ZPD-2, a Small Compound That Inhibits α-Synuclein Amyloid Aggregation and Its Seeded Polymerization
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Sumoylation inhibits α-synuclein aggregation and toxicity
Posttranslational modification of proteins by attachment of small ubiquitin-related modifier (SUMO) contributes to numerous cellular phenomena. Sumoylation sometimes creates and abolishes binding interfaces, but increasing evidence points to another role for sumoylation in promoting the solubility of aggregation-prone proteins. Using purified α-synuclein, an aggregation-prone protein implicated...
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within the ␣-synuclein molecule, which self-aggregates to 2 Department of Pathology form amyloid and is an efficient seed for formation of A subsequently found to belong to a larger family of molecules , including -synuclein (or phosphoneuroprotein 14) (Jakes et al. We characterized -synuclein, the non-amyloidogenic molecule is a natively unfolded protein (Weinreb et al., homolog of ␣-synucl...
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ژورنال
عنوان ژورنال: Frontiers in Molecular Neuroscience
سال: 2019
ISSN: 1662-5099
DOI: 10.3389/fnmol.2019.00306