Associated Papers
Disulfide-crosslink scanning reveals prion-induced conformational changes and prion strain-specific structures of the pathological prion protein PrPSc.
Taguchi Y et al.
The Journal of Biological Chemistry, 2018
Changing the solvent accessibility of the prion protein disulfide bond markedly influences its trafficking and effect on cell function.
Tabrett CA et al.
The Biochemical Journal, 2010
alpha-Helical domains promote translocation of intrinsically disordered polypeptides into the endoplasmic reticulum.
Miesbauer M et al.
The Journal of Biological Chemistry, 2009
Subcellular trafficking abnormalities of a prion protein with a disrupted disulfide loop.
Yanai A et al.
Febs Letters, 1999
Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix.
Muramoto T et al.
Nature Medicine, 1997
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