issue.12 , pp. 661-668
    • Carver, J.A.1    Rekas, A.2    Thorn, D.C.3    Wilson, M.R.4
  • 11
    • 0027330972 scopus 로고
    • αb Crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimers disease
    • Shinohara, H., Inaguma, Y., Goto, S., Inagaki, T., and Kato, K. (1993) αB Crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimers disease J. Neurol. Sci. 119, 203-208
    • (1993) J. Neurol. Sci. , vol.119 , pp. 203-208
    • Shinohara, H.1    Inaguma, Y.2    Goto, S.3    Inagaki, T.4    Kato, K.5
  • 14
    • 0032411158 scopus 로고    scopus 로고
    • Clusterin (apolipoprotein J) protein levels are increased in hippocampus and in frontal cortex in Alzheimer's disease
    • DOI 10.1006/exnr.1998.6892
    • Lidström, A. M., Bogdanovic, N., Hesse, C., Volkman, I., Davidsson, P., and Blennow, K. (1998) Clusterin (Apolipoprotein J) protein levels are increased in hippocampus and in frontal cortex in Alzheimers disease Exp. Neurol. 154, 511-521 (Pubitemid 29044220)
    • (1998) Experimental Neurology , vol.154 , Issue.2 , pp. 511-521
    • Lidstrom, A.-M.1    Bogdanovic, N.2    Hesse, C.3    Volkman, I.4    Davidsson, P.5    Blennow, K.6
  • 15
    • 84899571989 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloid-β: A predictor for synaptic dysfunction and neuron loss in Alzheimers disease
    • Bayer, T. A. and Wirths, O. (2010) Intracellular accumulation of amyloid-β: A predictor for synaptic dysfunction and neuron loss in Alzheimers disease Front. Aging Neurosci. 2, 8
    • (2010) Front. Aging Neurosci. , vol.2 , pp. 8
    • Bayer, T.A.1    Wirths, O.2
  • 19
    • 0033975837 scopus 로고    scopus 로고
    • Plasma and cerebrospinal fluid levels of amyloid β proteins 1-40 and 1- 42 in Alzheimer disease
    • Mehta, P. D., Pirttila, T., Mehta, S. P., Sersen, E. A., Aisen, P. S., and Wisniewski, H. M. (2000) Plasma and cerebrospinal fluid levels of amyloid-β proteins 1-40 and 1-42 in Alzheimer disease Arch. Neurol. 57, 100-105 (Pubitemid 30027637)
    • (2000) Archives of Neurology , vol.57 , Issue.1 , pp. 100-105
    • Mehta, P.D.1    Pirttila, T.2    Mehta, S.P.3    Sersen, E.A.4    Aisen, P.S.5    Wisniewski, H.M.6
  • 23
    • 0030786120 scopus 로고    scopus 로고
    • 1-42 amyloidogenesis
    • DOI 10.1016/S0014-5793(97)01180-0, PII S0014579397011800
    • Kudva, Y. C., Hiddinga, H. J., Butler, P. C., Mueske, C. S., and Eberhardt, N. L. (1997) Small heat shock proteins inhibit in vitro Aβ1-42 amyloidogenesis FEBS Lett. 416, 117-121 (Pubitemid 27470814)
    • (1997) FEBS Letters , vol.416 , Issue.1 , pp. 117-121
    • Kudva, Y.C.1    Hiddinga, H.J.2    Butler, P.C.3    Mueske, C.S.4    Eberhardt, N.L.5
  • 25
    • 34547823043 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
    • DOI 10.1096/fj.06-7986com
    • Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., and Wilson, M. R. (2007) The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures FASEB J. 21, 2312-2322 (Pubitemid 47230661)
    • (2007) FASEB Journal , vol.21 , Issue.10 , pp. 2312-2322
    • Yerbury, J.J.1    Poon, S.2    Meehan, S.3    Thompson, B.4    Kumita, J.R.5    Dobson, C.M.6    Wilson, M.R.7
  • 27
    • 34848929022 scopus 로고    scopus 로고
    • Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • DOI 10.1371/journal.pcbi.0030173
    • Cheon, M., Chang, I., Mohanty, S., Luheshi, L. M., Dobson, C. M., Vendruscolo, M., and Favrin, G. (2007) Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils PLoS Comput. Biol. 3, 1727-1738 (Pubitemid 47502977)
    • (2007) PLoS Computational Biology , vol.3 , Issue.9 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6    Favrin, G.7
  • 28
    • 84860389674 scopus 로고    scopus 로고
    • Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
    • Lee, J., Culyba, E. K., Powers, E. T., and Kelly, J. W. (2011) Amyloid-β forms fibrils by nucleated conformational conversion of oligomers Nat. Chem. Biol. 7, 602-609
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 602-609
    • Lee, J.1    Culyba, E.K.2    Powers, E.T.3    Kelly, J.W.4
  • 29
    • 42349107955 scopus 로고    scopus 로고
    • Site-directed mutations in the C-terminal extension of human αb-crystallin affect chaperone function and block amyloid fibril formation
    • Treweek, T. M., Ecroyd, H., Williams, D. M., Meehan, S., Carver, J. A., and Walker, M. J. (2007) Site-directed mutations in the C-terminal extension of human αB-crystallin affect chaperone function and block amyloid fibril formation PLoS One 2, e1046
    • (2007) PLoS One , vol.2 , pp. 1046
    • Treweek, T.M.1    Ecroyd, H.2    Williams, D.M.3    Meehan, S.4    Carver, J.A.5    Walker, M.J.6
  • 33
    • 0033548566 scopus 로고    scopus 로고
    • Clusterin has chaperone-like activity similar to that of small heat shock proteins
    • Humphreys, D. T. (1999) Clusterin has chaperone-like activity similar to that of small heat shock proteins J. Biol. Chem. 274, 6875
    • (1999) J. Biol. Chem. , vol.274 , pp. 6875
    • Humphreys, D.T.1
  • 35
    • 78149466716 scopus 로고    scopus 로고
    • αb-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide
    • Dehle, F., Ecroyd, H., Musgrave, I., and Carver, J. (2010) αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide Cell Stress Chaperones 15, 1013-1026
    • (2010) Cell Stress Chaperones , vol.15 , pp. 1013-1026
    • Dehle, F.1    Ecroyd, H.2    Musgrave, I.3    Carver, J.4
  • 36
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • Dobson, C. M. (2003) Protein folding and misfolding Nature 426, 884-890 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 37
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • Dobson, C. M. (1999) Protein misfolding, evolution and disease Trends Biochem. Sci. 24, 329-332 (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.