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The centriolar protein CPAP G-box: an amyloid fibril in a single domain

Publications associées (44)

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It is assumed that amyloid-beta aggregation is a crucial event in the pathogenesis of Alzheimer's disease. Novel 2,6-disubstituted pyridine derivatives were designed to interact with the beta-sheet conformation of A beta via donor-acceptor-donor hydrogen b ...

Pergamon-Elsevier Science Ltd2016

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Amyloid fibrils associated with neurodegenerative diseases, such as Parkinson's and Alzheimer's, consist of insoluble aggregates of α-synuclein and Aβ-42 proteins with a high β-sheet content. The aggregation of both proteins occurs by misfolding of the mon ...

Wiley-Blackwell2015

New Insights Into Amyloid Formation and Structure by Innovative Atomic Force Microscopy Methods

Francesco Simone Ruggeri

Today, more than 40 million people worldwide are affected by neurodegenerative disorders. Onset of these diseases is associated with insoluble fibrillar protein aggregates, termed amyloids. The molecular origin and the link between amyloid formation and di ...

EPFL2015

The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems

Alessandro Barducci

The OPEP coarse-grained protein model has been applied to a wide range of applications since its first release 15 years ago. The model, which combines energetic and structural accuracy and chemical specificity, allows the study of single protein properties ...

Royal Society of Chemistry2014

Nucleation Process of a Fibril Precursor in the C-Terminal Segment of Amyloid-beta

Fabio Pietrucci

By extended atomistic simulations in explicit solvent and bias-exchange metadynamics, we study the aggregation process of 18 chains of the C-terminal segment of amyloid-beta, an intrinsically disordered protein involved in Alzheimer's disease and prone to ...

Amer Physical Soc2013

All-atom simulations of crowding effects on ubiquitin dynamics

Matteo Dal Peraro, Luciano Andres Abriata, Enrico Spiga

It is well-known that crowded environments affect the stability of proteins, with strong biological and biotechnological implications; however, beyond this, crowding is also expected to affect the dynamic properties of proteins, an idea that is hard to pro ...

Iop Publishing Ltd2013

The doppel (Dpl) and prion (PrP) proteins share a very similar fold (three helices and two short beta-strands), while they differ significantly in sequence (only 25% homologous) and in disease-related beta-rich conformations that occur for PrP only. In a p ...

American Chemical Society2013

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

Hilal Lashuel, Bruno Claude Daniel Fauvet, Loay Awad, Mirva Hejjaoui

It has been more than a century since the first evidence linking the process of amyloid formation to the pathogenesis of Alzheimer's disease. During the last three decades in particular, increasing evidence from various sources (pathology, genetics, cell c ...

Elsevier2012

Structural Studies and Protein Engineering of Human O6-Alkylguanine-DNA Alkyltransferase

Birgit Mollwitz

The specific labeling of proteins with synthetic probes is a powerful approach to study protein function and protein tags have been widely used for this purpose. A well-established example for a self-labeling protein tag is SNAP-tag. It specifically reacts ...

EPFL2012

Starting from a disordered aggregate, we have simulated the formation of ordered amyloid-like beta structures in a system formed by 18 polyvaline chains in explicit solvent, employing molecular dynamics accelerated by bias-exchange metadynamics. We exploit ...

2012