Publications associées à Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils

Publications associées (9)

Self-driving microscopy detects the onset of protein aggregation and enables intelligent Brillouin imaging

Camille Valentine Cathala, Hilal Lashuel, Aleksandra Radenovic, Lely Feletti, Khalid Ashraf Mohie Ibrahim

The process of protein aggregation, central to neurodegenerative diseases like Huntington’s, is challenging to study due to its unpredictable nature and relatively rapid kinetics. Understanding its biomechanics is crucial for unraveling its role in disease ...

Springer Science and Business Media LLC2025

Enhancing mitochondrial quality control to fight neuromuscular degeneration in aging and disease

Mario Romani

Loss of mitochondrial function and proteostasis typify aging and age-associated degenerative disorders such as Alzheimer's disease and muscle aging. To date, no cure or preventive measure is available to manage these conditions. Alterations of cellular pro ...

EPFL2021

Calorie restriction slows age-related microbiota changes in an Alzheimer's disease model in female mice

Julia Chiara Vincentini

Alzheimer's disease (AD) affects an estimated 5.8 million Americans, and advanced age is the greatest risk factor. AD patients have altered intestinal microbiota. Accordingly, depleting intestinal microbiota in AD animal models reduces amyloid-beta (A beta ...

Springer Nature2019

Detection of Alzheimer’s disease amyloid-beta plaque deposition by deep brain impedance profiling

Philippe Renaud, Patrick Fraering, Amélie Barbara Hildegarde Béduer, Pierre Joris, Sébastien Mosser

OBJECTIVE: Alzheimer disease (AD) is the most common form of neurodegenerative disease in elderly people. Toxic brain amyloid-beta (ASS) aggregates and ensuing cell death are believed to play a central role in the pathogenesis of the disease. In this study ...

Iop Publishing Ltd2015

Lack of additive role of ageing in nigrostriatal neurodegeneration triggered by alpha-synuclein overexpression

Grégoire Courtine, Laetitia Danielle Philippine Baud

Introduction: Parkinson's disease (PD) is a progressive neurodegenerative disorder characterized by the loss of dopaminergic neurons as well as the presence of proteinaceous inclusions named Lewy bodies. alpha synuclein (alpha-syn) is a major constituent o ...

2015

Discovery and Structure Activity Relationship of Small Molecule Inhibitors of Toxic β-Amyloid-42 Fibril Formation

Hilal Lashuel, Andrea Pfeifer, Annalisa Ansaloni, Mohammad Asad Jan Qureshi

Increasing evidence implicates Aβ peptides self-assembly and fibril formation as crucial events in the pathogenesis of Alzheimer disease. Thus, inhibiting Aβ aggregation, among others, has emerged as a potential therapeutic intervention for this disorder. ...

Amer Soc Biochemistry Molecular Biology Inc2012

Self-Assembly of ß-Amyloid Peptides in Cells and on Solid Supports

Enrico Condemi

Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease and Huntington's disease share common mechanisms characterized by protein misfolding and aggregation, including formation of plaques or inclusion bodies. The rapid growing number o ...

EPFL2011

Structure and function of the molecular chaperone Hsp104 from yeast

Hilal Lashuel

The molecular chaperone Hsp104 plays a central role in the clearance of aggregates after heat shock and the propagation of yeast prions. Hsp104's disaggregation activity and prion propagation have been linked to its ability to resolubilize or remodel prote ...

Wiley-Blackwell2009

alpha -Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease

Patrick Aebischer, Bernard Schneider, Nicole Déglon, Christophe Lo Bianco

Parkinson's disease (PD) is characterized by the progressive loss of substantia nigra dopaminergic neurons and the presence of cytoplasmic inclusions named Lewy bodies. Two missense mutations of the alpha-synuclein (alpha-syn; A30P and A53T) have been desc ...

National Academy of Sciences2002