Conformational diseases constitute a group of heterologous disorders in which a constituent host protein undergoes changes in conformation, leading to aggregation and deposition. In order to understand the molecular mechanisms of amyloid-fibril formation, several in vitro and in vivo studies, thus including model and pathologically relevant proteins, have been performed. In this work we presented a detail analysis of the mechanism by which proteins undergo ordered aggregation into amyloid fibrils classified in three groups, namely (a) templating and nucleation; (b) linear, colloid-like assembly of spherical oligomers; and (c) domain-swapping.
COBISS.SI-ID: 24680231
Based on the observation that progressive myoclonus epilepsies (PMEs) and neurodegenerative diseases share common features of neurodegeneration, in this work we proposed that the two pathologies share common underlying molecular characteristics. It is well documented that autophagy is overloaded or impaired in neurodegenerative conditions including Lafora disease (EPM2). Although more research into this connection will be necessary, we proposed that existing therapies for PMEs could be enhanced using similar drugs as those used for the treatment of neurodegenerative diseases.
COBISS.SI-ID: 24607527
In this work we present a detailed analysis of the dual role of lysosomes and lysosomal cathepsins in the two main pathways of cell death, namely, apoptosis and autophagy. Destabilization of the lysosomal membranes by lysosomotropic detergents seems to be a promising strategy as it would not only disable autophagy, but also promote apoptosis through the initiation of the lysosomal pathway. On the other side, the impaired autophagy and lysosomal degradation linked with the increased oxidative stress underlie degenerative changes in the aging neurons.
COBISS.SI-ID: 25347879