Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form.
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NMR Structure of the Human Prion Protein with the Pathological Q212P Mutation Reveals Unique Structural FeaturesThermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in VivoThe effect of β2-α2 loop mutation on amyloidogenic properties of the prion proteinIntroducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitroNanopore analysis of wild-type and mutant prion protein (PrP(C)): single molecule discrimination and PrP(C) kinetics.Loss of anti-Bax function in Gerstmann-Sträussler-Scheinker syndrome-associated prion protein mutantsMolecular 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.Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycansThe role of the 132-160 region in prion protein conformational transitions.From conversion to aggregation: protofibril formation of the prion protein.Ligand binding promotes prion protein aggregation--role of the octapeptide repeatsHelix 3 is necessary and sufficient for prion protein's anti-Bax function.The consequences of pathogenic mutations to the human prion protein.Differential stability of the bovine prion protein upon urea unfoldingPathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.Interplay of buried histidine protonation and protein stability in prion misfolding.Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments.PRNP mutations in a series of apparently sporadic neurodegenerative dementias in China.The role of the amino acid residue at alpha1:189 in the binding of neuromuscular blocking agents to mouse and human muscle nicotinic acetylcholine receptors.Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviorsPrion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice.Aggregation of prion protein with insertion mutations is proportional to the number of inserts.Formation of critical oligomers is a key event during conformational transition of recombinant syrian hamster prion protein.Autocatalytic conversion of recombinant prion proteins displays a species barrier.The effect of disease-associated mutations on the folding pathway of human prion protein.Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.In silico analysis of prion protein mutants: a comparative study by molecular dynamics approach.Distinct effects of mutations on biophysical properties of human prion protein monomers and oligomers.
P2860
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P2860
Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Disease-associated F198S mutat ...... nversion to scrapie-like form.
@en
Disease-associated F198S mutat ...... nversion to scrapie-like form.
@nl
type
label
Disease-associated F198S mutat ...... nversion to scrapie-like form.
@en
Disease-associated F198S mutat ...... nversion to scrapie-like form.
@nl
prefLabel
Disease-associated F198S mutat ...... nversion to scrapie-like form.
@en
Disease-associated F198S mutat ...... nversion to scrapie-like form.
@nl
P2860
P356
P1476
Disease-associated F198S mutat ...... nversion to scrapie-like form.
@en
P2093
David L Vanik
Witold K Surewicz
P2860
P304
49065-49070
P356
10.1074/JBC.M207511200
P407
P577
2002-10-07T00:00:00Z