List of Publications

Recent Publications

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2025
1.	Goro Nishide, Keesiang Lim, Akiko Kobayashi, Yujia Qiu, Masaharu Hazawa, Toshio Ando, Yuki Okada, Richard W. Wong , Spatiotemporal Dynamics of Protamine-DNA Condensation Revealed by High-Speed Atomic Force Microscopy. Nucleic Acids Res. (in press) DOI: 10.1093/nar/gkaf152
2.	Muhammad Isman Sandira, Keesiang Lim, Takeshi Yoshida, Elma Sakinatus Sajidah, Shinnosuke Narimatsu, Reon Imakawa, Kota Yoshimura, Goro Nishide, Yujia Qiu, Azuma Taoka, Masaharu Hazawa, Toshio Ando, Rikinari Hanayama, Richard W. Wong, Nanoscopic Profiling of Small Extracellular Vesicles via High-Speed Atomic Force Microscopy (HS-AFM) Videography. J. Extracell. Vesicles 4:e270050 (2025). DOI: 10.1002/jev2.70050
3.	Daiki Muramatsu, Takahiro Watanabe-Nakayama, Mayumi Tsuji, Kenichi Umeda, Sadao Hikishima, Hiroto Nakano, Yasuhiro Sakashita, Tokuhei Ikeda, Hiroki Konno, Noriyuki Kodera, Toshio Ando, Moeko Noguchi-Shinohara, Kenjiro Ono, ALZ-801 prevents amyloid β-protein assembly and reduces cytotoxicity: A preclinical experimental study. FASEB 39, e70382 (2025). DOI: 10.1096/fj.202402622R
4.	Mingbo Qu, Lin Kong, Pengfei Li, Aijing Zhang, Toshio Ando, Qing Yang, High-speed atomic force microscopy reveals opposite traffic of processive chitinases impairs α-chitin biodegradation. Carbohydrate Polymers 352, 123176 (2025). DOI: 10.1016/j.carbpol.2024. 123176
2024
1.	Mingbo Qu, Xiaoxi Guo, Toshio Ando, Qing Yang, Functional role of carbohydrate-binding modules in multi-modular chitinase OfChtII. J. Biol. Chem. 300(9), 107622 (2024) . DOI: 10.1016/j.jbc.2024.107622 Open Access
2.	Hidenori Homma, Kien Xuan Ngo, Yuki Yoshioka, Hikari Tanaka, Maiko Inotsume, Kyota Fujita, Toshio Ando, and Hitoshi Okazawa, PQBP3/NOL7 is an intrinsically disordered protein. Biochem. Biophys. Res. Commun. 736, 150453 (2024). DOI: 10.1016/j.bbrc.2024.150453
3.	Yuki Yoshioka, Yong Huang, Xiaocen Jin, Kien Xuan Ngo, Tomohiro Kumaki, Meihua Jin, Saori Toyoda, Sumire Takayama, Kyota Fujita, Hidenori Homma, Toshio Ando, Hikari Tanaka, Hitoshi Okazawa, PQBP3/NOL7 prevents senescence by suppressing PSME3-mediated proteasomal Lamin B1 degradation. EMBO J. 43, 3968-3999 (2024). DOI: 10.1038/s44318-024-00192-4 Open Access
4.	Carlero, D., Fukuda, S., Bocanegra, R., Ando, T., Martín Benito, J., Ibarra, B. Conformational dynamics of influenza A virus ribonucleoprotein complexes during RNA synthesis. ACS Nano 18, 19518-19527. DOI: 10.1021/acsnano.4c01362 Open Access
5.	Toshio Ando, Shingo Fukuda, Kien Xuan Ngo, Holger Flechsig. High-speed atomic force microscopy for filming protein molecules in dynamic action. Annu. Rev. Biophys. 53, 19-39 (2024) DOI: 10.1146/annurev-biophys-030722-113353 Open Access
6.	Yujia Qiu, Elma Sakinatus Sajidah, Sota Kondo, Shinnosuke Narimatsu, Muhammad Isman Sandira, Yoshiki Higashiguchi, Goro Nishide, Azuma Taoka, Masaharu Hazawa, Yuka Inaba, Hiroshi Inoue, Ayami Matsushima, Yuki Okada, Mitsutoshi Nakada, Toshio Ando, Keesiang Lim, and Richard W. Wong, An efficient method for isolating and purifying nuclei from mice brain for single-molecule imaging using high-speed atomic force microscopy. Cells 13, 279 (2024). DOI: 10.3390/cells13030279 Open Access
2023
1.	Shingo Fukuda & Toshio Ando. Technical advances in high-speed atomic force microscopy. Biophys. Rev. 15, 2045-2058 (2023). DOI: 10.1007/s12551-023-01171-5
2.	Kazusa Takeda, Holger Flechsig, Ikumi Muro, Romain Amyot, Fuminori Kobayashi, Noriyuki Kodera, Toshio Ando, and Hiroki Konno, Structural dynamics of E6AP E3 ligase HECT domain and involvement of a flexible hinge loop in the ubiquitin chain synthesis mechanism. Nano Lett. 23, 11940-11948 (2023). DOI: 10.1021/acs.nanolett.3c04150
3.	G. Nishide, K. Lim, M. Tamura, A. Kobayashi, Q. Zhao, M. Hazawa, T. Ando, N. Nishide, R. W. Wong. Nonoscopic elucidation of spontaneous self-assembly of severe acute respiratory syndrome coronavirus 2 (SARS-COV-2) open reading frame 6 (ORF6) protein. J. Phys. Chem. Lett. 14, 8385-8396 (2023). DOI 10.1021/acs.jpclett.3c01440
4.	Holger Flechsig, Toshio Ando, Protein dynamics by the combination of high-speed AFM and computational modeling. Curr. Opin. Strcut. Biol. 80, 102591 (2023). DOI: 10.1016/j.sbi.2023.102591 (Link)
5.	Keesiang Lim, Goro Nishide, Elma Sakinatus Sajidah, Tomoyoshi Yamano, Yujia Qiu, Takeshi Yoshida, Akiko Kobayashi, Masaharu Hazawa, Toshio Ando, Rikinari Hanayama, and Richard W, Nanoscopic assessment of anti-SARS-CoV-2 spike neutralizing antibody using high-speed AFM. Nano Lett. 23, 619-628. DOI: 10.1021/acs.nanolett.2c04270
6.	Xiaocen Jin, Hikari Tanaka, Meihua Jin, Kyota Fujita, Hidenori Homma, Maiko Inotsume, Huan Yong, Kenichi Umeda, Noriyuki Kodera, Toshio Ando and Hitoshi Okazawa, PQBP5/NOL10 maintains and anchors the nucleolus under physiological and osmotic stress conditions. Nat. Commnun. 14, article number 9 (2023) PDF (Link) Open Access DOI: 10.1038/s41467-022-35602-w
7.	Y. Hayakawa, M. Takaine, K. X. Ngo, T. Imai, M. D. Yamada, A. B. Behjat, K. Umeda, K. Hirose, A. Yurtsever, N. Kodera , K. Tokuraku, O. Numata, T. Fukuma, T. Ando, K. Nakano, T. Q. P. Uyeda, Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II. Life Sci. Alliance 6, e202201469 (2023). (Link) Open Access DOI: 10.26508/lsa.202201469
2022
1.	Tomonori Ogane, Daisuke Noshiro, Toshio Ando, Atsuko Yamashita, Yuji Sugita, Yasuhiro Matsunaga, Development of hidden Markov modeling method for molecular orientations and structure estimation from high-speed atomic force microscopy time-series images. PLOS Computational Biology 18(12):e1010384 (2022) Open Access DOI: 10.1371/journal.pcbi.1010384
2.	Toshio Ando, Functional implications of dynamic structures of intrinsically disordered proteins revealed by high-speed AFM imaging. Biomolecules 12, 1876 (2022). (PDF) (Link) Open Access DOI: 10.3390/biom12121876
3.	E. S. Sajidah, K. Lim, T. Yamano, G. Nishide, Y. Qiu, T. Yoshida, H. Wang, A. Kobayashi, M. Hazawa, F. R. P. Dewi, R. Hanayama, T. Ando, R. W. Wong, Spatiotemporal tracking of small extracellular vesicle nanotopology in response to physicochemical stresses revealed by HS-AFM. J. Extracell. Vesicles 11, 12275 (2022). (Link) Open Access DOI: 10.1002/jev2.12275
4.	N. Kodera, T. Ando, Guide to studying intrinsically disordered proteins by high-speed atomic force microscopy. Methods 207, 44-56 (2022). DOI: 10.1016/j.ymeth.2022.08.008 (PDF) (Link)
5.	N. Kodera, T. Ando, Visualization of intrinsically disordered proteins by high-speed atomic force microscopy. Curr. Opin. Struct. Biol. 72, 260-266 (2022). DOI: 10.1016/j.sbi.2021.11.014 (Link)
6.	Masahiro Shimizu, Chihiro Okamoto, Kenichi Umeda, Shinji Watanabe, Toshio Ando, and Noriyuki Kodera^,"An ultrafast piezoelectric Z-scanner with a resonance frequency above 1.1 MHz for high-speed atomic force microscopy. Rev. Sci. Instrum. 93, 013701 (2022). DOI: 10.1063/5.0072722
7.	^{Sourav Maity, Gianluca Trinco, Pedro Buzon, Zaid R. Anshari, Noriyuki Kodera , Kien Xuan Ngo , Toshio Ando , Dirk J. Slotboom, and Wouter H. Roos, High-speed atomic force microscopy reveals a three-state elevator mechanism in the citrate transporter CitS. PNAS 119, e2113927119 (2022) DOI: 10.1073/pnas.2113927119}
8.	Bikash R. Sahoo; Christopher L. Souders; Takahiro W. Nakayama; Zhou Deng; Hunter Linton; Saba Suladze; Magdalena I. Ivanova; Bernd Reif; Toshio Ando; Christopher Martyniuk; Ayyalusamy Ramamoorthy, Conformational Tuning of Amylin by Charged Styrene-maleic-acid Copolymers. J. Mol. Biol. 434, 167385 (2022). DOI: 10.1016/j.jmb.2021.167385
9.	Yuanshu Zhou, Linhao Sun,Shinji Watanabe,and Toshio Ando, Recent Advances in the Glass Pipet: from Fundament to Applications. Anal. Chem. 94, 324-335 (2022). DOI: 10.1021/acs.analchem.1c04462
10.	Dong Wang, Linhao Sun, Satoru Okuda, Daisuke Yamamoto, Mizuho Nakayama, Hiroko Oshima, Hideyuki Saito, Yuta Kouyama, Koshi Mimori, Toshio Ando, Shinji Watanabe, Masanobu Oshima, Nano-scale physical properties characteristic to intestinal cancer cells identified by high speed-scanning ion conductance microscope . Biomaterials 280, 121256 (2022). DOI: 10.1016/j.biomaterials.2021.121256
2021
1.	Keesiang Lim, Goro Nishide, Takeshi Yoshida, Takahiro Watanabe-Nakayama, Akiko Kobayashi, Masaharu Hazawa, Rikinari Hanayama, Toshio Ando, Richard W. Wong, Millisecond dynamic of SARS-CoV-2 spike and its interaction with small extracellular vesicle (sEV)-based decoy. J. Extracell. Vesicles 10, e12170 (2021). DOI: 10.1002/jev2.12170 (Open access)
2.	Umeda K., Okamoto C., Shimizu M., Watanabe S., Ando T., Kodera N. Architecture of zero-latency ultrafast amplitude detector for high-speed atomic force microscopy. Appl. Phys. Lett. 119, 181602 (2021). DOI: 10.1063/5.0067224
3.	Toyonaga T, Kato T, Kawamoto A, Kodera N, Hamaguchi T, Tahara YO, Ando T, Namba K, Miyata M. Chained structure of dimeric F₁-like ATPase in Mycoplasma mobile gliding machinery. mBio 12, e01414-21 (2021). Open Access DOI: 10.1128/mBio.01414-21 (Link)
4.	Ando T. Biophysical reviews top five: atomic force microscopy in biophysics. Biophys. Rev. 13:455-458 (2021). (PDF) Open Access DOI: 10.1007/s12551-021-00820-x
5.	Kobayashi K, Kodera N, Kasai T, Tahara YO, Toyonaga T, Mizutani M, Fujiwara I, Ando T, Miyata M. (2021) Movements of Mycoplasma mobile Gliding Machinery Detected by High-Speed Atomic Force Microscopy. (2021) mBio. 12(3):e0004021. doi: 10.1128/mBio.00040-21.
6.	Arin Marchesi, Kenichi Umeda, Takumi Komekawa, Takeru Matsubara, Holger Flechsig, Toshio Ando, Shinji Watanabe, Noriyuki Kodera & Clemens M. Franz. An ultra-wide scanner for large-area high-speed atomic force microscopy with megapixel resolution. Sci. Rep. 11, 13003 (2021). DOI: 10.1038/s41598-021-92365-y (Link) Open Access
7.	Goro Nishide, Keesiang Lim, Mahmoud Shaaban Mohamed, Akiko Kobayashi, Masaharu Hazawa,　Takahiro Watanabe-Nakayama, Noriyuki Kodera, Toshio Ando, and Richard W. Wong. High-speed atomic force microscopy reveals spatiotemporal dynamics of histone protein H2A involution by DNA inchworming. J. Phys. Chem. Lett. 12, 3837−3846 (2021) . DOI: 10.1021/acs.jpclett.1c00697
8.	Shingo Fukuda, Toshio Ando, Faster high-speed atomic force microscopy for imaging of biomolecular processes. Rev. Sci. Instrum. 92, 033705 (2021). DOI: 10.1063/5.0032948 (PDF) (Link) Open Access
9.	Noriyuki Kodera, Daisuke Noshiro, Sujit K. Dora, Tetsuya Mori, Johnny Habchi, David Blocquel, Antoine Gruet, Marion Dosnon, Edoardo Salladini, Christophe Bignon, Yuko Fujioka, Takashi Oda, Nobuo N. Noda, Mamoru Sato, Marina Lotti, Mineyuki Mizuguchi, Sonia Longhi, Toshio Ando, Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. Nature Nanotechnology 16, 181-189 (2021). DOI:10.1038/s41565-020-00798-9 (Link)
10.	Oleg S. Matusovsky, Noriyuki Kodera, Caitlin MacEachen, Toshio Ando, Yu-Shu Cheng, Dilson E. Rassier , Millisecond conformational dynamics of skeletal myosin II power stroke studied by high-speed atomic force microscopy. ACS Nano. 15, 2229-2239 (2021) DOI: 10.1021/acsnano.0c06820
2020
1.	Kazuki Shigyou, Linhao Sun, Riku Yajima, Shohei Takigaura, Masashi Tajima, Hirotoshi Furusho, Yousuke Kikuchi, Keisuke Miyazawa, Takeshi Fukuma, Azuma Taoka, Toshio Ando, and Shinji Watanabe, Geometrical characterization of glass nanopipettes with sub-10 nm pore diameter by transmission electron microscopy. Analytical Chemistry 92(23), 15388-15393 (2020) DOI: 10.1021/acs.analchem.0c02884
2.	Yuki Kawasaki, Hirotaka Ariyama, Hajime Motomura, Daisuke Fujinami, Daisuke Noshiro, Toshio Ando and Daisuke Kohda, Two-state exchange dynamics in membrane-embedded oligosaccharyltransferase observed in real-time by high-speed AFM. J. Mol. Biol. 432, 5951-5965 (2020). DOI: 10.1016/j.jmb.2020.09.017
3.	Mingbo Qu, Takahiro Watanabe-Nakayama, Shaopeng Sun, Kenichi Umeda, Xiaoxi Guo, Yuansheng Liu, Toshio Ando, and Qing Yang, High-speed atomic force microscopy reveals factors affecting the processivity of chitinases during interfacial enzymatic hydrolysis of crystalline chitin. ACS Catal. 10, 13606−13615 (2020). DOI: 10.1021/acscatal.0c02751
4.	Keesiang Lim, Noriyuki Kodera, Hanbo Wang, Mahmoud Shaaban Mohamed, Masaharu Hazawa, Akiko Kobayashi, Takeshi Yoshida, Rikinari Hanayama, Seiji Yano, Toshio Ando, and Richard W. Wong, High-speed AFM reveals molecular dynamic of human influenza A hemagglutinin and its interaction with exosomes. Nano Lett. 20, 6320−6328 (2020). DOI: 10.1021/acs.nanolett.0c01755
5.	Mahmoud Shaaban Mohamed, Masaharu Hazawa, Akiko Kobayashi, Laurent Guillaud, Takahiro Watanabe-Nakayama, Mizuho Nakayama, Hanbo Wang, Noriyuki Kodera, Masanobu Oshima, Toshio Ando, Richard W. Wong, Spatiotemporally tracking of nano-biofilaments inside the nuclear pore complex core. Biomaterials 256, 120198 (2020). DOI: 10.1016/j.biomaterials.2020.120198
6.	Takahiro Watanabe-Nakayama, Maika Nawa, Hiroki Konno, Noriyuki Kodera, Toshio Ando, David B Teplow, and Kenjiro Ono, Self- and cross-seeding on α-synuclein fibril growth kinetics and structure observed by high-speed atomic force microscopy. ACS Nano 14, 9979-9989 (2020). DOI: 10.1021/acsnano.0c03074
7.	T. Ando, "Studies on the impellers generating force in muscle", Biophysical Reviews 12, 767-769 (2020). Biophysics of Human Anatomy and Physiology - a Special Issue in honor of Prof. Cristobal dos Remedios on the occasion of his 80th birthday. DOI: 10.1007/s12551-020-00705-5 Link
8.	Ping Zhang, Xiaoguo Liu, Pi Liu, Fei Wang, Hirotaka Ariyama, Toshio Ando, Jianping Lin, Jun Hu, Lihua Wang, Bin Li, Chunhai Fan "Capturing transient antibody conformations with DNA origami epitopes", Nat. Commun. 11, Article number: 3114 (2020). DOI: 10.1038/s41467-020-16949-4
9.	Yousuke Kikuchi, Nozomu Obana, Masanori Toyofuku, Noriyuki Kodera, Takamitsu Soma, Toshio Ando, Yoshihiro Fukumori, Nobuhiko Nomura and Azuma Taoka, "Diversity of physical properties of bacterial extracellular membrane vesicles revealed through atomic force microscopy phase imaging", Nanoscale 12, 7950-7959 (2020). DOI: 10.1039/c9nr10850e
10.	Hiroki Konno, Takahiro Watanabe-Nakayamaa, Takayuki Uchihashib,c, Momoko Okuda, Liwen Zhue, Noriyuki Kodera, Yousuke Kikuchi, Toshio Ando, and Hideki Taguchi, Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy, Proc. Natl. Acad. Sci. USA 117 (14) 7831-7836 (2020) .DOI: 10.1073/pnas.1916452117
11.	Yuko Fujioka, Jahangir Md. Alam, Daisuke Noshiro, Kazunari Mouri, Toshio Ando, Yasushi Okada, Alexander I. May, Roland L. Knorr, Kuninori Suzuki, Yoshinori Ohsumi & Nobuo N. Noda, Phase separation organizes the site of autophagosome formation, Nature 678, 301-305 (2020). DOI: 10.1038/s41586-020-1977-6
12.	Kee Siang Lim, Mahmoud Shaaban Mohamed, Hanbo Wang, Hartono, Masaharu Hazawa, Akiko Kobayashi, Dominic Chih-Cheng Voon, Noriyuki Kodera, Toshio Ando, Richard W. Wong, "Direct visualization of avian influenza H5N1 Hemagglutinin precursor and its conformational change by high-speed atomic force microscopy", BBA - General Subjects 1864: 129313 (7 pp) DOI: 10.1016/j.bbagen.2019.02.015 (Link)
13.	Takayuki Umakoshi, Shingo Fukuda, Ryota Iino, Takayuki Uchihashi, Toshio Ando, "High-speed near-field fluorescence microscopy combined with high-speed atomic force microscopy for biological studies", BBA-Gneral Subjeccts 1864: 129325 (10 pp) (2020) DOI:10.1016/j.bbagen.2019.03.011 (Link) PP
14.	T. Ando, "Biophysics in Kanazawa University", Biophysical Reviews 12, 249–251. DOI: 10.1007/s12551-020-00635-2
2019
1.	S. Watanabe, S. Kitazawa, L. Sun, N. Kodera, T. Ando, "Development of high-speed ion conductance microscopy", Rev. Sci. Instrum. 90, 123704 (2019). DOI: 10.1063/1.5118360. Scilight
2.	Yuhei Araiso, Akihisa Tsutsumi, Jian Qiu, Kenichiro Imai,Takuya Shiota, Jiyao Song, Caroline Lindau, Lena-Sophie Wenz, Haruka Sakaue,Kaori Yunoki, Shin Kawano, Junko Suzuki, Marilena Wischnewski, Conny Schütze, Hirotaka Ariyama, Toshio Ando, Thomas Becker,Trevor Lithgow, Nils Wiedemann, Nikolaus Pfanner, Masahide Kikkawa & Toshiya Endo, "Structure of the mitochondrial import gate reveals distinct preprotein paths", Nature 575: 395-401 (2019) DOI: 10.1038/s41586-019-1680-7 (Link)
3.	Linhao Sun, Kazuki Shigyou, Toshio Ando, and Shinji Watanabe, "Thermally Driven Approach To Fill Sub-10-nm Pipettes with Batch Production", Anal. Chem.91: 14080−14084 (2019). DOI:10.1021/acs.analchem.9b03848 (Link)
4.	Toshio Ando, High-speed atomic force microscopy, Curr. Opin. Chem. Biol. 51, 105-112 (2019) DOI: 10.1016/j.cbpa.2019.05.010 (Link)
5.	Yumi Inoue, Yuya Ogawa, Miki Kinoshita, Naoya Terahara, Masafumi Shimada, Noriyuki Kodera, Toshio Ando, Keiichi Namba, Akio Kitao, Katsumi Imada*, and Tohru Minamino, "Structural insights into the substrate specificity switch mechanism of the type III protein export apparatus", Structure 27:965-976 (2019). DOI:10.1016/j.str.2019.03.017 (Link)
6.	Bikash R. Sahoo, Takuya Genjo, Takahiro Watanabe-Nakayama, Andrea K. Stoddard, Toshio Ando, Kazuma Yasuhara, Carol A. Fierke, Ayyalusamy Ramamoorthy, "Cationic polymethacrylate-copolymer acts as an agonist for β-amyloid and antagonist for amylin fibrillation", Chem. Sci. 10: 3976-3986 (2019). DOI: 10.1039/C8SC05771K (PDF)
7.	Mikito Owa, Takayuki Uchihashi, Haruaki Yanagisawa, Takashi Yamano, Hiro Iguchi, Hideya Fukuzawa, Ken-ichi Wakabayashi, Toshio Ando, and Masahide Kikkawa, Inner lumen proteins stabilize doublet microtubules in cilia and flagella, Nat. Commun. 10, article no. 1143 (2019). DOI: 10.1038/s41467-019-09051-x. Open Access (PDF)
8.	Shintaro Maruyama, Kano Suzuki, Motonori Imamura, Hikaru Sasaki, Hideyuki Matsunami, Kenji Mizutani, Yasuko Saito, Fabiana L. Imai, Yoshiko Ishizuka-Katsura, Tomomi Kimura-Someya, Mikako Shirouzu, Takayuki Uchihashi, Toshio Ando, Ichiro Yamato & Takeshi Murata, Metastable asymmetrical structure of shaftless V₁ motor, Sci. Adv. 5(1), eaau8149 (2019). DOI: 10.1126/sciadv.aau8149 Open Access (PDF)
9.	S. Kori, L. Ferry, S. Matano, T. Jimenji, N. Kodera, T. Tsusaka, R. Matsumura, T. Oda, M. Sato, N. Dohmae N, T. Ando, Y. Shinkai, P. A. Defossez and K. Arita, "Structure of the UHRF1 Tandem Tudor Domain bound to a methylated non-histone protein, LIG1, reveals rules for binding and regulation". Structure 27, 485-496 (2019). DOI: 10.1016/j.str.2018.11.012. (PDF)
10.	E. Sone, D. Noshiro, Y. Ikebuchi, M. Nakagawa, M. Khan, Y. Tamura, M. Ikeda, M. Oki, R. Murali, T. Fujimori, T. Yoda, M. Honma, H. Suzuki, T. Ando, and K. Aoki, "The clustering-induction of RANKL molecules could stimulate early osteroblast differentiation", Biophys. Biochem. Res. Commun. 509: 435-440 (2019). DOI: 10.1016/j.bbrc.2018.12.093 (PDF)
11.	T. Haruyama, Y. Sugano, N. Kodera, T. Uchihashi, T. Ando, Y. Tanaka, H. Konno, and T. Tsukazaki, "Single-unit imaging of membrane protein-embedded nanodiscs from two oriented sides by high-speed atomic force microscopy", Structure 27, 152-160 (2019). DOI: 10.1016/j.str.2018.09.005. (PDF)
2018
1.	T. Brouns, H. De. Keersmaecker, S. Konrad, N. Kodera, T. Ando, J. Lipfert, S. De Feyter and W. Vanderlinden, "Free energy landscape and dynamics of supercoiled DNA by high-speed tomic force microscopy", ACS Nano 12 (12), 11907–11916 (2018). DOI: 10.1021/acsnano.8b06994.
2.	T. Ando et al., "Topical Review: The 2018 correlative microscopy techniques roadmap", J. Phys. D: Appl. Phys. 51, 443001 (42pp) (2018). DOI: 10.1088/1361-6463/aad055 Open Access (PDF)
3.	T. Mori, S. Sugiyama, M. Byme, C. H. Johnson, T. Uchihashi, T. Ando, "Revealing circadian mechanisms of integration and resilience by visualizing clock proteins working in real time", Nature Commun. 9:3245 (13 pages) (2018). DOI: 10.1038/s41467-018-05438-4. Oepn Access (PDF) (Link)
4.	T. Uchihashi, Y. Watanabe, Y. Nakazaki, T. Yamasaki, H. Watanabe, T. Maruno, K. Ishii, S. Uchiyama, C. Song, K. Murata, R. Iino, and T. Ando, "Dynamic structural states of ClpB involved in its disaggregation function", Nature Commun. 9:2147 (12 pages) (2018). DOI: 10.1038/s41467-018-04587-w. Open Access (PDF) (Link).
5.	T. Ravula, D. Ishikuro, N. Kodera, T. Ando, G. Anantharamaiah, A. Ramamoorthy, "Real time monitoring of lipid exchange via fusion of peptide based lipid-nanodiscs", Chem. Mater 30, 3204-3207 (2018). DOI: 10.1021/acs.chemmater.8b00946
6.	T. Umakoshi, H. Udaka, T. Uchihashi, T. Ando, M. Suzuki, "Quantum-dot antibody conjugation visualized at the single-molecule scale with high-speed aomic force microscopy", Colloids and Surfaces B: Biointerfaces 167: 267-274 (2018). DOI: 10.1016/j.colsurfb.2018.04.015 (Link)
7.	D. Noshiro and T. Ando, "Substrate protein dependence of GroEL-GroES interaction cycle revealed by high-speed AFM imaging", Philosophical Transactions B 373: 20170180 (2018). DOI: /10.1098/rstb.2017.0180. Open Access (PDF) (Link) Supplementary Information, Movie1, Movie 2, Movie 3
8.	N. Terahara, Y. Inoue, N. Kodera, Y. V. Morimoto, T. Uchihashi, K. Imada, T. Ando, K. Namba, and T. Minamino, "Insight into structural remodeling of the FlhA ring responsible for bacterial flagellar type III protein export", Sci. Adv. 4 (4), eaao7054.DOI: 10.1126/sciadv.aao7054 (Link)
9.	T. Haruyama, T. Uchihashi, Y. Yamada, N. Kodera, T. Ando and H. Konno, "Negatively charged lipids are essential for functional and structural switch of human 2-Cys peroxiredoxin II", J. Mol. Biol. 430(5):602-610 (2018). DOI: /10.1016/j.jmb.2017.12.020 (Link)
10.	T. Takeda, T. Kozai, H. Yang, D. Ishikuro, K. Seyama, Y Kumagai, T. Abe, H. Yamada, T. Uchihashi, T. Ando, K. Takei, "Dynamic clustering of dynamin-amphiphysin helices regulates membrane constriction and fission coupled with GTP hydrolysis", e-Life 7:e30246 (19 pages) (2018). DOI: /10.7554/eLife.30246 (Link)
2017
1.	T. Ando, High-speed atomic force microscopy and its future prospects. Biophys. Rev. 10:285–292 (2018). DOI: 10.1007/s12551-017-0356-5 (Shared PDF) This is a part of Special Issue on "Biomolecules to Bionanommechanics -- Fumio Arisaka's 70th Birthday".
2.	Mikihiro Shibata, Hiroshi Nishimasu, Noriyuki Kodera, Seiichi Hirano, Toshio Ando, Takayuki Uchihashi & Osamu Nureki. Real-space and real-time dynamics of CRISPR-Cas9 visualized by high-speed atomic force microscopy. Nat. Commun. 8, 1430 (9 pp) (2017). DOI: 10.1038/s41467-017-01466-8, Open Access (PDF)
3.	N. Terahara, N. Kodera, T. Uchihashi, T. Ando, K. Namba, T Minamino, "Na⁺-induced structurak transition of MotPS for stator assembly of the Bacillus fragellar motor", Sci. Adv. 3, eaao4119 (9 pp) (2017). DOI: 10.1126/sciadv.aao4119 (Link)
4.	M. Shibata, H. Watanabe, T. Uchihashi, T. Ando, R. Yasuda, “High-speed atomic force microscopy imaging of live mammalian cells”, Biophys. Physicobiol. 14, 127-135 (2017). DOI: 10.2142/biophysico.14.0_127
5.	S. Watanabe and T. Ando, "High-speed XYZ nanopositioner for scanning ion conductance microscopy", Appl. Phys. Lett. 111, 113106 (2017); doi: 10.1063/1.4993296
6.	S. Matsui, S. Hiroshige, T. Kureha, M. Shibata, T. Uchihashi, D. Suzuki, “Fast Adsorption of Soft Hydrogel Microspheres on Solid Surfaces in Aqueous Solutions” Angew. Chem. Int. Ed. 56, 12146-12149 (2017)..
7.	J. J. Keya, D. Inoue, Y. Suzuki, T. Kozai, D. Ishikuro, N. Kodera, T. Uchihashi, A. M. R. Kabir, M. Endo, K. Sada, and A. Kakugo, “High-Resolution Imaging of a Single Gliding Protofilament of Tubulins by HS-AFM”, Sci. Rep. 7, 6166 (2017).
8.	A. Sumino, T. Uchihashi, S. Oiki, “Oriented Reconstitution of the Full-Length KcsA Potassium Channel in a Lipid Bilayer for AFM Imaging”, J. Phys. Chem. Lett. 8, 785-793 (2017).
9.	T. Ando, "Directly watching biomolecules in action by high-speed atomic force microscopy", Biophys. Rev. 9, 421-429 (2017). DOI: 10.1007/s12551-017-0281-7 This is a part of a Special Issue for IUPAB Edinburgh Congress 2017, (Link)
10.	M S Mohamed, A. Kobayashi, A. Taoka, T. Watanabe-Nakayama, Y. Kikuchi, M. Hazawa, T. Minamoto,Y. Fukumori, N. Kodera, T. Uchihashi, T. Ando, and R. W. Wong, “High-speed atomic force microscopy reveals loss of nuclear pore resilience as a dying code in colorectal cancer cells”, ACS Nano 11, 5567−5578 (2017). DOI: 10.1021/acsnano.7b00906
11.	Yves F. Dufrêne, Toshio Ando, Ricardo Garcia, David Alsteens, David Martinez-Martin, Andreas Engel, Christoph Gerber and Daniel J. Müller, "Imaging modes of atomic force microscopy for application in molecular and cell biology", Nat. Nanotechnol. 12, 295-307 (2017). DOI: 10.1038/NNANO.2017.45 (Link)
12.	T. Ando, "High-speed Atomic Force Microscopy for Observing Protein Molecules in Dynamic Action", Proceedings of SPIE 10328, Selected Papers from the 31st International Congress on High-Speed Imaging and Photonics, 103281R (February 20, 2017). DOI:10.1117/12.2268795
2016
1.	K. Inoue, S. Ito, Y. Kato, Y. Nomura, M. Shibata, T. Uchihashi, S. Tsunoda, and H. Kandori, “Natural light-driven inward proton pump.” Nat. Commun. 7: 13415 (2016). DOI: 10.1038/ncomms13415
2.	D. Yamamoto and T. Ando Chaperonin GroEL-GroES functions as both alternating and non-alternating engines, J. Mol. Biol. 428, 3090-3101 (2016). DOI: 10.1016/j.jmb.2016.06.017 (Link) (Movie S1)
3.	Hayashi Yamamoto, Yuko Fujioka, Sho W. Suzuki, Daisuke Noshiro, Hironori Suzuki, Chika Kondo-Kakuta, Yayoi Kimura, Hisashi Hirano, Toshio Ando, Nobuo N. Noda, Yoshinori Ohsumi The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes, Dev. Cell 38:86-99 (2016). DOI: 10.1016/j.devcel.2016.06.015. (PDF) (Open Access)
4.	T. Watanabe-Nakayama, M. Itami, N. Kodera, T. Ando and H. Konno High-speed atomic force microscopy reveals strongly polarized movement of clostridial collagenase along collagen fibrils, Sci. Rep. 6:28975 (2016). DOI: 10.1038/srep28975. (Link)
5.	T. Uchihashi, H. Watanabe, S. Fukuda, M. Shibata and T. Ando "Functional extension of high-speed atomic force microscopy for wider biological applications", Ultramicroscopy 160, 182-196 (2016). DOI: 10.1016/j.ultramic.2015.10.017 (Link)
2015
1.	Wilaiwan Sriwimol, Aratee Aroonkesorn, Somsri Sakdee, Chalermpol Kanchanawarin, Takayuki Uchihashi, Toshio Ando and Chanan Angsuthanasombat "Potential pre-pore trimer formation by the Bacillus thuringiensis mosquito-specific toxin: Molecular insights into a critical prerequisite of membrane-bound monomers", J. Biol. Chem. 290 (34), 20793-20803 (2015). DOI: 10.1074/jbc.M114.627554 (Link)
2.	Shingo Fukuda, Takayuki Uchihashi, Toshio Ando "Method of mechanical holding of cantilever chip for tip-scan high-speed atomic force microscopy", Rev. Sci. Instrum. 86, 063703 (2015). DOI: 10.1063/1.4922381 (Link)
3.	Kouta Takeda, Takayuki Uchihashi, Hiroki Watanabe, Takuya Ishida, Kiyohiko Igarashi, Nobuhumi Nakamura, Hiroyuki Ohno, "Real-time dynamic adsorption processes of cytochrome c on an electrode observed through electrochemical high-speed atomic force microscopy", PLoS One e0116685 (10 pages), (2015). DOI:10.1371/journal.pone.0116685 (Link)
4.	T. Davies, N. Kodera, G. S. Kaminski Schierle, E. Rees, M. Erdelyi, C. F. Kaminski, T. Ando, M. Mishima , ”CYK4 Promotes Antiparallel Microtubule Bundling by Optimizing MKLP1 Neck Conformation”, PloS Biol. 13(4): e1002121 (26 pp). doi:10.1371/journal.pbio.1002121 (Link)
5.	M. Shibata, T. Uchihashi, T. Ando and R. Yasuda "Long-tip high-speed atomic force microscopy for nanometer-scale imaging in live cells" Scientific Reports 5, 8724 (7 pp) (2015). DOI:10.1038/srep08724 (Link)
6.	M. Imamura, T. Uchihashi, T. Ando, A. Leifert, U. Simon, A. D. Malay and J. G. Heddle "Probing structural dynamics of an artificial protein cage using high-speed atomic force microscopy", Nano Lett. 15 (2): 1331–1335 (2015). DOI: 10.1021/nl5045617 (Link)
7.	Kien Xuan Ngo, Noriyuki Kodera, Eisaku Katayama, Toshio Ando and Taro Q.P. Uyeda "Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed AFM", e-Life 4:e04806 (2015) DOI: 10.7554/eLife.04806 (Link) (PDF) (Supplements)
8.	N. Kodera, K. Uchida, T. Ando, and S. Aizawa "Two-ball structure of the flagellar hook-length control protein FliK as revealed by high-speed atomic force microscopy", J. Mol. Biol. 427, 406-414 (2015) doi: 10.1016/j.jmb.2014.11.007 (Link)

2014
1.	S. Ishino, T. Yamagami, M. Kitamura, N. Kodera, T. Mori, S. Sugiyama, T. Ando, N. Goda, T. Tenno, H. Hiroaki, and Y. Ishino "Multiple Interactions of the Intrinsically Disordered Region between the N-terminal Helicase and C-terminal Nuclease Domains of the Archaeal Hef Protein", J. Biol. Chem. 289: 21627-21639 (2014). DOI:10.1074/jbc.M114.554998 (Link)
2.	J. Preiner, N. Kodera, J. Tang, A. Ebner, M. Brameshuber, D. Blaas, N. Gelbmann, H. Gruber, T. Ando, and P. Hinterdorfer, "IgGs are made for walking on bacterial and viral surfaces", Nature Communications 5: 4394 (8 pp) (2014) DOI:10.1038/ncomms5394 (Link)
3.	T. Ando, "High-speed AFM imaging", Curr. Opin. Struct. Biol. 28: 63-68 (2014). DOI:10.1016/j.sbi.2014.07.011 (Link)
4.	N. Kodera and T. Ando, "The path to visualization of walking myosin V by high-speed atomic force microscopy", Biophys. Rev. 6:237-260 (2014). DOI:10.1007/s12551-014-0141-7 (PDF) (Link) (Open access) (Link2)
5.	Y. Shibafuji, A. Nakamura, T. Uchihashi, N. Sugimoto, S. Fukuda, H. Watanabe, M. Samejima, T. Ando, H. Noji, A. Koivula, K. Igarashi, and R. Iino, Single-molecule imaging analysis of elementary reaction steps of Trichoderma Reesei cellobiohydrolase I (Cel7A) hydrolyzing crystalline cell. J. Biol. Chem. 289:14056-14065 (2014) DOI:10.1074/jbc.M113.546085. (Link)
6.	T. Ando, T. Uchihashi, and S. Scheuring, "Filming biomolecular processes by high-speed atomic force microscopy", Chem. Rev. 114(6):3120-3188 (2014). DOI:10.1021/cr4003837. (PDF: Low resolution) (PDF: High resolution) (Link) (Selected to be featured in ACS Editors' Choice; Open access sponsored by ACS publications)
7.	A. Nakamura, H. Watanabe, T. Ishida, T. Uchihashi, M. Wada, T. Ando, K. Igarashi, and M. Samejima, "Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose", J. Am. Chem. Soc. 136:4584-4592 (2014). DOI:10.1021/ja4119994. (Link)
8.	K. Igarashi, T. Uchihashi, T. Uchiyama, H. Sugimoto, M. Wada, K. Suzuki, S. Sakuda, T. Ando, T. Watanabe, and M. Samejima, "Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin", Nature Communications 5: 3975 (2014). DOI:10.1038/ncomms4975 (Link)

2013
1.	Kentaro Noi, Daisuke Yamamoto, Shingo Nishikori, Ken-ichi Arita-Morioka, Toshio Ando and Teru Ogura, "High-speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97", Structure 21: 1992-2002 (2013). DOI: 10.1016/j.str.2013.08.017 (Link)
2.	Neval Yilmaz, Taro Yamada, Peter Greimel, Takayuki Uchihashi, Toshio Ando, and Toshihide Kobayashi, "Real-Time Visualization of Assembling of a Sphingomyelin-Specific Toxin", Biophys. J. 105, 1397-1405 (2013). DOI: 10.1016/j.bpj.2013.07.052 (Link)
3.	S. Fukuda, T. Uchihashi, R. Iino, Y. Okazaki, M. Yoshida, K. Igarashi, and T. Ando, "High-speed atomic force microscope combined with single-molecule fluorescence microscope", Rev. Sci. Instrum. 84, 073706 (2013). DOI: 10.1063/1.4813280 (Link)
4.	M. Hashimoto, N. Kodera, Y. Tsunaka, M. Oda, M. Tanimoto, T. Ando, K. Morikawa, and S. Tate, "Phosphorylation-Coupled Intramolecular Dynamics of Unstructured Regions in Chromatin Remodeler FACT", Biophys. J. 104: 2222-2234 (2013) DOI: 10.1016/j.bpj.2013.04.007 (Link)
5.	H. Watanabe, T. Uchihashi, T. Kobashi, M. Shibata, J. Nishiyama, R. Yasuda, and T. Ando, "Wide-area scanner for high-speed atomic force microscopy", Rev. Sci. Instrum. 84: 053702 (2013). DOI: 10.1063/1.4803449 (Link)
6.	T. Ando, "High-speed atomic force microscopy of protein dynamics: myosin on actin and rotary enzyme F1-ATPase", Microscopy & Analysis 27(3):10-13 (2013). (Link)
7.	H. Yamashita, K. Inoue, M. Shibata, T. Uchihashi, J. Sasaki, H. Kandori, and T. Ando, "Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy", J. Struct. Biol. 184: 2-11 (2013). DOI: 10.1016/j.jsb.2013.02.011 (Link)
8.	T. Ando, "Molecular machines directly observed by high-speed atomic force microscopy", FEBS Lett. 587: 997-1007 (2013). DOI: 10.1016/j.febslet.2012.12.024, (Link) (PDF) Open access
9.	T. Ando, T. Uchihashi, and N. Kodera, "High-speed AFM and applications to biomolecular systems", Annu. Rev. Biophys. 42: 393-414(2013).DOI: 10.1146/annurev-biophys-083012-130324 (Link)
10.	T. Ando, "High-speed atomic force microscopy", Microscopy 62(1):81-93 (2013). DOI: 10.1093/jmicro/dfs093 (Link)

2012
1.	T. Ando, T. Uchihashi, and N. Kodera, "High-speed atomic force microscopy", Jpn. J. Appl. Phys. 51:08KA02 (15 pp) (2012). DOI: 10.1143/JJAP.51.08KA02 (Link)
2.	H. Yamashita, A. Taoka, T. Uchihashi, T. Asano, T. Ando, and Y. Fukumori, "Single molecule imaging on living bacterial cell surface by high-speed AFM", J. Mol. Biol. 422(2) 300-309 (2012). DOI: 10.1016/j.jmb.2012.05.018 (Link) (Movie1, Movie2, Movie3, Movie4, Supplementary data)
3.	T. Uchihashi, N. Kodera, and T. Ando, "Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy", Nature Protocols 7(6): 1193-1206 (2012).DOI: 10.1038/nprot.2012.047 (Link)
4.	K. Igarashi, T. Uchihashi, A. Koivula, M. Wada, S. Kimura, M. Penttilä, T. Ando, and M. Samejima, "Visualization of cellobiohydrolase I from Trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy", Methods Enzymol. 510, 169-182 (2012). DOI: 10.1016/B978-0-12-415931-0.00009-4 (Link)
5.	T. Nojima, H. Konno, N. Kodera, K. Seio, H. Taguchi, M. Yoshida, “Nano-scale alignment of proteins on a flexible DNA backbone”, PLoS One 7(12): e52534 (5 pp) (2012). (Link)
6.	T. Ando, "High-speed atomic force microscopy coming of age", Nanotechnology 23: 062001 (27 pp) (2012). DOI: 10.1088/0957-4484/23/6/062001 (Link) (Editorial) This article has been selected by the editors of Nanotechnology for inclusion in the exclusive "Highlights 2012" collection.
7.	T. Ando and N. Kodera, "Visualization of mobility by atomic force microscopy", Methods Mol. Biol. 896: 57-69 (2012). DOI: 10.1007/978-1-4614-3704-8_4 (Link)

2011
1.	T. Uchihashi and T. Ando, "High-speed atomic force microscopy and biomolecular processes", Methods Mol. Biol. 736: 285-300 (2011). DOI: 10.1007/978-1-61779-105-5_18 (Link)
2.	K. Igarashi, T. Uchihashi, A. Koivula, M. Wada, S. Kimura, T. Okamoto, M. Penttilä, T. Ando, and M. Samejima, "Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface", Science 333:1279-1282 (2011). DOI 10.1126/science.1208386 (Link) (Supplementary Info) (Movie 1) (Movie 2) (Movie 3) (Movie 4) (Movie 5) (Movie 6) (Movie 7) (Movie 8) (Movie 9) (Science Japan)
3.	A. Laisne, M. Ewald, T. Ando, E. Lesniewska, and D. Pompon, "Self-assembly properties and dynamic of synthetic proteo-nucleic building blocks in solution and on surfaces", Bioconjugate Chem. 22:1824-1834 (2011) DOI: 10.1021/bc2002264 (Link).
4.	A. Miyagi, T. Ando and Y. L. Lyubchenko, "Dynamics of nucleosomes assessed with time-lapse high speed atomic force microscopy", Biochemistry 50: 7901-7908 (2011). DOI: 10.1021/bi200946z (this paper is highlighted in Biochemistry) (Link)
5.	T. Uchihashi, R. Iino, T. Ando, and H. Noji, "High-speed atomic force microscopy reveals rotary catalysis of rotorless F1-ATPase, Science 333, 755-758 (2011). DOI: 10.1126/science.1205510 (Link) (Supplementary_Inf) (Movie 1) (Movie 2) (Movie 3) (Movie 4) (Movie 5) (Movie 6) (Movie 7) (Movie 8)
6.	M. Shibata, T. Uchihashi, H. Yamashita, H. Kandori, and T. Ando, "Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy", Angewande Chemie International edition 50: 4410–4413 (2011). DOI: 10.1002/anie.201007544 (Link) (Supplementary_Info) (Movie 1) (Movie 2) (Movie 3) (Movie 4)
7.	Y. L. Lyubchenko, L. S. Shlyakhtenko, and T. Ando, "Imaging of nucleic acids with atomic force microscopy", Methods 54: 274-283 (2011). DOI: 10.1016/j.ymeth.2011.02.001 (Link)
8.	S. Inoue, T. Uchihashi, D. Yamamoto, and T. Ando, Direct observation of surfactant aggregate behavior on a mica surface using high-speed atomic force microscopy, Chem. Commun. 47: 4974–4976 (2011) DOI: 10.1039/C0CC05762B (Link)

2010
1.	N. Kodera, D. Yamamoto, R. Ishikawa, and T. Ando, Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 468: 72-76 (2010). DOI: 10.1038/nature09450 (Link) (Movie 1) (Movie 2) (Movie 3) (Movie 4) (Movie 5) (Movie 6) (supplementary info) (News & View)
2.	P.-E. Milhiet, D. Yamamoto, O. Berthoumieu, P. Dosset, Ch. Le Grimellec, J.-M. Verdier, S. Marchal, and T. Ando, “Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy”, PLos One 5 (11): e13240 (8 pp) (2010). DOI: 10.1371/journal.pone.0013240 (Link) (Movie S1, Movie S2, Movie S3) (supplementary info)
3.	D. Yamamoto, T. Uchihashi, N. Kodera, H. Yamashita, S. Nishikori, T. Ogura, M. Shibata, and T. Ando, High-speed atomic force microscopy techniques for observing dynamic biomolecular processes, Methods Enzymol. 475 (Part B): 541-564 (2010). DOI: 10.1016/S0076-6879(10)75020-5 (Link)
4.	D. Yamamoto, A. Taoka, T. Uchihashi, H. Sasaki, H. Watanabe, T. Ando, and Y. Fukumori, Visualization and structural analysis of the bacterial magnetic organelle magnetosome using atomic force microscopy, Proc. Natl. Acad. Sci. USA 107: 9382-9387 (2010). DOI: 10.1073/pnas.1001870107 (Link) (supplementary info + Movie)
5.	S. Sugimoto, K. Yamanaka, S. Nishikori, A. Miyagi, T. Ando, and T. Ogura, AAA+ chaperone ClpX regurates dynamics of prokaryotic cytoskeletal protein FtsZ, J. Biol. Chem. 285: 6648-6657 (2010). DOI: 10.1074/jbc.M109.080739 (Link)
6.	M.-C. Giocondi, D. Yamamoto, E. Lesniewska, P.-E. Milhiet, T. Ando, and Ch. Le Grimellec, Surface topography of membrane domains, Biochim. Biophys. Acta.-Biomembranes 1798: 703-718 (2010). DOI: 10.1016/j.bbamem.2009.09.015 (Link)
7.	M. Shibata, H. Yamashita, T. Uchihashi, H. Kandori, and T. Ando, High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin, Nature Nanotechnology 5, 208 - 212 (2010). DOI: 10.1038/nnano.2010.7 (Link) (Supplementary Information + Movies)

2009
1.	I. Casuso, N. Kodera, C. Le Grimellec, T. Ando, and S. Scheuring, Contact mode high-resolution high-speed atomic force microscopy movies of purple membrane, Biophys J, 97 (5): 1354-1361 (2009). DOI: 10.1016/j.bpj.2009.06.019 (Link)
2.	D. Yamamoto, N. Nagura, S. Omote, M. Taniguchi, and T. Ando, Streptavidin 2D crystal substrates for visualizing biomolecular processes by atomic force microscopy, Biophys. J. 97(8): 2358–2367 (2009). DOI: 10.1016/j.bpj.2009.07.046 (Link)
3.	H. Yamashita, K. Voïtchovsky, T. Uchihashi, S. Antoranz Contera, J. F. Ryan, and T. Ando, Dynamics of bacteriorhodopsin 2D crystal observed by high-speed atomic force microscopy, J. Struct. Biol. 167: 153-158 (2009). DOI: 10.1016/j.jsb.2009.04.011 (Link) (Supplementary Movies)
4.	K. Shinohara, N. Kodera, and T. Ando, Single-molecule imaging of a micro-Brownian motion of a chiral helical π-conjugated polymer as a molecular spring driven by thermal fluctuations.Chem Lett. 38(7): 690-691 (2009). DOI: 10.1246/cl.2007.1378 (Link)

2008
1.	T. Ando, T. Uchihashi, and T. Fukuma, High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes, Prog. Surf. Sci. 83: 337-437 (2008). DOI: 10.1016/j.progsurf.2008.09.001 (Link)
2.	D. Yamamoto, T. Uchihashi, N. Kodera, and T. Ando, Anisotropic diffusion of point defects in two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy, Nanotechnology 19: 384009 (9 pp) (2008). DOI: 10.1088/0957-4484/19/38/384009 (Link) (Supplementary Movie)
3.	A. Miyagi, Y. Tsunaka, T. Uchihashi, K. Mayanagi, S. Hirose, K. Morikawa, and T. Ando, Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy, Chem. Phys. Chem. 9(13):1859-1866 (2008). DOI: 10.1002/cphc.200800210 (Link)
4.	T. Fukuma, Y. Okazaki, N. Kodera, T. Uchihashi, and T. Ando, High resonance frequency force microscope scanner using inertia balance support, Appl. Phys. Lett. 92:243119 (2008). DOI: 10.1063/1.2951594 (Link)
5.	T. Ando, T. Uchihashi, N. Kodera, D. Yamamoto, M. Taniguchi, A. Miyagi, and H. Yamashita, High-speed AFM and nano-visualization of biomolecular processes, Pflügers Archiv -Eur. J. Physiol. 456:211-225 (2008). DOI: 10.1007/s00424-007-0406-0 (Link)
6.	T. Ando, Control techniques in high-speed atomic force microscopy, Proceedings of the American Control Conference, art. no. 4586984, pp. 3194-3200 (2008). DOI: 10.1109/ACC.2008.4586984 (PDF File)
7.	H. Iwase, H. Choi, M. Akabori, T. Suzuki, S. Yamada, D. Yamamoto and T. Ando, Fabrication of 3D micro-cantilevers based on MBE-grown strained semiconductor layers, Physica E: Low-dimensional Systems and Nanostructures 40(6): 2210-2213 (2008). DOI: 10.1016/j.physe.2007.11.016

2007
1.	T. Ando, T. Uchihashi, N. Kodera, D. Yamamoto, M. Taniguchi, A. Miyagi, and H. Yamashita, High-speed atomic force microscopy for observing dynamic biomolecular processes, J. Mol. Recognit. 20:448-458 (2007). DOI: 10.1002/jmr.843 (Link)
2.	H. Yamashita, T. Uchihashi, N. Kodera, A. Miyagi, D. Yamamoto, T. Ando, Tip-sample distance control using photo-thermal actuation of a small cantilever for high-speed atomic force microscopy, Rev. Sci. Instrum. 78:083702 (5 pp) (2007). DOI: 10.1063/1.2766825 (Link)
3.	K. Shinohara, N. Kodera, and T. Ando, Single molecular imaging of a micro-Brownian motion and a bond scission of a supramolecular chiral π-conjugated, Chem. Lett. 36: 1378-1379 (2007). DOI: 10.1246/cl.2007.1378 (Link)
4.	S. Morita, H. Yamada, and T. Ando, Japan AFM roadmap 2006, Nanotechnology 18:08401 (10 pages) (2007). DOI: 10.1088/0957-4484/18/8/084001 (Link)

2006
1.	T. Uchihashi, H. Yamashita, and T. Ando, Fast phase imaging in liquids using a rapid scan atomic force microscope, Appl. Phys. Lett. 89:213112 (3 pages) (2006). (Link) DOI: 10.1063/1.2387963
2.	N. Kodera, M. Sakashita, and T. Ando, Dynamic proportional-integral-differential controller for high-speed atomic force microscopy, Rev. Sci. Instrum. 77(8):083704 (7 pages) (2006). (Link) DOI: 10.1063/1.2336113
3.	H. Koide, T. Kinoshita, Y. Tanaka, S. Tanaka, N. Nagura, G. Meyer zu Hörste, A. Miyagi, and T. Ando, Identification of the specific IQ motif of myosin V from which calmodulin dissociates in the presence of Ca²⁺, Biochemistry 45(38):11598-11604 (2006). (Link) DOI: 10.1021/bi0613877
4.	M. Yokokawa, C. Wada, T. Ando, N. Sakai , A. Yagi, S.H. Yoshimura, and K. Takeyasu, Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL, EMBO J. 25:4567-4576 (2006). (Link) DOI: 10.1038/sj.emboj.7601326
5.	M. Yokokawa, S.H. Yoshimura, Y. Naito, T. Ando, A. Yagi, N. Sakai, and K. Takeyasu, Fast-scanning atomic force microscopy reveals the molecular mechanism of DNA cleavage by ApaI endonuclease, IEE Proc Nanobiotechnol. 153(4):60-66 (2006). DOI: 10.1049/ip-nbt:20050018
6.	T. Ando, T. Uchihashi, N. Kodera, A. Miyagi, R. Nakakita, H. Yamashita, and M. Sakashita, High-speed atomic force microscopy for studying the dynamic behavior of protein molecules at work, Jpn. J. Appl. Phys. 45(3B):1897-1903 (2006). (Link) DOI: 10.1143/JJAP.45.1897
7.	T. Uchihashi, N. Kodera, H. Itoh, H. Yamashita, and T. Ando, Feed-forward control for high-speed AFM imaging of biomolecules, Jpn. J. Appl. Phys. 45(3B):1904-1908 (2006). (Link) DOI: 10.1143/JJAP.45.1904

2005
1.	T. Ando, T. Uchihashi, N. Kodera, A. Miyagi, R. Nakakita, H. Yamashita, and K. Matada, High-speed AFM for capturing the dynamic behavior of protein molecules at work, e-J. Surf. Sci. Nanotechnol. 3:384-392 (2005). (Link) (Supplementary Movies) DOI: 10.1380/ejssnt.2005.384
2.	N. Kodera, H. Yamashita, and T. Ando, Active damping of the scanner for high-speed atomic force microscopy, Rev. Sci. Instrum. 76: 053708 (5pages) (2005). (Link) DOI: 10.1063/1.1903123

2000~2004
1.	N. Kodera, T. Kinoshita, T. Ito, and T. Ando, High-resolution imaging of myosin motor in action by a high-speed atomic force microscope, Adv. Exp. Med. Biol. 538:119-127 (2003). DOI: 10.1007/978-1-4419-9029-7_11
	R. Ishikawa, T. Sakamoto, T. Ando, S. Higashi-Fujime, and K. Kohama, Polarized actin bundles formed by human fascin-1: Their sliding and disassembly on myosin II and myosin V in vitro, J. Neurochem. 87:676-685 (2003). (Link) DOI: 10.1046/j.1471-4159.2003.02058.x
3.	T. Ando, N. Kodera, Y. Naito, T. Kinoshita, K. Furuta, and Y.Y. Toyoshima, A high-speed atomic force microscope for studying biological macromolecules in action, ChemPhysChem 4:1196-1202 (2003). (Link) DOI: 10.1002/cphc.200300795
	T. Ando, N. Kodera, D. Maruyama, E. Takai, K. Saito, and A. Toda, A High-speed atomic force microscope for studying biological macromolecules in action, Jpn. J. Appl. Phys. 41:4851-4856 (2002). (Link) DOI: 10.1143/JJAP.41.4851
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