Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.
about
Prion diseases: immunotargets and therapyMolecular mechanisms of disease-causing missense mutationsNanopore analysis of wild-type and mutant prion protein (PrP(C)): single molecule discrimination and PrP(C) kinetics.Effect of hydrophobic mutations in the H2-H3 subdomain of prion protein on stability and conversion in vitro and in vivo.Detection of prion seeding activity in the olfactory mucosa of patients with Fatal Familial InsomniaHeparin binding confers prion stability and impairs its aggregation.Structural and dynamic properties of the human prion protein.Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pHDynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Diverse effects on the native β-sheet of the human prion protein due to disease-associated mutations.Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes.The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensemblesEffects of the Pathogenic Mutation A117V and the Protective Mutation H111S on the Folding and Aggregation of PrP106-126: Insights from Replica Exchange Molecular Dynamics Simulations.Integrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survivalDisruption of the X-loop turn of the prion protein linked to scrapie resistance.Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular DynamicsPolar substitutions in helix 3 of the prion protein produce transmembrane isoforms that disturb vesicle trafficking.Systematic investigation of predicted effect of nonsynonymous SNPs in human prion protein gene: a molecular modeling and molecular dynamics study.Binding of bovine T194A PrP(C) by PrP(Sc)-specific antibodies: potential implications for immunotherapy of familial prion diseases.Safety, specificity and immunogenicity of a PrP(Sc)-specific prion vaccine based on the YYR disease specific epitope.Interplay of buried histidine protonation and protein stability in prion misfolding.Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms.Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Global human frequencies of predicted nuclear pathogenic variants and the role played by protein hydrophobicity in pathogenicity potential.Molecular Dynamics Simulations of the Temperature Induced Unfolding of Crambin Follow the Arrhenius Equation.Dominant-negative effects in prion diseases: insights from molecular dynamics simulations on mouse prion protein chimeras.Exploring the essential collective dynamics of interacting proteins: application to prion protein dimers.Molecular dynamics simulations and novel drug discovery.Perturbations in inter-domain associations may trigger the onset of pathogenic transformations in PrP(C): insights from atomistic simulations.Diversity in structural consequences of MexZ mutations in Pseudomonas aeruginosa.The mechanical response of hIAPP nanowires based on different bending direction simulations.Characterization of mutations in (prion) gene and their possible roles in neurodegenerative diseases
P2860
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P2860
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Pathogenic mutations in the hy ...... al instability and misfolding.
@ast
Pathogenic mutations in the hy ...... al instability and misfolding.
@en
Pathogenic mutations in the hy ...... al instability and misfolding.
@nl
type
label
Pathogenic mutations in the hy ...... al instability and misfolding.
@ast
Pathogenic mutations in the hy ...... al instability and misfolding.
@en
Pathogenic mutations in the hy ...... al instability and misfolding.
@nl
prefLabel
Pathogenic mutations in the hy ...... al instability and misfolding.
@ast
Pathogenic mutations in the hy ...... al instability and misfolding.
@en
Pathogenic mutations in the hy ...... al instability and misfolding.
@nl
P2860
P1476
Pathogenic mutations in the hy ...... al instability and misfolding.
@en
P2860
P304
P356
10.1016/J.JMB.2010.09.060
P407
P577
2010-10-07T00:00:00Z