메뉴 건너뛰기




Volumn 5, Issue 2, 2015, Pages 282-305

Seeking a mechanism for the toxicity of oligomeric α-synuclein

Author keywords

Aggregation; Amyloid fibrils; Neurodegeneration; Parkinson s disease; Toxic oligomers; synuclein

Indexed keywords

CELL DEATH; CELL DISRUPTION; CELL MEMBRANE DEPOLARIZATION; CYTOLYSIS; CYTOSOLIC FRACTION; CYTOTOXICITY; DEGENERATIVE DISEASE; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ENDOPLASMIC RETICULUM STRESS; EXPERIMENTAL MODEL; GEL PERMEATION CHROMATOGRAPHY; GENE EXPRESSION; GENE MUTATION; HUMAN; INFRARED SPECTROSCOPY; MEMBRANE PERMEABILITY; MOLECULAR DYNAMICS; NERVOUS SYSTEM INFLAMMATION; OLIGOMERIZATION; OXIDATIVE STRESS; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN INTERACTION; REVIEW; SIGNAL TRANSDUCTION; SOLUBILITY; UNFOLDED PROTEIN RESPONSE; ANIMAL; GENETICS; METABOLISM; MUTATION; PROTEIN MULTIMERIZATION; PROTEINOSIS;

EID: 85012093582     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5020282     Document Type: Review
Times cited : (180)

References (121)
  • 1
    • 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
    • Conway, K.A.; Lee, S.; Rochet, J.; Ding, T.T.; Williamson, R.E.; Lansbury, P.T. 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. PNAS 2000, 97, 571–576.
    • (2000) Implications for Pathogenesis and Therapy. PNAS , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.2    Rochet, J.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 2
  • 4
    • 84883174947 scopus 로고    scopus 로고
    • Parkinson’s disease dementia: Convergence of α-synuclein, tau and amyloid-β pathologies
    • Irwin, D.J.; Lee, V.M.-Y.; Trojanowski, J.Q. Parkinson’s disease dementia: Convergence of α-synuclein, tau and amyloid-β pathologies. Nat. Rev. Neurosci. 2013, 14, 626–636.
    • (2013) Nat. Rev. Neurosci , vol.14 , pp. 626-636
    • Irwin, D.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 5
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of α-synuclein: From structure and toxicity to therapeutic target
    • Lashuel, H.A.; Overk, C.R.; Oueslati, A.; Masliah, E. The many faces of α-synuclein: From structure and toxicity to therapeutic target. Nat. Rev. Neurosci. 2013, 14, 38–48.
    • (2013) Nat. Rev. Neurosci , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 6
    • 0033919992 scopus 로고    scopus 로고
    • Lewy bodies in Alzheimer’s disease: A neuropathological review of 145 cases using alpha-synuclein immunohistochemistry
    • Hamilton, R.L. Lewy bodies in Alzheimer’s disease: A neuropathological review of 145 cases using alpha-synuclein immunohistochemistry. Brain Pathol. 2000, 10, 378–384.
    • (2000) Brain Pathol , vol.10 , pp. 378-384
    • Hamilton, R.L.1
  • 7
    • 0037383760 scopus 로고    scopus 로고
    • Regional distribution of alpha-synuclein pathology in unimpaired aging and Alzheimer disease
    • Parkkinen, L.; Soininen, H.; Alafuzoff, I. Regional distribution of alpha-synuclein pathology in unimpaired aging and Alzheimer disease. J. Neuropathol. Exp. Neurol. 2003, 62, 363–367.
    • (2003) J. Neuropathol. Exp. Neurol. , vol.62 , pp. 363-367
    • Parkkinen, L.1    Soininen, H.2    Alafuzoff, I.3
  • 8
    • 7944238570 scopus 로고    scopus 로고
    • Lewy body-related alpha-synucleinopathy in the aged human brain
    • Jellinger, K.A. Lewy body-related alpha-synucleinopathy in the aged human brain. J. Neural Transm. 2004, 111, 1219–1235.
    • (2004) J. Neural Transm , vol.111 , pp. 1219-1235
    • Jellinger, K.A.1
  • 12
    • 84879601960 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein mutations
    • Kasten, M.; Klein, C. The many faces of alpha-synuclein mutations. Mov. Disord. 2013, 28, 697–701.
    • (2013) Mov. Disord , vol.28 , pp. 697-701
    • Kasten, M.1    Klein, C.2
  • 19
    • 34250796802 scopus 로고    scopus 로고
    • The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states
    • Fredenburg, R.A.; Rospigliosi, C.; Meray, R.K.; Kessler, J.C.; Lashuel, H.A.; Eliezer, D.; Lansbury, P.T.J. The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states. Biochemistry 2007, 46, 7107–7118.
    • (2007) Biochemistry , vol.46 , pp. 7107-7118
    • Fredenburg, R.A.1    Rospigliosi, C.2    Meray, R.K.3    Kessler, J.C.4    Lashuel, H.A.5    Eliezer, D.6    Lansbury, P.7
  • 21
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson’s Disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein
    • Li, J.; Uversky, V.N.; Fink, A.L. Effect of familial Parkinson’s Disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein. Biochemistry 2001, 40, 11604–11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 23
    • 77951842993 scopus 로고    scopus 로고
    • Methylation regulates alpha-synuclein expression and is decreased in Parkinson’s disease patients’ brains
    • Jowaed, A.; Schmitt, I.; Kaut, O.; Wüllner, U. Methylation regulates alpha-synuclein expression and is decreased in Parkinson’s disease patients’ brains. J. Neurosci. 2010, 30, 6355–6359.
    • (2010) J. Neurosci , vol.30 , pp. 6355-6359
    • Jowaed, A.1    Schmitt, I.2    Kaut, O.3    Wüllner, U.4
  • 24
    • 63449129338 scopus 로고    scopus 로고
    • Physiological and pathological role of alpha-synuclein in Parkinson’s disease through iron mediated oxidative stress; the role of a putative iron-responsive element
    • Olivares, D.; Huang, X.; Branden, L.; Greig, N.H.; Rogers, J.T. Physiological and pathological role of alpha-synuclein in Parkinson’s disease through iron mediated oxidative stress; the role of a putative iron-responsive element. Int. J. Mol. Sci. 2009, 10, 1226–1260.
    • (2009) Int. J. Mol. Sci , vol.10 , pp. 1226-1260
    • Olivares, D.1    Huang, X.2    Branden, L.3    Greig, N.H.4    Rogers, J.T.5
  • 25
    • 84907699043 scopus 로고    scopus 로고
    • Transglutaminase 2 exacerbates α-synuclein toxicity in mice and yeast
    • Grosso, H.; Woo, J.M.; Lee, K.W.; Im, J.Y.; Masliah, E.; Junn, E.; Mouradian, M.M. Transglutaminase 2 exacerbates α-synuclein toxicity in mice and yeast. FASEB J. 2014, 28, 4280–4291.
    • (2014) FASEB J , vol.28 , pp. 4280-4291
    • Grosso, H.1    Woo, J.M.2    Lee, K.W.3    Im, J.Y.4    Masliah, E.5    Junn, E.6    Mouradian, M.M.7
  • 26
    • 84859577559 scopus 로고    scopus 로고
    • α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer
    • Fauvet, B.; Mbefo, M.K.; Fares, M.-B.; Desobry, C.; Michael, S.; Ardah, M.T.; Tsika, E.; Coune, P.; Prudent, M.; Lion, N; et al. α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. J. Biol. Chem. 2012, 287, 15345–15364.
    • (2012) J. Biol. Chem. , vol.287 , pp. 15345-15364
    • Fauvet, B.1    Mbefo, M.K.2    Fares, M.-B.3    Desobry, C.4    Michael, S.5    Ardah, M.T.6    Tsika, E.7    Coune, P.8    Prudent, M.9    Lion, N.10
  • 27
    • 83455202793 scopus 로고    scopus 로고
    • α-synuclein misfolding and Parkinson’s disease. Biochim.Biophys
    • Breydo, L.; Wu, J.W.; Uversky, V.N. α-synuclein misfolding and Parkinson’s disease. Biochim.Biophys. Acta 2012, 1822, 261–285.
    • (2012) Acta , vol.1822 , pp. 261-285
    • Breydo, L.1    Wu, J.W.2    Uversky, V.N.3
  • 29
    • 84892794505 scopus 로고    scopus 로고
    • The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
    • Lorenzen, N.; Lemminger, L.; Pedersen, J.N.; Nielsen, S.B.; Otzen, D.E. The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. FEBS Lett. 2014, 588, 497–502.
    • (2014) FEBS Lett , vol.588 , pp. 497-502
    • Lorenzen, N.1    Lemminger, L.2    Pedersen, J.N.3    Nielsen, S.B.4    Otzen, D.E.5
  • 30
    • 77958455514 scopus 로고    scopus 로고
    • Rhoades, E. Effects of curvature and composition on α-synuclein binding to lipid vesicles
    • Middleton, E.R.; Rhoades, E. Effects of curvature and composition on α-synuclein binding to lipid vesicles. Biophys. J. 2010, 99, 2279–2288.
    • (2010) Biophys. J. , vol.99 , pp. 2279-2288
    • Middleton, E.R.1
  • 31
    • 84884250340 scopus 로고    scopus 로고
    • The function of α-synuclein
    • Bendor, J.T.; Logan, T.P.; Edwards, R.H. The function of α-synuclein. Neuron 2013, 79, 1044–1066.
    • (2013) Neuron , vol.79 , pp. 1044-1066
    • Bendor, J.T.1    Logan, T.P.2    Edwards, R.H.3
  • 33
    • 84919449363 scopus 로고    scopus 로고
    • α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation
    • Burré, J.; Sharma, M.; Südhof, T.C. α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation. Proc. Natl. Acad. Sci. USA 2014, 111, 4274–4283.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 4274-4283
    • Burré, J.1    Sharma, M.2    Südhof, T.C.3
  • 34
    • 78650763561 scopus 로고    scopus 로고
    • Membrane permeabilization byoligomeric α-synuclein: In search of the mechanism
    • Van Rooijen, B.D.; Claessens, M.M.A.E.; Subramaniam, V. Membrane permeabilization byoligomeric α-synuclein: In search of the mechanism. PLOS ONE 2010, 5, e14292.
    • (2010) PLOS ONE , vol.5
    • Van Rooijen, B.D.1    Claessens, M.2    Subramaniam, V.3
  • 35
    • 84880521916 scopus 로고    scopus 로고
    • α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling
    • Ouberai, M.M.; Wang, J.; Swann, M.J.; Galvagnion, C.; Guilliams, T.; Dobson, C.M.; Welland, M.E. α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling. J. Biol. Chem. 2013, 288, 20883–20895.
    • (2013) J. Biol. Chem , vol.288 , pp. 20883-20895
    • Ouberai, M.M.1    Wang, J.2    Swann, M.J.3    Galvagnion, C.4    Guilliams, T.5    Dobson, C.M.6    Welland, M.E.7
  • 36
    • 77956571912 scopus 로고    scopus 로고
    • Redox reactions of the α-synuclein-Cu2+ complex and their effects on neuronal cell viability
    • Wang, C.; Liu, L.; Zhang, L.; Peng, Y.; Zhou, F. Redox reactions of the α-synuclein-Cu2+ complex and their effects on neuronal cell viability. Biochemistry 2011, 49, 323–343.
    • (2011) Biochemistry , vol.49 , pp. 323-343
    • Wang, C.1    Liu, L.2    Zhang, L.3    Peng, Y.4    Zhou, F.5
  • 39
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza, J.M.; Giasson, B.I.; Chen, Q.; Lee, V.M.; Ischiropoulos, H. Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 2000, 275, 18344–18349.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 40
    • 84886777232 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding assessed with single molecule AFM force spectroscopy: Effect of pathogenic mutations
    • Krasnoslobodtsev, A.V.; Volkov, I.L.; Asiago, J.M.; Hindupur, J.; Rochet, J.-C.; Lyubchenko, Y.L. Alpha-synuclein misfolding assessed with single molecule AFM force spectroscopy: Effect of pathogenic mutations. Biochemistry 2013, 52, 1–22.
    • (2013) Biochemistry , vol.52 , pp. 1-22
    • Krasnoslobodtsev, A.V.1    Volkov, I.L.2    Asiago, J.M.3    Hindupur, J.4    Rochet, J.-C.5    Lyubchenko, Y.L.6
  • 42
    • 80052398365 scopus 로고    scopus 로고
    • α-synuclein occurs as a helically folded tetramer that resists aggregation
    • Bartels, T.; Choi, J.G.; Selkoe, D.J. α-synuclein occurs as a helically folded tetramer that resists aggregation. Nature 2012, 477, 107–110.
    • (2012) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 43
    • 84874769548 scopus 로고    scopus 로고
    • In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells
    • Dettmer, U.; Newman, A.J.; Luth, E.S.; Bartels, T.; Selkoe, D. In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells. J. Biol. Chem. 2013, 288, 6371–6385.
    • (2013) J. Biol. Chem , vol.288 , pp. 6371-6385
    • Dettmer, U.1    Newman, A.J.2    Luth, E.S.3    Bartels, T.4    Selkoe, D.5
  • 48
    • 0036415838 scopus 로고    scopus 로고
    • α-Synuclein, especially the Parkinson’s disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel, H.A.; Petre, B.M.; Wall, J.; Simon, M.; Nowak, R.J.; Walz, T.; Lansbury, P.T. α-Synuclein, especially the Parkinson’s disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 2002, 322, 1089–1102.
    • (2002) J. Mol. Biol , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury, P.T.7
  • 51
    • 65249162241 scopus 로고    scopus 로고
    • Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies
    • Paleologou, K.E.; Kragh, C.L.; Mann, D.M.A.; Salem, S.A.; Al-Shami, R.; Allsop, D.; Hassan, A.H.; Jensen, P.H.; El-Agnaf, O.M.A. Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain 2009, 132, 1093–1101.
    • (2009) Brain , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1    Kragh, C.L.2    Mann, D.3    Salem, S.A.4    Al-Shami, R.5    Allsop, D.6    Hassan, A.H.7    Jensen, P.H.8    El-Agnaf, O.9
  • 52
    • 65549114936 scopus 로고    scopus 로고
    • Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core
    • Van Rooijen, B.D.; Claessens, M.M.A.E.; Subramaniam, V. Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core. Biochim. Biophys. Acta 2009, 1788, 1271–1278.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1271-1278
    • Van Rooijen, B.D.1    Claessens, M.2    Subramaniam, V.3
  • 56
    • 84879229182 scopus 로고    scopus 로고
    • In vitro study of α-synuclein protofibrils by cryo-EM suggests a Cu2+-dependent aggregation pathway
    • Zhang, H.; Griggs, A.; Rochet, J.-C.; Stanciu, L.A. In vitro study of α-synuclein protofibrils by cryo-EM suggests a Cu2+-dependent aggregation pathway. Biophys. J. 2013, 104, 2706–2713.
    • (2013) Biophys. J , vol.104 , pp. 2706-2713
    • Zhang, H.1    Griggs, A.2    Rochet, J.-C.3    Stanciu, L.A.4
  • 57
    • 84887124634 scopus 로고    scopus 로고
    • The interplay between lipids and dopamine on α-synuclein oligomerization and membrane binding
    • Pham, C.L.L.; Cappai, R. The interplay between lipids and dopamine on α-synuclein oligomerization and membrane binding. Biosci. Rep. 2013, 33, 807–814.
    • (2013) Biosci. Rep , vol.33 , pp. 807-814
    • Pham, C.1    Cappai, R.2
  • 58
    • 68849102707 scopus 로고    scopus 로고
    • Unique copper-induced oligomers mediate alpha-synuclein toxicity
    • Wright, J.A.; Wang, X.; Brown, D.R. Unique copper-induced oligomers mediate alpha-synuclein toxicity. FASEB J. 2009, 23, 2384–2393.
    • (2009) FASEB J , vol.23 , pp. 2384-2393
    • Wright, J.A.1    Wang, X.2    Brown, D.R.3
  • 59
    • 77950644314 scopus 로고    scopus 로고
    • Copper binding regulates intracellular alpha-synuclein localisation, aggregation and toxicity
    • Wang, X.; Moualla, D.; Wright, J.A.; Brown, D.R. Copper binding regulates intracellular alpha-synuclein localisation, aggregation and toxicity. J. Neurochem. 2010, 113, 704–714.
    • (2010) J. Neurochem , vol.113 , pp. 704-714
    • Wang, X.1    Moualla, D.2    Wright, J.A.3    Brown, D.R.4
  • 64
    • 84858441755 scopus 로고    scopus 로고
    • Role of alpha-synuclein penetration into the membrane in the mechanisms of oligomer pore formation
    • Tsigelny, I.F.; Sharikov, Y.; Wrasidlo, W.; Gonzalez, T.; Desplats, P.A.; Spencer, B.; Masliah, E. Role of alpha-synuclein penetration into the membrane in the mechanisms of oligomer pore formation. FEBS J. 2012, 279, 1000–1013.
    • (2012) FEBS J , vol.279 , pp. 1000-1013
    • Tsigelny, I.F.1    Sharikov, Y.2    Wrasidlo, W.3    Gonzalez, T.4    Desplats, P.A.5    Spencer, B.6    Masliah, E.7
  • 65
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems
    • Butterfield, S.M.; Lashuel, H.A. Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems. Angew. Chem. Int. Ed. Engl. 2010, 49, 5628–5654.
    • (2010) Angew. Chem. Int. Ed. Engl , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 66
    • 84864538288 scopus 로고    scopus 로고
    • Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes
    • Schmidt, F.; Levin, J.; Kamp, F.; Kretzschmar, H.; Giese, A.; Bötzel, K. Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes. PLOS ONE 2012, 7, e42545.
    • (2012) PLOS ONE , pp. 7
    • Schmidt, F.1    Levin, J.2    Kamp, F.3    Kretzschmar, H.4    Giese, A.5    Bötzel, K.6
  • 67
    • 36249023636 scopus 로고    scopus 로고
    • Pore-forming proteins share structural and functional homology with amyloid oligomers
    • Yoshiike, Y.; Kayed, R.; Milton, S.C.; Takashima, A.; Glabe, C.G. Pore-forming proteins share structural and functional homology with amyloid oligomers. Neuromol. Med. 2007, 9, 270–275.
    • (2007) Neuromol. Med , vol.9 , pp. 270-275
    • Yoshiike, Y.1    Kayed, R.2    Milton, S.C.3    Takashima, A.4    Glabe, C.G.5
  • 68
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed, R.; Sokolov, Y.; Edmonds, B.; McIntire, T.M.; Milton, S.C.; Hall, J.E.; Glabe, C.G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 2004, 279, 46363–46366.
    • (2004) J. Biol. Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 69
    • 33751516396 scopus 로고    scopus 로고
    • Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure
    • Sokolov, Y.; Kozak, J.A.; Kayed, R.; Chanturiya, A.; Glabe, C.; Hall, J.E. Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure. J. Gen. Physiol. 2006, 128, 637–647.
    • (2006) J. Gen. Physiol , vol.128 , pp. 637-647
    • Sokolov, Y.1    Kozak, J.A.2    Kayed, R.3    Chanturiya, A.4    Glabe, C.5    Hall, J.E.6
  • 71
    • 84876891740 scopus 로고    scopus 로고
    • α-Synuclein oligomers: An amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions
    • Zijlstra, N.; Subramaniam, V. α-Synuclein oligomers: An amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions. Mol. Neurobiol. 2013, 47, 613–621.
    • (2013) Mol. Neurobiol , vol.47 , pp. 613-621
    • Zijlstra, N.1    Subramaniam, V.2
  • 72
    • 82655175456 scopus 로고    scopus 로고
    • Kinetic measurements give new insights into lipid membrane permeabilization by α-synuclein oligomers
    • Stöckl, M.; Claessens, M.M.A.E.; Subramaniam, V. Kinetic measurements give new insights into lipid membrane permeabilization by α-synuclein oligomers. Mol. Biosyst. 2012, 8, 338–345.
    • (2012) Mol. Biosyst , vol.8 , pp. 338-345
    • Stöckl, M.1    Claessens, M.2    Subramaniam, V.3
  • 73
    • 84879918450 scopus 로고    scopus 로고
    • α-Synuclein and mitochondria: Partners in crime?
    • Nakamura, K. α-Synuclein and mitochondria: Partners in crime? Neurotherapeutics 2013, 10, 391–399.
    • (2013) Neurotherapeutics , vol.10 , pp. 391-399
    • Nakamura, K.1
  • 74
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi, L.; Raghavendran, V.; Prabhu, B.M.; Avadhani, N.G.; Anandatheerthavarada, H.K. Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J. Biol. Chem. 2008, 283, 9089–9100.
    • (2008) J. Biol. Chem , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 76
    • 84905372211 scopus 로고    scopus 로고
    • Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction
    • Luth, E.S.; Stavrovskaya, I.G.; Bartels, T.; Kristal, B.S.; Selkoe, D.J. Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction. J. Biol. Chem. 2014, 289, 21490–21507.
    • (2014) J. Biol. Chem , vol.289 , pp. 21490-21507
    • Luth, E.S.1    Stavrovskaya, I.G.2    Bartels, T.3    Kristal, B.S.4    Selkoe, D.J.5
  • 77
    • 84887706170 scopus 로고    scopus 로고
    • The rescue of microtubule-dependent traffic recovers mitochondrial function in Parkinson’s disease
    • Esteves, A.R.; Gozes, I.; Cardoso, S.M. The rescue of microtubule-dependent traffic recovers mitochondrial function in Parkinson’s disease. Biochim. Biophys. Acta 2014, 1842, 7–21.
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 7-21
    • Esteves, A.R.1    Gozes, I.2    Cardoso, S.M.3
  • 78
    • 20144389524 scopus 로고    scopus 로고
    • Aggregated alpha-synuclein activates microglia: A process leading to disease progression in Parkinson’s disease
    • Zhang, W.; Wang, T.; Pei, Z.; Miller, D.S.; Wu, X.; Block, M.L.; Wilson, B.; Zhang, W.; Zhou, Y.; Hong, J.-S; et al. Aggregated alpha-synuclein activates microglia: A process leading to disease progression in Parkinson’s disease. FASEB J. 2005, 19, 533–542.
    • (2005) FASEB J , vol.19 , pp. 533-542
    • Zhang, W.1    Wang, T.2    Pei, Z.3    Miller, D.S.4    Wu, X.5    Block, M.L.6    Wilson, B.7    Zhang, W.8    Zhou, Y.9    Hong, J.-S.10
  • 79
    • 33947625072 scopus 로고    scopus 로고
    • Oligomeric alpha-synuclein inhibits tubulin polymerization. Biochem. Biophys. Res
    • Chen, L.; Jin, J.; Davis, J.; Zhou, Y.; Wang, Y.; Liu, J.; Lockhart, P.J.; Zhang, J. Oligomeric alpha-synuclein inhibits tubulin polymerization. Biochem. Biophys. Res. Commun. 2007, 356, 548–553.
    • (2007) Commun , vol.356 , pp. 548-553
    • Chen, L.1    Jin, J.2    Davis, J.3    Zhou, Y.4    Wang, Y.5    Liu, J.6    Lockhart, P.J.7    Zhang, J.8
  • 81
    • 0037040491 scopus 로고    scopus 로고
    • Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine
    • Junn, E.; Mouradian, M.M. Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine. Neurosci. Lett. 2002, 320, 146–150.
    • (2002) Neurosci. Lett , vol.320 , pp. 146-150
    • Junn, E.1    Mouradian, M.M.2
  • 82
    • 84859250911 scopus 로고    scopus 로고
    • NADPH oxidase 1-mediated oxidative stress leads to dopamine neuron death in Parkinson’s disease. Antioxid
    • Choi, D.-H.; Cristóvão, A.C.; Guhathakurta, S.; Lee, J.; Joh, T.H.; Beal, M.F.; Kim, Y.-S. NADPH oxidase 1-mediated oxidative stress leads to dopamine neuron death in Parkinson’s disease. Antioxid. Redox Signal. 2012, 16, 1033–1045.
    • (2012) Redox Signal , vol.16 , pp. 1033-1045
    • Choi, D.-H.1    Cristóvão, A.C.2    Guhathakurta, S.3    Lee, J.4    Joh, T.H.5    Beal, M.F.6    Kim, Y.-S.7
  • 84
    • 80052473816 scopus 로고    scopus 로고
    • Toll-like receptor 4 promotes α-synuclein clearance and survival of nigral dopaminergic neurons
    • Stefanova, N.; Fellner, L.; Reindl, M.; Masliah, E.; Poewe, W.; Wenning, G.K. Toll-like receptor 4 promotes α-synuclein clearance and survival of nigral dopaminergic neurons. Am. J. Pathol. 2011, 179, 954–963.
    • (2011) Am. J. Pathol , vol.179 , pp. 954-963
    • Stefanova, N.1    Fellner, L.2    Reindl, M.3    Masliah, E.4    Poewe, W.5    Wenning, G.K.6
  • 86
    • 84860219621 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is an early event in Alzheimer’s and Parkinson’s disease
    • Hoozemans, J.J.M.; van Haastert, E.S.; Nijholt, D.A.T.; Rozemuller, A.J.M.; Scheper, W. Activation of the unfolded protein response is an early event in Alzheimer’s and Parkinson’s disease. Neurodegener. Dis. 2012, 10, 212–215.
    • (2012) Neurodegener. Dis , vol.10 , pp. 212-215
    • Hoozemans, J.1    Van Haastert, E.S.2    Nijholt, D.3    Rozemuller, A.4    Scheper, W.5
  • 87
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic α-synuclein oligomer within endoplasmic reticulum occurs in α-synucleinopathy in vivo
    • Colla, E.; Jensen, P.H.; Pletnikova, O.; Troncoso, J.C.; Glabe, C.; Lee, M.K. Accumulation of toxic α-synuclein oligomer within endoplasmic reticulum occurs in α-synucleinopathy in vivo. J. Neurosci. 2012, 32, 3301–3305.
    • (2012) J. Neurosci , vol.32 , pp. 3301-3305
    • Colla, E.1    Jensen, P.H.2    Pletnikova, O.3    Troncoso, J.C.4    Glabe, C.5    Lee, M.K.6
  • 88
    • 84863230467 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is important for the manifestations of α-synucleinopathy in vivo
    • Colla, E.; Coune, P.; Liu, Y.; Pletnikova, O.; Troncoso, J.C.; Schneider, B.L.; Lee, M.K. Endoplasmic reticulum stress is important for the manifestations of α-synucleinopathy in vivo. J. Neurosci. 2012, 32, 3306–3320.
    • (2012) J. Neurosci , vol.32 , pp. 3306-3320
    • Colla, E.1    Coune, P.2    Liu, Y.3    Pletnikova, O.4    Troncoso, J.C.5    Schneider, B.L.6    Lee, M.K.7
  • 91
    • 77952900626 scopus 로고    scopus 로고
    • α-Synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi, N.; Helm, J.R.; Nycz, D.C.; Bentley, M.; Liang, Y.; Hay, J.C. α-Synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol. Biol. Cell 2010, 21, 1850–1863.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 93
    • 84879606955 scopus 로고    scopus 로고
    • α-Synuclein and protein degradation systems: A reciprocal relationship
    • Xilouri, M.; Brekk, O.R.; Stefanis, L. α-Synuclein and protein degradation systems: A reciprocal relationship. Mol. Neurobiol. 2013, 47, 537–551.
    • (2013) Mol. Neurobiol , vol.47 , pp. 537-551
    • Xilouri, M.1    Brekk, O.R.2    Stefanis, L.3
  • 94
    • 77951976610 scopus 로고    scopus 로고
    • Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome
    • Emmanouilidou, E.; Stefanis, L.; Vekrellis, K. Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome. Neurobiol. Aging 2010, 31, 953–968.
    • (2010) Neurobiol. Aging , vol.31 , pp. 953-968
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 95
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric alpha-synuclein bind to the S6’ proteasomal protein and inhibit proteasomal function
    • Snyder, H.; Mensah, K.; Theisler, C.; Lee, J.; Matouschek, A.; Wolozin, B. Aggregated and monomeric alpha-synuclein bind to the S6’ proteasomal protein and inhibit proteasomal function. J. Biol. Chem. 2003, 278, 11753–11759.
    • (2003) J. Biol. Chem , vol.278 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 96
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri, M.; Vogiatzi, T.; Vekrellis, K.; Park, D.; Stefanis, L. Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLOS ONE 2009, 4, e5515.
    • (2009) PLOS ONE , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 97
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo, A.M.; Stefanis, L.; Fredenburg, R.; Lansbury, P.T.; Sulzer, D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305, 1292–1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 99
    • 84860110592 scopus 로고    scopus 로고
    • Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure
    • Celej, M.S.; Sarroukh, R.; Goormaghtigh, E.; Fidelio, G.D.; Ruysschaert, J.-M.; Raussens, V. Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure. Biochem. J. 2012, 443, 719–726.
    • (2012) Biochem. J , vol.443 , pp. 719-726
    • Celej, M.S.1    Sarroukh, R.2    Goormaghtigh, E.3    Fidelio, G.D.4    Ruysschaert, J.-M.5    Raussens, V.6
  • 100
    • 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. Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys. J. 2012, 102, 2894–2905.
    • (2012) Biophys. J , vol.102 , pp. 2894-2905
    • Pieri, L.1    Madiona, K.2    Bousset, L.3    Melki, R.4
  • 101
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
    • Desplats, P.; Lee, H.; Bae, E.; Patrick, C.; Rockenstein, E.; Crews, L.; Spencer, B.; Masliah, E; Lee, S. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. PNAS 2009, 106, 13010–13015.
    • (2009) PNAS , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.2    Bae, E.3    Patrick, C.4    Rockenstein, E.5    Crews, L.6    Spencer, B.7    Masliah, E.8    Lee, S.9
  • 104
    • 84878230429 scopus 로고    scopus 로고
    • Lewy body-like α-synuclein aggregates resist degradation and impair macroautophagy
    • Tanik, S.A.; Schultheiss, C.E.; Volpicelli-Daley, L.A.; Brunden, K.R.; Lee, V.M.Y. Lewy body-like α-synuclein aggregates resist degradation and impair macroautophagy. J. Biol. Chem. 2013, 288, 15194–15210.
    • (2013) J. Biol. Chem , vol.288 , pp. 15194-15210
    • Tanik, S.A.1    Schultheiss, C.E.2    Volpicelli-Daley, L.A.3    Brunden, K.R.4    Lee, V.5
  • 105
    • 79953133327 scopus 로고    scopus 로고
    • Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species
    • Jan, A.; Adolfsson, O.; Allaman, I.; Buccarello, A.-L.; Magistretti, P.J.; Pfeifer, A.; Muhs, A.; Lashuel, H.A. Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species. J. Biol. Chem. 2011, 286, 8585–8596.
    • (2011) J. Biol. Chem , vol.286 , pp. 8585-8596
    • Jan, A.1    Adolfsson, O.2    Allaman, I.3    Buccarello, A.-L.4    Magistretti, P.J.5    Pfeifer, A.6    Muhs, A.7    Lashuel, H.A.8
  • 106
    • 84862188904 scopus 로고    scopus 로고
    • The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson’s disease
    • Wan, O.W.; Chung, K.K.K. The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson’s disease. PLOS ONE 2012, 7, e38545.
    • (2012) PLOS ONE , vol.7 , pp. 38545
    • Wan, O.W.1    Chung, K.2
  • 107
    • 23444455247 scopus 로고    scopus 로고
    • Dopamine promotes α-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway
    • Cherny, R.A.; Culvenor, J.G.; Bottomley, S.P.; Masters, C.L. Dopamine promotes α-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway. FASEB J. 2005, 19, 1377–1379.
    • (2005) FASEB J , vol.19 , pp. 1377-1379
    • Cherny, R.A.1    Culvenor, J.G.2    Bottomley, S.P.3    Masters, C.L.4
  • 108
    • 7544245555 scopus 로고    scopus 로고
    • Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers
    • Sparr, E.; Engel, M.F.M.; Sakharov, D.V.; Sprong, M.; Jacobs, J.; de Kruijff, B.; Höppener, J.W.M.; Killian, J.A. Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers. FEBS Lett. 2004, 577, 117–120.
    • (2004) FEBS Lett , vol.577 , pp. 117-120
    • Sparr, E.1    Engel, M.2    Sakharov, D.V.3    Sprong, M.4    Jacobs, J.5    De Kruijff, B.6    Höppener, J.7    Killian, J.A.8
  • 109
    • 0033669319 scopus 로고    scopus 로고
    • In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies
    • Gai, W.; Yuan, H.; Li, X.; Power, J.; Blumbergs, P.; Jensen, P. In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies. Exp. Neurol. 2000, 166, 324–333.
    • (2000) Exp. Neurol , vol.166 , pp. 324-333
    • Gai, W.1    Yuan, H.2    Li, X.3    Power, J.4    Blumbergs, P.5    Jensen, P.6
  • 111
    • 84867525379 scopus 로고    scopus 로고
    • Radiating amyloid fibril formation on the surface of lipid membranes through unit-assembly of oligomeric species of α-synuclein
    • Lee, J.-H.; Hong, C.-S.; Lee, S.; Yang, J.-E.; Park, Y.I.; Lee, D.; Hyeon, T.; Jung, S.; Paik, S.R. Radiating amyloid fibril formation on the surface of lipid membranes through unit-assembly of oligomeric species of α-synuclein. PLOS ONE 2012, 7, e47580.
    • (2012) PLOS ONE , vol.7
    • Lee, J.-H.1    Hong, C.-S.2    Lee, S.3    Yang, J.-E.4    Park, Y.I.5    Lee, D.6    Hyeon, T.7    Jung, S.8    Paik, S.R.9
  • 112
    • 84910664562 scopus 로고    scopus 로고
    • Membrane interactions and fibrillization of α-synuclein play an essential role in membrane disruption
    • Chaudhary, H.; Stefanovic, A.N.D.; Subramaniam, V.; Claessens, M.M.A.E. Membrane interactions and fibrillization of α-synuclein play an essential role in membrane disruption. FEBS Lett. 2014, 588, 4457–4463.
    • (2014) FEBS Lett , vol.588 , pp. 4457-4463
    • Chaudhary, H.1    Stefanovic, A.2    Subramaniam, V.3    Claessens, M.4
  • 113
    • 84898665782 scopus 로고    scopus 로고
    • Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity
    • Plotegher, N.; Greggio, E.; Bisaglia, M.; Bubacco, L. Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity. Q. Rev. Biophys. 2014, 47, 1–48.
    • (2014) Q. Rev. Biophys. , vol.47 , pp. 1-48
    • Plotegher, N.1    Greggio, E.2    Bisaglia, M.3    Bubacco, L.4
  • 115
    • 79952742454 scopus 로고    scopus 로고
    • In vivo demonstration that α-synuclein oligomers are toxic
    • Winner, B.; Jappelli, R.; Maji, S.K.; Desplats, P.A.; Boyer, L.; Aigner, S. In vivo demonstration that α-synuclein oligomers are toxic. PNAS 2011, 108, 4194–4199.
    • (2011) PNAS , vol.108 , pp. 4194-4199
    • Winner, B.1    Jappelli, R.2    Maji, S.K.3    Desplats, P.A.4    Boyer, L.5    Aigner, S.6
  • 118
    • 84862672217 scopus 로고    scopus 로고
    • Aggregation of αSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons
    • Taschenberger, G.; Garrido, M.; Tereshchenko, Y.; Bähr, M.; Zweckstetter, M.; Kügler, S. Aggregation of αSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons. Acta Neuropathol. 2012, 123, 671–683.
    • (2012) Acta Neuropathol , vol.123 , pp. 671-683
    • Taschenberger, G.1    Garrido, M.2    Tereshchenko, Y.3    Bähr, M.4    Zweckstetter, M.5    Kügler, S.6
  • 121
    • 77953853289 scopus 로고    scopus 로고
    • Baicalein reduces E46K α-synuclein aggregation in vitro and protects cells against E46K α-synuclein toxicity in cell models of familiar Parkinsonism
    • Li, Q.; Gillardon, F.; Hengerer, B.; Berlinicke, C. Baicalein reduces E46K α-synuclein aggregation in vitro and protects cells against E46K α-synuclein toxicity in cell models of familiar Parkinsonism. J. Neurochem. 2011, 114, 419–429
    • (2011) J. Neurochem , vol.114 , pp. 419-429
    • Li, Q.1    Gillardon, F.2    Hengerer, B.3    Berlinicke, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.