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

Related publications (37)

Discovery and characterization of novel stable tau oligomeric complexes: Implications for the role of Tau/phospholipid interactions in regulating its functions in health and disease

Hilal Lashuel, Anne-Laure Mahul Mellier, Nadine Aït Bouziad, Gizem Zorludemir

The microtubule-associated protein Tau plays a central role in the pathogenesis of Alzheimer's disease. Although Tau interaction with membranes is thought to affect some of its physiological functions and its aggregation properties, the sequence determinan ...
Nature Publishing Group2017

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

Hilal Lashuel, Nadine Aït Bouziad, Raffaele Mezzenga

Tau protein and its fragments self-assemble into amyloid fibrils in the presence of polyanions, such as heparin. By combining microscopy, scattering, and spectroscopy techniques, we studied the aggregation of the 26-mer Tau-derived peptide alone, Tau306-32 ...
Wiley-V C H Verlag Gmbh2016

Endogenous Regulators of Gamma-Secretase and Amyloid-Beta Production, and Engineering of Alzheimer's Disease Therapeutic Tools

Sébastien Mosser

Alzheimer s disease (AD) is a devastating neurodegenerative disease characterized by strong cognitive impairment and memory loss. These symptoms are caused by neuronal death, induced by two pathological hallmarks: extracellular senile plaques composed of a ...
EPFL2016

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

Hilal Lashuel, Patrick Droste

Background: Beside neurofibrillary tangles, amyloid plaques are the major histological hallmarks of Alzheimer's disease (AD) being composed of aggregated fibrils of beta-amyloid (A beta). During the underlying fibrillogenic pathway, starting from a surplus ...
Biomed Central Ltd2015

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

Hilal Lashuel, Bruno Claude Daniel Fauvet

Posttranslational modifications (PTMs) serve as molecular switches for regulating protein folding, function, and interactome and have been implicated in the misfolding and amyloid formation by several proteins linked to neurodegenerative diseases, includin ...
2015

Focal expression of adeno-associated viral-mutant tau induces widespread impairment in an APP mouse model

Patrick Aebischer, Bernard Schneider, Jean-Charles Bensadoun

Adeno-associated virus serotype 6 (AAV6) viral vectors encoding mutant and normal tau were used to produce focal tau pathology. Two mutant forms of tau were used; the P301S tau mutation is associated with neurofibrillary tangle formation in humans, and the ...
Elsevier Science Inc2013

Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method

Giovanni Dietler, Hilal Lashuel, Francesco Simone Ruggeri, Jae Sun Jeong, Raffaele Mezzenga

We report the investigation of the mechanical properties of different types of amyloid fibrils by the peak force quantitative nanomechanical (PF-QNM) technique. We demonstrate that this technique correctly measures the Young's modulus independent of the po ...
2012

The Gamma-Secretase-Mediated Proteolytic Processing of APP C-Terminal Fragments as a Therapeutic Target for Alzheimer's Disease

Jemila Houacine

Alzheimer's disease (AD) is a devastating neurodegenerative disorder which severely impairs cognitive functions by triggering neuronal cell death and synaptic loss, and finally leads the patients to death. Two main histopathological hallmarks can be found ...
EPFL2011

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

Co-pathological states of tau proteins in a 3D micropatterned neural cell culture

Philippe Renaud, Robert Meissner, Anja Kunze, Serena Brando

In vitro studies of Alzheimer’s disease are based on homogenously seeded neural cells. These studies reveal molecular pathway mechanism related to neurite degeneration, but they cannot analyze interactions between diseased and healthy cells. Furthermore, t ...
2011

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