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Volumn 112, Issue 18, 2015, Pages E5691-E5696

pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers

Author keywords

Amyloid; Disassembly; Fibrils; Membrane disruption; Oligomer

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; OLIGOMER; THIOFLAVINE; HEAT SHOCK PROTEIN 70; LYSOZYME; PROTEIN BINDING; RECOMBINANT PROTEIN; THIAZOLE DERIVATIVE;

EID: 84928963185     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1423174112     Document Type: Article
Times cited : (98)

References (34)
  • 1
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • Knowles TPJ, Vendruscolo M, Dobson CM (2014) The amyloid state and its association with protein misfolding diseases. Nat Rev Mol Cell Biol 15(6):384-396.
    • (2014) Nat Rev Mol Cell Biol , vol.15 , Issue.6 , pp. 384-396
    • Knowles, T.P.J.1    Vendruscolo, M.2    Dobson, C.M.3
  • 2
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300(5618):486-489.
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1
  • 3
    • 84862701723 scopus 로고    scopus 로고
    • Fibrillar α-synuclein and huntingtin exon1 assemblies are toxic to the cells
    • Pieri L, Madiona K, Bousset L, Melki R (2012) Fibrillar α-synuclein and huntingtin exon1 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
  • 4
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida Y, et al. (2009) Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc Natl Acad Sci USA 106(24):9679-9684.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.24 , pp. 9679-9684
    • Nekooki-Machida, Y.1
  • 5
    • 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
  • 6
    • 84878994873 scopus 로고    scopus 로고
    • Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
    • Cohen SI, et al. (2013) Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proc Natl Acad Sci USA 110(24):9758-9763.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.24 , pp. 9758-9763
    • Cohen, S.I.1
  • 7
    • 78650963274 scopus 로고    scopus 로고
    • Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
    • Olzscha H, et al. (2011) Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144(1):67-78.
    • (2011) Cell , vol.144 , Issue.1 , pp. 67-78
    • Olzscha, H.1
  • 8
    • 84892150877 scopus 로고    scopus 로고
    • Structural and functional characterization of two alpha-synuclein strains
    • Bousset L, et al. (2013) Structural and functional characterization of two alpha-synuclein strains. Nat Commun 4:2575.
    • (2013) Nat Commun , vol.4 , pp. 2575
    • Bousset, L.1
  • 9
    • 71749089460 scopus 로고    scopus 로고
    • Fibril fragmentation enhances amyloid cytotoxicity
    • Xue W-F, 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
  • 10
    • 84919799070 scopus 로고    scopus 로고
    • β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes
    • Jakhria T, et al. (2014) β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes. J Biol Chem 289(52):35781-35794.
    • (2014) J Biol Chem , vol.289 , Issue.52 , pp. 35781-35794
    • Jakhria, T.1
  • 11
    • 84904742860 scopus 로고    scopus 로고
    • Defined α-synuclein prion-like molecular assemblies spreading in cell culture
    • Aulić S, et al. (2014) Defined α-synuclein prion-like molecular assemblies spreading in cell culture. BMC Neurosci 15:69.
    • (2014) BMC Neurosci , vol.15 , pp. 69
    • Aulić, S.1
  • 12
    • 84905457722 scopus 로고    scopus 로고
    • β2-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH
    • Goodchild SC, et al. (2014) β2-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH. PLoS One 9:e104492.
    • (2014) PLoS One , vol.9 , pp. e104492
    • Goodchild, S.C.1
  • 13
    • 84870947924 scopus 로고    scopus 로고
    • Direct three-dimensional visualization of membrane disruption by amyloid fibrils
    • Milanesi L, et al. (2012) Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc Natl Acad Sci USA 109(50):20455-20460.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.50 , pp. 20455-20460
    • Milanesi, L.1
  • 14
    • 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
  • 15
    • 79957674907 scopus 로고    scopus 로고
    • Population of nonnative states of lysozyme variants drives amyloid fibril formation
    • Buell AK, et al. (2011) Population of nonnative states of lysozyme variants drives amyloid fibril formation. J Am Chem Soc 133(20):7737-7743.
    • (2011) J Am Chem Soc , vol.133 , Issue.20 , pp. 7737-7743
    • Buell, A.K.1
  • 16
    • 84904559289 scopus 로고    scopus 로고
    • Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly
    • Karamanos TK, Kalverda AP, Thompson GS, Radford SE (2014) Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. Mol Cell 55(2):214-226.
    • (2014) Mol Cell , vol.55 , Issue.2 , pp. 214-226
    • Karamanos, T.K.1    Kalverda, A.P.2    Thompson, G.S.3    Radford, S.E.4
  • 17
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado M, Merkel JS, Regan L (2000) A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc Natl Acad Sci USA 97(16):8979-8984.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.16 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 18
    • 83655184703 scopus 로고    scopus 로고
    • Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils
    • Bieschke J, et al. (2012) Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils. Nat Chem Biol 8(1):93-101.
    • (2012) Nat Chem Biol , vol.8 , Issue.1 , pp. 93-101
    • Bieschke, J.1
  • 19
    • 84880638556 scopus 로고    scopus 로고
    • Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta
    • Jiang L, et al. (2013) Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta. eLife 2:e00857.
    • (2013) eLife , vol.2 , pp. e00857
    • Jiang, L.1
  • 20
    • 84899410193 scopus 로고    scopus 로고
    • Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage
    • Narayan P, et al. (2014) Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage. Biochemistry 53(15):2442-2453.
    • (2014) Biochemistry , vol.53 , Issue.15 , pp. 2442-2453
    • Narayan, P.1
  • 21
    • 84899766632 scopus 로고    scopus 로고
    • Secondary structure in the core of amyloid fibrils formed from human β2m and its truncated variant ΔN6
    • Su Y, et al. (2014) Secondary structure in the core of amyloid fibrils formed from human β2m and its truncated variant ΔN6. J Am Chem Soc 136(17):6313-6325.
    • (2014) J Am Chem Soc , vol.136 , Issue.17 , pp. 6313-6325
    • Su, Y.1
  • 22
    • 47749118352 scopus 로고    scopus 로고
    • A common β-sheet architecture underlies in vitro and in vivo β2-microglobulin amyloid fibrils
    • Jahn TR, Tennent GA, Radford SE (2008) A common β-sheet architecture underlies in vitro and in vivo β2-microglobulin amyloid fibrils. J Biol Chem 283(25):17279-17286.
    • (2008) J Biol Chem , vol.283 , Issue.25 , pp. 17279-17286
    • Jahn, T.R.1    Tennent, G.A.2    Radford, S.E.3
  • 23
    • 80655128596 scopus 로고    scopus 로고
    • Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils
    • Porter MY, Routledge KE, Radford SE, Hewitt EW (2011) Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils. PLoS ONE 6(11):e27353.
    • (2011) PLoS ONE , vol.6 , Issue.11 , pp. e27353
    • Porter, M.Y.1    Routledge, K.E.2    Radford, S.E.3    Hewitt, E.W.4
  • 24
    • 35748986138 scopus 로고    scopus 로고
    • Investigation into the role of macrophages in the formation and degradation of β2-microglobulin amyloid fibrils
    • Morten IJ, Gosal WS, Radford SE, Hewitt EW (2007) Investigation into the role of macrophages in the formation and degradation of β2-microglobulin amyloid fibrils. J Biol Chem 282(40):29691-29700.
    • (2007) J Biol Chem , vol.282 , Issue.40 , pp. 29691-29700
    • Morten, I.J.1    Gosal, W.S.2    Radford, S.E.3    Hewitt, E.W.4
  • 25
    • 0037342671 scopus 로고    scopus 로고
    • Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy
    • Sengupta P, Garai K, Balaji J, Periasamy N, Maiti S (2003) Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy. Biophys J 84(3):1977-1984.
    • (2003) Biophys J , vol.84 , Issue.3 , pp. 1977-1984
    • Sengupta, P.1    Garai, K.2    Balaji, J.3    Periasamy, N.4    Maiti, S.5
  • 26
    • 33750294048 scopus 로고    scopus 로고
    • Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry
    • Smith AM, Jahn TR, Ashcroft AE, Radford SE (2006) Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J Mol Biol 364(1):9-19.
    • (2006) J Mol Biol , vol.364 , Issue.1 , pp. 9-19
    • Smith, A.M.1    Jahn, T.R.2    Ashcroft, A.E.3    Radford, S.E.4
  • 27
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Wetzel R (2002) Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci USA 99(3):1485-1490.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.3 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 28
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity
    • Danzer KM, et al. (2011) Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity. FASEB J 25(1):326-336.
    • (2011) FASEB J , vol.25 , Issue.1 , pp. 326-336
    • Danzer, K.M.1
  • 29
    • 71249140246 scopus 로고    scopus 로고
    • Chaperone proteostasis in Parkinson's disease: Stabilization of the Hsp70/alpha-synuclein complex by Hip
    • Roodveldt C, et al. (2009) Chaperone proteostasis in Parkinson's disease: Stabilization of the Hsp70/alpha-synuclein complex by Hip. EMBO J 28(23):3758-3770.
    • (2009) EMBO J , vol.28 , Issue.23 , pp. 3758-3770
    • Roodveldt, C.1
  • 30
    • 84872680675 scopus 로고    scopus 로고
    • Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation
    • Wang AM, et al. (2013) Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation. Nat Chem Biol 9(2):112-118.
    • (2013) Nat Chem Biol , vol.9 , Issue.2 , pp. 112-118
    • Wang, A.M.1
  • 31
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
    • Desplats P, et al. (2009) Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. Proc Natl Acad Sci USA 106(31):13010-13015.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.31 , pp. 13010-13015
    • Desplats, P.1
  • 32
    • 82755197062 scopus 로고    scopus 로고
    • Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast
    • Treusch S, et al. (2011) Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast. Science 334(6060):1241-1245.
    • (2011) Science , vol.334 , Issue.6060 , pp. 1241-1245
    • Treusch, S.1
  • 33
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova AT, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307(5707):262-265.
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1
  • 34
    • 30844456535 scopus 로고    scopus 로고
    • SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
    • Schanda P, Kupce E, Brutscher B (2005) SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J Biomol NMR 33(4):199-211.
    • (2005) J Biomol NMR , vol.33 , Issue.4 , pp. 199-211
    • Schanda, P.1    Kupce, E.2    Brutscher, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.