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Article
Open AccessBiophysical characterization of the phase separation of TDP-43 devoid of the C-terminal domain
Frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-TDP), amyotrophic lateral sclerosis (ALS) and limbic-predominant age-related TDP-43 encephalopathy (LATE) are associated with depositi...
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Article
Open AccessPutative novel CSF biomarkers of Alzheimer’s disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort
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Article
Open AccessA single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF
Amyloid-β42 (Aβ42) aggregation consists of a complex chain of nucleation events producing soluble oligomeric intermediates, which are considered the major neurotoxic agents in Alzheimer’s disease (AD). Cerebral l...
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Article
Open AccessEffects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies
Protein misfolding is a general hallmark of protein deposition diseases, such as Alzheimer’s disease or Parkinson’s disease, in which different types of aggregated species (oligomers, protofibrils and fibrils)...
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Article
Open AccessThe release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells
The self-assembly of α-synuclein (αS) into intraneuronal inclusion bodies is a key characteristic of Parkinson’s disease. To define the nature of the species giving rise to neuronal damage, we have investigate...
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Article
Open AccessTrodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism
The onset and progression of numerous protein misfolding diseases are associated with the presence of oligomers formed during the aberrant aggregation of several different proteins, including amyloid-β (Aβ) in...
