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• W3120283587 abstract "Eukaryotic cells express thousands of protein domains long believed to function in the absence of molecular order. These intrinsically disordered protein (IDP) domains are typified by gibberish-like repeats of only a limited number of amino acids that we refer to as domains of low sequence complexity. A decade ago, it was observed that these low complexity (LC) domains can undergo phase transition out of aqueous solution to form either liquid-like droplets or hydrogels. The self-associative interactions responsible for phase transition involve the formation of specific cross-β structures that are unusual in being labile to dissociation. Here we give evidence that the LC domains of two RNA binding proteins, ataxin-2 and TDP43, form cross-β interactions that specify biologically relevant redox sensors." @default.
• W3120283587 created "2021-01-18" @default.
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• W3120283587 date "2021-04-01" @default.
• W3120283587 modified "2023-10-17" @default.
• W3120283587 title "Redox-mediated regulation of low complexity domain self-association" @default.
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• W3120283587 doi "https://doi.org/10.1016/j.gde.2020.12.006" @default.
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