In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc).
about
Selective incorporation of polyanionic molecules into hamster prions.Recombinant prion protein induces a new transmissible prion disease in wild-type animals.Hot spots in prion protein for pathogenic conversionHighly efficient protein misfolding cyclic amplificationSynthetic prions with novel strain-specified propertiesGenesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion diseaseUV-light exposed prion protein fails to form amyloid fibrilsKosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded formA visual dual-aptamer logic gate for sensitive discrimination of prion diseases-associated isoform with reusable magnetic microparticles and fluorescence quantum dotsThe effect of β2-α2 loop mutation on amyloidogenic properties of the prion proteinShaking alone induces de novo conversion of recombinant prion proteins to β-sheet rich oligomers and fibrilsFormation of amyloid fibrils from β-amylaseTetracysteine-tagged prion protein allows discrimination between the native and converted formsRole of polysaccharide and lipid in lipopolysaccharide induced prion protein conversionPolyalanine-independent conformational conversion of nuclear poly(A)-binding protein 1 (PABPN1).Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Progress towards structural understanding of infectious sheep PrP-amyloid.NLRP3 inflammasome activation in macrophage cell lines by prion protein fibrils as the source of IL-1β and neuronal toxicity.Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process.Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversionEffect of hydrophobic mutations in the H2-H3 subdomain of prion protein on stability and conversion in vitro and in vivo.Conformational switching within individual amyloid fibrils.The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size.The dominant-negative effect of the Q218K variant of the prion protein does not require protein X.Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidylinositol anchor, partially impairs amyloid fibril formation.Probing structural differences in prion protein isoforms by tyrosine nitrationReversible monomer-oligomer transition in human prion protein.Cytotoxic aggregation and amyloid formation by the myostatin precursor proteinThe intriguing prion disorders.High-resolution structure of infectious prion protein: the final frontierLow density subcellular fractions enhance disease-specific prion protein misfolding.Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitroPyrroloquinoline quinone inhibits the fibrillation of amyloid proteins.Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity.Seeding specificity and ultrastructural characteristics of infectious recombinant prions.Direct evidence of generation and accumulation of β-sheet-rich prion protein in scrapie-infected neuroblastoma cells with human IgG1 antibody specific for β-form prion protein.N-terminal domain of prion protein directs its oligomeric association.Prion protein polymerisation triggered by manganese-generated prion protein seeds.
P2860
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P2860
In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc).
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
@zh-sg
2004年學術文章
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name
In vitro conversion of full-le ...... ith physical properties of PrP
@nl
In vitro conversion of full-le ...... hysical properties of PrP(Sc).
@en
type
label
In vitro conversion of full-le ...... ith physical properties of PrP
@nl
In vitro conversion of full-le ...... hysical properties of PrP(Sc).
@en
prefLabel
In vitro conversion of full-le ...... ith physical properties of PrP
@nl
In vitro conversion of full-le ...... hysical properties of PrP(Sc).
@en
P2093
P1476
In vitro conversion of full-le ...... hysical properties of PrP(Sc).
@en
P2093
Alexander S Parfenov
Ilia V Baskakov
Olga V Bocharova
Vadim V Salnikov
P304
P356
10.1016/J.JMB.2004.11.068
P407
P577
2004-12-19T00:00:00Z