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In vitro TDP-43 amyloid fibrils


ABSTRACT:

SUBMITTER: Matthias Schmidt 

PROVIDER: EMPIAR-11745 | biostudies-other |

REPOSITORIES: biostudies-other

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Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils.

Sharma Kartikay K   Stockert Fabian F   Shenoy Jayakrishna J   Berbon Mélanie M   Abdul-Shukkoor Muhammed Bilal MB   Habenstein Birgit B   Loquet Antoine A   Schmidt Matthias M   Fändrich Marcus M  

Nature communications 20240112 1


The transactive response DNA-binding protein-43 (TDP-43) is a multi-facet protein involved in phase separation, RNA-binding, and alternative splicing. In the context of neurodegenerative diseases, abnormal aggregation of TDP-43 has been linked to amyotrophic lateral sclerosis and frontotemporal lobar degeneration through the aggregation of its C-terminal domain. Here, we report a cryo-electron microscopy (cryo-EM)-based structural characterization of TDP-43 fibrils obtained from the full-length  ...[more]

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