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Cold Spring Harbor Perspectives in Biology|November 13, 2016
Cross-β Polymerization of Low Complexity Sequence DomainsMasato Kato, Steven L McKnightProceedings of the National Academy of Sciences of the United States of America|October 16, 2021
The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β coresMasato Kato, Steven L McKnightAnnual Review of Biochemistry|December 2, 2017
A Solid-State Conceptualization of Information Transfer from Gene to Message to ProteinMasato Kato, Steven L McKnightRNA (New York, N.Y.)|October 21, 2021
How do protein domains of low sequence complexity work?Masato Kato, Xiaoming Zhou, Steven L McKnightMethods (San Diego, Calif.)|June 19, 2017
Cross-β polymerization and hydrogel formation by low-complexity sequence proteinsMasato Kato, Yi Lin, Steven L McKnightCurrent Opinion in Cell Biology|October 23, 2023
How do disordered head domains assist in the assembly of intermediate filaments?Xiaoming Zhou, Masato Kato, Steven L McKnightCurrent Opinion in Genetics & Development|January 17, 2021
Redox-mediated regulation of low complexity domain self-associationMasato Kato, Benjamin P Tu, Steven L McKnightProceedings of the National Academy of Sciences of the United States of America|October 4, 2018
Structural characterization of the D290V mutation site in hnRNPA2 low-complexity-domain polymersDylan T Murray, Xiaoming Zhou, Masato Kato, et al.Biorxiv : the Preprint Server for Biology|September 11, 2023
Oxidative regulation of TDP-43 self-association by a β-to-α conformational switchJinge Gu, Xiaoming Zhou, Lillian Sutherland, et al.Proceedings of the National Academy of Sciences of the United States of America|September 10, 2020
Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filamentsVasiliy O Sysoev, Masato Kato, Lillian Sutherland, et al.Pageof 23