{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T16:40:48Z","timestamp":1791823248929,"version":"4.3.4"},"reference-count":50,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2010,10,8]],"date-time":"2010-10-08T00:00:00Z","timestamp":1286496000000},"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.0013240","type":"journal-article","created":{"date-parts":[[2010,10,8]],"date-time":"2010-10-08T18:59:02Z","timestamp":1286564342000},"page":"e13240","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":79,"title":["Deciphering the Structure, Growth and Assembly of Amyloid-Like Fibrils Using High-Speed Atomic Force Microscopy"],"prefix":"10.1371","volume":"5","author":[{"given":"Pierre-Emmanuel","family":"Milhiet","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daisuke","family":"Yamamoto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olivia","family":"Berthoumieu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrice","family":"Dosset","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Le Grimellec","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Michel","family":"Verdier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"St\u00e9phane","family":"Marchal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshio","family":"Ando","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2010,10,8]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"E207","DOI":"10.1038\/35041139","article-title":"Conformational disease.","volume":"2","author":"RR Kopito","year":"2000","journal-title":"Nat Cell Biol"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/S0197-4580(00)00160-3","article-title":"The cerebral proteopathies.","volume":"21","author":"LC Walker","year":"2000","journal-title":"Neurobiol Aging"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.sbi.2006.03.007","article-title":"Recent atomic models of amyloid fibril structure.","volume":"16","author":"R Nelson","year":"2006","journal-title":"Curr Opin Struct Biol"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-beta spines reveal varied steric zippers.","volume":"447","author":"MR Sawaya","year":"2007","journal-title":"Nature"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"9196","DOI":"10.1073\/pnas.142459399","article-title":"The protofilament structure of insulin amyloid fibrils.","volume":"99","author":"JL Jimenez","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1093\/emboj\/18.4.815","article-title":"Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.","volume":"18","author":"JL Jimenez","year":"1999","journal-title":"EMBO J"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/35065514","article-title":"Amyloid fibrils from muscle myoglobin.","volume":"410","author":"M Fandrich","year":"2001","journal-title":"Nature"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"8342","DOI":"10.1073\/pnas.0402254101","article-title":"Evidence for assembly of prions with left-handed beta-helices into trimers.","volume":"101","author":"C Govaerts","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1111\/j.1750-3639.2000.tb00263.x","article-title":"Toward an understanding of polyglutamine neurodegeneration.","volume":"10","author":"HL Paulson","year":"2000","journal-title":"Brain Pathol"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/S0092-8674(00)80514-0","article-title":"Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo.","volume":"90","author":"E Scherzinger","year":"1997","journal-title":"Cell"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"5591","DOI":"10.1073\/pnas.042681399","article-title":"Amyloid fibers are water-filled nanotubes.","volume":"99","author":"MF Perutz","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"5596","DOI":"10.1073\/pnas.042681599","article-title":"Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques.","volume":"99","author":"MF Perutz","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/S0969-2126(96)00104-9","article-title":"Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix.","volume":"4","author":"C Blake","year":"1996","journal-title":"Structure"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1038\/86188","article-title":"Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping.","volume":"8","author":"R Janowski","year":"2001","journal-title":"Nat Struct Biol"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1038\/nsb0901-770","article-title":"Crystal structure of the human prion protein reveals a mechanism for oligomerization.","volume":"8","author":"KJ Knaus","year":"2001","journal-title":"Nat Struct Biol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1016\/0016-5085(92)91516-7","article-title":"Inhibition of nucleation and crystal growth of calcium carbonate by human lithostathine.","volume":"103","author":"JP Bernard","year":"1992","journal-title":"Gastroenterology"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/s002239900082","article-title":"Calcium carbonate crystals promote calcium oxalate crystallization by heterogeneous or epitaxial nucleation: possible involvement in the control of urinary lithogenesis.","volume":"59","author":"S Geider","year":"1996","journal-title":"Calcif Tissue Int"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1074\/jbc.275.2.1057","article-title":"Mechanism of calcite crystal growth inhibition by the N-terminal undecapeptide of lithostathine.","volume":"275","author":"V Gerbaud","year":"2000","journal-title":"J Biol Chem"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1007\/s00775-002-0421-8","article-title":"Characterization of calcium binding properties of lithostathine.","volume":"8","author":"BI Lee","year":"2003","journal-title":"J Biol Inorg Chem"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1016\/S0006-291X(79)80031-5","article-title":"Characterization of a protein isolated from pancreatic calculi of men suffering from chronic calcifying pancreatitis.","volume":"87","author":"A De Caro","year":"1979","journal-title":"Biochem Biophys Res Commun"},{"key":"ref21","first-page":"733","article-title":"Expression of the regenerating gene in the pancreas of aging mice.","volume":"26","author":"R Perfetti","year":"1994","journal-title":"Transplant Proc"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1136\/gut.2004.053587","article-title":"Possible role of REG I alpha protein in ulcerative colitis and colitic cancer.","volume":"54","author":"A Sekikawa","year":"2005","journal-title":"Gut"},{"key":"ref23","first-page":"1195","article-title":"Reg I protein in healthy and seminoma human testis.","volume":"23","author":"V Mauro","year":"2008","journal-title":"Histol Histopathol"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"22266","DOI":"10.1074\/jbc.274.32.22266","article-title":"Biophysical characterization of lithostathine. Evidences for a polymeric structure at physiological pH and a proteolysis mechanism leading to the formation of fibrils.","volume":"274","author":"C Cerini","year":"1999","journal-title":"J Biol Chem"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"51770","DOI":"10.1074\/jbc.M306767200","article-title":"Lithostathine quadruple-helical filaments form proteinase K-resistant deposits in Creutzfeldt-Jakob disease.","volume":"278","author":"E Laurine","year":"2003","journal-title":"J Biol Chem"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"3313","DOI":"10.1093\/emboj\/20.13.3313","article-title":"Three-dimensional structure of the lithostathine protofibril, a protein involved in Alzheimer's disease.","volume":"20","author":"C Gregoire","year":"2001","journal-title":"EMBO J"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1002\/prot.340230418","article-title":"Crystallization and preliminary crystallographic study of human lithostathine.","volume":"23","author":"D Pignol","year":"1995","journal-title":"Proteins"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"2678","DOI":"10.1002\/j.1460-2075.1996.tb00628.x","article-title":"Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation.","volume":"15","author":"JA Bertrand","year":"1996","journal-title":"EMBO J"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s00424-007-0406-0","article-title":"High-speed AFM and nano-visualization of biomolecular processes.","volume":"456","author":"T Ando","year":"2008","journal-title":"Pflugers Arch"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/S1074-5521(97)90303-3","article-title":"Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein.","volume":"4","author":"JD Harper","year":"1997","journal-title":"Chem Biol"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/jsbi.1995.1024","article-title":"Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin.","volume":"115","author":"HH Bauer","year":"1995","journal-title":"J Struct Biol"},{"key":"ref32","first-page":"1325","article-title":"Morphology and mechanical stability of amyloid-like peptide fibrils.","volume":"18","author":"P Mesquida","year":"2007","journal-title":"J Mater Sci: Mater Med"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583598003400","article-title":"From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.","volume":"31","author":"M Sunde","year":"1998","journal-title":"Q Rev Biophys"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"12206","DOI":"10.1074\/jbc.M312452200","article-title":"Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation.","volume":"279","author":"JD Green","year":"2004","journal-title":"J Biol Chem"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.jmb.2005.07.029","article-title":"Multiple assembly pathways underlie amyloid-beta fibril polymorphisms.","volume":"352","author":"C Goldsbury","year":"2005","journal-title":"J Mol Biol"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1073\/pnas.0704305105","article-title":"Stepwise dynamics of epitaxially growing single amyloid fibrils.","volume":"105","author":"MS Kellermayer","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"37149","DOI":"10.1074\/jbc.M506917200","article-title":"Structure of the Prion Ure2p in Protein Fibrils Assembled in Vitro.","volume":"280","author":"N Fay","year":"2005","journal-title":"J Biol Chem"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"15009","DOI":"10.1021\/bi701842n","article-title":"Visualization and classification of amyloid beta supramolecular assemblies.","volume":"46","author":"H Yagi","year":"2007","journal-title":"Biochemistry"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"2481","DOI":"10.1110\/ps.062215206","article-title":"Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrils.","volume":"15","author":"N Ranson","year":"2006","journal-title":"Protein Science"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1016\/S0022-2836(02)00735-0","article-title":"Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils.","volume":"322","author":"HA Lashuel","year":"2002","journal-title":"J Mol Biol"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1016\/j.jmb.2008.11.005","article-title":"Abeta(1\u201340) fibril polymorphism implies diverse interaction patterns in amyloid fibrils.","volume":"386","author":"J Meinhardt","year":"2009","journal-title":"J Mol Biol"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1038\/197192b0","article-title":"Paired helical filaments in electron microscopy of Alzheimer's disease.","volume":"197","author":"M Kidd","year":"1963","journal-title":"Nature"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/S0006-3495(04)74130-2","article-title":"Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions.","volume":"86","author":"F Moreno-Herrero","year":"2004","journal-title":"Biophys J"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"20631","DOI":"10.1074\/jbc.271.34.20631","article-title":"Morphology and toxicity of Abeta-(1\u201342) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease.","volume":"271","author":"AE Roher","year":"1996","journal-title":"J Biol Chem"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1016\/j.bpj.2008.11.024","article-title":"Branching in amyloid fibril growth.","volume":"96","author":"CB Andersen","year":"2009","journal-title":"Biophys J"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.jmb.2004.04.051","article-title":"Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy.","volume":"340","author":"W Hoyer","year":"2004","journal-title":"J Mol Biol"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1007\/s00249-007-0253-0","article-title":"Oriented epitaxial growth of amyloid fibrils of the N27C mutant beta 25\u201335 peptide.","volume":"37","author":"A Karsai","year":"2008","journal-title":"Eur Biophys J"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.tibs.2006.01.002","article-title":"Amyloids, prions and the inherent infectious nature of misfolded protein aggregates.","volume":"31","author":"C Soto","year":"2006","journal-title":"Trends Biochem Sci"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"30199","DOI":"10.1074\/jbc.M303000200","article-title":"Assembly of the Yeast Prion Ure2p into Protein Fibrils: Thermodynamic and kinetic characterization.","volume":"278","author":"N Fay","year":"2003","journal-title":"J Biol Chem"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1002\/jmr.843","article-title":"High-speed atomic force microscopy for observing dynamic biomolecular processes.","volume":"20","author":"T Ando","year":"2007","journal-title":"J Mol Recognit"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0013240","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,6,5]],"date-time":"2019-06-05T10:18:28Z","timestamp":1559729908000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0013240"}},"subtitle":[],"editor":[{"given":"Mark R.","family":"Cookson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2010,10,8]]},"references-count":50,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2010,10,8]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0013240","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,10,8]]}}}