Publications associées à Maladie débilitante chronique

Trans‐seeding of Alzheimer‐related tau protein by a yeast prion

Henning Paul-Julius Stahlberg, Zhiva Skachokova

Abnormal tau protein aggregates constitute a hallmark of Alzheimer's disease. The mechanisms underlying the initiation of tau aggregation in sporadic neurodegeneration remain unclear. Here we investigate whether a non-human prion can seed tau aggregation. ...

2022

Rethinking protein aggregation and drug discovery in neurodegenerative diseases: Why we need to embrace complexity?

Hilal Lashuel

More than a century has passed since pathological protein aggregates were first identified in the brains of patients with neurodegenerative diseases (NDDs). Yet, we still do not have effective therapies to treat or slow the progression of these devastating ...

2021

Calpain-mediated tau fragmentation is altered in Alzheimer's disease progression

Andrea Pfeifer, Andreas Muhs

The aggregation of intracellular tau protein is a major hallmark of Alzheimer's disease (AD). The extent and the stereotypical spread of tau pathology in the AD brain are correlated with cognitive decline during disease progression. Here we present an in-d ...

Nature Research2018

Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding

Hilal Lashuel, Juan Kiwi, Bruno Claude Daniel Fauvet, Anass Chiki, Farah El Turk

Intracellular deposits of α-synuclein in the form of Lewy bodies are major hallmarks of Parkinson’s disease (PD) and a range of related neurodegenerative disorders. Post-translational modifications (PTMs) of α-synuclein are increasingly thought to be major ...

2018

In Vivo Longitudinal (1)H MRS Study of Transgenic Mouse Models of Prion Disease in the Hippocampus and Cerebellum at 14.1 T

Rolf Gruetter, Cristina Ramona Cudalbu, Mélanie Craveiro

In vivo (1)H MR spectroscopy allows the non invasive characterization of brain metabolites and it has been used for studying brain metabolic changes in a wide range of neurodegenerative diseases. The prion diseases form a group of fatal neurodegenerative d ...

Springer Verlag2015

Ultrafast photoinduced processes in metal - containing molecular complexes and in proteins

Roberto Monni

The aim of this thesis is to investigate the ultrafast inter¿ and intra¿molecular processes, occurring in both metal¿containing molecular complexes and in proteins, by means of ultrafast Transient Absorption (TA) spectroscopy. The first part of the thesis ...

EPFL2015

Two Misfolding Routes for the Prion Protein around pH 4.5

Ursula Röthlisberger, Ivano Tavernelli

Using molecular dynamics simulations, we show that the prion protein (PrP) exhibits a dual behavior, with two possible transition routes, upon protonation of H187 around pH 4.5, which mimics specific conditions encountered in endosomes. Our results suggest ...

Public Library Science2013

Elucidating the role of post-translational modifications of alpha-synuclein using semisynthesis : phosphorylation at Tyrosine 125 and monoubiquitination at Lysine 6

Mirva Hejjaoui

Alpha-synuclein (α-syn) is a natively unfolded protein that is closely linked to Parkinson’s disease (PD) by genetic, neuropathologic and biochemical evidence. Aggregated and fibrillar forms of α-syn are the main components of intracellular protein inclusi ...

EPFL2012

Characterisation of Living Matter Using Advanced Spectroscopy Techniques

Markus Bonda

In the context of an ageing society neurodegenerative disease have become more and more frequent among humans. Opposing the benefits of a longer life, these diseases have thus triggered research on neurons and how they interact with each other. In vitro as ...

EPFL2011

Nucleation Dependent Polymerization of Amyloid-ß (Aß) as an Important Determinant of Aß Amyloid Formation and Neurotoxicity : Implications for the Pathogenesis of Alzheimer's Disease and Design of Therapies

Mohammad Asad Jan Qureshi

Aggregation and fibril formation of amyloid-β (Aβ) peptides play a pivotal role in the pathogenesis of Alzheimer's disease (AD). Aβ peptides, principally comprising of 40 or 42 amino acid residues (Aβ40 and Aβ42), are produced by proteolytic processing of ...

EPFL2010