Title : Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion protein.

Pub. Date : 2010 Aug 23

PMID : 20808809






6 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Enzymatic depletion of endogenous nucleic acids or heparan sulphate (HS) from the PrP(C) substrate was found to specifically prevent PrP(res) formation seeded by mouse derived PrP(Sc). Heparitin Sulfate prion protein Mus musculus
2 Enzymatic depletion of endogenous nucleic acids or heparan sulphate (HS) from the PrP(C) substrate was found to specifically prevent PrP(res) formation seeded by mouse derived PrP(Sc). Heparitin Sulfate prion protein Mus musculus
3 Enzymatic depletion of endogenous nucleic acids or heparan sulphate (HS) from the PrP(C) substrate was found to specifically prevent PrP(res) formation seeded by mouse derived PrP(Sc). Heparitin Sulfate prion protein Mus musculus
4 Enzymatic depletion of endogenous nucleic acids or heparan sulphate (HS) from the PrP(C) substrate was found to specifically prevent PrP(res) formation seeded by mouse derived PrP(Sc). Heparitin Sulfate prion protein Mus musculus
5 Enzymatic depletion of endogenous nucleic acids or heparan sulphate (HS) from the PrP(C) substrate was found to specifically prevent PrP(res) formation seeded by mouse derived PrP(Sc). Heparitin Sulfate prion protein Mus musculus
6 Enzymatic depletion of endogenous nucleic acids or heparan sulphate (HS) from the PrP(C) substrate was found to specifically prevent PrP(res) formation seeded by mouse derived PrP(Sc). Heparitin Sulfate prion protein Mus musculus