α-Synuclein Aggregation in Treatment of Parkinson's Disease

Por um escritor misterioso

Descrição

Parkinson’s disease, the second most common neurodegenerative disorder worldwide, is characterized by the accumulation of protein deposits in the dopaminergic neurons. These deposits are primarily composed of aggregated forms of α-Synuclein (α-Syn). PD is a complex pathology initially associated with motor deficiencies, as a result of an acute neuronal loss in substantia nigra pars compacta (SNc), with a significant dopaminergic (DA) impairment.
α-Synuclein Aggregation in Treatment of Parkinson's Disease
Stress-induced p53 drives BAG5 cochaperone expression to control α-synuclein aggregation in Parkinson's disease - Figure f6
α-Synuclein Aggregation in Treatment of Parkinson's Disease
Active alpha-synuclein proteins
α-Synuclein Aggregation in Treatment of Parkinson's Disease
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α-Synuclein Aggregation in Treatment of Parkinson's Disease
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α-Synuclein Aggregation in Treatment of Parkinson's Disease
α‐Synuclein Radiotracer Development and In Vivo Imaging: Recent Advancements and New Perspectives - Alzghool - 2022 - Movement Disorders - Wiley Online Library
α-Synuclein Aggregation in Treatment of Parkinson's Disease
Interactions between iron and α-synuclein pathology in Parkinson's disease - ScienceDirect
α-Synuclein Aggregation in Treatment of Parkinson's Disease
Frontiers Targeting Alpha-Synuclein as a Therapy for Parkinson's Disease
α-Synuclein Aggregation in Treatment of Parkinson's Disease
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α-Synuclein Aggregation in Treatment of Parkinson's Disease
Therapeutics in the Pipeline Targeting α-Synuclein for Parkinson's Disease
α-Synuclein Aggregation in Treatment of Parkinson's Disease
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α-Synuclein Aggregation in Treatment of Parkinson's Disease
Exosomal transmission of α-synuclein initiates Parkinson's disease-like pathology
α-Synuclein Aggregation in Treatment of Parkinson's Disease
p21-activated kinase 4 controls the aggregation of α-synuclein by reducing the monomeric and aggregated forms of α-synuclein: involvement of the E3 ubiquitin ligase NEDD4-1
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