Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Cellular Prion Protein as a Receptor of Toxic Amyloid-β42 Oligomers Is Important for Alzheimer's Disease.
|
31417361 |
2019 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Ultrasensitive Detection of Amyloid-β Using Cellular Prion Protein on the Highly Conductive Au Nanoparticles-Poly(3,4-ethylene dioxythiophene)-Poly(thiophene-3-acetic acid) Composite Electrode.
|
31373200 |
2019 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Here, we have shown that NCAM1 peptide constructs carrying polycationic sequences derived from Aβ peptide (KKLVFF) and PrP protein (KKRPKP) significantly promote the S100A9 amyloid self-assembly in a concentration-dependent manner by making transient interactions with individual S100A9 molecules, perturbing its native structure and acting as catalysts.
|
31194501 |
2019 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Structural Mechanism of Barriers to Interspecies Seeding Transmissibility of Full-Length Prion Protein Amyloid.
|
31161647 |
2019 |
Amyloidosis
|
0.100 |
GeneticVariation
|
disease |
BEFREE |
Specific amyloid-β42 deposition in the brain of a Gerstmann-Sträussler-Scheinker disease patient with a P105L mutation on the prion protein gene.
|
30394185 |
2018 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Using paraffin-embedded sections, we applied histology and single- and multiple-labeling immunohistochemistry for PrP, p-tau, and Aβ to the three cases.
|
30240140 |
2018 |
Amyloidosis
|
0.100 |
GeneticVariation
|
disease |
BEFREE |
It is not understood why specific mutations in the prion protein gene (PRNP) cause cerebral amyloidosis and others cause CJD.
|
29887140 |
2018 |
Amyloidosis
|
0.100 |
GeneticVariation
|
disease |
BEFREE |
An in situ labeling using biotinylated Tat 48-57 peptide was employed in the brain tissue with amyloid deposits made up of Aβ (patients with AD and transgenic AD mice), of prion protein (patients with Gerstmann-Straussler-Scheinker disease), and other amyloidosis, processed by different fixations and pretreatments of histological sections.
|
29349578 |
2018 |
Amyloidosis
|
0.100 |
GeneticVariation
|
disease |
BEFREE |
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
|
28963458 |
2017 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Targeting glutamatergic and cellular prion protein mechanisms of amyloid β-mediated persistent synaptic plasticity disruption: Longitudinal studies.
|
28390893 |
2017 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro.
|
28373719 |
2017 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Prion-Protein-interacting Amyloid-β Oligomers of High Molecular Weight Are Tightly Correlated with Memory Impairment in Multiple Alzheimer Mouse Models.
|
26018073 |
2015 |
Amyloidosis
|
0.100 |
GeneticVariation
|
disease |
BEFREE |
This heterologous association induced aggregation of monomeric PrP and modified the structural properties of PrP amyloid fibrils.
|
25853328 |
2015 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Soluble Amyloid-β oligomers (Aβo) can trigger Alzheimer disease (AD) pathophysiology by binding to cell surface cellular prion protein (PrP(C)).
|
25148681 |
2014 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
For synthetic amyloid-β42, small oligomeric species showed prominent binding to PrP(C), whereas in Alzheimer's disease brains larger protein assemblies containing amyloid-β42 bound efficiently to PrP(C).
|
24519981 |
2014 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Structural and mechanistic commonalities of amyloid-β and the prion protein.
|
21862871 |
2013 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Because prion protein PrP-(23-98) was recently found to polymerize into amyloid-like and proteinase K-resistant spherical aggregates in the presence of NADPH plus copper ions, we tested to determine whether calreticulin (CRT) inhibits PrP-(23-98) aggregation in vitro.
|
21821925 |
2011 |
Amyloidosis
|
0.100 |
GeneticVariation
|
disease |
BEFREE |
In this report, we describe the clinical, histopathological and pathological prion protein (PrP(Sc)) characteristics of two Dutch patients carrying novel adjacent stop codon mutations in the C-terminal part of PRNP, resulting in either case in hereditary prion protein amyloidoses, but with strikingly different clinicopathological phenotypes.
|
19911184 |
2010 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Aggregation and amyloid fibril formation induced by chemical dimerization of recombinant prion protein in physiological-like conditions.
|
19710507 |
2009 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Amyloid-beta oligomers bind with nanomolar affinity to PrP(C), but the interaction does not require the infectious PrP(Sc) conformation.
|
19242475 |
2009 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Association between deposition of beta-amyloid and pathological prion protein in sporadic Creutzfeldt-Jakob disease.
|
18349519 |
2008 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
FDDNP binds to PrP-amyloid in postmortem human specimens, but has not been reported in vivo in prion disease.
|
17636066 |
2007 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Hereditary prion protein amyloidoses.
|
12733425 |
2003 |
Amyloidosis
|
0.100 |
GeneticVariation
|
disease |
BEFREE |
Gerstmann-Sträussler-Scheinker disease (GSS) is a cerebral amyloidosis associated with mutations in the prion protein (PrP) gene (PRNP).
|
11087738 |
2001 |
Amyloidosis
|
0.100 |
Biomarker
|
disease |
BEFREE |
Immunohistochemical studies showed that in addition to amyloid, these patients accumulate PrP deposits which are neither fluorescent nor birefringent when stained with thioflavin S and Congo red.
|
8939199 |
1996 |