{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T07:36:19Z","timestamp":1762673779004,"version":"build-2065373602"},"reference-count":42,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2010,8,1]],"date-time":"2010-08-01T00:00:00Z","timestamp":1280620800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2010,8,1]],"date-time":"2010-08-01T00:00:00Z","timestamp":1280620800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2010,8]]},"DOI":"10.1016\/j.jmb.2010.06.008","type":"journal-article","created":{"date-parts":[[2010,6,11]],"date-time":"2010-06-11T06:30:33Z","timestamp":1276237833000},"page":"7-12","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":16,"title":["The Unfolded State of the Murine Prion Protein and Properties of Single-point Mutants Related to Human Prion Diseases"],"prefix":"10.1016","volume":"401","author":[{"given":"Christian","family":"Gerum","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kai","family":"Schlepckow","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Harald","family":"Schwalbe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2010.06.008_bib1","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner","year":"1998","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.06.008_bib2","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/0014-5793(96)00610-2","article-title":"The ninth Datta lecture. Molecular biology of transmissible spongiform encephalopathies","volume":"389","author":"Weissmann","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jmb.2010.06.008_bib3","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1038\/214764a0","article-title":"Does the agent of scrapie replicate without nucleic acid?","volume":"214","author":"Alper","year":"1967","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2010.06.008_bib4","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1038\/2151043a0","article-title":"Self-replication and scrapie","volume":"215","author":"Griffith","year":"1967","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2010.06.008_bib5","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/S0092-8674(03)01031-6","article-title":"Mammalian prion biology: one century of evolving concepts","volume":"116","author":"Aguzzi","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2010.06.008_bib6","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1146\/annurev.neuro.24.1.519","article-title":"Prion diseases of humans and animals: their causes and molecular basis","volume":"24","author":"Collinge","year":"2001","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.jmb.2010.06.008_bib7","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1038\/nrmicro1025","article-title":"The state of the prion","volume":"2","author":"Weissmann","year":"2004","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jmb.2010.06.008_bib8","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1007\/s00439-005-0020-1","article-title":"Genetic prion disease: the EUROCJD experience","volume":"118","author":"Kov\u00e1cs","year":"2005","journal-title":"Hum. Genet."},{"key":"10.1016\/j.jmb.2010.06.008_bib9","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/sj.ejhg.5201544","article-title":"Prion disease genetics","volume":"14","author":"Mead","year":"2006","journal-title":"Eur. J. Hum. Genet."},{"key":"10.1016\/j.jmb.2010.06.008_bib10","doi-asserted-by":"crossref","first-page":"7672","DOI":"10.1021\/bi00245a003","article-title":"Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy","volume":"30","author":"Caughey","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.06.008_bib11","doi-asserted-by":"crossref","first-page":"10962","DOI":"10.1073\/pnas.90.23.10962","article-title":"Conversion of \u03b1-helices into \u03b2-sheets features in the formation of the scrapie prion proteins","volume":"90","author":"Pan","year":"1993","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.06.008_bib12","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1038\/11507","article-title":"Structural mobility of the human prion protein probed by backbone hydrogen exchange","volume":"6","author":"Hosszu","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jmb.2010.06.008_bib13","doi-asserted-by":"crossref","first-page":"16649","DOI":"10.1021\/bi051277k","article-title":"Definable equilibrium states in the folding of human prion protein","volume":"44","author":"Hosszu","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.06.008_bib14","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":"Swietnicki","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.06.008_bib15","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":"10.1016\/j.jmb.2010.06.008_bib16","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":"Apetri","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.06.008_bib17","doi-asserted-by":"crossref","first-page":"44589","DOI":"10.1074\/jbc.C200507200","article-title":"Kinetic intermediate in the folding of human prion protein","volume":"277","author":"Apetri","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.06.008_bib18","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.1126\/science.1183748","article-title":"Generating a prion with bacterially expressed recombinant prion protein","volume":"327","author":"Wang","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.jmb.2010.06.008_bib19","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":"Makarava","year":"2010","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.jmb.2010.06.008_bib20","doi-asserted-by":"crossref","first-page":"9452","DOI":"10.1002\/anie.200903771","article-title":"Unfolded-state structure and dynamics influence the fibril formation of human prion protein","volume":"48","author":"Gerum","year":"2009","journal-title":"Angew. Chem."},{"key":"10.1016\/j.jmb.2010.06.008_bib21","doi-asserted-by":"crossref","first-page":"2172","DOI":"10.1002\/pro.231","article-title":"Differential stability of the bovine prion protein upon urea unfolding","volume":"18","author":"Julien","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2010.06.008_bib22","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1002\/bip.20481","article-title":"The effect of the osmolyte trimethylamine N-oxide on the stability of the prion protein at low pH","volume":"82","author":"Granata","year":"2006","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2010.06.008_bib23","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":"Vanik","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.06.008_bib24","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0167-4838(99)00038-2","article-title":"Multiple folding pathways for heterologously expressed human prion protein","volume":"1431","author":"Jackson","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2010.06.008_bib25","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1023\/A:1022243006871","article-title":"Study of stability of variants of ovine prions with different susceptibilities to scrapie","volume":"71","author":"Rezaei","year":"2003","journal-title":"J. Thermal Anal. Cal."},{"key":"10.1016\/j.jmb.2010.06.008_bib26","doi-asserted-by":"crossref","first-page":"12522","DOI":"10.1074\/jbc.M211599200","article-title":"The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein","volume":"278","author":"Speare","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.06.008_bib27","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1021\/bi991967m","article-title":"Aggregation and fibrillization of the recombinant human prion protein huPrP90-231","volume":"39","author":"Swietnicki","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.06.008_bib28","doi-asserted-by":"crossref","first-page":"6982","DOI":"10.1021\/bi010232q","article-title":"On the mechanism of \u03b1-helix to \u03b2-sheet transition in the recombinant prion protein","volume":"40","author":"Morillas","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.06.008_bib29","doi-asserted-by":"crossref","first-page":"15880","DOI":"10.1021\/bi051455+","article-title":"Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231","volume":"44","author":"Apetri","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.06.008_bib30","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1016\/j.jmb.2008.07.052","article-title":"Evidence for stepwise formation of amyloid fibrils by the mouse prion protein","volume":"382","author":"Jain","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.06.008_bib31","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1016\/j.jmb.2005.06.040","article-title":"Competing pathways determine fibril morphology in the self-assembly of \u03942-microglobulin into amyloid","volume":"351","author":"Gosal","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.06.008_bib32","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1038\/nbt1012","article-title":"Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins","volume":"22","author":"Fernandez-Escamilla","year":"2004","journal-title":"Nat. Biotech."},{"key":"10.1016\/j.jmb.2010.06.008_bib33","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature01891","article-title":"Rationalization of the effects of mutations on peptide and protein aggregation rates","volume":"424","author":"Chiti","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2010.06.008_bib34","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1002\/cbic.200500196","article-title":"Characterization of disulfide bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR","volume":"6","author":"Collins","year":"2005","journal-title":"ChemBioChem"},{"key":"10.1016\/j.jmb.2010.06.008_bib35","first-page":"359","article-title":"Pulse sequences for removal of the effects of cross correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins","volume":"97","author":"Kay","year":"1992","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.jmb.2010.06.008_bib36","doi-asserted-by":"crossref","first-page":"5984","DOI":"10.1021\/bi00185a040","article-title":"Backbone dynamics of a free and a phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation","volume":"33","author":"Farrow","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.06.008_bib37","doi-asserted-by":"crossref","first-page":"10743","DOI":"10.1021\/ja0204776","article-title":"An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates","volume":"124","author":"Korshnev","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2010.06.008_bib38","unstructured":"Goddard, T. D. & Kneller, D. G. Sparky 3. University of California, San Francisco."},{"key":"10.1016\/j.jmb.2010.06.008_bib39","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/BF00227471","article-title":"1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects","volume":"5","author":"Wishart","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2010.06.008_bib40","doi-asserted-by":"crossref","first-page":"2970","DOI":"10.1021\/ja003760i","article-title":"Sequence-dependent correction of random coil chemical shifts","volume":"123","author":"Schwarzinger","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2010.06.008_bib41","first-page":"565","article-title":"Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy","volume":"67","author":"Bax","year":"1986","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.jmb.2010.06.008_bib42","doi-asserted-by":"crossref","first-page":"5490","DOI":"10.1021\/ja00014a071","article-title":"Empirical correlation between protein backbone conformation and C\u03b1 and C\u03b2 13C nuclear magnetic resonance chemical shifts","volume":"113","author":"Spera","year":"1991","journal-title":"J. Am. Chem. Soc."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610006248?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610006248?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T06:11:07Z","timestamp":1762668667000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283610006248"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,8]]},"references-count":42,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2010,8]]}},"alternative-id":["S0022283610006248"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2010.06.008","relation":{},"ISSN":["0022-2836"],"issn-type":[{"type":"print","value":"0022-2836"}],"subject":[],"published":{"date-parts":[[2010,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The Unfolded State of the Murine Prion Protein and Properties of Single-point Mutants Related to Human Prion Diseases","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2010.06.008","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}