Masato Hosokawa (former Chief Researcher of Tokyo Metropolitan Institute of Medical Science (TMIMS), Faculty of Pharmaceutical Science, Fukuoka University), Masami Masuda-Suzukake, Hiroshi Shitara, ...

Tauopathies are classified by which tau isoform forms fibrils—those with three microtubule-binding domain repeats (3R), those with four (4R), or those with both. What drives one isoform to aggregate ...

A research team at the University of Cologne has made a significant breakthrough in understanding the role of the tau protein in Alzheimer's disease. Using human induced pluripotent stem cells (iPSCs) ...

Our proteome is much bigger than our genome because one gene produces several variants of proteins called protein isoforms, whose disbalance is implicated in many diseases. A new bioengineered ...

Innovative new research has revealed that the activity of different versions of genes expressed in the brain is associated with the accumulation of the protein tau, which is a hallmark of Alzheimer's ...

Fused in sarcoma (FUS) and its binding partner proline- and glutamine-rich (SFPQ) regulates Mapt splicing, resulting balanced ratio of tau isoforms. Loss of interaction between FUS and SFPQ alters ...

Tauopathies are a group of neurodegenerative diseases associated with aggregated tau proteins. These diseases typically progress over the years, and their symptoms are linked to neurological ...

The specific tau isoforms, such as 3-repeat (3R) and 4-repeat (4R) isoforms, and the distinct conformational strains that misfolded tau can adopt are determinants of the molecular and clinical ...

Evidence continues to build for how well phospho-tau species in the cerebrospinal fluid or blood detect amyloid plaques, neurofibrillary tangles, and even neurodegeneration. The latest, from ...

The increasing knowledge on how protein tau is organized in live cells has shown that the protein forms nanometer-sized hotspots which are different from tau microtubules. These hotspots, essential ...