Self-assembly of recombinant prion protein of 106 residues

IV Baskakov, C Aagaard, I Mehlhorn, H Wille… - Biochemistry, 2000 - ACS Publications
The central event in the pathogenesis of prion diseases is a profound conformational
change of the prion protein (PrP) from an α-helical (PrPC) to a β-sheet-rich isoform (PrPSc) …
被引用次数：88 相关文章

Self-assembly of recombinant prion protein of 106 residues.

IV Baskakov, C Aagaard, I Mehlhorn, H Wille, D Groth… - Biochemistry, 2000 - europepmc.org
The central event in the pathogenesis of prion diseases is a profound conformational
change of the prion protein (PrP) from an alpha-helical (PrP (C)) to a beta-sheet-rich isoform …

[引用][C] Self-Assembly of Recombinant Prion Protein of 106 Residues

IV Baskakov, C Aagaard, I Mehlhorn, H Wille, D Groth… - Biochemistry, 2000 - cir.nii.ac.jp
Self-Assembly of Recombinant Prion Protein of 106 Residues | CiNii Research CiNii 国立情報学
研究所 学術情報ナビゲータ[サイニィ] 詳細へ移動 検索フォームへ移動 論文・データをさがす 大学 …

Self-assembly of recombinant prion protein of 106 residues

IV Baskakov, C Aagaard, I Mehlhorn, H Wille… - …, 2000 - pubmed.ncbi.nlm.nih.gov
The central event in the pathogenesis of prion diseases is a profound conformational
change of the prion protein (PrP) from an alpha-helical (PrP (C)) to a beta-sheet-rich isoform …