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Advanced filters: Author: Bogachan Tahirbegi Clear advanced filters

The p3 peptides (Aβ_17-40/42) rapidly form amyloid fibrils that cross-seed with full-length Aβ

The p3 peptide, Aβ(17-40/42), rapidly forms amyloid fibrils by secondary nucleation which cross-seeds with full-length Aβ peptide. Furthermore, p3 annular and oligomer structures are cytotoxic, disrupt membrane integrity and form ion-channel pores.

Yao Tian
Andrea P. Torres-Flores
John H. Viles
ResearchOpen Access27 Feb 2025
Nature Communications

Volume: 16, P: 1-13
Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease

Sara Teller
Islam Bogachan Tahirbegi
Jordi Soriano
ResearchOpen Access26 Nov 2015
Scientific Reports

Volume: 5, P: 1-16
The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition

α-Synuclein is a presynaptic protein whose aberrant aggregation is associated with Parkinson’s disease. Here, the authors show how αSynuclein-induced docking of synaptic vesicles is modulated by the lipid composition changes typically observed in neurodegeneration using an in vitro system.

Wing K. Man
Bogachan Tahirbegi
Giuliana Fusco
ResearchOpen Access10 Feb 2021
Nature Communications

Volume: 12, P: 1-10
A Novel Aβ₄₀ Assembly at Physiological Concentration

Bogachan Tahirbegi
Alastair J. Magness
Liming Ying
ResearchOpen Access11 Jun 2020
Scientific Reports

Volume: 10, P: 1-10

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