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Volumn 7, Issue 5, 2012, Pages

Effect of spermidine on misfolding and interactions of Alpha-synuclein

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; PROTEIN A30P; PROTEIN VARIANT; SPERMIDINE; UNCLASSIFIED DRUG;

EID: 84861471138     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0038099     Document Type: Article
Times cited : (49)

References (49)
  • 1
    • 74249111692 scopus 로고    scopus 로고
    • Brain α-synuclein accumulation in multiple system atrophy, Parkinson's disease and progressive supranuclear palsy: a comparative investigation
    • Tong J, Wong H, Guttman M, Ang LC, Forno LS, et al. (2010) Brain α-synuclein accumulation in multiple system atrophy, Parkinson's disease and progressive supranuclear palsy: a comparative investigation. Brain 133: 172-188.
    • (2010) Brain , vol.133 , pp. 172-188
    • Tong, J.1    Wong, H.2    Guttman, M.3    Ang, L.C.4    Forno, L.S.5
  • 2
    • 0029904487 scopus 로고    scopus 로고
    • NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded†
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT, (1996) NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded†. Biochemistry 35: 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.5
  • 4
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • Eliezer D, Kutluay E, Bussell R Jr, Browne G, (2001) Conformational properties of alpha-synuclein in its free and lipid-associated states. Journal of molecular biology 307: 1061-1073.
    • (2001) Journal of Molecular Biology , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell Jr., R.3    Browne, G.4
  • 5
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, et al. (1998) Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet 18: 106-108.
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5
  • 7
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, et al. (1997) Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease. Science 276: 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 9
    • 17844406856 scopus 로고    scopus 로고
    • α-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen L, Feany MB, (2005) α-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat Neurosci 8: 657-663.
    • (2005) Nat Neurosci , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 10
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway KA, Rochet JC, Bieganski RM, Lansbury PT Jr, (2001) Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294: 1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 12
    • 33747769942 scopus 로고    scopus 로고
    • α-Synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers
    • Beyer K, (2006) α-Synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers. Acta Neuropathologica 112: 237-251.
    • (2006) Acta Neuropathologica , vol.112 , pp. 237-251
    • Beyer, K.1
  • 13
    • 0032551656 scopus 로고    scopus 로고
    • Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease
    • Hashimoto M, Hsu LJ, Sisk A, Xia Y, Takeda A, et al. (1998) Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease. Brain Research 799: 301-306.
    • (1998) Brain Research , vol.799 , pp. 301-306
    • Hashimoto, M.1    Hsu, L.J.2    Sisk, A.3    Xia, Y.4    Takeda, A.5
  • 14
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky VN, Li J, Fink AL, (2001) Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. The Journal of biological chemistry 276: 44284-44296.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 15
    • 0031571624 scopus 로고    scopus 로고
    • Aluminum-induced structural alterations of the precursor of the non-A beta component of Alzheimer's disease amyloid
    • Paik SR, Lee JH, Kim DH, Chang CS, Kim J, (1997) Aluminum-induced structural alterations of the precursor of the non-A beta component of Alzheimer's disease amyloid. Archives of biochemistry and biophysics 344: 325-334.
    • (1997) Archives of Biochemistry and Biophysics , vol.344 , pp. 325-334
    • Paik, S.R.1    Lee, J.H.2    Kim, D.H.3    Chang, C.S.4    Kim, J.5
  • 18
    • 56249130752 scopus 로고    scopus 로고
    • alpha-Synuclein misfolding: single molecule AFM force spectroscopy study
    • Yu J, Malkova S, Lyubchenko YL, (2008) alpha-Synuclein misfolding: single molecule AFM force spectroscopy study. Journal of molecular biology 384: 992-1001.
    • (2008) Journal of Molecular Biology , vol.384 , pp. 992-1001
    • Yu, J.1    Malkova, S.2    Lyubchenko, Y.L.3
  • 23
    • 0032533733 scopus 로고    scopus 로고
    • The N-terminal region of non-A beta component of Alzheimer's disease amyloid is responsible for its tendency to assume beta-sheet and aggregate to form fibrils
    • El-Agnaf OM, Bodles AM, Guthrie DJ, Harriott P, Irvine GB, (1998) The N-terminal region of non-A beta component of Alzheimer's disease amyloid is responsible for its tendency to assume beta-sheet and aggregate to form fibrils. European journal of biochemistry/FEBS 258: 157-163.
    • (1998) European Journal of Biochemistry/FEBS , vol.258 , pp. 157-163
    • El-Agnaf, O.M.1    Bodles, A.M.2    Guthrie, D.J.3    Harriott, P.4    Irvine, G.B.5
  • 24
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, et al. (1998) Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nature genetics 18: 106-108.
    • (1998) Nature Genetics , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5
  • 25
    • 79958844273 scopus 로고    scopus 로고
    • Single-molecule atomic force microscopy force spectroscopy study of Abeta-40 interactions
    • Kim BH, Palermo NY, Lovas S, Zaikova T, Keana JF, et al. (2011) Single-molecule atomic force microscopy force spectroscopy study of Abeta-40 interactions. Biochemistry 50: 5154-5162.
    • (2011) Biochemistry , vol.50 , pp. 5154-5162
    • Kim, B.H.1    Palermo, N.Y.2    Lovas, S.3    Zaikova, T.4    Keana, J.F.5
  • 26
    • 56249130752 scopus 로고    scopus 로고
    • alpha-Synuclein misfolding: single molecule AFM force spectroscopy study
    • Yu J, Malkova S, Lyubchenko YL, (2008) alpha-Synuclein misfolding: single molecule AFM force spectroscopy study. J Mol Biol 384: 992-1001.
    • (2008) J Mol Biol , vol.384 , pp. 992-1001
    • Yu, J.1    Malkova, S.2    Lyubchenko, Y.L.3
  • 27
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson BI, Murray IV, Trojanowski JQ, Lee VM, (2001) A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. The Journal of biological chemistry 276: 2380-2386.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 29
    • 81455136019 scopus 로고    scopus 로고
    • Phosphorylation of α-Synuclein at Y125 and S129 Alters Its Metal Binding Properties: Implications for Understanding the Role of α-Synuclein in the Pathogenesis of Parkinson's Disease and Related Disorders
    • Lu Y, Prudent M, Fauvet B, Lashuel HA, Girault HH, (2011) Phosphorylation of α-Synuclein at Y125 and S129 Alters Its Metal Binding Properties: Implications for Understanding the Role of α-Synuclein in the Pathogenesis of Parkinson's Disease and Related Disorders. ACS Chemical Neuroscience 2: 667-675.
    • (2011) ACS Chemical Neuroscience , vol.2 , pp. 667-675
    • Lu, Y.1    Prudent, M.2    Fauvet, B.3    Lashuel, H.A.4    Girault, H.H.5
  • 31
    • 2942584868 scopus 로고    scopus 로고
    • NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation
    • Fernandez CO, Hoyer W, Zweckstetter M, Jares-Erijman EA, Subramaniam V, et al. (2004) NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation. The EMBO journal 23: 2039-2046.
    • (2004) The EMBO Journal , vol.23 , pp. 2039-2046
    • Fernandez, C.O.1    Hoyer, W.2    Zweckstetter, M.3    Jares-Erijman, E.A.4    Subramaniam, V.5
  • 32
    • 8544264002 scopus 로고    scopus 로고
    • Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro
    • Hoyer W, Cherny D, Subramaniam V, Jovin TM, (2004) Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. Biochemistry 43: 16233-16242.
    • (2004) Biochemistry , vol.43 , pp. 16233-16242
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 33
    • 38949139507 scopus 로고    scopus 로고
    • Conformational equilibria in monomeric alpha-synuclein at the single-molecule level
    • Sandal M, Valle F, Tessari I, Mammi S, Bergantino E, et al. (2008) Conformational equilibria in monomeric alpha-synuclein at the single-molecule level. PLoS biology 6: e6.
    • (2008) PLoS Biology , vol.6
    • Sandal, M.1    Valle, F.2    Tessari, I.3    Mammi, S.4    Bergantino, E.5
  • 35
    • 42649142233 scopus 로고    scopus 로고
    • Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation
    • Wu KP, Kim S, Fela DA, Baum J, (2008) Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation. Journal of molecular biology 378: 1104-1115.
    • (2008) Journal of Molecular Biology , vol.378 , pp. 1104-1115
    • Wu, K.P.1    Kim, S.2    Fela, D.A.3    Baum, J.4
  • 36
    • 51749125627 scopus 로고    scopus 로고
    • Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein
    • Heise H, Celej MS, Becker S, Riedel D, Pelah A, et al. (2008) Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein. Journal of molecular biology 380: 444-450.
    • (2008) Journal of Molecular Biology , vol.380 , pp. 444-450
    • Heise, H.1    Celej, M.S.2    Becker, S.3    Riedel, D.4    Pelah, A.5
  • 37
    • 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 alpha-synuclein
    • Li J, Uversky VN, Fink AL, (2001) Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry 40: 11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 38
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, et al. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proceedings of the National Academy of Sciences of the United States of America 97: 571-576.
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5
  • 40
    • 0035941305 scopus 로고    scopus 로고
    • Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations
    • Uversky VN, Lee HJ, Li J, Fink AL, Lee SJ, (2001) Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations. The Journal of biological chemistry 276: 43495-43498.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 43495-43498
    • Uversky, V.N.1    Lee, H.J.2    Li, J.3    Fink, A.L.4    Lee, S.J.5
  • 41
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky VN, Li J, Fink AL, (2001) Evidence for a partially folded intermediate in alpha-synuclein fibril formation. The Journal of biological chemistry 276: 10737-10744.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 42
    • 78249280020 scopus 로고    scopus 로고
    • Single Molecule Characterization of α-Synuclein in Aggregation-Prone States
    • Trexler AJ, Rhoades E, (2010) Single Molecule Characterization of α-Synuclein in Aggregation-Prone States. Biophysical Journal 99: 3048-3055.
    • (2010) Biophysical Journal , vol.99 , pp. 3048-3055
    • Trexler, A.J.1    Rhoades, E.2
  • 45
    • 80051521167 scopus 로고    scopus 로고
    • Structural role of compensatory amino acid replacements in the alpha-synuclein protein
    • Losasso V, Pietropaolo A, Zannoni C, Gustincich S, Carloni P, (2011) Structural role of compensatory amino acid replacements in the alpha-synuclein protein. Biochemistry 50: 6994-7001.
    • (2011) Biochemistry , vol.50 , pp. 6994-7001
    • Losasso, V.1    Pietropaolo, A.2    Zannoni, C.3    Gustincich, S.4    Carloni, P.5
  • 46
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway KA, Harper JD, Lansbury PT Jr, (2000) Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39: 2552-2563.
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 47
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein
    • Rochet JC, Conway KA, Lansbury PT Jr, (2000) Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. Biochemistry 39: 10619-10626.
    • (2000) Biochemistry , vol.39 , pp. 10619-10626
    • Rochet, J.C.1    Conway, K.A.2    Lansbury Jr., P.T.3
  • 48
    • 0032560621 scopus 로고    scopus 로고
    • Ionization-reactivity relationships for cysteine thiols in polypeptides
    • Bulaj G, Kortemme T, Goldenberg DP, (1998) Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry 37: 8965-8972.
    • (1998) Biochemistry , vol.37 , pp. 8965-8972
    • Bulaj, G.1    Kortemme, T.2    Goldenberg, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.