메뉴 건너뛰기




Volumn 7, Issue 8, 2012, Pages

Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; BAICALEIN; IRON; PORIN;

EID: 84864538288     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0042545     Document Type: Article
Times cited : (71)

References (31)
  • 1
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert M, (2001) Alpha-synuclein and neurodegenerative diseases. Nat Rev Neurosci 2: 492-501.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA, (2004) Protein aggregation and neurodegenerative disease. Nat Med 10: S10-S17.
    • (2004) Nat Med , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 4
    • 0242668337 scopus 로고    scopus 로고
    • Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis. Science 300: 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 5
    • 33644861975 scopus 로고    scopus 로고
    • Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
    • Glabe CG, Kayed R, (2006) Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology 66: S74-S78.
    • (2006) Neurology , vol.66
    • Glabe, C.G.1    Kayed, R.2
  • 6
    • 48149108245 scopus 로고    scopus 로고
    • Protein Aggregation in the Brain: The Molecular Basis for Alzheimer's and Parkinson's Diseases
    • Irvine GB, El Agnaf OM, Shankar GM, Walsh DM, (2008) Protein Aggregation in the Brain: The Molecular Basis for Alzheimer's and Parkinson's Diseases. Mol Med 14: 451-464.
    • (2008) Mol Med , vol.14 , pp. 451-464
    • Irvine, G.B.1    El Agnaf, O.M.2    Shankar, G.M.3    Walsh, D.M.4
  • 7
    • 0037073748 scopus 로고    scopus 로고
    • Golgi Fragmentation Occurs in the Cells with Prefibrillar alpha-Synuclein Aggregates and Precedes the Formation of Fibrillar Inclusion
    • Gosavi N, Lee HJ, Lee JS, Patel S, Lee SJ, (2002) Golgi Fragmentation Occurs in the Cells with Prefibrillar alpha-Synuclein Aggregates and Precedes the Formation of Fibrillar Inclusion. J Biol Chem 277: 48984-48992.
    • (2002) J Biol Chem , vol.277 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 8
    • 77958450202 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1
    • Kamp F, Exner N, Lutz AK, Wender N, Hegermann J, et al. (2010) Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1. EMBO J 29: 3571-3589.
    • (2010) EMBO J , vol.29 , pp. 3571-3589
    • Kamp, F.1    Exner, N.2    Lutz, A.K.3    Wender, N.4    Hegermann, J.5
  • 9
    • 0023804321 scopus 로고
    • Increased iron (III) and total iron content in post mortem substantia nigra of parkinsonian brain
    • Sofic E, Riederer P, Heinsen H, Beckmann H, Reynolds GP, et al. (1988) Increased iron (III) and total iron content in post mortem substantia nigra of parkinsonian brain. J Neural Transm 74: 199-205.
    • (1988) J Neural Transm , vol.74 , pp. 199-205
    • Sofic, E.1    Riederer, P.2    Heinsen, H.3    Beckmann, H.4    Reynolds, G.P.5
  • 10
    • 44849084558 scopus 로고    scopus 로고
    • Single Particle Characterization of Iron-induced Pore-forming α-synuclein Oligomers
    • Kostka M, Hogen T, Danzer KM, Levin J, Habeck M, et al. (2008) Single Particle Characterization of Iron-induced Pore-forming α-synuclein Oligomers. J Biol Chem 283: 10992-11003.
    • (2008) J Biol Chem , vol.283 , pp. 10992-11003
    • Kostka, M.1    Hogen, T.2    Danzer, K.M.3    Levin, J.4    Habeck, M.5
  • 11
    • 72949089048 scopus 로고    scopus 로고
    • Converse modulation of toxic α-synuclein oligomers in living cells by N′-benzylidene-benzohydrazide derivates and ferric iron
    • Hillmer A, Putcha P, Levin J, Högen T, Hyman BT, et al. (2010) Converse modulation of toxic α-synuclein oligomers in living cells by N′-benzylidene-benzohydrazide derivates and ferric iron. Biochem Biophys Res Commun 391: 461-466.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 461-466
    • Hillmer, A.1    Putcha, P.2    Levin, J.3    Högen, T.4    Hyman, B.T.5
  • 12
    • 79955671013 scopus 로고    scopus 로고
    • AMPA-receptor mediated excitatory synaptic transmission is enhanced by iron-induced α-synuclein oligomers
    • Hüls S, Högen T, Vasallo N, Danzer K, Hengerer B, et al. (2011) AMPA-receptor mediated excitatory synaptic transmission is enhanced by iron-induced α-synuclein oligomers. J Neurochem 117: 868-878.
    • (2011) J Neurochem , vol.117 , pp. 868-878
    • Hüls, S.1    Högen, T.2    Vasallo, N.3    Danzer, K.4    Hengerer, B.5
  • 13
    • 80054849102 scopus 로고    scopus 로고
    • Generation of Ferric Iron Links Oxidative Stress to α-Synuclein Oligomer Formation
    • Levin J, Högen T, Hillmer A, Bader B, Schmidt F, et al. (2011) Generation of Ferric Iron Links Oxidative Stress to α-Synuclein Oligomer Formation. Journal of Parkinson's Disease 1: 205-216.
    • (2011) Journal of Parkinson's Disease , vol.1 , pp. 205-216
    • Levin, J.1    Högen, T.2    Hillmer, A.3    Bader, B.4    Schmidt, F.5
  • 14
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel HA, Lansbury PT Jr, (2006) Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q Rev Biophys 39: 167-201.
    • (2006) Q Rev Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury Jr., P.T.2
  • 16
    • 78650763561 scopus 로고    scopus 로고
    • Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism
    • van Rooijen BD, Claessens MMAE, Subramaniam V, (2010) Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism. PLoS ONE 5: e14292.
    • (2010) PLoS ONE , vol.5
    • van Rooijen, B.D.1    Claessens, M.M.A.E.2    Subramaniam, V.3
  • 17
    • 82555170657 scopus 로고    scopus 로고
    • Mechanism of Membrane Interaction and Disruption by α-Synuclein
    • Reynolds NP, Soragni A, Rabe M, Verdes D, Liverani E, et al. (2011) Mechanism of Membrane Interaction and Disruption by α-Synuclein. J Am Chem Soc 133: 19366-19375.
    • (2011) J Am Chem Soc , vol.133 , pp. 19366-19375
    • Reynolds, N.P.1    Soragni, A.2    Rabe, M.3    Verdes, D.4    Liverani, E.5
  • 18
    • 2542461043 scopus 로고    scopus 로고
    • α-Synuclein Has a High Affinity for Packing Defects in a Bilayer Membrane
    • Nuscher B, Kamp F, Mehnert T, Odoy S, Haass C, et al. (2004) α-Synuclein Has a High Affinity for Packing Defects in a Bilayer Membrane. J Biol Chem 21: 21966-21975.
    • (2004) J Biol Chem , vol.21 , pp. 21966-21975
    • Nuscher, B.1    Kamp, F.2    Mehnert, T.3    Odoy, S.4    Haass, C.5
  • 19
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils
    • Zhu M, Rajamani S, Kaylor J, Han S, Zhou F, et al. (2004) The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils. J Biol Chem 279: 26846-26857.
    • (2004) J Biol Chem , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5
  • 20
    • 0000559465 scopus 로고
    • Reconstitution of Cell Membrane Structure in vitro and its Transformation into an Excitable System
    • Mueller P, Rudin DO, Tien HT, Wescott WC, (1962) Reconstitution of Cell Membrane Structure in vitro and its Transformation into an Excitable System. Nature 194: 979-980.
    • (1962) Nature , vol.194 , pp. 979-980
    • Mueller, P.1    Rudin, D.O.2    Tien, H.T.3    Wescott, W.C.4
  • 21
    • 84859386811 scopus 로고    scopus 로고
    • Two different binding modes of α-Synuclein to lipid vesicles depending on its aggregation state
    • Högen T, Levin J, Schmidt F, Caruana M, Vasallo N, et al. (2012) Two different binding modes of α-Synuclein to lipid vesicles depending on its aggregation state. Biophys J 102.
    • (2012) Biophys J , vol.102
    • Högen, T.1    Levin, J.2    Schmidt, F.3    Caruana, M.4    Vasallo, N.5
  • 22
    • 84864068694 scopus 로고    scopus 로고
    • Polyphenolic compounds are novel protective agents against lipid membrane damage by α-synuclein aggregates in vitro
    • Caruana M, Neuner J, Högen T, Schmidt F, Kamp F, et al. (2012) Polyphenolic compounds are novel protective agents against lipid membrane damage by α-synuclein aggregates in vitro. Biochim Biophys Acta.
    • (2012) Biochim Biophys Acta
    • Caruana, M.1    Neuner, J.2    Högen, T.3    Schmidt, F.4    Kamp, F.5
  • 23
    • 84872828850 scopus 로고    scopus 로고
    • Causal therapy of Parkinson's disease with anle138b, a novel protein aggregation inhibitor
    • Levin J, Wagner J, Ryazanov S, Leonov A, Shi S, et al. (2011) Causal therapy of Parkinson's disease with anle138b, a novel protein aggregation inhibitor. Mov Disord 26: S21.
    • (2011) Mov Disord , vol.26
    • Levin, J.1    Wagner, J.2    Ryazanov, S.3    Leonov, A.4    Shi, S.5
  • 24
    • 0021795850 scopus 로고
    • Ion Selectivity of Gram-Negative Bacterial Porins
    • Benz R, Schmid A, Hancock REW, (1985) Ion Selectivity of Gram-Negative Bacterial Porins. J Bacteriol 162: 722-727.
    • (1985) J Bacteriol , vol.162 , pp. 722-727
    • Benz, R.1    Schmid, A.2    Hancock, R.E.W.3
  • 25
    • 0030841732 scopus 로고    scopus 로고
    • Function and modulation of bacterial porins: insights from electrophysiology
    • Delcour AH, (1997) Function and modulation of bacterial porins: insights from electrophysiology. FEMS Microbiol Lett 151: 115-123.
    • (1997) FEMS Microbiol Lett , vol.151 , pp. 115-123
    • Delcour, A.H.1
  • 26
    • 0021813542 scopus 로고
    • Characterization of channels induced in planar bilayer membranes by detergent solubilised Eschericha coli porins
    • Lakey JH, Watts JP, Lea EJA, (1985) Characterization of channels induced in planar bilayer membranes by detergent solubilised Eschericha coli porins. Biochim Biophys Acta 817: 208-216.
    • (1985) Biochim Biophys Acta , vol.817 , pp. 208-216
    • Lakey, J.H.1    Watts, J.P.2    Lea, E.J.A.3
  • 27
    • 0027476160 scopus 로고
    • Asymmetry of orientation and voltage gating of the Acidovorax delafieldii porin Omp34 in lipid bilayers
    • Brunen M, Engelhardt H, (1993) Asymmetry of orientation and voltage gating of the Acidovorax delafieldii porin Omp34 in lipid bilayers. Eur J Biochem 212: 129-135.
    • (1993) Eur J Biochem , vol.212 , pp. 129-135
    • Brunen, M.1    Engelhardt, H.2
  • 29
    • 22244463206 scopus 로고    scopus 로고
    • Nanopore Unitary Permeability Measured by Electrochemical and Optical Single Transporter Recording
    • Hemmler R, Böse G, Wagner R, Peters R, (2005) Nanopore Unitary Permeability Measured by Electrochemical and Optical Single Transporter Recording. Biophys J 88: 4000-4007.
    • (2005) Biophys J , vol.88 , pp. 4000-4007
    • Hemmler, R.1    Böse, G.2    Wagner, R.3    Peters, R.4
  • 30
    • 0024505102 scopus 로고
    • Pore Formation by the Eschericha coli Hemolysin: Evidence for an Association-Dissociation Equilibrium of the Pore-Forming Aggregates
    • Benz R, Schmid A, Wagner W, Goebel W, (1989) Pore Formation by the Eschericha coli Hemolysin: Evidence for an Association-Dissociation Equilibrium of the Pore-Forming Aggregates. Infect Immun 57: 887-895.
    • (1989) Infect Immun , vol.57 , pp. 887-895
    • Benz, R.1    Schmid, A.2    Wagner, W.3    Goebel, W.4
  • 31
    • 0030447720 scopus 로고    scopus 로고
    • Structure of Stapphylococcal alpha-Hemolysin, a Hemptameric Transmembrane Pore
    • Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, et al. (1996) Structure of Stapphylococcal alpha-Hemolysin, a Hemptameric Transmembrane Pore. Science 274: 1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.