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Targeting α-synuclein post-translational modifications in Parkinson's disease

BEHAVIOURAL BRAIN RESEARCH (2023)

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Sumoylation inhibits α-synuclein aggregation and toxicity

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Ginkgolic Acid Inhibits Protein SUMOylation by Blocking Formation of the E1-SUMO Intermediate

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Polo-like Kinase 2 (PLK2) Phosphorylates α-Synuclein at Serine 129 in Central Nervous System

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The First N-terminal Amino Acids of α-Synuclein Are Essential for α-Helical Structure Formation In Vitro and Membrane Binding in Yeast

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SUMO-1 marks subdomains within glial cytoplasmic inclusions of multiple system atrophy

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α-synuclein locus duplication as a cause of familial Parkinson's disease

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Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy

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α-Synuclein in blood and brain from familial Parkinson disease with SNCA locus triplication

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Nuclear localization of α-synuclein and its interaction with histones

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Pathogenesis of Parkinson's disease:: Dopamine, vesicles and α-synuclein

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Structural and functional implications of C-terminal regions of α-synuclein

TD Kim et al.

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Conformational behavior of human α-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T

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Nonmotor fluctuations in Parkinson's disease -: Frequent and disabling

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α-Synuclein is phosphorylated in synucleinopathy lesions

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Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein

J Li et al.

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Review Cell Biology

Sumo, ubiquitin's mysterious cousin

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NATURE REVIEWS MOLECULAR CELL BIOLOGY (2001)

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Synucleins are a novel class of substrates for G protein-coupled receptor kinases

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Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease:: Implications for pathogenesis and therapy

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