{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T01:32:07Z","timestamp":1791163927172,"version":"4.1.0"},"reference-count":68,"publisher":"Public Library of Science (PLoS)","issue":"4","license":[{"start":{"date-parts":[[2012,4,9]],"date-time":"2012-04-09T00:00:00Z","timestamp":1333929600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0032558","type":"journal-article","created":{"date-parts":[[2012,4,9]],"date-time":"2012-04-09T20:51:18Z","timestamp":1334004678000},"page":"e32558","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":7,"title":["Beta-Strand Interfaces of Non-Dimeric Protein Oligomers Are Characterized by Scattered Charged Residue Patterns"],"prefix":"10.1371","volume":"7","author":[{"given":"Giovanni","family":"Feverati","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mounia","family":"Achoch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jihad","family":"Zrimi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Vuillon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claire","family":"Lesieur","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2012,4,9]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1146\/annurev.biophys.29.1.105","article-title":"Structural symmetry and protein function.","volume":"29","author":"DS Goodsell","year":"2000","journal-title":"Annu Rev Biophys Biomol Struct"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1017\/S0033583508004708","article-title":"Protein-protein interaction and quaternary structure.","volume":"41","author":"J Janin","year":"2008","journal-title":"Q Rev Biophys"},{"key":"ref3","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbamem.2008.01.026","article-title":"Pore formation: An ancient yet complex form of attack.","author":"I Iacovache","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"45","DOI":"10.3109\/09687689709068435","article-title":"Membrane insertion: The strategies of toxins (review).","volume":"14","author":"C Lesieur","year":"1997","journal-title":"Mol Membr Biol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1002\/jnr.10328","article-title":"Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies.","volume":"69","author":"MD Kirkitadze","year":"2002","journal-title":"J Neurosci Res"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrn1007","article-title":"Unfolding the role of protein misfolding in neurodegenerative diseases.","volume":"4","author":"C Soto","year":"2003","journal-title":"Nature Reviews Neuroscience"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1016\/j.neurobiolaging.2004.02.010","article-title":"Small assemblies of unmodified amyloid [beta]-protein are the proximate neurotoxin in Alzheimer's disease.","volume":"25","author":"W Klein","year":"2004","journal-title":"Neurobiology of aging"},{"key":"ref8","first-page":"1","article-title":"Amyloid peptides and proteins in review.","volume":"159","author":"RS Harrison","year":"2007","journal-title":"Rev Physiol Biochem Pharmacol"},{"key":"ref9","article-title":"Polymorphism in Alzheimer A amyloid organization reflects conformational selection in a rugged energy landscape.","author":"Y Miller","year":"2010","journal-title":"Chemical reviews"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0969-2126(98)00044-6","article-title":"Morphology of protein-protein interfaces.","volume":"6","author":"TA Larsen","year":"1998","journal-title":"Structure"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1126\/science.1150421","article-title":"Designed protein-protein association.","volume":"319","author":"D Grueninger","year":"2008","journal-title":"Science"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1093\/bib\/bbp001","article-title":"A survey of available tools and web servers for analysis of protein\u2013protein interactions and interfaces.","volume":"10","author":"N Tuncbag","year":"2009","journal-title":"Briefings in Bioinformatics"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"2082","DOI":"10.1110\/ps.062245906","article-title":"Revisiting the Voronoi description of protein-protein interfaces.","volume":"15","author":"F Cazals","year":"2006","journal-title":"Protein Sci"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1186\/1741-7007-5-43","article-title":"Spatial chemical conservation of hot spot interactions in protein-protein complexes.","volume":"5","author":"A Shulman-Peleg","year":"2007","journal-title":"BMC Biol"},{"key":"ref15","article-title":"Oligomeric Interfaces under the Lens: Gemini.","author":"Ga Feverati","year":"2010","journal-title":"Plos One"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1186\/1471-2091-4-14","article-title":"Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified.","volume":"4","author":"JJ Guidry","year":"2003","journal-title":"BMC Biochem"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1107\/S0365110X53001964","article-title":"The packing of alpha-helices: simple coiled-coils.","volume":"6","author":"FHC Crick","year":"1953","journal-title":"Acta Crystallogr"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1126\/science.252.5009.1162","article-title":"Predicting coiled coils from protein sequences.","volume":"252","author":"A Lupas","year":"1991","journal-title":"Science"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S0968-0004(96)10052-9","article-title":"Coiled coils: new structures and new functions.","volume":"21","author":"A Lupas","year":"1996","journal-title":"Trends Biochem Sci"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.jsb.2003.10.014","article-title":"Extended knobs-into-holes packing in classical and complex coiled-coil assemblies.","volume":"144","author":"J Walshaw","year":"2003","journal-title":"J Struct Biol"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1093\/bioinformatics\/btm274","article-title":"Secondary structure based analysis and classification of biological interfaces: identification of binding motifs in protein-protein interactions.","volume":"23","author":"M Guharoy","year":"2007","journal-title":"Bioinformatics"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/s10930-007-9108-x","article-title":"Characterization of protein-protein interfaces.","volume":"27","author":"C Yan","year":"2008","journal-title":"Protein J"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1093\/bioinformatics\/bti277","article-title":"PIBASE: a comprehensive database of structurally defined protein interfaces.","volume":"21","author":"FP Davis","year":"2005","journal-title":"Bioinformatics"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"127","DOI":"10.3109\/10409239609106582","article-title":"Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences.","volume":"31","author":"CJ Tsai","year":"1996","journal-title":"Crit Rev Biochem Mol Biol"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"22517","DOI":"10.1073\/pnas.1012820107","article-title":"Structural space of protein\u2013protein interfaces is degenerate, close to complete, and highly connected.","volume":"107","author":"M Gao","year":"2010","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ref26","article-title":"Three-dimensional modeling of protein interactions and complexes is going omics.","author":"A Stein","year":"2011","journal-title":"Current opinion in structural biology"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1006\/jmbi.1996.0424","article-title":"A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique.","volume":"260","author":"CJ Tsai","year":"1996","journal-title":"J Mol Biol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/j.sbi.2008.04.008","article-title":"Structural specificity in coiled-coil interactions.","volume":"18","author":"G Grigoryan","year":"2008","journal-title":"Curr Opin Struct Biol"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1006\/jmbi.2000.4320","article-title":"How to untwist an alpha-helix: structural principles of an alpha-helical barrel.","volume":"305","author":"CR Calladine","year":"2001","journal-title":"J Mol Biol"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1073\/pnas.0709068105","article-title":"Preferred side-chain constellations at antiparallel coiled-coil interfaces.","volume":"105","author":"EB Hadley","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1002\/pro.5560060106","article-title":"Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect.","volume":"6","author":"CJ Tsai","year":"1997","journal-title":"Protein Sci"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"999","DOI":"10.2174\/156802607780906717","article-title":"Trp\/Met\/Phe hot spots in protein-protein interactions: potential targets in drug design.","volume":"7","author":"B Ma","year":"2007","journal-title":"Current topics in medicinal chemistry"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"5772","DOI":"10.1073\/pnas.1030237100","article-title":"Protein\u2013protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces.","volume":"100","author":"B Ma","year":"2003","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.1073\/pnas.052706099","article-title":"Natural -sheet proteins use negative design to avoid edge-to-edge aggregation.","volume":"99","author":"JS Richardson","year":"2002","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"28","DOI":"10.2174\/138920308783565705","article-title":"Proteins as networks: usefulness of graph theory in protein science.","volume":"9","author":"A Krishnan","year":"2008","journal-title":"Curr Protein Pept Sci"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"2776","DOI":"10.1016\/j.febslet.2007.05.021","article-title":"Network analysis of protein dynamics.","volume":"581","author":"C Bode","year":"2007","journal-title":"FEBS Lett"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"2003","DOI":"10.1093\/bioinformatics\/btr191","article-title":"RING: networking interacting residues, evolutionary information and energetics in protein structures.","volume":"27","author":"AJ Martin","year":"2011","journal-title":"Bioinformatics"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1006\/jmbi.1998.2549","article-title":"Side-chain structures in the first turn of the alpha-helix.","volume":"287","author":"S Penel","year":"1999","journal-title":"J Mol Biol"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4.","volume":"227","author":"U Laemli","year":"1970","journal-title":"Nature"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"16697","DOI":"10.1074\/jbc.M110561200","article-title":"A kinetic model of intermediate formation during assembly of cholera toxin B-subunit pentamers.","volume":"277","author":"C Lesieur","year":"2002","journal-title":"J Biol Chem"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"2714","DOI":"10.1002\/elps.1150181505","article-title":"SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling.","volume":"18","author":"N Guex","year":"1997","journal-title":"Electrophoresis"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/S0022-2836(05)80134-2","article-title":"SCOP: a structural classification of proteins database for the investigation of sequences and structures.","volume":"247","author":"AG Murzin","year":"1995","journal-title":"J Mol Biol"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"2177","DOI":"10.1006\/jmbi.1998.2439","article-title":"The atomic structure of protein-protein recognition sites.","volume":"285","author":"L Lo Conte","year":"1999","journal-title":"J Mol Biol"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1006\/jmbi.2000.3518","article-title":"Molecular dynamics simulations of a [beta]-hairpin fragment of protein G: balance between side-chain and backbone forces1.","volume":"296","author":"B Ma","year":"2000","journal-title":"Journal of molecular biology"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0014-5793(91)80223-P","article-title":"An extension of secondary structure prediction towards the production of tertiary structure.","volume":"280","author":"RC Garratt","year":"1991","journal-title":"FEBS letters"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/367660a0","article-title":"Measurement of the b-sheet-forming propensities of amino acids.","volume":"367","author":"DL Minor Jr","year":"1994","journal-title":"Nature"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.jsb.2007.09.024","article-title":"[beta]-Sheet capping: Signals that initiate and terminate [beta]-sheet formation.","volume":"161","author":"F FarzadFard","year":"2008","journal-title":"Journal of structural biology"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1016\/S0969-2126(00)80023-4","article-title":"Sidechain interactions in parallel [beta] sheets: the energetics of cross-strand pairings.","volume":"7","author":"JS Merkel","year":"1999","journal-title":"Structure"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1002\/prot.10085","article-title":"Dissecting protein-protein recognition sites.","volume":"47","author":"P Chakrabarti","year":"2002","journal-title":"Proteins"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1073\/pnas.93.1.13","article-title":"Principles of protein-protein interactions.","volume":"93","author":"S Jones","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1016\/j.bbapap.2007.12.005","article-title":"Trimeric reassembly of the globular domain of human C1q.","volume":"1784","author":"P Tacnet","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"e15347","DOI":"10.1371\/journal.pone.0015347","article-title":"Cholera toxin B subunits assemble into pentamers - proposition of a fly-casting mechanism.","volume":"5","author":"J Zrimi","year":"2010","journal-title":"PLoS One"},{"key":"ref53","article-title":"Phylogenetic and functional analysis of histidine residues essential for pH-dependent multimerization of von Willebrand factor.","author":"LT Dang","year":"2011","journal-title":"Journal of Biological Chemistry"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"16052","DOI":"10.1073\/pnas.252340199","article-title":"De novo designed peptide-based amyloid fibrils.","volume":"99","author":"M Lopez De La Paz","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1073\/pnas.2634884100","article-title":"Sequence determinants of amyloid fibril formation.","volume":"101","author":"M L\u00f3pez De La Paz","year":"2004","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1042\/BST0370671","article-title":"Structural integrity of beta-sheet assembly.","volume":"37","author":"KE Marshall","year":"2009","journal-title":"Biochem Soc Trans"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"19118","DOI":"10.1074\/jbc.271.32.19118","article-title":"Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Kinetics and molecular basis of rate-limiting steps in vitro.","volume":"271","author":"LW Ruddock","year":"1996","journal-title":"J Biol Chem"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"e15153","DOI":"10.1371\/journal.pone.0015153","article-title":"Molecular basis of differential B-pentamer stability of Shiga toxins 1 and 2.","volume":"5","author":"DG Conrady","year":"2010","journal-title":"PLoS One"},{"key":"ref59","first-page":"760","article-title":"The structures of mutant forms of Hfq from Pseudomonas aeruginosa reveal the importance of the conserved His57 for the protein hexamer organization.","volume":"66","author":"O Moskaleva","year":"2010","journal-title":"Acta Crystallographica Section F: Structural Biology and Crystallization Communications"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1107\/S0907444904030008","article-title":"Structure of Pseudomonas aeruginosa Hfq protein.","volume":"61","author":"A Nikulin","year":"2005","journal-title":"Acta Crystallographica Section D: Biological Crystallography"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"2008","DOI":"10.1073\/pnas.93.5.2008","article-title":"Foldons, protein structural modules, and exons.","volume":"93","author":"AR Panchenko","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1006\/jmbi.1997.1205","article-title":"The foldon universe: a survey of structural similarity and self-recognition of independently folding units.","volume":"272","author":"AR Panchenko","year":"1997","journal-title":"J Mol Biol"},{"key":"ref63","first-page":"125","article-title":"Folding of beta-structured fibrous proteins and self-assembling peptides.","volume":"300","author":"A Mitraki","year":"2005","journal-title":"Methods Mol Biol"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.jmb.2004.07.008","article-title":"Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif.","volume":"342","author":"K Papanikolopoulou","year":"2004","journal-title":"J Mol Biol"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"8991","DOI":"10.1074\/jbc.M311791200","article-title":"Formation of highly stable chimeric trimers by fusion of an adenovirus fiber shaft fragment with the foldon domain of bacteriophage t4 fibritin.","volume":"279","author":"K Papanikolopoulou","year":"2004","journal-title":"J Biol Chem"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1006\/jmbi.1995.0456","article-title":"The three-dimensional crystal structure of cholera toxin.","volume":"251","author":"RG Zhang","year":"1995","journal-title":"J Mol Biol"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"1265","DOI":"10.1016\/j.jmb.2003.11.028","article-title":"Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms.","volume":"335","author":"Y Shomura","year":"2004","journal-title":"J Mol Biol"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1021\/bi0271401","article-title":"The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase.","volume":"42","author":"L Gan","year":"2003","journal-title":"Biochemistry"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0032558","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,20]],"date-time":"2018-10-20T00:05:42Z","timestamp":1539993942000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0032558"}},"subtitle":[],"editor":[{"given":"F. Gisou","family":"van der Goot","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2012,4,9]]},"references-count":68,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2012,4,9]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0032558","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,4,9]]}}}