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Dong et al. Neuroimmunol Neuroinflammation 2018;5:5 I http://dx.doi.org/10.20517/2347-8659.2017.47 Page 9 of 10

phosphorylation and ubiquitination of TDP-43 have been identified and recognized to be the source of
pathological protein aggregation, inclusion bodies formation and abnormal exosome secretion. Similar
to prion propagation and autophagy, these findings may help understand the relationship between
ubiquitinated TDP-43 and ALS pathogenesis. More research is needed on the metabolic pathways of
neurotoxic TDP-43 fragments.

DECLARATIONS
Authors’ contributions
Designed this study: Dong Y, Chen Y
Participated in material review and draft the manuscript: Dong Y
Revised the manuscript: Chen Y

Financial support and sponsorship
None.

Conflicts of interest
There are no conflicts of interest.

Patient consent
Not applicable.

Ethics approval
Not applicable.

Copyright
© The Author(s) 2018.

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