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Volumn 358, Issue 1, 2006, Pages 106-119

High-resolution atomic force microscopy of soluble Aβ42 oligomers

Author keywords

Alzheimer's disease; Amyloid beta; Atomic force microscopy; Protofibrils; Soluble oligomer

Indexed keywords

AMYLOID PRECURSOR PROTEIN; DIMER; MONOMER; OLIGOMER; PROTEIN ABETA42; UNCLASSIFIED DRUG;

EID: 33645108790     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.01.042     Document Type: Article
Times cited : (200)

References (72)
  • 1
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin, Notch, and the genesis and treatment of Alzheimer's disease
    • D.J. Selkoe Presenilin, Notch, and the genesis and treatment of Alzheimer's disease Proc. Natl Acad. Sci. USA 98 2001 11039 11041
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 0022547855 scopus 로고
    • X-ray-diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer-disease indicates cross-β conformation
    • D.A. Kirschner, C. Abraham, and D.J. Selkoe X-ray-diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer-disease indicates cross-β conformation Proc. Natl Acad. Sci. USA 83 1986 503 507
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 4
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • D.M. Hartley, D.M. Walsh, C.P.P. Ye, T. Diehl, S. Vasquez, and P.M. Vassilev Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons J. Neurosci. 19 1999 8876 8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6
  • 7
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • C.A. McLean, R.A. Cherny, F.W. Fraser, S.J. Fuller, M.J. Smith, and K. Beyreuther Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease Ann. Neurol. 46 1999 860 866
    • (1999) Ann. Neurol. , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4    Smith, M.J.5    Beyreuther, K.6
  • 8
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • L.F. Lue, Y.M. Kuo, A.E. Roher, L. Brachova, Y. Shen, and L. Sue Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease Am. J. Pathol. 155 1999 853 862
    • (1999) Am. J. Pathol. , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3    Brachova, L.4    Shen, Y.5    Sue, L.6
  • 9
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo
    • D.M. Walsh, I. Klyubin, J.V. Fadeeva, W.K. Cullen, R. Anwyl, and M.S. Wolfe Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 2002 535 539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6
  • 10
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • K.N. Dahlgren, A.M. Manelli, W.B. Stine Jr, L.K. Baker, G.A. Krafft, and M.J. LaDu Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability J. Biol. Chem. 277 2002 32046 32053
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 11
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis-structure and biological activity of protofibrillar intermediates
    • D.M. Walsh, D.M. Hartley, Y. Kusumoto, Y. Fezoui, M.M. Condron, and A. Lomakin Amyloid β-protein fibrillogenesis-structure and biological activity of protofibrillar intermediates J. Biol. Chem. 274 1999 25945 25952
    • (1999) J. Biol. Chem. , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 12
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis - Detection of a protofibrillar intermediate
    • D.M. Walsh, A. Lomakin, G.B. Benedek, M.M. Condron, and D.B. Teplow Amyloid β-protein fibrillogenesis - detection of a protofibrillar intermediate J. Biol. Chem. 272 1997 22364 22372
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 13
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid-β A4 peptides of Alzheimer's disease
    • C. Hilbich, B. Kisters-Woike, J. Reed, C.L. Masters, and K. Beyreuther Aggregation and secondary structure of synthetic amyloid-β A4 peptides of Alzheimer's disease J. Mol. Biol. 218 1991 149 163
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 15
    • 0028971326 scopus 로고
    • Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure
    • C. Soto, E.M. Castano, R.A. Kumar, R.C. Beavis, and B. Frangione Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure Neurosci. Letters 200 1995 105 108
    • (1995) Neurosci. Letters , vol.200 , pp. 105-108
    • Soto, C.1    Castano, E.M.2    Kumar, R.A.3    Beavis, R.C.4    Frangione, B.5
  • 18
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes
    • E. Terzi, G. Hölzemann, and J. Seelig Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes Biochemistry 36 1997 14845 14852
    • (1997) Biochemistry , vol.36 , pp. 14845-14852
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 19
    • 0033616779 scopus 로고    scopus 로고
    • Interactions of amyloid-β peptide (1-40) with ganglioside-containing membranes
    • K. Matsuzaki, and C. Horikiri Interactions of amyloid-β peptide (1-40) with ganglioside-containing membranes Biochemistry 38 1999 4137 4142
    • (1999) Biochemistry , vol.38 , pp. 4137-4142
    • Matsuzaki, K.1    Horikiri, C.2
  • 20
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ 1-40), which may potentially inhibit the fibril formation
    • S.R. Ji, Y. Wu, and S.F. Sui Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ 1-40), which may potentially inhibit the fibril formation J. Biol. Chem. 277 2002 6273 6279
    • (2002) J. Biol. Chem. , vol.277 , pp. 6273-6279
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 22
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and a pathogenic (E22G) form of Aβ 40 in vitro accumulate protofibrils, including amyloid pores
    • H.A. Lashuel, D.M. Hartley, B.M. Petre, J.S. Wall, M.N. Simon, T. Walz, and P.T. Lansbury Mixtures of wild-type and a pathogenic (E22G) form of Aβ 40 in vitro accumulate protofibrils, including amyloid pores J. Mol. Biol. 332 2003 795 808
    • (2003) J. Mol. Biol. , vol.332 , pp. 795-808
    • Lashuel, H.A.1    Hartley, D.M.2    Petre, B.M.3    Wall, J.S.4    Simon, M.N.5    Walz, T.6    Lansbury, P.T.7
  • 23
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimers Aβ peptides and the mechanism of amyloid aggregation
    • B. Soreghan, J. Kosmoski, and C. Glabe Surfactant properties of Alzheimers Aβ peptides and the mechanism of amyloid aggregation J. Biol. Chem. 269 1994 28551 28554
    • (1994) J. Biol. Chem. , vol.269 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 24
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Y.S. Gong, L. Chang, K.L. Viola, P.N. Lacor, M.P. Lambert, and C.E. Finch Alzheimer's disease-affected brain: presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss Proc. Natl Acad. Sci. USA 100 2003 10417 10422
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10417-10422
    • Gong, Y.S.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6
  • 25
    • 27144511230 scopus 로고    scopus 로고
    • β-Amyloid immunotherapy prevents synaptic degeneration in a mouse model of Alzheimer's disease
    • M. Buttini, E. Masliah, R. Barbour, H. Grajeda, R. Motter, and K. Johnson-Wood β-Amyloid immunotherapy prevents synaptic degeneration in a mouse model of Alzheimer's disease J. Neurosci. 25 2005 9096 9101
    • (2005) J. Neurosci. , vol.25 , pp. 9096-9101
    • Buttini, M.1    Masliah, E.2    Barbour, R.3    Grajeda, H.4    Motter, R.5    Johnson-Wood, K.6
  • 27
    • 0029878108 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid β peptide 25-35 is localized in the membrane hydrocarbon core: X-ray diffraction analysis
    • R.P. Mason, J.D. Estermyer, J.F. Kelly, and P.E. Mason Alzheimer's disease amyloid β peptide 25-35 is localized in the membrane hydrocarbon core: X-ray diffraction analysis Biochem. Biophys. Res. Commun. 222 1996 78 82
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 78-82
    • Mason, R.P.1    Estermyer, J.D.2    Kelly, J.F.3    Mason, P.E.4
  • 28
    • 0030928650 scopus 로고    scopus 로고
    • Lipid binding to amyloid β-peptide aggregates: Preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids
    • N.A. Avdulov, S.V. Chochina, U. Igbavboa, C.S. Warden, A.V. Vassiliev, and W.G. Wood Lipid binding to amyloid β-peptide aggregates: preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids J. Neurochem. 69 1997 1746 1752
    • (1997) J. Neurochem. , vol.69 , pp. 1746-1752
    • Avdulov, N.A.1    Chochina, S.V.2    Igbavboa, U.3    Warden, C.S.4    Vassiliev, A.V.5    Wood, W.G.6
  • 29
    • 0010806403 scopus 로고    scopus 로고
    • Interactions of Alzheimer's amyloid-β peptides with lipid membranes
    • K.Y.C. Lee, A. Muresan, and C. Ege Interactions of Alzheimer's amyloid-β peptides with lipid membranes Biophys. J. 80 2001 23A
    • (2001) Biophys. J. , vol.80
    • Lee, K.Y.C.1    Muresan, A.2    Ege, C.3
  • 31
    • 1242269712 scopus 로고    scopus 로고
    • Architecture of the Alzheimer's AβP ion channel pore
    • N. Arispe Architecture of the Alzheimer's AβP ion channel pore J. Membr. Biol. 197 2004 33 48
    • (2004) J. Membr. Biol. , vol.197 , pp. 33-48
    • Arispe, N.1
  • 32
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [A(P-(1-40)] in bilayer membranes
    • N. Arispe, H.B. Pollard, and E. Rojas Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [A(P-(1-40)] in bilayer membranes Proc. Natl Acad. Sci. USA 90 1993 10573 10577
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 33
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid (protein forms calcium channels in bilayer-membranes: Blockade by tromethamine and aluminum
    • N. Arispe, E. Rojas, and H.B. Pollard Alzheimer disease amyloid (protein forms calcium channels in bilayer-membranes: blockade by tromethamine and aluminum Proc. Natl Acad. Sci. USA 90 1993 567 571
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 34
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • R. Kayed, Y. Sokolov, B. Edmonds, T.M. McIntire, S.C. Milton, J.E. Hall, and C.G. Glabe Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases J. Biol. Chem. 279 2004 46363 46366
    • (2004) J. Biol. Chem. , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 35
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease
    • J.W. Lustbader, M. Cirilli, C. Lin, H.W. Xu, K. Takuma, and N. Wang ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease Science 304 2004 448 452
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3    Xu, H.W.4    Takuma, K.5    Wang, N.6
  • 36
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of Aβ 1-40: Implications for the search for Aβ fibril formation inhibitors
    • C.S. Goldsbury, S. Wirtz, S.A. Müller, S. Sunderji, P. Wicki, U. Aebi, and P. Frey Studies on the in vitro assembly of Aβ 1-40: implications for the search for Aβ fibril formation inhibitors J. Struct. Biol. 130 2000 217 231
    • (2000) J. Struct. Biol. , vol.130 , pp. 217-231
    • Goldsbury, C.S.1    Wirtz, S.2    Müller, S.A.3    Sunderji, S.4    Wicki, P.5    Aebi, U.6    Frey, P.7
  • 38
  • 40
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • J. Hardy Amyloid, the presenilins and Alzheimer's disease Trends Neurosci. 20 1997 154 159
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 41
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • A. Goate, M.C. Chartier-Harlin, M. Mullan, J. Brown, F. Crawford, and L. Fidani Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease Nature 349 1991 704 706
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3    Brown, J.4    Crawford, F.5    Fidani, L.6
  • 42
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • J.D. Harper, S.S. Wong, C.M. Lieber, and P.T. Lansbury Observation of metastable Aβ amyloid protofibrils by atomic force microscopy Chem. Biol. 4 1997 119 125
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 43
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of a (amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • J.D. Harper, S.S. Wong, C.M. Lieber, and P.T. Lansbury Assembly of A (amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease Biochemistry 38 1999 8972 8980
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 44
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation
    • T. Kowalewski, and D.M. Holtzman In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: new insights into mechanism of β-sheet formation Proc. Natl Acad. Sci. USA 96 1999 3688 3693
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 45
    • 0037076539 scopus 로고    scopus 로고
    • Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
    • M.R. Nichols, M.A. Moss, D.K. Reed, W.L. Lin, R. Mukhopadhyay, J.H. Hoh, and T.L. Rosenberry Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy Biochemistry 41 2002 6115 6127
    • (2002) Biochemistry , vol.41 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 49
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling
    • M. Torok, S. Milton, R. Kayed, P. Wu, T. McIntire, C.G. Glabe, and R. Langen Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling J. Biol. Chem. 277 2002 40810 40815
    • (2002) J. Biol. Chem. , vol.277 , pp. 40810-40815
    • Torok, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5    Glabe, C.G.6    Langen, R.7
  • 50
    • 0035797795 scopus 로고    scopus 로고
    • Structural features of the Aβ amyloid fibril elucidated by limited proteolysis
    • I. Kheterpal, A. Williams, C. Murphy, B. Bledsoe, and R. Wetzel Structural features of the Aβ amyloid fibril elucidated by limited proteolysis Biochemistry 40 2001 11757 11767
    • (2001) Biochemistry , vol.40 , pp. 11757-11767
    • Kheterpal, I.1    Williams, A.2    Murphy, C.3    Bledsoe, B.4    Wetzel, R.5
  • 51
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • A.T. Petkova, R.D. Leapman, Z.H. Guo, W.M. Yau, M.P. Mattson, and R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils Science 307 2005 262 265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.H.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 52
    • 24044507958 scopus 로고    scopus 로고
    • Multiple assembly pathways underlie amyloid-β fibril polymorphisms
    • C. Goldsbury, P. Frey, V. Olivieri, U. Aebi, and S.A. Müller Multiple assembly pathways underlie amyloid-β fibril polymorphisms J. Mol. Biol. 352 2005 282 298
    • (2005) J. Mol. Biol. , vol.352 , pp. 282-298
    • Goldsbury, C.1    Frey, P.2    Olivieri, V.3    Aebi, U.4    Müller, S.A.5
  • 54
    • 0035865539 scopus 로고    scopus 로고
    • Temperature-induced conformational changes in amyloid (1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system
    • H.L. Chu, and S.Y. Lin Temperature-induced conformational changes in amyloid (1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system Biophys. Chem. 89 2001 173 180
    • (2001) Biophys. Chem. , vol.89 , pp. 173-180
    • Chu, H.L.1    Lin, S.Y.2
  • 55
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • W.C. Johnson Analyzing protein circular dichroism spectra for accurate secondary structures Proteins: Struct. Funct. Genet. 35 1999 307 312
    • (1999) Proteins: Struct. Funct. Genet. , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 57
    • 0037168446 scopus 로고    scopus 로고
    • Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance
    • O.N. Antzutkin, R.D. Leapman, J.J. Balbach, and R. Tycko Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance Biochemistry 41 2002 15436 15450
    • (2002) Biochemistry , vol.41 , pp. 15436-15450
    • Antzutkin, O.N.1    Leapman, R.D.2    Balbach, J.J.3    Tycko, R.4
  • 58
    • 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
    • J.T. Jarrett, E.P. Berger, and P.T. Lansbury 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
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 59
    • 17644397372 scopus 로고    scopus 로고
    • Aβ 40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid
    • K.L. Sciarretta, D.J. Gordon, A.T. Petkova, R. Tycko, and S.C. Meredith Aβ 40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid Biochemistry 44 2005 6003 6014
    • (2005) Biochemistry , vol.44 , pp. 6003-6014
    • Sciarretta, K.L.1    Gordon, D.J.2    Petkova, A.T.3    Tycko, R.4    Meredith, S.C.5
  • 60
    • 14644390240 scopus 로고    scopus 로고
    • Structural role of glycine in amyloid fibrils formed from transmembrane α-helices
    • W. Liu, E. Crocker, W. Zhang, J.I. Elliott, B. Luy, and H. Li Structural role of glycine in amyloid fibrils formed from transmembrane α-helices Biochemistry 44 2005 3591 3597
    • (2005) Biochemistry , vol.44 , pp. 3591-3597
    • Liu, W.1    Crocker, E.2    Zhang, W.3    Elliott, J.I.4    Luy, B.5    Li, H.6
  • 61
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid β-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • M. Pitschke, R. Prior, M. Haupt, and D. Riesner Detection of single amyloid β-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy Nature Med. 4 1998 832 834
    • (1998) Nature Med. , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 62
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • L.K. Tamm, and S.A. Tatulian Infrared spectroscopy of proteins and peptides in lipid bilayers Quart. Rev. Biophys. 30 1997 365 429
    • (1997) Quart. Rev. Biophys. , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 64
    • 0001116334 scopus 로고    scopus 로고
    • A magnetically driven oscillating probe microscope for operation in liquids
    • W.H. Han, S.M. Lindsay, and T.W. Jing A magnetically driven oscillating probe microscope for operation in liquids Appl. Phys. Letters 69 1996 4111 4113
    • (1996) Appl. Phys. Letters , vol.69 , pp. 4111-4113
    • Han, W.H.1    Lindsay, S.M.2    Jing, T.W.3
  • 65
    • 0032866779 scopus 로고    scopus 로고
    • Direct observation of one-dimensional diffusion and transcription by Escherichia coli RNA polymerase
    • M. Guthold, X. Zhu, C. Rivetti, G. Yang, N.H. Thomson, and S. Kasas Direct observation of one-dimensional diffusion and transcription by Escherichia coli RNA polymerase Biophys. J. 77 1999 2284 2294
    • (1999) Biophys. J. , vol.77 , pp. 2284-2294
    • Guthold, M.1    Zhu, X.2    Rivetti, C.3    Yang, G.4    Thomson, N.H.5    Kasas, S.6
  • 68
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • E.L. Florin, V.T. Moy, and H.E. Gaub Adhesion forces between individual ligand-receptor pairs Science 264 1994 415 417
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 69
    • 0029863919 scopus 로고    scopus 로고
    • DNA binding to mica correlates with cationic radius: Assay by atomic force microscopy
    • H.G. Hansma, and D.E. Laney DNA binding to mica correlates with cationic radius: assay by atomic force microscopy Biophys. J. 70 1996 1933 1939
    • (1996) Biophys. J. , vol.70 , pp. 1933-1939
    • Hansma, H.G.1    Laney, D.E.2
  • 70
    • 0029127492 scopus 로고
    • High-resolution atomic-force microscopy of DNA: The pitch of the double helix
    • J. Mou, D.M. Czajkowsky, Y. Zhang, and Z. Shao High-resolution atomic-force microscopy of DNA: the pitch of the double helix FEBS Letters 371 1995 279 282
    • (1995) FEBS Letters , vol.371 , pp. 279-282
    • Mou, J.1    Czajkowsky, D.M.2    Zhang, Y.3    Shao, Z.4
  • 72
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • R. Tycko Progress towards a molecular-level structural understanding of amyloid fibrils Curr. Opin. Struct. Biol. 14 2004 96 103
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.