{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T22:19:34Z","timestamp":1792793974886,"version":"4.5.0"},"reference-count":57,"publisher":"Public Library of Science (PLoS)","issue":"4","license":[{"start":{"date-parts":[[2011,4,28]],"date-time":"2011-04-28T00:00:00Z","timestamp":1303948800000},"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.0019093","type":"journal-article","created":{"date-parts":[[2011,4,28]],"date-time":"2011-04-28T17:20:00Z","timestamp":1304011200000},"page":"e19093","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":53,"title":["Dynamic Diagnosis of Familial Prion Diseases Supports the \u03b22-\u03b12 Loop as a Universal Interference Target"],"prefix":"10.1371","volume":"6","author":[{"given":"Massimiliano","family":"Meli","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria","family":"Gasset","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giorgio","family":"Colombo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2011,4,28]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"1516","DOI":"10.1056\/NEJM200105173442006","article-title":"Shattuck lecture-Neurodegenerative diseases and prions.","volume":"344","author":"SB Prusiner","year":"2001","journal-title":"N Engl J Med"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1152\/physrev.00006.2009","article-title":"Prions: protein aggregation and infectious diseases.","volume":"89","author":"A Aguzzi","year":"2009","journal-title":"Physiol Rev"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1126\/science.7909169","article-title":"Structural clues to prion replication.","volume":"264","author":"FE Cohen","year":"1994","journal-title":"Science"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"10940","DOI":"10.1073\/pnas.89.22.10940","article-title":"Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.","volume":"189","author":"M Gasset","year":"1992","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"10962","DOI":"10.1073\/pnas.90.23.10962","article-title":"Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl.","volume":"90","author":"KM Pan","year":"1993","journal-title":"Acad Sci USA"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1021\/ar0500618","article-title":"The structural biology of protein aggregation diseases: Fundamental questions and some answers.","volume":"39","author":"D Eisenberg","year":"2006","journal-title":"Acc Chem Res"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1007\/s00401-009-0633-x","article-title":"Recombinant prion protein induces a new transmissible prion disease in wild-type animals.","volume":"119","author":"N Makarava","year":"2010","journal-title":"Acta Neuropathol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1093\/protein\/gzp037","article-title":"Short protein segments can drive a non-fibrillizing protein into the amyloid state.","volume":"22","author":"PK Teng","year":"2009","journal-title":"Protein Eng Des Sel"},{"key":"ref9","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":"ref10","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/382180a0","article-title":"NMR structure of the mouse prion protein domain PrP(121\u2013231).","volume":"382","author":"R Riek","year":"1996","journal-title":"Nature"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1073\/pnas.97.1.145","article-title":"NMR solution structure of the human prion protein.","volume":"97","author":"R Zahn","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"8340","DOI":"10.1073\/pnas.97.15.8340","article-title":"NMR structures of three single-residue variants of the human prion protein.","volume":"97","author":"L Calzolai","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref13","first-page":"646","article-title":"Prion protein NMR structures of elk and of mouse\/elk hybrids Proc Natl Acad Sci USA","volume":"102","author":"AD Gossert","year":"2005"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"3222","DOI":"10.1096\/fj.09-153924","article-title":"The oligomerization properties of prion protein are restricted to the H2H3 domain.","volume":"24","author":"N Chakroun","year":"2010","journal-title":"FASEB J"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"21004","DOI":"10.1074\/jbc.M110.111815","article-title":"Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.","volume":"285","author":"M Adrover","year":"2010","journal-title":"J Biol Chem"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"18946","DOI":"10.1073\/pnas.0706522104","article-title":"Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure.","volume":"104","author":"NJ Cobb","year":"2007","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"9488","DOI":"10.1021\/bi1013134","article-title":"The \u03b1-Helical C-Terminal Domain of Full-Length Recombinant PrP Converts to an In-Register Parallel \u03b2-Sheet Structure in PrP Fibrils: Evidence from Solid State Nuclear Magnetic Resonance.","volume":"49","author":"R Tycko","year":"2010","journal-title":"Biochemistry"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"3258","DOI":"10.1021\/bi982714g","article-title":"Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein.","volume":"38","author":"S Liemann","year":"1999","journal-title":"Biochemistry"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1016\/j.jmb.2010.09.060","article-title":"Pathogenic Mutations in the Hydrophobic Core of the Human Prion Protein Can Promote Structural Instability and Misfolding.","volume":"404","author":"MW van der Kamp","year":"2010","journal-title":"J Mol Biol"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"31048","DOI":"10.1074\/jbc.273.47.31048","article-title":"Familial mutations and the thermodynamic stability of the recombinant human prion protein.","volume":"273","author":"W Swietnicki","year":"1998","journal-title":"J Biol Chem"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"33650","DOI":"10.1074\/jbc.C000483200","article-title":"Solution structure of the E200K variant of human prion protein - Implications for the mechanism of pathogenesis in familial prion diseases.","volume":"275","author":"YB Zhang","year":"2000","journal-title":"J Biol Chem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"49065","DOI":"10.1074\/jbc.M207511200","article-title":"Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form.","volume":"277","author":"DL Vanik","year":"2002","journal-title":"J Biol Chem"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"18008","DOI":"10.1074\/jbc.M313581200","article-title":"The effect of disease-associated mutations on the folding pathway of human prion protein.","volume":"279","author":"AC Apetri","year":"2004","journal-title":"J Biol Chem"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1126\/science.279.5352.827","article-title":"A transmembrane form of the prion protein in neurodegenerative disease.","volume":"279","author":"RS Hegde","year":"1998","journal-title":"Science"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"15","DOI":"10.3233\/JAD-2003-5103","article-title":"Aggresome formation by mutant prion proteins: the unfolding role of proteasomes in familial prion disorders.","volume":"5","author":"RS Mishra","year":"2003","journal-title":"J Alzheimers Dis"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"e1000479","DOI":"10.1371\/journal.ppat.1000479","article-title":"Selective processing and metabolism of disease-causing mutant prion proteins.","volume":"5","author":"A Ashok","year":"2009","journal-title":"PLoS Pathog"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"2201","DOI":"10.1016\/S0002-9440(10)64692-5","article-title":"Prion proteins with different conformations accumulate in Gerstmann-Str\u00e4ussler-Scheinker disease caused by A117V and F198S mutations.","volume":"158","author":"P Piccardo","year":"2001","journal-title":"Am J Pathol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1002\/prot.20804","article-title":"The determinants of stability in the human prion protein: insights into folding and misfolding from the analysis of the change in the stabilization energy distribution in different conditions.","volume":"62","author":"S Colacino","year":"2006","journal-title":"Proteins"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"3270","DOI":"10.1002\/prot.22834","article-title":"Structural facets of disease-linked human prion protein mutants: A molecular dynamic study.","volume":"78","author":"G Rossetti","year":"2010","journal-title":"Proteins"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"9874","DOI":"10.1021\/bi101449f","article-title":"Diverse effects on the native \u03b2-sheet of the human Prion Protein due to disease-associated mutations.","volume":"49","author":"W Chen","year":"2010","journal-title":"Biochemistry"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"3908","DOI":"10.1529\/biophysj.105.075341","article-title":"Structural instability of the prion protein upon M205S\/R mutations revealed by molecular dynamics simulations.","volume":"90","author":"T Hirschberger","year":"2006","journal-title":"Biophys J"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"e4296","DOI":"10.1371\/journal.pone.0004296","article-title":"Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.","volume":"4","author":"G Colombo","year":"2009","journal-title":"PLoS One"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"2825","DOI":"10.1007\/s00018-010-0363-1","article-title":"The structural intolerance of the PrP alpha-fold for polar substitution of the helix-3 methionines.","volume":"67","author":"S Lisa","year":"2010","journal-title":"Cell Mol Life Sci"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"e1000977","DOI":"10.1371\/journal.ppat.1000977","article-title":"Oxidation of Helix-3 methionines precedes the formation of PK resistant PrP.","volume":"6","author":"T Canello","year":"2010","journal-title":"PLoS Pathog"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"8866","DOI":"10.1021\/bi800801f","article-title":"Methionine sulfoxides on PrPSc: a prion-specific covalent signature.","volume":"47","author":"T Canello","year":"2008","journal-title":"Biochemistry"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"7756","DOI":"10.1073\/pnas.0902688106","article-title":"Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein.","volume":"106","author":"C Wolschner","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.1016\/j.bpj.2010.01.014","article-title":"Predicting interaction sites from the energetics of isolated proteins: a new approach to epitope mapping.","volume":"98","author":"G Scarabelli","year":"2010","journal-title":"Biophys J"},{"key":"ref38","first-page":"2554","article-title":"Crystal structure of human prion protein bound to a therapeutic antibody Proc Natl Acad Sci U S A","volume":"106","author":"SV Antonyuk","year":"2009"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/36337","article-title":"Prion (PrPSc)-specific epitope defined by a monoclonal antibody.","volume":"390","author":"C Korth","year":"1997","journal-title":"Nature"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1038\/35089090","article-title":"Antibodies inhibit prion propagation and clear cell cultures of prion infectivity.","volume":"412","author":"D Peretz","year":"2001","journal-title":"Nature"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"e3872","DOI":"10.1371\/journal.pone.0003872","article-title":"The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.","volume":"3","author":"M Polymenidou","year":"2008","journal-title":"PLoS One"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"11921","DOI":"10.1073\/pnas.0702671104","article-title":"Hot spots in prion protein for pathogenic conversion.","volume":"104","author":"K Kuwata","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"12853","DOI":"10.1021\/jp905572w","article-title":"Regulating the conformation of prion protein through ligand binding.","volume":"113","author":"N Yamamoto","year":"2009","journal-title":"J Phys Chem B"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"10069","DOI":"10.1073\/pnas.94.19.10069","article-title":"Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation.","volume":"94","author":"K Kaneko","year":"1997","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"15489","DOI":"10.1074\/jbc.M100288200","article-title":"Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain.","volume":"276","author":"M Horiuchi","year":"2001","journal-title":"J Biol Chem"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"10254","DOI":"10.1073\/pnas.0400014101","article-title":"Insight into the PrPC\u2013&gt;PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants.","volume":"101","author":"F Eghiaian","year":"2004","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"3741","DOI":"10.1099\/vir.0.82083-0","article-title":"Ovine prion protein variant A136R154L168Q171 increases resistance to experimental challenge with bovine spongiform encephalopathy agent.","volume":"87","author":"W Goldmann","year":"2006","journal-title":"J Gen Virol"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"17610","DOI":"10.1073\/pnas.1009062107","article-title":"Pharmacological chaperone for the structured domain of human prion protein.","volume":"107","author":"AJ Nicoll","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.jmb.2009.04.040","article-title":"NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects.","volume":"389","author":"B Christen","year":"2009","journal-title":"J Mol Biol"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1073\/pnas.0810680105","article-title":"De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis.","volume":"106","author":"CJ Sigurdson","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1126\/science.1186121","article-title":"Biochemistry. An ensemble view of allostery.","volume":"237","author":"V Hilser","year":"2010","journal-title":"Science"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1126\/science.1169377","article-title":"Sending signals dynamically.","volume":"324","author":"RG Smock","year":"2009","journal-title":"Science"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1038\/nchembio.232","article-title":"The role of dynamic conformational ensembles in biomolecular recognition.","volume":"5","author":"DD Boehr","year":"2009","journal-title":"Nat Chem Biol"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1080\/10715760600918142","article-title":"Protein oxidation and aging.","volume":"40","author":"ER Stadtman","year":"2006","journal-title":"Free Radic Res"},{"key":"ref55","first-page":"229","article-title":"Neurodegeneration and oxidative stress: prion disease results from loss of antioxidant defence.","volume":"43","author":"DR Brown","year":"2005","journal-title":"Folia Neuropathol"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"7414","DOI":"10.1073\/pnas.0607745104","article-title":"Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen\/deuterium exchange and disulfide linkage.","volume":"104","author":"F Eghiaian","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/0263-7855(90)80070-V","article-title":"What if: a molecular modeling and drug design program.","volume":"8","author":"G Vriend","year":"1990","journal-title":"J Mol Graph"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0019093","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,6,10]],"date-time":"2019-06-10T07:09:21Z","timestamp":1560150561000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0019093"}},"subtitle":[],"editor":[{"given":"Annalisa","family":"Pastore","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2011,4,28]]},"references-count":57,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2011,4,28]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0019093","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,4,28]]}}}