{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T04:17:35Z","timestamp":1792642655085,"version":"4.5.0"},"reference-count":71,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2007,9,1]],"date-time":"2007-09-01T00:00:00Z","timestamp":1188604800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100005156","name":"Alexander von Humboldt-Stiftung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005156","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008053","name":"Fundaci\u00f3n Antorchas","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008053","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002923","name":"Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas","doi-asserted-by":"publisher","award":["3-1"],"award-info":[{"award-number":["3-1"]}],"id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002923","name":"Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas","doi-asserted-by":"publisher","award":["ZW 71\/2-1-"],"award-info":[{"award-number":["ZW 71\/2-1-"]}],"id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003074","name":"Agencia Nacional de Promoci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003074","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004410","name":"European Molecular Biology Organization","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004410","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004189","name":"Max-Planck-Gesellschaft","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004189","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2007,9]]},"DOI":"10.1016\/j.jmb.2007.07.009","type":"journal-article","created":{"date-parts":[[2007,7,18]],"date-time":"2007-07-18T07:28:04Z","timestamp":1184743684000},"page":"708-722","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":107,"title":["Structural Characterization of the Intrinsically Unfolded Protein \u03b2-Synuclein, a Natural Negative Regulator of \u03b1-Synuclein Aggregation"],"prefix":"10.1016","volume":"372","author":[{"given":"Carlos W.","family":"Bertoncini","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rodolfo M.","family":"Rasia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gonzalo R.","family":"Lamberto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andres","family":"Binolfi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markus","family":"Zweckstetter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Griesinger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudio O.","family":"Fernandez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2007.07.009_bib1","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nrm1589","article-title":"Intrinsically unstructured proteins and their functions","volume":"6","author":"Dyson","year":"2005","journal-title":"Nature Rev. Mol. Cell. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib2","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1110\/ps.4210102","article-title":"Natively unfolded proteins: a point where biology waits for physics","volume":"11","author":"Uversky","year":"2002","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.07.009_bib3","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0896-6273(01)00177-5","article-title":"Cellular defenses against unfolded proteins. A cell biologist thinks about neurodegenerative diseases","volume":"29","author":"Sherman","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.jmb.2007.07.009_bib4","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2007.07.009_bib5","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0166-2236(97)01213-7","article-title":"The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease","volume":"21","author":"Clayton","year":"1998","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.jmb.2007.07.009_bib6","doi-asserted-by":"crossref","first-page":"9335","DOI":"10.1523\/JNEUROSCI.18-22-09335.1998","article-title":"Persyn, a member of the synuclein family, has a distinct pattern of expression in the developing nervous system","volume":"18","author":"Buchman","year":"1998","journal-title":"J. Neurosci."},{"key":"10.1016\/j.jmb.2007.07.009_bib7","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.cell.2005.09.028","article-title":"Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration","volume":"123","author":"Chandra","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2007.07.009_bib8","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.jmb.2007.07.009_bib9","doi-asserted-by":"crossref","first-page":"7871","DOI":"10.1021\/bi030086j","article-title":"Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease","volume":"42","author":"Volles","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.07.009_bib10","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0896-6273(01)00462-7","article-title":"beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor","volume":"32","author":"Hashimoto","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.jmb.2007.07.009_bib11","doi-asserted-by":"crossref","first-page":"11970","DOI":"10.1074\/jbc.M109541200","article-title":"Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins","volume":"277","author":"Uversky","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.07.009_bib12","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/S0006-8993(01)02772-X","article-title":"Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease","volume":"914","author":"Rockenstein","year":"2001","journal-title":"Brain Res."},{"key":"10.1016\/j.jmb.2007.07.009_bib13","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1038\/sj.gt.3302349","article-title":"An antiaggregation gene therapy strategy for Lewy body disease utilizing beta-synuclein lentivirus in a transgenic model","volume":"11","author":"Hashimoto","year":"2004","journal-title":"Gene Ther."},{"key":"10.1016\/j.jmb.2007.07.009_bib14","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/bi020604a","article-title":"Beta-synuclein inhibits formation of alpha-synuclein protofibrils: a possible therapeutic strategy against Parkinson's disease","volume":"42","author":"Park","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.07.009_bib15","doi-asserted-by":"crossref","first-page":"3607","DOI":"10.1021\/cr030403s","article-title":"Unfolded proteins and protein folding studied by NMR","volume":"104","author":"Dyson","year":"2004","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jmb.2007.07.009_bib16","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 alpha-synuclein","volume":"102","author":"Bertoncini","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.07.009_bib17","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1021\/ja044834j","article-title":"Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations","volume":"127","author":"Dedmon","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2007.07.009_bib18","doi-asserted-by":"crossref","first-page":"45996","DOI":"10.1074\/jbc.M106777200","article-title":"Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein","volume":"276","author":"Bussell","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.07.009_bib19","doi-asserted-by":"crossref","first-page":"30649","DOI":"10.1074\/jbc.C500288200","article-title":"Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation","volume":"280","author":"Bertoncini","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.07.009_bib20","doi-asserted-by":"crossref","first-page":"16424","DOI":"10.1021\/bi991765q","article-title":"Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques","volume":"38","author":"Wilkins","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.07.009_bib21","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S0065-3233(08)60401-5","article-title":"Protein denaturation","volume":"23","author":"Tanford","year":"1968","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.jmb.2007.07.009_bib22","series-title":"Physical Chemistry of Macromolecules","author":"Tanford","year":"1961"},{"key":"10.1016\/j.jmb.2007.07.009_bib23","doi-asserted-by":"crossref","first-page":"4659","DOI":"10.1021\/bi00471a022","article-title":"A novel-approach for sequential assignment of H-1, C-13, And N-15 spectra of larger proteins-heteronuclear triple-resonance 3-dimensional NMR-spectroscopy\u2013application to calmodulin","volume":"29","author":"Ikura","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.07.009_bib24","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.jmb.2007.07.009_bib25","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1023\/A:1011239023422","article-title":"Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: application to unfolded proteins","volume":"20","author":"Panchal","year":"2001","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2007.07.009_bib26","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1110\/ps.051867106","article-title":"Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein","volume":"15","author":"McNulty","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.07.009_bib27","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/BF00227471","article-title":"1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects","volume":"5","author":"Wishart","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2007.07.009_bib28","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1080\/10409230591008143","article-title":"Is there or isn't there? The case for (and against) residual structure in chemically denatured proteins","volume":"40","author":"McCarney","year":"2005","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib29","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1006\/jmbi.1995.0619","article-title":"Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation","volume":"254","author":"Serrano","year":"1995","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib30","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1006\/jmbi.1996.0041","article-title":"Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations","volume":"255","author":"Smith","year":"1996","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib31","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.1110\/ps.062465306","article-title":"Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation","volume":"15","author":"Marsh","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.07.009_bib32","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1002\/bip.10354","article-title":"NMR identification of left-handed polyproline type II helices","volume":"69","author":"Lam","year":"2003","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2007.07.009_bib33","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.jmb.2007.07.009_bib34","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1110\/ps.0233303","article-title":"Weak alignment offers new NMR opportunities to study protein structure and dynamics","volume":"12","author":"Bax","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.07.009_bib35","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1126\/science.1060438","article-title":"Persistence of native-like topology in adenatured protein in 8(M urea","volume":"293","author":"Shortle","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.jmb.2007.07.009_bib36","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1016\/j.jmb.2004.05.022","article-title":"Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings","volume":"340","author":"Mohana-Borges","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib37","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1016\/j.jmb.2004.04.037","article-title":"Short-range, long-range and transition state interactions in the denatured state of ACBP from residual dipolar couplings","volume":"339","author":"Fieber","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib38","doi-asserted-by":"crossref","first-page":"15647","DOI":"10.1021\/ja035427v","article-title":"On the origin of residual dipolar couplings from denatured proteins","volume":"125","author":"Louhivuori","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2007.07.009_bib39","doi-asserted-by":"crossref","first-page":"12646","DOI":"10.1021\/ja048287d","article-title":"On the interpretation of residual dipolar couplings as reporters of molecular dynamics","volume":"126","author":"Fredriksson","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2007.07.009_bib40","doi-asserted-by":"crossref","first-page":"7012","DOI":"10.1002\/anie.200602317","article-title":"Charge-induced molecular alignment of intrinsically disordered proteins","volume":"45","author":"Skora","year":"2006","journal-title":"Angew Chem. Int. Ed. Engl."},{"key":"10.1016\/j.jmb.2007.07.009_bib41","doi-asserted-by":"crossref","first-page":"3032","DOI":"10.1021\/ja067482k","article-title":"Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and Tau","volume":"129","author":"Cho","year":"2007","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2007.07.009_bib42","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1126\/science.1124964","article-title":"New tools provide new insights in NMR studies of protein dynamics","volume":"312","author":"Mittermaier","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.jmb.2007.07.009_bib43","doi-asserted-by":"crossref","first-page":"8347","DOI":"10.1074\/jbc.M510748200","article-title":"HIV-1 Tat is a natively unfolded protein: the solution conformation and dynamics of reduced HIV-1 Tat-(1-72) by NMR spectroscopy","volume":"281","author":"Shojania","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2007.07.009_bib44","doi-asserted-by":"crossref","first-page":"9390","DOI":"10.1021\/bi036314r","article-title":"The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure","volume":"43","author":"Thapar","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.07.009_bib45","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1110\/ps.051974506","article-title":"Characterization of the unfolded state of bovine alpha-lactalbumin and comparison with unfolded states of homologous proteins","volume":"15","author":"Wirmer","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.07.009_bib46","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1110\/ps.051803606","article-title":"Secondary structure and dynamics of micelle bound beta- and gamma-synuclein","volume":"15","author":"Sung","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2007.07.009_bib47","doi-asserted-by":"crossref","first-page":"13885","DOI":"10.1073\/pnas.0505129102","article-title":"Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings","volume":"102","author":"Bouvignies","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.07.009_bib48","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s10858-005-5686-0","article-title":"A thorough dynamic interpretation of residual dipolar couplings in ubiquitin","volume":"34","author":"Lakomek","year":"2006","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.jmb.2007.07.009_bib49","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.jmb.2007.07.009_bib50","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1002\/bip.20227","article-title":"The structure of \u201cunstructured\u201d regions in peptides and proteins: role of the polyproline II helix in protein folding and recognition","volume":"80","author":"Rath","year":"2005","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2007.07.009_bib51","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1002\/prot.10477","article-title":"Host-guest scale of left-handed polyproline II helix formation","volume":"53","author":"Rucker","year":"2003","journal-title":"Proteins: Struct. Funct. Genet."},{"key":"10.1016\/j.jmb.2007.07.009_bib52","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/S0065-3233(02)62008-X","article-title":"Is polyproline II a major backbone conformation in unfolded proteins?","volume":"62","author":"Shi","year":"2002","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.jmb.2007.07.009_bib53","doi-asserted-by":"crossref","first-page":"17964","DOI":"10.1073\/pnas.0507124102","article-title":"Polyproline II propensities from GGXGG peptides reveal an anticorrelation with\u00a0beta-sheet scales","volume":"102","author":"Shi","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.07.009_bib54","doi-asserted-by":"crossref","first-page":"1744","DOI":"10.1073\/pnas.0510549103","article-title":"Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins","volume":"103","author":"Makowska","year":"2006","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2007.07.009_bib55","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1093\/bioinformatics\/bth476","article-title":"DisProt: a database of protein disorder","volume":"21","author":"Vucetic","year":"2005","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2007.07.009_bib56","doi-asserted-by":"crossref","first-page":"3435","DOI":"10.1093\/bioinformatics\/bti537","article-title":"FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded","volume":"21","author":"Prilusky","year":"2005","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2007.07.009_bib57","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0898-6568(98)00059-X","article-title":"Regulatory role of SH3 domain-mediated protein-protein interactions in synaptic vesicle endocytosis","volume":"11","author":"McPherson","year":"1999","journal-title":"Cell Signal"},{"key":"10.1016\/j.jmb.2007.07.009_bib58","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1096\/fasebj.14.2.231","article-title":"The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains","volume":"14","author":"Kay","year":"2000","journal-title":"FASEB J."},{"key":"10.1016\/j.jmb.2007.07.009_bib59","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1212\/01.WNL.0000139870.14385.3C","article-title":"Beta-synuclein gene alterations in dementia with Lewy bodies","volume":"63","author":"Ohtake","year":"2004","journal-title":"Neurology"},{"key":"10.1016\/j.jmb.2007.07.009_bib60","doi-asserted-by":"crossref","first-page":"3938","DOI":"10.1111\/j.1742-4658.2005.04812.x","article-title":"The Alzheimer beta-peptide shows temperature-dependent transitions between left-handed 3-helix, beta-strand and random coil secondary structures","volume":"272","author":"Danielsson","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2007.07.009_bib61","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1006\/jmbi.2000.3981","article-title":"Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme","volume":"301","author":"Blanch","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib62","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1016\/j.jmb.2006.06.044","article-title":"Evidence for polyproline II helical structure in short polyglutamine tracts","volume":"361","author":"Chellgren","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib63","doi-asserted-by":"crossref","first-page":"5527","DOI":"10.1021\/bi052662c","article-title":"Hyperphosphorylation of tau induces local polyproline II helix","volume":"45","author":"Bielska","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2007.07.009_bib64","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.jmb.2005.10.053","article-title":"Oligoproline effects on polyglutamine conformation and aggregation","volume":"355","author":"Bhattacharyya","year":"2006","journal-title":"J. Mol.Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib65","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S0022-2836(02)00775-1","article-title":"Dependence of alpha-synuclein aggregate morphology on solution conditions","volume":"322","author":"Hoyer","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib66","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1038\/4176","article-title":"Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions","volume":"5","author":"Hansen","year":"1998","journal-title":"Nature Struct. Biol."},{"key":"10.1016\/j.jmb.2007.07.009_bib67","doi-asserted-by":"crossref","first-page":"7793","DOI":"10.1021\/ja001068h","article-title":"Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments","volume":"122","author":"R\u00fcckert","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2007.07.009_bib68","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1023\/A:1018304117895","article-title":"Characterisation of protein unfolding by NMR diffusion measurements","volume":"10","author":"Jones","year":"1997","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2007.07.009_bib69","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1007\/BF00211779","article-title":"Spectral density-function mapping using 15N relaxation data exclusively","volume":"6","author":"Farrow","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2007.07.009_bib70","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1006\/jmre.1998.1361","article-title":"Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra","volume":"131","author":"Ottiger","year":"1998","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.jmb.2007.07.009_bib71","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283607009230?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283607009230?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T06:07:37Z","timestamp":1762668457000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283607009230"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,9]]},"references-count":71,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2007,9]]}},"alternative-id":["S0022283607009230"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2007.07.009","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2007,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural Characterization of the Intrinsically Unfolded Protein \u03b2-Synuclein, a Natural Negative Regulator of \u03b1-Synuclein Aggregation","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2007.07.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2007 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}