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• W3091863785 abstract "Accumulation of ubiquitin-positive, tau- and α-synuclein-negative intracellular inclusions of TDP-43 in the central nervous system represents the major hallmark correlated to amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U). Such inclusions have variably been described as amorphous aggregates or more structured deposits having amyloid properties. Here we have purified full-length TDP-43 (FL TDP-43) and its C-terminal domain (Ct TDP-43) to investigate the morphological, structural and tinctorial features of aggregates formed in vitro by them at pH 7.4 and 37 °C. AFM images indicate that both protein variants show a tendency to form filaments. Moreover, we show that both FL TDP-43 and Ct TDP-43 filaments possess a largely disordered secondary structure, as ascertained by far-UV circular dichroism and Fourier transform infra-red spectroscopy, do not bind Congo red and induce a very weak increase of thioflavin T fluorescence, indicating the absence of a clear amyloid-like signature." @default.
• W3091863785 created "2020-10-15" @default.
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• W3091863785 date "2020-10-07" @default.
• W3091863785 modified "2023-09-26" @default.
• W3091863785 title "Full-length TDP-43 and its C-terminal domain form filaments <i>in vitro</i> having non-amyloid properties" @default.
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• W3091863785 doi "https://doi.org/10.1080/13506129.2020.1826425" @default.
• W3091863785 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33026249" @default.
• W3091863785 hasPublicationYear "2020" @default.
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