Elzbieta Glaser

TL;DR: This work presents a unique import mechanism for Aβ in mitochondria and demonstrates both in vitro and in vivo that Aβ is located to the mitochondrial cristae, and shows that extracellulary applied Aβ can be internalized by human neuroblastoma cells and can colocalize with mitochondrial markers.

TL;DR: It is revealed that nanomolar concentrations of amyloid β-peptide increased inositol-1,4,5-triphosphate receptor and voltage-dependent anion channel protein expression and elevated the number of ER–mitochondria contact points and mitochondrial calcium concentrations.

TL;DR: The interaction of signal peptides with Hsp70 during the import process is supported by biochemical and bioinformatic studies.

TL;DR: The human PreP homologue, hPreP, is identified and characterized, and its capacity to degrade the amyloid β-protein (Aβ) in brain mitochondria is shown, and Molecular modeling of h presequence peptidase allowed us to identify Cys90 and Cys527 that form disulfide bridges under oxidized conditions and might be involved in redox regulation of the enzyme.

TL;DR: The findings reveal a general mechanism by which Aβ peptide can induce the multiple diverse mitochondrial dysfunctions accompanying Alzheimer's disease.