Influence of the N-terminal domain on the aggregation properties of the prion protein.
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The crystal structure of an octapeptide repeat of the Prion protein in complex with a Fab fragment of the POM2 antibodyThe octarepeat region of the prion protein is conformationally altered in PrP(Sc)Prion protein self-peptides modulate prion interactions and conversion.Probing structural differences in prion protein isoforms by tyrosine nitrationMolecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLSCyclin-dependent kinase 5 phosphorylation of familial prion protein mutants exacerbates conversion into amyloid structure.Characterization of four new monoclonal antibodies against the distal N-terminal region of PrP(c).Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycansA multistage pathway for human prion protein aggregation in vitro: from multimeric seeds to β-oligomers and nonfibrillar structures.Role of prion protein aggregation in neurotoxicity.Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregationA polymer physics perspective on driving forces and mechanisms for protein aggregation"Click peptides"--chemical biology-oriented synthesis of Alzheimer's disease-related amyloid beta peptide (abeta) analogues based on the "O-acyl isopeptide method".Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assemblyDecrypting Prion Protein Conversion into a β-Rich Conformer by Molecular DynamicsPrions in the environment: occurrence, fate and mitigationSite-specific modification of Alzheimer's peptides by cholesterol oxidation products enhances aggregation energetics and neurotoxicityInfluence of gold-bipyridyl derivants on aggregation and disaggregation of the prion neuropeptide PrP106-126.Assessment of the PrPc Amino-Terminal Domain in Prion Species Barriers.Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependentThe kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration".Aggregation of prion protein with insertion mutations is proportional to the number of inserts.Investigation of the effect of glycosylation on human prion protein by molecular dynamics.Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.Confined Water in Amyloid-Competent Oligomers of the Prion Protein.The Effect of N-Terminal Domain Removal towards the Biochemical and Structural Features of a Thermotolerant Lipase from an Antarctic Pseudomonas sp. Strain AMS3.
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P2860
Influence of the N-terminal domain on the aggregation properties of the prion protein.
description
2005 nî lūn-bûn
@nan
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
2005年论文
@zh
2005年论文
@zh-cn
name
Influence of the N-terminal domain on the aggregation properties of the prion protein.
@en
type
label
Influence of the N-terminal domain on the aggregation properties of the prion protein.
@en
prefLabel
Influence of the N-terminal domain on the aggregation properties of the prion protein.
@en
P2860
P356
P1433
P1476
Influence of the N-terminal domain on the aggregation properties of the prion protein.
@en
P2093
Kristen N Frankenfield
P2860
P304
P356
10.1110/PS.051434005
P577
2005-08-01T00:00:00Z