Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform
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Progress on low susceptibility mechanisms of transmissible spongiform encephalopathiesTreatment of Prion Disease with Heterologous Prion ProteinsTransgenic Rabbits Expressing Ovine PrP Are Susceptible to ScrapieTransgenic Mouse Bioassay: Evidence That Rabbits Are Susceptible to a Variety of Prion IsolatesUnique Structural Characteristics of the Rabbit Prion ProteinSolution Structure and Dynamics of the I214V Mutant of the Rabbit Prion ProteinPrion disease susceptibility is affected by -structure folding propensity and local side-chain interactions in PrPAtomic Structures Suggest Determinants of Transmission Barriers in Mammalian Prion DiseaseN-Terminal Helix-Cap in α-Helix 2 Modulates β-State Misfolding in Rabbit and Hamster Prion ProteinsIntroducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitroTetracysteine-tagged prion protein allows discrimination between the native and converted formsPulling rabbits to reveal the secrets of the prion proteinEffect of hydrophobic mutations in the H2-H3 subdomain of prion protein on stability and conversion in vitro and in vivo.Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and volesA proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.A molecular switch controls interspecies prion disease transmission in mice.Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171.The contrasting effect of macromolecular crowding on amyloid fibril formation.Sequence-dependent prion protein misfolding and neurotoxicity.Prion protein misfolding.Prion strain-dependent differences in conversion of mutant prion proteins in cell culture.Strain fidelity of chronic wasting disease upon murine adaptation.Fibril formation of the rabbit/human/bovine prion proteinsHow does domain replacement affect fibril formation of the rabbit/human prion proteinsDid the prion protein become vulnerable to misfolding after an evolutionary divide and conquer event?Structure of the β2-α2 loop and interspecies prion transmissionPolymorphisms and variants in the prion protein sequence of European moose (Alces alces), reindeer (Rangifer tarandus), roe deer (Capreolus capreolus) and fallow deer (Dama dama) in Scandinavia.Unique Properties of the Rabbit Prion Protein OligomerNaturally prion resistant mammals: a utopia?The [URE3] prion in Candida.Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysisPrion protein misfolding and disease.The role of crowded physiological environments in prion and prion-like protein aggregationStructural factors underlying the species barrier and susceptibility to infection in prion disease.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.Scrapie infection of prion protein-deficient cell line upon ectopic expression of mutant prion proteins.Potential approaches for heterologous prion protein treatment of prion diseases.Cellular factors implicated in prion replication.In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.
P2860
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P2860
Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform
description
2003 nî lūn-bûn
@nan
2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Multiple amino acid residues w ...... mation of its abnormal isoform
@ast
Multiple amino acid residues w ...... mation of its abnormal isoform
@en
Multiple amino acid residues w ...... mation of its abnormal isoform
@nl
type
label
Multiple amino acid residues w ...... mation of its abnormal isoform
@ast
Multiple amino acid residues w ...... mation of its abnormal isoform
@en
Multiple amino acid residues w ...... mation of its abnormal isoform
@nl
prefLabel
Multiple amino acid residues w ...... mation of its abnormal isoform
@ast
Multiple amino acid residues w ...... mation of its abnormal isoform
@en
Multiple amino acid residues w ...... mation of its abnormal isoform
@nl
P2093
P2860
P1433
P1476
Multiple amino acid residues w ...... mation of its abnormal isoform
@en
P2093
Eberhard Pfaff
Ina Vorberg
Suzette A Priola
P2860
P304
P356
10.1128/JVI.77.3.2003-2009.2003
P407
P577
2003-02-01T00:00:00Z