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Volumn 28, Issue 1, 2014, Pages 63-68

High-speed AFM imaging

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; ATOMIC FORCE MICROSCOPE; ATOMIC FORCE MICROSCOPY; CAMERA; DIODE; FEEDBACK SYSTEM; HIGH SPEED ATOMIC FORCE MICROSCOPY; IMAGE ANALYSIS; IMAGE PROCESSING; IMAGING SYSTEM; MOLECULAR DYNAMICS; POLARIZATION; PROCESS DESIGN; PROTEIN CONFORMATION; PROTEIN DNA INTERACTION; PROTEIN PURIFICATION; REVIEW; CHEMISTRY; PROCEDURES;

EID: 84905833890     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.07.011     Document Type: Review
Times cited : (80)

References (45)
  • 1
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo H., Balci H., Ishitsuka Y., Buranachai C., Ha T. Advances in single-molecule fluorescence methods for molecular biology. Annu Rev Biochem 2008, 77:51-76.
    • (2008) Annu Rev Biochem , vol.77 , pp. 51-76
    • Joo, H.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 2
    • 34547878369 scopus 로고    scopus 로고
    • New directions in single-molecule imaging and analysis
    • Moerner W.E. New directions in single-molecule imaging and analysis. Proc Natl Acad Sci U S A 2007, 104:12596-12601.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12596-12601
    • Moerner, W.E.1
  • 4
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • Huang B., Bates M., Zhuang X. Super-resolution fluorescence microscopy. Annu Rev Biochem 2009, 78:993-1016.
    • (2009) Annu Rev Biochem , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 7
    • 54149113310 scopus 로고    scopus 로고
    • High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes
    • Ando T., Uchihashi T., Fukuma T. High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes. Prog Surf Sci 2008, 83:337-437.
    • (2008) Prog Surf Sci , vol.83 , pp. 337-437
    • Ando, T.1    Uchihashi, T.2    Fukuma, T.3
  • 8
    • 84877779703 scopus 로고    scopus 로고
    • High-speed AFM and applications to biomolecular systems
    • Ando T., Uchihashi T., Kodera N. High-speed AFM and applications to biomolecular systems. Annu Rev Biophys 2013, 42:393-414.
    • (2013) Annu Rev Biophys , vol.42 , pp. 393-414
    • Ando, T.1    Uchihashi, T.2    Kodera, N.3
  • 9
    • 84855981532 scopus 로고    scopus 로고
    • High-speed atomic force microscopy coming of age
    • Ando T. High-speed atomic force microscopy coming of age. Nanotechnology 2012, 23:062001.
    • (2012) Nanotechnology , vol.23 , pp. 062001
    • Ando, T.1
  • 10
    • 84896608413 scopus 로고    scopus 로고
    • Filming biomolecular processes by high-speed atomic force microscopy
    • Ando T., Uchihashi T., Scheuring S. Filming biomolecular processes by high-speed atomic force microscopy. Chem Rev 2014, 114:3120-3188.
    • (2014) Chem Rev , vol.114 , pp. 3120-3188
    • Ando, T.1    Uchihashi, T.2    Scheuring, S.3
  • 11
    • 84864856920 scopus 로고    scopus 로고
    • Single molecule imaging on living bacterial cell surface by high-speed AFM
    • Yamashita H., Taoka A., Uchihashi T., Asano T., Ando T., Fukumori Y. Single molecule imaging on living bacterial cell surface by high-speed AFM. J Mol Biol 2012, 422:300-309.
    • (2012) J Mol Biol , vol.422 , pp. 300-309
    • Yamashita, H.1    Taoka, A.2    Uchihashi, T.3    Asano, T.4    Ando, T.5    Fukumori, Y.6
  • 12
    • 84880364773 scopus 로고    scopus 로고
    • A hybrid high-speed atomic force-optical microscope for visualizing single membrane proteins on eukaryotic cells
    • Colom A., Casuso I., Rico F., Scheuring S. A hybrid high-speed atomic force-optical microscope for visualizing single membrane proteins on eukaryotic cells. Nat Commun 2013, 4:2155.
    • (2013) Nat Commun , vol.4 , pp. 2155
    • Colom, A.1    Casuso, I.2    Rico, F.3    Scheuring, S.4
  • 14
    • 84865814021 scopus 로고    scopus 로고
    • Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy
    • Uchihashi T., Kodera N., Ando T. Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy. Nat Protoc 2012, 7:1193-1206.
    • (2012) Nat Protoc , vol.7 , pp. 1193-1206
    • Uchihashi, T.1    Kodera, N.2    Ando, T.3
  • 15
    • 79955510966 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy
    • Shibata M., Uchihashi T., Yamashita H., Kandori H., Ando T. Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy. Angew Chem Int Ed 2011, 50:4410-4413.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 4410-4413
    • Shibata, M.1    Uchihashi, T.2    Yamashita, H.3    Kandori, H.4    Ando, T.5
  • 16
    • 77749324964 scopus 로고    scopus 로고
    • High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin
    • Shibata M., Yamashita H., Uchihashi T., Kandori H., Ando T. High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin. Nat Nanotechnol 2010, 5:208-212.
    • (2010) Nat Nanotechnol , vol.5 , pp. 208-212
    • Shibata, M.1    Yamashita, H.2    Uchihashi, T.3    Kandori, H.4    Ando, T.5
  • 17
    • 84884820053 scopus 로고    scopus 로고
    • Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy
    • Yamashita H., Inoue K., Shibata M., Uchihashi T., Sasaki J., Kandori H., Ando T. Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy. J Struct Biol 2013, 184:2-11.
    • (2013) J Struct Biol , vol.184 , pp. 2-11
    • Yamashita, H.1    Inoue, K.2    Shibata, M.3    Uchihashi, T.4    Sasaki, J.5    Kandori, H.6    Ando, T.7
  • 21
  • 22
    • 77954176463 scopus 로고    scopus 로고
    • Acid-sensing ion channel (ASIC) 1a undergoes a height transition in response to acidification
    • Yokokawa M., Carnally S.M., Henderson R.M., Takeyasu K., Edwardson J.M. Acid-sensing ion channel (ASIC) 1a undergoes a height transition in response to acidification. FEBS Lett 2010, 584:3107-3110.
    • (2010) FEBS Lett , vol.584 , pp. 3107-3110
    • Yokokawa, M.1    Carnally, S.M.2    Henderson, R.M.3    Takeyasu, K.4    Edwardson, J.M.5
  • 23
    • 77949908054 scopus 로고    scopus 로고
    • AAA+ chaperone ClpX regurates dynamics of prokaryotic cytoskeletal protein FtsZ
    • Sugimoto S., Yamanaka K., Nishikori S., Miyagi A., Ando T., Ogura T. AAA+ chaperone ClpX regurates dynamics of prokaryotic cytoskeletal protein FtsZ. J Biol Chem 2010, 285:6648-6657.
    • (2010) J Biol Chem , vol.285 , pp. 6648-6657
    • Sugimoto, S.1    Yamanaka, K.2    Nishikori, S.3    Miyagi, A.4    Ando, T.5    Ogura, T.6
  • 24
    • 84887402236 scopus 로고    scopus 로고
    • High-speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97
    • Noi K., Yamamoto D., Nishikori S., Arita-Morioka K., Ando T., Ogura T. High-speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97. Structure 2013, 21:1992-2002.
    • (2013) Structure , vol.21 , pp. 1992-2002
    • Noi, K.1    Yamamoto, D.2    Nishikori, S.3    Arita-Morioka, K.4    Ando, T.5    Ogura, T.6
  • 25
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin V by high-speed atomic force microscopy
    • Kodera N., Yamamoto D., Ishikawa R., Ando T. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 2010, 468:72-76.
    • (2010) Nature , vol.468 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 26
    • 84866492389 scopus 로고    scopus 로고
    • High-speed atomic force microscopy: cooperative adhesion and dynamic equilibrium of junctional microdomain membrane proteins
    • Colom A., Casuso I., Boudier T., Scheuring S. High-speed atomic force microscopy: cooperative adhesion and dynamic equilibrium of junctional microdomain membrane proteins. J Mol Biol 2012, 423:249-256.
    • (2012) J Mol Biol , vol.423 , pp. 249-256
    • Colom, A.1    Casuso, I.2    Boudier, T.3    Scheuring, S.4
  • 28
    • 51349093802 scopus 로고    scopus 로고
    • Anisotropic diffusion of point defects in two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy
    • Yamamoto D., Uchihashi T., Kodera N., Ando T. Anisotropic diffusion of point defects in two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy. Nanotechnology 2008, 19:384009.
    • (2008) Nanotechnology , vol.19 , pp. 384009
    • Yamamoto, D.1    Uchihashi, T.2    Kodera, N.3    Ando, T.4
  • 29
    • 77958178581 scopus 로고    scopus 로고
    • Experimental evidence for membrane-mediated protein-protein interaction
    • Casuso I., Sens P., Rico F., Scheuring S. Experimental evidence for membrane-mediated protein-protein interaction. Biophys J 2010, 99:L47-L49.
    • (2010) Biophys J , vol.99
    • Casuso, I.1    Sens, P.2    Rico, F.3    Scheuring, S.4
  • 32
    • 84884340337 scopus 로고    scopus 로고
    • Real-time visualization of assembling of a sphingomyelin-specific toxin
    • Yilmaz N., Yamada T., Greimel P., Uchihashi T., Ando T., Kobayashi T. Real-time visualization of assembling of a sphingomyelin-specific toxin. Biophys J 2013, 105:1397-1405.
    • (2013) Biophys J , vol.105 , pp. 1397-1405
    • Yilmaz, N.1    Yamada, T.2    Greimel, P.3    Uchihashi, T.4    Ando, T.5    Kobayashi, T.6
  • 33
    • 53049099593 scopus 로고    scopus 로고
    • Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy
    • Miyagi A., Tsunaka Y., Uchihashi T., Mayanagi K., Hirose S., Morikawa K., Ando T. Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy. Chem Phys Chem 2008, 9:1859-1866.
    • (2008) Chem Phys Chem , vol.9 , pp. 1859-1866
    • Miyagi, A.1    Tsunaka, Y.2    Uchihashi, T.3    Mayanagi, K.4    Hirose, S.5    Morikawa, K.6    Ando, T.7
  • 34
    • 84878138537 scopus 로고    scopus 로고
    • Phosphorylation-coupled intramolecular dynamics of unstructured regions in chromatin remodeler FACT
    • Hashimoto M., Kodera N., Tsunaka Y., Oda M., Tanimoto M., Ando T., Morikawa K., Tate S. Phosphorylation-coupled intramolecular dynamics of unstructured regions in chromatin remodeler FACT. Biophys J 2013, 104:2222-2234.
    • (2013) Biophys J , vol.104 , pp. 2222-2234
    • Hashimoto, M.1    Kodera, N.2    Tsunaka, Y.3    Oda, M.4    Tanimoto, M.5    Ando, T.6    Morikawa, K.7    Tate, S.8
  • 35
    • 79955497376 scopus 로고    scopus 로고
    • Spindle microtubules generate tension-dependent changes in the distribution of inner kinetochore proteins
    • Suzuki A., Hori T., Nishino T., Usukura J., Miyagi A., Morikawa K., Fukagawa T. Spindle microtubules generate tension-dependent changes in the distribution of inner kinetochore proteins. J Cell Biol 2011, 193:125-140.
    • (2011) J Cell Biol , vol.193 , pp. 125-140
    • Suzuki, A.1    Hori, T.2    Nishino, T.3    Usukura, J.4    Miyagi, A.5    Morikawa, K.6    Fukagawa, T.7
  • 37
    • 84857407275 scopus 로고    scopus 로고
    • Specificity of binding of single-stranded DNA-binding protein to its target
    • Shlyakhtenko L.S., Lushnikov A.Y., Miyagi A., Lyubchenko Y.L. Specificity of binding of single-stranded DNA-binding protein to its target. Biochemistry 2012, 51:1500-1509.
    • (2012) Biochemistry , vol.51 , pp. 1500-1509
    • Shlyakhtenko, L.S.1    Lushnikov, A.Y.2    Miyagi, A.3    Lyubchenko, Y.L.4
  • 38
    • 84055217526 scopus 로고    scopus 로고
    • Visual analysis of concerted cleavage by type IIF restriction enzyme SfiI in subsecond time region
    • Suzuki Y., Gilmore J.L., Yoshimura S.H., Henderson R.M., Lyubchenko Y.L., Takeyasu K. Visual analysis of concerted cleavage by type IIF restriction enzyme SfiI in subsecond time region. Biophys J 2011, 101:2992-2998.
    • (2011) Biophys J , vol.101 , pp. 2992-2998
    • Suzuki, Y.1    Gilmore, J.L.2    Yoshimura, S.H.3    Henderson, R.M.4    Lyubchenko, Y.L.5    Takeyasu, K.6
  • 40
    • 80052704421 scopus 로고    scopus 로고
    • Dynamics of nucleosomes assessed with time-lapse high-speed atomic force microscopy
    • Miyagi A., Ando T., Lyubchenko Y.L. Dynamics of nucleosomes assessed with time-lapse high-speed atomic force microscopy. Biochemistry 2011, 50:7901-7908.
    • (2011) Biochemistry , vol.50 , pp. 7901-7908
    • Miyagi, A.1    Ando, T.2    Lyubchenko, Y.L.3
  • 41
    • 77952348128 scopus 로고    scopus 로고
    • High-speed atomic force microscopy for large scan sizes using small cantilevers
    • Braunsmann C., Schäffer T.E. High-speed atomic force microscopy for large scan sizes using small cantilevers. Nanotechnology 2010, 21:225705.
    • (2010) Nanotechnology , vol.21 , pp. 225705
    • Braunsmann, C.1    Schäffer, T.E.2
  • 42
    • 77950860384 scopus 로고    scopus 로고
    • Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy
    • Fantner G.E., Barbero R.J., Gray D.S., Belcher A.M. Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy. Nat Nanotechnol 2010, 5:280-285.
    • (2010) Nat Nanotechnol , vol.5 , pp. 280-285
    • Fantner, G.E.1    Barbero, R.J.2    Gray, D.S.3    Belcher, A.M.4
  • 44
    • 84862476813 scopus 로고    scopus 로고
    • Tip-enhanced fluorescence microscopy at 10 nanometer resolution
    • Gerton J.M., Wade L.A., Lessard G.A., Ma Z., Quake S.R. Tip-enhanced fluorescence microscopy at 10 nanometer resolution. Phys Rev Lett 2004, 93:180801.
    • (2004) Phys Rev Lett , vol.93 , pp. 180801
    • Gerton, J.M.1    Wade, L.A.2    Lessard, G.A.3    Ma, Z.4    Quake, S.R.5
  • 45
    • 0033032860 scopus 로고    scopus 로고
    • Evanescent field excitation and measurement of dye fluorescence in a metallic probe near-field scanning optical microscope
    • Hayazawa N., Inouye Y., Kawata S. Evanescent field excitation and measurement of dye fluorescence in a metallic probe near-field scanning optical microscope. J Microsc 1999, 194:472-476.
    • (1999) J Microsc , vol.194 , pp. 472-476
    • Hayazawa, N.1    Inouye, Y.2    Kawata, S.3


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