Publications de Sophie Vieweg | EPFL Graph Search

The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1

Giovanni Dietler, Hilal Lashuel, Anass Chiki, Francesco Simone Ruggeri, Anne-Laure Mahul Mellier, Sophie Vieweg, Sean Michael Deguire, Urszula Beata Cendrowska, Nathan Alain Denis Riguet

Converging evidence points to the N-terminal domain comprising the first 17 amino acids of the Huntingtin protein (Nt17) as a key regulator of its aggregation, cellular properties and toxicity. In this study, we further investigated the interplay between N ...

Elsevier2021

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM

Hilal Lashuel, Anass Chiki, Nadine Aït Bouziad, Francesco Stellacci, Paulo Henrique Jacob Silva, Marie Mueller, Zekiye Pelin Güven, Sophie Vieweg, Urszula Beata Cendrowska

Increasing evidence suggests that amyloid polymorphism gives rise to different strains of amyloids with distinct toxicities and pathology-spreading properties. Validating this hypothesis is challenging due to a lack of tools and methods that allow for the ...

National Academy of Sciences2020

The role of the polyglutamine and N-terminal domains in regulating the aggregation and structural properties of Huntingtin Exon 1

Sophie Vieweg

Huntington Disease (HD) is caused by a CAG repeat expansion in the huntingtin gene leading to the formation of mutant Huntingtin protein (Htt) with an expanded polyglutamine (polyQ) domain (>36Q). Generation of short N-terminal Htt fragments by proteolysis ...

EPFL2017

Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6

Giovanni Dietler, Hilal Lashuel, Anass Chiki, Annalisa Ansaloni, Francesco Simone Ruggeri, Ritwik Burai, Sophie Vieweg, Sean Michael Deguire, Urszula Beata Cendrowska

Herein, we used protein semisynthesis to investigate, for the first time, the effect of lysine acetylation and phosphorylation, as well as the crosstalk between these modifications on the structure and aggregation of mutant huntingtin exon1 (Httex1). Our r ...

Wiley-Blackwell2017

An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation

Hilal Lashuel, Annalisa Ansaloni, Sophie Vieweg, John Blaine Warner IV

The first exon of the Huntingtin protein (Httex1) is one of the most actively studied Htt fragments because its overexpression in R6/2 transgenic mice has been shown to recapitulate several key features of Huntington disease. However, the majority of bioph ...

Amer Soc Biochemistry Molecular Biology Inc2016