메뉴 건너뛰기




Volumn 104, Issue 12, 2013, Pages 2706-2713

In vitro study of α-synuclein protofibrils by Cryo-EM suggests a Cu2+-dependent aggregation pathway

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; COPPER;

EID: 84879229182     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.04.050     Document Type: Article
Times cited : (33)

References (38)
  • 1
  • 2
    • 66949117423 scopus 로고    scopus 로고
    • The scientific and clinical basis for the treatment of Parkinson disease
    • C.W. Olanow, M.D. Stern, and K. Sethi The scientific and clinical basis for the treatment of Parkinson disease Neurology 72 2009 S65 S73
    • (2009) Neurology , vol.72
    • Olanow, C.W.1    Stern, M.D.2    Sethi, K.3
  • 3
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of α-synuclein
    • A.L. Fink The aggregation and fibrillation of α-synuclein Acc. Chem. Res. 39 2006 628 634
    • (2006) Acc. Chem. Res. , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 4
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26 2003 267 298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 5
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease?
    • M.S. Goldberg, and P.T. Lansbury Jr. Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson's disease? Nat. Cell Biol. 2 2000 E115 E119
    • (2000) Nat. Cell Biol. , vol.2
    • Goldberg, M.S.1    Lansbury, Jr.P.T.2
  • 6
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative disease Nat. Med. 10 Suppl 2004 S10 S17
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 7
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 8
    • 78649894243 scopus 로고    scopus 로고
    • Mechanistic study of self-assembling peptide RADA16-I in formation of nanofibers and hydrogels
    • 011007-011006
    • H. Zhang, H. Luo, and X. Zhao Mechanistic study of self-assembling peptide RADA16-I in formation of nanofibers and hydrogels J.Nanotechnol. Eng. Med 1 2010 011007-011006
    • (2010) J.Nanotechnol. Eng. Med , vol.1
    • Zhang, H.1    Luo, H.2    Zhao, X.3
  • 9
    • 65249179551 scopus 로고    scopus 로고
    • Designed amphiphilic peptide forms stable nanoweb, slowly releases encapsulated hydrophobic drug, and accelerates animal hemostasis
    • L.P. Ruan, and H.Y. Zhang X. Zhao Designed amphiphilic peptide forms stable nanoweb, slowly releases encapsulated hydrophobic drug, and accelerates animal hemostasis Proc. Natl. Acad. Sci. USA 106 2009 5105 5110
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5105-5110
    • Ruan, L.P.1    Zhang, H.Y.2    Zhao, X.3
  • 10
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini, and E. Giannoni M. Stefani Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Stefani, M.3
  • 11
    • 39649085356 scopus 로고    scopus 로고
    • Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-I
    • Z. Ye, and H. Zhang X. Zhao Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-I J. Pept. Sci. 14 2008 152 162
    • (2008) J. Pept. Sci. , vol.14 , pp. 152-162
    • Ye, Z.1    Zhang, H.2    Zhao, X.3
  • 12
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • R. Kayed, and E. Head C.G. Glabe Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Glabe, C.G.3
  • 13
    • 78650763561 scopus 로고    scopus 로고
    • Membrane permeabilization by oligomeric α-synuclein: In search of the mechanism
    • B.D. van Rooijen, M.M. Claessens, and V. Subramaniam Membrane permeabilization by oligomeric α-synuclein: in search of the mechanism PLoS ONE 5 2010 e14292
    • (2010) PLoS ONE , vol.5 , pp. 14292
    • Van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 14
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • K.A. Conway, and S.J. Lee P.T. Lansbury Jr. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy Proc. Natl. Acad. Sci. USA 97 2000 571 576
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Lansbury, Jr.P.T.3
  • 15
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • K.A. Conway, J.D. Harper, and P.T. Lansbury Jr. Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid Biochemistry 39 2000 2552 2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, Jr.P.T.3
  • 16
    • 0037072284 scopus 로고    scopus 로고
    • Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • T.T. Ding, and S.J. Lee P.T. Lansbury Jr. Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes Biochemistry 41 2002 10209 10217
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Lansbury, Jr.P.T.3
  • 17
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • H.A. Lashuel, and B.M. Petre 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
    • (2002) J. Mol. Biol. , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Lansbury, Jr.P.T.3
  • 18
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • H.A. Lashuel, and D. Hartley P.T. Lansbury Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 418 2002 291
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Lansbury, Jr.P.T.3
  • 19
    • 63249103989 scopus 로고    scopus 로고
    • Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer
    • R. Kayed, and A. Pensalfini C. Glabe Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer J. Biol. Chem. 284 2009 4230 4237
    • (2009) J. Biol. Chem. , vol.284 , pp. 4230-4237
    • Kayed, R.1    Pensalfini, A.2    Glabe, C.3
  • 20
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and a pathogenic (E22G) form of Aβ40 in vitro accumulate protofibrils, including amyloid pores
    • H.A. Lashuel, and D.M. Hartley P.T. Lansbury Jr. Mixtures of wild-type and a pathogenic (E22G) form of Aβ40 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    Lansbury, Jr.P.T.3
  • 21
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • H. Lin, R. Bhatia, and R. Lal Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology FASEB J. 15 2001 2433 2444
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 22
    • 0142040121 scopus 로고    scopus 로고
    • Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein
    • F. Sokolowski, and A.J. Modler D. Naumann Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein J. Biol. Chem. 278 2003 40481 40492
    • (2003) J. Biol. Chem. , vol.278 , pp. 40481-40492
    • Sokolowski, F.1    Modler, A.J.2    Naumann, D.3
  • 23
    • 0141653970 scopus 로고    scopus 로고
    • The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies
    • Y. Porat, and S. Kolusheva E. Gazit The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies Biochemistry 42 2003 10971 10977
    • (2003) Biochemistry , vol.42 , pp. 10971-10977
    • Porat, Y.1    Kolusheva, S.2    Gazit, E.3
  • 24
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • H.A. Lashuel, and P.T. Lansbury Jr. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q. Rev. Biophys. 39 2006 167 201
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, Jr.P.T.2
  • 25
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: A common structural link for protein-misfolding disease
    • A. Quist, and I. Doudevski R. Lal Amyloid ion channels: a common structural link for protein-misfolding disease Proc. Natl. Acad. Sci. USA 102 2005 10427 10432
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lal, R.3
  • 26
    • 72549099399 scopus 로고    scopus 로고
    • Misfolded amyloid ion channels present mobile β-sheet subunits in contrast to conventional ion channels
    • H. Jang, and F.T. Arce R. Nussinov Misfolded amyloid ion channels present mobile β-sheet subunits in contrast to conventional ion channels Biophys. J. 97 2009 3029 3037
    • (2009) Biophys. J. , vol.97 , pp. 3029-3037
    • Jang, H.1    Arce, F.T.2    Nussinov, R.3
  • 27
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of α-synuclein oligomers stabilized by the flavonoid baicalein
    • D.-P. Hong, A.L. Fink, and V.N. Uversky Structural characteristics of α-synuclein oligomers stabilized by the flavonoid baicalein J. Mol. Biol. 383 2008 214 223
    • (2008) J. Mol. Biol. , vol.383 , pp. 214-223
    • Hong, D.-P.1    Fink, A.L.2    Uversky, V.N.3
  • 28
    • 33644527256 scopus 로고    scopus 로고
    • Characterization of oligomers during α-synuclein aggregation using intrinsic tryptophan fluorescence
    • A. Dusa, and J. Kaylor A.L. Fink Characterization of oligomers during α-synuclein aggregation using intrinsic tryptophan fluorescence Biochemistry 45 2006 2752 2760
    • (2006) Biochemistry , vol.45 , pp. 2752-2760
    • Dusa, A.1    Kaylor, J.2    Fink, A.L.3
  • 29
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim. Biophys. Sin. (Shanghai) 39 2007 549 559
    • (2007) Acta Biochim. Biophys. Sin. (Shanghai) , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 30
    • 78649808726 scopus 로고    scopus 로고
    • Negative staining and cryo-negative staining of macromolecules and viruses for TEM
    • S. De Carlo, and J.R. Harris Negative staining and cryo-negative staining of macromolecules and viruses for TEM Micron 42 2011 117 131
    • (2011) Micron , vol.42 , pp. 117-131
    • De Carlo, S.1    Harris, J.R.2
  • 32
    • 38949167084 scopus 로고    scopus 로고
    • New structures help the modeling of toxic amyloidβ ion channels
    • H.B. Jang, and J. Zheng R. Nussinov New structures help the modeling of toxic amyloidβ ion channels Trends Biochem. Sci. 33 2008 91 100
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 91-100
    • Jang, H.B.1    Zheng, J.2    Nussinov, R.3
  • 33
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β 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-β protein Chem. Biol. 4 1997 951 959
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, Jr.P.T.3
  • 34
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • M.P. Lambert, and A.K. Barlow W.L. Klein Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins Proc. Natl. Acad. Sci. USA 95 1998 6448 6453
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Klein, W.L.3
  • 35
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • D.M. Walsh, and A. Lomakin 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    Teplow, D.B.3
  • 37
    • 15444373250 scopus 로고    scopus 로고
    • Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
    • R.M. Rasia, and C.W. Bertoncini C.O. Fernández Structural characterization of copper(II) binding to α-synuclein: insights into the bioinorganic chemistry of Parkinson's disease Proc. Natl. Acad. Sci. USA 102 2005 4294 4299
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4294-4299
    • Rasia, R.M.1    Bertoncini, C.W.2    Fernández, C.O.3
  • 38
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • V.N. Uversky, J. Li, and A.L. Fink Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure J. Biol. Chem. 276 2001 44284 44296
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.