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
Time dynamics of photothermal vs optoacoustic response in mid IR nanoscale biospectroscopy
Cornell University Library; http://arxiv.org/abs/1509.00726v1.
Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid β peptides
Physical Chemistry Chemical Physics; DOI: 10.1039/C5CP03343H.
Prostaglandin signaling suppresses beneficial microglial function in Alzheimer’s disease models.
The Journal of Clinical Investigation; doi:10.1172/JCI77487.
In Silico and in Vitro Study of Binding Affinity of Tripeptides to Amyloid β Fibrils: Implications for Alzheimer’s Disease.
The Journal of Physical Chemistry; DOI: 10.1021/acs.jpcb.5b00006.
Endogenous Docosahexaenoic Acid (DHA) Prevents Aβ1–42 Oligomer-Induced Neuronal Injury
Molecular Neurobiology; DOI:10.1007/s12035-015-9224-0.