Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of T...
Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43
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London: Nature Publishing Group UK
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Language
English
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London: Nature Publishing Group UK
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Trans-activation response DNA-binding protein of 43 kDa (TDP-43) regulates RNA processing and forms neuropathological aggregates in patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Investigating TDP-43 post-translational modifications, we discovered that K84 acetylation reduced nuclear import whereas K136 acetylat...
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Full title
Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43
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TN_cdi_doaj_primary_oai_doaj_org_article_5d612ba76c204e148f11afe0e162e337
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_5d612ba76c204e148f11afe0e162e337
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-022-28822-7
