{"id":1197,"date":"2024-06-12T15:08:54","date_gmt":"2024-06-12T06:08:54","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/yonekura\/?page_id=1197"},"modified":"2026-04-20T14:04:16","modified_gmt":"2026-04-20T05:04:16","slug":"ronbun-en","status":"publish","type":"page","link":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/yonekura\/ronbun-en\/","title":{"rendered":"\u8ad6\u6587\uff08\u82f1\u8a9e\uff09"},"content":{"rendered":"

\u8ad6\u6587\uff08\u82f1\u8a9e\uff09<\/strong><\/span><\/h1>\n

2026<\/strong>\u5e74\u5ea6<\/strong><\/h2>\n
    \n
  1. Baba A, Yokoyama K, Sato K, Asanuma S, Olsson U, Kawabata T, Unabara D<\/strong><\/span>, Hamaguchi T<\/strong><\/span>, Yonekura K<\/strong><\/span>, Imai M,\u00a0<\/span>\u201cGrowth of Fatty Acid Vesicles Coupled with Amino Acid Sequences of Peptides toward Evolvable Protocells\u201d, Communications Chemistry<\/strong><\/em>, in press<\/li>\n
  2. Cai HL, Shimada A, Hamaguchi T<\/strong><\/span>, Mizoguchi A, Yonekura K<\/strong><\/span>, Tsuchiyama K, Shimada M, Ebihara A, Tani K, Nakagawa T \u201cCryo-EM Structures of Alcohol Oxidase Isozymes Reveal Structural Determinants of Cofactor Variation and Enzymatic Activity in Ogataea methanolica<\/em>\u201d, Microbial Biotechnology, 2026\u5e744\u670818\u65e5, doi: 10.1111\/1751-7915.70355<\/a><\/li>\n<\/ol>\n

    2025\u5e74\u5ea6<\/strong><\/h2>\n
      \n
    1. Iwasawa M, <\/span>Miura K<\/span>, Kashihara M<\/span>, Kitagawa H<\/span>, Ohno M<\/span>, Unabara D<\/strong><\/span>,\u00a0Hamaguchi T<\/strong><\/span>, Yonekura K<\/strong><\/span>,\u00a0<\/span>\u201cDirect Visualization and Quantitative Analysis of Silica Nanoparticle Dispersion States in Saline Solution via Cryo-TEM\u201d, ACS Measurement Science Au<\/strong><\/em>, 2026\u5e742\u67084\u65e5, doi:10.1021\/acsmeasuresciau.5c00158<\/a><\/li>\n
    2. Li S, Shounai O, Kato M, Ikeuchi K<\/strong><\/span>, Inada T, \u201cCollision-induced ribosome degradation driven by ribosome competition and translational perturbations\u201d, Nature Communications<\/strong><\/em>, 2025\u5e7412\u670812\u65e5, doi:10.1038\/s41467-025-66026-x<\/a><\/li>\n
    3. Maejima Y, Takabatake A, Takeda SI, Fudouzi H, Kishikawa K, Unabara D<\/strong><\/span>, Hamaguchi T<\/strong><\/span>, Yonekura K<\/strong><\/span>, Kureha T, Mitomo H, Ito K, Osaka K, Kanie K, Kohri M. \u201cVisualization of the Assembly Behaviors of Gel Layer-Coated Melanin Particles at the Air\/Water Interface via Structural Color.\u201d, Langmuir., 2025\u5e7411\u6708doi:10.1021\/acs.langmuir.5c03990<\/a><\/li>\n
    4. Taspika M, Yachi T, Shi X, Unabara D<\/strong><\/span>,\u00a0Hamaguchi T<\/strong><\/span>, Yonekura K<\/strong><\/span>, Yonamine Y, Mitomo H, Ijiro K, “<\/span>Controlled Assembly of Gold Nanodiscs via DNA Hybridization: Tuning Plasmonic Coupling via Interparticle Gap Distance and Multimerization Degree“<\/span>, Langmuir<\/em><\/strong>, 2025\u5e7410\u670817\u65e5, doi:10.1021\/acs.langmuir.5c04270<\/a><\/li>\n
    5. Fukunaga TM, Takaba K, Yoshida S, Maki-Yonekura S, Yonekura K<\/strong><\/span>, Isobe H, “Expanded segments of three-dimensional carbonaceous nets with chirality: Synthesis and structures”, Chemical Science <\/strong><\/em>16,\u00a0 2025\u5e7410\u67088\u65e5, doi:10.1039\/d5sc06999h<\/a><\/span><\/li>\n
    6. Kawakami K,<\/span><\/span> Bandou-Uotani M,<\/span><\/span> Kida M,<\/span><\/span> Kato Y,<\/span><\/span> Hirota Y,<\/span><\/span> Hirose Y,<\/span><\/span> Kosumi D<\/i>,<\/span><\/span> Yonekura K<\/strong><\/span>, “Preparation, structural characterization, and ultrafast energy transfer dynamics of the phycobilisome\u2013photosystem II megacomplex in a thermophilic cyanobacterium”, Plant and Cell Physiology<\/em><\/strong>,\u00a0 2025\u5e749\u670810\u65e5, doi:10.1093\/pcp\/pcaf076<\/a><\/span><\/li>\n
    7. Unabara D<\/strong><\/span>, <\/span>Sato Y.K.<\/strong>, <\/span>Hamaguchi T<\/strong><\/span>, Yonekura K<\/strong><\/span>, “Low-Dose Elemental Mapping of Light Atoms in Liquid-phase Materials Using Cryo-EELS”, Analytical Chemistry<\/strong><\/em>, 2025\u5e747\u670831\u65e5, doi:10.1021\/acs.analchem.5c02121<\/a><\/li>\n
    8. Yachi T, Watanabe H, Niwa R, Unabara D<\/strong><\/span>, Hamaguchi T<\/span><\/strong>, Yonamine Y, Yonekura K<\/strong><\/span>, Ijiro K, Mitomo H, “Versatile Nanoparticle Capsule Formation With Enhanced Encapsulation Efficiency via Solute-Induced Liquid\u2013Liquid Phase Separation”, Small<\/strong><\/em>, 2025\u5e745\u67087\u65e5, doi:10.1002\/smll.202502573<\/a><\/li>\n
    9. Morimoto J, Yokomine M, Shiratori Y, Ueda T, Nakamuro T, Takaba K, Saori Maki-Yonekura, Umezawa K, Miyanishi K, Fukuda Y, Watanabe T, <\/span>Suga M, <\/span>Inayoshi A, <\/span>Yoshida T, <\/span>Mizukami W, <\/span>Takeuchi K, <\/span>Yonekura K<\/strong><\/span>, <\/span>Nakamura E, <\/span>Sando S, <\/span>“Bottom-up design of peptide shapes in water using oligomers of N-methyl-L\/D-alanine”, Chemical Science<\/em><\/strong> 16, 2025\u5e745\u67082\u65e5, doi:10.1039\/d5sc01483b<\/a><\/li>\n<\/ol>\n

      2024\u5e74\u5ea6<\/strong><\/h2>\n
        \n
      1. Toyonaga T<\/strong><\/span>, Kato T, Kawamoto A, Miyata T, Kawakami K, Fujita J, Hamaguchi T<\/strong><\/span>, Namba K, Miyata M, “Dimeric assembly of F1-like ATPase for the gliding motility of Mycoplasma”, Science Advances<\/em><\/strong>, 2025\u5e742\u670826\u65e5, doi:10.1126\/sciadv.adr9319<\/a><\/li>\n
      2. Kurokawa H<\/strong><\/span>, Maki-Yonekura S, Takaba K, Higashino T, Inoue S, Hasegawa A, Yonekura K<\/strong><\/span>, “3D Electron Diffraction Structure of an Organic Semiconductor Reveals Conformational Polymorphism”, Journal of the American Chemical Society<\/em><\/strong>,
        \n2025\u5e742\u67086\u65e5, doi:        https:\/\/doi.org\/10.1021\/jacs.4c12734<\/a><\/li>\n
      3. Sugahara M, Maki-Yonekura S, Inoue I, Takaba K, Narai S, Naitow H, Kang J, Tono K, Numata K, Ishikawa T, Yabashi M,\u00a0 Yonekura K<\/strong><\/span>, “High throughput protein serial crystallography using a grease matrix and a large-area support film”, bioRxiv<\/em><\/strong>, 2025\u5e74\uff11\u670831\u65e5, doi:https:\/\/doi.org\/10.1101\/2025.01.31.635837<\/a><\/li>\n
      4. Kanno A, Tanifuji R, Yoshida S, Sato S, Maki-Yonekura S, Takaba K, Kang J, Tono K, Yonekura K<\/strong><\/span>, Oguri H, “Streamlined modular synthesis of saframycin substructure via copper-catalyzed three-component assembly and gold-promoted 6-endo cyclization”, The Beilstein Journal of Organic Chemistry<\/em><\/strong>, 2025\u5e741\u670828\u65e5, doi:https:\/\/doi.org\/10.3762\/bjoc.21.14<\/a><\/li>\n
      5. Fukasawa Y, Komatsu K, Sato M, Maki-Yonekura S, Kurokawa H<\/strong><\/span>, Yonekura K<\/strong><\/span>, Kobayashi H, “A Graph-based Molecular Structure Identification Method via Feature Extraction for Three-dimensional Electron Diffraction Data”, 2024 Twelfth International Symposium on Computing and Networking Workshops (CANDARW) 325-329,
        \n2024\u5e7411\u670826\u65e5, doi:        https:\/\/ieeexplore.ieee.org\/document\/10817860<\/a><\/li>\n
      6. Hasegawa T, Inoue S, Tsuzuki S, Horiuchi S, Matsui H, Okada T, Kumai R, Yonekura K<\/strong><\/span>, Maki-Yonekura S, “Exploration and development of Molecule-based Printed Electronics Materials: an integrated approach using experimental, computational, and data sciences”, Science and Technology of Advanced Materials<\/em><\/strong><\/a>, 2024\u5e7411\u670813\u65e5, doi:10.1080\/14686996.2024.24<\/a>\u3000\uff08\u62db\u5f85\uff09<\/li>\n
      7. Nikaido K, Inoue S, Tsuzuki S, Kumai R, Matsui H, Takaba K, Maki-Yonekura S, Yonekura K<\/strong><\/span>, Hasegawa T, “Emergence of mixing-induced polymorphic phase with higher mobility in alkylated layered organic semiconductors”, Physical Review Materials<\/em><\/strong>, 2024\u5e7411\u67081\u65e5, doi:https:\/\/doi.org\/10.1103\/physrevmaterials.8.115601<\/a><\/li>\n
      8. Yonekura K<\/strong>,<\/span> “Artificial Intelligence-Driven Data Acquisition for Single-Particle Cryo-EM and Three-Dimensional Electron Diffraction”, Cryo-Electron Microscopy in Structural Biology<\/em><\/strong>, 2024\u5e7410\u670817\u65e5, doi:10.1201\/9781003326106<\/a>\uff08\u62db\u5f85\uff09<\/li>\n
      9. Tani K, Maki-Yonekura S, Kanno R, Negami T, Hamaguchi T<\/strong><\/span>, Hall M, Mizoguchi A, M. Humbel B, Terada T, Yonekura K<\/strong><\/span>, Doi T, “Structure of endothelin ETB receptor\u2013Gi complex in a conformation stabilized by unique NPxxL motif”, Communications Biology<\/a><\/em><\/strong>, 2024\u5e7410\u670816\u65e5<\/li>\n<\/ol>\n

        2023\u5e74\u5ea6<\/span><\/strong><\/h2>\n
          \n
        1. Kato K, Hamaguchi T<\/strong><\/span>, Kumazawa M, Nakajima Y, Ifuku K, Hirooka S, Hirose Y, Miyagishima S, Suzuki T, Kawakami K, Dohmae N, Yonekura K<\/strong><\/span>, Shen J, Nagao R, “The structure of PSI-LHCI from Cyanidium caldarium<\/em> provides evolutionary insights into conservation and diversity of red-lineage LHCs”, Proceedings of the National Academy of Sciences of the United States of America<\/strong>, <\/em>2024\u5e743\u6708, doi:10.1073\/pnas.2319658121<\/a><\/li>\n
        2. Takaba K, Maki-Yonekura S, Inoue I, Tono K, Fukuda Y, Shiratori Y, Peng Y, Morimoto J, Inoue S, Higashino T, Sando S, Hasegawa T, Yabashi M, Yonekura K<\/strong><\/span>, “Comprehensive Application of XFEL Microcrystallography for Challenging Targets in Various Organic Compounds”, Journal of the American Chemical Society<\/em><\/strong>, 2024\u5e742\u670828\u65e5, doi: 10.1021\/jacs.3c11523<\/a><\/li>\n
        3. Kosumi D, Bandou-Uotani M, Kato S,Kawakami K, Yonekura K<\/span><\/strong>, Kamiya N, “Reinvestigation on primary processes of PSII-dimer from Thermosynechococcus vulcanus<\/em> by femtosecond pump-probe spectroscopy”, Photosynthesis Research<\/em><\/strong>, 2024\u5e742\u670824\u65e5, doi:https:\/\/doi.org\/10.1007\/s11120-024-01076-8<\/a><\/li>\n
        4. Higashino T, Inoue S, Arai S, Tsuzuki S, Matsui H, Kumai R, Takaba K, Maki-Yonekura S, Kurokawa H<\/strong><\/span>, Inoue I, Tono K, Yonekura K<\/strong><\/span>, Hasegawa T, “Effects of Thiophene-Fused Isomer on High-Layered Crystallinity in \u03c0-Extended and Alkylated Organic Semiconductors”, Chemistry of Materials<\/strong><\/em> 36(2) 848-859, 2024\u5e741\u67085\u65e5, doi:10.1021\/acs.chemmater.3c02500<\/a><\/li>\n
        5. Yonekura K<\/strong><\/span>, Maki-Yonekura S, Kiyofumi Takaba, “Applications and limitations of electron 3D crystallography”, Structure<\/em><\/strong> 31(11) 1328-1334, 2023\u5e7411\u67082\u65e5,doi: 10.1016\/j.str.2023.09.007<\/a>\u3000(\u62db\u5f85\uff09<\/li>\n
        6. Kato K, Hamaguchi T<\/strong><\/span>, Kumazawa M, Nakajima Y, Ifuku K, Hirooka S, Hirose Y, Miyagishima S, Suzuki T, Kawakami K, Dohmae N, Yonekura K, Jian-Ren S, Nagao R, “Structure of PSI-LHCI from Cyanidium caldarium<\/em> provides evolutionary insights into conservation and diversity of red-lineage LHCs”, BioRxiv<\/em><\/strong>, 2023\u5e7410\u670827\u65e5, doi:10.1101\/2023.10.25.563911<\/a><\/li>\n
        7. Takaba K, Maki-Yonekura S, Inoue I,\u00a0 Tono K, Fukuda Y, Shiratori Y, Peng Y, Morimoto J, Inoue S, Higashino T, Sando S, Hasegawa T, Yabashi M, Yonekura K<\/strong>,<\/span> “Comprehensive application of XFEL micro crystallography for novel organic compounds”,\u00a0ChemRxiv<\/em><\/strong>, 2023\u5e7410\u67085\u65e5, doi:10.26434\/chemrxiv-2023-69p99<\/a><\/li>\n
        8. Ono-Ogasawara C, Yamamoto S, Ogura Y, Okamura H, Takaba K, Yoshida S, Sato S, Yonekura K<\/strong><\/span>, Takikawa H, “Synthesis of (\u00b1)-zeapyranolactone, a noncanonical strigolactone isolated from maize, and determination of its overall relative configuration”, Tetrahedron Letters<\/em><\/strong> 127(1) 1-4, 2023\u5e749\u6708, doi:10.1016\/j.tetlet.2023.154695<\/a><\/li>\n
        9. Aizawa H, Sato T, Maki-Yonekura S, Yonekura K<\/span><\/strong>, Takaba K, Hamaguchi T<\/strong><\/span>, Minato T, M. Yamamoto H, “Enantioselectivity of discretized helical supramolecule consisting of achiral cobalt phthalocyanines via chiral-induced spin selectivity effect”, Nature Communications<\/strong> 14<\/em>(1), 2023\u5e747\u670828\u65e5, doi:10.1038\/s41467-023-40133-z<\/a><\/li>\n
        10. Maki-Yonekura S, Kawakami K, Takaba K, Hamaguchi T<\/strong><\/span>, Yonekura K,<\/strong><\/span>\u00a0<\/strong>“Measurement of charges and chemical bonding in a cryo-EM structure”, Communications Chemistry<\/em><\/strong> 6(1), 2023\u5e745\u670831\u65e5 \uff08\u30d7\u30ec\u30b9\u30ea\u30ea\u30fc\u30b9<\/a>\uff09, doi:10.1038\/s42004-023-00900-x<\/a><\/li>\n
        11. \n
          Morimoto J, Shiratori Y, Yokomine M, Ueda T, Nakamuro T, Takaba K, Maki-Yonekura S, Umezawa K, Miyanishi K, Fukuda Y, Watanabe T, Mizukami W, Takeuchi K, Yonekura K<\/strong><\/span>, Nakamura E, Sando S, “Bottom-up design of peptide nanoshapes in water using oligomers of N-methyl-L\/D-alanine”, ChemRxiv<\/em><\/strong>, 2023\u5e745\u670816\u65e5, doi:10.26434\/chemrxiv-2023-c4mw6<\/a><\/div>\n<\/li>\n<\/ol>\n

          2022\u5e74\u5ea6<\/strong><\/h2>\n
            \n
          1. Takaba K, Maki-Yonekura S, Inoue I, Tono K, Hamaguchi T<\/span><\/strong>, Kawakami K, Naitow H, Ishikawa T, Yabashi M, Yonekura K<\/strong><\/span>*, “Structural resolution of a small organic molecule by serial X-ray free-electron laser and electron crystallography”, N<\/em>ature Chemistry <\/em><\/strong>15 491-497, 2023\u5e743\u670820\u65e5(\u30d7\u30ec\u30b9\u30ea\u30ea\u30fc\u30b9<\/a>) , doi:10.1038\/s41557-023-01162-9<\/a><\/li>\n
          2. Himiyama T*, Hamaguchi T<\/strong><\/span>, Yonekura K<\/strong><\/span>, Nakamura T, “Unnaturally Distorted Hexagonal Protein Ring Alternatingly Reorganized from Two Distinct Chemically Modified Proteins”, Bioconjugate Chemistry<\/em><\/strong> 34(4) 764-771, 2023\u5e743\u67088\u65e5, doi:10.1021\/acs.bioconjchem.3c00057<\/a><\/li>\n
          3. Matsuike D, Tahara Y.-O., Nonaka T, Wu H.N, Hamaguchi T<\/span><\/strong>, Kudo H, Hayashi Y, Arai M, Miyata M, “Structure and Function of Gli123 Involved in Mycoplasma mobile<\/em> Gliding”,\u00a0 Journal of Bacteriology <\/strong><\/em>Vol. 205. No. 3, 2023\u5e742\u67087\u65e5<\/li>\n
          4. Kosumi D, Bandou-Uotani M, Kato S, Kawakami K, Yonekura K<\/strong><\/span>, Kamiya N, “Ultrafast energy transfer and charge separation dynamics in PSII-dimer from Thermosynechococcus vulcanus”<\/em>, Research Square, <\/em><\/strong>2023\u5e742\u670827\u65e5, doi:10.21203\/rs.3.rs-2613905\/v1<\/a><\/li>\n
          5. Nagao R*, Kato K, Hamaguchi T(equally contribution)<\/strong><\/span>, Ueno Y, Tsuboshita N, Shimizu S, Furutani M, Ehira S, Nakajima Y, Kawakami K, Suzuki T, Dohmae N, Akimoto S, Yonekura K<\/strong><\/span>*, Shen J.R*, “Structure of a monomeric photosystem I core associated with iron-stressed-induced-A proteins from Anabaena<\/em> sp. PCC 7120″, N<\/em>ature Communications<\/em><\/strong>. 14, 920, 2023\u5e742\u670817\u65e5 (\u30d7\u30ec\u30b9\u30ea\u30ea\u30fc\u30b9<\/a>), doi:10.1038\/s41467-023-36504-1<\/a><\/li>\n
          6. Sekiyama N, Takaba K, Maki-Yonekura S, Akagi K., Ohtani Y, Imamura K, Terakawa T, Yamashita K, Yonekura K<\/strong><\/span>, Kodama T.S, Tochio H, “ALS mutations in the TIA-1 prion-like domain induce pathological structures”,\u00a0 Proc. Natl. Acad. Sci. USA<\/strong><\/em> 119, e2122523119 (2022), 2022\u5e749\u670820\u65e5, doi:10.1073\/pnas.2122523119<\/a><\/li>\n
          7. Kato K, Hamaguchi T<\/span><\/strong>\u00a0(equally contribution<\/em>)<\/strong><\/span>, Nagao R, Kawakami K, Ueno Y, Suzuki T, Uchida H, Murakami A, Nakajima Y, Yokono M, Akimoto S, Dohmae N, Yonekura K<\/strong><\/span>, and Shen J.R. 2022. “Structural Basis for the Absence of Low-Energy Chlorophylls in a Photosystem I Trimer from Gloeobacter violaceus”<\/em>, ELife<\/em><\/strong> 11:73990. doi: 10.7554\/ELIFE.73990<\/a>.(\u30d7\u30ec\u30b9\u30ea\u30ea\u30fc\u30b9<\/a>)<\/li>\n
          8. Kawakami K, Hamaguchi T<\/span><\/strong>\u00a0(equally contribution<\/em>)<\/strong><\/span>, Hirose Y, Kosumi D, Miyata M, Kamiya N, and Yonekura K<\/strong><\/span>, “Core and Rod Structures of a Thermophilic Cyanobacterial Light-Harvesting Phycobilisome”, Nature Communications<\/strong> 2022 13:1<\/em> 13(1):1\u201313, doi:10.1038\/s41467-022-30962-9<\/a>. 2022\u5e746\u6708(\u30d7\u30ec\u30b9\u30ea\u30ea\u30fc\u30b9<\/a>)<\/li>\n
          9. Kimura A,\u00a0 Kitoh-Nishioka H, Aota T, Hamaguchi T<\/span><\/strong>, Yonekura K<\/strong><\/span>, Kawakami K, Shinzawa-Itoh K, Inoue-Kashino N, Ifuku K, Yamashita E, Kashino Y, and Itoh S, “Theoretical Model of the Far-Red-Light-Adapted Photosystem I Reaction Center of Cyanobacterium Acaryochloris marina<\/em> Using Chlorophyll d and the Effect of Chlorophyll Exchange”, The Journal of Physical Chemistry B<\/em><\/strong> 126(22):4009\u201321, doi:10.1021\/ACS.JPCB.2C00869<\/a>.2022\u5e745\u670826\u65e5<\/li>\n
          10. Kato K, Hamaguchi T (equally contribution)<\/strong><\/span>, Nagao R, Kawakami K, Ueno Y, Suzuki T, Uchida H, Murakami A, Nakajima Y, Yokono M, “Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus”<\/em>, eLife<\/strong><\/em> 11, 2022\u5e744\u670811\u65e5, doi:10.7554\/elife.73990<\/a><\/li>\n<\/ol>\n

            2021\u5e74\u5ea6\u4ee5\u524d\uff082019\u4ee5\u964d\u8ad6\u6587\u306e\u307f\uff09<\/h2>\n
              \n
            1. Kato K, Hamaguchi T<\/strong><\/span>, Ryo Nagao, Kawakami K, Ueno Y, Suzuki T, Uchida H, Murakami A, Nakajima Y, Yokono M, Akimoto S, Dohmae N, Yonekura K<\/strong><\/span>, Jian-Ren Shen, “Structural basis for the absence of low-energy chlorophylls responsible for photoprotection from a primitive cyanobacterial PSI”doi:10.1101\/2021.09.29.462462<\/a><\/li>\n
            2. Takaba K,Maki-Yonekura S,Inoue I,Tono K,Hamaguchi T,<\/strong><\/span>Kawakami K,Naitow H,Ishikawa T,Yabashi M,Yonekura K,<\/strong><\/span>“Hydrogen properties in an organic molecule revealed by XFEL and electron crystallography”,doi:https:\/\/doi.org\/10.26434\/chemrxiv-2021-jvbfl<\/a><\/li>\n
            3. Yonekura K<\/strong><\/span>,Maki-Yonekura S,Naitow H,Hamaguchi T<\/strong><\/span>,Takaba K,”Machine learning-based real-time object locator\/evaluator for cryo-EM data collection”,Communications Biology<\/strong><\/em>,doi:https:\/\/doi.org\/10.1038\/s42003-021-02577-1<\/a><\/li>\n
            4. Maki-Yonekura S,Kawakami K,Hamaguchi T,Takaba K,Yonekura K<\/strong><\/span>,”Hydrogen properties and charges in a sub-1.2 \u00c5 resolution cryo-EM structure revealed by a cold field emission beam”,doi : 10.1101\/2021.12.21.473430<\/a><\/li>\n
            5. Inoue S, Nikaido K, Higashino T, Arai S, Tanaka M, Kumai R, Tsuzuki S, Horiuchi S, Sugiyama H, Segawa Y, Takaba K, Maki-Yonekura S, Yonekura K<\/strong><\/span>, and Hasegawa T. 2022.\u00a0 “Emerging Disordered Layered-Herringbone Phase in Organic Semiconductors Unveiled by Electron Crystallography.” Chemistry of Materials<\/em><\/strong> 34(1). doi: 10.1021\/acs.chemmater.1c02793<\/a>.<\/li>\n
            6. Hamaguchi T<\/span><\/strong>, Kawakami K, Shinzawa-Itoh K, Inoue-Kashino N, Itoh S, Ifuku K, Yamashita E, Maeda K, Yonekura K<\/strong><\/span>, and Kashino Y. 2021. “Structure of the Far-Red Light Utilizing Photosystem I of Acaryochloris marina<\/em>.” Nature Communications<\/em> 12(1):2333. doi: 10.1038\/s41467-021-22502-8.<\/li>\n
            7. Hiragi K, Nishio K, Moriyama S, Hamaguchi T<\/span><\/strong>, Mizoguchi A, Yonekura K<\/strong><\/span>, Tani K, and Mizushima T. 2021. “Structural Insights into the Targeting Specificity of Ubiquitin Ligase for S. cerevisiae<\/em> Isocitrate Lyase but Not C. Albicans Isocitrate Lyase.” Journal of Structural Biology<\/em><\/strong> 213(3):107748. doi: 10.1016\/j.jsb.2021.107748.<\/li>\n
            8. Kato K, Miyazaki N, Hamaguchi T<\/span><\/strong>\u00a0(equally contribution<\/em>)<\/strong><\/span>, Nakajima Y, Akita F, Yonekura K<\/strong><\/span>, and Shen J.R. 2021. “High-Resolution Cryo-EM Structure of Photosystem II Reveals Damage from High-Dose Electron Beams.” Communications Biology<\/em><\/strong> 4(1):382. doi: 10.1038\/s42003-021-01919-3.<\/li>\n
            9. Kawakami K, Nagao R, Tahara Y-O., Hamaguchi T<\/span><\/strong>, Suzuki T, Dohmae N, Kosumi D, Shen J.R, Miyata M, Yonekura K<\/strong><\/span>, and Kamiya N, 2021, “Structural Implications for a Phycobilisome Complex from the Thermophilic Cyanobacterium Thermosynechococcus vulcanus<\/em>.” Biochimica et Biophysica Acta (BBA) – Bioenergetics<\/em> 1862(9):148458, doi: 10.1016\/J.BBABIO.2021.148458.<\/li>\n
            10. Yonekura K<\/strong><\/span>, Maki-Yonekura S, Hamaguchi T<\/span><\/strong>, Naitow H, Takaba K, and Kawakami K, 2021, “Cryo-EM and ED with a Cold-Field Emission Beam and Energy Filtration”, 233\u201341, doi: 10.1007\/978-981-16-2982-2_23.<\/li>\n
            11. Yonekura K<\/strong><\/span>, Maki-Yonekura S, Naitow H, Hamaguchi T<\/span><\/strong>, and Takaba K, 2021, “Machine Learning-Based Real-Time Object Locator\/Evaluator for Cryo-EM Data Collection”, Communications Biology<\/strong> 2021 4:1<\/em> 4(1):1\u20138, doi: 10.1038\/s42003-021-02577-1.\u3000(\u30d7\u30ec\u30b9\u30ea\u30ea\u30fc\u30b9<\/a>)<\/li>\n
            12. \u00a0Yu H, Hamaguchi T<\/span><\/strong>\u00a0(equally contribution)<\/strong><\/span>, Nakajima Y, Kato K, Kawakami K, Akita F, Yonekura K<\/strong><\/span>, and Shen J.R. 2021, “Cryo-EM Structure of Monomeric Photosystem II at 2.78 \u00c5 Resolution Reveals Factors Important for the Formation of Dimer”, Biochimica et Biophysica Acta (BBA)<\/strong> – Bioenergetics<\/strong><\/em> 1862(10):148471, doi: 10.1016\/J.BBABIO.2021.148471.<\/li>\n
            13. Yonekura K<\/strong><\/span>, Maki-Yonekura S, Takaba K, Hamaguchi T<\/span><\/strong>, Naitow H, and Kawakami K, 2021, “Complementary Use of High-Resolution and High-Precision Cryo-ED and EM”, Microscopy and Microanalysis<\/em><\/strong> 27(S1), doi: 10.1017\/s143192762100132x.<\/li>\n
            14. Kato K, Takaba K, Maki-Yonekura S, Mitoma N, Nakanishi Y, Nishihara T, Hatakeyama T, Kawada T, Hijikata Y, Pirillo J, Scott L.T, Yonekura K<\/strong><\/span>, Segawa Y, and Itami K, 2021, “Double-Helix Supramolecular Nanofibers Assembled from Negatively Curved Nanographenes”, Journal of the American Chemical Society<\/em><\/strong> 143(14), doi: 10.1021\/jacs.1c00863.<\/li>\n
            15. Maki-Yonekura S,\u00a0 Hamaguchi T<\/span><\/strong>, Naitow H, Takaba K, and Yonekura K<\/strong>,<\/span> 2020, “Advances in Cryo-EM and ED with a Cold-Field Emission Beam and Energy Filtration \u2014Refinements of the CRYO ARM 300 System in RIKEN SPring-8 Center\u2014”, Microscopy<\/em><\/strong> 2020:1\u20139, doi: 10.1093\/jmicro\/dfaa052.<\/li>\n
            16. Takaba K, Maki-Yonekura S, Inoue S, Hasegawa T, and Yonekura K<\/strong>,<\/span> 2021, “Protein and Organic-Molecular Crystallography With 300kV Electrons on a Direct Electron Detector”, Frontiers in Molecular Biosciences<\/em><\/strong> 7, doi: 10.3389\/fmolb.2020.612226.<\/li>\n
            17. Yonekura K<\/strong><\/span>, Maki-Yonekura S, Hamaguchi T<\/span><\/strong>, Naitow H, Takaba K, and Kawakami K, 2021, “Cryo-EM and ED with a Cold-Field Emission Beam and Energy Filtration”, 233\u201341. doi: 10.1007\/978-981-16-2982-2_23.<\/li>\n
            18. Naitow H, Hamaguchi T<\/span><\/strong>(equally contribution)<\/strong><\/span>, Maki-Yonekura S, Isogai M, Yoshikawa N, and Yonekura K<\/strong><\/span>. n.d. “Apple Latent Spherical Virus Structure with Stable Capsid Frame Supports Quasi-Stable Protrusions Expediting Genome Release”, doi: 10.1038\/s42003-020-01217-4.<\/li>\n
            19. Takaba K, Maki-Yonekura S, and Yonekura K<\/strong>,<\/span> 2020, “Collecting Large Datasets of Rotational Electron Diffraction with ParallEM and SerialEM”,\u00a0Journal of Structural Biology <\/em><\/strong>211(2):107549, doi: 10.1016\/j.jsb.2020.107549.<\/li>\n
            20. Kurokawa H<\/strong><\/span>, Ambo T, Takahashi S, and Koyama T, 2020, “Crystal Structure of Thermobifida fusca<\/em> Cis-Prenyltransferase Reveals the Dynamic Nature of Its RXG Motif-Mediated Inter-Subunit Interactions Critical for Its Catalytic Activity”, Biochemical and Biophysical Research Communications<\/em> 532(3), doi: 10.1016\/j.bbrc.2020.08.062.<\/li>\n
            21. Hamaguchi T<\/span><\/strong>, and Yonekura K<\/strong>,<\/span> 2020, “Tidy up Cryo-EM Sample Grids with 3D Printed Tools” Journal of Structural Biology<\/em><\/strong> 209(1):107414, doi: 10.1016\/j.jsb.2019.107414.<\/li>\n
            22. Guzm\u00e1n-Afonso C, Hong Y.L, Colaux H, Iijima H, Saitow A, Fukumura T, Aoyama Y, Motoki S, Oikawa T, Yamazaki T, Yonekura K<\/strong><\/span>, and Nishiyama Y, 2019, “Understanding Hydrogen-Bonding Structures of Molecular Crystals via Electron and NMR Nanocrystallography.” Nature Communications<\/em><\/strong> 10(1), doi: 10.1038\/s41467-019-11469-2.<\/li>\n
            23. Kato T, Makino F, Nakane T, Terahara N, Kaneko T, Shimizu Y, Motoki S, Ishikawa I, Yonekura K<\/strong><\/span>, and Namba K, 2019, “CryoTEM with a Cold Field Emission Gun That Moves Structural Biology into a New Stage”, Microscopy and Microanalysis<\/em><\/strong> 25(S2), doi: 10.1017\/s1431927619005725.<\/li>\n
            24. Kubota M, Matsuoka R, Suzuki T, Yonekura K<\/strong><\/span>, Yanagi Y, and Hashiguchi T, 2019, “Molecular Mechanism of the Flexible Glycan Receptor Recognition by Mumps Virus”, Journal of Virology<\/em><\/strong> 93(15), doi: 10.1128\/jvi.00344-19.<\/li>\n
            25. Hamaguchi T<\/span><\/strong>,\u00a0 Maki-Yonekura S, Naitow H, Matsuura Y, Ishikawa T, and Yonekura K<\/strong>,<\/span> 2019, “A New Cryo-EM System for Single Particle Analysis”, Journal of Structural Biology<\/em><\/strong> 207(1):40\u201348, doi: 10.1016\/j.jsb.2019.04.011.<\/li>\n
            26. Yonekura K<\/strong><\/span>,\u00a0 Ishikawa T, and Maki-Yonekura S, 2019, “A New Cryo-EM System for Electron 3D Crystallography by EEFD.” Journal of Structural Biology<\/em> 206(2), doi: 10.1016\/j.jsb.2019.03.009.<\/li>\n
            27. Hamaguchi T<\/span><\/strong>, Kawakami M, Furukawa H, and Miyata M, 2019, “Identification of Novel Protein Domain for Sialyloligosaccharide Binding Essential to Mycoplasma mobile<\/em> Gliding”, FEMS Microbiology Letters<\/em><\/strong> 366(3), doi: 10.1093\/femsle\/fnz016.<\/li>\n<\/ol>\n","protected":false},"excerpt":{"rendered":"

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