Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain.
about
Human prion protein sequence elements impede cross-species chronic wasting disease transmission.Prion protein self-peptides modulate prion interactions and conversion.Isolation and characterization of a polymerized prion protein.Mapping of possible prion protein self-interaction domains using peptide arraysPeptide ligand screening of alpha-synuclein aggregation modulators by in silico panningDynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Recent advances in prion chemotherapeutics.Progress in prion vaccines and immunotherapies.Cellular prion protein promotes Brucella infection into macrophagesNMR structure and CD titration with metal cations of human prion alpha2-helix-related peptides.From conversion to aggregation: protofibril formation of the prion protein.PrP antibody binding-induced epitope modulation evokes immunocooperativityCharacterization of cell-surface prion protein relative to its recombinant analogue: insights from molecular dynamics simulations of diglycosylated, membrane-bound human prion protein.PrP Knockout Cells Expressing Transmembrane PrP Resist Prion InfectionConversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes.The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation.Intercellular transfer of the cellular prion protein.An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrP(Sc) aggregatesStability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant.Conformational change, aggregation and fibril formation induced by detergent treatments of cellular prion protein.Effect of glycosylphosphatidylinositol anchor-dependent and -independent prion protein association with model raft membranes on conversion to the protease-resistant isoform.Amidation and structure relaxation abolish the neurotoxicity of the prion peptide PrP106-126 in vivo and in vitro.Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jacob's disease-affected and normal brain tissue.Polyclonal anti-PrP auto-antibodies induced with dimeric PrP interfere efficiently with PrPSc propagation in prion-infected cells.
P2860
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P2860
Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Inhibition of interactions and ...... the C-terminal folded domain.
@en
Inhibition of interactions and ...... the C-terminal folded domain.
@nl
type
label
Inhibition of interactions and ...... the C-terminal folded domain.
@en
Inhibition of interactions and ...... the C-terminal folded domain.
@nl
prefLabel
Inhibition of interactions and ...... the C-terminal folded domain.
@en
Inhibition of interactions and ...... the C-terminal folded domain.
@nl
P2093
P2860
P356
P1476
Inhibition of interactions and ...... the C-terminal folded domain.
@en
P2093
P2860
P304
15489-15497
P356
10.1074/JBC.M100288200
P407
P577
2001-02-01T00:00:00Z