Conformational diversity in prion protein variants influences intermolecular beta-sheet formation - Test2 - elhamkhani - TriplyDB

Conformational diversity in prion protein variants influences intermolecular beta-sheet formation

Conformational diversity in prion protein variants influences intermolecular beta-sheet formation

http://www.wikidata.org/entity/Q24318672

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Synthetic prions with novel strain-specified properties NMR Structure of the Human Prion Protein with the Pathological Q212P Mutation Reveals Unique Structural Features Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion Disease Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicity Structural and dynamic properties of the human prion protein.Diverse effects on the native β-sheet of the human prion protein due to disease-associated mutations.Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles Influence of pH on the human prion protein: insights into the early steps of misfolding.Molecular biology and pathology of prion strains in sporadic human prion diseases.Effect of glycans and the glycophosphatidylinositol anchor on strain dependent conformations of scrapie prion protein: improved purifications and infrared spectra.Transgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease.Requirements for mutant and wild-type prion protein misfolding in vitro.Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interface Protective V127 prion variant prevents prion disease by interrupting the formation of dimer and fibril from molecular dynamics simulations.Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules Polymorphism at 129 dictates metastable conformations of the human prion protein N-terminal β-sheet.Biochemical and strain properties of CJD prions: complexity versus simplicity.Allosteric function and dysfunction of the prion protein.Early structural features in mammalian prion conformation conversion.The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein.Fatal Familial Insomnia: Clinical Aspects and Molecular Alterations.Changing the solvent accessibility of the prion protein disulfide bond markedly influences its trafficking and effect on cell function.Molecular dynamics studies on the buffalo prion protein.Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors Normal modes of prion proteins: from native to infectious particle Epitope scanning indicates structural differences in brain-derived monomeric and aggregated mutant prion proteins related to genetic prion diseases.Distinct effects of mutations on biophysical properties of human prion protein monomers and oligomers.Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3.The Evolutionary unZIPping of a Dimerization Motif—A Comparison of ZIP and PrP Architectures.Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease

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Conformational diversity in prion protein variants influences intermolecular beta-sheet formation

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2010 nî lūn-bûn

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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

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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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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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Conformational diversity in pr ...... molecular beta-sheet formation

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The EMBO Journal

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Conformational diversity in pr ...... molecular beta-sheet formation

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Karen J Knaus

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Krystyna Surewicz

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Lizamma Antony

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Seungjoo Lee

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P2860

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

PROCHECK: a program to check the stereochemical quality of protein structures

NMR solution structure of the human prion protein

NMR structure of the bovine prion protein

NMR structures of three single-residue variants of the human prion protein

Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases

Crystal structure of the human prion protein reveals a mechanism for oligomerization

Crystal structure of human prion protein bound to a therapeutic antibody

Maximum-likelihood density modification

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1

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29

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38114635

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19927125

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identical protein binding

Major prion protein

Prion protein family

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2808380

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