Conformational pH dependence of intermediate states during oligomerization of the human prion protein.
about
Prion disease susceptibility is affected by -structure folding propensity and local side-chain interactions in PrPMolecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pHN-terminal domain of prion protein directs its oligomeric association.Two misfolding routes for the prion protein around pH 4.5.Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathwayPartially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.Disruption of the X-loop turn of the prion protein linked to scrapie resistance.Opening Pandora's jar: a primer on the putative roles of CRMP2 in a panoply of neurodegenerative, sensory and motor neuron, and central disorders.Single-molecule approaches to prion protein misfoldingConformational properties of beta-PrP.Monitoring prion protein stability by NMR.Distinct effects of mutations on biophysical properties of human prion protein monomers and oligomers.Effect of the electrostatic surface potential on the oligomerization of full-length human recombinant prion protein at single-molecule level.
P2860
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P2860
Conformational pH dependence of intermediate states during oligomerization of the human prion protein.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Conformational pH dependence o ...... on of the human prion protein.
@en
type
label
Conformational pH dependence o ...... on of the human prion protein.
@en
prefLabel
Conformational pH dependence o ...... on of the human prion protein.
@en
P2860
P356
P1433
P1476
Conformational pH dependence o ...... ion of the human prion protein
@en
P2093
Abdessamad Tahiri-Alaoui
Remo Gerber
P2860
P304
P356
10.1110/PS.073163308
P577
2008-01-24T00:00:00Z