Results 131 to 140 of about 83,002 (289)
Lack of pathogenic potential of peripheral α-synuclein aggregates from Parkinson’s disease patients
In Parkinson’s disease (PD) there is widespread accumulation in the brain of abnormal α-synuclein aggregates forming intraneuronal Lewy bodies (LB). It is now well established that LB-type α-synuclein aggregates also occur in the peripheral autonomic ...
Ariadna Recasens +6 more
doaj +1 more source
Active-Site-Directed Inhibitors of Prolyl Oligopeptidase Abolish Its Conformational Dynamics [PDF]
Deciphering conformational dynamics is crucial for understanding the biological functions of proteins and for designing compounds targeting them. In particular, providing an accurate description of microsecond–millisecond motions opens the opportunity ...
Bernadó +34 more
core +3 more sources
The Emerging Parkinson's Disease Oxylipin‐Ome
ABSTRACT Parkinson Disease (PD) is increasingly considered a proteinopathy and lipidopathy. This proteinopathy+lipidopathy paradigm has been further refined to a fatty acid (FA)‐opathy, centering dysregulated FA metabolism as fundamental in PD lipid dysfunction.
Julia C. Kelliher, Saranna Fanning
wiley +1 more source
Recapitulating Parkinson's disease pathology in a three-dimensional human neural cell culture model. [PDF]
Extensive loss of dopaminergic neurons, and aggregation of the protein α-synuclein into ubiquitin-positive Lewy bodies represents a major neuropathological hallmark of Parkinson's disease. At present the generation of large nuclear-associated Lewy bodies
Dalton, Caroline F +4 more
core +2 more sources
ABSTRACT Current therapies for Parkinson's disease (PD) fail to concurrently address α‐synuclein (α‐syn) aggregation and microglia‐mediated neuroinflammation. Herein, we engineer a near‐infrared‐II (NIR‐II) phototheranostic nanoplatform, CAG/FD1080@MM‐aTRPV4, for synergistic regulation of microglial function and real‐time monitoring of PD pathology. We
Hsuan Lo +9 more
wiley +1 more source
Polo-like kinase 2 modulates α-synuclein protein levels by regulating its mRNA production
Variations in the α-synuclein-encoding SNCA gene represent the greatest genetic risk factor for Parkinson's disease (PD), and duplications/triplications of SNCA cause autosomal dominant familial PD.
Rikke H. Kofoed +9 more
doaj +1 more source
{\alpha}-synuclein ({\alpha}-syn) is an intrinsically disordered protein which is considered to be one of the causes of Parkinson's disease. This protein forms amyloid fibrils when in a highly concentrated solution.
Kikuchi, Macoto, Shirai, Nobu C.
core +1 more source
An orthogonal ionic‐liquid extraction (Orth‐iEA) enables selective isolation of amyloid fibrils. TMGBF4 disrupts hydrogen‐bonded β‐sheet networks to solubilize amyloid aggregates, whereas C12ImCl interacts with hydrophobic regions of non‐amyloid proteins.
Shiying Zheng +10 more
wiley +1 more source
A series of Fe2+/viscosity cascade‐activated NIR fluorescence probes (NP1–5) are synthesized, and NP3 is selected for its optimal properties. To verify application of NP3 in ferroptosis intervention in PD, PQR NPs, is constructed by NP3 and quercetin self‐assembling.
Lixia Guo +11 more
wiley +1 more source
Introduction: Cell therapeutic clinical trials using fetal mesencephalic tissue provided a proof-of-concept for regenerative therapy in patients with Parkinson's disease.
Serina Gima +7 more
doaj +1 more source

