Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses | Nature Communications
Interactions between Amyloid-β and Tau Fragments Promote Aberrant Aggregates: Implications for Amyloid Toxicity | The Journal of Physical Chemistry B
Exosomes and microRNAs: New potential therapeutic candidates in Alzheimer disease therapy - Iranifar - 2019 - Journal of Cellular Physiology - Wiley Online Library
Deeply conserved synteny and the evolution of metazoan chromosomes | Science Advances
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Frontiers | Epigenetics in Alzheimer's Disease
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A combinatorial native MS and LC-MS/MS approach reveals high intrinsic phosphorylation of human Tau but minimal levels of other key modifications - Journal of Biological Chemistry
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Amyloid β-Protein and the Genetics of Alzheimer's Disease* - Journal of Biological Chemistry
