{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T19:05:45Z","timestamp":1784055945799,"version":"3.55.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1006563","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2017,8,22]],"date-time":"2017-08-22T00:00:00Z","timestamp":1503360000000}}],"reference-count":77,"publisher":"Public Library of Science (PLoS)","issue":"8","license":[{"start":{"date-parts":[[2017,8,10]],"date-time":"2017-08-10T00:00:00Z","timestamp":1502323200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS045585"],"award-info":[{"award-number":["NS045585"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"DOI":"10.1371\/journal.ppat.1006563","type":"journal-article","created":{"date-parts":[[2017,8,10]],"date-time":"2017-08-10T18:18:12Z","timestamp":1502389092000},"page":"e1006563","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":52,"title":["Cross-seeding of prions by aggregated \u03b1-synuclein leads to transmissible spongiform encephalopathy"],"prefix":"10.1371","volume":"13","author":[{"given":"Elizaveta","family":"Katorcha","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natallia","family":"Makarava","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Young Jin","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1188-170X","authenticated-orcid":true,"given":"Iris","family":"Lindberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mervyn J.","family":"Monteiro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabor G.","family":"Kovacs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2821-0942","authenticated-orcid":true,"given":"Ilia V.","family":"Baskakov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2017,8,10]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"1516","DOI":"10.1056\/NEJM200105173442006","article-title":"Shattuck Lecture\u2014Neurodegenerative diseases and prions","volume":"344","author":"SB Prusiner","year":"2001","journal-title":"NEnglJMed"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"E189","DOI":"10.3390\/ijms17020189","article-title":"Molecular Pathological Classification of Neurodegenerative Diseases: Turning towards Precision Medicine","volume":"2","author":"GG Kovacs","year":"2016","journal-title":"Int J Mol Sci"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1046\/j.1440-1789.2001.00407.x","article-title":"An atypical case of sporadic Creutzfeldt-Jakob disease with Parkinson&apos;s disease","volume":"21","author":"T Iida","year":"2001","journal-title":"Neuropathology"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1111\/j.1440-1789.2007.00755.x","article-title":"A sporadic case of Creutzfeldt-Jakob disease with beta-amyloid deposits and alpha-synuclein inclusions","volume":"27","author":"A Vital","year":"2007","journal-title":"Neuropathology"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1007\/s00401-010-0766-y","article-title":"Variably protease-sensitive prionopathy in a PRNP codon 129 heterozygous UK patient with co-existing tay, \u03b1 synuclein and A\u03b2 pathology","volume":"120","author":"MW Head","year":"2010","journal-title":"Acta Neuropath"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1111\/j.1440-1789.2011.01232.x","article-title":"&quot;Preclinical&quot; MSA in definite Creutzfeldt-Jakob disease","volume":"32","author":"R Rodriguez-Diehl","year":"2012","journal-title":"Neuropathology"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1097\/NEN.0b013e3181abdae8","article-title":"The nigrostriatal pathway in Creutzfeldt-Jakob disease","volume":"68","author":"A Vital","year":"2009","journal-title":"J Neuropathol Exp Neurol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1136\/jnnp.71.1.33","article-title":"Patients with Alzheimer&apos;s disease and dementia with Lewy bodies mistaken for Creutzfeldt-Jakob disease","volume":"71","author":"HJ Tschampa","year":"2001","journal-title":"J Neurol Neurosurg Psychiatry"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"e82","DOI":"10.1186\/s13195-014-0082-1","article-title":"Prevalence of mixed pathologies in the aging brain","volume":"6","author":"J Rahimi","year":"2014","journal-title":"Alzheimers Res Ther"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/s00401-010-0713-y","article-title":"Genetic Creutzfeldt-Jakob disease associated with the E200K mutation: characterization of a complex proteinopathy","volume":"121","author":"GG Kovacs","year":"2011","journal-title":"Acta Neuropath"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1212\/WNL.55.9.1401","article-title":"Dementia with Lewy bodies in a neuropathologic series of suspected Creutzfeldt-Jakob disease","volume":"55","author":"S Haik","year":"2000","journal-title":"Neurology"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1007\/s00401-001-0499-z","article-title":"Alpha-synuclein-immunoreactive deposits in human and animal prion diseases","volume":"103","author":"S Haik","year":"2002","journal-title":"Acta Neuropath(Berlin)"},{"key":"ref13","first-page":"78","article-title":"Alpha-synuclein accumulates in the brain of scrapie-affected sheep and goats","volume":"137","author":"KT Adjou","year":"2007","journal-title":"JCompPathol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1007\/BF00713522","article-title":"Colocalization of prion protein and beta protein in the same amyloid plaques in patients with Gerstmann-Straussler syndrom","volume":"83","author":"M Miyazono","year":"1992","journal-title":"Acta Neuropathol"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1007\/BF00198444","article-title":"Ulstrastructural evidence for collocalization of kappa light chain- and beta 2-microglobulin -derived amyloid using double labelling immunogold electron microscopy","volume":"429","author":"M Takahashi","year":"1996","journal-title":"Virchows Arch"},{"key":"ref16","first-page":"113","article-title":"Colocalization of different types of amyloid in the walls of cerebral blood vessels of patients from cerebral amyloid angiopathy and spontaneous intracranial hemorrhage: a report of 5 cases","volume":"23","author":"RA Galuske","year":"2004","journal-title":"ClinNeuropathol"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1111\/bpa.12411","article-title":"Tau Pathology in Creutzfeldt-Jakob Disease Revisited","volume":"27","author":"GG Kovacs","year":"2017","journal-title":"Brain Pathol"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1097\/NEN.0b013e318217d95f","article-title":"Transmission of prion strains in a transgenic mouse model overexpressing human A53T mutated \u03b1-synuclein","volume":"70","author":"AL Mougenot","year":"2011","journal-title":"J Neuropathol Exp Neurol"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"184","DOI":"10.4161\/pri.19806","article-title":"Prion infection promotes extensive accumulation of \u03b1-synuclein in aged human \u03b1-synuclein transgenic mice","volume":"6","author":"E Masliah","year":"2012","journal-title":"Prion"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0092-8674(01)00427-5","article-title":"Prions affect the appearance of other prions: the story of [PIN(+)]","volume":"106","author":"IL Derkatch","year":"2001","journal-title":"Cell"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"12934","DOI":"10.1073\/pnas.0404968101","article-title":"Effects of Q\/N-rich, polyQ, and non-polyQ, amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro","volume":"101","author":"IL Derkatch","year":"2004","journal-title":"ProcAcadNatlSciUSA"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"172","DOI":"10.2353\/ajpath.2007.060576","article-title":"Cross-seeding and cross-competition in mouse apolipoprotein A-II amyloid fibrils and protein A amyloid fibrils","volume":"171","author":"J Yan","year":"2007","journal-title":"American Journal of Pathology"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/s00401-015-1525-x","article-title":"Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo","volume":"131","author":"B Vasconcelos","year":"2016","journal-title":"Acta Neuropath"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.cell.2013.05.057","article-title":"Distinct alpha-synuclein strains differentially promote tau inclusions in neurons","volume":"154","author":"JL Guo","year":"2013","journal-title":"Cell"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1126\/science.1082324","article-title":"Initiation and synergistic fibrillization of tau and alpha-synuclein","volume":"300","author":"BI Giasson","year":"2003","journal-title":"Science"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"7345","DOI":"10.1523\/JNEUROSCI.6351-11.2012","article-title":"A New Mechanism for Transmissible Prion Diseases","volume":"32","author":"N Makarava","year":"2012","journal-title":"J Neurosci"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1074\/jbc.M112.419531","article-title":"Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification","volume":"288","author":"N Makarava","year":"2013","journal-title":"J Biol Chem"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"e1002419","DOI":"10.1371\/journal.ppat.1002419","article-title":"Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease","volume":"7","author":"N Makarava","year":"2011","journal-title":"PLoS Pathogen"},{"key":"ref29","first-page":"1334","article-title":"Dichotomous versus palm-type mechanisms of lateral assembly of amyloid fibrils","volume":"15","author":"N Makarava","year":"2006","journal-title":"ProtScience"},{"key":"ref30","first-page":"36704","article-title":"Highly promiscuous nature of prion polymerization","volume":"282","author":"N Makarava","year":"2007","journal-title":"JBiolChem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1038\/ncomms1730","article-title":"Fast and ultrasensitive method for quantitating prion infectivity titer","volume":"3","author":"N Makarava","year":"2012","journal-title":"Nature Commun"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"2575","DOI":"10.1038\/ncomms3575","article-title":"Structural and functional characterization of two alpha-synuclein strains","volume":"4","author":"L Bousset","year":"2013","journal-title":"Nat Commun"},{"key":"ref33","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":"H Heise","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref34","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":"SB Nielsen","year":"2013","journal-title":"PLoS One"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"10328","DOI":"10.1073\/pnas.1604645113","article-title":"Mutations associated with familial Parkinson\u2019s disease alter the initiation and amplification steps of \u03b1-synuclein aggregation","volume":"113","author":"P Flagmeier","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"37630","DOI":"10.1038\/srep37630","article-title":"Nanomolar oligomerization and selective co-aggregation of \u03b1-synuclein pathogenic mutants revealed by single-molecule fluorescence","author":"E Sierecki","year":"2016","journal-title":"Sci Rep"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"358","DOI":"10.3389\/fnins.2016.00358","article-title":"Multifaceted role of sialylation in prion diseases","volume":"10","author":"IV Baskakov","year":"2016","journal-title":"Front Neurosci"},{"key":"ref38","first-page":"40429","article-title":"Identification of Novel Proteinase K-resistant C-terminal Fragments of PrP in Creutzfeldt-Jakob Disease","volume":"278","author":"WQ Zou","year":"2003","journal-title":"JBiolChem"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"61","DOI":"10.4161\/pri.1.1.3828","article-title":"H-type bovine spongiform encephalopathy: complex molecular features and similarities with human prion diseases","volume":"1","author":"AG Biacabe","year":"2007","journal-title":"Prion"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.virusres.2014.10.002","article-title":"The diversity and relationship of prion protein self-replicating states","volume":"207","author":"N Klimova","year":"2015","journal-title":"Virus Research"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"13434","DOI":"10.1021\/bi9610562","article-title":"Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain","volume":"35","author":"DA Kocisko","year":"1996","journal-title":"Biochemistry"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.1093\/brain\/awg205","article-title":"Regional heterogeneity of cellular prion protein isoforms in the mouse brain","volume":"126","author":"V Beringue","year":"2003","journal-title":"Brain"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1186\/s40478-015-0248-5","article-title":"Two alternative pathways for generating transmissible prion disease de novo","volume":"3","author":"N Makarava","year":"2015","journal-title":"Acta Neuropathologica Communications"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1016\/j.ajpath.2015.11.013","article-title":"New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions","volume":"186","author":"N Makarava","year":"2016","journal-title":"Am J Pathol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1016\/j.ajpath.2013.07.024","article-title":"Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles","volume":"183","author":"GG Kovacs","year":"2013","journal-title":"Am J Pathol"},{"key":"ref46","first-page":"15988","article-title":"The same primary structure of the prion protein yields two distinct self-propagating states","volume":"283","author":"N Makarava","year":"2008","journal-title":"JBiolChem"},{"key":"ref47","first-page":"908","article-title":"Two amyloid states of the prion protein display significantly different folding patterns","volume":"400","author":"VG Ostapchenko","year":"2010","journal-title":"JMolBiol"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"e12","DOI":"10.1371\/journal.ppat.0020012","article-title":"Efficient Transmission and Characterization of Creutzfeldt-Jakob Disease Strains in Bank Voles","volume":"2","author":"R Nonno","year":"2006","journal-title":"PLOS Pathog"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"e1003219","DOI":"10.1371\/journal.ppat.1003219","article-title":"Chronic wasting disease in bank voles: characterisation of the shortest incubation time model for prion diseases","volume":"9","author":"MA Di Bari","year":"2013","journal-title":"PLoS Pathog"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/S1474-4422(06)70413-6","article-title":"Predicting susceptibility and incubation time of human-to-human transmission of vCJD","volume":"5","author":"MT Bishop","year":"2006","journal-title":"Lancet Neurol"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"6358","DOI":"10.1093\/emboj\/cdf653","article-title":"BSE prions propagate as either variant CJD-like or sporadic CJD-like prion stains in transgenic mice expressing human prion protein","volume":"21","author":"EA Asante","year":"2002","journal-title":"EMBO J"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"e1003759","DOI":"10.1371\/journal.ppat.1003759","article-title":"The Evolution of Transmissible Prions: The Role of Deformed Templating","volume":"9","author":"N Makarava","year":"2013","journal-title":"PLOS Pathog"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"2618","DOI":"10.1016\/j.febslet.2009.05.044","article-title":"Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classification","volume":"583","author":"IV Baskakov","year":"2009","journal-title":"FEBS Lett"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"18349","DOI":"10.1073\/pnas.0806270105","article-title":"Molecular structural basis for polymorphism in Alzheimer&apos;s beta-amyloid fibrils","volume":"105","author":"AK Paravastu","year":"2008","journal-title":"ProcAcadNatlSciUSA"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","article-title":"Molecular structure of \u03b2-amyloid fibrils in Alzheimer&apos;s disease brain tissue","volume":"154","author":"J Lu","year":"2013","journal-title":"Cell"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"10329","DOI":"10.1073\/pnas.1408968111","article-title":"Distinct synthetic A\u03b2 prion strains producing different amyloid deposits in bigenic mice","volume":"111","author":"J Stohr","year":"2014","journal-title":"Proc Acad Natl Sci U S A"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"10323","DOI":"10.1073\/pnas.1408900111","article-title":"Serial propagation of distinct strains of A\u03b2 prions from Alzheimer&apos;s disease patients","volume":"111","author":"CJ Watts","year":"2014","journal-title":"Proc Acad Natl Sci U S A"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"7443","DOI":"10.1073\/pnas.0812033106","article-title":"Seeded growth of b-amyloid fibrils from Alzheimer&apos;s brain-derived fibrils produces a distinct fibril structure","volume":"106","author":"AK Paravastu","year":"2009","journal-title":"ProcAcadNatlSciUSA"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1017\/S0317167100047156","article-title":"Coexistance of idiopathic Parkinson&apos;s disease and Creutzfeldt Jakob disease","volume":"12","author":"C Ezrin-Waters","year":"1985","journal-title":"Can J Neurol Sci"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"\u00e0-Synuclein in Lewy bodies","volume":"388","author":"MG Spillantini","year":"1997","journal-title":"Nature"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1002\/ana.21966","article-title":"First Appraisal of Brain Pathology Owing to A30P Mutant Alpha-Synuclein","volume":"67","author":"K Seidel","year":"2010","journal-title":"Ann Neurol"},{"key":"ref62","first-page":"S73","article-title":"Neuropathological Staging of Brain Pathology in Sporadic Parkinson\u2019s disease: Separating the Wheat from the Chaff","volume":"7","author":"H Braak","year":"2017","journal-title":"J Parkinsons Dis"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"13010","DOI":"10.1073\/pnas.0903691106","article-title":"Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein","volume":"106","author":"P Desplats","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"6016","DOI":"10.1523\/JNEUROSCI.0692-05.2005","article-title":"Intravesicular localization and exocytosis of alpha-synuclein and its aggregates","volume":"25","author":"HJ Lee","year":"2005","journal-title":"J Neurosci"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"6838","DOI":"10.1523\/JNEUROSCI.5699-09.2010","article-title":"Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival","volume":"30","author":"E Emmanouilidou","year":"2010","journal-title":"J Neurosci"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/1750-1326-7-42","article-title":"Exosomal cell-to-cell transmission of alpha synuclein oligomers","volume":"7","author":"KM Danzer","year":"2012","journal-title":"Mol Neurodegener"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.nbd.2014.05.020","article-title":"Intracellular processing of disease-associated \u03b1-synuclein in the human brain suggests prion-like cell-to-cell spread","volume":"69","author":"GG Kovacs","year":"2014","journal-title":"Neurobiol Dis"},{"key":"ref68","article-title":"Involvement of Cellular Prion Protein in \u03b1-Synuclein Transport in Neurons","author":"L Urrea","year":"2017","journal-title":"Mol Neurobiol"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"e0168700","DOI":"10.1371\/journal.pone.0168700","article-title":"Aggregated Alpha-Synuclein Transfer Efficiently between Cultured Human Neuron-Like Cells and Localize to Lysosomes","volume":"11","author":"J Domert","year":"2016","journal-title":"PLoS One"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1002\/path.1711660404","article-title":"Lysosomes as key organelles in the pathogenesis of prion encephalopathies","volume":"166","author":"L Laszlo","year":"1992","journal-title":"JPathol"},{"key":"ref71","first-page":"851","article-title":"Synthesis and trafficking of prion proteins in cultured cells","volume":"3","author":"A Taraboulos","year":"1992","journal-title":"MolBiolCell"},{"key":"ref72","first-page":"15922","article-title":"A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells","volume":"21","author":"SL Shyng","year":"1993","journal-title":"JBiolChem"},{"key":"ref73","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":"ref74","first-page":"645","article-title":"In vitro conversion of full length mammalian prion protein produces amyloid form with physical property of PrPSc","volume":"346","author":"OV Bocharova","year":"2005","journal-title":"JMolBiol"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"E4708","DOI":"10.1073\/pnas.1601091113","article-title":"The neural chaperone proSAAS blocks \u03b1-synuclein fibrillation and neurotoxicity","volume":"113","author":"TS Jarvela","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"e1001277","DOI":"10.1371\/journal.ppat.1001277","article-title":"Highly Efficient Protein Misfolding Cyclic Amplification","volume":"7","author":"N Gonzalez-Montalban","year":"2011","journal-title":"PLoS Pathogen"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"30205","DOI":"10.1074\/jbc.M112.392985","article-title":"Stabilization of a prion strain of synthetic origin requires multiple serial passages","volume":"287","author":"N Makarava","year":"2012","journal-title":"J Biol Chem"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1006563","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2017,8,22]],"date-time":"2017-08-22T00:00:00Z","timestamp":1503360000000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.ppat.1006563","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,26]],"date-time":"2024-06-26T04:30:44Z","timestamp":1719376244000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1006563"}},"subtitle":[],"editor":[{"given":"David","family":"Westaway","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2017,8,10]]},"references-count":77,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2017,8,10]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1006563","relation":{"new_version":[{"id-type":"doi","id":"10.1371\/journal.ppat.1006563","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,8,10]]}}}