Anne‐Laure Mahul‐Mellier

This paper identifies compounds that enhance protein turnover in human neurons using a live-cell imaging platform and validates their efficacy in reducing a-synuclein aggregates.

The paper maps the lipidomic architecture of the adult mouse brain at micrometric scale, revealing spatial lipid organization and its functional relevance.

This paper uses cryo-ET to study amyloid fibrils in neurodegenerative brain tissue, revealing ultrastructural details of fibril polymorphs and their association with disease.

This study introduces a microfluidic platform to assess membrane integrity in live neuronal cells by measuring dielectric properties, showing its ability to detect different forms of alpha-synuclein's effects on membrane capacitance.

This study identifies WDR44 as a driver of de novo α-synuclein aggregation at the lysosomal membrane, linking early aggregation events to neuronal dysfunction in Parkinson's Disease.

The paper determines the cryo-EM structure of alpha-synuclein fibrils with the E83Q mutation, revealing structural changes linked to enhanced aggregation and pathogenicity.

This paper introduces a site-specific organometallic method to install tyrosine phosphorylation mimics in alpha-synuclein, revealing that di- and tri-phosphorylation slow aggregation and reduce seeding activity.

This study uses human iPSC-derived dopaminergic neurons to model Parkinson's Lewy body pathology without genetic modification, revealing mechanisms of aSyn aggregation and morphological diversity.

The paper develops human tri-lineage brain microtissues composed of neurons, astrocytes, and microglia, showing they recapitulate cell-cell interactions and pathological processes.

This study investigates how C-terminal truncations of alpha-synuclein (aSyn) affect Lewy body (LB) formation and pathology in Parkinson's disease by analyzing their role in fibril processing and aggregation.

This study shows that nitration of alpha-synuclein after fibrillization reduces its seeding activity and pathology formation in neurons and in vivo.

The paper shows that neighboring post-translational modifications affect the detection of phosphorylated alpha-synuclein at Serine 129 by existing antibodies.

The paper investigates the effects of the E83Q mutation on alpha-synuclein aggregation and toxicity, finding it accelerates fibrillization and enhances pathological features in neuronal models.

The paper examines the biochemical composition, interactome, and ultrastructural properties of nuclear and cytoplasmic Htt inclusions in mammalian cells and neurons.

This study shows that the Nt17 domain regulates Httex1 aggregation, toxicity, and cellular uptake through its conformation and interaction with polyQ repeats.

This study develops a neuronal model of Lewy body formation and shows that the process of Lewy body maturation, not just fibrillization, drives neurodegeneration in synucleinopathies.

Calpain-1/2 cleavage of the alpha-synuclein C-terminus after fibril formation is reported to drive seeding, aggregation and the maturation of Lewy-body-like inclusions in primary neurons.