TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD

@inproceedings{Chou2017TDP43PD,
  title={TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD},
  author={Ching-Chieh Chou and Yi Zhang and Mfon E Umoh and Spencer W Vaughan and Ileana Lorenzini and Feilin Liu and Melissa Sayegh and Paul Gregory Donlin-Asp and Yu Chen and Duc M Duong and Nicholas T Seyfried and Maureen A. Powers and Thomas L Kukar and Chadwick M. Hales and Marla Gearing and Nigel J. Cairns and Kevin B. Boylan and Dennis W. Dickson and Rosa Rademakers and Yong-Jie Zhang and Leonard Petrucelli and Rita R Sattler and Daniela C. Zarnescu and Jonathan D. Glass and Wilfried Rossoll},
  booktitle={Nature Neuroscience},
  year={2017}
}
The cytoplasmic mislocalization and aggregation of TAR DNA-binding protein-43 (TDP-43) is a common histopathological hallmark of the amyotrophic lateral sclerosis and frontotemporal dementia disease spectrum (ALS/FTD). However, the composition of aggregates and their contribution to the disease process remain unknown. Here we used proximity-dependent biotin identification (BioID) to interrogate the interactome of detergent-insoluble TDP-43 aggregates and found them enriched for components of… CONTINUE READING
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