Publications related to Pharmacological and biochemical assessment of γ-secretase-mediated APP processing involved in Alzheimer's disease

Related publications (12)

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

Hilal Lashuel, Henning Paul-Julius Stahlberg, Galina Limorenko, Rajasekhar Kolla, Meltem Tatli

The authors report a method for producing co-factor-free fibrils from all full-length Tau isoforms. The method paves the way for reconstituting pathology resembling Tau fibrils and enables screening of Tau aggregation-modifying compounds for targeted thera ...

Nature Research2023

Tau accumulation in degradative organelles is associated to lysosomal stress

Maurizio Molinari

Neurodegenerative disorders are characterized by the brain deposition of insoluble amyloidogenic proteins, such as alpha-synuclein or Tau, and the concomitant deterioration of cell functions such as the autophagy-lysosomal pathway (ALP). The ALP is involve ...

Nature Portfolio2023

Regulation and function of a hemicleaved Activin-A processing intermediate in melanoma

Manon Bulliard

Activin-A is a Transforming Growth Factor-B (TGFB)-related cytokine that regulates various biological processes including cell proliferation and differentiation through autocrine, paracrine or endocrine signaling. Activin-A expression is upregulated in mul ...

EPFL2023

Alzheimer's Disease Biomarkers in Idiopathic Normal Pressure Hydrocephalus: Linking Functional Connectivity and Clinical Outcome

Dimitri Nestor Alice Van De Ville, Alessandra Griffa

Background: Alzheimer's disease (AD) pathology impacts the response to treatment in patients with idiopathic normal pressure hydrocephalus (iNPH), possibly through changes in resting-state functional connectivity (rs-FC). ...

IOS PRESS2021

Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on alpha-synuclein amyloid formation

Giovanni Dietler, Giovanni Longo, Francesco Simone Ruggeri, Jiangtao Zhou

The formation of amyloid fibrils is a characterizing feature of a range of protein misfolding diseases, including Parkinson's disease. The propensity of native proteins to form such amyloid fibril, both in vitro and in vivo, is highly sensitive to the surr ...

2020

Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

Oleg Boyarkine, Vladimir Kopysov, Natalia Nagornova

The early stages of fibril formation are difficult to capture in solution. We use cold-ion spectroscopy to examine an 11-residue peptide derived from the protein transthyretin and clusters of this fibre-forming peptide containing up to five units in the ga ...

Wiley-Blackwell2018

Reduction of Abeta amyloid pathology in APPPS1 transgenic mice in the absence of gut microbiota

Theo Lasser, Tristan Bolmont, Taoufiq Harach

Alzheimer’s disease is the most common form of dementia in the western world, however there is no cure available for this devastating neurodegenerative disorder. Despite clinical and experimental evidence implicating the intestinal microbiota in a number o ...

Nature Research2017

Perturbations of the Straight Transmembrane alpha-Helical Structure of the Amyloid Precursor Protein Affect Its Processing by gamma-Secretase

Matteo Dal Peraro, Patrick Fraering, Mitko Dimitrov, Thomas Lemmin

Background: Amyloid- neurotoxicity depends on the specificity of the proteolytic cleavage of the amyloid precursor protein (APP) transmembrane domain. Results: The APP transmembrane -helix is straight in a biological membrane bilayer. Conclusion: The flexi ...

American Society for Biochemistry and Molecular Biology2014

Imaging brain amyloid deposition using grating-based differential phase contrast tomography

Patrick Aebischer, Jean-Charles Bensadoun, Peter Modregger

One of the core pathological features of Alzheimer's disease (AD) is the accumulation of amyloid plaques in the brain. Current efforts of medical imaging research aim at visualizing amyloid plaques in living patients in order to evaluate the progression of ...

Elsevier2012

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

On the origin of the MR image phase contrast: An in vivo MR microscopy study of the rat brain at 14.1 T

Rolf Gruetter, José Pedro Rebelo Ferreira Marques, Rajika Maddage

Recent studies at high magnetic fields using the phase of gradient-echo MR images have shown the ability to unveil cortical substructure in the human brain. To investigate the contrast mechanisms in phase imaging, this study extends, for the first time, ph ...

Elsevier2009

Visualizing odorant receptor trafficking in living cells down to the single-molecule level

Horst Arthur Vogel, Horst Pick, Jean-Manuel Segura, Valérie Jacquier

Despite the importance of trafficking for regulating G protein-coupled receptor signaling, for many members of the seven transmembrane helix protein family, such as odorant receptors, little is known about this process in live cells. Here, the complete lif ...

National Academy of Sciences2006