Benjamin M. Petre

TL;DR: It is shown that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloids diseases.

TL;DR: It is shown that a highly bent integrin conformation is physiological and has low affinity for biological ligands.

TL;DR: Two mutations in the alpha-synuclein gene (A30P and A53T) have been linked to autosomal dominant early-onset Parkinson's disease and the formation of pore-like oligomeric structures may explain the membrane permeabilization activity of alpha- synuclein protofibrils.

TL;DR: Biophysical studies revealed that the Arctic mutation accelerates both Abeta oligomerization and fibrillogenesis in vitro and an increase in the ratio of Abeta(WT)/Abeta(MUT(Arctic)), therefore, may result in the accumulation of potential neurotoxic protofibrils and acceleration of disease progression in familial Alzheimer's disease mutation carriers.

TL;DR: It is demonstrated that, in vitro, PA28 can associate with 'singly capped’ 26S (i.e. 19S–20S) proteasomes, and during breakdown of proteins, the complexes containing PA28β or PA28α generated a pattern of peptides different from those generated by 26S proteasome, without altering mean product length.