Toshio Ando
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Toshio Ando has a total of 66 co-authors. Here are the top co-authors by number of shared publications:
- Takayuki Uchihashi
Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan
17 shared publications - Noriyuki Kodera
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan
14 shared publications Daisuke Yamamoto
Department of Mathematics and Physics, Graduate School of Natural Science and Technology, Kanazawa University
6 shared publicationsAtsushi Miyagi
Physics, School of Science, Kanazawa University
5 shared publicationsHayato Yamashita
Department of Physics, Kanazawa University, Kakuma-machi, Kanazawa (Japan), Fax: (+81) 76-264-5739 http://www.s.kanazawa-u.ac.jp/phys/biophys/index.htm
5 shared publicationsMasaaki Taniguchi
†Department of Physics, Kanazawa University, Kanazawa, Japan
4 shared publications
Latest Publications
- 26 October 2018
- Published by Oxford University Press (OUP) in Microscopy
- Vol. 67 (suppl_2) , i24
2pB_SS4-3Movement of Gliding Motors in Mycoplasma mobile Visualized by High-speed AFM
Mycoplasma mobile, a pathogenic bacterium glides on solid surfaces with a unique mechanism. In the mechanism, “legs” on a cell repeatedly catch and pull sialylated oligosaccharides on host cells. The force for gliding is generated on an internal structure which consists of gliding motors evolved from F-type ATPase/synthase [1]. However, the actual movement of gliding machinery has not been observed. In this study, we focused on visualizing the movement of gliding motors in living cells by high-speed AFM [2].
- 26 October 2018
- Published by Oxford University Press (OUP) in Microscopy
- Vol. 67 (suppl_2) , i24
2pB_SS4-3Movement of Gliding Motors in Mycoplasma mobile Visualized by High-speed AFM
Mycoplasma mobile, a pathogenic bacterium glides on solid surfaces with a unique mechanism. In the mechanism, “legs” on a cell repeatedly catch and pull sialylated oligosaccharides on host cells. The force for gliding is generated on an internal structure which consists of gliding motors evolved from F-type ATPase/synthase [1]. However, the actual movement of gliding machinery has not been observed. In this study, we focused on visualizing the movement of gliding motors in living cells by high-speed AFM [2].
- 26 October 2018
- Published by Oxford University Press (OUP) in Microscopy
- Vol. 67 (suppl_2) , i23
2pB_SS4-1One particle physical property analysis of bacterial membrane vesicle using high-speed AFM
Membrane vesicle (MV) is a small spherical particle which is produced by bacteria. Although the importance of examining the properties of individual MVs has been increasing in recent years, only the analysis of physical properties in bulk has been done. In this study, we observed the MVs produced by four bacterial species in PBS using high-speed atomic force microscopy with tapping mode, and clarify the physical property of individual MV from phase image. The phase image showed the diversity of MVs physical property such as elasticity. We developed a method to compare the physical property between different samples from phase images. We compared the physical properties of bacterial MVs and liposomes made from bacterial lipid extract. The all species of MVs showed physical heterogeneous, whereas the liposomes showed physical homogenous. Therefore, the physical property analysis using high-speed AFM revealed that the MVs have physical diversity driven from biological phenomena.
- 26 October 2018
- Published by Oxford University Press (OUP) in Microscopy
- Vol. 67 (suppl_2) , i23
2pB_SS4-1One particle physical property analysis of bacterial membrane vesicle using high-speed AFM
Membrane vesicle (MV) is a small spherical particle which is produced by bacteria. Although the importance of examining the properties of individual MVs has been increasing in recent years, only the analysis of physical properties in bulk has been done. In this study, we observed the MVs produced by four bacterial species in PBS using high-speed atomic force microscopy with tapping mode, and clarify the physical property of individual MV from phase image. The phase image showed the diversity of MVs physical property such as elasticity. We developed a method to compare the physical property between different samples from phase images. We compared the physical properties of bacterial MVs and liposomes made from bacterial lipid extract. The all species of MVs showed physical heterogeneous, whereas the liposomes showed physical homogenous. Therefore, the physical property analysis using high-speed AFM revealed that the MVs have physical diversity driven from biological phenomena.
- 1 February 2017
- Published by Elsevier in Biophysical Journal
- Vol. 112 (3) , 469a
Nano-Space Video Imaging Reveals Structural Dynamics of Fibrous Protein Assembly and Relevant Enzymes
- 1 February 2017
- Published by Elsevier in Biophysical Journal
- Vol. 112 (3) , 469a
Nano-Space Video Imaging Reveals Structural Dynamics of Fibrous Protein Assembly and Relevant Enzymes
- 1 January 2016
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 56 (3) , 159-161
Visualization of Living Cells by High-speed Atomic Force Microscopy
- 1 January 2016
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 56 (3) , 159-161
Visualization of Living Cells by High-speed Atomic Force Microscopy
- 1 April 2014
- Vol. 86 (2) , 127-36
[Direct observation of rotary catalysis of rotorless F1-ATPase with high-speed AFM].
- 1 April 2014
- Vol. 86 (2) , 127-36
[Direct observation of rotary catalysis of rotorless F1-ATPase with high-speed AFM].
- 1 January 2014
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 54 (supplement) , S220
2P153 ATP-less walking of myosin V on actin filaments(11. Molecular motor,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
- 1 January 2014
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 54 (supplement) , S220
2P153 ATP-less walking of myosin V on actin filaments(11. Molecular motor,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
- 1 January 2014
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 54 (supplement) , S222
2P166 Direct observation of functioning myosin VI by high-speed AFM(11. Molecular motor,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
- 1 January 2014
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 54 (supplement) , S222
2P166 Direct observation of functioning myosin VI by high-speed AFM(11. Molecular motor,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
- 1 January 2014
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 54 (supplement) , S190
1P296 Simultaneous imaging of dynamic structural and chemical events in protein by high-speed AFM combined with single-molecule TIRFM(27. Bioimaging,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
- 1 January 2014
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 54 (supplement) , S190
1P296 Simultaneous imaging of dynamic structural and chemical events in protein by high-speed AFM combined with single-molecule TIRFM(27. Bioimaging,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
- 1 January 2013
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 53 (supplement) , S131
1P157 High-Speed-AFM Observation of Processive Movement of Cytoplasmic Dynein(11.Molecular motor,Poster,The 51st Annual Meeting of the Biophysical Society of Japan)
- 1 January 2013
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 53 (supplement) , S131
1P157 High-Speed-AFM Observation of Processive Movement of Cytoplasmic Dynein(11.Molecular motor,Poster,The 51st Annual Meeting of the Biophysical Society of Japan)