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Predicting slow structural transitions in macromolecular systems: Conformational floodingThe novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP sheddingIntracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion diseasePropagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factorPrionsHot spots in prion protein for pathogenic conversionSolution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseasesSolution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoformRapid folding of the prion protein captured by pressure-jumpChanging a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers.Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugsPreclinical deposition of pathological prion protein in muscle of experimentally infected primatesIn situ photodegradation of incorporated polyanion does not alter prion infectivityIntroducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitroCritical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion proteinPrPC directly interacts with proteins involved in signaling pathwaysPrion fragment peptides are digested with membrane type matrix metalloproteinases and acquire enzyme resistance through Cu²⁺-bindingVariety of antiprion compounds discovered through an in silico screen based on cellular-form prion protein structure: Correlation between antiprion activity and binding affinity.Potent inhibition of scrapie prion replication in cultured cells by bis-acridines.Paracrine diffusion of PrP(C) and propagation of prion infectivity by plasma membrane-derived microvesiclesCellular biology of prion diseases.PrPSc accumulation in neuronal plasma membranes links Notch-1 activation to dendritic degeneration in prion diseases.Notch-1 activation and dendritic atrophy in prion disease.Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitroRedox control of prion and disease pathogenesis.Gramicidin D conformation, dynamics and membrane ion transport.The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3.Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice.Prion protein genes and prion diseases: studies in transgenic mice.N-glycans and glycosylphosphatidylinositol-anchor act on polarized sorting of mouse PrP(C) in Madin-Darby canine kidney cells.Heterodimer formation and crystal nucleation of gramicidin D.Exploring 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.Molecular dynamics simulation of dimeric and monomeric forms of human prion protein: insight into dynamics and propertiesBalanced branching in transcription termination.Direct observation of multiple misfolding pathways in a single prion protein moleculeCharacterizing antiprion compounds based on their binding properties to prion proteins: implications as medical chaperones.Prions.Selective re-routing of prion protein to proteasomes and alteration of its vesicular secretion prevent PrP(Sc) formation.
P2860
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P2860
description
1994 nî lūn-bûn
@nan
1994 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Structural clues to prion replication.
@ast
Structural clues to prion replication.
@en
Structural clues to prion replication.
@nl
type
label
Structural clues to prion replication.
@ast
Structural clues to prion replication.
@en
Structural clues to prion replication.
@nl
prefLabel
Structural clues to prion replication.
@ast
Structural clues to prion replication.
@en
Structural clues to prion replication.
@nl
P2093
P356
P1433
P1476
Structural clues to prion replication.
@en
P2093
P304
P356
10.1126/SCIENCE.7909169
P407
P577
1994-04-01T00:00:00Z