Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments.
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Selective incorporation of polyanionic molecules into hamster prions.Rapid folding of the prion protein captured by pressure-jumpThe 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 vitroFolding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods.Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.Prion protein self-peptides modulate prion interactions and conversion.Prion diseases and their biochemical mechanisms.Direct observation of multiple misfolding pathways in a single prion protein moleculePathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.Influence of pH on the human prion protein: insights into the early steps of misfolding.Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.Microsecond folding dynamics of apomyoglobin at acidic pHProtease-sensitive prions with 144-bp insertion mutationsFolding kinetics of the human prion protein probed by temperature jump.Comparing the energy landscapes for native folding and aggregation of PrP.The consequences of pathogenic mutations to the human prion protein.Advances in turbulent mixing techniques to study microsecond protein folding reactions.Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region.Allosteric function and dysfunction of the prion protein.A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.Synthesis of double-fluorescent labeled prion protein for FRET analysis.Conformational pH dependence of intermediate states during oligomerization of the human prion protein.Prion protein dynamics before aggregation.Structural and hydration properties of the partially unfolded states of the prion protein.The elusive intermediate on the folding pathway of the prion protein.
P2860
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P2860
Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Early intermediate in human pr ...... ultrarapid mixing experiments.
@en
type
label
Early intermediate in human pr ...... ultrarapid mixing experiments.
@en
prefLabel
Early intermediate in human pr ...... ultrarapid mixing experiments.
@en
P2093
P2860
P356
P1476
Early intermediate in human pr ...... ultrarapid mixing experiments
@en
P2093
Adrian C Apetri
Kosuke Maki
Witold K Surewicz
P2860
P304
11673-11678
P356
10.1021/JA063880B
P407
P577
2006-09-01T00:00:00Z