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Volumn 117, Issue 37, 2013, Pages 10737-10741

A relationship between the aggregation rates of α-synuclein variants and the β-sheet populations in their monomeric forms

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; NEURODEGENERATIVE DISEASES; PROTEINS;

EID: 84884507134     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp405614j     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting Proteostasis for Disease Intervention
    • Balch, W. E.; Morimoto, R. I.; Dillin, A.; Kelly, J. W. Adapting Proteostasis for Disease Intervention Science 2008, 319, 916-919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease Annu. Rev. Biochem. 2006, 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 33847662852 scopus 로고    scopus 로고
    • Soluble Protein Oligomers in Neurodegeneration: Lessons from the Alzheimer's Amyloid Beta-Peptide
    • Haass, C.; Selkoe, D. J. Soluble Protein Oligomers in Neurodegeneration: Lessons from the Alzheimer's Amyloid Beta-Peptide Nat. Rev. Mol. Cell Biol. 2007, 8, 101-112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 5
    • 12944304172 scopus 로고    scopus 로고
    • Mapping Long-Range Interactions in Alpha-Synuclein Using Spin-Label NMR and Ensemble Molecular Dynamics Simulations
    • Dedmon, M. M.; Lindorff-Larsen, K.; Christodoulou, J.; Vendruscolo, M.; Dobson, C. M. Mapping Long-Range Interactions in Alpha-Synuclein Using Spin-Label NMR and Ensemble Molecular Dynamics Simulations J. Am. Chem. Soc. 2005, 127, 476-477
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 476-477
    • Dedmon, M.M.1    Lindorff-Larsen, K.2    Christodoulou, J.3    Vendruscolo, M.4    Dobson, C.M.5
  • 7
    • 66949152096 scopus 로고    scopus 로고
    • Parkinson's Disease
    • Lees, A. J.; Hardy, J.; Revesz, T. Parkinson's Disease Lancet 2009, 373, 2055-2066
    • (2009) Lancet , vol.373 , pp. 2055-2066
    • Lees, A.J.1    Hardy, J.2    Revesz, T.3
  • 8
    • 77958449984 scopus 로고    scopus 로고
    • Alpha-Synuclein: Membrane Interactions and Toxicity in Parkinson's Disease
    • Auluck, P. K.; Caraveo, G.; Lindquist, S. Alpha-Synuclein: Membrane Interactions and Toxicity in Parkinson's Disease Annu. Rev. Cell Dev. Biol. 2010, 26, 211-233
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 9
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein Occurs Physiologically as a Helically Folded Tetramer That Resists Aggregation
    • Bartels, T.; Choi, J. G.; Selkoe, D. J. Alpha-Synuclein Occurs Physiologically as a Helically Folded Tetramer That Resists Aggregation Nature 2011, 477, 107-U123
    • (2011) Nature , vol.477
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 10
    • 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, K. A.; Lee, S. J.; Rochet, J. C.; Ding, T. T.; Williamson, R. E.; Lansbury, P. T. 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 Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 571-576
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , 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    Lansbury, P.T.6
  • 11
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-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. Alpha-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
  • 12
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinson's Disease: Structure and Aggregation of Alpha-Synuclein
    • Uversky, V. N.; Eliezer, D. Biophysics of Parkinson's Disease: Structure and Aggregation of Alpha-Synuclein Curr. Protein Pept. Sci. 2009, 10, 483-499
    • (2009) Curr. Protein Pept. Sci. , vol.10 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 14
    • 84875553835 scopus 로고    scopus 로고
    • On-Surface Aggregation of Alpha-Synuclein at Nanomolar Concentrations Results in Two Distinct Growth Mechanisms
    • Rabe, M.; Soragni, A.; Reynolds, N. P.; Verdes, D.; Liverani, E.; Riek, R.; Seeger, S. On-Surface Aggregation of Alpha-Synuclein at Nanomolar Concentrations Results in Two Distinct Growth Mechanisms ACS Chem. Neurosci. 2013, 4, 408-417
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 408-417
    • Rabe, M.1    Soragni, A.2    Reynolds, N.P.3    Verdes, D.4    Liverani, E.5    Riek, R.6    Seeger, S.7
  • 15
    • 77954758860 scopus 로고    scopus 로고
    • SDS-Induced Fibrillation of Alpha-Synuclein: An Alternative Fibrillation Pathway
    • Giehm, L.; Oliveira, C. L. P.; Christiansen, G.; Pedersen, J. S.; Otzen, D. E. SDS-Induced Fibrillation of Alpha-Synuclein: An Alternative Fibrillation Pathway J. Mol. Biol. 2010, 401, 115-133
    • (2010) J. Mol. Biol. , vol.401 , pp. 115-133
    • Giehm, L.1    Oliveira, C.L.P.2    Christiansen, G.3    Pedersen, J.S.4    Otzen, D.E.5
  • 16
    • 84866337296 scopus 로고    scopus 로고
    • Interplay between Desolvation and Secondary Structure in Mediating Cosolvent and Temperature Induced Alpha-Synuclein Aggregation
    • Anderson, V. L.; Webb, W. W.; Eliezer, D. Interplay between Desolvation and Secondary Structure in Mediating Cosolvent and Temperature Induced Alpha-Synuclein Aggregation. Phys. Biol. 2012, 9, 056005-0560013.
    • (2012) Phys. Biol. , vol.9 , pp. 056005-0560013
    • Anderson, V.L.1    Webb, W.W.2    Eliezer, D.3
  • 18
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the Pathogenic Form of Alpha-Synuclein and Its Mechanism of Neurotoxicity in Parkinson's Disease
    • Volles, M. J.; Lansbury, P. T. Zeroing in on the Pathogenic Form of Alpha-Synuclein and Its Mechanism of Neurotoxicity in Parkinson's Disease Biochemistry 2003, 42, 7871-7878
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury, P.T.2
  • 21
    • 78649640867 scopus 로고    scopus 로고
    • Stable Alpha-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-Domain Co-Chaperones
    • Hinault, M. P.; Cuendet, A. F. H.; Mattoo, R. U. H.; Mensi, M.; Dietler, G.; Lashuel, H. A.; Goloubinoff, P. Stable Alpha-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-Domain Co-Chaperones J. Biol. Chem. 2010, 285, 38173-38182
    • (2010) J. Biol. Chem. , vol.285 , pp. 38173-38182
    • Hinault, M.P.1    Cuendet, A.F.H.2    Mattoo, R.U.H.3    Mensi, M.4    Dietler, G.5    Lashuel, H.A.6    Goloubinoff, P.7
  • 23
    • 80052087039 scopus 로고    scopus 로고
    • The A53T Mutation Is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse Alpha-Synuclein
    • Kang, L. J.; Wu, K. P.; Vendruscolo, M.; Baum, J. The A53T Mutation Is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse Alpha-Synuclein J. Am. Chem. Soc. 2011, 133, 13465-13470
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13465-13470
    • Kang, L.J.1    Wu, K.P.2    Vendruscolo, M.3    Baum, J.4
  • 24
    • 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. Structural Role of Compensatory Amino Acid Replacements in the Alpha-Synuclein Protein Biochemistry 2011, 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
  • 25
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer's Disease: Strategies for Disease Modification
    • Citron, M. Alzheimer's Disease: Strategies for Disease Modification Nat. Rev. Drug Discovery 2010, 9, 387-398
    • (2010) Nat. Rev. Drug Discovery , vol.9 , pp. 387-398
    • Citron, M.1
  • 26
    • 77955327536 scopus 로고    scopus 로고
    • Intrinsically Disordered Proteins Are Potential Drug Targets
    • Metallo, S. J. Intrinsically Disordered Proteins Are Potential Drug Targets Curr. Opin. Chem. Biol. 2010, 14, 481-488
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 481-488
    • Metallo, S.J.1
  • 27
    • 59649115080 scopus 로고    scopus 로고
    • Amyloid Beta-Protein Assembly as a Therapeutic Target of Alzheimer's Disease
    • Yamin, G.; Ono, K.; Inayathullah, M.; Teplow, D. B. Amyloid Beta-Protein Assembly as a Therapeutic Target of Alzheimer's Disease Curr. Pharm. Des. 2008, 14, 3231-3246
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 3231-3246
    • Yamin, G.1    Ono, K.2    Inayathullah, M.3    Teplow, D.B.4
  • 28
    • 84884516817 scopus 로고    scopus 로고
    • Identification of Small-Molecule Binding Pockets in the Soluble Monomeric Form of the Abeta42 Peptide
    • Zhu, M.; De Simone, A.; Schenk, D.; Toth, G.; Dobson, C. M.; Vendruscolo, M. Identification of Small-Molecule Binding Pockets in the Soluble Monomeric Form of the Abeta42 Peptide J. Chem. Phys. 2013, 139, 035101
    • (2013) J. Chem. Phys. , vol.139 , pp. 035101
    • Zhu, M.1    De Simone, A.2    Schenk, D.3    Toth, G.4    Dobson, C.M.5    Vendruscolo, M.6
  • 29
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the Effects of Mutations on Peptide and Protein Aggregation Rates
    • Chiti, F.; Stefani, M.; Taddei, N.; Ramponi, G.; Dobson, C. M. Rationalization of the Effects of Mutations on Peptide and Protein Aggregation Rates Nature 2003, 424, 805-808
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 31
    • 84858634014 scopus 로고    scopus 로고
    • Determination of Secondary Structure Populations in Disordered States of Proteins Using Nuclear Magnetic Resonance Chemical Shifts
    • Camilloni, C.; De Simone, A.; Vranken, W. F.; Vendruscolo, M. Determination of Secondary Structure Populations in Disordered States of Proteins Using Nuclear Magnetic Resonance Chemical Shifts Biochemistry 2012, 51, 2224-2231
    • (2012) Biochemistry , vol.51 , pp. 2224-2231
    • Camilloni, C.1    De Simone, A.2    Vranken, W.F.3    Vendruscolo, M.4
  • 32
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of Secondary Structure Propensities to Sequence Differences between Alpha- and Gamma-Synuclein: Implications for Fibrillation
    • Marsh, J. A.; Singh, V. K.; Jia, Z. C.; Forman-Kay, J. D. Sensitivity of Secondary Structure Propensities to Sequence Differences between Alpha- and Gamma-Synuclein: Implications for Fibrillation Protein Sci. 2006, 15, 2795-2804
    • (2006) Protein Sci. , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.C.3    Forman-Kay, J.D.4
  • 33
    • 84862555977 scopus 로고    scopus 로고
    • N-Terminal Acetylation of Alpha-Synuclein Induces Increased Transient Helical Propensity and Decreased Aggregation Rates in the Intrinsically Disordered Monomer
    • Kang, L. J.; Moriarty, G. M.; Woods, L. A.; Ashcroft, A. E.; Radford, S. E.; Baum, J. N-Terminal Acetylation of Alpha-Synuclein Induces Increased Transient Helical Propensity and Decreased Aggregation Rates in the Intrinsically Disordered Monomer Protein Sci. 2012, 21, 911-917
    • (2012) Protein Sci. , vol.21 , pp. 911-917
    • Kang, L.J.1    Moriarty, G.M.2    Woods, L.A.3    Ashcroft, A.E.4    Radford, S.E.5    Baum, J.6
  • 34
    • 84865249504 scopus 로고    scopus 로고
    • Characterization of Semisynthetic and Naturally N-Alpha-Acetylated Alpha-Synuclein in Vitro and in Intact Cells Implications for Aggregation and Cellular Properties of Alpha-Synuclein
    • Fauvet, B.; Fares, M. B.; Samuel, F.; Dikiy, I.; Tandon, A.; Eliezer, D.; Lashuel, H. A. Characterization of Semisynthetic and Naturally N-Alpha-Acetylated Alpha-Synuclein in Vitro and in Intact Cells Implications for Aggregation and Cellular Properties of Alpha-Synuclein J. Biol. Chem. 2012, 287, 28243-28262
    • (2012) J. Biol. Chem. , vol.287 , pp. 28243-28262
    • Fauvet, B.1    Fares, M.B.2    Samuel, F.3    Dikiy, I.4    Tandon, A.5    Eliezer, D.6    Lashuel, H.A.7
  • 35
    • 84862893457 scopus 로고    scopus 로고
    • Impact of N-Terminal Acetylation of Alpha-Synuclein on Its Random Coil and Lipid Binding Properties
    • Maltsev, A. S.; Ying, J. F.; Bax, A. Impact of N-Terminal Acetylation of Alpha-Synuclein on Its Random Coil and Lipid Binding Properties Biochemistry 2012, 51, 5004-5013
    • (2012) Biochemistry , vol.51 , pp. 5004-5013
    • Maltsev, A.S.1    Ying, J.F.2    Bax, A.3
  • 37
    • 84884516817 scopus 로고    scopus 로고
    • Identication of small-molecule binding pockets in the soluble monomeric form of the A42 peptide
    • Zhu, M.; De Simone, A.; Schenk, D.; Toth, G.; Dobson, C. M.; Vendruscolo, M. Identication of small-molecule binding pockets in the soluble monomeric form of the A42 peptide J. Chem. Phys. 2013, 139, 035101
    • (2013) J. Chem. Phys. , vol.139 , pp. 035101
    • Zhu, M.1    De Simone, A.2    Schenk, D.3    Toth, G.4    Dobson, C.M.5    Vendruscolo, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.