{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,18]],"date-time":"2026-02-18T01:04:34Z","timestamp":1771376674327,"version":"3.50.1"},"reference-count":65,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,10,1]],"date-time":"2016-10-01T00:00:00Z","timestamp":1475280000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["HHSN261200800001E"],"award-info":[{"award-number":["HHSN261200800001E"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Center for Cancer Research"},{"DOI":"10.13039\/501100004543","name":"China Scholarship Council","doi-asserted-by":"publisher","award":["CSC201306065001"],"award-info":[{"award-number":["CSC201306065001"]}],"id":[{"id":"10.13039\/501100004543","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2016,10]]},"DOI":"10.1016\/j.ejmech.2016.01.044","type":"journal-article","created":{"date-parts":[[2016,1,25]],"date-time":"2016-01-25T02:47:51Z","timestamp":1453690071000},"page":"841-850","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":31,"special_numbering":"C","title":["Coupling of the non-amyloid-component (NAC) domain and the KTK(E\/Q)GV repeats stabilize the \u03b1-synuclein fibrils"],"prefix":"10.1016","volume":"121","author":[{"given":"Liang","family":"Xu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ruth","family":"Nussinov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7383-719X","authenticated-orcid":false,"given":"Buyong","family":"Ma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2016.01.044_bib1","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1096\/fj.03-0338rev","article-title":"Alpha-synuclein and Parkinson's disease","volume":"18","author":"Recchia","year":"2004","journal-title":"FASEB J."},{"key":"10.1016\/j.ejmech.2016.01.044_bib2","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2016.01.044_bib3","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1007\/s12035-014-8818-2","article-title":"\u03b1-Synuclein misfolding versus aggregation relevance to Parkinson's disease: critical assessment and modeling","volume":"51","author":"Berrocal","year":"2014","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib4","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1002\/path.4328","article-title":"Neuronal inclusions of \u03b1-synuclein contribute to the pathogenesis of Krabbe disease","volume":"232","author":"Smith","year":"2014","journal-title":"J.\u00a0Pathol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib5","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and dynamics of micelle-bound human -synuclein","volume":"280","author":"Ulmer","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib6","doi-asserted-by":"crossref","first-page":"8657","DOI":"10.1021\/ja100646t","article-title":"A\u00a0combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins","volume":"132","author":"Rao","year":"2010","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2016.01.044_bib7","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.\u00a0Mol. Biol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib8","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1016\/S0002-9440(10)64777-3","article-title":"The role of NAC in amyloidogenesis in Alzheimer's disease","volume":"156","author":"Hashimoto","year":"2000","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib9","doi-asserted-by":"crossref","first-page":"13782","DOI":"10.1021\/bi026284c","article-title":"Structural and functional implications of C-terminal regions of alpha-synuclein","volume":"41","author":"Kim","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib10","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.febslet.2011.01.009","article-title":"The role of the C-terminus of human alpha-synuclein: intra-disulfide bonds between the C-terminus and other regions stabilize non-fibrillar monomeric isomers","volume":"585","author":"Hong","year":"2011","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ejmech.2016.01.044_bib11","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.molmed.2013.04.002","article-title":"The remarkable conformational plasticity of alpha-synuclein: blessing or curse?","volume":"19","author":"Deleersnijder","year":"2013","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.ejmech.2016.01.044_bib12","doi-asserted-by":"crossref","first-page":"15871","DOI":"10.1073\/pnas.0506109102","article-title":"Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR","volume":"102","author":"Heise","year":"2005","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ejmech.2016.01.044_bib13","doi-asserted-by":"crossref","first-page":"8637","DOI":"10.1073\/pnas.0712179105","article-title":"The fold of alpha-synuclein fibrils","volume":"105","author":"Vilar","year":"2008","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ejmech.2016.01.044_bib14","doi-asserted-by":"crossref","first-page":"E1994","DOI":"10.1073\/pnas.1421204112","article-title":"Structural characterization of toxic oligomers that are kinetically trapped during \u03b1-synuclein fibril formation","volume":"112","author":"Chen","year":"2015","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ejmech.2016.01.044_bib15","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/s12104-011-9324-3","article-title":"Solid-state NMR sequential assignments of \u03b1-synuclein","volume":"6","author":"Gath","year":"2011","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.ejmech.2016.01.044_bib16","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms3575","article-title":"Structural and functional characterization of two alpha-synuclein strains","volume":"4","author":"Bousset","year":"2013","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2016.01.044_bib17","doi-asserted-by":"crossref","first-page":"37530","DOI":"10.1074\/jbc.M305266200","article-title":"Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling","volume":"278","author":"Der-Sarkissian","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib18","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1016\/j.jmb.2008.03.017","article-title":"Characterization of conformational and dynamic properties of natively unfolded human and mouse \u03b1-Synuclein ensembles by NMR: implication for aggregation","volume":"378","author":"Wu","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib19","doi-asserted-by":"crossref","first-page":"17342","DOI":"10.1073\/pnas.0506723102","article-title":"3D structure of Alzheimer's amyloid-beta(1-42) fibrils","volume":"102","author":"Luhrs","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2016.01.044_bib20","doi-asserted-by":"crossref","first-page":"4227","DOI":"10.1002\/anie.201309001","article-title":"\u015e. Akg\u00fcl, J. Lecher, D. Willbold, M. Stoldt, W. Hoyer, Sequestration of a \u03b2-Hairpin for Control of \u03b1-Synuclein Aggregation","volume":"53","author":"Mirecka","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.ejmech.2016.01.044_bib21","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1074\/jbc.M008919200","article-title":"A\u00a0Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of alpha-synuclein Is Essential for Filament Assembly","volume":"276","author":"Giasson","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib22","doi-asserted-by":"crossref","first-page":"10005","DOI":"10.1021\/acs.jpcb.5b03760","article-title":"A\u00a0proposed atomic structure of the self-assembly of the non-amyloid-\u03b2 component of human \u03b1-Synuclein as derived by computational tools","volume":"119","author":"Atsmon-Raz","year":"2015","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.ejmech.2016.01.044_bib23","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1038\/ng0298-106","article-title":"Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease","volume":"18","author":"Kruger","year":"1998","journal-title":"Nat. Genet."},{"key":"10.1016\/j.ejmech.2016.01.044_bib24","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1002\/ana.10795","article-title":"The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia","volume":"55","author":"Zarranz","year":"2004","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib25","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1002\/mds.25421","article-title":"Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease","volume":"28","author":"Appel-Cresswell","year":"2013","journal-title":"Mov. Disord."},{"key":"10.1016\/j.ejmech.2016.01.044_bib26","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1007\/s00401-013-1096-7","article-title":"alpha-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson's disease and multiple system atrophy?","volume":"125","author":"Kiely","year":"2013","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib27","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1002\/ana.23894","article-title":"G51D alpha-synuclein mutation causes a novel parkinsonian-pyramidal syndrome","volume":"73","author":"Lesage","year":"2013","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib28","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1126\/science.276.5321.2045","article-title":"Mutation in the alpha-synuclein gene identified in families with Parkinson's disease","volume":"276","author":"Polymeropoulos","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2016.01.044_bib29","doi-asserted-by":"crossref","first-page":"e2181","DOI":"10.1016\/j.neurobiolaging.2014.03.024","article-title":"Novel alpha-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology","volume":"35","author":"Pasanen","year":"2014","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.ejmech.2016.01.044_bib30","doi-asserted-by":"crossref","first-page":"3142","DOI":"10.1021\/bi501369k","article-title":"Oligomers of Parkinson's disease-related \u03b1-synuclein mutants have similar structures but distinctive membrane permeabilization properties","volume":"54","author":"Stefanovic","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib31","doi-asserted-by":"crossref","first-page":"e67713","DOI":"10.1371\/journal.pone.0067713","article-title":"Wildtype and A30P Mutant Alpha-Synuclein Form Different Fibril Structures","volume":"8","author":"Kahle","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2016.01.044_bib32","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.jmb.2008.05.026","article-title":"Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein","volume":"380","author":"Heise","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib33","doi-asserted-by":"crossref","first-page":"6925","DOI":"10.1021\/bi400999d","article-title":"The Parkinson's disease-associated H50Q mutation accelerates \u03b1-Synuclein aggregation in\u00a0vitro","volume":"52","author":"Ghosh","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib34","doi-asserted-by":"crossref","first-page":"6419","DOI":"10.1021\/bi5010365","article-title":"The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates alpha-synuclein aggregation and membrane binding","volume":"53","author":"Ghosh","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib35","doi-asserted-by":"crossref","first-page":"292","DOI":"10.5607\/en.2014.23.4.292","article-title":"Alpha-Synuclein function and dysfunction on cellular membranes","volume":"23","author":"Snead","year":"2014","journal-title":"Exp. Neurobiol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib36","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1016\/j.bbadis.2009.06.010","article-title":"The effect of amino acid substitution in the imperfect repeat sequences of alpha-synuclein on fibrillation","volume":"1792","author":"Harada","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ejmech.2016.01.044_bib37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7150\/ijbs.3.1","article-title":"Effect of reparation of repeat sequences in the human alpha-synuclein on fibrillation ability","volume":"3","author":"Sode","year":"2007","journal-title":"Int. J. Biol. Sci."},{"key":"10.1016\/j.ejmech.2016.01.044_bib38","doi-asserted-by":"crossref","first-page":"4194","DOI":"10.1073\/pnas.1100976108","article-title":"In\u00a0vivo demonstration that alpha-synuclein oligomers are toxic","volume":"108","author":"Winner","year":"2011","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ejmech.2016.01.044_bib39","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.expneurol.2005.10.019","article-title":"The alpha-synuclein mutation E46K promotes aggregation in cultured cells","volume":"197","author":"Pandey","year":"2006","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib40","doi-asserted-by":"crossref","first-page":"7107","DOI":"10.1021\/bi7000246","article-title":"The Impact of the E46K mutation on the properties of \u03b1-Synuclein in Its monomeric and oligomeric states","volume":"46","author":"Fredenburg","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib41","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1021\/bi401543z","article-title":"Site-specific fluorescence dynamics of \u03b1-Synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations","volume":"53","author":"Sahay","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib42","doi-asserted-by":"crossref","first-page":"13353","DOI":"10.1021\/jp077036z","article-title":"Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrils","volume":"111","author":"Kloepper","year":"2007","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.ejmech.2016.01.044_bib43","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/S0006-3495(03)74550-0","article-title":"A\u00a0general model for amyloid fibril assembly based on morphological studies using atomic force microscopy","volume":"85","author":"Khurana","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.ejmech.2016.01.044_bib44","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.\u00a0Mol. Biol."},{"key":"10.1016\/j.ejmech.2016.01.044_bib45","doi-asserted-by":"crossref","first-page":"L1","DOI":"10.1016\/j.bpj.2011.05.052","article-title":"Electron paramagnetic resonance spectroscopy measures the distance between the external \u03b2-Strands of folded \u03b1-Synuclein in amyloid fibrils","volume":"101","author":"Karyagina","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.ejmech.2016.01.044_bib46","doi-asserted-by":"crossref","first-page":"8837","DOI":"10.1002\/anie.201503018","article-title":"Contact between the \u03b21 and \u03b22 Segments of \u03b1-Synuclein that Inhibits Amyloid Formation","volume":"54","author":"Shaykhalishahi","year":"2015","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.ejmech.2016.01.044_bib47","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1002\/prot.22240","article-title":"Very short peptides with stable folds: building on the interrelationship of Trp\/Trp, Trp\/cation, and Trp\/backbone-amide interaction geometries","volume":"75","author":"Eidenschink","year":"2009","journal-title":"Proteins Struct. Funct. Bioinforma."},{"key":"10.1016\/j.ejmech.2016.01.044_bib48","doi-asserted-by":"crossref","first-page":"11577","DOI":"10.1039\/C5RA00325C","article-title":"Binding interactions of agents that alter \u03b1-synuclein aggregation","volume":"5","author":"Sivanesam","year":"2015","journal-title":"RSC Adv."},{"key":"10.1016\/j.ejmech.2016.01.044_bib49","doi-asserted-by":"crossref","first-page":"8202","DOI":"10.1021\/bi200760h","article-title":"Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state","volume":"50","author":"Huggins","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib50","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib51","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1016\/j.bbamem.2008.01.012","article-title":"Dimeric structures of alpha-synuclein bind preferentially to lipid membranes","volume":"1778","author":"Giannakis","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ejmech.2016.01.044_bib52","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"Chimera\u2013a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib53","doi-asserted-by":"crossref","first-page":"7785","DOI":"10.1021\/bi400911p","article-title":"Effect of charged amino acid side chain length at non-hydrogen bonded strand positions on \u03b2-Hairpin stability","volume":"52","author":"Kuo","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2016.01.044_bib54","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1007\/s00726-015-1916-2","article-title":"Effect of charged amino acid side chain length on lateral cross-strand interactions between carboxylate- and guanidinium-containing residues in a \u03b2-hairpin","volume":"47","author":"Kuo","year":"2015","journal-title":"Amino Acid."},{"key":"10.1016\/j.ejmech.2016.01.044_bib55","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.ejmech.2014.08.004","article-title":"Molecular dynamics in drug design","volume":"91","author":"Zhao","year":"2015","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib56","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ejmech.2014.10.078","article-title":"Molecular dynamics: new advances in drug discovery","volume":"91","author":"Milardi","year":"2015","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib57","doi-asserted-by":"crossref","first-page":"11196","DOI":"10.1021\/acs.jpcb.5b03116","article-title":"Destabilization of Alzheimer's A\u03b242 protofibrils with a novel drug candidate wgx-50 by molecular dynamics simulations","volume":"119","author":"Fan","year":"2015","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.ejmech.2016.01.044_bib58","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib59","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/jcc.540040211","article-title":"CHARMM: A program for macromolecular energy, minimization, and dynamics calculations","volume":"4","author":"Brooks","year":"1983","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.ejmech.2016.01.044_bib60","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1021\/jp973084f","article-title":"All-atom empirical potential for molecular modeling and dynamics studies of proteins","volume":"102","author":"MacKerell","year":"1998","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.ejmech.2016.01.044_bib61","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.ejmech.2016.01.044_bib62","doi-asserted-by":"crossref","first-page":"4613","DOI":"10.1063\/1.470648","article-title":"Constant pressure molecular dynamics simulation: The Langevin piston method","volume":"103","author":"Feller","year":"1995","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.ejmech.2016.01.044_bib63","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: An N\u22c5log(N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.ejmech.2016.01.044_bib64","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0021-9991(77)90098-5","article-title":"Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes","volume":"23","author":"Ryckaert","year":"1977","journal-title":"J.\u00a0Comput. Phys."},{"key":"10.1016\/j.ejmech.2016.01.044_bib65","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1002\/jcc.10272","article-title":"New analytic approximation to the standard molecular volume definition and its application to generalized Born calculations","volume":"24","author":"Lee","year":"2003","journal-title":"J.\u00a0Comput. Chem."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523416300459?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523416300459?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,8,10]],"date-time":"2019-08-10T01:42:06Z","timestamp":1565401326000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523416300459"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,10]]},"references-count":65,"alternative-id":["S0223523416300459"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2016.01.044","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2016,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Coupling of the non-amyloid-component (NAC) domain and the KTK(E\/Q)GV repeats stabilize the \u03b1-synuclein fibrils","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2016.01.044","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}