메뉴 건너뛰기




Volumn 19, Issue 3, 2012, Pages 315-327

Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; OLIGOMER; PROTEIN MISFOLDED OLIGOMER; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 84858978818     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.02.003     Document Type: Review
Times cited : (230)

References (124)
  • 1
    • 30344457011 scopus 로고    scopus 로고
    • Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation
    • DOI 10.1016/j.jmb.2005.11.034, PII S0022283605014221
    • R. Bader, R. Bamford, J. Zurdo, B.F. Luisi, and C.M. Dobson Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation J. Mol. Biol. 356 2006 189 208 (Pubitemid 43069737)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.1 , pp. 189-208
    • Bader, R.1    Bamford, R.2    Zurdo, J.3    Luisi, B.F.4    Dobson, C.M.5
  • 6
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Abeta 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 Abeta 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
  • 8
    • 79251631002 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
    • C. Bleiholder, N.F. Dupuis, T. Wyttenbach, and M.T. Bowers Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation Nat. Chem. 3 2011 172 177
    • (2011) Nat. Chem. , vol.3 , pp. 172-177
    • Bleiholder, C.1    Dupuis, N.F.2    Wyttenbach, T.3    Bowers, M.T.4
  • 10
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • M. Bouchard, J. Zurdo, E.J. Nettleton, C.M. Dobson, and C.V. Robinson Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy Protein Sci. 9 2000 1960 1967
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 12
    • 12544259221 scopus 로고    scopus 로고
    • Reversal of protein aggregation provides evidence for multiple aggregated States
    • M. Calamai, C. Canale, A. Relini, M. Stefani, F. Chiti, and C.M. Dobson Reversal of protein aggregation provides evidence for multiple aggregated States J. Mol. Biol. 346 2005 603 616
    • (2005) J. Mol. Biol. , vol.346 , pp. 603-616
    • Calamai, M.1    Canale, C.2    Relini, A.3    Stefani, M.4    Chiti, F.5    Dobson, C.M.6
  • 15
    • 33644919388 scopus 로고    scopus 로고
    • Doxycycline disrupts transthyretin amyloid: Evidence from studies in a FAP transgenic mice model
    • DOI 10.1096/fj.05-4509com
    • I. Cardoso, and M.J. Saraiva Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model FASEB J. 20 2006 234 239 (Pubitemid 44933170)
    • (2006) FASEB Journal , vol.20 , Issue.2 , pp. 234-239
    • Cardoso, I.1    Saraiva, M.J.2
  • 16
    • 66049093067 scopus 로고    scopus 로고
    • Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation
    • N. Carulla, M. Zhou, M. Arimon, M. Gairí, E. Giralt, C.V. Robinson, and C.M. Dobson Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation Proc. Natl. Acad. Sci. USA 106 2009 7828 7833
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7828-7833
    • Carulla, N.1    Zhou, M.2    Arimon, M.3    Gairí, M.4    Giralt, E.5    Robinson, C.V.6    Dobson, C.M.7
  • 17
    • 33846565857 scopus 로고    scopus 로고
    • Early Kinetics of Amyloid Fibril Formation Reveals Conformational Reorganisation of Initial Aggregates
    • DOI 10.1016/j.jmb.2006.12.007, PII S0022283606016664
    • N. Cerdà-Costa, A. Esteras-Chopo, F.X. Avilés, L. Serrano, and V. Villegas Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates J. Mol. Biol. 366 2007 1351 1363 (Pubitemid 46186391)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.4 , pp. 1351-1363
    • Cerda-Costa, N.1    Esteras-Chopo, A.2    Aviles, F.X.3    Serrano, L.4    Villegas, V.5
  • 18
    • 50949097728 scopus 로고    scopus 로고
    • Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake
    • S.M. Chafekar, F. Baas, and W. Scheper Oligomer-specific Abeta toxicity in cell models is mediated by selective uptake Biochim. Biophys. Acta 1782 2008 523 531
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 523-531
    • Chafekar, S.M.1    Baas, F.2    Scheper, W.3
  • 19
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid
    • DOI 10.1038/nsmb1345, PII NSMB1345
    • S. Chimon, M.A. Shaibat, C.R. Jones, D.C. Calero, B. Aizezi, and Y. Ishii Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid Nat. Struct. Mol. Biol. 14 2007 1157 1164 (Pubitemid 350223342)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.12 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3    Calero, D.C.4    Aizezi, B.5    Ishii, Y.6
  • 20
    • 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
  • 23
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • DOI 10.1523/JNEUROSCI.1189-06.2006
    • A. Deshpande, E. Mina, C. Glabe, and J. Busciglio Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons J. Neurosci. 26 2006 6011 6018 (Pubitemid 44318367)
    • (2006) Journal of Neuroscience , vol.26 , Issue.22 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 24
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 25
    • 33644527256 scopus 로고    scopus 로고
    • Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence
    • A. Dusa, J. Kaylor, S. Edridge, N. Bodner, D.P. Hong, and A.L. Fink Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence Biochemistry 45 2006 2752 2760
    • (2006) Biochemistry , vol.45 , pp. 2752-2760
    • Dusa, A.1    Kaylor, J.2    Edridge, S.3    Bodner, N.4    Hong, D.P.5    Fink, A.L.6
  • 26
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • DOI 10.1038/nsmb1068, PII N1068
    • C.M. Eakin, A.J. Berman, and A.D. Miranker A native to amyloidogenic transition regulated by a backbone trigger Nat. Struct. Mol. Biol. 13 2006 202 208 (Pubitemid 43348505)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.3 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 28
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • T. Eichner, and S.E. Radford A diversity of assembly mechanisms of a generic amyloid fold Mol. Cell 43 2011 8 18
    • (2011) Mol. Cell , vol.43 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 29
    • 83055176454 scopus 로고    scopus 로고
    • Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR
    • N.L. Fawzi, J. Ying, R. Ghirlando, D.A. Torchia, and G.M. Clore Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR Nature 480 2011 268 272
    • (2011) Nature , vol.480 , pp. 268-272
    • Fawzi, N.L.1    Ying, J.2    Ghirlando, R.3    Torchia, D.A.4    Clore, G.M.5
  • 30
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • DOI 10.1016/S0076-6879(99)09019-9
    • F. Ferrone Analysis of protein aggregation kinetics Methods Enzymol. 309 1999 256 274 (Pubitemid 29446454)
    • (1999) Methods in Enzymology , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 31
    • 79952748803 scopus 로고    scopus 로고
    • Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation
    • L. Giehm, D.I. Svergun, D.E. Otzen, and B. Vestergaard Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation Proc. Natl. Acad. Sci. USA 108 2011 3246 3251
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3246-3251
    • Giehm, L.1    Svergun, D.I.2    Otzen, D.E.3    Vestergaard, B.4
  • 33
    • 24044507958 scopus 로고    scopus 로고
    • Multiple assembly pathways underlie amyloid-beta fibril polymorphisms
    • DOI 10.1016/j.jmb.2005.07.029, PII S002228360500817X
    • C. Goldsbury, P. Frey, V. Olivieri, U. Aebi, and S.A. Müller Multiple assembly pathways underlie amyloid-beta fibril polymorphisms J. Mol. Biol. 352 2005 282 298 (Pubitemid 41213315)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.2 , pp. 282-298
    • Goldsbury, C.1    Frey, P.2    Olivieri, V.3    Aebi, U.4    Muller, S.A.5
  • 34
    • 0037010287 scopus 로고    scopus 로고
    • Amyloid beta-protein affects cholesterol metabolism in cultured neurons: Implications for pivotal role of cholesterol in the amyloid cascade
    • DOI 10.1002/jnr.10347
    • J.S. Gong, N. Sawamura, K. Zou, J. Sakai, K. Yanagisawa, and M. Michikawa Amyloid beta-protein affects cholesterol metabolism in cultured neurons: implications for pivotal role of cholesterol in the amyloid cascade J. Neurosci. Res. 70 2002 438 446 (Pubitemid 35222380)
    • (2002) Journal of Neuroscience Research , vol.70 , Issue.3 , pp. 438-446
    • Gong, J.-S.1    Sawamura, N.2    Zou, K.3    Sakai, J.4    Yanagisawa, K.5    Michikawa, M.6
  • 36
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
    • J.D. Harper, C.M. Lieber, and P.T. Lansbury Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein Chem. Biol. 4 1997 951 959 (Pubitemid 28050379)
    • (1997) Chemistry and Biology , vol.4 , Issue.12 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr., P.T.3
  • 37
  • 38
    • 79960320827 scopus 로고    scopus 로고
    • Isolating toxic insulin amyloid reactive species that lack β-sheets and have wide pH stability
    • C.L. Heldt, D. Kurouski, M. Sorci, E. Grafeld, I.K. Lednev, and G. Belfort Isolating toxic insulin amyloid reactive species that lack β-sheets and have wide pH stability Biophys. J. 100 2011 2792 2800
    • (2011) Biophys. J. , vol.100 , pp. 2792-2800
    • Heldt, C.L.1    Kurouski, D.2    Sorci, M.3    Grafeld, E.4    Lednev, I.K.5    Belfort, G.6
  • 42
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: Polypeptide conformations on competing pathways
    • DOI 10.1016/j.abb.2007.05.015, PII S0003986107002731, Highlight Issue: Protein Folding
    • T.R. Jahn, and S.E. Radford Folding versus aggregation: polypeptide conformations on competing pathways Arch. Biochem. Biophys. 469 2008 100 117 (Pubitemid 350214559)
    • (2008) Archives of Biochemistry and Biophysics , vol.469 , Issue.1 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 43
    • 79951607134 scopus 로고    scopus 로고
    • Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions
    • S. Jain, and J.B. Udgaonkar Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions Biochemistry 50 2011 1153 1161
    • (2011) Biochemistry , vol.50 , pp. 1153-1161
    • Jain, S.1    Udgaonkar, J.B.2
  • 44
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • J.T. Jarrett, and P.T. Lansbury Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73 1993 1055 1058 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 45
    • 84856226648 scopus 로고    scopus 로고
    • Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments
    • M. Jayaraman, R. Kodali, B. Sahoo, A.K. Thakur, A. Mayasundari, R. Mishra, C.B. Peterson, and R. Wetzel Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments J. Mol. Biol. 415 2011 881 899
    • (2011) J. Mol. Biol. , vol.415 , pp. 881-899
    • Jayaraman, M.1    Kodali, R.2    Sahoo, B.3    Thakur, A.K.4    Mayasundari, A.5    Mishra, R.6    Peterson, C.B.7    Wetzel, R.8
  • 46
    • 17044381327 scopus 로고    scopus 로고
    • Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids
    • E.M. Jones, and W.K. Surewicz Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids Cell 121 2005 63 72
    • (2005) Cell , vol.121 , pp. 63-72
    • Jones, E.M.1    Surewicz, W.K.2
  • 48
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • R. Kayed, E. Head, J.L. Thompson, T.M. McIntire, S.C. Milton, C.W. Cotman, and C.G. Glabe Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 49
    • 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 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
  • 51
    • 25444433798 scopus 로고    scopus 로고
    • Characterization of oligomeric intermediates in alpha-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein
    • DOI 10.1016/j.jmb.2005.08.046, PII S0022283605009836
    • J. Kaylor, N. Bodner, S. Edridge, G. Yamin, D.P. Hong, and A.L. Fink Characterization of oligomeric intermediates in alpha-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein J. Mol. Biol. 353 2005 357 372 (Pubitemid 41356722)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.2 , pp. 357-372
    • Kaylor, J.1    Bodner, N.2    Edridge, S.3    Yamin, G.4    Hong, D.-P.5    Fink, A.L.6
  • 52
    • 33749838193 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry - A window into amyloid structure
    • I. Kheterpal, and R. Wetzel Hydrogen/deuterium exchange mass spectrometry - a window into amyloid structure Acc. Chem. Res. 39 2006 584 593
    • (2006) Acc. Chem. Res. , vol.39 , pp. 584-593
    • Kheterpal, I.1    Wetzel, R.2
  • 53
    • 33746781304 scopus 로고    scopus 로고
    • Structural Differences in Abeta Amyloid Protofibrils and Fibrils Mapped by Hydrogen Exchange - Mass Spectrometry with On-line Proteolytic Fragmentation
    • DOI 10.1016/j.jmb.2006.06.066, PII S0022283606008102
    • I. Kheterpal, M. Chen, K.D. Cook, and R. Wetzel Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange - mass spectrometry with on-line proteolytic fragmentation J. Mol. Biol. 361 2006 785 795 (Pubitemid 44177742)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.4 , pp. 785-795
    • Kheterpal, I.1    Chen, M.2    Cook, K.D.3    Wetzel, R.4
  • 55
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • DOI 10.1016/j.sbi.2007.01.007, PII S0959440X07000085, Foldinf and Binding / Protein-Nucleic Interactions
    • R. Kodali, and R. Wetzel Polymorphism in the intermediates and products of amyloid assembly Curr. Opin. Struct. Biol. 17 2007 48 57 (Pubitemid 46242190)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 57
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes
    • DOI 10.1021/bi0001980
    • J.J. Kremer, M.M. Pallitto, D.J. Sklansky, and R.M. Murphy Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes Biochemistry 39 2000 10309 10318 (Pubitemid 30663053)
    • (2000) Biochemistry , vol.39 , Issue.33 , pp. 10309-10318
    • Kremer, J.J.1    Pallitto, M.M.2    Sklansky, D.J.3    Murphy, R.M.4
  • 58
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • DOI 10.1038/nature03679
    • R. Krishnan, and S.L. Lindquist Structural insights into a yeast prion illuminate nucleation and strain diversity Nature 435 2005 765 772 (Pubitemid 40839721)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 59
    • 58149400915 scopus 로고    scopus 로고
    • Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation
    • S. Kumar, and J.B. Udgaonkar Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation J. Mol. Biol. 385 2009 1266 1276
    • (2009) J. Mol. Biol. , vol.385 , pp. 1266-1276
    • Kumar, S.1    Udgaonkar, J.B.2
  • 62
    • 79952796718 scopus 로고    scopus 로고
    • Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways
    • A.R.A. Ladiwala, J.S. Dordick, and P.M. Tessier Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways J. Biol. Chem. 286 2011 3209 3218
    • (2011) J. Biol. Chem. , vol.286 , pp. 3209-3218
    • Ladiwala, A.R.A.1    Dordick, J.S.2    Tessier, P.M.3
  • 64
    • 68549141378 scopus 로고    scopus 로고
    • Methods for structural characterization of prefibrillar intermediates and amyloid fibrils
    • A.E. Langkilde, and B. Vestergaard Methods for structural characterization of prefibrillar intermediates and amyloid fibrils FEBS Lett. 583 2009 2600 2609
    • (2009) FEBS Lett. , vol.583 , pp. 2600-2609
    • Langkilde, A.E.1    Vestergaard, B.2
  • 65
    • 84655162704 scopus 로고    scopus 로고
    • Soluble Aβ oligomer production and toxicity
    • M.E. Larson, and S.E. Lesné Soluble Aβ oligomer production and toxicity J. Neurochem. 120 Suppl. 1 2012 125 139
    • (2012) J. Neurochem. , vol.120 , Issue.SUPPL. 1 , pp. 125-139
    • Larson, M.E.1    Lesné, S.E.2
  • 66
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brain
    • C.A. Lasagna-Reeves, C.G. Glabe, and R. Kayed Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brain J. Biol. Chem. 286 2011 22122 22130
    • (2011) J. Biol. Chem. , vol.286 , pp. 22122-22130
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 68
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • H.A. Lashuel, D. Hartley, B.M. Petre, T. Walz, and P.T. Lansbury Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 418 2002 291 (Pubitemid 34790672)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 69
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • DOI 10.1016/S0022-2836(02)00735-0
    • H.A. Lashuel, B.M. Petre, J. Wall, M. Simon, R.J. Nowak, T. Walz, and P.T. Lansbury Jr. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils J. Mol. Biol. 322 2002 1089 1102 (Pubitemid 35266514)
    • (2002) Journal of Molecular Biology , vol.322 , Issue.5 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury Jr., P.T.7
  • 70
    • 79959342196 scopus 로고    scopus 로고
    • Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity
    • N.B. Last, E. Rhoades, and A.D. Miranker Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity Proc. Natl. Acad. Sci. USA 108 2011 9460 9465
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 9460-9465
    • Last, N.B.1    Rhoades, E.2    Miranker, A.D.3
  • 71
    • 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
  • 73
    • 79955440719 scopus 로고    scopus 로고
    • Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics
    • C. Liu, M.R. Sawaya, P.N. Cheng, J. Zheng, J.S. Nowick, and D. Eisenberg Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics J. Am. Chem. Soc. 133 2011 6736 6744
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6736-6744
    • Liu, C.1    Sawaya, M.R.2    Cheng, P.N.3    Zheng, J.4    Nowick, J.S.5    Eisenberg, D.6
  • 78
    • 39749112546 scopus 로고    scopus 로고
    • Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
    • DOI 10.1021/bi701899y
    • A.M. Morris, M.A. Watzky, J.N. Agar, and R.G. Finke Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth Biochemistry 47 2008 2413 2427 (Pubitemid 351304547)
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2413-2427
    • Morris, A.M.1    Watzky, M.A.2    Agar, J.N.3    Finke, R.G.4
  • 79
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • A.M. Morris, M.A. Watzky, and R.G. Finke Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature Biochim. Biophys. Acta 1794 2009 375 397
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 80
    • 79151470406 scopus 로고    scopus 로고
    • The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of α-synuclein oligomers with distinct biochemical, morphological, and functional properties
    • T. Näsström, T. Fagerqvist, M. Barbu, M. Karlsson, F. Nikolajeff, A. Kasrayan, M. Ekberg, L. Lannfelt, M. Ingelsson, and J. Bergström The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of α-synuclein oligomers with distinct biochemical, morphological, and functional properties Free Radic. Biol. Med. 50 2011 428 437
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 428-437
    • Näsström, T.1    Fagerqvist, T.2    Barbu, M.3    Karlsson, M.4    Nikolajeff, F.5    Kasrayan, A.6    Ekberg, M.7    Lannfelt, L.8    Ingelsson, M.9    Bergström, J.10
  • 81
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Y. Nekooki-Machida, M. Kurosawa, N. Nukina, K. Ito, T. Oda, and M. Tanaka Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity Proc. Natl. Acad. Sci. USA 106 2009 9679 9684
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 82
    • 70450257636 scopus 로고    scopus 로고
    • Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains
    • A. Noguchi, S. Matsumura, M. Dezawa, M. Tada, M. Yanazawa, A. Ito, M. Akioka, S. Kikuchi, M. Sato, and S. Ideno Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains J. Biol. Chem. 284 2009 32895 32905
    • (2009) J. Biol. Chem. , vol.284 , pp. 32895-32905
    • Noguchi, A.1    Matsumura, S.2    Dezawa, M.3    Tada, M.4    Yanazawa, M.5    Ito, A.6    Akioka, M.7    Kikuchi, S.8    Sato, M.9    Ideno, S.10
  • 83
    • 1242316998 scopus 로고    scopus 로고
    • Probing Solvent Accessibility of Transthyretin Amyloid by Solution NMR Spectroscopy
    • DOI 10.1074/jbc.M310605200
    • A. Olofsson, J.H. Ippel, S.S. Wijmenga, E. Lundgren, and A. Ohman Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy J. Biol. Chem. 279 2004 5699 5707 (Pubitemid 38220599)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5699-5707
    • Olofsson, A.1    Ippel, J.H.2    Wijmenga, S.S.3    Lundgren, E.4    Ohman, A.5
  • 86
    • 79960260042 scopus 로고    scopus 로고
    • Familial Parkinson disease mutations influence α-synuclein assembly
    • K. Ono, T. Ikeda, J.I. Takasaki, and M. Yamada Familial Parkinson disease mutations influence α-synuclein assembly Neurobiol. Dis. 43 2011 715 724
    • (2011) Neurobiol. Dis. , vol.43 , pp. 715-724
    • Ono, K.1    Ikeda, T.2    Takasaki, J.I.3    Yamada, M.4
  • 88
    • 79951971438 scopus 로고    scopus 로고
    • Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer
    • A. Orte, R.W. Clarke, and D. Klenerman Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer ChemPhysChem 12 2011 491 499
    • (2011) ChemPhysChem , vol.12 , pp. 491-499
    • Orte, A.1    Clarke, R.W.2    Klenerman, D.3
  • 89
    • 77951990084 scopus 로고    scopus 로고
    • Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates
    • K. Pagano, F. Bemporad, F. Fogolari, G. Esposito, P. Viglino, F. Chiti, and A. Corazza Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates J. Biol. Chem. 285 2010 14689 14700
    • (2010) J. Biol. Chem. , vol.285 , pp. 14689-14700
    • Pagano, K.1    Bemporad, F.2    Fogolari, F.3    Esposito, G.4    Viglino, P.5    Chiti, F.6    Corazza, A.7
  • 90
    • 79960003359 scopus 로고    scopus 로고
    • Conformer-specific hydrogen exchange analysis of Aβ(1-42) oligomers by top-down electron capture dissociation mass spectrometry
    • J. Pan, J. Han, C.H. Borchers, and L. Konermann Conformer-specific hydrogen exchange analysis of Aβ(1-42) oligomers by top-down electron capture dissociation mass spectrometry Anal. Chem. 83 2011 5386 5393
    • (2011) Anal. Chem. , vol.83 , pp. 5386-5393
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 91
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of beta-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
    • A.K. Paravastu, I. Qahwash, R.D. Leapman, S.C. Meredith, and R. Tycko Seeded growth of beta-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure Proc. Natl. Acad. Sci. USA 106 2009 7443 7448
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Leapman, R.D.3    Meredith, S.C.4    Tycko, R.5
  • 94
    • 25844493690 scopus 로고    scopus 로고
    • Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide
    • DOI 10.1021/ja054663y
    • S.A. Petty, and S.M. Decatur Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide J. Am. Chem. Soc. 127 2005 13488 13489 (Pubitemid 41401188)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.39 , pp. 13488-13489
    • Petty, S.A.1    Decatur, S.M.2
  • 95
    • 15444367176 scopus 로고    scopus 로고
    • Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates
    • DOI 10.1021/bi047445a
    • S.A. Petty, T. Adalsteinsson, and S.M. Decatur Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates Biochemistry 44 2005 4720 4726 (Pubitemid 40396750)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4720-4726
    • Petty, S.A.1    Adalsteinsson, T.2    Decatur, S.M.3
  • 96
    • 79251539305 scopus 로고    scopus 로고
    • Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers
    • P.M. Pifer, E.A. Yates, and J. Legleiter Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers PLoS ONE 6 2011 e16248
    • (2011) PLoS ONE , vol.6 , pp. 16248
    • Pifer, P.M.1    Yates, E.A.2    Legleiter, J.3
  • 97
    • 23444447864 scopus 로고    scopus 로고
    • Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    • DOI 10.1016/j.jmb.2005.06.043, PII S0022283605007151
    • G. Plakoutsi, F. Bemporad, M. Calamai, N. Taddei, C.M. Dobson, and F. Chiti Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates J. Mol. Biol. 351 2005 910 922 (Pubitemid 41111905)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.4 , pp. 910-922
    • Plakoutsi, G.1    Bemporad, F.2    Calamai, M.3    Taddei, N.4    Dobson, C.M.5    Chiti, F.6
  • 98
    • 15844403848 scopus 로고    scopus 로고
    • Annular alpha-synuclein oligomers are potentially toxic agents in alpha-synucleinopathy. Hypothesis
    • D.L. Pountney, N.H. Voelcker, and W.P. Gai Annular alpha-synuclein oligomers are potentially toxic agents in alpha-synucleinopathy. Hypothesis Neurotox. Res. 7 2005 59 67
    • (2005) Neurotox. Res. , vol.7 , pp. 59-67
    • Pountney, D.L.1    Voelcker, N.H.2    Gai, W.P.3
  • 99
    • 48649109730 scopus 로고    scopus 로고
    • Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: Application to Abeta(1-40) fibrillogenesis
    • W. Qi, A. Zhang, D. Patel, S. Lee, J.L. Harrington, L. Zhao, D. Schaefer, T.A. Good, and E.J. Fernandez Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesis Biotechnol. Bioeng. 100 2008 1214 1227
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 1214-1227
    • Qi, W.1    Zhang, A.2    Patel, D.3    Lee, S.4    Harrington, J.L.5    Zhao, L.6    Schaefer, D.7    Good, T.A.8    Fernandez, E.J.9
  • 100
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • A. Quintas, D.C. Vaz, I. Cardoso, M.J. Saraiva, and R.M. Brito Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants J. Biol. Chem. 276 2001 27207 27213
    • (2001) J. Biol. Chem. , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.4    Brito, R.M.5
  • 105
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • DOI 10.1126/science.289.5483.1317
    • T.R. Serio, A.G. Cashikar, A.S. Kowal, G.J. Sawicki, J.J. Moslehi, L. Serpell, M.F. Arnsdorf, and S.L. Lindquist Nucleated conformational conversion and the replication of conformational information by a prion determinant Science 289 2000 1317 1321 (Pubitemid 30656041)
    • (2000) Science , vol.289 , Issue.5483 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6    Arnsdorf, M.F.7    Lindquist, S.L.8
  • 107
    • 77951081386 scopus 로고    scopus 로고
    • Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
    • D.P. Smith, S.E. Radford, and A.E. Ashcroft Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry Proc. Natl. Acad. Sci. USA 107 2010 6794 6798
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6794-6798
    • Smith, D.P.1    Radford, S.E.2    Ashcroft, A.E.3
  • 108
    • 41549161190 scopus 로고    scopus 로고
    • The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins
    • DOI 10.1021/ja076628s
    • G. Soldi, F. Bemporad, and F. Chiti The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins J. Am. Chem. Soc. 130 2008 4295 4302 (Pubitemid 351466425)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.13 , pp. 4295-4302
    • Soldi, G.1    Bemporad, F.2    Chiti, F.3
  • 109
    • 0037066715 scopus 로고    scopus 로고
    • Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH
    • DOI 10.1074/jbc.M109229200
    • P.O. Souillac, V.N. Uversky, I.S. Millett, R. Khurana, S. Doniach, and A.L. Fink Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH J. Biol. Chem. 277 2002 12666 12679 (Pubitemid 34952626)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 12666-12679
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5    Fink, A.L.6
  • 110
    • 0038047044 scopus 로고    scopus 로고
    • Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN
    • DOI 10.1021/bi034652m
    • P.O. Souillac, V.N. Uversky, and A.L. Fink Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN Biochemistry 42 2003 8094 8104 (Pubitemid 36807726)
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 8094-8104
    • Souillac, P.O.1    Uversky, V.N.2    Fink, A.L.3
  • 111
    • 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
  • 117
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • D.M. Walsh, and D.J. Selkoe A beta oligomers - a decade of discovery J. Neurochem. 101 2007 1172 1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 121
    • 24644447303 scopus 로고    scopus 로고
    • Seeding-dependent propagation and maturation of amyloid fibril conformation
    • DOI 10.1016/j.jmb.2005.07.061, PII S0022283605008740
    • K. Yamaguchi, S. Takahashi, T. Kawai, H. Naiki, and Y. Goto Seeding-dependent propagation and maturation of amyloid fibril conformation J. Mol. Biol. 352 2005 952 960 (Pubitemid 41267080)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.4 , pp. 952-960
    • Yamaguchi, K.-I.1    Takahashi, S.2    Kawai, T.3    Naiki, H.4    Goto, Y.5
  • 123
    • 79958081714 scopus 로고    scopus 로고
    • Polymorphic structures of Alzheimer's β-amyloid globulomers
    • X. Yu, and J. Zheng Polymorphic structures of Alzheimer's β-amyloid globulomers PLoS ONE 6 2011 e20575
    • (2011) PLoS ONE , vol.6 , pp. 20575
    • Yu, X.1    Zheng, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.