Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
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Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variantsRelationships between PrPSc stability and incubation time for United States scrapie isolates in a natural host systemFull-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.Mapping of possible prion protein self-interaction domains using peptide arraysIn vitro and in vivo neurotoxicity of prion protein oligomers.Nanopore analysis reveals differences in structural stability of ovine PrP(C) proteins corresponding to scrapie susceptible (VRQ) and resistance (ARR) genotypes.Guanidine-HCl dependent structural unfolding of M-crystallin: fluctuating native state like topologies and intermolecular association.Prion protein misfolding.Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate stateMicrosecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.PrP assemblies: spotting the responsible regions in prion propagation.Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.Interaction between Shadoo and PrP Affects the PrP-Folding PathwayIdentification of amino acid variation in the prion protein associated with classical scrapie in Canadian dairy goatsUnique Properties of the Rabbit Prion Protein OligomerHeme as an optical probe of a conformational transition of ovine recPrP.The peculiar nature of unfolding of the human prion protein.The reconstitution of mammalian prion infectivity de novo.Structural factors underlying the species barrier and susceptibility to infection in prion disease.Prions and manganese: A maddening beast.Prion protein oligomer and its neurotoxicity.Caprine PrP variants harboring Asp-146, His-154 and Gln-211 alleles display reduced convertibility upon interaction with pathogenic murine prion protein in scrapie infected cells.Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation.The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro.Ovine plasma prion protein levels show genotypic variation detected by C-terminal epitopes not exposed in cell-surface PrPCGlycan-controlled epitopes of prion protein include a major determinant of susceptibility to sheep scrapie.Insights into Mechanisms of Transmission and Pathogenesis from Transgenic Mouse Models of Prion Diseases.A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.Stability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant.Left handed beta helix models for mammalian prion fibrils.Copper induces increased beta-sheet content in the scrapie-susceptible ovine prion protein PrPVRQ compared with the resistant allelic variant PrPARR.Molecular and transmission characteristics of primary-passaged ovine scrapie isolates in conventional and ovine PrP transgenic mice.Proteinase K-sensitive disease-associated ovine prion protein revealed by conformation-dependent immunoassay.Polymorphisms at amino acid residues 141 and 154 influence conformational variation in ovine PrP.Acid-induced molten globule state of a prion protein: crucial role of Strand 1-Helix 1-Strand 2 segment.The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein.Blood clearance of the prion protein introduced by intravenous route in sheep is influenced by host genetic and physiopathologic factors.Joint Scientific Opinion on any possible epidemiological or molecular association between TSEs in animals and humansInhibition of Prion Propagation by 3,4-Dimethoxycinnamic Acid.Ovine PrP transgenic Drosophila show reduced locomotor activity and decreased survival.
P2860
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P2860
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
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
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
@en
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
@nl
type
label
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
@en
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
@nl
prefLabel
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
@en
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
@nl
P2093
P1476
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants.
@en
P2093
Eric Treguer
Frederic Eghiaian
Human Rezaei
Jeanne Grosclaude
Pascale Debey
Pascale Mentre
Thomas Haertle
Yvan Choiset
P304
P356
10.1016/S0022-2836(02)00856-2
P407
P577
2002-09-01T00:00:00Z