Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
HT does not modify the natively unfolded structure of Syn, rather, it stabilizes specific regions of the molecule leading to inhibition of protein fibrillation.
|
31756328 |
2020 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
An aminoglycoside antibiotic inhibits both lipid-induced and solution-phase fibrillation of α-synuclein in vitro.
|
31453599 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Aggregates of fibrillated α-Syn are the major component of Lewy bodies (LB), a pathologic hallmark of idiopathic Parkinson's disease (PD).
|
30954607 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Contribution of syndecans to cellular uptake and fibrillation of α-synuclein and tau.
|
31719623 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
We infer that inhibition of α-Syn fibrillation/aggregation is primarily driven by hydrophobic interactions between Safranal and the protein.
|
31505208 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
A hallmark of Parkinson's disease is the presence of Lewy bodies consisting of lipids and proteins, mainly fibrillated α-synuclein (aSN). aSN is an intrinsically disordered protein exerting its physiological role in an ensemble of states, one of which coexists in large assemblies with lipids, recently termed co-structures.
|
31747254 |
2019 |
Fibrillation
|
0.100 |
AlteredExpression
|
disease |
BEFREE |
Furthermore, we demonstrated that in the α-Syn transduced-PC12 cells, EGCG can inhibit the overexpression and fibrillation of α-Syn in the cells, and reduce Cu(II)-induced reactive oxygen species (ROS), protecting the cells against Cu(II)-mediated toxicity.
|
31416122 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Oleuropein derivatives from olive fruit extracts reduce α-synuclein fibrillation and oligomer toxicity.
|
30655291 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
The kinetics of α-Syn fibrillation establishes that Cr-SPs are very effective in inhibiting fibrillation of α-Syn mutants.
|
31385584 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Although it is known to co-exist with the fibrillar deposits of α-Synuclein (Lewy bodies), a hallmark in Parkinson's disease (PD), the effect of potential therapeutic modulators on the fibrillation pathway of γ-Syn remains unexplored.
|
30394624 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
The different concentrations of these nanoparticles and special coating of each particle had an effect on the kinetics of β-amyloid and α-synuclein fibrillations.
|
30774334 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
ARSA inhibited the in vitro fibrillation of α-synuclein in a dose-dependent manner.
|
31312839 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Erratum: Effect of superparamagnetic nanoparticles coated with various electric charges on α-synuclein and β-amyloid proteins fibrillation process [Corrigendum].
|
31507317 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
SCGN physically binds α-synuclein and rescues it from detrimental fibrillation.
|
31617346 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Transmission electron microscopy analysis of the aggregates produced by the native alpha-synuclein under fibrillation conditions revealed the presence of 355-441-nm fibrils.
|
30639428 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Nile red and intrinsic fluorescence spectroscopy, CD, Congo red adsorption, and TEM studies indicated that ZVFe NP increased the propensity of α-synuclein into the amyloid fibrillation.
|
31417259 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
This attenuation of α-synuclein fibrillation was not seen for the reduced form of FapC ΔR1R2R3.
|
31459612 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Ginsenoside Rb1 has been shown to protect dopaminergic neurons (DA) from death and inhibit α-synuclein fibrillation and toxicity <i>in vitro</i>.
|
30958793 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
The presence of partially structured helices in natively unfolded amyloid-β42 (Aβ42) and α-synuclein (αS) has been shown to accelerate fibrillation in the onset of Alzheimer's and Parkinson's disease, respectively.
|
30917651 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
With N-isobutyryl-l-cysteine (L-NIBC) protected AuNCs as an example, we show that AuNCs effectively prevent α-Synuclein (α-Syn) fibrillation in in vitro experiments.
|
30576972 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
The fibrillation of αS in vitro is described by a nucleation-elongation process involving the formation of a critical nucleus.
|
31799519 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
α-Synuclein (α-Syn) is a small natively unfolded protein that its fibrillation is the causative factor of Parkinson's disease.
|
31185031 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Binding of Noradrenaline to Native and Intermediate States during the Fibrillation of α-Synuclein Leads to the Formation of Stable and Structured Cytotoxic Species.
|
30917654 |
2019 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
Here, we show that monomeric RL enhances the ability of αSN to permeabilize membranes, while micellar RL rapidly induces protein β-sheet structure with a worm-like fibrillary appearance, which cannot seed RL-free fibrillation but transforms into linear fibrils faster than αSN fibrillating on its own.
|
29572816 |
2018 |
Fibrillation
|
0.100 |
Biomarker
|
disease |
BEFREE |
We also emphasize the recent investigations on residual secondary structure formation in dynamic conformational ensembles of amyloid-β and α-synuclein, such as β-structure linked to the oligomerization and fibrillation mechanisms related to the pathologies of Alzheimer's and Parkinson's diseases.
|
29364151 |
2018 |