메뉴 건너뛰기




Volumn 109, Issue 50, 2012, Pages 20455-20460

Direct three-dimensional visualization of membrane disruption by amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; LIPOSOME;

EID: 84870947924     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1206325109     Document Type: Article
Times cited : (160)

References (53)
  • 1
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475(7356):324-332.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 2
    • 32944457929 scopus 로고    scopus 로고
    • Amyloidosis
    • Pepys MB (2006) Amyloidosis. Annu Rev Med 57:223-241.
    • (2006) Annu Rev Med , vol.57 , pp. 223-241
    • Pepys, M.B.1
  • 3
    • 78651252910 scopus 로고    scopus 로고
    • Molecular pathology of human prion disease
    • Wadsworth JDF, Collinge J (2011) Molecular pathology of human prion disease. Acta Neuropathol 121(1):69-77.
    • (2011) Acta Neuropathol , vol.121 , Issue.1 , pp. 69-77
    • Wadsworth, J.D.F.1    Collinge, J.2
  • 5
    • 84863988708 scopus 로고    scopus 로고
    • A molecular history of the amyloidoses
    • 10.1016/jmb.2012.01.024
    • Buxbaum JN, Linke RP (2012) A molecular history of the amyloidoses. J Mol Biol 421(2-3):142-159, 10.1016/jmb.2012.01.024.
    • (2012) J Mol Biol , vol.421 , Issue.2-3 , pp. 142-159
    • Buxbaum, J.N.1    Linke, R.P.2
  • 6
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • Eichner T, Radford SE (2011) A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 43(1):8-18.
    • (2011) Mol Cell , vol.43 , Issue.1 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 7
    • 80054752317 scopus 로고    scopus 로고
    • Molecular basis for amyloid-beta polymorphism
    • Colletier JP, et al. (2011) Molecular basis for amyloid-beta polymorphism. Proc Natl Acad Sci USA 108(41):16938-16943.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.41 , pp. 16938-16943
    • Colletier, J.P.1
  • 8
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • DOI 10.1017/S0033583506004422, PII S0033583506004422
    • Lashuel HA, Lansbury PT, Jr. (2006) Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q Rev Biophys 39(2):167-201. (Pubitemid 44711851)
    • (2006) Quarterly Reviews of Biophysics , vol.39 , Issue.2 , pp. 167-201
    • Lashuel, H.A.1    Lansbury Jr., P.T.2
  • 9
    • 33344463679 scopus 로고    scopus 로고
    • Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
    • Glabe CG (2006) Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol Aging 27(4):570-575.
    • (2006) Neurobiol Aging , vol.27 , Issue.4 , pp. 570-575
    • Glabe, C.G.1
  • 10
    • 84855750207 scopus 로고    scopus 로고
    • 2+) imaging implicates Aβ1-42 amyloid pores in Alzheimer's disease pathology
    • 2+) imaging implicates Aβ1-42 amyloid pores in Alzheimer's disease pathology. J Cell Biol 195(3):515-524.
    • (2011) J Cell Biol , vol.195 , Issue.3 , pp. 515-524
    • Demuro, A.1    Smith, M.2    Parker, I.3
  • 11
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems
    • Butterfield SM, Lashuel HA (2010) Amyloidogenic protein-membrane interactions: mechanistic insight from model systems. Angew Chem Int Ed Engl 49(33):5628-5654.
    • (2010) Angew Chem Int Ed Engl , vol.49 , Issue.33 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 12
    • 82555170657 scopus 로고    scopus 로고
    • Mechanism of membrane interaction and disruption by α-synuclein
    • Reynolds NP, et al. (2011) Mechanism of membrane interaction and disruption by α-synuclein. J Am Chem Soc 133(48):19366-19375.
    • (2011) J Am Chem Soc , vol.133 , Issue.48 , pp. 19366-19375
    • Reynolds, N.P.1
  • 13
    • 78049290389 scopus 로고    scopus 로고
    • Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity
    • Stefani M (2010) Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity. FEBS J 277(22):4602-4613.
    • (2010) FEBS J , vol.277 , Issue.22 , pp. 4602-4613
    • Stefani, M.1
  • 14
    • 38049072191 scopus 로고    scopus 로고
    • Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers
    • Domanov YA, Kinnunen PKJ (2008) Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers. J Mol Biol 376(1):42-54.
    • (2008) J Mol Biol , vol.376 , Issue.1 , pp. 42-54
    • Domanov, Y.A.1    Kinnunen, P.K.J.2
  • 16
    • 84856545963 scopus 로고    scopus 로고
    • Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1
    • Bucciantini M, et al. (2012) Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1. FASEB J 26(2):818-831.
    • (2012) FASEB J , vol.26 , Issue.2 , pp. 818-831
    • Bucciantini, M.1
  • 17
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • DOI 10.1074/jbc.M511174200
    • Novitskaya V, Bocharova OV, Bronstein I, Baskakov IV (2006) Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J Biol Chem 281(19):13828-13836. (Pubitemid 43855298)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 18
    • 77957243833 scopus 로고    scopus 로고
    • The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity
    • Mossuto MF, et al. (2010) The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. J Mol Biol 402(5):783-796.
    • (2010) J Mol Biol , vol.402 , Issue.5 , pp. 783-796
    • Mossuto, M.F.1
  • 19
    • 84862701723 scopus 로고    scopus 로고
    • Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells
    • Pieri L, Madiona K, Bousset L, Melki R (2012) Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys J 102(12):2894-2905.
    • (2012) Biophys J , vol.102 , Issue.12 , pp. 2894-2905
    • Pieri, L.1    Madiona, K.2    Bousset, L.3    Melki, R.4
  • 20
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
    • Tomic JL, Pensalfini A, Head E, Glabe CG (2009) Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction. Neurobiol Dis 35(3):352-358.
    • (2009) Neurobiol Dis , vol.35 , Issue.3 , pp. 352-358
    • Tomic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, C.G.4
  • 21
    • 51249115821 scopus 로고    scopus 로고
    • Formation of toxic Abeta(1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: Polymorphisms in Abeta(1-40) fibrils
    • Okada T, Ikeda K, Wakabayashi M, Ogawa M, Matsuzaki K (2008) Formation of toxic Abeta(1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: Polymorphisms in Abeta(1-40) fibrils. J Mol Biol 382(4):1066-1074.
    • (2008) J Mol Biol , vol.382 , Issue.4 , pp. 1066-1074
    • Okada, T.1    Ikeda, K.2    Wakabayashi, M.3    Ogawa, M.4    Matsuzaki, K.5
  • 23
    • 77952711519 scopus 로고    scopus 로고
    • Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation
    • Tyedmers J, et al. (2010) Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc Natl Acad Sci USA 107(19):8633-8638.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.19 , pp. 8633-8638
    • Tyedmers, J.1
  • 25
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles TPJ, et al. (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326(5959):1533-1537.
    • (2009) Science , vol.326 , Issue.5959 , pp. 1533-1537
    • Knowles, T.P.J.1
  • 26
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue WF, Homans SW, Radford SE (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 105(26):8926-8931.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.26 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 27
    • 71749089460 scopus 로고    scopus 로고
    • Fibril fragmentation enhances amyloid cytotoxicity
    • Xue WF, et al. (2009) Fibril fragmentation enhances amyloid cytotoxicity. J Biol Chem 284(49):34272-34282.
    • (2009) J Biol Chem , vol.284 , Issue.49 , pp. 34272-34282
    • Xue, W.F.1
  • 28
    • 67349152747 scopus 로고    scopus 로고
    • 2)-microglobulin assemble into elaborate amyloid fibrils
    • 2)- microglobulin assemble into elaborate amyloid fibrils. J Mol Biol 389(1):48-57.
    • (2009) J Mol Biol , vol.389 , Issue.1 , pp. 48-57
    • White, H.E.1
  • 29
    • 77952759080 scopus 로고    scopus 로고
    • 2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling
    • 2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling. J Biol Chem 285(22):17137-17147.
    • (2010) J Biol Chem , vol.285 , Issue.22 , pp. 17137-17147
    • Ladner, C.L.1
  • 30
    • 78650159249 scopus 로고    scopus 로고
    • Griffin RG Intermolecular alignment in beta(2)-microglobulin amyloid fibrils
    • Debelouchina GT, Platt GW, Bayro MJ, Radford SE (2010) Griffin RG Intermolecular alignment in beta(2)-microglobulin amyloid fibrils. J Am Chem Soc 132:17077-17079.
    • (2010) J Am Chem Soc , vol.132 , pp. 17077-17079
    • Debelouchina, G.T.1    Platt, G.W.2    Bayro, M.J.3    Radford, S.E.4
  • 31
    • 33144471714 scopus 로고    scopus 로고
    • 2-microglobulin amyloid formation at neutral pH
    • 2-microglobulin amyloid formation at neutral pH. Biochemistry 45(7):2311-2321.
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2311-2321
    • Myers, S.L.1
  • 32
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley SJ, Saibil HR (2006) The mechanism of pore formation by bacterial toxins. Curr Opin Struct Biol 16(2):230-236.
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.2 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 34
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • Hebda JA, Miranker AD (2009) The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes. Annu Rev Biophys 38:125-152.
    • (2009) Annu Rev Biophys , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 36
    • 38049056730 scopus 로고    scopus 로고
    • Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice
    • Martins IC, et al. (2008) Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J 27(1):224-233.
    • (2008) EMBO J , vol.27 , Issue.1 , pp. 224-233
    • Martins, I.C.1
  • 37
    • 77950684398 scopus 로고    scopus 로고
    • Effect of lipid type on the binding of lipid vesicles to islet amyloid polypeptide amyloid fibrils
    • Sasahara K, Hall D, Hamada D (2010) Effect of lipid type on the binding of lipid vesicles to islet amyloid polypeptide amyloid fibrils. Biochemistry 49(14):3040-3048.
    • (2010) Biochemistry , vol.49 , Issue.14 , pp. 3040-3048
    • Sasahara, K.1    Hall, D.2    Hamada, D.3
  • 38
    • 34548291359 scopus 로고    scopus 로고
    • Surface structure of amyloid-beta fibrils contributes to cytotoxicity
    • DOI 10.1021/bi700455c
    • Yoshiike Y, Akagi T, Takashima A (2007) Surface structure of amyloid-beta fibrils contributes to cytotoxicity. Biochemistry 46(34):9805-9812. (Pubitemid 47328586)
    • (2007) Biochemistry , vol.46 , Issue.34 , pp. 9805-9812
    • Yoshiike, Y.1    Akagi, T.2    Takashima, A.3
  • 39
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • DOI 10.1016/j.jmb.2004.06.086, PII S0022283604007983
    • Knight JD, Miranker AD (2004) Phospholipid catalysis of diabetic amyloid assembly. J Mol Biol 341(5):1175-1187. (Pubitemid 39099208)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 40
    • 84859175662 scopus 로고    scopus 로고
    • Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains
    • Boucrot E, et al. (2012) Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains. Cell 149(1):124-136.
    • (2012) Cell , vol.149 , Issue.1 , pp. 124-136
    • Boucrot, E.1
  • 41
    • 75349097530 scopus 로고    scopus 로고
    • A causative link between the structure of aberrant protein oligomers and their toxicity
    • Campioni S, et al. (2010) A causative link between the structure of aberrant protein oligomers and their toxicity. Nat Chem Biol 6(2):140-147.
    • (2010) Nat Chem Biol , vol.6 , Issue.2 , pp. 140-147
    • Campioni, S.1
  • 42
    • 79952742454 scopus 로고    scopus 로고
    • In vivo demonstration that alpha-synuclein oligomers are toxic
    • Winner B, et al. (2011) In vivo demonstration that alpha-synuclein oligomers are toxic. Proc Natl Acad Sci USA 108(10):4194-4199.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.10 , pp. 4194-4199
    • Winner, B.1
  • 43
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • Cremades N, et al. (2012) Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 149(5):1048-1059.
    • (2012) Cell , vol.149 , Issue.5 , pp. 1048-1059
    • Cremades, N.1
  • 44
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • DOI 10.1038/nature04396
    • McMahon HT, Gallop JL (2005) Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438(7068):590-596. (Pubitemid 41740562)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 45
    • 77950528480 scopus 로고    scopus 로고
    • Architecture of a nascent viral fusion pore
    • Lee K-K (2010) Architecture of a nascent viral fusion pore. EMBO J 29(7):1299-1311.
    • (2010) EMBO J , vol.29 , Issue.7 , pp. 1299-1311
    • Lee, K.-K.1
  • 46
    • 77749234000 scopus 로고    scopus 로고
    • Kinesin motor activation: Microtubules pull the switches
    • Fourniol F, Moores CA (2010) Kinesin motor activation: Microtubules pull the switches. Proc Natl Acad Sci USA 107(9):3949-3950.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.9 , pp. 3949-3950
    • Fourniol, F.1    Moores, C.A.2
  • 47
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • DOI 10.1038/nature03251
    • Otomo T, et al. (2005) Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433(7025):488-494. (Pubitemid 40204299)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 48
    • 23444445907 scopus 로고    scopus 로고
    • 2-microglobulin into amyloid
    • 2-microglobulin into amyloid. J Mol Biol 351(4):850-864.
    • (2005) J Mol Biol , vol.351 , Issue.4 , pp. 850-864
    • Gosal, W.S.1
  • 50
    • 78649499176 scopus 로고    scopus 로고
    • Mutual modulation between membrane-embedded receptor clustering and ligand binding in lipid membranes
    • Tomas S, Milanesi L (2010) Mutual modulation between membrane-embedded receptor clustering and ligand binding in lipid membranes. Nat Chem 2(12):1077-1083.
    • (2010) Nat Chem , vol.2 , Issue.12 , pp. 1077-1083
    • Tomas, S.1    Milanesi, L.2
  • 52
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • DOI 10.1006/jsbi.1996.0013
    • Kremer JR, Mastronarde DN, McIntosh JR (1996) Computer visualization of three-dimensional image data using IMOD. J Struct Biol 116(1):71-76. (Pubitemid 26093126)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 53
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis AS, Hegerl R (2001) Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J Struct Biol 135(3):239-250.
    • (2001) J Struct Biol , vol.135 , Issue.3 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.