Autocatalytic conversion of recombinant prion proteins displays a species barrier.
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Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" modelThermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in VivoPlasmodium falciparum merozoite surface protein 3: oligomerization, self-assembly, and heme complex formationThe dominant-negative effect of the Q218K variant of the prion protein does not require protein X.Prion diseases and their biochemical mechanisms.Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALSStrain-specified characteristics of mouse synthetic prions.Water-soluble hybrid nanoclusters with extra bright and photostable emissions: a new tool for biological imaging.Prion protein misfolding.Cell-free formation of misfolded prion protein with authentic prion infectivity.Prion species barrier between the closely related yeast proteins is detected despite coaggregation.A systematic investigation of production of synthetic prions from recombinant prion proteinSlow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.Synthetic prions.Prion detection by an amyloid seeding assay.The reconstitution of mammalian prion infectivity de novo.Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils.Prion-prion interactionsHeterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).Prion propagation in vitro: are we there yet?Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange.Influence of the N-terminal domain on the aggregation properties of the prion protein.Y145Stop is sufficient to induce de novo generation prions using protein misfolding cyclic amplification.Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease.Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation.The presence of valine at residue 129 in human prion protein accelerates amyloid formation.Role of N-terminal familial mutations in prion protein fibrillization and prion amyloid propagation in vitro.Discovery of small molecules binding to the normal conformation of prion by combining virtual screening and multiple biological activity evaluation methods.Confined Water in Amyloid-Competent Oligomers of the Prion Protein.In vitro conversion and seeded fibrillization of posttranslationally modified prion protein.
P2860
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P2860
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
@en
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
@nl
type
label
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
@en
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
@nl
prefLabel
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
@en
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
@nl
P2860
P356
P1476
Autocatalytic conversion of recombinant prion proteins displays a species barrier.
@en
P2093
Ilia V Baskakov
P2860
P304
P356
10.1074/JBC.M310594200
P407
P577
2003-12-10T00:00:00Z