메뉴 건너뛰기




Volumn 4, Issue , 2014, Pages

Ultrasonic force microscopy for nanomechanical characterization of early and late-stage amyloid-β peptide aggregation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; MULTIPROTEIN COMPLEX;

EID: 84893852887     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep04004     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 2342609768 scopus 로고    scopus 로고
    • Statespecific projections through 2025 of Alzheimer disease prevalence
    • Hebert, L. E., Scherr, P. A., Bienias, J. L., Bennett, D. A. & Evans, D. A. Statespecific projections through 2025 of Alzheimer disease prevalence. Neurology 62, 1645-1645 (2004)
    • (2004) Neurology , vol.62 , pp. 1645-1645
    • Hebert, L.E.1    Scherr, P.A.2    Bienias, J.L.3    Bennett, D.A.4    Evans, D.A.5
  • 2
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • Walsh, D. M. & Selkoe, D. J. A beta Oligomers - a decade of discovery. J. Neurochem. 101, 1172-1184 (2007)
    • (2007) J. Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 4
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • DOI 10.1038/nrn1007
    • Soto, C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4, 49-60 (2003) (Pubitemid 37271088)
    • (2003) Nature Reviews Neuroscience , vol.4 , Issue.1 , pp. 49-60
    • Soto, C.1
  • 5
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta-protein (A beta) assembly: A beta 40 and A beta 42 oligomerize through distinct pathways
    • Bitan, G. et al. Amyloid beta-protein (A beta) assembly: A beta 40 and A beta 42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. U. S. A. 100, 330-335 (2003)
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 330-335
    • Bitan, G.1
  • 6
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state
    • Pallitto, M. M. & Murphy, R. M. A mathematical model of the kinetics of betaamyloid fibril growth from the denatured state. Biophys. J. 81, 1805-1822 (2001) (Pubitemid 32783616)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 7
    • 0033849811 scopus 로고    scopus 로고
    • Probing the kinetics of beta-Amyloid selfassociation
    • Murphy, R. M. & Pallitto, M. R. Probing the kinetics of beta-Amyloid selfassociation. J. Struct. Biol. 130, 109-122 (2000)
    • (2000) J. Struct. Biol , vol.130 , pp. 109-122
    • Murphy, R.M.1    Pallitto, M.R.2
  • 8
    • 84858984601 scopus 로고    scopus 로고
    • Unraveling the early events of amyloid-beta protein (a beta) aggregation: Techniques for the determination of a beta aggregate size
    • Pryor, N. E., Moss, M. A. & Hestekin, C. N. Unraveling the Early Events of Amyloid-beta Protein (A beta) Aggregation: Techniques for the Determination of A beta Aggregate Size. Int. J. Mol. Sci. 13, 3038-3072 (2012)
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 3038-3072
    • Pryor, N.E.1    Moss, M.A.2    Hestekin, C.N.3
  • 9
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • DOI 10.1016/j.tibs.2004.08.009, PII S0968000404002105
    • Glabe, C. G. Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem.Sci. 29, 542-547 (2004) (Pubitemid 39265171)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.10 , pp. 542-547
    • Glabe, C.G.1
  • 10
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimers brains impair synaptic plasticity and memory
    • Shankar, G. M. et al. Amyloid-beta protein dimers isolated directly from Alzheimers brains impair synaptic plasticity and memory. Nat. Med. 14, 837-842 (2008)
    • (2008) Nat. Med , vol.14 , pp. 837-842
    • Shankar, G.M.1
  • 11
    • 84855964378 scopus 로고    scopus 로고
    • Template-Assisted lateral growth of amyloid-beta 42 fibrils studied by differential labeling with gold Nanoparticles
    • Arimon,M., Sanz, F., Giralt, E.&Carulla, N. Template-Assisted Lateral Growth of Amyloid-beta 42 Fibrils Studied by Differential Labeling with Gold Nanoparticles. Bioconjugate Chem. 23, 27-32 (2012)
    • (2012) Bioconjugate Chem , vol.23 , pp. 27-32
    • Arimon, M.1    Sanz, F.2    Giralt, E.3    Carulla, N.4
  • 12
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers - A novel pathway of amyloid formation
    • DOI 10.1016/S0022-2836(02)01175-0
    • Modler, A. J., Gast, K., Lutsch, G. & Damaschun, G. Assembly of amyloid protofibrils via critical oligomers - A novel pathway of amyloid formation. J. Mol. Biol. 325, 135-148 (2003) (Pubitemid 36153003)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.1 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 13
    • 78649905337 scopus 로고    scopus 로고
    • Amyloid structure and assembly: Insights from scanning transmission electron microscopy
    • Goldsbury, C. et al. Amyloid structure and assembly: Insights from scanning transmission electron microscopy. J. Struct. Biol. 173, 1-13 (2011)
    • (2011) J. Struct. Biol , vol.173 , pp. 1-13
    • Goldsbury, C.1
  • 15
    • 78649878435 scopus 로고    scopus 로고
    • Effect of cholesterol and amyloid-beta peptide on structure and function of mixed-lipid films and pulmonary surfactant BLES: An atomic force microscopy study
    • Hane, F., Drolle, E. & Leonenko, Z. Effect of cholesterol and amyloid-beta peptide on structure and function of mixed-lipid films and pulmonary surfactant BLES: an atomic force microscopy study. Nanomed - Nanotechn. Biol. Med. 6, 808-814 (2010)
    • (2010) Nanomed - Nanotechn. Biol. Med , vol.6 , pp. 808-814
    • Hane, F.1    Drolle, E.2    Leonenko, Z.3
  • 17
    • 23444450012 scopus 로고    scopus 로고
    • Fine structure study of A beta(1-42) fibrillogenesis with atomic force microscopy
    • Arimon,M. et al. Fine structure study of A beta(1-42) fibrillogenesis with atomic force microscopy. FASEB Journal 19, 1344 (2005)
    • (2005) FASEB Journal , vol.19 , pp. 1344
    • Arimon, M.1
  • 18
    • 84893867651 scopus 로고    scopus 로고
    • High resolution investigations of beta-Amyloid fibrillization by atomic force microscopy
    • Blackley, H. K. L. et al. High resolution investigations of beta-Amyloid fibrillization by atomic force microscopy. FASEB Journal 13, A1574 (1999)
    • (1999) FASEB Journal , vol.13
    • Blackley, H.K.L.1
  • 22
    • 0032682065 scopus 로고    scopus 로고
    • Elastic mapping of heterogeneous nanostructures with ultrasonic force microscopy (UFM) Surf
    • Dinelli, F., Assender, H. E., Takeda, N., Briggs, G. A. D. & Kolosov, O. V. Elastic mapping of heterogeneous nanostructures with ultrasonic force microscopy (UFM) Surf. Interface Anal. 27, 562-567 (1999)
    • (1999) Interface Anal , vol.27 , pp. 562-567
    • Dinelli, F.1    Assender, H.E.2    Takeda, N.3    Briggs, G.A.D.4    Kolosov, O.V.5
  • 24
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • Harper, J. D., Lieber, C. M.&Lansbury, P. T. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimers disease amyloidbeta protein. Chemistry and Biology 4, 951-959 (1997) (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
  • 25
    • 33748634773 scopus 로고
    • Surface adhesion and elastic properties of mica
    • Gaines, G. L. & Tabor, D. Surface adhesion and elastic properties of mica. Nature 178, 1304-1305 (1956)
    • (1956) Nature , vol.178 , pp. 1304-1305
    • Gaines, G.L.1    Tabor, D.2
  • 26
    • 0035997230 scopus 로고    scopus 로고
    • Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy
    • DOI 10.1016/S0196-9781(02)00061-X, PII S019697810200061X
    • Parbhu, A., Lin, H., Thimm, J. & Lal, R. Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy. Peptides 23, 1265-1270 (2002) (Pubitemid 34786705)
    • (2002) Peptides , vol.23 , Issue.7 , pp. 1265-1270
    • Parbhu, A.1    Lin, H.2    Thimm, J.3    Lal, R.4
  • 27
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of a beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimers disease
    • Harper, J. D., Wong, S. S., Lieber, C. M. & Lansbury, P. T. Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimers disease. Biochemistry 38, 8972-8980 (1999)
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 28
    • 0036291280 scopus 로고    scopus 로고
    • Poly-L-lysine dissolves fibrillar aggregation of the Alzheimer β-amyloid peptide in vitro
    • DOI 10.1006/bbrc.2002.6514
    • Nguyen, K. V., Gendrault, J.-L. & Wolff, C.-M. Poly-l-lysine Dissolves Fibrillar Aggregation of the Alzheimer b-Amyloid Peptide in Vitro. Biochem. Biophys. Res. Commun. 291, 764-768 (2002) (Pubitemid 34694340)
    • (2002) Biochemical and Biophysical Research Communications , vol.291 , Issue.4 , pp. 764-768
    • Nguyen, K.V.1    Gendrault, J.-L.2    Wolff, C.-M.3
  • 29
    • 77951022973 scopus 로고    scopus 로고
    • Size-dependent neurotoxicity of beta-Amyloid oligomers
    • Cizas, P. et al. Size-dependent neurotoxicity of beta-Amyloid oligomers. Arch. Biochem. Biophys. 496, 84-92 (2010)
    • (2010) Arch. Biochem. Biophys , vol.496 , pp. 84-92
    • Cizas, P.1
  • 33
    • 78651359826 scopus 로고    scopus 로고
    • Ultrasonic force microscopy: Detection and imaging of ultra-thin molecular domains
    • Dinelli, F., Albonetti, C. & Kolosov, O. V. Ultrasonic force microscopy: Detection and imaging of ultra-thin molecular domains. Ultramicroscopy 111, 267-272 (2011)
    • (2011) Ultramicroscopy , vol.111 , pp. 267-272
    • Dinelli, F.1    Albonetti, C.2    Kolosov, O.V.3
  • 34
    • 79952258282 scopus 로고    scopus 로고
    • The unique alzheimers beta-Amyloid triangular fibril has a cavity along the fibril axis under physiological Conditions
    • Miller, Y., Ma, B. Y. & Nussinov, R. The Unique Alzheimers beta-Amyloid Triangular Fibril Has a Cavity along the Fibril Axis under Physiological Conditions. J. Am. Chem. Soc. 133, 2742-2748 (2011)
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 2742-2748
    • Miller, Y.1    Ma, B.Y.2    Nussinov, R.3
  • 35
    • 77956269194 scopus 로고    scopus 로고
    • Hollow core of alzheimers a beta(42) amyloid observed by cryoem is relevant at physiological pH
    • Miller, Y., Ma, B. Y., Tsai, C. J. & Nussinov, R. Hollow core of Alzheimers A beta(42) amyloid observed by cryoEM is relevant at physiological pH. Proc. Natl. Acad. Sci. U.S.A. 107, 14128-14133 (2010)
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14128-14133
    • Miller, Y.1    Ma, B.Y.2    Tsai, C.J.3    Nussinov, R.4
  • 36
    • 0022912701 scopus 로고
    • Ultrastructure of amyloid fibrils in Alzheimer's disease and Down's syndrome
    • Miyakawa, T., Watanabe, K. & Katsuragi, S. Ultrastructure of amyloid fibrils in Alzheimers-Disease and Downs-Syndrome. Virchows Arch. B-Cell Path. Incl. Molec. Path. 52, 99-106 (1986) (Pubitemid 17233931)
    • (1986) Virchows Archiv Abteilung B Cell Pathology , vol.52 , Issue.2 , pp. 99-106
    • Miyakawa, T.1    Watanabe, K.2    Katsuragi, S.3
  • 37
    • 0038204160 scopus 로고    scopus 로고
    • Afm and stm study of beta-Amyloid aggregation on graphite
    • Wang, Z. G. et al. AFM and STM study of beta-Amyloid aggregation on graphite. Ultramicroscopy 97, 73-79 (2003)
    • (2003) Ultramicroscopy , vol.97 , pp. 73-79
    • Wang, Z.G.1
  • 38
    • 79958058969 scopus 로고    scopus 로고
    • Recent progress in understanding Alzheimers beta-Amyloid structures
    • Fandrich, M., Schmidt, M. & Grigorieff, N. Recent progress in understanding Alzheimers beta-Amyloid structures. Trends Biochem.Sci. 36, 338-345 (2011)
    • (2011) Trends Biochem.Sci , vol.36 , pp. 338-345
    • Fandrich, M.1    Schmidt, M.2    Grigorieff, N.3
  • 39
    • 73949117777 scopus 로고    scopus 로고
    • Comparison of alzheimer ab(1-40) and ab (1-42) amyloid fibrils reveals similar protofilament structures
    • Schmidt, M. et al. Comparison of Alzheimer Ab(1-40) and Ab(1-42) Amyloid Fibrils Reveals Similar Protofilament Structures. Proc. Natl. Acad. Sci. U.S.A. 106, 19813-19818 (2009)
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 19813-19818
    • Schmidt, M.1
  • 40
    • 0033600590 scopus 로고    scopus 로고
    • Amyloid beta protein (1-40) forms calciumpermeable, Zn21-sensitive channel in reconstituted lipid vesicles
    • Lin, H., Zhu, Y. W. J. & Lal, R. Amyloid beta protein (1-40) forms calciumpermeable, Zn21-sensitive channel in reconstituted lipid vesicles. Biochemistry 38, 11189-11196 (1999)
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.W.J.2    Lal, R.3
  • 41
    • 0033637078 scopus 로고    scopus 로고
    • Ultrastructural organization of amyloid fibrils by atomic force microscopy
    • Chamberlain, A. K. et al. Ultrastructural organization of amyloid fibrils by atomic force microscopy. Biophys. J. 79, 3282-3293 (2000)
    • (2000) Biophys. J , vol.79 , pp. 3282-3293
    • Chamberlain, A.K.1
  • 42
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • DOI 10.1146/annurev.biochem.66.1.385
    • Harper, J. D. & Lansbury, P. T. Models of amyloid seeding in Alzheimiers disease and scrapie: Mechanistic truths and physiological consequences of the timedependent solubility of amyloid proteins. Annu. Rev. Biochem. 66, 385-407 (1997) (Pubitemid 27274662)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 43
    • 63849293323 scopus 로고    scopus 로고
    • Interprotofilament interactions between Alzheimers A beta(1-42) peptides in amyloid fibrils revealed by cryoEM
    • Zhang, R. et al. Interprotofilament interactions between Alzheimers A beta(1-42) peptides in amyloid fibrils revealed by cryoEM. Proc. Natl. Acad. Sci. U.S.A. 106, 4653-4658 (2009)
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 4653-4658
    • Zhang, R.1
  • 46
    • 38349011533 scopus 로고    scopus 로고
    • Mechanisms of protein fibril formation: Nucleated polymerization with competing off-pathway aggregation
    • Powers, E. T. & Powers, D. L. Mechanisms of protein fibril formation: Nucleated polymerization with competing off-pathway aggregation. Biophys. J. 94, 379-391 (2008)
    • (2008) Biophys. J , vol.94 , pp. 379-391
    • Powers, E.T.1    Powers, D.L.2
  • 48
    • 70849088649 scopus 로고    scopus 로고
    • Overcoming synthetic A beta peptide aging: A new approach to an age-old problem
    • Manzoni, C. et al. Overcoming synthetic A beta peptide aging: a new approach to an age-old problem. Amyloid 16, 71-80 (2009)
    • (2009) Amyloid , vol.16 , pp. 71-80
    • Manzoni, C.1
  • 51
    • 2942666601 scopus 로고    scopus 로고
    • Methods in Molecular BiologyTM (eds PierCarlo Braga & Davide Ricci Ch. 16
    • Kiselyova, O. & Yaminsky, I. in Atomic Force Microscopy Vol. 242 Methods in Molecular BiologyTM (eds PierCarlo Braga & Davide Ricci) Ch. 16, 217-230 (Humana Press, 2004)
    • (2004) Atomic Force Microscopy , vol.242 , pp. 217-230
    • Kiselyova, O.1    Yaminsky, I.2
  • 52
    • 34047109564 scopus 로고    scopus 로고
    • Wsxm: A software for scanning probe microscopy and a tool for nanotechnology
    • Horcas, I. et al.WSXM: A software for scanning probe microscopy and a tool for nanotechnology. Rev. Sci. Instrum. 78, 013705 (2007)
    • (2007) Rev. Sci. Instrum , vol.78 , pp. 013705
    • Horcas, I.1
  • 53
    • 80053595082 scopus 로고    scopus 로고
    • Protein engineering to stabilize soluble amyloid beta-protein aggregates for structural and functional studies
    • Hard, T. Protein engineering to stabilize soluble amyloid beta-protein aggregates for structural and functional studies. FEBS Journal 278, 3884-3892 (2011)
    • (2011) FEBS Journal , vol.278 , pp. 3884-3892
    • Hard, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.