Inhibition of Amyloid β-Induced Lipid Membrane Permeation and Amyloid β Aggregation by K162
ACS Chem. Neurosci; doi.org/10.1021/acschemneuro.0c00754
Pseudopeptide Amyloid Aggregation Inhibitors: In Silico, Single Molecule and Cell Viability Studies
International Journal of Molecular Science; doi.org/10.3390/ijms22031051
Plasma metabolomics of presymptomatic PSEN1-H163Y mutation carriers: a pilot study
Annals of Clinical and Translational Neurology; https://doi.org/10.1002/acn3.51296
Retinal ganglion cell loss and gliosis in the retinofugal projection following intravitreal exposure to amyloid-beta
ScienceDirect; https://doi.org/10.1016/j.nbd.2020.105146
Quantitative Measurement of Cerebrospinal Fluid Amyloid-β Species by Mass Spectrometry
Journal of Alzheimer’s Disease; doi: 10.3233/JAD-200987
Quantification of Amyloid-β in Plasma by Simple and Highly Sensitive Immunoaffinity Enrichment and LC-MS/MS Assay
The Journal of Applied Laboratory Medicine; https://doi.org/10.1093/jalm/jfaa225
Changes in the brain transcriptome after DNA Aβ42 trimer immunization in a 3xTg-AD mouse model
ScienceDirect; doi.org/10.1016/j.nbd.2020.105221
Correlation of pyroglutamate amyloid β and ptau Ser202/Thr205 levels in Alzheimer’s disease and related murine models.
PLOS ONE; doi.org/10.1371/journal.pone.0235543.
The monomers, oligomers, and fibrils of amyloid-β inhibit the activity of mitoBKCa channels by a membrane-mediated mechanism.
Biochimica et Biophysica Acta (BBA); Biomembranes; doi.org/10.1016/j.bbamem.2020.183337..
Copper(II) partially protects three histidine residues and the N‐terminus of amyloid‐β peptide from diethyl pyrocarbonate (DEPC) modification ..
FEBSPRESS; doi.org/10.1002/2211-5463.12857.