Mariana A. Hartshorn

TL;DR: It is shown that human A beta directly produces hydrogen peroxide (H2O2) by a mechanism that involves the reduction of metal ions, Fe(III) or Cu(II), setting up conditions for Fenton-type chemistry.

TL;DR: Results indicate that H+-induced conformational changes unmask a metal-binding site on Aβ that mediates reversible assembly of the peptide that explains the recently reported enrichment of these metal ions in amyloid plaques in Alzheimer's disease.

TL;DR: It is reported that Cu(II) markedly potentiates the neurotoxicity exhibited by Abeta in cell culture, suggesting that certain redox active metal ions may be important in exacerbating and perhaps facilitating Abeta-mediated oxidative damage in Alzheimer's disease.

TL;DR: Evidence is presented that the zinc-induced precipitation of Aβ is mediated by a peptide dimer and favored by conditions that promote α-helical and diminish β-sheet conformations, suggesting a possible therapeutic strategy for the resolubilization of some forms of A β deposit in the disease.

TL;DR: In vitro evidence that trace levels of zinc, copper, and iron are the actual initiators of the classic Aβ1–42-mediated seeding process and Aβ oligomerization is presented, suggesting that protein self-assembly and oligomers are not spontaneous in this system as previously thought, and that there may be an obligatory role for metal ions in initiating Aβ amyloidosis and oligomerized.