The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
about
Potential roles for prions and protein-only inheritance in cancerα-Cleavage of cellular prion proteinStructure of the Flexible Amino-Terminal Domain of Prion Protein Bound to a Sulfated GlycanRapid folding of the prion protein captured by pressure-jumpSimulations of proteins with inhomogeneous degrees of freedom: The effect of thermostatsFull-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.Revealing different aggregation pathways of amyloidogenic proteins by ultrasound velocimetry.Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.The effect of Aβ on IAPP aggregation in the presence of an isolated β-cell membrane.Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.PrP charge structure encodes interdomain interactionsMutant p53 aggregates into prion-like amyloid oligomers and fibrils: implications for cancer.PrP antibody binding-induced epitope modulation evokes immunocooperativityThe peculiar interaction between mammalian prion protein and RNAThermodynamic characterization of the unfolding of the prion protein.Understanding and identifying amino acid repeats.Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids.Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cellsAggregation and amyloid fibril formation induced by chemical dimerization of recombinant prion protein in physiological-like conditions.Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.Effects of metal binding on solubility and resistance of physiological prions depend on tissues and glycotypes.Aggregation of prion protein with insertion mutations is proportional to the number of inserts.A potential mechanism for Cu2+ reduction, beta-cleavage, and beta-sheet initiation within the N-terminal domain of the prion protein: insights from density functional theory and molecular dynamics calculations.A self-assembled nanotube for the direct aldol reaction in water.
P2860
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P2860
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
@ast
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
@en
type
label
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
@ast
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
@en
prefLabel
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
@ast
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
@en
P2093
P2860
P50
P1433
P1476
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
@en
P2093
Julia Kraineva
Luís M T R Lima
Mariana P B Gomes
P2860
P304
P356
10.1529/BIOPHYSJ.105.067603
P407
P577
2005-07-22T00:00:00Z