B01-3 明石 知子（横浜市立大学大学院 生命医科学研究科）

B01-3 明石 知子（横浜市立大学大学院 生命医科学研究科）

  1. R. Tamura, R. Oi, S. Akashi, M. K. Kaneko, Y. Kato, T. Nogi: “Application of the NZ-1 Fab as a Crystallization Chaperone for PA Tag-inserted Target Proteins” Protein Sci. 28, 823-836 (2019) DOI: https://doi.org/10.1002/pro.3580
  2. K. Saikusa, D. Kato, A. Nagadoi, H. Kurumizaka, S. Akashi: “Native Mass Spectrometry of Protein and DNA Complexes Prepared in Non-volatile Buffers.” J. Am. Soc. Mass Spectrom. 31, 711-718 (2020) DOI: https://doi.org/10.1021/jasms.9b00145
  3. K. Takano, S. Arai, S. Sakamoto, H. Ushijima, T. Ikegami, K. Saikusa, T. Konuma, I. Hamachi, S. Akashi: “Screening of Protein-ligand Interactions under Crude Conditions by Native Mass Spectrometry” Anal. Bioanal. Chem. 412, 4037-4043 (2020) DOI: https://doi.org/10.1007/s00216-020-02649-x
  4. B. Mylemans, I. Laier, K. Kamata, S. Akashi, H. Noguchi, J. R. H. Tame, A. R. D. Voet: “Structural Plasticity of a Designer Protein Sheds Light on β-propeller Protein Evolution” FEBS J. 288, 530-545 (2021) DOI: https://doi.org/10.1111/febs.15347
  5. K. Saikusa, H. Hidaka, S. Izumi, S. Akashi: “Mass Spectrometric Characterization of Histone H3 Isolated from in vitro Reconstituted and Acetylated Nucleosome Core Particle” Mass Spectrom (Tokyo) 9, A0090 (2020) DOI: https://doi.org/10.5702/massspectrometry.A0090
  6. W. Sakamoto, N. Azegami, T. Konuma, S. Akashi: “Single-Cell Native Mass Spectrometry of Human Erythrocytes” Anal. Chem. 93, 6583-6588 (2021) DOI: https://doi.org/10.1021/acs.analchem.1c00588
  7. 【領域内連携】M. Tajiri, H. Aoki, A. Shintani, K. Sue, S. Akashi, Y. Furukawa: “Metal Distribution in Cu/Zn-superoxide Dismutase Revealed by Native Mass Spectrometry” Free Radic. Biol. Med., 183, 60-68 (2022) DOI: https://doi.org/10.1016/j.freeradbiomed.2022.03.014
  8. Y. Imaizumi, K. Takanuki, T. Miyake, M.  Takemoto, K. Hirata, M. Hirose, R. Oi, T. Kobayashi, K. Miyoshi, R. Aruga, T. Yokoyama, S. Katagiri, H. Matsuura, K. Iwasaki, T. Kato, M. K. Kaneko, Y. Kato, M. Tajiri, S. Akashi, O. Nureki, Y. Hizukuri, Y. Akiyama, *T. Nogi: “Mechanistic Insights into Intramembrane Proteolysis by E. coli Site-2 Protease Homolog RseP.” Sci Adv. 8, eabp9011 (2022) DOI: https://doi.org/10.1126/sciadv.abp9011
  9. T. Tanaka, T. Ekimoto, M. Nagatomo, M. Neyazaki, E. Shimoji, T. Yamane, S. Kanagawa, R. Oi, E. Mihara, J. Takagi, S. Akashi, M. Ikeguchi, T. Nogi: “Hybrid in vitro/in silico Analysis of Low-affinity Protein-protein Interactions That Regulate Signal Transduction by Sema6D” Protein Sci. 31, e4452 (2022) DOI: https://doi.org/10.1002/pro.4452
  10. N. Azegami, R. Taguchi, N. Suzuki, Y. Sakata, T. Konuma, S. Akashi: “Native Mass Spectrometry of BRD4 Bromodomains Linked to a Long Disordered Region” Mass Spectrom. (Tokyo) A0110 (2022) DOI: https://doi.org/10.5702/massspectrometry.A0110
  11. M. Tajiri, S. Imai, T. Konuma, K. Shimamoto, I. Shimada, S. Akashi: “Evaluation of Drug Responses to Human β2AR Using Native Mass Spectrometry.” ACS Omega, 8, 24544-24551 (2023) DOI: https://doi.org/10.1021/acsomega.3c02737
  12. N. Ishimoto, J.-H. Park, K. Kawakami, M. Tajiri, K. Mizutani, S. Akashi, J. R. H. Tame, A. Inoue, S.-Y. Park: “Structural Basis of Chemokine Receptor 1 Ligand Binding and Activation.” Nat. Commun., 14, 4107 (2023) DOI: https://doi.org/10.1038/s41467-023-39799-2
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