Results 11 to 20 of about 1,144,970 (369)
Toxicity of extracellular alpha-synuclein is independent of intracellular alpha-synuclein
Scientific Reports, 2022 Parkinson′s disease (PD) pathology progresses throughout the nervous system affecting numerous neuronal structures. It has been postulated that the progression of the pathology is based on a prion-like disease mechanism partly due to the seeding effect ...
Yanina Dening +16 more
semanticscholar +7 more sources
Neural connectivity predicts spreading of alpha-synuclein pathology in fibril-injected mouse models: Involvement of retrograde and anterograde axonal propagation [PDF]
Neurobiology of Disease, 2020 In Parkinson's disease, some of the first alpha-synuclein aggregates appear in the olfactory system and the dorsal motor nucleus of the vagus nerve before spreading to connected brain regions.
Christopher Mezias +3 more
doaj +4 more sources
Alpha-Synuclein Aggregation in Parkinson's Disease [PDF]
Frontiers in Medicine, 2021 Parkinson's disease (PD), a neurodegenerative disorder characterized by distinct aging-independent loss of dopaminergic neurons in substantia nigra pars compacta (SNpc) region urging toward neuronal loss.
E. Srinivasan +7 more
semanticscholar +5 more sources
Alpha synuclein in hematopoiesis and immunity
Heliyon, 2019 Parkinson's disease (PD) is the second most common neurodegenerative condition and intracellular deposition of Lewy bodies in the substantia nigra (SN), which can cause dopaminergic neuronal death, is the hallmark of this syndrome. α-synuclein (syn) is a
Yu Pei, Robert W. Maitta
doaj +4 more sources
C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging. [PDF]
PLoS Genetics, 2008 Inclusions in the brain containing alpha-synuclein are the pathological hallmark of Parkinson's disease, but how these inclusions are formed and how this links to disease is poorly understood. We have developed a C.
Tjakko J van Ham +5 more
doaj +11 more sources
Cryo-EM structure of alpha-synuclein fibrils
eLife, 2018 Intracellular inclusions of alpha-synuclein are the neuropathological hallmark of progressive disorders called synucleinopathies. Alpha-synuclein fibrils are associated with transmissive cell-to-cell propagation of pathology.
R. Guerrero-Ferreira +7 more
semanticscholar +8 more sources
Synapsin Condensates Recruit alpha-Synuclein.
Journal of Molecular Biology, 2021 Neurotransmission relies on the tight spatial and temporal regulation of the synaptic vesicle (SV) cycle. Nerve terminals contain hundreds of SVs that form tight clusters. These clusters represent a distinct liquid phase in which one component of the phase are SVs and the other synapsin 1, a highly abundant synaptic protein.
Christian Hoffmann +7 more
semanticscholar +5 more sources
The Membrane Interaction of Alpha-Synuclein [PDF]
Frontiers in Cellular Neuroscience, 2021 A presynaptic protein closely related to Parkinson's disease (PD), α-synuclein (α-Syn), has been studied extensively regarding its pathogenic mechanisms. As a physiological protein in presynapses, however, α-Syn's physiological function remains unclear.
Cencen Liu +7 more
openaire +4 more sources
Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K. [PDF]
, 2013 PMCID: PMC3591419This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited ...
A Loquet +50 more
core +17 more sources
Alpha-Synuclein and Its Role in Melanocytes [PDF]
Cells, 2022 Pigmentation is an important process in skin physiology and skin diseases and presumably also plays a role in Parkinson’s disease (PD). In PD, alpha-Synuclein (aSyn) has been shown to be involved in the pigmentation of neurons. The presynaptic protein is intensively investigated for its pathological role in PD, but its physiological function remains ...
Nicole Rachinger +5 more
openaire +3 more sources