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研究業績

  1. Nagahata, N., Kato, K., Yamada, S., Kannan, S., Okazaki, S., Isayama, Y., Hiraizumi, M., Yamashita, K., Koonin, E.V., Zhang, F., et al. (2026)
    Structural visualization of the molecular evolution of CRISPR-Cas9.
    Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-025-01743-x.
  2. Hsu, T., Wang, X., Isayama, Y., Jung, V., Zhang, J., van Gompel, E., Maadadi, H., Torres, C., Shimazaki-Takahashi, A., Kurihara, N… Kato, K. and Hur, S. (2026).
    MDA5 multimerization on LINE RNA drives pathogenic extracellular immune complexes in autoimmunity.
    bioRxiv, 2026.01.27.702129. https://doi.org/10.64898/2026.01.27.702129.
  3. Kurihara N, Isayama Y, Zhang J, Yamashita T, Awaji K, Ito Y, Yoshizaki A, Kouwaki T, Oshiumi H, Nishimasu H, Shibata M, Nureki O, and Kato, K. (2026)
    Molecular mechanism of MDA5 nucleation and filament formation by LGP2
    Molecular Cell, 10.1016/j.molcel.2025.12.019.
  4. Kanayama, D., Terasaka, N., Kato, K., Okazaki, S., and Suga, H. (2025). A nonviral Neo-nucleocapsid for cell-specific RNA delivery developed by pseudo-cyclic peptide grafting and directed evolution.
    Angew. Chem. Int. Ed Engl., e19027 (2025). 10.1002/anie.202519027
  5. Ishikawa, J., Kato, K., Kannan, S., Okazaki, S., Ishiguro, S., Yamashita, K., Yachie, N., Nishizawa, T., Zhang, F., and Nishimasu, H. (2025). Structural insights into RNA-guided RNA editing by the Cas13b-ADAR2 complex.
    Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-025-01529-1.
  6. Teranishi-Ikawa, Y., Soeda, T., Koga, H., Yamaguchi, K., Kato, K., Esaki, K., Asanuma, K., Funaki, M., Ichiki, M., Ikuta, Y., et al. (2023).
    A bispecific antibody NXT007 exerts a hemostatic activity in hemophilia A monkeys enough to keep a non-hemophiliac state.
    J. Thromb. Haemost. 10.1016/j.jtha.2023.09.034.
  7. Jiang, K., Lim, J., Sgrizzi, S., Trinh, M., Kayabolen, A., Yutin, N., Bao, W., Kato, K., Koonin, E.V., Gootenberg, J.S., et al. (2023).
    Programmable RNA-guided DNA endonucleases are widespread in eukaryotes and their viruses.
    Sci Adv 9, eadk0171. 10.1126/sciadv.adk0171.
  8. Kato, K., Okazaki, S., Schmitt-Ulms, C., Jiang, K., Zhou, W., Ishikawa, J., Isayama, Y., Adachi, S., Nishizawa, T., Makarova, K.S., et al. (2022).
    RNA-triggered protein cleavage and cell growth arrest by the type III-E CRISPR nuclease-protease.
    Science 378, 882–889. 10.1126/science.add7347.
  9. Kato, K., Okazaki, S., Kannan, S., Altae-Tran, H., Esra Demircioglu, F., Isayama, Y., Ishikawa, J., Fukuda, M., Macrae, R.K., Nishizawa, T., et al. (2022).
    Structure of the IscB–ωRNA ribonucleoprotein complex, the likely ancestor of CRISPR-Cas9.
    Nat. Commun. 13, 1–10. 10.1038/s41467-022-34378-3.
  10. Kato, K., Zhou, W., Okazaki, S., Isayama, Y., Nishizawa, T., Gootenberg, J.S., Abudayyeh, O.O., and Nishimasu, H. (2022).
    Structure and engineering of the type III-E CRISPR-Cas7-11 effector complex.
    Cell 185, 2324–2337.e16. 10.1016/j.cell.2022.05.003.
  11. Kato, K., Ahmad, S., Zhu, Z., Young, J.M., Mu, X., Park, S., Malik, H.S., and Hur, S. (2021).
    Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases.
    Mol. Cell 81, 599–613.e8. 10.1016/j.molcel.2020.11.047.
  12. Kato, K., Nishimasu, H., Oikawa, D., Hirano, S., Hirano, H., Kasuya, G., Ishitani, R., Tokunaga, F., and Nureki, O. (2018).
    Structural insights into cGAMP degradation by Ecto-nucleotide pyrophosphatase phosphodiesterase 1.
    Nat. Commun. 9, 4424. 10.1038/s41467-018-06922-7.
  13. Kato, K., Omura, H., Ishitani, R., and Nureki, O. (2017).
    Cyclic GMP-AMP as an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA.
    Annu. Rev. Biochem. 86, 541–566. 10.1146/annurev-biochem-061516-044813.
  14. Palazzo, L., Daniels, C.M., Nettleship, J.E., Rahman, N., McPherson, R.L., Ong, S.-E., Kato, K., Nureki, O., Leung, A.K.L., and Ahel, I. (2016).
    ENPP1 processes protein ADP-ribosylation in vitro.
    FEBS J. 283, 3371–3388. 10.1111/febs.13811.
  15. Kato, K.Palazzo, L., Daniels, C.M., Nettleship, J.E., Rahman, N., McPherson, R.L., Ong, S.-E., Kato, K., Nureki, O., Leung, A.K.L., and Ahel, I. (2016).
    ENPP1 processes protein ADP-ribosylation in vitro.
    FEBS J. 283, 3371–3388. 10.1111/febs.13811.
  16. Morita, J., Kato, K., Nakane, T., Kondo, Y., Fukuda, H., Nishimasu, H., Ishitani, R., and Nureki, O. (2016).
    Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide.
    Nat. Commun. 7, 12383. 10.1038/ncomms12383.
  17. Kato, K., Satouh, Y., Nishimasu, H., Kurabayashi, A., Morita, J., Fujihara, Y., Oji, A., Ishitani, R., Ikawa, M., and Nureki, O. (2016).
    Structural and functional insights into IZUMO1 recognition by JUNO in mammalian fertilization.
    Nat. Commun. 7, 12198. 10.1038/ncomms12198.
  18. Kato, K., Ikeda, H., Miyakawa, S., Futakawa, S., Nonaka, Y., Fujiwara, M., Okudaira, S., Kano, K., Aoki, J., Morita, J., et al. (2016).
    Structural basis for specific inhibition of Autotaxin by a DNA aptamer.
    Nat. Struct. Mol. Biol. 23, 395–401. 10.1038/nsmb.3200.
  19. Morita, J., Kano, K., Kato, K., Takita, H., Sakagami, H., Yamamoto, Y., Mihara, E., Ueda, H., Sato, T., Tokuyama, H., et al. (2016).
    Structure and biological function of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase.
    Sci. Rep. 6, 20995. 10.1038/srep20995.
  20. Kato, K., Ishii, R., Hirano, S., Ishitani, R., and Nureki, O. (2015).
    Structural Basis for the Catalytic Mechanism of DncV, Bacterial Homolog of Cyclic GMP-AMP Synthase.
    Structure 23, 843–850. 10.1016/j.str.2015.01.023.
  21. Morita, J., Kato, K., Mihara, E., Ishitani, R., Takagi, J., Nishimasu, H., Aoki, J., and Nureki, O. (2014).
    Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6.
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 70, 794–799. 10.1107/S2053230X14008929.
  22. Kato, K., Ishii, R., Goto, E., Ishitani, R., Tokunaga, F., and Nureki, O. (2013).
    Structural and functional analyses of DNA-sensing and immune activation by human cGAS.
    PLoS One 8, e76983. 10.1371/journal.pone.0076983.
  23. Kato, K., Nishimasu, H., Okudaira, S., Mihara, E., Ishitani, R., Takagi, J., Aoki, J., and Nureki, O. (2012).
    Crystal structure of Enpp1, an extracellular glycoprotein involved in bone mineralization and insulin signaling.
    Proc. Natl. Acad. Sci. U. S. A.
    109, 16876–16881. 10.1073/pnas.1208017109.
  24. Kato, K., Nishimasu, H., Mihara, E., Ishitani, R., Takagi, J., Aoki, J., and Nureki, O. (2012).
    Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp1. Acta Crystallogr.
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
    68, 778–782. 10.1107/S1744309112019306.

東京科学大学 総合研究院

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Mechanistic Immunology Research Unit

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