原著論文
・Flagellar polymorphism-dependent bacterial swimming motility in a structured environment
*Y. Kinosita, *Y. Sowa, BPPB, 20,e200024 (2023),DOI: 10.2142/biophysico.bppb-v20.0024

・Antiparallel dimer structure of CELSR cadherin in solution revealed by high-speed atomic force microscopy
*S. Nishiguchi, *R. Kasai, *T. Uchihashi, Proc. Natl. Acad. Sci. U.S.A., 120, e2302047120 (2023), DOI: 10.1073/pnas.2302047120

・Creation of Single Molecular Conjugate of Metal-organic Cage and DNA
T. Nakajo, S. Kusaka, H. Hiraoka, K. Nomura, N. Matsubara, R. Baba, Y. Yoshida, K. Nakamoto, M. Honma, H. Iguchi, T. Uchihashi, H. Abe and *R. Matsuda, Chem. Commun., 59,4974-4977 (2023), DOI: 10.1039/D3CC00460K

・Development of a Versatile Protein Labeling Tool for Live-Cell Imaging Using Fluorescent β-Lactamase Inhibitors
M. Minoshima, T. Umeno, K. Kadooka, M. Roux, N. Yamada, *K. Kikuchi, Angew. Chem. Int. Ed., 62, e20231704 (2023), DOI: 10.1002/anie.202301704

・https://inflammregen.biomedcentral.com/articles/10.1186/s41232-023-00268-4
S. Yari, *J. Kikuta, H. Shigyo, Y. Miyamoto, D. Okuzaki, Y. Furusawa, M. Minoshima, K. Kikuchi, *M. Ishii, Inflamm Regener, 43,18 (2023), DOI: 10.1186/s41232-023-00268-4

・Biosynthesis of highly branched gold nanoparticles through structural engineering of fatty acids
*Y. Yue, Y. Yokota, T. Uchihashi, iScience, 20,105864 (2023), DOI:10.1016/j.isci.2022.105864

・Disulfide Bond-Mediated Oligomerization of a Green Fluorescent Protein in Solution
J. W. Soon , *K. Oohora, *T. Uchihashi and *T. Hayashii, Chem. Lett., 52,105-109 (2023), DOI: 10.1246/cl.220495

・Decoding of the ubiquitin code for clearance of colliding ribosomes by the RQT complex
*Y. Matsuo, T. Uchihashi and *T. Inada, Nat. Commun., 14,79 (2023), DOI: 10.1038/s41467-022-35608-4

・3D structure of ring-shaped microtubule swarms revealed by high-speed atomic force microscopy
M. R. Rashid, C. Ganser, M. Akter, S. R. Nasrin, A. M. R. Kabir, K. Sada, T. Uchihashi, and *A. Kakugo, Chem. Lett., 52,100-104 (2023), DOI: 10.1246/cl.220491

・Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface
T. Uchiyama, T. Uchihashi, T. Ishida, A. Nakamura, J. V. Vermaas, M. F. Crowley, M. Samejima, G. T. Beckham, *K. Igarashi, Sci. Adv., 8,eade5155 (2022), DOI:10.1126/sciadv.ade5155

・The rapid evolution of flagellar ion selectivity in experimental populations of E. coli
P. Ridone, T. Ishida, A. Lin, D. T. Humphreys , E. Giannoulatou, Y. Sowa, *M. A. B. Baker, Sci Adv., 8,eabq2492 (2022), DOI: 10.1126/sciadv.abq2492

・Hybrid, Dual Visible and Near-Infrared Fluorescence Emission of (6, 5) Single-Walled Carbon Nanotubes Modified with Fluorescein through Aryl Diazonium Salt Chemistry
*M. M. Tomczyk, M. Minoshima, K. Kikuchi, A. B. Grzechnik, Z. Starosolski, R. Bhavane, M. Zalewski, *N. Kuźnik, Nanotechnology, 34, 055703 (2023), DOI: 10.1088/1361-6528/ac9c6a

・Tip-scan high-speed atomic force microscopy with a uniaxial substrate stretching device for studying dynamics of biomolecules under mechanical stress
F. Y. Chan, R. Kurosaki, C. Ganser, T. Takeda, and *T. Uchihashi, Rev. Sci. Instrum., 93,113703 (2022), DOI:10.1063/5.0111017

・Mechanism of the Irreversible Transition from Pentamer to Monomer at pH 2 in a Blue Proteorhodopsin
M. Sumikawa, R. A.Yoshizumi, T. Uchihashi, and *H. Kandori, Biochemistry, 61, 1936-1944 (2022), DOI: 10.1021/acs.biochem.2c00328

・Multiple dimeric structures and strand-swap dimerization of E-cadherin in solution visualized by high-speed atomic force microscopy
*S. Nishiguchi, T. Furuta, and *T. Uchihashi, Proc. Natl. Acad. Sci. U.S.A., 119,e2208067119 (2022), DOI: 10.1073/pnas.2208067119

・Photoinitiator-Free Two-Photon Polymerization of Biocompatible Materials for 3D Micro/Nanofabrication
A. Nakayama, Y. Kumamoto, M. Minoshima, K. Kikuchi, A. Taguchi, *K. Fujita, Adv. Opt. Mater., 10,2200474 (2022), DOI: 10.1002/adom.202200474

・Efficient Visible/NIR Light-driven Uncaging of Hydroxylated Thiazole Orange-based Caged Compounds in Aqueous Media
R. Hashimoto, M. Minoshima, S. Sakata, F. Ono, H. Ishii, Y. Watakabe, T. Nemoto, S. Yanaka, K. Kato, *K. Kikuchi, Chem. Sci., 13,7462-7467 (2022), DOI: 10.1039/d2sc02364d

・The Lipid-Binding Defective Dynamin 2 Mutant in Charcot-Marie-Tooth Disease Impairs Proper Actin Bundling and Actin Organization in Glomerular Podocytes
E. Hamasaki, N. Wakita, H. Yasuoka, H. Nagaoka, M. Morita, E. Takashima, T. Uchihashi, T. Takeda, T. Abe, J. W. Lee, T. Iimura, M. A. Saleem, N. Ogo, A. Asai, A. Narita, *K. Takei and *H. Yamada, Front. Cell Dev. Biol., 10,8845092090 (2022), DOI: 10.3389/fcell.2022.884509

・pH‐Sensitive Polymethacrylates as Potential Contrast Agents in 9F MRI
M. Zalewski, D. Janasik, A. Kapała, M. Minoshima, F. Sugihara, W. Raj, J. Pietrasik, K. Kikuchi, *T. Krawczyk, Macromol Chem Phys., 223,2965 (2022), 2200027 (2022), DOI:10.1002/macp.202200027

・Bayesian-based decipherment of in-depth information in bacterial chemical sensing beyond pleasant/unpleasant responses
H. Tanaka, Y. Kazuta, Y. Naruse, Y. Tominari, H. Umehara, Y. Sowa, T. Sagawa, K. Oiwa, M. Okada, *I.Kawagishi, * H. Kojima, Sci Rep., 12,2965 (2022), DOI: 10.1038/s41598-022-06732-4

・Quantitative Visualization of the Interaction between Complement Component C1 and Immunoglobulin G: The Effect of CH1 Domain Deletion
S. Yanaka, S. Nishiguchi, R. Yogo, H. Watanabe, J. Shen, H. Yagi, *T. Uchihashi, and *K. Kato, Int. J. Mol. Sci., 23,2090 (2022), DOI: 10.3390/ijms23042090

・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

・Shape-selective one-step synthesis of branched gold nanoparticles on the crystal surface of redox-active PdII-macrocycles
Y. Yamashita, *S. Tashiro, Y. Ishii, T. Uchihashi, N. Matsushita, R. Kubota, and *M. Shionoya, Dalton Trans., 51,1318-1324 (2022), DOI: 10.1039/D1DT03973C

・Molecular Origin of the Anomalous pH Effect in Blue Proteorhodopsin
M. Sumikawa, R. Abe-Yoshizumi, T. Uchihashi, and *H. Kandori, J. Phys. Chem. Lett., 12,12225-12229 (2021), DOI: 10.1021/acs.jpclett.1c03355

・Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade
M. Yagi-Utsumi, K. Aoki, H. Watanabe, C. Song, S. Nishimura, T. Satoh, S. Yanaka, C. Ganser, S. Tanaka, V. Schnapka, E. Wai Goh, Y. Furutani, K. Murata, T. Uchihashi, K. Arakawa & *K. Kato, Sci. Rep., 11, 21328 (2021), DOI: 10.1038/s41598-021-00724-6

・Construction of ferritin hydrogels utilizing subunit–subunit interactions
M. Yamanaka, T. Mashima, M. Ogihara, M. Okamoto, T. Uchihashi, and *S. Hirota, PLoS ONE, 16, e0259052 (2021), DOI: 10.1371/journal.pone.0259052

・Novel Amiloride Derivatives That Inhibit Bacterial Motility across Multiple Strains and Stator Types
MI. Islam, JH. Bae, T. Ishida, P. Ridone, J.Lin, MJ. Kelso, Y. Sowa, BJ. Buckley, *MAB. Baker, J. Bacteriol., 203,e0036721 (2021), DOI: 10.1128/JB.00367-21

・Deformation of microtubules regulates translocation dynamics of kinesin
S. R. Nasrin, C. Ganser, S. Nishikawa, A. M. R. Kabir, K. Sada, T. Yamashita, M. Keguchi, T. Uchihashi, H. Hess, and *A. Kakugo, Sci. Adv., 7, eabf2211 (2021), DOI: 10.1126/sciadv.abf2211

・Cardioluminescence in Transgenic Zebrafish Larvae: A Calcium Imaging Tool to Study Drug Effects and Pathological Modeling
M. Vicente, J. Salgado-Almario, M. M. Collins, A. Martínez-Sielva, M. Minoshima, K. Kikuchi, B. Domingo, *J. Llopis, Biomedicines, 9, 1294 (2021), DOI: 10.3390/biomedicines9101294

・Tardigrade Secretory-Abundant Heat-Soluble Protein Has a Flexible β-Barrel Structure in Solution and Keeps This Structure in Dehydration
K. Miyazawa, S. G. Itoh, H. Watanabe, T. Uchihashi, S.Yanaka, M. Yagi-Utsumi, K. Kato, K. Arakawa, and *H. Okumura, J. Phys. Chem. B, 125, 9145–9154 (2021), DOI: 10.1021/acs.jpcb.1c04850

・Reconstruction of Three-Dimensional Conformations of Bacterial ClpB from High-Speed Atomic-Force-Microscopy Images
B. Dasgupta, O. Miyashita, T. Uchihashi and *F. Tama, Front. Mole. Biosci: Biological Modeling and Simulation, 8, 704274 (2021), DOI: 10.3389/fmolb.2021.704274

・Anti-Siglec-15 antibody suppresses bone resorption by inhibiting osteoclast multinucleation without attenuating bone formation
H. Tsukazaki, *J. Kikuta, T. Ao, A. Morimoto, C. Fukuda, E. Tsuda, M. Minoshima, K. Kikuchi, T. Kaito, *M. Ishii, Bone, 152, 116095 (2021), DOI: 10.1016/j.bone.2021.116095

・The FlhA linker mediates flagellar protein export switching during flagellar assembly.
Y. Inoue, M. Kinoshita, M. Kida, N. Takekawa, K. Namba, *K. Imada, *T. Minamino, Commun. Biol., 4, 646 (2021), DOI: 10.1038/s42003-021-02177-z

・JRAB/MICAL-L2 undergoes liquid–liquid phase separation to form tubular recycling endosomes
*A. Sakane, Taka-aki Yano, T. Uchihashi, K. Horikawa, Y. Hara, I. Imoto, S. Kurisu, H. Yamada, K. Takei and *T. Sasaki, Commun. Biol., 4, 551 (2021), DOI: 10.1038/s42003-021-02080-7

・Development of Off-On Switching 19F MRI Probes for Cathepsin K Activity Detection
Y. Konishi, A. Okunishi, F. Sugihara, T. Nakamura, K. Akazawa, M. Minoshima, *K. Kikuchi, Bull. Chem. Soc. Jpn., 94,1690-1694 (2021), DOI: 10.1246/bcsj.20210099

・Non-close-packed arrangement of soft elastomer microspheres on solid substrates
Y. Sasaki, S. Hiroshige, M. Takizawa, Y. Nishizawa, T. Uchihashi, H. Minato and *D. Suzuki, RSC Advances, 11,14562-14567 (2021), DOI: 10.1039/D1RA02688G

・Nanostructure and thermoresponsiveness of poly (N-isopropyl methacrylamide)-based hydrogel microspheres prepared via aqueous free radical precipitation polymerization
Y. Nishizawa, H. Minato, T. Inui, I. Saito, T. Kureha, M. Shibayama, *T. Uchihashi and *D. Suzuki, RSC Advances, 11,13130-13137 (2021), DOI: 10.1039/D1RA01650D

・Formation of Single Double-Layered Coacervate of Poly (N,N-diethylacrylamide) in Water by a Laser Tweezer
M. Matsumoto, T. Asoh, T. Shoji, and *Y. Tsuboi,Langmuir, 37,2874-2883 (2021), DOI: 10.1021/acs.langmuir.0c03009

・Dynamic Assembly/Disassembly of Staphylococcus aureus FtsZ Visualized by High-Speed Atomic Force Microscopy
J. Fujita, S. Sugiyama, H. Terakado, M. Miyazaki, M. Ozawa, N. Ueda, N. Kuroda, S.-i. Tanaka, T. Yoshizawa,*T. Uchihashi and *H. Matsumura, Int. J. Mol. Sci., 22,1697 (2021), DOI: 10.3390/ijms22041697

・Revisiting the Rate-Limiting Step of the ANS-Protein Binding at the Protein Surface and Inside the Hydrophobic Cavity
C. Ota, S.-i. Tanaka, and *K. Takano, Molecules., 26, 420 (2021), DOI: 10.3390/molecules26020420

・Exploring mutable conserved sites and fatal non-conserved sites by random mutation of esterase from Sulfolobus tokodaii and subtilisin from Thermococcus kodakarensis
S.-i. Tanaka, M. Tsutaki, S. Yamamoto, H. Mizutani, R. Kurahashi, A. Hirata, *K. Takano, Int J Biol Macromol., 170,343-353 (2021), DOI: 10.1016/j.ijbiomac.2020.12.171

・Nanostructures, Thermoresponsiveness, and Assembly Mechanism of Hydrogel Microspheres during Aqueous Free-Radical Precipitation Polymerization
Y. Nishizawa, H. Minato, T. Inui, *T. Uchihashi, *D. Suzuki, Langmuir, 37,151–159 (2021), DOI:10.1021/acs.langmuir.0c02654

・Insertion loop‐mediated folding propagation governs efficient maturation of hyperthermophilic Tk‐subtilisin at high temperatures
R. Uehara, N. Dan, H. Amesaka, T. Yoshizawa, Y. Koga, S. Kanaya, K. Takano, H. Matsumura, and *S.-i. Tanaka, FEBS Lett., 595,452-461 (2021), DOI: 10.1002/1873-3468.14028

・Spectroscopic evidence of the salt-induced conformational change around the localized electric charges on the protein surface of fibronectin type III
C. Ota, Y. Fukuda, S.-i. Tanaka, and *K. Takano, Langmuir, 36, 14243-14254 (2020), DOI: 10.1021/acs.langmuir.0c02367

・Structural insights into the mechanism of rhodopsin phosphodiesteras
T. Ikuta, W. Shihoya, M. Sugiura, K. Yoshida, M. Watari, T. Tokano, K. Yamashita, K. Katayama, S. P. Tsunoda, T. Uchihashi, *H.Kandori and O. Nureki*, Nat. Commun., 11, 5605(2020), DOI: 10.1038/s41467-020-19376-7

・Novel Babesia bovis exported proteins that modify properties of infected red blood cells
H. Hakimi, T. J. Templeton, M. Sakaguchi, J. Yamagishi, S. Miyazaki, K. Yahata, T. Uchihashi, S.i. Kawazu, O. Kaneko, *M. Asada, PLoS pathogens, 16, e1008917 (2020), DOI: 110.1371/journal.ppat.1008917

・Distinct chemotactic behavior in the original Escherichia coli K-12 depending on forward-and-backward swimming, not on run-tumble movements.
Y. Kinosita, T. Ishida, M. Yoshida, R. Ito, YV. Morimoto, K. Goto, RM. Berry, T. Nishizaka, Y. Sowa, Sci. Rep., 10,15887 (2020), DOI: 10.1038/s41598-020-72429-1

・Thermo-Plasmonic Trapping of Living Cyanobacteria on a Gold Nanopyramidal Dimer Array: Implications for Plasmonic Biochips
S. Naka, T. Shoji, S. Fujii, K. Ueno, Y. Wakisaka, K. Murakoshi, T. Mizoguchi, H. Tamiaki and *Y. Tsuboi, ACS Appl. Nano Mater., 3,10067-10072 (2020), DOI: 10.1021/acsanm.0c02071

・Nanostructure-assisted optical tweezers for microspectroscopic polymer analysis
*T. Shoji and Y. Tsuboi, Polym J., 53,271-281 (2020), DOI: 10.1038/s41428-020-00410-w

・Optical Trapping of Polystyrene Nanoparticles on Black Silicon: Implications for Trapping and Studying Bacteria and Viruses
S. Komoto, T. Nagai, R. Takao, K. Ushiro, M. Matsumoto, *T. Shoji, D. P. Linklater, S. Juodkazis and *Y. Tsuboi, ACS Appl. Nano Mater., 3,9831-9841 (2020), DOI: 10.1021/acsanm.0c01901

・Microanalysis of Single Poly(N-isopropylacrylamide) Droplet Produced by an Optical Tweezer in Water: Isotacticity Dependence of Growth and Chemical Structure of the Droplet
K. Ushiro, *T. Shoji, M. Matsumoto, T.-A. Asoh, H. Horibe, Y. Katsumoto and *Y. Tsuboi, J. Phys. Chem. B, 124,8454-8463 (2020), DOI: 10.1021/acs.jpcb.0c06932

・Hybrid Rubisco with complete replacement of rice Rubisco small subunits by sorghum counterparts confers C4-plant-like high catalytic activity
*H. Matsumura, K. Shiomi, A. Yamamoto, Y. Taketani, N. Kobayashi, T. Yoshizawa, S.-i. Tanaka, H. Yoshikawa, M. Endo, and *H. Fukayama, Mol. Plant, 13,1570-1581 (2020), DOI: 10.1016/j.molp.2020.08.012

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

・Convergent evolution of processivity in bacterial and fungal cellulases
T. Uchiyama, T. Uchihashi, A. Nakamurad, H. Watanabec, S. Kanekoe, M. Samejimaa, and *K. Igarashi, Proc. Natl Acad. Sci. USA, 117, 19896-19903 (2020), DOI: 10.1073/pnas.2011366117

・Assembly mechanism of a supramolecular MS-ring complex to initiate bacterial flagellar biogenesis in Vibrio species
H. Terashima, K. Hirano, Y. Inoue, T. Tokano, A. Kawamoto, T. Kato, E. Yamaguchi, K. Namba, T. Uchihashi, S. Kojima and *M. Homma, J. Bacteriol., 202, e00236-20 (2020), DOI: 10.1128/JB.00236-20

・Crystal structure of a GH1 β-glucosidase from Hamamotoa singularis
R. Uehara, R. Iwamoto, S. Aoki, T. Yoshizawa, K. Takano, H. Matsumura, and *S.-i. Tanaka, Protein Sci., 29,2000-2008 (2020)

・ Microflow system promotes acetaminophen crystal nucleation
A. Nishigaki, M. Maruyama, M. Numata, C. Kanzaki, S.-i. Tanaka, H. Yoshikawa, M. Imanishi, M. Yoshimura, Y. Mori, and *K. Takano, Eng. Life Sci., 20, 395-401 (2020), DOI: 10.1002/elsc.202000021

・Coupling ion specificity of the flagellar stator proteins MotA1/MotB1 of Paenibacillus sp. TCA20.
S. Onoe, M. Yoshida, N. Terahara, Y. Sowa, Biomolecules, 10, E1078 (2020), DOI: 10.3390/biom10071078

・Direct visualization of the conformational change of FUS/TLS upon binding to promoter-associated non-coding RNA
N. Hamad, H. Watanabe, T. Uchihashi, R.Kurokawa, T. Nagata, and *M. Katahira, J. Chem. Commun., 56, 9134-9137 (2020), DOI:10.1039/D0CC03776A

・Structural Dynamics of a Protein Domain Relevant to the Water-Oxidizing Complex in Photosystem II as Visualized by High-Speed Atomic Force Microscopy
T. Tokano, Y. Kato, S. Sugiyama, *T. Uchihashi, and T. Noguchi, J. Phys. Chem. B., 124, 5847-5857 (2020), DOI: 10.1021/acs.jpcb.0c03892

・Highly active enzymes produced by directed evolution with stability-based selection
R. Kurahashi, S.-i. Tanaka, and *K. Takano, Enzyme Microb. Technol., 140, 109626 (2020), DOI: 10.1016/j.enzmictec.2020.109626

・Thermoresponsive structural changes of single poly (N-isopropyl acrylamide) hydrogel microspheres under densely packed conditions on a solid substrate
H. Minato, Y. Nishizawa, *T. Uchihashi, *D. Suzuki, Polym.J., 52, 1137–1141 (2020), DOI: 10.1038/s41428-020-0372-3

・Schizorhodopsins: A family of rhodopsins from Asgard archaea that function as light-driven inward H+ pumps
*K. Inoue, S. P. Tsunoda, M. Singh, S. Tomida, S. Hososhima, M. Konno, R. Nakamura, H. Watanabe, P. A. Bulzu, H. L. Banciu, A. Ş. Andrei, T. Uchihashi, R. Ghai, O. Béjà and *H. Kandori, Science Advances, 6, eaaz2441 (2020), DOI: 10.1126/sciadv.aaz2441

・Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy
H. Konno, T. Watanabe-Nakayama, T. Uchihashi, M. Okuda, L. Zhu, N. Kodera, Y. Kikuchi, T. Ando, *H. Taguchi, Proc. Natl. Acad. of Sci. USA, 117, 831-7836, DOI: 110.1073/pnas.1916452117

・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.

・Plasmonic Manipulation of DNA using a Combination of Optical and Thermophoretic Forces:
Separation of Different-Sized DNA from Mixture Solution
T. Shoji, K. Itoh, J. Saitoh, N. Kitamura, T. Yoshii, K. Murakoshi, Y. Yamada, T. Yokoyama, H. Ishihara, *Y. Tsuboi, Sci. Rep., 10, 3349 (2020), DOI: 10.1038/s41598-020-60165-5

・Single-molecule imaging analysis reveals the mechanism of a high-catalytic-activity mutant of chitinase A
from Serratia marcescens
A. Visootsat, A. Nakamura, P. Vignon, H. Watanabe, T. Uchihashi and *R. Iino, J. Biol. Chem., 295, 1915-1925 (2020), DOI: 10.1074/jbc.RA119.012078

・High pressure inhibits signaling protein binding to the flagellar motor
and bacterial chemotaxis through enhanced hydration
H. Hata, Y. Nishihara, M. Nishiyama, Y. Sowa, I. Kawagishi, *A. Kitao, Sci. Rep., 10, 2351 (2020), DOI: 10.1038/s41598-020-59172-3

・Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli
T. Yoshizawa, J. Fujita, H. Terakado, M. Ozawa, N. Kuroda, S. Tanaka, R. Uehara, *H. Matsumura, Acta Crystallogr F Struct Biol Commun., 76, 86-93 (2020), DOI: 10.1107/S2053230X2000076X

・Supramolecular tholos-like architecture constituted by archaeal proteins without functional annotation
M. Yagi-Utsumi, A. Sikdar, C. Song, J. Park, R. Inoue, H. Watanabe, R. N. Burton-Smith, T. Kozai, T. Suzuki, A. Kodama, K. Ishii, H. Yagi, T. Satoh, S. Uchiyama, T. Uchihashi, K. Joo, J. Lee, M. Sugiyama, K. Murata and *K. Kato, Sci. Rep., 10,1540 (2020), DOI: 10.1038/s41598-020-58371-2

・Rad50 zinc hook functions as a constitutive dimerization module interchangeable with SMC hinge
H. Tatebe, C. T. Lim, H. Konno, K. Shiozaki, A. Shinohara, *T. Uchihashi, *A. Furukohri, Nat. Commun., 11, 370 (2020), DOI: 10.1038/s41467-019-14025-0

・Spectroscopic Signature of the Steric Strains
in an Escherichia coli RNase HI Cavity-Filling Destabilized Mutant Protein
C. Ota, H. Suzuki, S. Tanaka, *K. Takano, J Phys Chem B., 124, 91-100 (2020), DOI: 10.1021/acs.jpcb.9b09852

・Thermoresponsive Micellar Assembly Constructed from a Hexameric Hemoprotein Modified
with Poly(N-isopropylacrylamide) toward an Artificial Light-Harvesting System
S. Hirayama, *K. Oohora, *T. Uchihashi, *T. Hayashi, J. Am. Chem. Soc., 142, 1822-1831 (2020), DOI: 10.1021/jacs.9b10080

・On-Membrane Dynamic Interplay between Anti-GM1 IgG Antibodies and Complement Component C1q
*S. Yanaka, R. Yogo#, H. Watanabe#, Y. Taniguchi, T. Satoh, N. Komura, H. Ando, H. Yagi, N. Yuki, *T. Uchihashi, *K. Kato, International Journal of Molecular Sciences, 21, 147 (2020), DOI: 10.3390/ijms21010147

・Construction of a Hexameric Hemoprotein Sheet and Direct Observation of Dynamic Processes of Its Formation
*K. Oohora, S. Hirayama, *T. Uchihashi and *T. Hayashi, Chem. Lett., 49, 186-190 (2020), DOI: 10.1246/cl.190855,

・Regular Assembly of Polymer Nanoparticles by Optical Trapping Enhanced with a Random Array of
Si Needles for Reconfigurable Photonic Crystals in Liquid
*I. Hanasaki, T. Shoji, *Y. Tsuboi, ACS Appl. Nano Mater., 2, 7637-7643 (2019), DOI: 10.1021/acsanm.9b01707

・Crystal structure of heliorhodopsin
W. Shihoya, K. Inoue, M. Singh, M. Konno, S. Hososhima, K. Yamashita, K. Ikeda, A. Higuchi, T. Izume, S. Okazaki, M. Hashimoto, R. Mizutori, S. Tomida, Y. Yamauchi, R. Abe-Yoshizumi, K. Katayama, S. P. Tsunoda, M. Shibata, Y. Furutani, A. Pushkarev, O. Béjà, T. Uchihashi, *H. Kandori and *O. Nureki, Nature, 574, 132-136 (2019), DOI: 10.1038/s41586-019-1604-6

・Nanotraffic Lights: Rayleigh Scattering Microspectroscopy of Optically Trapped Octahedral Gold Nanoparticles
*T. Shoji, M. Tamura, T. Kameyama, T. Iida, Y. Tsuboi, T. Torimoto, J. Phys. Chem. C, 37, 23096-23102 (2019), DOI: 10.1021/acs.jpcc.9b05077

・The Fab portion of immunoglobulin G contributes to its binding to Fcγ receptor III
R. Yogo, Yuki Yamaguchi, H. Watanabe, H. Yagi, T. Satoh, M. Nakanishi, M. Onitsuka, T. Omasa, M. Shimada, T. Maruno, Tetsuo Torisu, S. Watanabe, D. Higo, T. Uchihashi, S. Yanaka, S. Uchiyama and *K. Kato,Sci. Rep. , 9,11957 (2019), DOI: 10.1038/s41598-019-48323-w

・Protein Uptake into Individual Hydrogel Microspheres Visualized by High-Speed Atomic Force Microscopy
S. Matsui, K. Hosho, H. Minato, *T. Uchihashi, *D. Suzuki,
Chem. Commun. ,55,10064-10067 (2019),DOI: 10.1039/C9CC05116C

・Dynamics of Inter-Molecular Interactions Between Single Aβ42 Oligomeric and Aggregate Species
by High-Speed Atomic Force Microscopy
L. Feng, H. Wantanabe, P. Molino, G. Wallace, S. Lam Phung, T. Uchihashi, *M. Higgins, Journal of Molecular Biology ,431, 2687-2699 (2019), DOI: 10.1016/j.jmb.2019.04.044

・Investigation of Ag and Cu Filament Formation inside the Metal Sulfide Layer of an Atomic switch based on Point Contact Spectroscopy
A. Aiba, R. Koizumi, T. Tsuruoka, K. Terabe, K. Tsukagoshi, S. Kaneko, S. Fujii, T. Nishino, *M. Kiguchi,
ACS Appl. Mater. Inter., 11, 27178-27182 (2019), DOI:10.1021/acsami.9b05523

・High-speed AFM reveals accelerated binding of agitoxin-2 to a K+ channel by induced fit
*A. Sumino, T. Sumikama, *T. Uchihashi, *S. Oiki,
Science Advances, 5,eaax0495(2019), DOI:10.1021/acsami.9b05523

・Identifying the Molecular Adsorption Site of a Single Molecule Junction
Through Combined Raman and Conductance Studies
S. Kaneko, E. Montes, S. Suzuki, S. Fujii, T. Nishino, K. Tsukagoshi, K. Ikeda, H. Kano, H. Nakamura, H. Vázquez, *M. Kiguchi, Chem. Sci., 10, 6261–6269 (2019),DOI: 10.1039/C9SC00701F

Effect of Bias Voltage on Single Molecule Junction Investigated by Surface Enhanced Raman Scattering
K. Yasuraoka, S. Kaneko, S. Fujii, T. Nishino, K. Tsukagoshi, G. Juhasz, *M. Kiguchi, J. Phys. Chem. C, 123, 15267−15272 (2019), DOI 10.1021/acs.jpcc.9b02286

・Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits
T. Sekiguchi, T. Satoh, E. Kurimoto, C. Son, T. Kozai, H. Watanabe, K. Ishii, H. Yagi, S. Yanaka S. Uchiyama, T. Uchihashi, K. Murata, *K. Kato
International Journal of Molecular Sciences, 202608 (2019), DOI: 0.3390/ijms20092308

・Non‐Thermoresponsive Decanano‐sized Domains in Thermoresponsive Hydrogel Microspheres
Revealed by Temperature‐Controlled High‐Speed Atomic Force Microscopy
Y. Nishizawa, S. Matsui, K. Urayama, T. Kureha, M. Shibayama, *T. Uchihashi and *D. Suzuki, Angew. Chem. Int. Ed. , 58,8809-8813 (2019),DOI:10.1002/anie.201903483

・Activity-stability trade-off in random mutant proteins
R. Kurahashi, S. Tanaka, *K. Takano, J Biosci Bioeng. , 128, 405-409 (2019),
DOI: 10.1016/j.jbiosc.2019.03.017.

・Construction of a Quadrangular Tetramer and a Cage-Like Hexamer
from Three-Helix Bundle-Linked Fusion Proteins
T. Miyamoto, Y. Hayashi, K. Yoshida, H. Watanabee, T. Uchihashi, K. Yonezawa, N. Shimizu, H. Kamikubo, *S. Hirota, ACS Synth. Biol.,81112-1120 (2019), DOI: 10.1021/acssynbio.9b00019

・Hydrogel Microellipsoids that Form Robust String‐Like Assemblies at the Air/Water Interface
K. Honda, Y. Sazuka, K. Iizuka, S. Matsui, T. Uchihashi, T. Kureha, M. Shibayama, T. Watanabe, *D. Suzuki,
Angewandte Chemie International Edition, 58, 7294-7298 (2019), DOI:10.1002/anie.201901611

書籍/総説・解説
・ Recent advances in bioimaging with high-speed atomic force microscopy
*T. Uchihashi, C. Ganser, Biophysical Reviews, 12, 363-369 (2020), DOI:10.1039/D0NR01121E

・ Diffracted X-ray tracking method for recording single-molecule protein motions
*H. Shimizu, Biochim Biophys Acta Gen Subj. , 1864, 129361 (2020), DOI: 10.1016/j.bbagen.2019.05.004.

・ 高速原子間力顕微鏡による生体・合成高分子の動態イメージング
*内橋貴之, 高分子, 68, 564-568 (2019)

・"ナノ構造体を用いる光ピンセットの開発”, 東海林竜也, 分析化学, 68, 315-324 (2019), DOI: 10.2116/bunsekikagaku.68.315

・「図説 表面分析ハンドブック」, 日本表面真空学会 (Ed.) ,
“高速原子間力顕微鏡”, 内橋貴之, 23. 8, 朝倉書店, (2020), ISBN: 978-4-254-20170-3　C3050

・「膜タンパク質工学ハンドブック」, 津本浩平・浜窪隆雄 (Eds) ,
“高速原子間力顕微鏡によるタンパク質の構造ダイナミクス解析” , 内橋貴之, エヌ・ティー・エス, (2020), 第1編 第2章15, ISBN: 978-4-86043-537-0 C3045

・「自己修復材料、自己組織化、形状記憶材料の開発と応用事例」,
“高速原子間力顕微鏡による分子の自己組織化過程のリアルタイムでの観察” , 内橋貴之, エヌ・ティー・エス, 357-364 (2020), ISBN: 978-4-86104-781-7