L
Laura Pieri
Researcher at University of Florence
Publications - 54
Citations - 3883
Laura Pieri is an academic researcher from University of Florence. The author has contributed to research in topics: Medicine & Protein aggregation. The author has an hindex of 20, co-authored 48 publications receiving 3301 citations. Previous affiliations of Laura Pieri include French Institute of Health and Medical Research & Centre national de la recherche scientifique.
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Journal ArticleDOI
α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells
Christian Hansen,Elodie Angot,Ann-Louise Bergström,Jennifer A. Steiner,Laura Pieri,Gesine Paul,Tiago F. Outeiro,Ronald Melki,Pekka Kallunki,Karina Fog,Jia-Yi Li,Patrik Brundin +11 more
TL;DR: In vivo transfer of α-syn between host cells and grafted dopaminergic neurons in mice overexpressing human α- syn and results suggest that α- Syn propagation is a key element in the progression of Parkinson disease pathology.
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Structural and functional characterization of two alpha-synuclein strains
Luc Bousset,Laura Pieri,Gemma Ruiz-Arlandis,Julia Gath,Poul Henning Jensen,Birgit Habenstein,Karine Madiona,Vincent Olieric,Anja Böckmann,Beat H. Meier,Ronald Melki +10 more
TL;DR: It is shown that the two strains of α-synuclein have different structures, levels of toxicity, and in vitro and in vivo seeding and propagation properties, which may account for differences in disease progression in different individuals/cell types and/or types of synucleinopathies.
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G51D α-synuclein mutation causes a novel parkinsonian-pyramidal syndrome.
Suzanne Lesage,Mathieu Anheim,Franck Letournel,Luc Bousset,Aurélie Honoré,Nelly Rozas,Laura Pieri,Karine Madiona,Alexandra Durr,Ronald Melki,Christophe Verny,Alexis Brice +11 more
TL;DR: A French family with a parkinsonian–pyramidal syndrome harboring a novel heterozygous SNCA mutation is described.
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Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes.
Saïda Abounit,Luc Bousset,Frida Loria,Seng Zhu,Fabrice de Chaumont,Laura Pieri,Jean-Christophe Olivo-Marin,Ronald Melki,Chiara Zurzolo +8 more
TL;DR: Using quantitative fluorescence microscopy with co‐cultured neurons, it is shown that α‐synuclein fibrils efficiently transfer from donor to acceptor cells through tunneling nanotubes (TNTs) inside lysosomal vesicles, revealing a possible novel role of TNTs and lysOSomes in the progression of synucleinopathies.
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Fibrillar α-Synuclein and Huntingtin Exon 1 Assemblies Are Toxic to the Cells
TL;DR: Overall, the data indicate that fibrillar α-syn and HttEx1, rather than their precursor oligomers, are highly cytotoxic, the toxicity being associated to their ability to bind and permeabilize the cell membranes.