{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,5,13]],"date-time":"2025-05-13T17:07:07Z","timestamp":1747156027088,"version":"3.40.5"},"reference-count":68,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2016,5,1]],"date-time":"2016-05-01T00:00:00Z","timestamp":1462060800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100003074","name":"Agencia Nacional de Promoci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","award":["PICT 2013-2603"],"award-info":[{"award-number":["PICT 2013-2603"]}],"id":[{"id":"10.13039\/501100003074","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002923","name":"CONICET","doi-asserted-by":"publisher","award":["PIP-2011-2013"],"award-info":[{"award-number":["PIP-2011-2013"]}],"id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Secretaria de Ciencia y Tecnolog\u00eda, Universidad Nacional de C\u00f3rdoba","award":["SECyT-UNC 2014-2015"],"award-info":[{"award-number":["SECyT-UNC 2014-2015"]}]},{"DOI":"10.13039\/501100003033","name":"Ministerio de Ciencia, Tecnolog\u00eda e Innovaci\u00f3n Productiva","doi-asserted-by":"publisher","award":["BE\/12\/01"],"award-info":[{"award-number":["BE\/12\/01"]}],"id":[{"id":"10.13039\/501100003033","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002923","name":"CONICET","doi-asserted-by":"publisher","award":["V4\/325C"],"award-info":[{"award-number":["V4\/325C"]}],"id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"name":"F.R.S.-FNRS","award":["#70214.12"],"award-info":[{"award-number":["#70214.12"]}]},{"name":"SAO-FRA","award":["S#14025"],"award-info":[{"award-number":["S#14025"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2016,5]]},"DOI":"10.1016\/j.bbapap.2016.01.011","type":"journal-article","created":{"date-parts":[[2016,2,2]],"date-time":"2016-02-02T04:31:08Z","timestamp":1454387468000},"page":"501-510","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"title":["Structural remodeling during amyloidogenesis of physiological N\u03b1-acetylated \u03b1-synuclein"],"prefix":"10.1016","volume":"1864","author":[{"given":"J. Ignacio","family":"Gallea","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rabia","family":"Sarroukh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pablo","family":"Yunes-Quartino","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean-Marie","family":"Ruysschaert","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vincent","family":"Raussens","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7831-9244","authenticated-orcid":false,"given":"M. Soledad","family":"Celej","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2016.01.011_bb0005","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3406","article-title":"The many faces of alpha-synuclein: from structure and toxicity to therapeutic target","volume":"14","author":"Lashuel","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0010","doi-asserted-by":"crossref","first-page":"282","DOI":"10.3390\/biom5020282","article-title":"Seeking a mechanism for the toxicity of oligomeric alpha-synuclein","volume":"5","author":"Roberts","year":"2015","journal-title":"Biomolecules"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0015","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1016\/j.cell.2012.03.037","article-title":"Direct observation of the interconversion of normal and toxic forms of alpha-synuclein","volume":"149","author":"Cremades","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0020","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1007\/s00401-011-0926-8","article-title":"Aggregation of alphaSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons","volume":"123","author":"Taschenberger","year":"2012","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0025","doi-asserted-by":"crossref","first-page":"2107","DOI":"10.1038\/cdd.2015.79","article-title":"Fibril growth and seeding capacity play key roles in alpha-synuclein-mediated apoptotic cell death","volume":"22","author":"Mahul-Mellier","year":"2015","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0030","doi-asserted-by":"crossref","first-page":"19509","DOI":"10.1074\/jbc.274.28.19509","article-title":"alpha-Synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease","volume":"274","author":"Wood","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0035","doi-asserted-by":"crossref","first-page":"10737","DOI":"10.1074\/jbc.M010907200","article-title":"Evidence for a partially folded intermediate in alpha-synuclein fibril formation","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0040","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.jmb.2005.08.046","article-title":"Characterization of oligomeric intermediates in alpha-synuclein fibrillation: FRET studies of Y125W\/Y133F\/Y136F alpha-synuclein","volume":"353","author":"Kaylor","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0045","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.jmb.2005.10.071","article-title":"Secondary structure of \u03b1-synuclein oligomers: characterization by raman and atomic force microscopy","volume":"355","author":"Apetri","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0050","doi-asserted-by":"crossref","first-page":"9228","DOI":"10.1038\/srep09228","article-title":"Structure based aggregation studies reveal the presence of helix-rich intermediate during alpha-synuclein aggregation","volume":"5","author":"Ghosh","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0055","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1016\/j.bpj.2012.01.051","article-title":"Supramolecular non-amyloid intermediates in the early stages of alpha-synuclein aggregation","volume":"102","author":"Fauerbach","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0060","doi-asserted-by":"crossref","first-page":"15871","DOI":"10.1073\/pnas.0506109102","article-title":"Molecular-level secondary structure, polymorphism, and dynamics of full-length \u03b1-synuclein fibrils studied by solid-state NMR","volume":"102","author":"Heise","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0065","doi-asserted-by":"crossref","first-page":"8637","DOI":"10.1073\/pnas.0712179105","article-title":"The fold of \u03b1-synuclein fibrils","volume":"105","author":"Vilar","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0070","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1006\/jmbi.2001.4538","article-title":"Conformational properties of alpha-synuclein in its free and lipid-associated states","volume":"307","author":"Eliezer","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0075","doi-asserted-by":"crossref","first-page":"1430","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","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0080","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1016\/j.bpj.2013.07.044","article-title":"Identification of fibril-like tertiary contacts in soluble monomeric alpha-synuclein","volume":"105","author":"Esteban-Martin","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0085","doi-asserted-by":"crossref","first-page":"2640","DOI":"10.1016\/j.febslet.2015.07.013","article-title":"Structural, morphological, and functional diversity of amyloid oligomers","volume":"589","author":"Breydo","year":"2015","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0090","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1016\/j.jmb.2009.10.021","article-title":"Tryptophan fluorescence reveals structural features of alpha-synuclein oligomers","volume":"394","author":"van Rooijen","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0095","doi-asserted-by":"crossref","first-page":"9097","DOI":"10.1021\/bi4009193","article-title":"Characterizing the dynamics of alpha-synuclein oligomers using hydrogen\/deuterium exchange monitored by mass spectrometry","volume":"52","author":"Mysling","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0100","doi-asserted-by":"crossref","first-page":"17482","DOI":"10.1021\/ja9077599","article-title":"Structural properties of pore-forming oligomers of alpha-synuclein","volume":"131","author":"Kim","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0105","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1042\/BJ20111924","article-title":"Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure","volume":"443","author":"Celej","year":"2012","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0110","doi-asserted-by":"crossref","first-page":"3859","DOI":"10.1021\/ja411577t","article-title":"The role of stable alpha-synuclein oligomers in the molecular events underlying amyloid formation","volume":"136","author":"Lorenzen","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0115","doi-asserted-by":"crossref","first-page":"E1994","DOI":"10.1073\/pnas.1421204112","article-title":"Structural characterization of toxic oligomers that are kinetically trapped during alpha-synuclein fibril formation","volume":"112","author":"Chen","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0120","doi-asserted-by":"crossref","first-page":"26733","DOI":"10.1074\/jbc.M114.566695","article-title":"Structural insights into amyloid oligomers of the Parkinson disease-related protein alpha-synuclein","volume":"289","author":"Gallea","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0125","doi-asserted-by":"crossref","first-page":"29739","DOI":"10.1074\/jbc.M600933200","article-title":"Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease","volume":"281","author":"Anderson","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0130","doi-asserted-by":"crossref","first-page":"28243","DOI":"10.1074\/jbc.M112.383711","article-title":"Characterization of semisynthetic and naturally Nalpha-acetylated alpha-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of alpha-synuclein","volume":"287","author":"Fauvet","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0135","doi-asserted-by":"crossref","first-page":"5004","DOI":"10.1021\/bi300642h","article-title":"Impact of N-terminal acetylation of alpha-synuclein on its random coil and lipid binding properties","volume":"51","author":"Maltsev","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0140","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1002\/pro.2088","article-title":"N-terminal acetylation of alpha-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer","volume":"21","author":"Kang","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0145","article-title":"Mechanistic insight into the relationship between N-terminal acetylation of alpha-synuclein and fibril formation rates by NMR and fluorescence","volume":"8","author":"Kang","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0150","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0015801","article-title":"Targeted amino-terminal acetylation of recombinant proteins in E. coli","volume":"5","author":"Johnson","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0155","doi-asserted-by":"crossref","first-page":"4867","DOI":"10.1529\/biophysj.107.125211","article-title":"Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of \u03b1-synuclein","volume":"94","author":"Celej","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0160","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1002\/bip.1976.360150402","article-title":"Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet","volume":"15","author":"Chirgadze","year":"1976","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0165","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1002\/bip.360250307","article-title":"Examination of the secondary structure of proteins by deconvolved FTIR spectra","volume":"25","author":"Byler","year":"1986","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0170","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1007\/978-1-4615-1863-1_10","article-title":"Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures","volume":"23","author":"Goormaghtigh","year":"1994","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0175","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1007\/978-1-4615-1863-1_8","article-title":"Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds","volume":"23","author":"Goormaghtigh","year":"1994","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0180","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1017\/S0033583502003815","article-title":"What vibrations tell us about proteins","volume":"35","author":"Barth","year":"2002","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0185","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0005-2736(85)90521-8","article-title":"Production of large unilamellar vesicles by a rapid extrusion procedure: characterization of size distribution, trapped volume and ability to maintain a membrane potential","volume":"812","author":"Hope","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0190","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/S0021-9258(18)70226-3","article-title":"Phosphorus assay in column chromatography","volume":"234","author":"Bartlett","year":"1959","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0195","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1042\/BJ20150617","article-title":"Amyloid fibrils are the molecular trigger of inflammation in Parkinson's disease","volume":"471","author":"Gustot","year":"2015","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0200","doi-asserted-by":"crossref","first-page":"205","DOI":"10.2174\/138920311795860151","article-title":"Small molecule fluorescent probes for the detection of amyloid self-assembly in vitro and in vivo","volume":"12","author":"Bertoncini","year":"2011","journal-title":"Curr. Protein Pept. Sci."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0205","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1016\/j.bbamem.2009.03.010","article-title":"Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core","volume":"1788","author":"van Rooijen","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0210","doi-asserted-by":"crossref","first-page":"3314","DOI":"10.1110\/ps.041024904","article-title":"FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils","volume":"13","author":"Zandomeneghi","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0215","doi-asserted-by":"crossref","first-page":"2328","DOI":"10.1016\/j.bbamem.2013.04.012","article-title":"ATR-FTIR: a \u201crejuvenated\u201d tool to investigate amyloid proteins","volume":"1828","author":"Sarroukh","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0220","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1002\/bip.1976.360150403","article-title":"Infrared spectra and resonance interaction of amide-I vibration of the paraellel-chain pleated sheets","volume":"15","author":"Chirgadze","year":"1976","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0225","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1002\/bip.360240804","article-title":"Amide I band of IR spectrum and structure of collagen and related polypeptides","volume":"24","author":"Lazarev","year":"1985","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0230","doi-asserted-by":"crossref","first-page":"10925","DOI":"10.1021\/bi00202a011","article-title":"Characterization of the interaction of natural proline-rich peptides with five different SH3 domains","volume":"33","author":"Viguera","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0235","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1046\/j.0014-2956.2001.02633.x","article-title":"A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins","volume":"269","author":"Syme","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0240","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.1021\/ja0356176","article-title":"Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein","volume":"126","author":"Maiti","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0245","doi-asserted-by":"crossref","first-page":"056005","DOI":"10.1088\/1478-3975\/9\/5\/056005","article-title":"Interplay between desolvation and secondary structure in mediating cosolvent and temperature induced alpha-synuclein aggregation","volume":"9","author":"Anderson","year":"2012","journal-title":"Phys. Biol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0250","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1021\/bi3001825","article-title":"Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts","volume":"51","author":"Camilloni","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0255","doi-asserted-by":"crossref","first-page":"1754","DOI":"10.1002\/cbic.201300244","article-title":"Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of alpha-synuclein","volume":"14","author":"Roche","year":"2013","journal-title":"Chembiochem"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0260","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.str.2013.10.020","article-title":"Predictive atomic resolution descriptions of intrinsically disordered hTau40 and alpha-synuclein in solution from NMR and small angle scattering","volume":"22","author":"Schwalbe","year":"2014","journal-title":"Structure"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0265","doi-asserted-by":"crossref","first-page":"3788","DOI":"10.1016\/j.febslet.2008.10.009","article-title":"Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing","volume":"582","author":"van Rooijen","year":"2008","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0270","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0275","doi-asserted-by":"crossref","first-page":"24970","DOI":"10.1074\/jbc.M700368200","article-title":"Investigation of \u03b1-synuclein fibril structure by site-directed spin labeling","volume":"282","author":"Chen","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0280","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1016\/j.bbamcr.2008.06.010","article-title":"Phosphorylation, lipid raft interaction and traffic of alpha-synuclein in a yeast model for Parkinson","volume":"1783","author":"Zabrocki","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0285","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1002\/pro.666","article-title":"The N-end rule pathway and regulation by proteolysis","volume":"20","author":"Varshavsky","year":"2011","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0290","doi-asserted-by":"crossref","first-page":"9443","DOI":"10.1074\/jbc.273.16.9443","article-title":"Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes","volume":"273","author":"Davidson","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0295","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1042\/BJ20090379","article-title":"Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide","volume":"421","author":"Cerf","year":"2009","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0300","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1007\/s00018-010-0529-x","article-title":"Transformation of amyloid beta(1\u201340) oligomers into fibrils is characterized by a major change in secondary structure","volume":"68","author":"Sarroukh","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0305","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1016\/j.jmb.2008.06.063","article-title":"Conformational plasticity of the Gerstmann\u2013Straussler\u2013Scheinker disease peptide as indicated by its multiple aggregation pathways","volume":"381","author":"Natalello","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0310","doi-asserted-by":"crossref","first-page":"6895","DOI":"10.1021\/bi800279y","article-title":"Early stages of misfolding and association of beta2-microglobulin: insights from infrared spectroscopy and dynamic light scattering","volume":"47","author":"Fabian","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0315","doi-asserted-by":"crossref","first-page":"4003","DOI":"10.1021\/jp4003559","article-title":"Parallel beta-sheet fibril and antiparallel beta-sheet oligomer: new insights into amyloid formation of hen egg white lysozyme under heat and acidic condition from FTIR spectroscopy","volume":"117","author":"Zou","year":"2013","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbapap.2016.01.011_bb0320","doi-asserted-by":"crossref","first-page":"7831","DOI":"10.1038\/ncomms8831","article-title":"Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation","volume":"6","author":"Ruggeri","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0325","doi-asserted-by":"crossref","first-page":"135103","DOI":"10.1063\/1.4896381","article-title":"Early oligomerization stages for the non-amyloid component of alpha-synuclein amyloid","volume":"141","author":"Eugene","year":"2014","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0330","doi-asserted-by":"crossref","first-page":"015005","DOI":"10.1088\/1478-3975\/6\/1\/015005","article-title":"A role for helical intermediates in amyloid formation by natively unfolded polypeptides?","volume":"6","author":"Abedini","year":"2009","journal-title":"Phys. Biol."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0335","doi-asserted-by":"crossref","first-page":"5099","DOI":"10.1073\/pnas.0711731105","article-title":"Stabilization of a beta-hairpin in monomeric Alzheimer's amyloid-beta peptide inhibits amyloid formation","volume":"105","author":"Hoyer","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.01.011_bb0340","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.jmb.2011.11.023","article-title":"Selective molecular recognition in amyloid growth and transmission and cross-species barriers","volume":"421","author":"Ma","year":"2012","journal-title":"J. Mol. Biol."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963916300036?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963916300036?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,6,3]],"date-time":"2022-06-03T00:01:29Z","timestamp":1654214489000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963916300036"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,5]]},"references-count":68,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2016,5]]}},"alternative-id":["S1570963916300036"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2016.01.011","relation":{},"ISSN":["1570-9639"],"issn-type":[{"type":"print","value":"1570-9639"}],"subject":[],"published":{"date-parts":[[2016,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural remodeling during amyloidogenesis of physiological N\u03b1-acetylated \u03b1-synuclein","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbapap.2016.01.011","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2016 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}