Histone H1 Favors Folding and Parallel Fibrillar Aggregation of the 1–42 Amyloid-β Peptide.
ACS Publications; DOI: 10.1021/la504089g.
Comparative Pathobiology of Aβ and the Unique Susceptibility of Humans to Alzheimer’s Disease.
Neurobiology of Aging; DOI: http://dx.doi.org/10.1016/j.neurobiolaging.2016.04.019.
Complex System Assembly Underlies a Two-Tiered Model of Highly Delocalized Electrons.
ACS Publications; DOI: 10.1021/acs.jpclett.6b00699.
A novel nicotinic mechanism underlies β-amyloid-induced neurotoxicity.
Science Direct; doi:10.1016/j.neuropharm.2015.04.025.
The Ca2+ channel inhibitor 2-APB reverses β-amyloid-induced LTP deficit in hippocampus by blocking BAX and caspase-3 hyperactivation.
British Journal of Pharmacology; DOI: 10.1111/bph.13048.
Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.
The Journal of Physical Chemistry; DOI: 10.1021/acs.jpclett.5b00918.
In vitro fibrillization of Alzheimer’s amyloid-β peptide (1-42).
AIP Advances; https://doi.org/10.1063/1.4921071.
Development of fluorescent probes that bind and stain amyloid plaques in Alzheimer’s disease.
Springer Link; DOI 10.1007/s12272-015-0617-4.
Amyloid Properties of the Mouse Egg Zona Pellucida.
PLOS One; doi: 10.1371/journal.pone.0129907.
Bioenergetic mechanisms in astrocytes may contribute to amyloid plaque deposition and toxicity.
The Journal of Biological Chemistry; doi: 10.1074/jbc.M114.618157.