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• W4317715915 abstract "Abstract Transactive response element DNA/RNA-binding protein 43 kDa (TDP-43) is the causative protein of amyotrophic lateral sclerosis (ALS); several ALS-associated mutants of TDP-43 have been identified. TDP-43 has several domains: an N-terminal domain, two RNA/DNA-recognition motifs, and a C-terminal intrinsically disordered region (IDR). Its structures have been partially determined, but the whole structure remains elusive. In this study, we investigate the possible end-to-end distance between the N- and C-termini of TDP-43, its alterations due to ALS-associated mutations in the IDR, and its apparent molecular shape in live cells using Förster resonance energy transfer (FRET) and fluorescence correlation spectroscopy (FCS). Further-more, the interaction between ALS-associated TDP-43 and heteronuclear ribonucleoprotein A1 (hnRNP A1) is slightly stronger than that of wild-type TDP-43. Our findings provide insights into the structure of wild-type and ALS-associated mutants of TDP-43 in a cell." @default.
• W4317715915 created "2023-01-23" @default.
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• W4317715915 date "2023-01-22" @default.
• W4317715915 modified "2023-10-17" @default.
• W4317715915 title "Intracellular conformation of amyotrophic lateral sclerosis-causative TDP-43" @default.
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• W4317715915 doi "https://doi.org/10.1101/2023.01.22.525050" @default.
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