However, the mechanism by which TDP-43 mutations lead to neurodegeneration is unclear.

Results: We identified multiple phosphorylation sites in carboxyl-terminal regions of deposited TDP-43.

This is consistent with new emerging ideas about TDP-43 functions in dendrites.

We recently identified TDP-43 as the major pathological protein in sporadic ALS.

Moreover, enforced repression of cryptic exons prevented cell death in TDP-43-deficient cells.

Previous studies reported that abnormal phosphorylation takes place in deposited TDP-43.

However, no prior studies have investigated the interactions between TDP-43 oligomers and tau.

TDP-43 inclusions were found in each region of all the cases.

Interestingly, patients with TdP exhibit more bradycardia as such with VT.

We found no associations between atherosclerosis ratings and a-synuclein or TDP-43 lesion ratings.

How increased and disease-causing mutant forms of TDP-43 induce cell death remains unclear.

Accumulation of TDP-43 is associated with neuronal death in the brain.

The TdP events are not concentrated in the first week.

Autopsy in three family members showed a consistent and unique subtype of FTLD-TDP pathology.

These findings may have important implications for accumulated or mutant TDP-43 induced neurodegenerative diseases.

Pathological TDP-43 was present only rarely in the CO group.