메뉴 건너뛰기




Volumn 21, Issue 6, 2014, Pages 732-742

Direct observations of amyloid β Self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; PROTEIN AGGREGATE;

EID: 84902954469     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2014.03.014     Document Type: Article
Times cited : (108)

References (42)
  • 1
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • DOI 10.1016/j.neuron.2005.01.040
    • L.M. Billings, S. Oddo, K.N. Green, J.L. McGaugh, and F.M. LaFerla Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice Neuron 45 2005 675 688 (Pubitemid 40320703)
    • (2005) Neuron , vol.45 , Issue.5 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 3
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, A β1-42, in differentiated PC12 cells
    • DOI 10.1016/S0006-8993(96)01262-0, PII S0006899396012620
    • D. Burdick, J. Kosmoski, M.F. Knauer, and C.G. Glabe Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, A β 1-42, in differentiated PC12 cells Brain Res. 746 1997 275 284 (Pubitemid 27060356)
    • (1997) Brain Research , vol.746 , Issue.1-2 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 8
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 9
    • 33947164189 scopus 로고    scopus 로고
    • Aβ peptides can enter the brain through a defective blood-brain barrier and bind selectively to neurons
    • DOI 10.1016/j.brainres.2007.01.070, PII S0006899307001278
    • P.M. Clifford, S. Zarrabi, G. Siu, K.J. Kinsler, M.C. Kosciuk, V. Venkataraman, M.R. D'Andrea, S. Dinsmore, and R.G. Nagele Aβ peptides can enter the brain through a defective blood-brain barrier and bind selectively to neurons Brain Res. 1142 2007 223 236 (Pubitemid 46413194)
    • (2007) Brain Research , vol.1142 , Issue.1 , pp. 223-236
    • Clifford, P.M.1    Zarrabi, S.2    Siu, G.3    Kinsler, K.J.4    Kosciuk, M.C.5    Venkataraman, V.6    D'Andrea, M.R.7    Dinsmore, S.8    Nagele, R.G.9
  • 10
    • 84863981137 scopus 로고    scopus 로고
    • From macroscopic measurements to microscopic mechanisms of protein aggregation
    • S.I. Cohen, M. Vendruscolo, C.M. Dobson, and T.P. Knowles From macroscopic measurements to microscopic mechanisms of protein aggregation J. Mol. Biol. 421 2012 160 171
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.4
  • 13
    • 77953140497 scopus 로고    scopus 로고
    • Fluorescence lifetime dynamics of enhanced green fluorescent protein in protein aggregates with expanded polyglutamine
    • V. Ghukasyan, C.C. Hsu, C.R. Liu, F.J. Kao, and T.H. Cheng Fluorescence lifetime dynamics of enhanced green fluorescent protein in protein aggregates with expanded polyglutamine J. Biomed. Opt. 15 2010 016008
    • (2010) J. Biomed. Opt. , vol.15 , pp. 016008
    • Ghukasyan, V.1    Hsu, C.C.2    Liu, C.R.3    Kao, F.J.4    Cheng, T.H.5
  • 14
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • G.G. Glenner, and C.W. Wong Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein Biochem. Biophys. Res. Commun. 120 1984 885 890 (Pubitemid 14104991)
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 16
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • J. Hardy, and D. Allsop Amyloid deposition as the central event in the aetiology of Alzheimer's disease Trends Pharmacol. Sci. 12 1991 383 388
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 17
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide
    • X. Hu, S.L. Crick, G. Bu, C. Frieden, R.V. Pappu, and J.-M. Lee Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide Proc. Natl. Acad. Sci. USA 106 2009 20324 20329
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.-M.6
  • 18
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • DOI 10.1021/bi00069a001
    • J.T. Jarrett, E.P. Berger, and P.T. Lansbury Jr. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease Biochemistry 32 1993 4693 4697 (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 19
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • D. Kaganovich, R. Kopito, and J. Frydman Misfolded proteins partition between two distinct quality control compartments Nature 454 2008 1088 1095
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 22
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • R. Kayed, E. Head, F. Sarsoza, T. Saing, C.W. Cotman, M. Necula, L. Margol, J. Wu, L. Breydo, and J.L. Thompson et al. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers Mol. Neurodegener. 2 2007 18
    • (2007) Mol. Neurodegener. , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5    Necula, M.6    Margol, L.7    Wu, J.8    Breydo, L.9    Thompson, J.L.10
  • 23
    • 33750117120 scopus 로고    scopus 로고
    • Detection of novel intracellular α-synuclein oligomeric species by fluorescence lifetime imaging
    • DOI 10.1096/fj.05-5422com
    • J. Klucken, T.F. Outeiro, P. Nguyen, P.J. McLean, and B.T. Hyman Detection of novel intracellular α-synuclein oligomeric species by fluorescence lifetime imaging FASEB J. 20 2006 2050 2057 (Pubitemid 44953904)
    • (2006) FASEB Journal , vol.20 , Issue.12 , pp. 2050-2057
    • Klucken, J.1    Outeiro, T.F.2    Nguyen, P.3    McLean, P.J.4    Hyman, B.T.5
  • 24
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein
    • M.F. Knauer, B. Soreghan, D. Burdick, J. Kosmoski, and C.G. Glabe Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein Proc. Natl. Acad. Sci. USA 89 1992 7437 7441
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 25
    • 84860389674 scopus 로고    scopus 로고
    • Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
    • J. Lee, E.K. Culyba, E.T. Powers, and J.W. Kelly Amyloid-β forms fibrils by nucleated conformational conversion of oligomers Nat. Chem. Biol. 7 2011 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
  • 31
    • 84877045867 scopus 로고    scopus 로고
    • A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence
    • D. Pinotsi, A.K. Buell, C.M. Dobson, G.S. Kaminski Schierle, and C.F. Kaminski A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence ChemBioChem 14 2013 846 850
    • (2013) ChemBioChem , vol.14 , pp. 846-850
    • Pinotsi, D.1    Buell, A.K.2    Dobson, C.M.3    Kaminski Schierle, G.S.4    Kaminski, C.F.5
  • 32
    • 84892140751 scopus 로고    scopus 로고
    • Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy
    • D. Pinotsi, A.K. Buell, C. Galvagnion, C.M. Dobson, G.S. Kaminski Schierle, and C.F. Kaminski Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy Nano Lett. 14 2014 339 345
    • (2014) Nano Lett. , vol.14 , pp. 339-345
    • Pinotsi, D.1    Buell, A.K.2    Galvagnion, C.3    Dobson, C.M.4    Kaminski Schierle, G.S.5    Kaminski, C.F.6
  • 34
    • 34247864013 scopus 로고    scopus 로고
    • Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged α-synuclein
    • DOI 10.1038/nmeth1026, PII NMETH1026
    • M.J. Roberti, C.W. Bertoncini, R. Klement, E.A. Jares-Erijman, and T.M. Jovin Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged α-synuclein Nat. Methods 4 2007 345 351 (Pubitemid 46766980)
    • (2007) Nature Methods , vol.4 , Issue.4 , pp. 345-351
    • Roberti, M.J.1    Bertoncini, C.W.2    Klement, R.3    Jares-Erijman, E.A.4    Jovin, T.M.5
  • 36
    • 0035793953 scopus 로고    scopus 로고
    • Acidic pH promotes the formation of toxic fibrils from β-amyloid peptide
    • DOI 10.1016/S0006-8993(00)03322-9, PII S0006899300033229
    • Y. Su, and P.-T. Chang Acidic pH promotes the formation of toxic fibrils from β-amyloid peptide Brain Res. 893 2001 287 291 (Pubitemid 32171924)
    • (2001) Brain Research , vol.893 , Issue.1-2 , pp. 287-291
    • Su, Y.1    Chang, P.-T.2
  • 37
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain
    • DOI 10.1523/JNEUROSCI.5167-03.2004
    • R.H. Takahashi, C.G. Almeida, P.F. Kearney, F. Yu, M.T. Lin, T.A. Milner, and G.K. Gouras Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain J. Neurosci. 24 2004 3592 3599 (Pubitemid 38481116)
    • (2004) Journal of Neuroscience , vol.24 , Issue.14 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 38
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • R.E. Thompson, D.R. Larson, and W.W. Webb Precise nanometer localization analysis for individual fluorescent probes Biophys. J. 82 2002 2775 2783 (Pubitemid 34441314)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 39
    • 38749118235 scopus 로고    scopus 로고
    • Highly inclined thin illumination enables clear single-molecule imaging in cells
    • DOI 10.1038/nmeth1171, PII NMETH1171
    • M. Tokunaga, N. Imamoto, and K. Sakata-Sogawa Highly inclined thin illumination enables clear single-molecule imaging in cells Nat. Methods 5 2008 159 161 (Pubitemid 351181742)
    • (2008) Nature Methods , vol.5 , Issue.2 , pp. 159-161
    • Tokunaga, M.1    Imamoto, N.2    Sakata-Sogawa, K.3
  • 40
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain
    • D.M. Walsh, B.P. Tseng, R.E. Rydel, M.B. Podlisny, and D.J. Selkoe The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain Biochemistry 39 2000 10831 10839
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 42
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • DOI 10.1006/jmbi.1996.0133
    • S.J. Wood, B. Maleeff, T. Hart, and R. Wetzel Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ J. Mol. Biol. 256 1996 870 877 (Pubitemid 26108825)
    • (1996) Journal of Molecular Biology , vol.256 , Issue.5 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.