Folding and Misfolding of Amyloid-β40 and 42 in Alzheimer’s Disease.
Biophysics and Biochemistry of Protein Aggregation; https://doi.org/10.1142/9789813202382_0007.
Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer's Aβ peptide.
Nanomedicine: Nanotechnology, Biology and Medicine; https://doi.org/10.1016/j.nano.2016.10.006.
P2X receptor overexpression induced by soluble oligomers of amyloid beta peptide potentiates synaptic failure and neuronal dyshomeostasis in cellular models of Alzheimer's disease.
Europe PMC; doi: 10.1016/j.neuropharm.2017.10.027.
Structure-activity relationships for flavone interactions with amyloid β reveal a novel anti-aggregatory and neuroprotective effect of 2′,3′,4′-trihydroxyflavone (2-D08).
Science Direct Bioorganic & Medicinal Chemistry; https://doi.org/10.1016/j.bmc.2017.05.041.
Multifunctional Effect of Human Serum Albumin Reduces Alzheimer’s Disease Related Pathologies in the 3xTg Mouse Model.
Journal of Alzheimer’s Disease; doi: 10.3233/JAD-150694..
Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps.
J Vis Exp.; doi: 10.3791/54215.
Fullerenol C60(OH)16 prevents amyloid fibrillization of Aβ40 – in vitro and in silico approach.
Phys Chem Chem Phys; doi: 10.1039/c6cp00901h.
Amyloid β oligomers elicit mitochondrial transport defects and fragmentation in a time-dependent and pathway-specific manner
Molecular Brain; DOI: 10.1186/s13041-016-0261-z.
Inhibition of Aβ42 oligomerization in yeast by a PICALM ortholog and certain FDA approved drugs
Microbial Cell; doi: 10.15698/mic2016.02.476.
Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.
Scientific Reports; https://doi.org/10.1038/srep39374.