Publications

1. 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.
2. 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.
3. 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.
4. 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.
5. 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.
6. 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.
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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.
13. 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.
14. 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.
15. 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.
16. 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.
17. 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.
18. 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.
19. 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.
    Sect. F Struct. Biol. Cryst. Commun. 68, 778–782. 10.1107/S1744309112019306.