Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein.
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Conformational diversity in prion protein variants influences intermolecular beta-sheet formationSolution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseasesThe contribution of polar group burial to protein stability is strongly context-dependentNMR Structure of the Human Prion Protein with the Pathological Q212P Mutation Reveals Unique Structural FeaturesRapid folding of the prion protein captured by pressure-jumpInsight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variantsElectron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion proteinIntroducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitroMicrocanonical thermostatistics of coarse-grained proteins with amyloidogenic propensity.Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Effect of hydrophobic mutations in the H2-H3 subdomain of prion protein on stability and conversion in vitro and in vivo.Sequence determinants of amyloid fibril formationHydrogen/deuterium exchange and aggregation of a polyvaline and a polyleucine alpha-helix investigated by matrix-assisted laser desorption ionization mass spectrometry.Water molecules as structural determinants among prions of low sequence identity.The role of disulfide bridge in the folding and stability of the recombinant human prion protein.High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility.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 pHPrion and water: tight and dynamical hydration sites have a key role in structural stability.Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.The role of dimerization in prion replicationExploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignmentsStability and Cu(II) binding of prion protein variants related to inherited human prion diseases.PrP overdrive: does inhibition of α-cleavage contribute to PrP(C) toxicity and prion disease?Autocatalytic self-propagation of misfolded prion proteinPathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.The prion hypothesis: from biological anomaly to basic regulatory mechanism.Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.The molecular pathology of CJD: old and new variants.Review: contribution of transgenic models to understanding human prion disease.Separating instability from aggregation propensity in γS-crystallin variants.Nucleic acid induced unfolding of recombinant prion protein globular fragment is pH dependent.Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions.Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.Global analysis of protein folding thermodynamics for disease state characterizationHuman prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycansRequirements for mutant and wild-type prion protein misfolding in vitro.The cellular prion protein (PrP(C)): its physiological function and role in disease
P2860
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P2860
Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Influence of amino acid substi ...... of the cellular prion protein.
@en
Influence of amino acid substi ...... of the cellular prion protein.
@nl
type
label
Influence of amino acid substi ...... of the cellular prion protein.
@en
Influence of amino acid substi ...... of the cellular prion protein.
@nl
prefLabel
Influence of amino acid substi ...... of the cellular prion protein.
@en
Influence of amino acid substi ...... of the cellular prion protein.
@nl
P356
P1433
P1476
Influence of amino acid substi ...... of the cellular prion protein.
@en
P2093
Glockshuber R
P304
P356
10.1021/BI982714G
P407
P577
1999-03-01T00:00:00Z