DOI: 10.1074/jbc.m114.566695. Structural Insights into Amyloid Oligomers of the Parkinson Disease-related Protein α-Synuclein

Structural Insights into Amyloid Oligomers of the Parkinson Disease-related Protein α-Synuclein

10.1074/jbc.m114.566695

Crossref journal-article

Elsevier BV

Journal of Biological Chemistry (78)

Bibliography

Gallea, J. I., & Celej, M. S. (2014). Structural Insights into Amyloid Oligomers of the Parkinson Disease-related Protein Î±-Synuclein. Journal of Biological Chemistry, 289(39), 26733â26742.

Authors 2

J. Ignacio Gallea (first)
M. Soledad Celej (additional)

References 50 Referenced 54

10.1038/nrn3406 / Nat. Rev. Neurosci / The many faces of α-synuclein: from structure and toxicity to therapeutic target by Lashuel (2013)
10.1016/j.cell.2010.11.050 / Cell / Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions by Olzscha (2011)
10.1002/anie.200906670 / Angew. Chem. Int. Ed. Engl / Amyloidogenic protein-membrane interactions: mechanistic insight from model systems by Butterfield (2010)
10.1101/gad.1657108 / Genes Dev / Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging by Morimoto (2008)
10.1038/416507a / Nature / Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases by Bucciantini (2002)
10.1038/nrn2786 / Nat. Rev. Neurosci / Prion-like mechanisms in neurodegenerative diseases by Frost (2010)
10.1038/nature10324 / Nature / α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation by Bartels (2011)
10.1074/jbc.M111.318949 / J. Biol. Chem / α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer by Fauvet (2012)
10.1016/j.bpj.2013.07.044 / Biophys. J / Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein by Esteban-Martín (2013)
10.1073/pnas.0712179105 / Proc. Natl. Acad. Sci. U.S.A / The fold of α-synuclein fibrils by Vilar (2008)
10.1073/pnas.0506109102 / Proc. Natl. Acad. Sci. U.S.A / Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR by Heise (2005)
10.1038/ncomms3575 / Nat. Commun / Structural and functional characterization of two α-synuclein strains by Bousset (2013)
10.1021/bi0102398 / Biochemistry / Vesicle permeabilization by protofibrillar α-synuclein: implications for the pathogenesis and treatment of Parkinson's disease by Volles (2001)
10.1021/ja9077599 / J. Am. Chem. Soc / Structural properties of pore-forming oligomers of α-synuclein by Kim (2009)
10.1042/BJ20111924 / Biochem. J / Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure by Celej (2012)
10.1016/j.jmb.2009.10.021 / J. Mol. Biol / Tryptophan fluorescence reveals structural features of α-synuclein oligomers by van Rooijen (2009)
10.1021/bi4009193 / Biochemistry / Characterizing the dynamics of α-synuclein oligomers using hydrogen/deuterium exchange monitored by mass spectrometry by Mysling (2013)
10.1016/j.febslet.2006.02.032 / FEBS Lett / Cysteine misincorporation in bacterially expressed human α-synuclein by Masuda (2006)
10.1021/bi00658a025 / Biochemistry / N-(1-pyrene)maleimide: a fluorescent cross-linking reagent by Wu (1976)
10.1016/S0021-9258(18)32211-7 / J. Biol. Chem / Synthesis, spectral properties, and use of 6-acryloyl-2-dimethylaminonaphthalene (Acrylodan). A thiol-selective, polarity-sensitive fluorescent probe by Prendergast (1983)
10.1016/j.bpj.2013.12.009 / Biophys. J / Elucidating the aggregation number of dopamine-induced α-synuclein oligomeric assemblies by Zijlstra (2014)
10.1002/anie.201200813 / Angew Chem. Int. Ed. Engl / Molecular composition of sub-stoichiometrically labeled α-synuclein oligomers determined by single-molecule photobleaching by Zijlstra (2012)
10.1016/j.jmb.2008.03.034 / J. Mol. Biol / Multiparametric fluorescence detection of early stages in the amyloid protein aggregation of pyrene-labeled α-synuclein by Thirunavukkuarasu (2008)
10.1038/nbt1012 / Nat. Biotechnol / Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins by Fernandez-Escamilla (2004)
10.1038/nmeth.1432 / Nat. Methods / Exploring the sequence determinants of amyloid structure using position-specific scoring matrices by Maurer-Stroh (2010)
10.1039/b706784b / Chem. Soc. Rev / The Zyggregator method for predicting protein aggregation propensities by Tartaglia (2008)
10.1016/0022-2836(82)90515-0 / J. Mol. Biol / A simple method for displaying the hydropathic character of a protein by Kyte (1982)
10.1523/JNEUROSCI.2617-07.2007 / J. Neurosci / Different species of α-synuclein oligomers induce calcium influx and seeding by Danzer (2007)
10.1016/j.bbamem.2009.03.010 / Biochim Biophys. Acta / Lipid bilayer disruption by oligomeric α-synuclein depends on bilayer charge and accessibility of the hydrophobic core by van Rooijen (2009)
10.1021/ja411577t / J. Am. Chem. Soc / The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation by Lorenzen (2014)
10.1021/bi9003843 / Biochemistry / A triple emission fluorescent probe reveals distinctive amyloid fibrillar polymorphism of wild-type α-synuclein and its familial Parkinson's disease mutants by Celej (2009)
{'key': '10.1074/jbc.M114.566695_bib32', 'series-title': 'Molecular Fluorescence: Principles and Applications', 'first-page': '200', 'author': 'Valeur', 'year': '2001'} / Molecular Fluorescence: Principles and Applications by Valeur (2001)
10.1016/S0006-3495(94)80799-4 / Biophys. J / The use of fluorescence methods to monitor unfolding transitions in proteins by Eftink (1994)
10.1074/jbc.M400348200 / J. Biol. Chem / Prefibrillar amyloid protein aggregates share common features of cytotoxicity by Bucciantini (2004)
10.1074/jbc.R800016200 / J. Biol. Chem / Structural classification of toxic amyloid oligomers by Glabe (2008)
10.2174/138920311795860151 / Curr. Protein Pept Sci / Small molecule fluorescent probes for the detection of amyloid self-assembly in vitro and in vivo by Bertoncini (2011)
10.1038/nature03679 / Nature / Structural insights into a yeast prion illuminate nucleation and strain diversity by Krishnan (2005)
10.1038/nchembio.283 / Nat. Chem. Biol / A causative link between the structure of aberrant protein oligomers and their toxicity by Campioni (2010)
10.1073/pnas.0902603106 / Proc. Natl. Acad. Sci. U.S.A / Structural and mechanistic basis behind the inhibitory interaction of PcTS on α-synuclein amyloid fibril formation by Lamberto (2009)
10.1038/3311 / Nat. Med / Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease by Conway (1998)
10.1073/pnas.97.2.571 / Proc. Natl. Acad. Sci. U.S.A / 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 by Conway (2000)
10.1074/jbc.M008919200 / J. Biol. Chem / A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly by Giasson (2001)
10.1021/bi8002378 / Biochemistry / Characterization of α-synuclein interactions with selected aggregation-inhibiting small molecules by Rao (2008)
10.1073/pnas.0407146102 / Proc. Natl. Acad. Sci. U.S.A / Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein by Bertoncini (2005)
10.1021/ja044834j / J. Am. Chem. Soc / Mapping long-range interactions in α-synuclein using spin-label NMR and ensemble molecular dynamics simulations by Dedmon (2005)
10.1021/ja0561901 / J. Am. Chem. Soc / Tertiary contact formation in α-synuclein probed by electron transfer by Lee (2005)
10.1021/ja9105495 / J. Am. Chem. Soc / Detection of transient interchain interactions in the intrinsically disordered protein α-synuclein by NMR paramagnetic relaxation enhancement by Wu (2010)
10.1016/j.jmb.2005.08.046 / J. Mol. Biol / Characterization of oligomeric intermediates in α-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F α-synuclein by Kaylor (2005)
10.1021/ja102838n / J. Am. Chem. Soc / Fluorescent ratiometric MFC probe sensitive to early stages of α-synuclein aggregation by Yushchenko (2010)
10.1021/bi2000824 / Biochemistry / Residue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assembly by Yap (2011)

Dates

Type	When
Created	11 years ago (Aug. 21, 2014, 2:52 a.m.)
Deposited	4 years, 5 months ago (March 11, 2021, 3:22 p.m.)
Indexed	5 days, 10 hours ago (Aug. 24, 2025, 7:05 p.m.)
Issued	10 years, 11 months ago (Sept. 1, 2014)
Published	10 years, 11 months ago (Sept. 1, 2014)
Published Print	10 years, 11 months ago (Sept. 1, 2014)

Funders 0

None

BibTeX

@article{Gallea_2014, title={Structural Insights into Amyloid Oligomers of the Parkinson Disease-related Protein α-Synuclein}, volume={289}, ISSN={0021-9258}, url={http://dx.doi.org/10.1074/jbc.m114.566695}, DOI={10.1074/jbc.m114.566695}, number={39}, journal={Journal of Biological Chemistry}, publisher={Elsevier BV}, author={Gallea, J. Ignacio and Celej, M. Soledad}, year={2014}, month=sep, pages={26733–26742} }

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      "volume": "105",
      "author": "Esteban-Mart\u00edn",
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      "author": "Thirunavukkuarasu",
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      "year": "2010",
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      "volume": "37",
      "author": "Tartaglia",
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      "volume": "157",
      "author": "Kyte",
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      "volume": "27",
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      "author": "van Rooijen",
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      "article-title": "The role of stable \u03b1-synuclein oligomers in the molecular events underlying amyloid formation",
      "volume": "136",
      "author": "Lorenzen",
      "year": "2014",
      "journal-title": "J. Am. Chem. Soc"
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      "DOI": "10.1021/bi9003843",
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      "volume": "48",
      "author": "Celej",
      "year": "2009",
      "journal-title": "Biochemistry"
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      "series-title": "Molecular Fluorescence: Principles and Applications",
      "first-page": "200",
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      "DOI": "10.1016/S0006-3495(94)80799-4",
      "article-title": "The use of fluorescence methods to monitor unfolding transitions in proteins",
      "volume": "66",
      "author": "Eftink",
      "year": "1994",
      "journal-title": "Biophys. J"
    },
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      "first-page": "31374",
      "DOI": "10.1074/jbc.M400348200",
      "article-title": "Prefibrillar amyloid protein aggregates share common features of cytotoxicity",
      "volume": "279",
      "author": "Bucciantini",
      "year": "2004",
      "journal-title": "J. Biol. Chem"
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      "article-title": "Structural classification of toxic amyloid oligomers",
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      "author": "Glabe",
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      "volume": "12",
      "author": "Bertoncini",
      "year": "2011",
      "journal-title": "Curr. Protein Pept Sci"
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      "first-page": "765",
      "DOI": "10.1038/nature03679",
      "article-title": "Structural insights into a yeast prion illuminate nucleation and strain diversity",
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      "author": "Krishnan",
      "year": "2005",
      "journal-title": "Nature"
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      "first-page": "140",
      "DOI": "10.1038/nchembio.283",
      "article-title": "A causative link between the structure of aberrant protein oligomers and their toxicity",
      "volume": "6",
      "author": "Campioni",
      "year": "2010",
      "journal-title": "Nat. Chem. Biol"
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    {
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      "first-page": "21057",
      "DOI": "10.1073/pnas.0902603106",
      "article-title": "Structural and mechanistic basis behind the inhibitory interaction of PcTS on \u03b1-synuclein amyloid fibril formation",
      "volume": "106",
      "author": "Lamberto",
      "year": "2009",
      "journal-title": "Proc. Natl. Acad. Sci. U.S.A"
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      "first-page": "1318",
      "DOI": "10.1038/3311",
      "article-title": "Accelerated in vitro fibril formation by a mutant \u03b1-synuclein linked to early-onset Parkinson disease",
      "volume": "4",
      "author": "Conway",
      "year": "1998",
      "journal-title": "Nat. Med"
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      "first-page": "571",
      "DOI": "10.1073/pnas.97.2.571",
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      "volume": "97",
      "author": "Conway",
      "year": "2000",
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      "article-title": "A hydrophobic stretch of 12 amino acid residues in the middle of \u03b1-synuclein is essential for filament assembly",
      "volume": "276",
      "author": "Giasson",
      "year": "2001",
      "journal-title": "J. Biol. Chem"
    },
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      "first-page": "4651",
      "DOI": "10.1021/bi8002378",
      "article-title": "Characterization of \u03b1-synuclein interactions with selected aggregation-inhibiting small molecules",
      "volume": "47",
      "author": "Rao",
      "year": "2008",
      "journal-title": "Biochemistry"
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      "DOI": "10.1073/pnas.0407146102",
      "article-title": "Release of long-range tertiary interactions potentiates aggregation of natively unstructured \u03b1-synuclein",
      "volume": "102",
      "author": "Bertoncini",
      "year": "2005",
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      "first-page": "476",
      "DOI": "10.1021/ja044834j",
      "article-title": "Mapping long-range interactions in \u03b1-synuclein using spin-label NMR and ensemble molecular dynamics simulations",
      "volume": "127",
      "author": "Dedmon",
      "year": "2005",
      "journal-title": "J. Am. Chem. Soc"
    },
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      "first-page": "16388",
      "DOI": "10.1021/ja0561901",
      "article-title": "Tertiary contact formation in \u03b1-synuclein probed by electron transfer",
      "volume": "127",
      "author": "Lee",
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      "journal-title": "J. Am. Chem. Soc"
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      "article-title": "Detection of transient interchain interactions in the intrinsically disordered protein \u03b1-synuclein by NMR paramagnetic relaxation enhancement",
      "volume": "132",
      "author": "Wu",
      "year": "2010",
      "journal-title": "J. Am. Chem. Soc"
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      "DOI": "10.1016/j.jmb.2005.08.046",
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      "volume": "353",
      "author": "Kaylor",
      "year": "2005",
      "journal-title": "J. Mol. Biol"
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      "volume": "132",
      "author": "Yushchenko",
      "year": "2010",
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      "DOI": "10.1021/bi2000824",
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      "volume": "50",
      "author": "Yap",
      "year": "2011",
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