G
Gemma Ruiz-Arlandis
Researcher at Centre national de la recherche scientifique
Publications - 4
Citations - 780
Gemma Ruiz-Arlandis is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Huntingtin & Protein aggregation. The author has an hindex of 3, co-authored 4 publications receiving 634 citations.
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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.
Journal ArticleDOI
Molecular Interaction between the Chaperone Hsc70 and the N-terminal Flank of Huntingtin Exon 1 Modulates Aggregation
TL;DR: The mechanism of interaction between a huntingtin exon 1 fragment of increasing polyQ lengths (HttEx1Qn), the aggregation of which is tightly associated with Huntington's disease, and molecular chaperone Hsc70 is dissected to lay the foundations of future therapeutic strategies targeting huntingtin aggregation in Huntington disease.
Journal ArticleDOI
Binding, internalization and fate of Huntingtin Exon1 fibrillar assemblies in mitotic and nonmitotic neuroblastoma cells.
TL;DR: The aggregation of Huntingtin protein and its moiety encoded by its Exon1 into fibrillar structures inside neurons is the molecular hallmark of Huntington's disease and prion‐like transmission of these aggregates between cells has been demonstrated.
Molecular Interaction between the Chaperone Hsc70 and the N-terminal Flank of Huntingtin Exon 1 Modulates
TL;DR: It is shown that Hsc70, together with its Hsp40 co-chaperones, inhibits HttEx1Qn aggregation and modifies the structural, seeding, and infectious properties of the resulting fibrils in a polyQ-independent manner.