{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T20:52:48Z","timestamp":1788382368413,"version":"build-2803163510"},"reference-count":51,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,8]],"date-time":"2020-09-08T00:00:00Z","timestamp":1599523200000},"content-version":"vor","delay-in-days":2776,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,2]]},"DOI":"10.1074\/jbc.m112.423715","type":"journal-article","created":{"date-parts":[[2012,12,4]],"date-time":"2012-12-04T12:04:46Z","timestamp":1354622686000},"page":"2994-3002","source":"Crossref","is-referenced-by-count":17,"title":["Burial of the Polymorphic Residue 129 in Amyloid Fibrils of Prion Stop Mutants"],"prefix":"10.1016","volume":"288","author":[{"given":"Lukasz","family":"Skora","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis","family":"Fonseca-Ornelas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Romina V.","family":"Hofele","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dietmar","family":"Riedel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin","family":"Giller","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jens","family":"Watzlawik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walter J.","family":"Schulz-Schaeffer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Henning","family":"Urlaub","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Becker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markus","family":"Zweckstetter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M112.423715_bib1","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1146\/annurev.pathmechdis.3.121806.154326","article-title":"Molecular mechanisms of prion pathogenesis","volume":"3","author":"Aguzzi","year":"2008","journal-title":"Annu. Rev. Pathol."},{"key":"10.1074\/jbc.M112.423715_bib2","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/1531-8249(199908)46:2<224::AID-ANA12>3.0.CO;2-W","article-title":"Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects","volume":"46","author":"Parchi","year":"1999","journal-title":"Ann. Neurol"},{"key":"10.1074\/jbc.M112.423715_bib3","doi-asserted-by":"crossref","first-page":"2566","DOI":"10.2353\/ajpath.2009.090623","article-title":"Similarities between forms of sheep scrapie and Creutzfeldt-Jakob disease are encoded by distinct prion types","volume":"175","author":"Wemheuer","year":"2009","journal-title":"Am. J. Pathol."},{"key":"10.1074\/jbc.M112.423715_bib4","doi-asserted-by":"crossref","first-page":"10168","DOI":"10.1073\/pnas.97.18.10168","article-title":"Genetic influence on the structural variations of the abnormal prion protein","volume":"97","author":"Parchi","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib5","first-page":"353","article-title":"Polymorphism at codon 129 of the prion protein gene determines cerebellar pathology in Creutzfeldt-Jakob disease","volume":"15","author":"Schulz-Schaeffer","year":"1996","journal-title":"Clin. Neuropathol"},{"key":"10.1074\/jbc.M112.423715_bib6","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1093\/brain\/awm063","article-title":"Creutzfeldt-Jakob disease in Germany: a prospective 12-year surveillance","volume":"130","author":"Heinemann","year":"2007","journal-title":"Brain"},{"key":"10.1074\/jbc.M112.423715_bib7","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/128_2011_166","article-title":"Transgenic mouse models and prion strains","volume":"305","author":"Telling","year":"2011","journal-title":"Top Curr. Chem."},{"key":"10.1074\/jbc.M112.423715_bib8","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0065-3233(01)57018-7","article-title":"Three-dimensional structures of prion proteins","volume":"57","author":"W\u00fcthrich","year":"2001","journal-title":"Adv. Protein Chem."},{"key":"10.1074\/jbc.M112.423715_bib9","doi-asserted-by":"crossref","first-page":"16990","DOI":"10.1073\/pnas.0909006106","article-title":"Natural and synthetic prion structure from x-ray fiber diffraction","volume":"106","author":"Wille","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib10","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1038\/nm883","article-title":"A prion protein epitope selective for the pathologically misfolded conformation","volume":"9","author":"Paramithiotis","year":"2003","journal-title":"Nat. Med."},{"key":"10.1074\/jbc.M112.423715_bib11","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nsmb.2035","article-title":"Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange","volume":"18","author":"Smirnovas","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1074\/jbc.M112.423715_bib12","doi-asserted-by":"crossref","first-page":"8342","DOI":"10.1073\/pnas.0402254101","article-title":"Evidence for assembly of prions with left-handed \u03b2-helices into trimers","volume":"101","author":"Govaerts","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib13","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.abb.2007.08.010","article-title":"Electron crystallography of the scrapie prion protein complexed with heavy metals","volume":"467","author":"Wille","year":"2007","journal-title":"Arch Biochem. Biophys."},{"key":"10.1074\/jbc.M112.423715_bib14","doi-asserted-by":"crossref","first-page":"81","DOI":"10.4161\/pri.2.2.7059","article-title":"Left handed \u03b2 helix models for mammalian prion fibrils","volume":"2","author":"Kunes","year":"2008","journal-title":"Prion"},{"key":"10.1074\/jbc.M112.423715_bib15","doi-asserted-by":"crossref","first-page":"1510","DOI":"10.1073\/pnas.0608447104","article-title":"\u03b2-Sheet core of human prion protein amyloid fibrils as determined by hydrogen\/deuterium exchange","volume":"104","author":"Lu","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib16","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1002\/jms.1572","article-title":"Hydrogen\/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils","volume":"44","author":"Nazabal","year":"2009","journal-title":"J. Mass Spectrom"},{"key":"10.1074\/jbc.M112.423715_bib17","doi-asserted-by":"crossref","first-page":"32303","DOI":"10.1074\/jbc.M110.114504","article-title":"Probing the conformation of a prion protein fibril with hydrogen exchange","volume":"285","author":"Damo","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.423715_bib18","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1073\/pnas.0307178101","article-title":"From conversion to aggregation: protofibril formation of the prion protein","volume":"101","author":"DeMarco","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib19","first-page":"358","article-title":"Immunohistological evaluation of Creutzfeldt-Jakob disease with reference to the type PrPres deposition","volume":"15","author":"Tateishi","year":"1996","journal-title":"Clin. Neuropathol"},{"key":"10.1074\/jbc.M112.423715_bib20","doi-asserted-by":"crossref","first-page":"12069","DOI":"10.1073\/pnas.2033281100","article-title":"Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation","volume":"100","author":"Kundu","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib21","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S1097-2765(04)00155-8","article-title":"Molecular basis of barriers for interspecies transmissibility of mammalian prions","volume":"14","author":"Vanik","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M112.423715_bib22","first-page":"30242","article-title":"Prion protein helix1 promotes aggregation but is not converted into \u03b2-sheet","volume":"281","author":"Watzlawik","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.423715_bib23","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/ana.22264","article-title":"Familial prion disease with Alzheimer disease-like Tau pathology and clinical phenotype","volume":"69","author":"Jayadev","year":"2011","journal-title":"Ann. Neurol"},{"key":"10.1074\/jbc.M112.423715_bib24","doi-asserted-by":"crossref","first-page":"6284","DOI":"10.1073\/pnas.0711716105","article-title":"Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils","volume":"105","author":"Helmus","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib25","doi-asserted-by":"crossref","first-page":"2393","DOI":"10.1021\/ja909827v","article-title":"Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy","volume":"132","author":"Helmus","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1074\/jbc.M112.423715_bib26","doi-asserted-by":"crossref","first-page":"13934","DOI":"10.1021\/ja206469q","article-title":"Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy","volume":"133","author":"Helmus","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1074\/jbc.M112.423715_bib27","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":"Liemann","year":"1999","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M112.423715_bib28","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1002\/pro.570","article-title":"Conserved core of amyloid fibrils of wild type and A30P mutant \u03b1-synuclein","volume":"20","author":"Cho","year":"2011","journal-title":"Protein Sci."},{"key":"10.1074\/jbc.M112.423715_bib29","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"},{"key":"10.1074\/jbc.M112.423715_bib30","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1021\/ar00028a001","article-title":"Methodological advances in protein","volume":"26","author":"Bax","year":"1993","journal-title":"Acc. Chem. Res."},{"key":"10.1074\/jbc.M112.423715_bib31","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":"10.1074\/jbc.M112.423715_bib32","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1063\/1.1695690","article-title":"Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient","volume":"42","author":"Stejskal","year":"1965","journal-title":"J. Chem. Phys."},{"key":"10.1074\/jbc.M112.423715_bib33","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1006\/jmra.1995.1176","article-title":"An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses","volume":"115","author":"Wu","year":"1995","journal-title":"J. Magn. Reson. A"},{"key":"10.1074\/jbc.M112.423715_bib34","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/S0003-2697(02)00612-7","article-title":"Protein surface mapping by chemical oxidation: structural analysis by mass spectrometry","volume":"313","author":"Sharp","year":"2003","journal-title":"Anal. Biochem."},{"key":"10.1074\/jbc.M112.423715_bib35","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1021\/ac026117i","article-title":"Stop and go extraction tips for matrix-assisted laser desorption\/ionization, nanoelectrospray, and LC\/MS sample pretreatment in proteomics","volume":"75","author":"Rappsilber","year":"2003","journal-title":"Anal. Chem."},{"key":"10.1074\/jbc.M112.423715_bib36","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1038\/nbt.1511","article-title":"MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies, and proteome-wide protein quantification","volume":"26","author":"Cox","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"10.1074\/jbc.M112.423715_bib37","doi-asserted-by":"crossref","first-page":"1794","DOI":"10.1021\/pr101065j","article-title":"Andromeda: a peptide search engine integrated into the MaxQuant environment","volume":"10","author":"Cox","year":"2011","journal-title":"J. Proteome Res."},{"key":"10.1074\/jbc.M112.423715_bib38","doi-asserted-by":"crossref","first-page":"1692","DOI":"10.1016\/j.jasms.2008.07.013","article-title":"Quantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: application to galectin-1","volume":"19","author":"Charv\u00e1tov\u00e1","year":"2008","journal-title":"J. Am. Soc. Mass Spectrom"},{"key":"10.1074\/jbc.M112.423715_bib39","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1051\/jphysrad:01934005010049700","article-title":"Brownian motion of an ellipsoid. I. Dielectric dispersion for ellipsoidal molecules","volume":"5","author":"Perrin","year":"1934","journal-title":"J. Phys. Radium"},{"key":"10.1074\/jbc.M112.423715_bib40","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1038\/nsb792","article-title":"Mapping the core of the \u03b22-microglobulin amyloid fibril by H\/D exchange","volume":"9","author":"Hoshino","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"10.1074\/jbc.M112.423715_bib41","doi-asserted-by":"crossref","first-page":"3514","DOI":"10.1021\/cr0682047","article-title":"Hydroxyl radical-mediated modification of proteins as probes for structural proteomics","volume":"107","author":"Xu","year":"2007","journal-title":"Chem. Rev."},{"key":"10.1074\/jbc.M112.423715_bib42","doi-asserted-by":"crossref","first-page":"15534","DOI":"10.1021\/bi051369+","article-title":"Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation","volume":"44","author":"Breydo","year":"2005","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M112.423715_bib43","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1073\/pnas.93.2.744","article-title":"Vascular variant of prion protein cerebral amyloidosis with Tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP","volume":"93","author":"Ghetti","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.423715_bib44","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1007\/s00401-009-0609-x","article-title":"Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP","volume":"119","author":"Jansen","year":"2010","journal-title":"Acta Neuropathol"},{"key":"10.1074\/jbc.M112.423715_bib45","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1002\/j.1460-2075.1991.tb07977.x","article-title":"Amyloid protein of Gerstmann-Str\u00e4ussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58","volume":"10","author":"Tagliavini","year":"1991","journal-title":"EMBO J."},{"key":"10.1074\/jbc.M112.423715_bib46","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1006\/jmbi.1999.2831","article-title":"Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein","volume":"289","author":"Wopfner","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1074\/jbc.M112.423715_bib47","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1128\/JVI.72.2.1153-1159.1998","article-title":"Overexpression of nonconvertible PrPc \u0394114\u2013121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrPSc accumulation","volume":"72","author":"H\u00f6lscher","year":"1998","journal-title":"J. Virol."},{"key":"10.1074\/jbc.M112.423715_bib48","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1002\/pro.2170","article-title":"Determination of amyloid core structure using chemical shifts","volume":"21","author":"Skora","year":"2012","journal-title":"Protein Sci."},{"key":"10.1074\/jbc.M112.423715_bib49","doi-asserted-by":"crossref","first-page":"8190","DOI":"10.1074\/jbc.M513417200","article-title":"Role of N-terminal familial mutations in prion protein fibrillization and prion amyloid propagation in vitro","volume":"281","author":"Jones","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.423715_bib50","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/352340a0","article-title":"Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease","volume":"352","author":"Palmer","year":"1991","journal-title":"Nature"},{"key":"10.1074\/jbc.M112.423715_bib51","doi-asserted-by":"crossref","first-page":"31390","DOI":"10.1074\/jbc.M401754200","article-title":"Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant: implications for disease susceptibility to Creutzfeldt-Jakob disease","volume":"279","author":"Tahiri-Alaoui","year":"2004","journal-title":"J. Biol. Chem."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820464191?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820464191?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M112.423715","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T15:22:49Z","timestamp":1641309769000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820464191"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,2]]},"references-count":51,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2013,2]]}},"alternative-id":["S0021925820464191"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m112.423715","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,2]]}}}