Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion Disease
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Atomic Structures Suggest Determinants of Transmission Barriers in Mammalian Prion DiseaseTowards a Pharmacophore for AmyloidMolecular basis for amyloid- polymorphismCrystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer FormationMeasurement of amyloid formation by turbidity assay-seeing through the cloudAn Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicityHuman prion protein sequence elements impede cross-species chronic wasting disease transmission.A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.Molecular biology and pathology of prion strains in sporadic human prion diseases.Structural insights into functional and pathological amyloid.De novo design and experimental characterization of ultrashort self-associating peptidesThe Distribution of Prion Protein Allotypes Differs Between Sporadic and Iatrogenic Creutzfeldt-Jakob Disease PatientsThe yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17Aggregation of amyloids in a cellular context: modelling and experiment.The amyloid state of proteins in human diseases.The activities of amyloids from a structural perspective.Toward the Atomic Structure of PrPSc.N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent PathwaysMolecular dynamics simulation of temperature induced unfolding of animal prion protein.Towards the design of anti-amyloid short peptide helices.Are Amyloid Fibrils RNA-Traps? A Molecular Dynamics Perspective.Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease
P2860
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P2860
Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion Disease
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2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年论文
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name
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@ast
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@en
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@nl
type
label
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@ast
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@en
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@nl
prefLabel
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@ast
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@en
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
@nl
P2860
P3181
P356
P1476
Crystallographic Studies of Pr ...... ibility to Human Prion Disease
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P2093
Marcin I Apostol
Michael R Sawaya
P2860
P304
P3181
P356
10.1074/JBC.C110.158303
P407
P577
2010-09-24T00:00:00Z