Publications by Anass Chiki | EPFL Graph Search

Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation

Graham Knott, Romain Hamelin, Anne-Laure Mahul Mellier, Nadine Aït Bouziad, Jonathan Jean-Pierre Ricci, Yllza Jasiqi, Mary-Claude Croisier-Coeytaux, Anass Chiki, Melek Firat Altay, Somanath Jagannath

Alpha-synuclein (aSyn) post-translational modifications (PTM), especially phosphorylation at serine 129 and C-terminal truncations, are highly enriched in Lewy bodies (LB), Lewy neurites, and other pathological aggregates in Parkinson's disease and synucle ...

Springer Science and Business Media LLC2025

Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore

Hilal Lashuel, Matteo Dal Peraro, Chan Cao, Lucien Fabrice Krapp, Simon Finn Mayer, Juan Francisco Bada Juarez, Anass Chiki, Pedro José Santana Ribeiro Magalhães

Protein post-translational modifications (PTMs) play a crucial role in countless biological processes, profoundly modulating protein properties on both spatial and temporal scales. Protein PTMs have also emerged as reliable biomarkers for several diseases. ...

Amer Chemical Soc2023

The role of PTM crosstalks in Httex1 structure, aggregation and membrane interaction

Hilal Lashuel, Matteo Dal Peraro, Luciano Andres Abriata, Lucien Fabrice Krapp, Charlotte Julie Caroline Gehin, Anass Chiki, Driss Boudeffa, Rajasekhar Kolla, Zhidian Zhang

CELL PRESS2022

Structural Basis of Huntingtin Fibril Polymorphism Revealed by Cryogenic Electron Microscopy of Exon 1 HTT Fibrils

Hilal Lashuel, Sergey Nazarov, Anass Chiki, Driss Boudeffa

The lack of detailed insight into the structure of aggregates formed by the huntingtin protein (HTT) has hampered the efforts to develop therapeutics and diagnostics targeting pathology formation in the brain of patients with Huntington's disease. To addre ...

2022

Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity

Hilal Lashuel, Nicolas Jean Philippe Guex, Christian Iseli, Anne-Laure Mahul Mellier, Jonathan Jean-Pierre Ricci, Yllza Jasiqi, Anass Chiki, Sean Michael Deguire, Ritwik Burai, Melek Firat Altay

Antibodies against phosphorylated alpha-synuclein (aSyn) at 5129 have emerged as the primary tools to investigate, monitor, and quantify aSyn pathology in the brain and peripheral tissues of patients with Parkinson's disease and other neurodegenerative dis ...

NATURE PORTFOLIO2022

Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates

Hilal Lashuel, Anass Chiki

Huntington's disease (HD) is caused by a CAG trinucleotide repeat expansion in the first exon of the huntingtin (HTT) gene coding for the huntingtin (HTT) protein. The misfolding and consequential aggregation of CAG-expanded mutant HTT (mHTT) underpin HD p ...

Nature Portfolio2021

Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation

Hilal Lashuel, Matteo Dal Peraro, Luciano Andres Abriata, Lucien Fabrice Krapp, Anass Chiki, Driss Boudeffa, Iman Rostami, Rajasekhar Kolla, Zhidian Zhang

Post-translational modifications (PTMs) within the first 17 amino acids (Nt17) of the Huntingtin protein (Htt) have been shown to inhibit the aggregation and attenuate the toxicity of mutant Htt proteins in vitro and in various models of Huntington’s disea ...

2021

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

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

TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models

Johan Auwerx, Hilal Lashuel, Laurent Mouchiroud, Anass Chiki, Lara Petricca, Ramanath Narayana Hegde

Phosphorylation of the N‐terminal domain of the huntingtin (HTT ) protein has emerged as an important regulator of its localization, structure, aggregation, clearance and toxicity. However, validation of the effect of bona fide phosphorylation in vivo and ...

2020

A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of alpha-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in alpha-synuclein research

Hilal Lashuel, Anass Chiki, Sonia Donzelli, Muhammed Muazzam Kamil Syed

Increasing evidence suggests that the process of alpha-synuclein (alpha-syn) aggregation from monomers into amyloid fibrils and Lewy bodies, via oligomeric intermediates plays an essential role in the pathogenesis of different synucleinopathies, including ...

Wiley-Blackwell2020