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Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms

AuthorsLisa, Silvia; Domingo, Beatriz; Martínez, Javier CSIC ORCID; Gilch, Sabine; Llopis, J. F.; Schätzl, Hermann M.
Issue Date2012
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 287: 36693-36701 (2012)
AbstractBackground: In vivo folding could play an essential role in prion neurodegenerations. Results: Artificial mutants causing labile PrP folds when expressed in cells originate toxic CtmPrP featured by the absence of the intramolecular disulfide bond. Conclusion: Oxidative folding impairment facilitates the formation of the toxic PrP forms. Significance: Unveiling the mechanism facilitating the formation of toxic PrP forms is crucial for the understanding and prevention of prion disorders. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
DescriptionThis article has been withdrawn (November 15, 2017)
Publisher version (URL)
Identifiersdoi: 10.1074/jbc.M112.398776
issn: 0021-9258
Appears in Collections:(IQFR) Artículos

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