Amyloid Core Formed of Full-Length Recombinant Mouse Prion Protein Involves Sequence 127–143 but Not Sequence 107–126

Development of the Structural Core and of Conformational Heterogeneity during the Conversion of Oligomers of the Mouse Prion Protein to Worm-like Amyloid Fibrils

(2012) Jogender Singh et al.   JOURNAL OF MOLECULAR BIOLOGY

Dynamics of polymerization shed light on the mechanisms that lead to multiple amyloid structures of the prion protein

(2011) Maria-Teresa Alvarez-Martinez et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment

(2011) Tai-Yan Liao et al.   FEBS Journal

Globular Domain of the Prion Protein Needs to Be Unlocked by Domain Swapping to Support Prion Protein Conversion

(2011) Iva Hafner-Bratkovič et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular Structure of Amyloid Fibrils Formed by Residues 127 to 147 of the Human Prion Protein

(2010) Ni-Shian Lin et al.   CHEMISTRY-A EUROPEAN JOURNAL

FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence

(2009) S. O. Garbuzynskiy et al.   BIOINFORMATICS

Core Structure of Amyloid Fibrils Formed by Residues 106–126 of the Human Prion Protein

(2009) Patrick Walsh et al.   STRUCTURE

Critical Region for Amyloid Fibril Formation of Mouse Prion Protein: Unusual Amyloidogenic Properties of the Helix 2 Peptide†

(2008) Kei-ichi Yamaguchi et al.   BIOCHEMISTRY

Amyloid-Degrading Ability of Nattokinase fromBacillus subtilisNatto

(2008) Ruei-Lin Hsu et al.   JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

Steric Zipper of the Amyloid Fibrils Formed by Residues 109–122 of the Syrian Hamster Prion Protein

(2008) Shin-Wen Lee et al.   JOURNAL OF MOLECULAR BIOLOGY