原著論文
・Cross-linked crystals of dirhodium tetraacetate/RNase A adduct can be used as heterogeneous catalysts
D. Loreto, B. Maity, T. Morita, H. Nakamura, *A. Merlino, and *T. Ueno, Inorg. Chem., 62, 7515-7524 (2023), DOI: 10.1021/acs.inorgchem.3c00852

・Elucidating Conformational Dynamics and Thermostability of Designed Aromatic Clusters by Using Protein Cages
Y. Hishikawa, H. Noya, S. Nagatoishi, T. Yoshidome, B. Maity, K. Tsumoto, S. Abe, and *T. Ueno, Chem. Eur. J., 29, e202300488(2023), DOI: 10.1002/chem.202300488

・Apo-ferritin Caged Pt Nanoparticles for Selective Hydrogenation of p-Chloronitrobenzene
ZY. Zhou, Y. Zheng, C. Lu, B. Maity, Y. Chen, *T. Ueno, Z. Liua, and *D. Lu, ACS Appl. Nano Mater.,, 6, 5835-5843, (2023), DOI: 10.1021/acsanm.3c00231

・Design of a Hierarchical Assembly at a Solid-liquid Interface using an Asymmetric Protein Needle
K. Kikuchi, K. Date, and *T. Ueno, Langmuir, 39, 2389-2397 (2023), DOI: 10.1021/acs.langmuir.2c03146

・Engineering of an in-cell protein crystal for fastening a metastable conformation of a target miniprotein
M. Kojima, S. Abe, T. Furuta, D. P. Tran, K. Hirata, K. Yamashita, Y. Hishikawa, A. Kitao, *T. Ueno, Biomater. Sci.,11,1350-1357 (2022), DOI: 10.1039/d2bm01759h

・Rapid and sensitive SARS-CoV-2 detection using a homogeneous fluorescent immunosensor Quenchbody with crowding agents
B. Zhu, N. Nosaka, S. Kanamaru, J. Dong, Y. Dai, A. Inoue, Y. Yang, K. Kobayashi, T. Kitaguchi, H. Iwasaki, R. Koike, K. Wakabayashi and *H. Ueda, Analyst, 147, 4971-4979 (2022), DOI: 10.1039/D2AN01051H

・Cell-free Protein Crystallization for Nanocrystal Structure Determination
S. Abe, J. Tanaka, M. Kojma, S. Kanamaru, K. Hirata, K. Yamashita, A. Kobayashi, and *T. Ueno, Sci. Rep., 12, 16031 (2022), DOI: 10.1038/s41598-022-19681-9

・Design of a gold clustering site in an engineered apo-ferritin cage
C. Lu, B. Maity, X. Peng, N. Ito, S. Abe, X. Sheng, *T. Ueno *D. Lu, Commun. Chem., 5, 39 (2022),DOI: 10.1038/s42004-022-00651-1

・Heterogeneous IgE reactivities to Staphylococcus pseudintermedius strains in dogs with atopic dermatitis, and the identification of DM13-domain-containing protein as a bacterial IgE-reactive molecule
I. T. Uchiyama, H. Tsurui, H. Shimakura, T. Nasukawa, I. Imanishi, J. Uchiyama, T. Fukuyama, S. Sakamoto, K. Morisawa, M. Fujimura, H. Murakami, S. Kanamaru, K. Kurokawa, K. Kawamoto, K. Iyori and M. Sakaguchi, FEMS Microbiol　Lett., 369, fnac019 (2022), DOI: 10.1093/femsle/fnac019

・Importance of the Subunit−Subunit Interface in Ferritin Disassembly: A Molecular Dynamics Study
Zhipeng Li, B. Maity, Y. Hishikawa, T. Ueno, and *D. Lu, Langmuir, 38, 1106−1113 (2022), DOI: 10.1021/acs.langmuir.1c02753

・Controlled Uptake of an Iridium Complex inside Engineered apo-Ferritin Nanocages: Study of Structure and Catalysis
M. Taher, B. Maity, T. Nakane, S. Abe, *T. Ueno, *S. Mazumdar, Angew. Chem.Int. Ed., 61, e202116623 (2022), DOI:10.1002/anie.202116623

・Protein Needles Designed to Self-Assemble through Needle Tip Engineering
K. Kikuchi ,T. Fukuyama, T. Uchihashi, T. Furuta, Y. T. Maeda , and *T Ueno, Small, 18, 2106401 (2022), DOI: 10.1002/smll.202106401

・Dynamic Behavior of Cargo Proteins Regulated by Linker Peptides on a Protein Needle Scaffold
Q. D. Nguyen ,K. Kikuchi ,M. Kojima , and *T Ueno, Chemistry Letters, 51, 73-76 (2022), DOI: 10.1246/cl.210599

・Design of an In-Cell Protein Crystal for the Environmentally Responsive Construction of a Supramolecular Filament
S. Abe, T. T. Pham, H. Negishi, K. Yamashita, K. Hirata, T. Ueno, Angew. Chem., Int. Ed., 60, 12341-12345 (2021), DOI: 10.1002/anie.202102039

・A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity
A. Zdravković, J. M. Daley, Arijit Dutta, T. Niwa, Y. Murayama, S. Kanamaru, K. Ito, T. Maki, B. Argunhan, M. Takahashi, H. Tsubouchi, P. Sung and *H. Iwasaki, Proc. Natl. Acad. Sci. (USA), 118, e2016287118 (2021), DOI: 10.1073/pnas.2016287118

・The versatile manipulations of self-assembled proteins in vaccine design
D. Q. Nguyen, K. Kikuchi, B. Maity, T. Ueno, Int. J. Mol. Sci., 22, 1934-1954 (2021), DOI: 10.3390/ijms22041934

・In-Cell Engineering of Protein Crystals with Nanoporous Structures for Promoting Cascade Reactions
T. K. Nguyen, S. Abe, M. Kasamatsu, B. Maity, K. Yamashita, K. Hirata, M. Kojima, T. Ueno, ACS Appl. Nano. Mater., 4, 1672-1681 (2021), DOI: 10.1021/acsanm.0c03129

・Structure and Function of the T4 Spackle Protein Gp61.3
*S. Kanamaru, K. Uchida, M. Nemoto, A. Fraser, F. Arisaka and P. G. Leiman, Viruses, 12, 1070 (2020), DOI: 10.3390/v12101070

・Single-molecule level dynamic observation of disassembly of the apo-ferritin cage in solution
B. Maity, Z.P. Li, K. Niwase, C. Ganser, T. Furuta†, T. Uchihashi, D. Lu, T. Ueno, PCCP, 22, 18562-18572 (2020), DOI: 10.1039/D0CP02069A

・Real-time tracking reveals catalytic roles for the two DNA binding sites of Rad51
K. Ito, Y. Murayama, Y. Kurokawa, S. Kanamaru, Y. Kokabu, T. Maki, T. Mikawa, B. Argunhan, H. Tsubouchi, M. Ikeguchi, M. Takahashi and *H. Iwasaki, Nat. Commun., 11, 2950 (2020), DOI: 10.1038/s41467-020-16750-3

・Design of Multinuclear Gold Binding Site at the Two-fold Symmetric Interface of the Ferritin Cage
Y. Hishikawa, B. Maity, N. Ito, S. Abe, D. Lu, *T. Ueno, Chem. Lett., 49, 840-844 (2020), DOI: 10.1246/cl.200217

・Site-Selective Protein Chemical Modification of Exposed Tyrosine Residues Using Tyrosine Click Reaction
S. Sato, M. Matsumura, T. Kadonosono, S. Abe, T. Ueno, H. Ueda, *H. Nakamura, Bioconjugate Chem., 31, 1417–1424 (2020), DOI: 10.1021/acs.bioconjchem.0c00120

・Dynamic behavior of an artificial protein needle contacting a membrane observed by high-speed atomic force microscopy
T. Ueno, *K. Niwase, D. Tsubokawa, K. Kikuchi, N. Takai, T. Furuta, R. Kawano, T. Uchihashi, Nanoscale, 12, 8166-8173 (2020), DOI: 10.1039/D0NR01121E

・Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex
B. Argunhan, M. Sakakura, N. Afshar, M. Kurihara, K. Ito, T. Maki, S. Kanamaru, Y. Murayama, H. Tsubouchi, M. Takahashi, H. Takahashi, *H. Iwasaki, eLife, 9, e52566 (2020), DOI: 10.7554/eLife.52566

・Coordination design of cadmium ions at the 4-fold axis channel of the apo-ferritin cage
S. Abe, N. Ito, B. Maity, C. Lu, D. Lu, *T. Ueno, Dalton Trans., 48, 9759-9764 (2019), DOI: 10.1039/C9DT00609E

・Encapsulation of biomacromolecules by soaking and co-crystallization into porous protein crystals of hemocyanin
T. Hashimoto, Y. Ye, A. Matsuno, Y. Ohnishi, A. Kitamura, M. Kinjo, S. Abe, T. Ueno, M. Yao, T. Ogawa, T. Matsui,*Y. Tanaka, Biochem. Biophys. Res. Coomun., 509, 577-584 (2019), DOI: 10.1016/j.bbrc.2018.12.096

・Construction of Supramolecular Nanotubes from Protein Crystals
T. K. Nguyen, H. Negishi, S. Abe, *T. Ueno, Chem. Sci., 10, 1046-1051 (2019), DOI: 10.1039/C8SC04167A

書籍/総説・解説
・“細胞内タンパク質結晶を利用した超分子構造体合成”
安部 聡, 上野隆史,超分子研究会 アニュアルレビュー,, , (2022)

・"タンパク質カゴ「フェリチン」に組み込んだ金属錯体による不斉反応の効率化"
安部 聡, 上野隆史,超バイオサイエンスとインダストリー,, 80 , 478-479(2022)

・"細胞内タンパク質結晶の分子設計による生体固体材料の機能創製"
安部 聡, 上野隆史,日本結晶成長学会誌,, 49 , 1-9 (2022)

・"Artificial metalloenzymes based on protein assembly"
B. Maity, M. Taher, S. Mazumdar, T. Ueno,Chem. Rev.,, 469 , 214593 (2023), DOI: 10.1016/j.ccr.2022.214593

・Engineering of protein crystals for development of bionanomaterials
M. Kojima, S. Abe and *T. Ueno, Biomater. Sci., 10, 354-367 (2022),DOI: 10.1039/D1BM01752G

・“はたらく分子マシン(7)「分子サイズの小さな針」”
上野隆史, 現代化学, 601, 52-55, 4月号 (2021)

・Engineering of protein crystals for development of bionanomaterials
T. K. Nguyen, T. T. Pham, *T. Ueno, Jpn. J. Appl. Phys., 58, SI0802 (2019),DOI: 10.7567/1347-4065/ab1399

・Recent progresses in the accumulation of metal ions into the apo-ferritin cage: Experimental and theoretical perspectives
Basudev Maity, Yuki Hishikawa, DiannanLu, Takafumi Ueno*, Polyhedron, 172, 104-111 (2019), DOI: 10.1016/j.poly.2019.03.048

・「Advances in Bioorganometallic Chemistry」,"Tailoring Organometallic Complexes into Protein Scaffolds:
Structures and Functions"
B.Maity, S.Abe, *T.Ueno ,Editor; T.Hirao, T.Moriuchi, ELSEVIER, 329-346 (2019), ISBN: 978-0-12-814197-7

・「Functional Polymer Complexes」,"Functionalization of Artificial Metalloenzymes"
S. Abe, and T. Ueno, , (2023), ISBN:

・「Protein Cages」,T. Ueno, S. Lim, K. Xia (Eds),"A Generalized Method for Metal Fixation in Horse Spleen L-Ferritin Cage"
B. Maity, and T. Ueno, Springer, (2023), ISBN: 978-1-0716-3221-5

・「Cell-Inspired Materials and Engineering」,D. O. Wang, D. Packwood (Eds),Construction of Multistep Catalytic Systems in Protein Assemblies”
H. Tabe and T. Ueno, D. O. Wang, D. Packwood,29-44, Springer, (2021), ISBN: 978-3-030-55924-3

・「タンパク質結晶を利用した分子・ナノ粒子触媒」 “光エネルギー変換における分子触媒の新展開”
安部　聡, 上野隆史, 化学同人, (2020), ISBN: 9784759813982

・「人口金属酵素による機能創成」, “機能性高分子金属錯体”,
安部　聡, 上野隆史, 錯体化学会フロンティア選書, 三共出版 (2020), 324, ISBN: 978-4-7827-0791-3

・「Advances in Bioorganometallic Chemistry」, T. Hirao, T. Moriuchi (Eds),“Tailoring Organometallic Complexes into Protein Scaffolds: Structures and Functions”, B. Maity, S. Abe, *T. Ueno, 329-346, ELSEVIER, (2019), ISBN: 978-0-12-814197-7

・「生命機能に迫る分子の最新化学」,"人工金属酵素の次世代設計" ,
上野隆史, 化学同人, (2018), ISBN: 97847598139