In this work our group managed to improve the model for teh mechanism of amyloid fibril formation by stefin B - as an appropriate model. We included in the simulation the transformation of initial oligomers.
COBISS.SI-ID: 26998567
As amyloid forming proteins resemble pore forming toxins, this study bears relevance to this project. PI contributed with conformational and kinetical studies of these steps.
COBISS.SI-ID: 2836815
In this paper Mira P- et al., have determined how EPM1 mutants cleavages occur. This is important as a more open structure of the mutants allows cathepsins to process them faster and thus to lose any inhibitory activity and even worse, to promote aggregation.
COBISS.SI-ID: 26511655