Dr Scotter and Dr Swanson from the University of Auckland in collaboration with researchers at the University of Queensland have published a paper on everything you ever wanted to know about TDP-43 in ALS/MND/FTD.
Topics explored include:
- How the pathogenic changes to TDP-43, drive disease-associated aggregation in TDP-43 proteinopathies.
- How pathological TDP-43 species are formed and contribute to cellular dysfunction and toxicity, via both loss-of-function and gain-of-function mechanisms.
- The role of protein homeostasis mechanisms, in combating TDP-43 aggregation and discuss how their dysfunction likely promotes disease pathogenesis and progression.
- Evaluation of pre-clinical studies aimed at enhancing TDP-43 protein clearance via these mechanisms and provide insight on promising strategies for future therapeutic advances.
Click here to read the full paper TDP-43 pathology: From noxious assembly to therapeutic removal
