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Volumn 21, Issue 8, 2011, Pages 461-469

Atomic force microscopy: A nanoscopic window on the cell surface

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Indexed keywords

ANTIBIOTIC AGENT;

EID: 79960924956     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2011.04.008     Document Type: Review
Times cited : (324)

References (70)
  • 1
    • 0034328878 scopus 로고    scopus 로고
    • Grabbing the cat by the tail: manipulating molecules one by one
    • Bustamante C., et al. Grabbing the cat by the tail: manipulating molecules one by one. Nat. Rev. Mol. Cell Biol. 2000, 1:130-136.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 130-136
    • Bustamante, C.1
  • 2
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • Sotomayor M., Schulten K. Single-molecule experiments in vitro and in silico. Science 2007, 316:1144-1148.
    • (2007) Science , vol.316 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 3
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman K.C., Nagy A.K. Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nat. Methods 2008, 5:491-505.
    • (2008) Nat. Methods , vol.5 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.K.2
  • 4
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: probing proteins with AFM-based force spectroscopy
    • Puchner E.M., Gaub H.E. Force and function: probing proteins with AFM-based force spectroscopy. Curr. Opin. Struct. Biol. 2009, 19:605-614.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 605-614
    • Puchner, E.M.1    Gaub, H.E.2
  • 5
    • 65949083762 scopus 로고    scopus 로고
    • Force probing surfaces of living cells to molecular resolution
    • Müller D.J., et al. Force probing surfaces of living cells to molecular resolution. Nat. Chem. Biol. 2009, 5:383-390.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 383-390
    • Müller, D.J.1
  • 6
    • 79551525710 scopus 로고    scopus 로고
    • Five challenges to bringing single-molecule force spectroscopy into living cells
    • Dufrêne Y.F., et al. Five challenges to bringing single-molecule force spectroscopy into living cells. Nat. Methods 2011, 8:123-127.
    • (2011) Nat. Methods , vol.8 , pp. 123-127
    • Dufrêne, Y.F.1
  • 7
    • 0012618901 scopus 로고
    • Atomic force microscope
    • Binnig G., et al. Atomic force microscope. Phys. Rev. Lett. 1986, 56:930-933.
    • (1986) Phys. Rev. Lett. , vol.56 , pp. 930-933
    • Binnig, G.1
  • 8
    • 33845285999 scopus 로고    scopus 로고
    • How the doors to the nanoworld were opened
    • Gerber C., Lang H.P. How the doors to the nanoworld were opened. Nat. Nanotechnol. 2006, 1:3-5.
    • (2006) Nat. Nanotechnol. , vol.1 , pp. 3-5
    • Gerber, C.1    Lang, H.P.2
  • 9
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer P., Dufrêne Y.F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 2006, 3:347-355.
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrêne, Y.F.2
  • 10
    • 46749107184 scopus 로고    scopus 로고
    • Single-cell force spectroscopy
    • Helenius J., et al. Single-cell force spectroscopy. J. Cell Sci. 2008, 121:1785-1791.
    • (2008) J. Cell Sci. , vol.121 , pp. 1785-1791
    • Helenius, J.1
  • 11
    • 50649125304 scopus 로고    scopus 로고
    • Structure and mechanics of membrane proteins
    • Engel A., Gaub H.E. Structure and mechanics of membrane proteins. Annu. Rev. Biochem. 2008, 77:127-148.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 127-148
    • Engel, A.1    Gaub, H.E.2
  • 12
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin E.L., et al. Adhesion forces between individual ligand-receptor pairs. Science 1994, 264:415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1
  • 13
    • 0033772174 scopus 로고    scopus 로고
    • Discrete interactions in cell adhesion measured by single-molecule force spectroscopy
    • Benoit M., et al. Discrete interactions in cell adhesion measured by single-molecule force spectroscopy. Nat. Cell Biol. 2000, 2:313-317.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 313-317
    • Benoit, M.1
  • 14
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans E.A., Calderwood D.A. Forces and bond dynamics in cell adhesion. Science 2007, 316:1148-1153.
    • (2007) Science , vol.316 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.A.2
  • 15
    • 58849161367 scopus 로고    scopus 로고
    • LFA-1 binding destabilizes the JAM-A homophilic interaction during leukocyte transmigration
    • Wojcikiewicz E.P., et al. LFA-1 binding destabilizes the JAM-A homophilic interaction during leukocyte transmigration. Biophys. J. 2009, 96:285-293.
    • (2009) Biophys. J. , vol.96 , pp. 285-293
    • Wojcikiewicz, E.P.1
  • 17
    • 85015087906 scopus 로고    scopus 로고
    • Ten years of tension: single-molecule DNA mechanics
    • Bustamante C., et al. Ten years of tension: single-molecule DNA mechanics. Nature 2003, 421:423-427.
    • (2003) Nature , vol.421 , pp. 423-427
    • Bustamante, C.1
  • 18
    • 0031277393 scopus 로고    scopus 로고
    • Mapping cell wall polysaccharides of living microbial cells using atomic force microscopy
    • Gad M., et al. Mapping cell wall polysaccharides of living microbial cells using atomic force microscopy. Cell Biol. Int. 1997, 21:697-706.
    • (1997) Cell Biol. Int. , vol.21 , pp. 697-706
    • Gad, M.1
  • 19
    • 0034097199 scopus 로고    scopus 로고
    • Affinity imaging of red blood cells using an atomic force microscope
    • Grandbois M., et al. Affinity imaging of red blood cells using an atomic force microscope. J. Histochem. Cytochem. 2000, 48:719-724.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 719-724
    • Grandbois, M.1
  • 20
    • 34447297851 scopus 로고    scopus 로고
    • Nano-scale dynamic recognition imaging on vascular endothelial cells
    • Chtcheglova L.A., et al. Nano-scale dynamic recognition imaging on vascular endothelial cells. Biophys. J. 2007, 93:L11-L13.
    • (2007) Biophys. J. , vol.93
    • Chtcheglova, L.A.1
  • 21
    • 30944464087 scopus 로고    scopus 로고
    • Fluorescence microscopy today
    • Yuste R. Fluorescence microscopy today. Nat. Methods 2005, 2:902-904.
    • (2005) Nat. Methods , vol.2 , pp. 902-904
    • Yuste, R.1
  • 22
    • 58149236663 scopus 로고    scopus 로고
    • Microscopy and its focal switch
    • Hell S.W. Microscopy and its focal switch. Nat. Methods 2009, 6:24-32.
    • (2009) Nat. Methods , vol.6 , pp. 24-32
    • Hell, S.W.1
  • 23
    • 0026917533 scopus 로고
    • From molecules to cells: imaging soft samples with the atomic force microscope
    • Radmacher M., et al. From molecules to cells: imaging soft samples with the atomic force microscope. Science 1992, 257:1900-1905.
    • (1992) Science , vol.257 , pp. 1900-1905
    • Radmacher, M.1
  • 24
    • 0028321782 scopus 로고
    • Imaging of the membrane surface of MDCK cells by atomic force microscopy
    • Le Grimellec C., et al. Imaging of the membrane surface of MDCK cells by atomic force microscopy. Biophys. J. 1994, 67:36-41.
    • (1994) Biophys. J. , vol.67 , pp. 36-41
    • Le Grimellec, C.1
  • 25
    • 62449128088 scopus 로고    scopus 로고
    • Potassium softens vascular endothelium and increases nitric oxide release
    • Oberleithner H., et al. Potassium softens vascular endothelium and increases nitric oxide release. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:2829-2834.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2829-2834
    • Oberleithner, H.1
  • 26
    • 49649113590 scopus 로고    scopus 로고
    • Towards nanomicrobiology using atomic force microscopy
    • Dufrêne Y.F. Towards nanomicrobiology using atomic force microscopy. Nat. Rev. Microbiol. 2008, 6:674-680.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 674-680
    • Dufrêne, Y.F.1
  • 27
    • 34547479707 scopus 로고    scopus 로고
    • In vitro high-resolution structural dynamics of single germinating bacterial spores
    • Plomp M., et al. In vitro high-resolution structural dynamics of single germinating bacterial spores. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:9644-9649.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9644-9649
    • Plomp, M.1
  • 28
    • 69949127771 scopus 로고    scopus 로고
    • In vivo imaging of S-layer nanoarrays on Corynebacterium glutamicum
    • Dupres V., et al. In vivo imaging of S-layer nanoarrays on Corynebacterium glutamicum. Langmuir 2009, 25:9653-9655.
    • (2009) Langmuir , vol.25 , pp. 9653-9655
    • Dupres, V.1
  • 29
    • 2442650314 scopus 로고    scopus 로고
    • Atomic force microscopy of cell growth and division in Staphylococcus aureus
    • Touhami A., et al. Atomic force microscopy of cell growth and division in Staphylococcus aureus. J. Bacteriol. 2004, 186:3286-3295.
    • (2004) J. Bacteriol. , vol.186 , pp. 3286-3295
    • Touhami, A.1
  • 30
    • 77951118493 scopus 로고    scopus 로고
    • Improvement of the pore trapping method to immobilize vital coccoid bacteria for high-resolution AFM: a study of Staphylococcus aureus
    • Turner R.D., et al. Improvement of the pore trapping method to immobilize vital coccoid bacteria for high-resolution AFM: a study of Staphylococcus aureus. J. Microsc. 2010, 238:102-110.
    • (2010) J. Microsc. , vol.238 , pp. 102-110
    • Turner, R.D.1
  • 31
    • 84856069728 scopus 로고    scopus 로고
    • Imaging the nanoscale organization of peptidoglycan in living Lactococcus lactis cells
    • Andre G., et al. Imaging the nanoscale organization of peptidoglycan in living Lactococcus lactis cells. Nat. Commun. 2010, 1. 10.1038/ncomms1027.
    • (2010) Nat. Commun. , vol.1
    • Andre, G.1
  • 32
    • 0033987136 scopus 로고    scopus 로고
    • Detection of rokitamycin-induced morphostructural alterations in Helicobacter pylori by atomic force microscopy
    • Braga P.C., Ricci D. Detection of rokitamycin-induced morphostructural alterations in Helicobacter pylori by atomic force microscopy. Chemotherapy 2000, 46:15-22.
    • (2000) Chemotherapy , vol.46 , pp. 15-22
    • Braga, P.C.1    Ricci, D.2
  • 33
    • 33750221475 scopus 로고    scopus 로고
    • Atomic force microscopy study of different effects of natural and semisynthetic β-lactam on the cell envelope of Escherichia coli
    • Yang L., et al. Atomic force microscopy study of different effects of natural and semisynthetic β-lactam on the cell envelope of Escherichia coli. Anal. Chem. 2006, 78:7341-7345.
    • (2006) Anal. Chem. , vol.78 , pp. 7341-7345
    • Yang, L.1
  • 34
    • 33750305347 scopus 로고    scopus 로고
    • Ethambutol-induced alterations in Mycobacterium bovis BCG imaged by atomic force microscopy
    • Verbelen C., et al. Ethambutol-induced alterations in Mycobacterium bovis BCG imaged by atomic force microscopy. FEMS Microbiol. Lett. 2006, 264:192-197.
    • (2006) FEMS Microbiol. Lett. , vol.264 , pp. 192-197
    • Verbelen, C.1
  • 35
    • 43149092678 scopus 로고    scopus 로고
    • Organization of the mycobacterial cell wall: a nanoscale view
    • Alsteens D., et al. Organization of the mycobacterial cell wall: a nanoscale view. Pflugers Arch.: Eur. J. Physiol. 2008, 456:117-125.
    • (2008) Pflugers Arch.: Eur. J. Physiol. , vol.456 , pp. 117-125
    • Alsteens, D.1
  • 36
    • 57349182243 scopus 로고    scopus 로고
    • Direct observation of Staphylococcus aureus cell wall digestion by lysostaphin
    • Francius G., et al. Direct observation of Staphylococcus aureus cell wall digestion by lysostaphin. J. Bacteriol. 2008, 190:7904-7909.
    • (2008) J. Bacteriol. , vol.190 , pp. 7904-7909
    • Francius, G.1
  • 37
    • 77749324964 scopus 로고    scopus 로고
    • High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin
    • Shibata M., et al. High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin. Nat. Nanotechnol. 2010, 5:208-212.
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 208-212
    • Shibata, M.1
  • 38
    • 77950860384 scopus 로고    scopus 로고
    • Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy
    • Fantner G.E., et al. 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
  • 39
    • 0038203342 scopus 로고    scopus 로고
    • Quantification of cell adhesion force with AFM: distribution of vitronectin receptors on a living MC3T3-E1 cell
    • Kim H., et al. Quantification of cell adhesion force with AFM: distribution of vitronectin receptors on a living MC3T3-E1 cell. Ultramicroscopy 2003, 97:359-363.
    • (2003) Ultramicroscopy , vol.97 , pp. 359-363
    • Kim, H.1
  • 40
    • 33745614624 scopus 로고    scopus 로고
    • Quantification of the number of EP3 receptors on a living CHO cell surface by the AFM
    • Kim H., et al. Quantification of the number of EP3 receptors on a living CHO cell surface by the AFM. Ultramicroscopy 2006, 106:652-662.
    • (2006) Ultramicroscopy , vol.106 , pp. 652-662
    • Kim, H.1
  • 41
    • 38949173971 scopus 로고    scopus 로고
    • Elastic membrane heterogeneity of living cells revealed by stiff nanoscale membrane domains
    • Roduit C., et al. Elastic membrane heterogeneity of living cells revealed by stiff nanoscale membrane domains. Biophys. J. 2008, 94:1521-1532.
    • (2008) Biophys. J. , vol.94 , pp. 1521-1532
    • Roduit, C.1
  • 42
    • 77349121168 scopus 로고    scopus 로고
    • Improved localization of cellular membrane receptors using combined fluorescence microscopy and simultaneous topography and recognition imaging
    • Duman M., et al. Improved localization of cellular membrane receptors using combined fluorescence microscopy and simultaneous topography and recognition imaging. Nanotechnology 2010, 21:115504.
    • (2010) Nanotechnology , vol.21 , pp. 115504
    • Duman, M.1
  • 43
    • 79954607124 scopus 로고    scopus 로고
    • Fluorescence and atomic force microscopy imaging of wall teichoic acids in Lactobacillus plantarum
    • Andre G., et al. Fluorescence and atomic force microscopy imaging of wall teichoic acids in Lactobacillus plantarum. ACS Chem. Biol. 2011, 6:366-376.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 366-376
    • Andre, G.1
  • 44
    • 77956216058 scopus 로고    scopus 로고
    • Single-molecule atomic force microscopy reveals clustering of the yeast plasma-membrane sensor Wsc1
    • Heinisch J.J., et al. Single-molecule atomic force microscopy reveals clustering of the yeast plasma-membrane sensor Wsc1. PLoS ONE 2010, 5:e11104.
    • (2010) PLoS ONE , vol.5
    • Heinisch, J.J.1
  • 45
    • 78650547219 scopus 로고    scopus 로고
    • Force-induced formation and propagation of adhesion nanodomains in living fungal cells
    • Alsteens D., et al. Force-induced formation and propagation of adhesion nanodomains in living fungal cells. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:20744-20749.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 20744-20749
    • Alsteens, D.1
  • 46
    • 0034969594 scopus 로고    scopus 로고
    • Direct, high-resolution measurement of furrow stiffening during division of adherent cells
    • Matzke R., et al. Direct, high-resolution measurement of furrow stiffening during division of adherent cells. Nat. Cell Biol. 2001, 3:607-610.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 607-610
    • Matzke, R.1
  • 47
    • 0034127331 scopus 로고    scopus 로고
    • Drug-induced changes of cytoskeletal structure and mechanics in fibroblasts: An atomic force microscopy study
    • Rotsch C., Radmacher M. Drug-induced changes of cytoskeletal structure and mechanics in fibroblasts: An atomic force microscopy study. Biophys. J. 2000, 78:520-535.
    • (2000) Biophys. J. , vol.78 , pp. 520-535
    • Rotsch, C.1    Radmacher, M.2
  • 48
    • 33846314328 scopus 로고    scopus 로고
    • Reversible stress softening of actin networks
    • Chaudhuri O., et al. Reversible stress softening of actin networks. Nature 2007, 445:295-298.
    • (2007) Nature , vol.445 , pp. 295-298
    • Chaudhuri, O.1
  • 49
    • 36048995394 scopus 로고    scopus 로고
    • Plasma sodium stiffens vascular endothelium and reduces nitric oxide release
    • Oberleithner H., et al. Plasma sodium stiffens vascular endothelium and reduces nitric oxide release. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:16281-16286.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 16281-16286
    • Oberleithner, H.1
  • 50
    • 78649846598 scopus 로고    scopus 로고
    • Real-time monitoring of cell elasticity reveals oscillating myosin activity
    • Schillers H., et al. Real-time monitoring of cell elasticity reveals oscillating myosin activity. Biophys. J. 2010, 99:3639-3646.
    • (2010) Biophys. J. , vol.99 , pp. 3639-3646
    • Schillers, H.1
  • 51
    • 62549099525 scopus 로고    scopus 로고
    • Real-time monitoring of angiotensin II-induced contractile response and cytoskeleton remodeling in individual cells by atomic force microscopy
    • Cuerrier C.M., et al. Real-time monitoring of angiotensin II-induced contractile response and cytoskeleton remodeling in individual cells by atomic force microscopy. Pflugers Arch. 2009, 457:1361-1372.
    • (2009) Pflugers Arch. , vol.457 , pp. 1361-1372
    • Cuerrier, C.M.1
  • 52
    • 68949130196 scopus 로고    scopus 로고
    • Effect of thrombin and bradykinin on endothelial cell mechanical properties monitored through membrane deformation
    • Cuerrier C.M., et al. Effect of thrombin and bradykinin on endothelial cell mechanical properties monitored through membrane deformation. J. Mol. Recognit. 2009, 22:389-396.
    • (2009) J. Mol. Recognit. , vol.22 , pp. 389-396
    • Cuerrier, C.M.1
  • 53
    • 67651160666 scopus 로고    scopus 로고
    • Cell nanomechanics and focal adhesions are regulated by retinol and conjugated linoleic acid in a dose-dependent manner
    • Silberberg Y.R., et al. Cell nanomechanics and focal adhesions are regulated by retinol and conjugated linoleic acid in a dose-dependent manner. Nanotechnology 2009, 20:285103.
    • (2009) Nanotechnology , vol.20 , pp. 285103
    • Silberberg, Y.R.1
  • 54
    • 36849037967 scopus 로고    scopus 로고
    • Nanomechanical analysis of cells from cancer patients
    • Cross S.E., et al. Nanomechanical analysis of cells from cancer patients. Nat. Nanotechnol. 2007, 2:780-783.
    • (2007) Nat. Nanotechnol. , vol.2 , pp. 780-783
    • Cross, S.E.1
  • 55
    • 67651085393 scopus 로고    scopus 로고
    • Atomic force microscopy detects differences in the surface brush of normal and cancerous cells
    • Iyer S., et al. Atomic force microscopy detects differences in the surface brush of normal and cancerous cells. Nat Nanotechnol. 2009, 4:389-393.
    • (2009) Nat Nanotechnol. , vol.4 , pp. 389-393
    • Iyer, S.1
  • 56
    • 69949150648 scopus 로고    scopus 로고
    • Biology and physics of cell shape changes in development
    • Paluch E., Heisenberg C.-P. Biology and physics of cell shape changes in development. Curr. Biol. 2009, 19:R790-R799.
    • (2009) Curr. Biol. , vol.19
    • Paluch, E.1    Heisenberg, C.-P.2
  • 57
    • 63449127363 scopus 로고    scopus 로고
    • The actin cytoskeleton in spindle assembly and positioning
    • Kunda P., Baum B. The actin cytoskeleton in spindle assembly and positioning. Trends Cell Biol. 2009, 19:174-179.
    • (2009) Trends Cell Biol. , vol.19 , pp. 174-179
    • Kunda, P.1    Baum, B.2
  • 58
    • 78651388574 scopus 로고    scopus 로고
    • Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding
    • Stewart M.P., et al. Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding. Nature 2011, 469:226-230.
    • (2011) Nature , vol.469 , pp. 226-230
    • Stewart, M.P.1
  • 59
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V., Sheetz M. Local force and geometry sensing regulate cell functions. Nat. Rev. Mol. Cell Biol. 2006, 7:265-275.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 60
    • 69949143112 scopus 로고    scopus 로고
    • Conformational changes and signaling in cell and matrix physics
    • Brown A.E.X., Discher D.E. Conformational changes and signaling in cell and matrix physics. Curr. Biol. 2009, 19:R781-R789.
    • (2009) Curr. Biol. , vol.19
    • Brown, A.E.X.1    Discher, D.E.2
  • 61
    • 70350336876 scopus 로고    scopus 로고
    • The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo
    • Dupres V., et al. The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo. Nat. Chem. Biol. 2009, 5:857-862.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 857-862
    • Dupres, V.1
  • 62
    • 68649107640 scopus 로고    scopus 로고
    • Unfolding individual Als5p adhesion proteins on live cells
    • Alsteens D., et al. Unfolding individual Als5p adhesion proteins on live cells. ACS Nano 2009, 3:1677-1682.
    • (2009) ACS Nano , vol.3 , pp. 1677-1682
    • Alsteens, D.1
  • 63
    • 60749130274 scopus 로고    scopus 로고
    • Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways
    • Vogel V., Sheetz M.P. Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways. Curr. Opin. Cell Biol. 2009, 21:38-46.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 38-46
    • Vogel, V.1    Sheetz, M.P.2
  • 64
    • 34248167593 scopus 로고    scopus 로고
    • Revealing early steps of alpha2beta1 integrin-mediated adhesion to collagen type I by using single-cell force spectroscopy
    • Taubenberger A., et al. Revealing early steps of alpha2beta1 integrin-mediated adhesion to collagen type I by using single-cell force spectroscopy. Mol. Biol. Cell 2007, 18:1634-1644.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1634-1644
    • Taubenberger, A.1
  • 65
    • 79952311503 scopus 로고    scopus 로고
    • Single cell force spectroscopy of T cells recognizing a myelin-derived peptide on antigen presenting cell
    • Hoffmann S., et al. Single cell force spectroscopy of T cells recognizing a myelin-derived peptide on antigen presenting cell. Immunol. Lett. 2011, 136:13-20.
    • (2011) Immunol. Lett. , vol.136 , pp. 13-20
    • Hoffmann, S.1
  • 66
    • 77950645792 scopus 로고    scopus 로고
    • Stimulated single-cell force spectroscopy to quantify cell adhesion receptor crosstalk
    • Friedrichs J., et al. Stimulated single-cell force spectroscopy to quantify cell adhesion receptor crosstalk. Proteomics 2010, 10:1455-1462.
    • (2010) Proteomics , vol.10 , pp. 1455-1462
    • Friedrichs, J.1
  • 67
    • 43149088966 scopus 로고    scopus 로고
    • Tensile forces govern germ layer organization during gastrulation
    • Krieg M., et al. Tensile forces govern germ layer organization during gastrulation. Nat. Cell Biol. 2008, 10:429-436.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 429-436
    • Krieg, M.1
  • 68
    • 78649951770 scopus 로고    scopus 로고
    • Control of directed cell migration in vivo by membrane-to-cortex attachment
    • Diz-Muñoz A., et al. Control of directed cell migration in vivo by membrane-to-cortex attachment. PLoS Biol. 2010, 8:e1000544.
    • (2010) PLoS Biol. , vol.8
    • Diz-Muñoz, A.1
  • 69
    • 78649288192 scopus 로고    scopus 로고
    • Electrostatic cell-surface repulsion initiates lumen formation in developing blood vessels
    • 2003-2009
    • Strilić B., et al. Electrostatic cell-surface repulsion initiates lumen formation in developing blood vessels. Curr. Biol. 2010, 20. 2003-2009.
    • (2010) Curr. Biol. , vol.20
    • Strilić, B.1
  • 70
    • 70449555128 scopus 로고    scopus 로고
    • Immune synapse formation determines interaction forces between T cells and antigen-presenting cells measured by atomic force microscopy
    • Hosseini B.H., et al. Immune synapse formation determines interaction forces between T cells and antigen-presenting cells measured by atomic force microscopy. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:17852-17857.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 17852-17857
    • Hosseini, B.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.