Hilal A. Lashuel

Membrane permeabilization: a common mechanism in protein-misfolding diseases.

Amyloid fibril formation by macrophage migration inhibitory factor.

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's disease.

Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies.

One-pot total chemical synthesis of human α-synuclein.

The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.

The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity.

Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease.

Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo.

Structural differences of amyloid-β fibrils revealed by antibodies from phage display.

Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein.

Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons.

Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's disease.

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.

Phosphorylation of huntingtin at residue T3 is decreased in Huntington's disease and modulates mutant huntingtin protein conformation.

Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes.