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.
In vitro fibrillization of Alzheimer’s amyloid-β peptide (1-42)
AIP Advances; https://doi.org/10.1063/1.4921071.
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.
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
Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid β peptides
Physical Chemistry Chemical Physics; DOI: 10.1039/C5CP03343H.