SNCA, synuclein alpha, 6622

N. diseases: 449; N. variants: 66
Source: ALL
Disease Score gda Association Type Type Original DB Sentence supporting the association PMID PMID Year
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
Fibrillation
0.100 Biomarker disease BEFREE An aminoglycoside antibiotic inhibits both lipid-induced and solution-phase fibrillation of α-synuclein in vitro. 31453599 2019
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
Fibrillation
0.100 Biomarker disease BEFREE Contribution of syndecans to cellular uptake and fibrillation of α-synuclein and tau. 31719623 2019
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
Fibrillation
0.100 Biomarker disease BEFREE Oleuropein derivatives from olive fruit extracts reduce α-synuclein fibrillation and oligomer toxicity. 30655291 2019
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
Fibrillation
0.100 Biomarker disease BEFREE ARSA inhibited the in vitro fibrillation of α-synuclein in a dose-dependent manner. 31312839 2019
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
Fibrillation
0.100 Biomarker disease BEFREE SCGN physically binds α-synuclein and rescues it from detrimental fibrillation. 31617346 2019
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
Fibrillation
0.100 Biomarker disease BEFREE This attenuation of α-synuclein fibrillation was not seen for the reduced form of FapC ΔR1R2R3. 31459612 2019
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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
CUI: C0232197
Disease: Fibrillation
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