@article{oai:repo.qst.go.jp:00084661,
 author = {Masato, Kato and P Tu, Benjamin and L McKnight, Steven and Masato, Kato},
 journal = {Current Opinion in Genetics & Development},
 month = {Apr},
 note = {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.},
 pages = {111--118},
 title = {Redox-mediated regulation of low complexity domain self-association},
 volume = {67},
 year = {2021}
}