Copper and Zinc Interactions with Cellular Prion Proteins Change Solubility of Full-Length Glycosylated Isoforms and Induce the Occurrence of Heterogeneous Phenotypes

Open Access

Peer-reviewed

Research Article

Svetlana Brim,

Affiliation Institute for Hygiene, University of Münster, Robert Koch-Strasse 41, 48149 Münster, Germany
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Martin H. Groschup,

Affiliation Friedrich-Loeffler-Institute (FLI), Institute for Novel and Emerging Infectious Diseases, Boddenblick 5a, 17493 Greifswald, Insel Riems, Germany
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Thorsten Kuczius

* E-mail: thorsten.kuczius@ukmuenster.de

Affiliation Institute for Hygiene, University of Münster, Robert Koch-Strasse 41, 48149 Münster, Germany
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Zinc
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Solubility
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Copper
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Centrifugation
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Protein interactions
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Genetically modified animals
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Prion diseases
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Chemiluminescence
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