Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation

Misfolding of the mammalian prion protein (PrP) is implicated in the pathogenesis of prion diseases. We analyzed wild type PrP in comparison with different PrP mutants and identified determinants of the in vivo folding pathway of PrP. The complete N terminus of PrP including the putative transmembra...

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Veröffentlicht in:	The Journal of biological chemistry 2003-04, Vol.278 (17), p.14961-14970
Hauptverfasser:	Winklhofer, Konstanze F, Heske, Johanna, Heller, Ulrich, Reintjes, Anja, Muranyi, Walter, Moarefi, Ismail, Tatzelt, Jorg
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cell Membrane - chemistry Glycosylation Glycosylphosphatidylinositols Mannose Mice Polysaccharides - biosynthesis Polysaccharides - chemistry Protein Folding Protein Processing, Post-Translational Protein Structure, Tertiary Protein Transport PrPC Proteins - biosynthesis PrPC Proteins - chemistry PrPC Proteins - genetics PrPC Proteins - metabolism Transfection Tumor Cells, Cultured
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