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• W2989505896 abstract "The RNA-binding proteins TDP-43 and FUS are tied as the third leading known genetic cause for amyotrophic lateral sclerosis (ALS), and TDP-43 proteopathies are found in nearly all ALS patients. Both the natural function and contribution to pathology for TDP-43 remain unclear. The intersection of functions between TDP-43 and FUS can focus attention for those natural functions mostly likely to be relevant to disease. Here, we compare the role played by TDP-43 and FUS, maintaining chromatin stability for dividing HEK293T cells. We also determine and compare the interactomes of TDP-43 and FUS, quantitating changes in those before and after DNA damage. Finally, selected interactions with known importance to DNA damage repair were validated by co-immunoprecipitation assays. This study uncovered TDP-43 and FUS binding to several factors important to DNA repair mechanisms that can be replication-dependent, -independent, or both. These results provide further evidence that TDP-43 has an important role in DNA stability and provide new ways that TDP-43 can bind to the machinery that guards DNA integrity in cells." @default.
• W2989505896 created "2019-11-22" @default.
• W2989505896 creator A5026360375 @default.
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• W2989505896 date "2019-11-06" @default.
• W2989505896 modified "2023-10-10" @default.
• W2989505896 title "Changes to the TDP-43 and FUS Interactomes Induced by DNA Damage" @default.
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• W2989505896 doi "https://doi.org/10.1021/acs.jproteome.9b00575" @default.
• W2989505896 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6947635" @default.
• W2989505896 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31693373" @default.
• W2989505896 hasPublicationYear "2019" @default.
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