Article

Enhanced in vitro aggregation, but not phase separation, of TDP-43 and its C-terminal fragments generate deep-blue autofluorescence

2024-11-24

Abstract excerpt

As misfolding and aggregation of the RNA/DNA-binding protein, TDP-43, are linked to devastating TDP-43 proteinopathies like amyotrophic lateral sclerosis (ALS), distinction of the nature of the aggregated TDP-43 species being liquid-like non-pathogenic or solid-like pathogenic is important for mechanistic elucidation and therapeutic targeting. Here, we examined if in vitro enhancement of the TDP-43 aggregation ca...

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Literature Corpus work: f85fd204-401a-5656-8609-b16fbe7d0f84
DOI: 10.1101/2024.11.23.624964

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Enhanced in vitro aggregation, but not phase separation, of TDP-43 and its C-terminal fragments generate deep-blue autofluorescenceDOI 10.1101/2024.11.23.624964Read

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Enhanced <i>in vitro</i> aggregation, but not phase separation, of TDP-43 and its C-terminal fragments generate deep-blue autofluorescence

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