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α-Synuclein Structure and Function
StudioMolekuul, Shutterstockα-Synuclein is an integral component of Lewy bodies which are comprised of protein clumps and are a pathological hallmark of Parkinson’s disease. Here is the latest research on α-Synuclein structure and function.
Glucocerebrosidase Defects as a Major Risk Factor for Parkinson's Disease
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding
α-Synuclein Translocates to the Nucleus to Activate Retinoic-Acid-Dependent Gene Transcription
The function of bacterial HtrA is evolutionally conserved in mammalian HtrA2/Omi
Long-range Regulation of Partially Folded Amyloidogenic Peptides
Hsp27 reduces glycation-induced toxicity and aggregation of alpha-synuclein
A new MAP-Rasagiline conjugate reduces α-synuclein inclusion formation in a cell model
α-synuclein inclusions are abundant in non-neuronal cells in the anterior olfactory nucleus of the Parkinson's disease olfactory bulb
Role of Alterations in Protein Kinase p38γ in the Pathogenesis of the Synaptic Pathology in Dementia With Lewy Bodies and α-Synuclein Transgenic Models
Immunotherapies for Aging-Related Neurodegenerative Diseases-Emerging Perspectives and New Targets
Neurodegeneration-Associated Proteins in Human Olfactory Neurons Collected by Nasal Brushing
Proteostasis of α-Synuclein and Its Role in the Pathogenesis of Parkinson's Disease
Protein trapping leads to altered synaptic proteostasis in synucleinopathies
SARS-CoV-2: at the crossroad between aging and neurodegeneration
Increased alpha-synuclein tear fluid levels in patients with Parkinson's disease
Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy
Freezing and piercing of in vitro asymmetric plasma membrane by α-synuclein
Inhibition of HDAC6 activity protects dopaminergic neurons from alpha-synuclein toxicity
Interaction of the chaperones alpha B-crystallin and CHIP with fibrillar alpha-synuclein: Effects on internalization by cells and identification of interacting interfaces
Understanding Creutzfeldt-Jackob disease from a viewpoint of amyloidogenic evolvability
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