We focused our attention on interaction between a-synuclein and a isoform of 14-3-3. It was found that 14-3-3 inhibits synucleinaggregation in vitro leading to the formation of aggregates morphologically different from classical synuclein fibrils. The goal is thecharacterisation of both the aggregates and their mechanism of formation.
14-3-3 Protein Can Act As A Molecular Chaperon That Inhibits -Synuclein Aggregation In Vitro.
Munari F;CAPALDI, Stefano;MONACO, Ugo Luigi;
2010-01-01
Abstract
We focused our attention on interaction between a-synuclein and a isoform of 14-3-3. It was found that 14-3-3 inhibits synucleinaggregation in vitro leading to the formation of aggregates morphologically different from classical synuclein fibrils. The goal is thecharacterisation of both the aggregates and their mechanism of formation.
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