Results 71 to 80 of about 928,578 (204)
α-Synuclein interacts directly but reversibly with psychosine: implications for α-synucleinopathies
Aggregation of α-synuclein, the hallmark of α-synucleinopathies such as Parkinson’s disease, occurs in various glycosphingolipidoses. Although α-synuclein aggregation correlates with deficiencies in the lysosomal degradation of glycosphingolipids (GSL ...
Hazem Abdelkarim +15 more
doaj +1 more source
Ample evidence suggests that α-synuclein is released from cells and propagated from one area of the brain to others via cell-to-cell transmission. In terms of their prion-like behavior, α-synuclein propagation plays key roles in the pathogenesis and ...
Se Hee Oh +7 more
doaj +1 more source
Striatal dopamine transmission is subtly modified in human A53Tα-synuclein overexpressing mice [PDF]
Mutations in, or elevated dosage of, SNCA, the gene for α-synuclein (α-syn), cause familial Parkinson's disease (PD). Mouse lines overexpressing the mutant human A53Tα-syn may represent a model of early PD.
Auburger, G +15 more
core +1 more source
Molecular editing of bilobalide uncovers BB56, a PREP‐engaging chemotype with enhanced anti‐inflammatory activity in microglia. Integrated CETSA‐MS, SAR, and pathway analyses link BB56 to attenuation of p38 MAPK/NF‐κB and NLRP3‐associated inflammatory signaling, highlighting bilobalide editing as a strategy for developing neuroinflammation‐modulating ...
Chanin Sillapachaiyaporn +20 more
wiley +1 more source
Neuroprotective function of Omi to α-synuclein-induced neurotoxicity
Astract: The main pathological hallmark of Parkinson's disease (PD) is the presence of Lewy bodies, which mainly consist of aggregated α-synuclein. Based on the neurotoxicity of oligomeric α-synuclein and its significance in the aetiology of PD, there ...
Hea-Jong Chung +3 more
doaj +1 more source
LRRK2‐mutant induced pluripotent stem cells (iPSCs) were derived from a patient with Parkinson's disease (PD). Using CRISPR/Cas9–mediated gene editing, the pathogenic LRRK2 mutations were precisely corrected, and isogenic dopaminergic neural progenitor cells (DA‐NPCs) were subsequently generated.
Qing Yan +29 more
wiley +1 more source
DDX39A unwinds viral RNA G-quadruplexes to limit α-Synuclein amyloidogenesis
Summary: Amyloid aggregates of α-Synuclein are hallmarks of Parkinson’s disease (PD) and related neurodegenerative disorders. Literature suggests that mRNA G-quadruplexes (rG4s) bind to α-Synuclein, facilitating its amyloidogenesis.
Aanchal Jain +9 more
doaj +1 more source
Structural Polymorphism of polyG Inclusions Revealed by In Situ Cryo‐Electron Tomography
Correlative cryo‐electron tomography in primary cortical neurons and NIID mouse brain tissue reveals that polyG inclusions are interconnected ribbon‐like assemblies rather than canonical amyloid fibrils. Multiple compartment‐specific ribbon states show distinct 26S proteasome accessibility, while cytoplasmic ribbons contact and deform ER‐like ...
Yunwen Qian +12 more
wiley +1 more source
Plasma and Serum Alpha-Synuclein as a Biomarker of Diagnosis in Patients With Parkinson's Disease
Background: Parkinson's disease (PD) is the second most common neurodegenerative disease, and α-synuclein plays a critical role in the pathogenesis of PD.
Chun-Wei Chang +5 more
doaj +1 more source
α-Synuclein binding activity of the plant growth promoter asterubine
Preventing the aggregation of certain amyloid proteins has the potential to slow down the progression of diseases like Alzheimer’s, Parkinson’s, and type 2 diabetes mellitus. During a high-throughput screen of 300 Australian marine invertebrate extracts,
Prebble, Dale W +7 more
core +1 more source

