Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
oleh: Tariq Afroz, Eva-Maria Hock, Patrick Ernst, Chiara Foglieni, Melanie Jambeau, Larissa A. B. Gilhespy, Florent Laferriere, Zuzanna Maniecka, Andreas Plückthun, Peer Mittl, Paolo Paganetti, Frédéric H. T. Allain, Magdalini Polymenidou
| Format: | Article |
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| Diterbitkan: | Nature Portfolio 2017-06-01 |
Deskripsi
TDP-43 aggregation is observed in amyotrophic lateral sclerosis. Here the authors combine X-ray crystallography, nuclear magnetic resonance and electron microscopy studies and show that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dynamic oligomers antagonizing pathologic aggregation.