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Volumn 13, Issue 5, 2008, Pages 316-325

Use of AFM in bio-related systems

Author keywords

[No Author keywords available]

Indexed keywords

MICROSCOPIC EXAMINATION;

EID: 49849092263     PISSN: 13590294     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cocis.2008.02.002     Document Type: Review
Times cited : (46)

References (77)
  • 3
  • 4
    • 4244111185 scopus 로고
    • Tunneling microscope through a controllable vacuum gap
    • Binnig G., and Rohrer H. Tunneling microscope through a controllable vacuum gap. Appl Phys Lett 40 (1982) 178-180
    • (1982) Appl Phys Lett , vol.40 , pp. 178-180
    • Binnig, G.1    Rohrer, H.2
  • 5
    • 0021410769 scopus 로고
    • Optical stethoscopy: image recording with resolution l / 20
    • Pohl D.W., Denk W., and Lanz M. Optical stethoscopy: image recording with resolution l / 20. Appl Phys Lett 44 (1984) 651-653
    • (1984) Appl Phys Lett , vol.44 , pp. 651-653
    • Pohl, D.W.1    Denk, W.2    Lanz, M.3
  • 6
    • 0021287941 scopus 로고
    • Development of a 500 Å spatial resolution light microscope: 1. Light is efficiently transmitted through l / 16 diameter apertures
    • Lewis A., Isaacson M., Harootunian A., and Murray A. Development of a 500 Å spatial resolution light microscope: 1. Light is efficiently transmitted through l / 16 diameter apertures. Ultramicroscopy 13 (1984) 227-228
    • (1984) Ultramicroscopy , vol.13 , pp. 227-228
    • Lewis, A.1    Isaacson, M.2    Harootunian, A.3    Murray, A.4
  • 7
    • 0000704117 scopus 로고
    • The topografiner: an instrument for measuring surface microtopography
    • Young R., Ward J., and Scire F. The topografiner: an instrument for measuring surface microtopography. Rev Sci Instrum 43 (1972) 999-1011
    • (1972) Rev Sci Instrum , vol.43 , pp. 999-1011
    • Young, R.1    Ward, J.2    Scire, F.3
  • 9
    • 20844437419 scopus 로고    scopus 로고
    • True molecular resolution in liquid by frequency-modulation atomic force microscopy
    • Fukuma T., Kobayashi K., Matsushige K., and Yamada H. True molecular resolution in liquid by frequency-modulation atomic force microscopy. Appl Phys Lett 86 (2005) 193108-193110
    • (2005) Appl Phys Lett , vol.86 , pp. 193108-193110
    • Fukuma, T.1    Kobayashi, K.2    Matsushige, K.3    Yamada, H.4
  • 10
    • 33847721438 scopus 로고    scopus 로고
    • Direct imaging of lipid-ion network formation under physiological conditions by frequency modulation atomic force microscopy
    • Fukuma T., Higgins M.J., and Jarvis S.P. Direct imaging of lipid-ion network formation under physiological conditions by frequency modulation atomic force microscopy. Phys Rev Lett 98 (2007) 106101-106104
    • (2007) Phys Rev Lett , vol.98 , pp. 106101-106104
    • Fukuma, T.1    Higgins, M.J.2    Jarvis, S.P.3
  • 12
    • 49849083256 scopus 로고    scopus 로고
    • Azobenzene-containing Langmuir-Blodgett films in the near field of a scanning Kelvin microscope tip by irradiation
    • Karageorgiev P., Stiller B., Prescher D., Dietzel B., Schulz B., and Brehmer L. Azobenzene-containing Langmuir-Blodgett films in the near field of a scanning Kelvin microscope tip by irradiation. Langmuir 16 (2000) 515-518
    • (2000) Langmuir , vol.16 , pp. 515-518
    • Karageorgiev, P.1    Stiller, B.2    Prescher, D.3    Dietzel, B.4    Schulz, B.5    Brehmer, L.6
  • 13
    • 0000136456 scopus 로고    scopus 로고
    • Surface potential images of microstructured organosilane self-assembled monolayers acquired by Kelvin probe force microscopy
    • Sugimura H., Hayashi K., Saito N., Takai O., and Nakagiri N. Surface potential images of microstructured organosilane self-assembled monolayers acquired by Kelvin probe force microscopy. Jpn J Appl Phys 40 (2001) L174-L176
    • (2001) Jpn J Appl Phys , vol.40
    • Sugimura, H.1    Hayashi, K.2    Saito, N.3    Takai, O.4    Nakagiri, N.5
  • 14
    • 0035848210 scopus 로고    scopus 로고
    • Unambiguous interpretation of atomically resolved force microscopy images of an insulator
    • Foster A.S., Barth C., Shluger A.L., and Reichling M. Unambiguous interpretation of atomically resolved force microscopy images of an insulator. Phys Rev Lett 86 (2001) 2373-2376
    • (2001) Phys Rev Lett , vol.86 , pp. 2373-2376
    • Foster, A.S.1    Barth, C.2    Shluger, A.L.3    Reichling, M.4
  • 15
    • 33646677697 scopus 로고    scopus 로고
    • Real topography, atomic relaxations, and short-range chemical interactions in atomic force microscopy: the case of the a-Sn/Si(111)-(√3 × √3)R30 surface
    • Sugimoto Y., Custance O., Jelinek P., Morita S., Pérez R., and Abe M. Real topography, atomic relaxations, and short-range chemical interactions in atomic force microscopy: the case of the a-Sn/Si(111)-(√3 × √3)R30 surface. Phys Rev B 73 (2006) 205329-205337
    • (2006) Phys Rev B , vol.73 , pp. 205329-205337
    • Sugimoto, Y.1    Custance, O.2    Jelinek, P.3    Morita, S.4    Pérez, R.5    Abe, M.6
  • 18
    • 8744234038 scopus 로고    scopus 로고
    • Algorithms for scanned probe microscope image simulation, surface reconstruction, and tip estimation
    • Villarrubia J.S. Algorithms for scanned probe microscope image simulation, surface reconstruction, and tip estimation. J Res Natl Inst Stand Technol 102 (1997) 425-455
    • (1997) J Res Natl Inst Stand Technol , vol.102 , pp. 425-455
    • Villarrubia, J.S.1
  • 19
    • 0031273451 scopus 로고    scopus 로고
    • On the factors affecting the contrast of height and phase images in tapping mode atomic force microscopy
    • Brandsch Bar G., and Whangbo M.H. On the factors affecting the contrast of height and phase images in tapping mode atomic force microscopy. Langmuir 13 (1997) 6349-6353
    • (1997) Langmuir , vol.13 , pp. 6349-6353
    • Brandsch Bar, G.1    Whangbo, M.H.2
  • 20
    • 12844268321 scopus 로고
    • Scanning tunneling and atomic force microscopy studies of Langmuir-Blodgett films
    • Derose J.A., and Leblanc R.M. Scanning tunneling and atomic force microscopy studies of Langmuir-Blodgett films. Surf Sci Rep 22 (1995) 73-126
    • (1995) Surf Sci Rep , vol.22 , pp. 73-126
    • Derose, J.A.1    Leblanc, R.M.2
  • 21
    • 0034695038 scopus 로고    scopus 로고
    • Advances in the characterization of supported lipid films with the atomic force microscope
    • Dufrêne Y.F., and Lee G.U. Advances in the characterization of supported lipid films with the atomic force microscope. Biochim Bhiophys Acta 1509 (2000) 14-41
    • (2000) Biochim Bhiophys Acta , vol.1509 , pp. 14-41
    • Dufrêne, Y.F.1    Lee, G.U.2
  • 23
    • 0000363707 scopus 로고
    • Atomic scale imaging of alkanethiolate monolayers at gold surfaces with atomic force microscopy
    • Alves C.A., Smith E.L., and Porter M.D. Atomic scale imaging of alkanethiolate monolayers at gold surfaces with atomic force microscopy. J Am Chem Soc 114 (1992) 1222-1227
    • (1992) J Am Chem Soc , vol.114 , pp. 1222-1227
    • Alves, C.A.1    Smith, E.L.2    Porter, M.D.3
  • 24
    • 0000147076 scopus 로고
    • Domain structures in Langmuir-Blodgett films investigated by atomic force microscopy
    • Chi L.F., Anders M., Fuchs H., Johynston R.R., and Ringsdorf H. Domain structures in Langmuir-Blodgett films investigated by atomic force microscopy. Science 259 (1993) 213-216
    • (1993) Science , vol.259 , pp. 213-216
    • Chi, L.F.1    Anders, M.2    Fuchs, H.3    Johynston, R.R.4    Ringsdorf, H.5
  • 25
    • 0031352107 scopus 로고    scopus 로고
    • Quantitative analysis of holes in supported bilayers providing the adsorption energy of surfactants on solid substrate
    • Bassereau P., and Pincet F. Quantitative analysis of holes in supported bilayers providing the adsorption energy of surfactants on solid substrate. Langmuir 13 (1997) 7003-7007
    • (1997) Langmuir , vol.13 , pp. 7003-7007
    • Bassereau, P.1    Pincet, F.2
  • 26
    • 0029069245 scopus 로고
    • Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids
    • Mou J., Yang J., and Shao Z. Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids. J Mol Biol 248 (1995) 507-512
    • (1995) J Mol Biol , vol.248 , pp. 507-512
    • Mou, J.1    Yang, J.2    Shao, Z.3
  • 27
    • 0026168724 scopus 로고
    • Imaging nanometer scale defects in Langmuir-Blodgett films with the atomic force microscope
    • Hansma H.G., Gould S.A.C., Hansma P.K., Gaub H.E., Longo M.L., and Zasadzinski J.A.N. Imaging nanometer scale defects in Langmuir-Blodgett films with the atomic force microscope. Langmuir 7 (1991) 1051-1054
    • (1991) Langmuir , vol.7 , pp. 1051-1054
    • Hansma, H.G.1    Gould, S.A.C.2    Hansma, P.K.3    Gaub, H.E.4    Longo, M.L.5    Zasadzinski, J.A.N.6
  • 29
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A., and Müller D.J. Observing single biomolecules at work with the atomic force microscope. Nat Struct Biol 7 (2000) 715-718
    • (2000) Nat Struct Biol , vol.7 , pp. 715-718
    • Engel, A.1    Müller, D.J.2
  • 30
    • 33846940059 scopus 로고    scopus 로고
    • Mechanical unfolding of proteins: insights into biology, structure and folding
    • Forman J.R., and Clarke J. Mechanical unfolding of proteins: insights into biology, structure and folding. Curr Opin Struct Biol 17 (2007) 58-66
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 58-66
    • Forman, J.R.1    Clarke, J.2
  • 31
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Reif M., Gautel M., Oesterhelt F., Fernandez J.M., and Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276 (1997) 1109-1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Reif, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 32
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • Fisher T.E., Marszalek P.E., and Fernandez J.M. Stretching single molecules into novel conformations using the atomic force microscope. Nat Struct Biol 7 (2000) 719-724
    • (2000) Nat Struct Biol , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 35
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez J.M., and Li H. Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science 303 (2004) 1674-1678
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 36
    • 13444306206 scopus 로고    scopus 로고
    • Protein unfolding and refolding under force: methodologies for nanomechanics
    • Samori B., Zuccheri G., and Bachieri P. Protein unfolding and refolding under force: methodologies for nanomechanics. Chem Phys Chem 6 (2005) 29-34
    • (2005) Chem Phys Chem , vol.6 , pp. 29-34
    • Samori, B.1    Zuccheri, G.2    Bachieri, P.3
  • 37
    • 0029883621 scopus 로고    scopus 로고
    • Detection and localization of individual antibody-antigen recognition events by atomic force microscopy
    • Hinterdorfer P., Baumgartner W., Gruber H.J., Schilcher K., and Schindler H. Detection and localization of individual antibody-antigen recognition events by atomic force microscopy. Proc Natl Acad Sci USA 93 (1996) 3477-3481
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3477-3481
    • Hinterdorfer, P.1    Baumgartner, W.2    Gruber, H.J.3    Schilcher, K.4    Schindler, H.5
  • 38
    • 0028309424 scopus 로고
    • Adhesive forces between individual ligand-receptor pairs
    • Florin E.L., Moy V.T., and Gaub H.E. Adhesive forces between individual ligand-receptor pairs. Science 264 (1994) 415-417
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 39
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Reif M., Gautel M., Oesterhelt F., Fernandez J.M., and Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276 (1997) 1109-1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Reif, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 41
    • 2442448427 scopus 로고    scopus 로고
    • The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
    • Schlierf M., Li H.B., and Fernandez J.M. The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques. Proc Natl Acad Sci USA 101 (2004) 7299-7304
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7299-7304
    • Schlierf, M.1    Li, H.B.2    Fernandez, J.M.3
  • 42
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez J.M., and Li H. Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science 303 (2004) 1674-1678
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 43
    • 34147138772 scopus 로고    scopus 로고
    • Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy
    • Brujic J., Hermans R.I.Z., Garcia-Manyes S., Walther K., and Fernandez J.M. Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy. Biophys J 92 (2007) 2896-2903
    • (2007) Biophys J , vol.92 , pp. 2896-2903
    • Brujic, J.1    Hermans, R.I.Z.2    Garcia-Manyes, S.3    Walther, K.4    Fernandez, J.M.5
  • 44
    • 0035022143 scopus 로고    scopus 로고
    • From images to interactions: high-resolution phase imaging in tapping-mode atomic force microscopy
    • Stark M., Möller C., Müller D.J., and Guckenberger R. From images to interactions: high-resolution phase imaging in tapping-mode atomic force microscopy. Biophys J 80 (2001) 3009-3018
    • (2001) Biophys J , vol.80 , pp. 3009-3018
    • Stark, M.1    Möller, C.2    Müller, D.J.3    Guckenberger, R.4
  • 45
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: what is achieved and what is needed
    • Shao Z., Jou J., Czaijkowsky D.M., Yang J., and Yuan J.Y. Biological atomic force microscopy: what is achieved and what is needed. Adv Phys 45 (1996) 1-86
    • (1996) Adv Phys , vol.45 , pp. 1-86
    • Shao, Z.1    Jou, J.2    Czaijkowsky, D.M.3    Yang, J.4    Yuan, J.Y.5
  • 46
    • 34147216110 scopus 로고    scopus 로고
    • Ultra-resolution imaging of a self-assembling biomolecular system using robust carbon nanotube AFM probes
    • Carnally S., Barrow K., Alexander M.R., Hayes C.J., Stolnik S., Tendler S.J.B., et al. Ultra-resolution imaging of a self-assembling biomolecular system using robust carbon nanotube AFM probes. Langmuir 23 (2007) 3906-3911
    • (2007) Langmuir , vol.23 , pp. 3906-3911
    • Carnally, S.1    Barrow, K.2    Alexander, M.R.3    Hayes, C.J.4    Stolnik, S.5    Tendler, S.J.B.6
  • 47
    • 4644327867 scopus 로고    scopus 로고
    • Single-walled carbon nanotube AFM probes: optimal imaging resolution of nanoclusters and biomolecules in ambient and fluid environment
    • Chen L., Cheung C.L., Ashby P.D., and Lieber C.M. Single-walled carbon nanotube AFM probes: optimal imaging resolution of nanoclusters and biomolecules in ambient and fluid environment. Nano Lett 4 (2004) 1725-1731
    • (2004) Nano Lett , vol.4 , pp. 1725-1731
    • Chen, L.1    Cheung, C.L.2    Ashby, P.D.3    Lieber, C.M.4
  • 48
    • 33751225988 scopus 로고    scopus 로고
    • High resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer
    • Milhiet P.E., Gubellini F., Berquand A., Dosset P., Rigaud J.L., Le Grimellec C., et al. High resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer. Biophys J 91 (2006) 3268-3275
    • (2006) Biophys J , vol.91 , pp. 3268-3275
    • Milhiet, P.E.1    Gubellini, F.2    Berquand, A.3    Dosset, P.4    Rigaud, J.L.5    Le Grimellec, C.6
  • 49
    • 0032170742 scopus 로고    scopus 로고
    • Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer
    • Bayburt T.H., Carlson J.W., and Sligar S.G. Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer. J Struct Biol 123 (1998) 37-44
    • (1998) J Struct Biol , vol.123 , pp. 37-44
    • Bayburt, T.H.1    Carlson, J.W.2    Sligar, S.G.3
  • 50
    • 0141785134 scopus 로고    scopus 로고
    • Adsorption of DNA to mica mediated by divalent counterions: a theoretical and experimental study
    • Pastré D., Piétrement O., Fusil S., Landousy F., Jeusset J., David M.O., et al. Adsorption of DNA to mica mediated by divalent counterions: a theoretical and experimental study. Biophys J 85 (2003) 2507-2518
    • (2003) Biophys J , vol.85 , pp. 2507-2518
    • Pastré, D.1    Piétrement, O.2    Fusil, S.3    Landousy, F.4    Jeusset, J.5    David, M.O.6
  • 51
    • 0033513804 scopus 로고    scopus 로고
    • Two-dimensional crystallization of proteins on lipid monolayers at the air-water interface and transfer to an electron microscopy grid
    • Brisson A., Bergsma-Schutter W., Oling F., Lambert O., and Reviakine I. Two-dimensional crystallization of proteins on lipid monolayers at the air-water interface and transfer to an electron microscopy grid. J Cryst Growth 196 (1999) 456-470
    • (1999) J Cryst Growth , vol.196 , pp. 456-470
    • Brisson, A.1    Bergsma-Schutter, W.2    Oling, F.3    Lambert, O.4    Reviakine, I.5
  • 55
    • 17044388175 scopus 로고    scopus 로고
    • A mechanical microscope: high-speed atomic force microscopy
    • Humphris A.D.L., Miles M.J., and Hobbs J.K. A mechanical microscope: high-speed atomic force microscopy. Appl Phys Lett 86 (2005) 034106-034108
    • (2005) Appl Phys Lett , vol.86 , pp. 034106-034108
    • Humphris, A.D.L.1    Miles, M.J.2    Hobbs, J.K.3
  • 56
    • 0031028425 scopus 로고    scopus 로고
    • Escherichia coli RNA polymerase activity observed using atomic force microscopy
    • Kasas S., Thomson N.H., Smith B.L., Hansma H.G., Zhu X., Guthold M., et al. Escherichia coli RNA polymerase activity observed using atomic force microscopy. Biochemistry 36 (1997) 461-468
    • (1997) Biochemistry , vol.36 , pp. 461-468
    • Kasas, S.1    Thomson, N.H.2    Smith, B.L.3    Hansma, H.G.4    Zhu, X.5    Guthold, M.6
  • 57
    • 0035942167 scopus 로고    scopus 로고
    • Visualization of unwinding activity of duplex RNA by dbpA, a DEAD box helicase, at single-molecule resolution by atomic force microscopy
    • Henn A., Medalia O., Shi S.P., Steinberg M., Francheschi F., and Sagi I. Visualization of unwinding activity of duplex RNA by dbpA, a DEAD box helicase, at single-molecule resolution by atomic force microscopy. Proc Nat Acad Sci USA 98 (2001) 5007-5012
    • (2001) Proc Nat Acad Sci USA , vol.98 , pp. 5007-5012
    • Henn, A.1    Medalia, O.2    Shi, S.P.3    Steinberg, M.4    Francheschi, F.5    Sagi, I.6
  • 59
    • 22444442001 scopus 로고    scopus 로고
    • Relationship between interfacial forces measured by colloid-probe atomic force microscopy and protein resistance of poly(ethylene glycol)-grafted poly(l-lysine) adlayers on niobia surfaces
    • Pasche S., Textor M., Meagher L., Spencer N.D., and Griesser H.J. Relationship between interfacial forces measured by colloid-probe atomic force microscopy and protein resistance of poly(ethylene glycol)-grafted poly(l-lysine) adlayers on niobia surfaces. Langmuir 21 (2005) 6508-6520
    • (2005) Langmuir , vol.21 , pp. 6508-6520
    • Pasche, S.1    Textor, M.2    Meagher, L.3    Spencer, N.D.4    Griesser, H.J.5
  • 60
    • 0033772174 scopus 로고    scopus 로고
    • Discrete molecular interactions in cell adhesion measured by force spectroscopy
    • Benoit M., Gabriel D., Gerisch G., and Gaub H.E. Discrete molecular interactions in cell adhesion measured by force spectroscopy. Nat Cell Biol 2 (2000) 313-317
    • (2000) Nat Cell Biol , vol.2 , pp. 313-317
    • Benoit, M.1    Gabriel, D.2    Gerisch, G.3    Gaub, H.E.4
  • 61
    • 4544250739 scopus 로고    scopus 로고
    • Surface probe measurements of the elasticity of sectioned tissue, thin gels and polyelectrolyte multilayer films: correlations between substrate stiffness and cell adhesion
    • Engler A.J., Richert L., Wong J.Y., Picart C., and Discher D.E. Surface probe measurements of the elasticity of sectioned tissue, thin gels and polyelectrolyte multilayer films: correlations between substrate stiffness and cell adhesion. Surf Sci 570 (2004) 142-154
    • (2004) Surf Sci , vol.570 , pp. 142-154
    • Engler, A.J.1    Richert, L.2    Wong, J.Y.3    Picart, C.4    Discher, D.E.5
  • 62
    • 0037783430 scopus 로고    scopus 로고
    • Nanoscale mapping of the elasticity of microbial cells by atomic force microscopy
    • Touhami A., Nysten B., and Dufrêne Y.F. Nanoscale mapping of the elasticity of microbial cells by atomic force microscopy. Langmuir 19 (2003) 4539-4543
    • (2003) Langmuir , vol.19 , pp. 4539-4543
    • Touhami, A.1    Nysten, B.2    Dufrêne, Y.F.3
  • 64
    • 0036916050 scopus 로고    scopus 로고
    • Measuring cell adhesion forces with the atomic force microscope at the molecular level
    • Benoit M., and Gaub H.E. Measuring cell adhesion forces with the atomic force microscope at the molecular level. Cells Tissues Organs 172 (2002) 174-189
    • (2002) Cells Tissues Organs , vol.172 , pp. 174-189
    • Benoit, M.1    Gaub, H.E.2
  • 65
    • 27744587245 scopus 로고    scopus 로고
    • Force measurements with the atomic force microscope: technique, interpretation and applications
    • Butt H.J., Cappella B., and Kappl M. Force measurements with the atomic force microscope: technique, interpretation and applications. Surf Sci Reports 59 (2005) 1-152
    • (2005) Surf Sci Reports , vol.59 , pp. 1-152
    • Butt, H.J.1    Cappella, B.2    Kappl, M.3
  • 66
    • 33748798176 scopus 로고    scopus 로고
    • Cell mechanics using atomic force microscopy-based single-cell compression
    • Lulevich V., Zink T., Chen H.Y., Liu F.T., and Liu G.Y. Cell mechanics using atomic force microscopy-based single-cell compression. Langmuir 22 (2006) 8151-8155
    • (2006) Langmuir , vol.22 , pp. 8151-8155
    • Lulevich, V.1    Zink, T.2    Chen, H.Y.3    Liu, F.T.4    Liu, G.Y.5
  • 67
    • 33646195654 scopus 로고    scopus 로고
    • Force microscopy of nonadherent cells: a comparison of leukemia cell deformability
    • Rosenbluth M.J., Lam W.A., and Fletcher D.A. Force microscopy of nonadherent cells: a comparison of leukemia cell deformability. Biophys J 90 (2006) 2994-3003
    • (2006) Biophys J , vol.90 , pp. 2994-3003
    • Rosenbluth, M.J.1    Lam, W.A.2    Fletcher, D.A.3
  • 68
    • 84870682377 scopus 로고    scopus 로고
    • Electrical scanning probe microscopy of biomolecules on surfaces and at interfaces
    • Kalinin S., and Gruverman A. (Eds), Springer, New York
    • Lee I., and Greenbaum E. Electrical scanning probe microscopy of biomolecules on surfaces and at interfaces. In: Kalinin S., and Gruverman A. (Eds). Scanning probe microscopy electrical and electromechanical phenomena at the nanoscale (2007), Springer, New York 601-614
    • (2007) Scanning probe microscopy electrical and electromechanical phenomena at the nanoscale , pp. 601-614
    • Lee, I.1    Greenbaum, E.2
  • 69
    • 0000123454 scopus 로고    scopus 로고
    • Measurement of electrostatic potentials above oriented single photosynthetic reaction centers
    • Lee I., Lee J.W., Stubna A., and Greenbaum E. Measurement of electrostatic potentials above oriented single photosynthetic reaction centers. J Phys Chem B 104 (2000) 2439-2443
    • (2000) J Phys Chem B , vol.104 , pp. 2439-2443
    • Lee, I.1    Lee, J.W.2    Stubna, A.3    Greenbaum, E.4
  • 70
    • 27144435179 scopus 로고    scopus 로고
    • Fabrication of a photoelectronic device by direct chemical binding of the photosynthetic reaction center protein to metal surfaces
    • Frolov L., Rosenwaks Y., Carmeli C., and Carmeli I. Fabrication of a photoelectronic device by direct chemical binding of the photosynthetic reaction center protein to metal surfaces. Adv Mater 17 (2005) 2434-2437
    • (2005) Adv Mater , vol.17 , pp. 2434-2437
    • Frolov, L.1    Rosenwaks, Y.2    Carmeli, C.3    Carmeli, I.4
  • 71
  • 72
    • 33744797638 scopus 로고    scopus 로고
    • Sequence dependence of charge transport properties of DNA
    • Nogues C., Cohen S.R., Daube S., Apter N., and Naaman R. Sequence dependence of charge transport properties of DNA. J Phys Chem B 110 (2006) 8910-8913
    • (2006) J Phys Chem B , vol.110 , pp. 8910-8913
    • Nogues, C.1    Cohen, S.R.2    Daube, S.3    Apter, N.4    Naaman, R.5
  • 73
    • 23844550265 scopus 로고    scopus 로고
    • Direct measurement of electrical transport through single DNA molecules of complex sequence
    • Cohen H., Nogues C., Naaman R., and Porath D. Direct measurement of electrical transport through single DNA molecules of complex sequence. Proc Natl Acad Sci 102 (2005) 11589-11593
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 11589-11593
    • Cohen, H.1    Nogues, C.2    Naaman, R.3    Porath, D.4
  • 74
    • 3042837719 scopus 로고    scopus 로고
    • Direct conduction measurement of single DNA molecules in aqueous solution
    • Xu B., Zhang P., Lik X., and Tao N. Direct conduction measurement of single DNA molecules in aqueous solution. Nano Lett 4 (2004) 1105-1108
    • (2004) Nano Lett , vol.4 , pp. 1105-1108
    • Xu, B.1    Zhang, P.2    Lik, X.3    Tao, N.4
  • 75
    • 0036472252 scopus 로고    scopus 로고
    • Imaging the surface potential of active purple membrane
    • Knapp H.F., Mesquida P., and Stemmer A. Imaging the surface potential of active purple membrane. Surf Int Anal 33 (2002) 108-112
    • (2002) Surf Int Anal , vol.33 , pp. 108-112
    • Knapp, H.F.1    Mesquida, P.2    Stemmer, A.3
  • 76
    • 0344082893 scopus 로고    scopus 로고
    • Fluid electric force microscopy for charge density mapping in biological systems
    • Johnson A.S., Nehl C.L., Mason M.G., and Hafner J.H. Fluid electric force microscopy for charge density mapping in biological systems. Langmuir 19 (2003) 10007-10010
    • (2003) Langmuir , vol.19 , pp. 10007-10010
    • Johnson, A.S.1    Nehl, C.L.2    Mason, M.G.3    Hafner, J.H.4
  • 77
    • 3142747583 scopus 로고    scopus 로고
    • Single spin detection by magnetic resonance force microscopy
    • Rugar B., Budakian R., Mamin H.J., and Chui B.W. Single spin detection by magnetic resonance force microscopy. Nature 430 (2004) 329-332
    • (2004) Nature , vol.430 , pp. 329-332
    • Rugar, B.1    Budakian, R.2    Mamin, H.J.3    Chui, B.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.