Title : Amino acid conditions near the GPI anchor attachment site of prion protein for the conversion and the GPI anchoring.

Pub. Date : 2010 Jan 22

PMID : 20040362






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored protein, and the C-terminal GPI anchor signal sequence (GPI-SS) of PrP is cleaved before GPI anchoring. Glycosylphosphatidylinositols prion protein Mus musculus
2 Prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored protein, and the C-terminal GPI anchor signal sequence (GPI-SS) of PrP is cleaved before GPI anchoring. Glycosylphosphatidylinositols prion protein Mus musculus
3 Prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored protein, and the C-terminal GPI anchor signal sequence (GPI-SS) of PrP is cleaved before GPI anchoring. Glycosylphosphatidylinositols prion protein Mus musculus
4 Prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored protein, and the C-terminal GPI anchor signal sequence (GPI-SS) of PrP is cleaved before GPI anchoring. Glycosylphosphatidylinositols prion protein Mus musculus
5 The present study shows that mutations in the GPI-SS can affect the GPI anchoring and the conversion efficiency of PrP. Glycosylphosphatidylinositols prion protein Mus musculus
6 We clarified for the first time the omega site of murine PrP and the amino acid conditions near the omega site for the conversion as well as GPI anchoring. Glycosylphosphatidylinositols prion protein Mus musculus