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Volumn 74, Issue 8, 2011, Pages

High-resolution atomic force microscopy and spectroscopy of native membrane proteins

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EID: 79961064868     PISSN: 00344885     EISSN: None     Source Type: Journal    
DOI: 10.1088/0034-4885/74/8/086601     Document Type: Review
Times cited : (120)

References (385)
  • 2
    • 33845285999 scopus 로고    scopus 로고
    • How the doors to the nanoworld were opened
    • Gerber C and Lang H P 2006 How the doors to the nanoworld were opened Nature Nanotechnol. 1 3-5
    • (2006) Nature Nanotechnol. , vol.1 , Issue.1 , pp. 3-5
    • Gerber, C.1    Lang, H.P.2
  • 3
    • 48649106769 scopus 로고    scopus 로고
    • AFM: A nanotool in membrane biology
    • Muller D J 2008 AFM: a nanotool in membrane biology Biochemistry 47 7986-98
    • (2008) Biochemistry , vol.47 , Issue.31 , pp. 7986-7998
    • Muller, D.J.1
  • 6
    • 0026657705 scopus 로고
    • Measuring local surface charge densities in electrolyte solutions with a scanning force microscope
    • Butt H-J 1992 Measuring local surface charge densities in electrolyte solutions with a scanning force microscope Biophys. J. 63 578-82
    • (1992) Biophys. J. , vol.63 , Issue.2 , pp. 578-582
    • Butt, H.-J.1
  • 7
    • 0037923070 scopus 로고    scopus 로고
    • The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
    • Muller D J and Engel A 1997 The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions Biophys. J. 73 1633-44 (Pubitemid 27360752)
    • (1997) Biophysical Journal , vol.73 , Issue.3 , pp. 1633-1644
    • Muller, D.J.1    Engel, A.2
  • 8
    • 0028020713 scopus 로고
    • Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy
    • Schabert F A and Engel A 1994 Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy Biophys. J. 67 2394-3403
    • (1994) Biophys. J. , vol.67 , Issue.6 , pp. 2394-3403
    • Schabert, F.A.1    Engel, A.2
  • 9
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope
    • Muller D J, Fotiadis D, Scheuring S, Müller S A and Engel A 1999 Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope Biophys. J. 76 1101-11 (Pubitemid 29264591)
    • (1999) Biophysical Journal , vol.76 , Issue.2 , pp. 1101-1111
    • Muller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Muller, S.A.4    Engel, A.5
  • 10
    • 0141595787 scopus 로고    scopus 로고
    • Tapping-mode atomic force microscopy produces faithful high-resolution images of protein surfaces
    • Moller C, Allen M, Elings V, Engel A and Muller D J 1999 Tapping-mode atomic force microscopy produces faithful high-resolution images of protein surfaces Biophys. J. 77 1150-8 (Pubitemid 29362486)
    • (1999) Biophysical Journal , vol.77 , Issue.2 , pp. 1150-1158
    • Moller, C.1    Allen, M.2    Elings, V.3    Engel, A.4    Muller, D.J.5
  • 12
    • 0036712485 scopus 로고    scopus 로고
    • Dynamic atomic force microscopy methods
    • PII S0167572902000778
    • García R and Pérez R 2002 Dynamic atomic force microscopy methods Surf. Sci. Rep. 47 197-301 (Pubitemid 35022824)
    • (2002) Surface Science Reports , vol.47 , Issue.6-8 , pp. 197-301
    • Garcia, R.1    Perez, R.2
  • 13
    • 29744465291 scopus 로고    scopus 로고
    • Probing attractive forces at the nanoscale using higher-harmonic dynamic force microscopy
    • Crittenden S, Raman A and Reifenberger R 2005 Probing attractive forces at the nanoscale using higher-harmonic dynamic force microscopy Phys. Rev. B 72 235422
    • (2005) Phys. Rev. , vol.72 , Issue.23 , pp. 235422
    • Crittenden, S.1    Raman, A.2    Reifenberger, R.3
  • 14
    • 23844539629 scopus 로고    scopus 로고
    • Single polymer chains as specific transducers of molecular recognition in scanning probe microscopy
    • DOI 10.1021/ja051642v
    • Gabai R, Segev L and Joselevich E 2005 Single polymer chains as specific transducers of molecular recognition in scanning probe microscopy J. Am. Chem. Soc. 127 11390-8 (Pubitemid 41176900)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.32 , pp. 11390-11398
    • Gabai, R.1    Segev, L.2    Joselevich, E.3
  • 15
    • 34547698856 scopus 로고    scopus 로고
    • An atomic force microscope tip designed to measure time-varying nanomechanical forces
    • DOI 10.1038/nnano.2007.226, PII NNANO2007226
    • Sahin O, Magonov S, Su C, Quate C F and Solgaard O 2007 An atomic force microscope tip designed to measure time-varying nanomechanical forces Nature Nanotechnol. 2 507-14 (Pubitemid 47220072)
    • (2007) Nature Nanotechnology , vol.2 , Issue.8 , pp. 507-514
    • Sahin, O.1    Magonov, S.2    Su, C.3    Quate, C.F.4    Solgaard, O.5
  • 16
    • 34547467104 scopus 로고    scopus 로고
    • Higher harmonic atomic force microscopy: Imaging of biological membranes in liquid
    • Preiner J, Tang J, Pastushenko V and Hinterdorfer P 2007 Higher harmonic atomic force microscopy: imaging of biological membranes in liquid Phys. Rev. Lett. 99 046102
    • (2007) Phys. Rev. Lett. , vol.99 , Issue.4 , pp. 046102
    • Preiner, J.1    Tang, J.2    Pastushenko, V.3    Hinterdorfer, P.4
  • 17
    • 37649030405 scopus 로고    scopus 로고
    • Resonant harmonic response in tapping-mode atomic force microscopy
    • Sahin O, Quate C F, Solgaard O and Atalar A 2004 Resonant harmonic response in tapping-mode atomic force microscopy Phys. Rev. B 69 165416
    • (2004) Phys. Rev. , vol.69 , Issue.16 , pp. 165416
    • Sahin, O.1    Quate, C.F.2    Solgaard, O.3    Atalar, A.4
  • 18
    • 34548455960 scopus 로고    scopus 로고
    • Dynamic force spectroscopy using cantilever higher flexural modes
    • Sugimoto Y, Innami S, Abe M, Custance O and Morita S 2007 Dynamic force spectroscopy using cantilever higher flexural modes Appl. Phys. Lett. 91 093120
    • (2007) Appl. Phys. Lett. , vol.91 , Issue.9 , pp. 093120
    • Sugimoto, Y.1    Innami, S.2    Abe, M.3    Custance, O.4    Morita, S.5
  • 19
    • 33748689566 scopus 로고    scopus 로고
    • Multifrequency, repulsive-mode amplitude-modulated atomic force microscopy
    • Proksch R 2006 Multifrequency, repulsive-mode amplitude-modulated atomic force microscopy Appl. Phys. Lett. 89 113121
    • (2006) Appl. Phys. Lett. , vol.89 , Issue.11 , pp. 113121
    • Proksch, R.1
  • 20
    • 40849113667 scopus 로고    scopus 로고
    • Theory of multifrequency atomic force microscopy
    • Lozano J R and Garcia R 2008 Theory of multifrequency atomic force microscopy Phys. Rev. Lett. 100 076102
    • (2008) Phys. Rev. Lett. , vol.100 , Issue.7 , pp. 076102
    • Lozano, J.R.1    Garcia, R.2
  • 22
    • 34547842520 scopus 로고    scopus 로고
    • Dynamics of tapping mode atomic force microscopy in liquids: Theory and experiments
    • Basak S and Raman A 2007 Dynamics of tapping mode atomic force microscopy in liquids: theory and experiments Appl. Phys. Lett. 91 064107
    • (2007) Appl. Phys. Lett. , vol.91 , Issue.6 , pp. 064107
    • Basak, S.1    Raman, A.2
  • 23
    • 38349174189 scopus 로고    scopus 로고
    • Force microscopy imaging of individual protein molecules with sub-pico newton force sensitivity
    • Patil S, Martinez N F, Lozano J R and Garcia R 2007 Force microscopy imaging of individual protein molecules with sub-pico newton force sensitivity J. Mol. Recognit. 20 516-23
    • (2007) J. Mol. Recognit. , vol.20 , Issue.6 , pp. 516-523
    • Patil, S.1    Martinez, N.F.2    Lozano, J.R.3    Garcia, R.4
  • 24
    • 43149093581 scopus 로고    scopus 로고
    • Recent progress in AFM molecular recognition studies
    • Dufrne Y and Hinterdorfer P 2008 Recent progress in AFM molecular recognition studies Pflüg. Arch. Eur. J. Physiol. 456 237-45
    • (2008) Pflüg. Arch. Eur. J. Physiol. , vol.456 , Issue.1 , pp. 237-245
    • Dufrne, Y.1    Hinterdorfer, P.2
  • 25
    • 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 2010 Improved localization of cellular membrane receptors using combined fluorescence microscopy and simultaneous topography and recognition imaging Nanotechnology 21 115504
    • (2010) Nanotechnology , vol.21 , Issue.11 , pp. 115504
    • Duman, M.1
  • 27
    • 61649121899 scopus 로고    scopus 로고
    • Recognition imaging and highly ordered molecular templating of bacterial S-layer nanoarrays containing affinity-tags
    • Tang J et al 2008 Recognition imaging and highly ordered molecular templating of bacterial S-layer nanoarrays containing affinity-tags Nano Lett. 8 4312-9
    • (2008) Nano Lett. , vol.8 , Issue.12 , pp. 4312-4319
    • Tang, J.1
  • 31
    • 0029637281 scopus 로고
    • Atomic resolution of the silicon (111)-(7 × 7) surface by atomic force microscopy
    • Giessibl F J 1995 Atomic resolution of the silicon (111)-(7 × 7) surface by atomic force microscopy Science 267 68-71
    • (1995) Science , vol.267 , Issue.5194 , pp. 68-71
    • Giessibl, F.J.1
  • 33
    • 34249696578 scopus 로고    scopus 로고
    • The Supramolecular Assemblies of Voltage-dependent Anion Channels in the Native Membrane
    • DOI 10.1016/j.jmb.2007.04.073, PII S002228360700602X
    • Hoogenboom B W, Suda K, Engel A and Fotiadis D 2007 The supramolecular assemblies of voltage-dependent anion channels in the native membrane J. Mol. Biol. 370 246-55 (Pubitemid 46829218)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.2 , pp. 246-255
    • Hoogenboom, B.W.1    Suda, K.2    Engel, A.3    Fotiadis, D.4
  • 36
    • 3042609738 scopus 로고    scopus 로고
    • Fast contact-mode atomic force microscopy on biological specimen by model-based control
    • DOI 10.1016/j.ultramic.2003.11.008, PII S0304399104000373
    • Schitter G, Stark R W and Stemmer A 2004 Fast contact-mode atomic force microscopy on biological specimen by model-based control Ultramicroscopy 100 253-7 (Pubitemid 38834133)
    • (2004) Ultramicroscopy , vol.100 , Issue.3-4 , pp. 253-257
    • Schitter, G.1    Stark, R.W.2    Stemmer, A.3
  • 37
    • 67650293632 scopus 로고    scopus 로고
    • Making a commercial atomic force microscope more accurate and faster using positive position feedback control
    • Mahmood I A and Moheimani S O R 2009 Making a commercial atomic force microscope more accurate and faster using positive position feedback control Rev. Sci. Instrum. 80 063705
    • (2009) Rev. Sci. Instrum. , vol.80 , Issue.6 , pp. 063705
    • Mahmood, I.A.1    Moheimani, S.O.R.2
  • 38
    • 77952999101 scopus 로고    scopus 로고
    • Cantilevered bimorph-based scanner for high speed atomic force microscopy with large scanning range
    • Zhou Y, Shang G, Cai W and Yao J-E 2010 Cantilevered bimorph-based scanner for high speed atomic force microscopy with large scanning range Rev. Sci. Instrum. 81 053708
    • (2010) Rev. Sci. Instrum. , vol.81 , Issue.5 , pp. 053708
    • Zhou, Y.1    Shang, G.2    Cai, W.3    Yao, J.-E.4
  • 39
    • 49149111739 scopus 로고    scopus 로고
    • An integrated approach to piezoactuator positioning in high-speed atomic force microscope imaging
    • Yan Y, Wu Y, Zou Q and Su C 2008 An integrated approach to piezoactuator positioning in high-speed atomic force microscope imaging Rev. Sci. Instrum. 79 073704
    • (2008) Rev. Sci. Instrum. , vol.79 , Issue.7 , pp. 073704
    • Yan, Y.1    Wu, Y.2    Zou, Q.3    Su, C.4
  • 42
    • 17044388175 scopus 로고    scopus 로고
    • A mechanical microscope: High-speed atomic force microscopy
    • Humphris A D L, Miles M J and Hobbs J K 2005 A mechanical microscope: high-speed atomic force microscopy Appl. Phys. Lett. 86 034106
    • (2005) Appl. Phys. Lett. , vol.86 , Issue.3 , pp. 034106
    • Humphris, A.D.L.1    Miles, M.J.2    Hobbs, J.K.3
  • 43
    • 0041339761 scopus 로고    scopus 로고
    • Ultrahigh-speed scanning near-field optical microscopy capable of over 100 frames per second
    • Humphris A D L, Hobbs J K and Miles M J 2003 Ultrahigh-speed scanning near-field optical microscopy capable of over 100 frames per second Appl. Phys. Lett. 83 6-8
    • (2003) Appl. Phys. Lett. , vol.83 , Issue.1 , pp. 6-8
    • Humphris, A.D.L.1    Hobbs, J.K.2    Miles, M.J.3
  • 46
    • 3042654725 scopus 로고    scopus 로고
    • Rigid design of fast scanning probe microscopes using finite element analysis
    • DOI 10.1016/j.ultramic.2003.11.009, PII S0304399104000385
    • Kindt J H, Fantner G E, Cutroni J A and Hansma P K 2004 Rigid design of fast scanning probe microscopes using finite element analysis Ultramicroscopy 100 259-65 (Pubitemid 38834134)
    • (2004) Ultramicroscopy , vol.100 , Issue.3-4 , pp. 259-265
    • Kindt, J.H.1    Fantner, G.E.2    Cutroni, J.A.3    Hansma, P.K.4
  • 48
    • 33750485825 scopus 로고    scopus 로고
    • High-speed atomic force microscopy
    • DOI 10.1126/science.1133497
    • Hansma P K, Schitter G, Fantner G E and Prater C 2006 Applied physics - high-speed atomic force microscopy Science 314 601-2 (Pubitemid 44646370)
    • (2006) Science , vol.314 , Issue.5799 , pp. 601-602
    • Hansma, P.K.1    Schitter, G.2    Fantner, G.E.3    Prater, C.4
  • 50
    • 54149113310 scopus 로고    scopus 로고
    • High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes
    • Ando T, Uchihashi T and Fukuma T 2008 High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes Prog. Surf. Sci. 83 337-437
    • (2008) Prog. Surf. Sci. , vol.83 , Issue.7-9 , pp. 337-437
    • Ando, T.1    Uchihashi, T.2    Fukuma, T.3
  • 51
    • 51349093802 scopus 로고    scopus 로고
    • Anisotropic diffusion of point defects in a two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy
    • Yamamoto D, Uchihashi T, Kodera N and Ando T 2008 Anisotropic diffusion of point defects in a two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy Nanotechnology 19 384009
    • (2008) Nanotechnology , vol.19 , Issue.38 , pp. 384009
    • Yamamoto, D.1    Uchihashi, T.2    Kodera, N.3    Ando, T.4
  • 52
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin v by high-speed atomic force microscopy
    • Kodera N, Yamamoto D, Ishikawa R and Ando T 2010 Video imaging of walking myosin V by high-speed atomic force microscopy Nature 468 72-6
    • (2010) Nature , vol.468 , Issue.7320 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 54
    • 77749324964 scopus 로고    scopus 로고
    • High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin
    • Shibata M, Yamashita H, Uchihashi T, Kandori H and Ando T 2010 High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin Nature Nanotechnol. 5 208-12
    • (2010) Nature Nanotechnol. , vol.5 , Issue.3 , pp. 208-212
    • Shibata, M.1    Yamashita, H.2    Uchihashi, T.3    Kandori, H.4    Ando, T.5
  • 55
    • 0040298977 scopus 로고    scopus 로고
    • Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
    • DOI 10.1006/jmbi.1998.2441
    • Muller D J, Sass H-J, Muller S A, Büldt G and Engel A 1999 Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane J. Mol. Biol. 285 1903-9 (Pubitemid 29078159)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 1903-1909
    • Muller, D.J.1    Sass, H.-J.2    Muller, S.A.3    Buldt, G.4    Engel, A.5
  • 56
    • 33745596817 scopus 로고    scopus 로고
    • Microfabricated torsion levers optimized for low force and high-frequency operation in fluids
    • DOI 10.1016/j.ultramic.2005.11.014, PII S0304399106000568
    • Beyder A and Sachs F 2006 Microfabricated torsion levers optimized for low force and high-frequency operation in fluids Ultramicroscopy 106 838-46 (Pubitemid 43994329)
    • (2006) Ultramicroscopy , vol.106 , Issue.8-9 , pp. 838-846
    • Beyder, A.1    Sachs, F.2
  • 57
    • 0033772174 scopus 로고    scopus 로고
    • Discrete interactions in cell adhesion measured by single-molecule force spectroscopy
    • Benoit M, Gabriel D, Gerisch G and Gaub H E 2000 Discrete interactions in cell adhesion measured by single-molecule force spectroscopy Nature Cell Biol. 2 313-7
    • (2000) Nature Cell Biol. , vol.2 , Issue.6 , pp. 313-317
    • Benoit, M.1    Gabriel, D.2    Gerisch, G.3    Gaub, H.E.4
  • 58
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy V, Florin E and Gaub H 1994 Intermolecular forces and energies between ligands and receptors Science 266 257-9 (Pubitemid 24343509)
    • (1994) Science , vol.266 , Issue.5183 , pp. 257-259
    • Moy, V.T.1    Florin, E.-L.2    Gaub, H.E.3
  • 59
    • 73149094951 scopus 로고    scopus 로고
    • Atomic force microscopy: A powerful molecular toolkit in nanoproteomics
    • Dufrne Y F 2009 Atomic force microscopy: a powerful molecular toolkit in nanoproteomics Proteomics 9 5400-5
    • (2009) Proteomics , vol.9 , Issue.24 , pp. 5400-5405
    • Dufrne, Y.F.1
  • 61
    • 2142803260 scopus 로고    scopus 로고
    • Mechanosensitive channels: Multiplicity of families and gating paradigms
    • Sukharev S and Corey D P 2004 Mechanosensitive channels: multiplicity of families and gating paradigms Sci. STKE 2004 re4
    • (2004) Sci. STKE , vol.2004 , Issue.219
    • Sukharev, S.1    Corey, D.P.2
  • 62
    • 70349448090 scopus 로고    scopus 로고
    • Mechanotransduction by hair cells: Models, molecules, and mechanisms
    • Gillespie P G and Müller U 2009 Mechanotransduction by hair cells: models, molecules, and mechanisms Cell 139 33-44
    • (2009) Cell , vol.139 , Issue.1 , pp. 33-44
    • Gillespie, P.G.1    Müller, U.2
  • 63
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: Converting force into biochemical signals
    • DOI 10.1146/annurev.biophys.35.040405.102013
    • Vogel V 2006 Mechanotransduction involving multimodular proteins: converting force into biochemical signals Annu. Rev. Biophys. Biomol. Struct. 35 459-88 (Pubitemid 43877387)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 459-488
    • Vogel, V.1
  • 64
    • 33644849450 scopus 로고    scopus 로고
    • Nanospring behaviour of ankyrin repeats
    • DOI 10.1038/nature04437, PII N04437
    • Lee G, Abdi K, Jiang Y, Michaely P, Bennett V and Marszalek P E 2006 Nanospring behaviour of ankyrin repeats Nature 440 246-9 (Pubitemid 43372106)
    • (2006) Nature , vol.440 , Issue.7081 , pp. 246-249
    • Lee, G.1    Abdi, K.2    Jiang, Y.3    Michaely, P.4    Bennett, V.5    Marszalek, P.E.6
  • 66
    • 34447642312 scopus 로고    scopus 로고
    • Detecting molecular interactions that stabilize, activate and guide ligand-binding of the sodium/proton antiporter MjNhaP1 from Methanococcus jannaschii
    • DOI 10.1016/j.jsb.2007.02.010, PII S1047847707000573
    • Kedrov A, Wegmann S, Smits S H J, Goswami P, Baumann H and Muller D J 2007 Detecting molecular interactions that stabilize, activate and guide ligand-binding of the sodium/proton antiporter MjNhaP1 from Methanococcus jannaschii. J. Struct. Biol. 159 290-301 (Pubitemid 47095401)
    • (2007) Journal of Structural Biology , vol.159 , Issue.SPEC. ISS. , pp. 290-301
    • Kedrov, A.1    Wegmann, S.2    Smits, S.H.J.3    Goswami, P.4    Baumann, H.5    Muller, D.J.6
  • 67
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • DOI 10.1016/j.jmb.2004.05.026, PII S0022283604005947
    • Kedrov A, Ziegler C, Janovjak H, Kühlbrandt W and Muller D J 2004 Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy J. Mol. Biol. 340 1143-52 (Pubitemid 38968707)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.5 , pp. 1143-1152
    • Kedrov, A.1    Ziegler, C.2    Janovjak, H.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 68
    • 0034616309 scopus 로고    scopus 로고
    • Unfolding pathways of individual bacteriorhodopsins
    • DOI 10.1126/science.288.5463.143
    • Oesterhelt F, Oesterhelt D, Pfeiffer M, Engel A, Gaub H E and Muller D J 2000 Unfolding pathways of individual bacteriorhodopsins Science 288 143-6 (Pubitemid 30203048)
    • (2000) Science , vol.288 , Issue.5463 , pp. 143-146
    • Oesterhelt, F.1    Oesterhelt, D.2    Pfeiffer, M.3    Engel, A.4    Gaub, H.E.5    Muller, D.J.6
  • 69
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • DOI 10.1016/j.str.2004.12.005
    • Cisneros D A, Oesterhelt D and Muller D J 2005 Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin Structure 13 235-42 (Pubitemid 40247699)
    • (2005) Structure , vol.13 , Issue.2 , pp. 235-242
    • Cisneros, D.A.1    Oesterhelt, D.2    Muller, D.J.3
  • 71
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • Rief M, Gautel M, Oesterhelt F, Fernandez J M and Gaub H E 1997 Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276 1109-12 (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 72
    • 0031042739 scopus 로고    scopus 로고
    • Single molecule force spectroscopy on polysaccharides by atomic force microscopy
    • DOI 10.1126/science.275.5304.1295
    • Rief M, Oesterhelt F, Heymann B and Gaub H E 1997 Single molecule force spectroscopy on polysaccharides by atomic force microscopy Science 275 1295-7 (Pubitemid 27114155)
    • (1997) Science , vol.275 , Issue.5304 , pp. 1295-1297
    • Rief, M.1    Oesterhelt, F.2    Heymann, B.3    Gaub, H.E.4
  • 73
  • 76
    • 0001832838 scopus 로고    scopus 로고
    • Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water
    • Oesterhelt F, Rief M and Gaub H E 1999 Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water New J. Phys. 1 6
    • (1999) New J. Phys. , vol.1 , pp. 6
    • Oesterhelt, F.1    Rief, M.2    Gaub, H.E.3
  • 78
    • 84982060514 scopus 로고
    • Röntgenuntersuchung gelöster Fadenmoleküle
    • Kratky O and Porod G 1949 Röntgenuntersuchung gelöster Fadenmoleküle Rec. Trav. Chim. Pays-Bas. 68 1106-22
    • (1949) Rec. Trav. Chim. Pays-Bas. , vol.68 , Issue.12 , pp. 1106-1122
    • Kratky, O.1    Porod, G.2
  • 80
    • 0026495432 scopus 로고
    • Direct mechanical measurements of the elasticity of single DNA molecules by using magnetic beads
    • Smith S B, Finzi L and Bustamante C 1992 Direct mechanical measurements of the elasticity of single DNA molecules by using magnetic beads Science 258 1122-6
    • (1992) Science , vol.258 , Issue.5085 , pp. 1122-1126
    • Smith, S.B.1    Finzi, L.2    Bustamante, C.3
  • 81
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell G I 1978 Models for the specific adhesion of cells to cells Science 200 618-27
    • (1978) Science , vol.200 , Issue.4342 , pp. 618-627
    • Bell, G.I.1
  • 82
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - Lifetime - And chemistry in single molecular bonds
    • DOI 10.1146/annurev.biophys.30.1.105
    • Evans E 2001 Probing the relation between force-lifetime- and chemistry in single molecular bonds Annu. Rev. Biophys. Biomol. Struct. 30 105-28 (Pubitemid 32566158)
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 105-128
    • Evans, E.1
  • 83
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans E and Ritchie K 1997 Dynamic strength of molecular adhesion bonds Biophys. J. 72 1541-55 (Pubitemid 27133095)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 84
    • 0032227720 scopus 로고    scopus 로고
    • Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy
    • Evans E 1999 Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy Faraday Discuss. 111 1-16
    • (1999) Faraday Discuss. , vol.111 , pp. 1-16
    • Evans, E.1
  • 86
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • DOI 10.1038/nsb0197-10
    • Dill K A and Chan H S 1997 From Levinthal to pathways to funnels Nature Struct. Biol. 4 10-9 (Pubitemid 27020916)
    • (1997) Nature Structural Biology , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 87
    • 0032993447 scopus 로고    scopus 로고
    • Polymer principles and protein folding
    • Dill K 1999 Polymer principles and protein folding Protein Sci. 8 1166-80 (Pubitemid 29264947)
    • (1999) Protein Science , vol.8 , Issue.6 , pp. 1166-1180
    • Dill, K.A.1
  • 89
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • DOI 10.1038/16219
    • Merkel R, Nassoy P, Leung A, Ritchie K and Evans E 1999 Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy Nature 397 50-3 (Pubitemid 29038244)
    • (1999) Nature , vol.397 , Issue.6714 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 90
    • 0026877444 scopus 로고
    • Classical cadherins
    • Kemler R 1992 Classical cadherins Sem. Cell Biol. 3 149-55
    • (1992) Sem. Cell Biol. , vol.3 , Issue.3 , pp. 149-155
    • Kemler, R.1
  • 92
    • 0031215026 scopus 로고    scopus 로고
    • Quantification of cell adhesion using a spinning disc device and application to surface-reactive materials
    • DOI 10.1016/S0142-9612(97)00042-2, PII S0142961297000422
    • Garca A J, Ducheyne P and Boettiger D 1997 Quantification of cell adhesion using a spinning disc device and application to surface-reactive materials Biomaterials 18 1091-8 (Pubitemid 27342984)
    • (1997) Biomaterials , vol.18 , Issue.16 , pp. 1091-1098
    • Garcia, A.J.1    Ducheyne, P.2    Boettiger, D.3
  • 95
    • 57049166474 scopus 로고    scopus 로고
    • A bond for a lifetime: Employing membrane nanotubes from living cells to determine receptor-ligand kinetics
    • Krieg M, Helenius J, Heisenberg C P and Muller D J 2008 A bond for a lifetime: employing membrane nanotubes from living cells to determine receptor-ligand kinetics Angew. Chem. Int. Edn Engl. 47 9775-7
    • (2008) Angew. Chem. Int. Edn Engl. , vol.47 , Issue.50 , pp. 9775-9777
    • Krieg, M.1    Helenius, J.2    Heisenberg, C.P.3    Muller, D.J.4
  • 97
    • 0037022522 scopus 로고    scopus 로고
    • Correction of microrheological measurements of soft samples with atomic force microscopy for the hydrodynamic drag on the cantilever
    • DOI 10.1021/la0110850
    • Alcaraz J, Buscemi L, Puig-De-Morales M, Colchero J, Baró A and Navajas D 2002 Correction of microrheological measurements of soft samples with atomic force microscopy for the hydrodynamic drag on the cantilever Langmuir 18 716-21 (Pubitemid 35384102)
    • (2002) Langmuir , vol.18 , Issue.3 , pp. 716-721
    • Alcaraz, J.1    Buscemi, L.2    Puig-De-Morales, M.3    Colchero, J.4    Baro, A.5    Navajas, D.6
  • 98
    • 13744260911 scopus 로고    scopus 로고
    • Hydrodynamic effects in fast AFM single-molecule force measurements
    • DOI 10.1007/s00249-004-0430-3
    • Janovjak H, Struckmeier J and Muller D J 2005 Hydrodynamic effects in fast AFM single-molecule force measurements Eur. Biophys. J. 34 91-6 (Pubitemid 40238922)
    • (2005) European Biophysics Journal , vol.34 , Issue.1 , pp. 91-96
    • Janovjak, H.1    Struckmeier, J.2    Muller, D.J.3
  • 99
    • 27644473726 scopus 로고    scopus 로고
    • Temperature softening of a protein in single-molecule experiments
    • DOI 10.1016/j.jmb.2005.09.070, PII S0022283605011496
    • Schlierf M and Rief M 2005 Temperature softening of a protein in single-molecule experiments J. Mol. Biol. 354 497-503 (Pubitemid 41579861)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.2 , pp. 497-503
    • Schlierf, M.1    Rief, M.2
  • 100
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-dependent equilibrium fluctuations of single calmodulin molecules
    • Junker J P, Ziegler F and Rief M 2009 Ligand-dependent equilibrium fluctuations of single calmodulin molecules Science 323 633-7
    • (2009) Science , vol.323 , Issue.5914 , pp. 633-637
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 102
    • 65249086684 scopus 로고    scopus 로고
    • Ultrastable atomic force microscopy: Atomic-scale stability and registration in ambient conditions
    • King G M, Carter A R, Churnside A B, Eberle L S and Perkins T T 2009 Ultrastable atomic force microscopy: atomic-scale stability and registration in ambient conditions Nano Lett. 9 1451-6
    • (2009) Nano Lett. , vol.9 , Issue.4 , pp. 1451-1456
    • King, G.M.1    Carter, A.R.2    Churnside, A.B.3    Eberle, L.S.4    Perkins, T.T.5
  • 105
    • 18444364820 scopus 로고    scopus 로고
    • Automated alignment and pattern recognition of single-molecule force spectroscopy data
    • DOI 10.1111/j.1365-2818.2005.01478.x
    • Kuhn M, Janovjak H, Hubain M and Muller D J 2005 Automated alignment and pattern recognition of single-molecule force spectroscopy data J. Microsc. 218 125-32 (Pubitemid 40646644)
    • (2005) Journal of Microscopy , vol.218 , Issue.2 , pp. 125-132
    • Kuhn, M.1    Janovjak, H.2    Hubain, M.3    Muller, D.J.4
  • 106
    • 33846693208 scopus 로고    scopus 로고
    • A novel pattern recognition algorithm to classify membrane protein unfolding pathways with high-throughput single-molecule force spectroscopy
    • Marsico A, Labudde D, Sapra T, Muller D J and Schroeder M 2007 A novel pattern recognition algorithm to classify membrane protein unfolding pathways with high-throughput single-molecule force spectroscopy Bioinformatics 23 e231-6
    • (2007) Bioinformatics , vol.23 , Issue.2
    • Marsico, A.1    Labudde, D.2    Sapra, T.3    Muller, D.J.4    Schroeder, M.5
  • 107
    • 33747872339 scopus 로고    scopus 로고
    • Analysis assistant for single-molecule force spectroscopy data on membrane proteins - MPTV
    • DOI 10.1093/bioinformatics/btl138
    • Mueller F, Muller D J and Labudde D 2006 Analysis assistant for single-molecule force spectroscopy data on membrane proteins - MPTV Bioinformatics 22 1796-9 (Pubitemid 44288349)
    • (2006) Bioinformatics , vol.22 , Issue.14 , pp. 1796-1799
    • Mueller, F.1    Muller, D.J.2    Labudde, D.3
  • 108
    • 79551579055 scopus 로고    scopus 로고
    • Open source platform for the execution and analysis of mechanical refolding experiments
    • Aioanei D, Brucale M and Samori B 2011 Open source platform for the execution and analysis of mechanical refolding experiments Bioinformatics 27 423-5
    • (2011) Bioinformatics , vol.27 , Issue.3 , pp. 423-425
    • Aioanei, D.1    Brucale, M.2    Samori, B.3
  • 111
    • 77954956306 scopus 로고    scopus 로고
    • Lipidomics: Coming to grips with lipid diversity
    • Shevchenko A and Simons K 2010 Lipidomics: coming to grips with lipid diversity Nature Rev. Mol. Cell Biol. 11 593-8
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , Issue.8 , pp. 593-598
    • Shevchenko, A.1    Simons, K.2
  • 112
    • 0017356323 scopus 로고
    • Membrane asymmetry
    • Rothman J E and Lenard J 1977 Membrane asymmetry Science 195 743-53
    • (1977) Science , vol.195 , Issue.4280 , pp. 743-753
    • Rothman, J.E.1    Lenard, J.2
  • 113
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data: III. Complete structure
    • Wiener M C and White S H 1992 Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data: III. Complete structure Biophys. J. 61 434-47
    • (1992) Biophys. J. , vol.61 , Issue.2 , pp. 434-447
    • Wiener, M.C.1    White, S.H.2
  • 114
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • New York: Academic
    • Oesterhelt D and Stoeckenius W 1974 Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Methods in Enzymology ed L P Sidney Fleischer (New York: Academic) pp 667-78
    • (1974) Methods in Enzymology , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 116
    • 0037099393 scopus 로고    scopus 로고
    • Conformational changes in surface structures of isolated connexin 26 gap junctions
    • DOI 10.1093/emboj/cdf365
    • Muller D J, Hand G M, Engel A and Sosinsky G E 2002 Conformational changes in surface structures of isolated connexin 26 gap junctions EMBO J. 21 3598-607 (Pubitemid 34787034)
    • (2002) EMBO Journal , vol.21 , Issue.14 , pp. 3598-3607
    • Muller, D.J.1    Hand, G.M.2    Engels, A.3    Sosinsky, G.E.4
  • 117
  • 119
    • 33846014316 scopus 로고    scopus 로고
    • The supramolecular architecture of junctional microdomains in native lens membranes
    • DOI 10.1038/sj.embor.7400858, PII 7400858
    • Buzhynskyy N, Hite R K, Walz T and Scheuring S 2006 The supramolecular architecture of junctional microdomains in native lens membranes EMBO Rep. 8 51-5 (Pubitemid 46043800)
    • (2007) EMBO Reports , vol.8 , Issue.1 , pp. 51-55
    • Buzhynskyy, N.1    Hite, R.K.2    Walz, T.3    Scheuring, S.4
  • 120
    • 58149290253 scopus 로고    scopus 로고
    • Lipids in the assembly of membrane proteins and organization of protein supercomplexes: Implications for lipid-linked disorders
    • Bogdanov M, Mileykovskaya E and Dowhan W 2008 Lipids in the assembly of membrane proteins and organization of protein supercomplexes: implications for lipid-linked disorders Subcell. Biochem. 49 197-239
    • (2008) Subcell. Biochem. , vol.49 , pp. 197-239
    • Bogdanov, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 121
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • DOI 10.1016/j.bbamem.2004.05.012, PII S0005273604001592, Lipid-Protein Interactions
    • Lee A G 2004 How lipids affect the activities of integral membrane proteins Biochim. Biophys. Acta Biomembr. 1666 62-87 (Pubitemid 39425199)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 62-87
    • Lee, A.G.1
  • 122
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirements of membrane proteins - A putative bottleneck in heterologous expression
    • DOI 10.1016/S0005-2736(02)00708-3
    • Opekarov M and Tanner W 2003 Specific lipid requirements of membrane proteins - a putative bottleneck in heterologous expression Biochim. Biophys. Acta Biomembr. 1610 11-22 (Pubitemid 36173992)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1610 , Issue.1 , pp. 11-22
    • Opekarova, M.1    Tanner, W.2
  • 123
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • DOI 10.1006/jsbi.1997.3875
    • Muller D J, Amrein M and Engel A 1997 Adsorption of biological molecules to a solid support for scanning probe microscopy J. Struct. Biol. 119 172-88 (Pubitemid 27325792)
    • (1997) Journal of Structural Biology , vol.119 , Issue.2 , pp. 172-188
    • Muller, D.J.1    Amrein, M.2    Engel, A.3
  • 125
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • DOI 10.1006/jmbi.1998.2359
    • Muller D J and Engel A 1999 Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy J. Mol. Biol. 285 1347-51 (Pubitemid 29060437)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1347-1351
    • Muller, D.J.1    Engel, A.2
  • 126
    • 0027138210 scopus 로고
    • Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution
    • Karrasch S, Dolder M, Schabert F, Ramsden J and Engel A 1993 Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution Biophys. J. 65 2437-46 (Pubitemid 24005975)
    • (1993) Biophysical Journal , vol.65 , Issue.6 , pp. 2437-2446
    • Karrasch, S.1    Dolder, M.2    Schabert, F.3    Ramsden, J.4    Engel, A.5
  • 129
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: Scientific and practical applications
    • Sackmann E 1996 Supported membranes: scientific and practical applications Science 271 43-8 (Pubitemid 26033275)
    • (1996) Science , vol.271 , Issue.5245 , pp. 43-48
    • Sackmann, E.1
  • 131
    • 21344468842 scopus 로고    scopus 로고
    • Adsorption of fibrinogen on tantalum oxide, titanium oxide and gold studied by the QCM-D technique
    • DOI 10.1016/j.colsurfb.2005.04.007, PII S0927776505001311
    • Hemmersam A G, Foss M, Chevallier J and Besenbacher F 2005 Adsorption of fibrinogen on tantalum oxide, titanium oxide and gold studied by the QCM-D technique Colloids Surf. B 43 208-15 (Pubitemid 40909844)
    • (2005) Colloids and Surfaces B: Biointerfaces , vol.43 , Issue.3-4 , pp. 208-215
    • Hemmersam, A.G.1    Foss, M.2    Chevallier, J.3    Besenbacher, F.4
  • 132
    • 5444270593 scopus 로고    scopus 로고
    • Time-dependent conformational changes in fibrinogen measured by atomic force microscopy
    • Agnihotri A and Siedlecki C A 2004 Time-dependent conformational changes in fibrinogen measured by atomic force microscopy Langmuir 20 8846-52
    • (2004) Langmuir , vol.20 , Issue.20 , pp. 8846-8852
    • Agnihotri, A.1    Siedlecki, C.A.2
  • 135
    • 26444569477 scopus 로고    scopus 로고
    • Probing BSA binding to citrate-coated gold nanoparticles and surfaces
    • DOI 10.1021/la050588t
    • Brewer S H, Glomm W R, Johnson M C, Knag M K and Franzen S 2005 Probing BSA binding to citrate-coated gold nanoparticles and surfaces Langmuir 21 9303-7 (Pubitemid 41433978)
    • (2005) Langmuir , vol.21 , Issue.20 , pp. 9303-9307
    • Brewer, S.H.1    Glomm, W.R.2    Johnson, M.C.3    Knag, M.K.4    Franzen, S.5
  • 137
  • 138
    • 0035979768 scopus 로고    scopus 로고
    • Two-dimensional crystals: A powerful approach to assess structure, function and dynamics of membrane proteins
    • DOI 10.1016/S0014-5793(01)02746-6, PII S0014579301027466
    • Stahlberg H, Fotiadis D, Scheuring S, Rémigy H, Braun T, Mitsuoka K, Fujiyoshi Y and Engel A 2001 Two-dimensional crystals: a powerful approach to assess structure, function and dynamics of membrane proteins FEBS Lett. 504 166-72 (Pubitemid 32787065)
    • (2001) FEBS Letters , vol.504 , Issue.3 , pp. 166-172
    • Stahlberg, H.1    Fotiadis, D.2    Scheuring, S.3    Remigy, H.4    Braun, T.5    Mitsuoka, K.6    Fujiyoshi, Y.7    Engel, A.8
  • 139
    • 33751225988 scopus 로고    scopus 로고
    • High-resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer
    • DOI 10.1529/biophysj.106.087791
    • Milhiet P-E, Gubellini F, Berquand A, Dosset P, Rigaud J-L, Le Grimellec C and Lèvy D 2006 High-resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer Biophys. J. 91 3268-75 (Pubitemid 44788261)
    • (2006) Biophysical Journal , vol.91 , Issue.9 , pp. 3268-3275
    • Milhiet, P.-E.1    Gubellini, F.2    Berquand, A.3    Dosset, P.4    Rigaud, J.-L.5    Le Grimellec, C.6    Levy, D.7
  • 140
    • 0036629043 scopus 로고    scopus 로고
    • Membrane proteins: Functional and structural studies using reconstituted proteoliposomes and 2-D crystals
    • Rigaud J L 2002 Membrane proteins: functional and structural studies using reconstituted proteoliposomes and 2-D crystals Braz. J. Med. Biol. Res. 35 753-66
    • (2002) Braz. J. Med. Biol. Res. , vol.35 , Issue.7 , pp. 753-766
    • Rigaud, J.L.1
  • 141
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • DOI 10.1016/j.bbamem.2004.04.011, PII S0005273604001610, Lipid-Protein Interactions
    • Seddon A M, Curnow P and Booth P J 2004 Membrane proteins, lipids and detergents: not just a soap opera Biochim. Biophys. Acta Biomembr. 1666 105-17 (Pubitemid 39425201)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 142
    • 0030459599 scopus 로고    scopus 로고
    • Architecture and function of membrane proteins in planar supported bilayers: A study with photosynthetic reaction centers
    • DOI 10.1021/bi961432i
    • Salafsky J, Groves J T and Boxer S G 1996 Architecture and function of membrane proteins in planar supported bilayers: a study with photosynthetic reaction centers Biochemistry 35 14773-81 (Pubitemid 26423810)
    • (1996) Biochemistry , vol.35 , Issue.47 , pp. 14773-14781
    • Salafsky, J.1    Groves, J.T.2    Boxer, S.G.3
  • 143
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • DOI 10.1038/nature04164, PII N04164
    • Tanaka M and Sackmann E 2005 Polymer-supported membranes as models of the cell surface Nature 437 656-63 (Pubitemid 41486528)
    • (2005) Nature , vol.437 , Issue.7059 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 144
    • 44849123226 scopus 로고    scopus 로고
    • An entropic perspective of protein stability on surfaces
    • Knotts T A IV, Rathore N and De Pablo J J 2008 An entropic perspective of protein stability on surfaces Biophys. J. 94 4473-83
    • (2008) Biophys. J. , vol.94 , Issue.11 , pp. 4473-4483
    • Knotts, T.A.I.V.1    Rathore, N.2    De Pablo, J.J.3
  • 145
    • 33847737459 scopus 로고    scopus 로고
    • Stability of a protein tethered to a surface
    • Friedel M, Baumketner A and Shea J-E 2007 Stability of a protein tethered to a surface J. Chem. Phys. 126 095101
    • (2007) J. Chem. Phys. , vol.126 , Issue.9 , pp. 095101
    • Friedel, M.1    Baumketner, A.2    Shea, J.-E.3
  • 146
    • 26444593315 scopus 로고    scopus 로고
    • Structure and stability of a model three-helix-bundle protein on tailored surfaces
    • DOI 10.1002/prot.20581
    • Knotts IV T A, Rathore N and De Pablo J J 2005 Structure and stability of a model three-helix-bundle protein on tailored surfaces Proteins: Struct. Funct. Bioinf. 61 385-97 (Pubitemid 41429146)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.2 , pp. 385-397
    • Knotts IV, T.A.1    Rathore, N.2    De Pablo, J.J.3
  • 147
    • 77956975006 scopus 로고    scopus 로고
    • Predicting stability of alpha-helical, orthogonal-bundle proteins on surfaces
    • Wei S and Knotts IV T A 2010 Predicting stability of alpha-helical, orthogonal-bundle proteins on surfaces J. Chem. Phys. 133 115102
    • (2010) J. Chem. Phys. , vol.133 , Issue.11 , pp. 115102
    • Wei, S.1    Knotts, I.V.T.A.2
  • 148
    • 0035608351 scopus 로고    scopus 로고
    • Functional tethered membranes
    • DOI 10.1016/S1367-5931(01)00269-1, PII S1367593101002691
    • Sinner E-K and Knoll W 2001 Functional tethered membranes Curr. Opin. Chem. Biol. 5 705-11 (Pubitemid 33153168)
    • (2001) Current Opinion in Chemical Biology , vol.5 , Issue.6 , pp. 705-711
    • Sinner, E.-K.1    Knoll, W.2
  • 149
    • 27944496013 scopus 로고    scopus 로고
    • Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy
    • DOI 10.1007/s00249-005-0010-1
    • Kufer S K, Dietz H, Albrecht C, Blank K, Kardinal A, Rief M and Gaub H E 2005 Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy Eur. Biophys. J. 35 72-8 (Pubitemid 41667027)
    • (2005) European Biophysics Journal , vol.35 , Issue.1 , pp. 72-78
    • Kufer, S.K.1    Dietz, H.2    Albrecht, C.3    Blank, K.4    Kardinal, A.5    Rief, M.6    Gaub, H.E.7
  • 151
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer P and Dufrene Y F 2006 Detection and localization of single molecular recognition events using atomic force microscopy Nature Methods 3 347-55
    • (2006) Nature Methods , vol.3 , Issue.5 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 152
    • 77952176659 scopus 로고    scopus 로고
    • Thiol-based, site-specific and covalent immobilization of biomolecules for single-molecule experiments
    • Zimmermann J L, Nicolaus T, Neuert G and Blank K 2010 Thiol-based, site-specific and covalent immobilization of biomolecules for single-molecule experiments Nature Protoc. 5 975-85
    • (2010) Nature Protoc. , vol.5 , Issue.6 , pp. 975-985
    • Zimmermann, J.L.1    Nicolaus, T.2    Neuert, G.3    Blank, K.4
  • 154
    • 4644305444 scopus 로고    scopus 로고
    • Controlled immobilization of membrane proteins to surfaces for fourier transform infrared investigations
    • Rigler P, Ulrich W-P and Vogel H 2004 Controlled immobilization of membrane proteins to surfaces for fourier transform infrared investigations Langmuir 20 7901-3
    • (2004) Langmuir , vol.20 , Issue.19 , pp. 7901-7903
    • Rigler, P.1    Ulrich, W.-P.2    Vogel, H.3
  • 155
    • 24744472221 scopus 로고    scopus 로고
    • High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: A generic platform for protein chip technologies
    • DOI 10.1002/chem.200500154
    • Tinazli A, Tang J, Valiokas R, Picuric S, Lata S, Piehler J, Liedberg B and Tampé R 2005 High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: a generic platform for protein chip technologies Chem. - Eur. J. 11 5249-59 (Pubitemid 41288235)
    • (2005) Chemistry - A European Journal , vol.11 , Issue.18 , pp. 5249-5259
    • Tinazli, A.1    Tang, J.2    Valiokas, R.3    Picuric, S.4    Lata, S.5    Piehler, J.6    Liedberg, B.7    Tampe, R.8
  • 156
    • 0033635139 scopus 로고    scopus 로고
    • Design of supported membranes tethered via metal-affinity ligand-receptor pairs
    • Rädler U, Mack J, Persike N, Jung G and Tampé R 2000 Design of supported membranes tethered via metal-affinity ligand-receptor pairs Biophys. J. 79 3144-52
    • (2000) Biophys. J. , vol.79 , Issue.6 , pp. 3144-3152
    • Rädler, U.1    MacK, J.2    Persike, N.3    Jung, G.4    Tampé, R.5
  • 157
    • 10344264935 scopus 로고    scopus 로고
    • The protein-tethered lipid bilayer: A novel mimic of the biological membrane
    • DOI 10.1529/biophysj.104.046169
    • Giess F, Friedrich M G, Heberle J, Naumann R L and Knoll W 2004 The protein-tethered lipid bilayer: a novel mimic of the biological membrane Biophys. J. 87 3213-20 (Pubitemid 40468578)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 3213-3220
    • Giess, F.1    Friedrich, M.G.2    Heberle, J.3    Naumann, R.L.4    Knoll, W.5
  • 159
    • 0027625621 scopus 로고
    • Ultralarge atomically flat template-stripped Au surfaces for scanning probe microscopy
    • Hegner M, Wagner P and Semenza G 1993 Ultralarge atomically flat template-stripped Au surfaces for scanning probe microscopy Surf. Sci. 291 39-46
    • (1993) Surf. Sci. , vol.291 , Issue.1-2 , pp. 39-46
    • Hegner, M.1    Wagner, P.2    Semenza, G.3
  • 160
    • 0036075731 scopus 로고    scopus 로고
    • Stable self-assembly of a protein engineering scaffold on gold surfaces
    • DOI 10.1110/ps.0206102
    • Terrettaz S, Ulrich W-P, Vogel H, Hong Q, Dover L G and Lakey J H 2002 Stable self-assembly of a protein engineering scaffold on gold surfaces Protein Sci. 11 1917-25 (Pubitemid 34791411)
    • (2002) Protein Science , vol.11 , Issue.8 , pp. 1917-1925
    • Terrettaz, S.1    Ulrich, W.-P.2    Vogel, H.3    Hong, Q.4    Dover, L.G.5    Lakey, J.H.6
  • 162
    • 10444286675 scopus 로고    scopus 로고
    • +-ATP-ase into the thiolipid biomimetic assemblies via the fusion of proteoliposomes
    • +-ATP-ase into the thiolipid biomimetic assemblies via the fusion of proteoliposomes Langmuir 20 11127-33
    • (2004) Langmuir , vol.20 , Issue.25 , pp. 11127-11133
    • Zebrowska, A.1    Krysinski, P.2
  • 163
    • 29444456640 scopus 로고    scopus 로고
    • Tethered bilayer lipid membranes based on monolayers of thiolipids mixed with a complementary dilution molecule. 1. Incorporation of channel peptides
    • DOI 10.1021/la051771p
    • He L, Robertson J W, Li J, Karcher I, Schiller S M, Knoll W and Naumann R 2005 Tethered bilayer lipid membranes based on monolayers of thiolipids mixed with a complementary dilution molecule: I. Incorporation of channel peptides Langmuir 21 11666-72 (Pubitemid 43011505)
    • (2005) Langmuir , vol.21 , Issue.25 , pp. 11666-11672
    • He, L.1    Robertson, J.W.F.2    Li, J.3    Karcher, I.4    Schiller, S.M.5    Knoll, W.6    Naumann, R.7
  • 164
    • 2442551468 scopus 로고    scopus 로고
    • Supported membranes with well-defined polymer tethers - Incorporation of cell receptors
    • Purrucker O, Förtig A, Jordan R and Tanaka M 2004 Supported membranes with well-defined polymer tethers - incorporation of cell receptors ChemPhysChem 5 327-35
    • (2004) ChemPhysChem , vol.5 , Issue.3 , pp. 327-335
    • Purrucker, O.1    Förtig, A.2    Jordan, R.3    Tanaka, M.4
  • 165
    • 0033860735 scopus 로고    scopus 로고
    • Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: Silane-polyethyleneglycol-lipid as a cushion and covalent linker
    • Wagner M L and Tamm L K 2000 Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: silane- polyethyleneglycol-lipid as a cushion and covalent linker Biophys. J. 79 1400-14
    • (2000) Biophys. J. , vol.79 , Issue.3 , pp. 1400-1414
    • Wagner, M.L.1    Tamm, L.K.2
  • 166
    • 0028272653 scopus 로고
    • A new class of thiolipids for the attachment of lipid bilayers on gold surfaces
    • Lang H, Duschl C and Vogel H 1994 A new class of thiolipids for the attachment of lipid bilayers on gold surfaces Langmuir 10 197-210
    • (1994) Langmuir , vol.10 , Issue.1 , pp. 197-210
    • Lang, H.1    Duschl, C.2    Vogel, H.3
  • 167
    • 0037434143 scopus 로고    scopus 로고
    • Archaea analogue thiolipids for tethered bilayer lipid membranes on ultrasmooth gold surfaces
    • DOI 10.1002/anie.200390080
    • Schiller S M, Naumann R, Lovejoy K, Kunz H and Knoll W 2003 Archaea analogue thiolipids for tethered bilayer lipid membranes on ultrasmooth gold surfaces Angew. Chem. Int. Edn Engl. 42 208-11 (Pubitemid 36125579)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.2 , pp. 208-211
    • Schiller, S.M.1    Naumann, R.2    Lovejoy, K.3    Kunz, H.4    Knoll, W.5
  • 169
    • 70350755708 scopus 로고    scopus 로고
    • Modulation of substrate-membrane interactions by linear poly(2-methyl-2-oxazoline) spacers revealed by x-ray reflectivity and ellipsometry
    • Seitz P C, Reif M D, Konovalov O V, Jordan R and Tanaka M 2009 Modulation of substrate-membrane interactions by linear poly(2-methyl-2-oxazoline) spacers revealed by x-ray reflectivity and ellipsometry ChemPhysChem 10 2876-83
    • (2009) ChemPhysChem , vol.10 , Issue.16 , pp. 2876-2883
    • Seitz, P.C.1    Reif, M.D.2    Konovalov, O.V.3    Jordan, R.4    Tanaka, M.5
  • 170
    • 4644266072 scopus 로고    scopus 로고
    • Incorporation of integrins into artificial planar lipid membranes: Characterization by plasmon-enhanced fluorescence spectroscopy
    • DOI 10.1016/j.ab.2004.05.022, PII S0003269704004294
    • Sinner E-K, Reuning U, Kök F N, Sacc B, Moroder L, Knoll W and Oesterhelt D 2004 Incorporation of integrins into artificial planar lipid membranes: characterization by plasmon-enhanced fluorescence spectroscopy Anal. Biochem. 333 216-24 (Pubitemid 39278042)
    • (2004) Analytical Biochemistry , vol.333 , Issue.2 , pp. 216-224
    • Sinner, E.-K.1    Reuning, U.2    Kok, F.N.3    Sacca, B.4    Moroder, L.5    Knoll, W.6    Oesterhelt, D.7
  • 172
    • 0037066260 scopus 로고    scopus 로고
    • Cell adhesion as wetting transition?
    • Sackmann E and Bruinsma R F 2002 Cell adhesion as wetting transition? ChemPhysChem 3 262-9
    • (2002) ChemPhysChem , vol.3 , Issue.3 , pp. 262-269
    • Sackmann, E.1    Bruinsma, R.F.2
  • 173
    • 0037635409 scopus 로고    scopus 로고
    • Functional incorporation of integrins into solid supported membranes on ultrathin films of cellulose: Impact on adhesion
    • Goennenwein S, Tanaka M, Hu B, Moroder L and Sackmann E 2003 Functional incorporation of integrins into solid supported membranes on ultrathin films of cellulose: impact on adhesion Biophys. J. 85 646-55 (Pubitemid 36753666)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 646-655
    • Goennenwein, S.1    Tanaka, M.2    Hu, B.3    Moroder, L.4    Sackmann, E.5
  • 174
  • 175
    • 27144546706 scopus 로고    scopus 로고
    • Lipid bilayers on polyacrylamide brushes for inclusion of membrane proteins
    • DOI 10.1021/la051116h
    • Smith E A, Coym J W, Cowell S M, Tokimoto T, Hruby V J, Yamamura H I and Wirth M J 2005 Lipid bilayers on polyacrylamide brushes for inclusion of membrane proteins Langmuir 21 9644-50 (Pubitemid 41507019)
    • (2005) Langmuir , vol.21 , Issue.21 , pp. 9644-9650
    • Smith, E.A.1    Coym, J.W.2    Cowell, S.M.3    Tokimoto, T.4    Hruby, V.J.5    Yamamura, H.I.6    Wirth, M.J.7
  • 177
    • 48549091092 scopus 로고    scopus 로고
    • Supported lipid bilayers on spacious and pH-responsive polymer cushions with varied hydrophilicity
    • Renner L, Osaki T, Chiantia S, Schwille P, Pompe T and Werner C 2008 Supported lipid bilayers on spacious and pH-responsive polymer cushions with varied hydrophilicity J. Phys. Chem. B 112 6373-8
    • (2008) J. Phys. Chem. , vol.112 , Issue.20 , pp. 6373-6378
    • Renner, L.1    Osaki, T.2    Chiantia, S.3    Schwille, P.4    Pompe, T.5    Werner, C.6
  • 179
    • 0033330452 scopus 로고    scopus 로고
    • High electric resistance polymer/lipid composite films on indium-tin-oxide electrodes
    • DOI 10.1021/la990341u
    • Hillebrandt H, Wiegand G, Tanaka M and Sackmann E 1999 High electric resistance polymer/lipid composite films on indium-tin-oxide electrodes Langmuir 15 8451-9 (Pubitemid 30514749)
    • (1999) Langmuir , vol.15 , Issue.24 , pp. 8451-8459
    • Hillebrandt, H.1    Wiegand, G.2    Tanaka, M.3    Sackmann, E.4
  • 180
    • 0029664490 scopus 로고    scopus 로고
    • 2 and glass surfaces with ultrathin dextran films and deposition of lipid bilayers
    • DOI 10.1016/0956-5663(96)83292-1
    • 2 and glass surfaces with ultrathin dextran films and deposition of lipid bilayers Biosensors Bioelectron. 11 565-77 (Pubitemid 26155144)
    • (1996) Biosensors and Bioelectronics , vol.11 , Issue.6-7 , pp. 565-577
    • Elender, G.1    Kuhner, M.2    Sackmann, E.3
  • 181
    • 0242355021 scopus 로고    scopus 로고
    • Pore-suspending lipid bilayers on porous alumina investigated by electrical impedance spectroscopy
    • Drexler J and Steinem C 2003 Pore-suspending lipid bilayers on porous alumina investigated by electrical impedance spectroscopy J. Phys. Chem. B 107 11245-54
    • (2003) J. Phys. Chem. , vol.107 , Issue.40 , pp. 11245-11254
    • Drexler, J.1    Steinem, C.2
  • 182
    • 20444407699 scopus 로고    scopus 로고
    • Glutamate receptor incorporated in a mixed hybrid bilayer lipid membrane array, as a sensing element of a biosensor working under flowing conditions
    • DOI 10.1021/ja042904g
    • Favero G, Campanella L, Cavallo S, D'Annibale A, Perrella M, Mattei E and Ferri T 2005 Glutamate receptor incorporated in a mixed hybrid bilayer lipid membrane array, as a sensing element of a biosensor working under flowing conditions J. Am. Chem. Soc. 127 8103-11 (Pubitemid 40799667)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.22 , pp. 8103-8111
    • Favero, G.1    Campanella, L.2    Cavallo, S.3    D'Annibale, A.4    Perrella, M.5    Mattei, E.6    Ferri, T.7
  • 183
    • 22244463206 scopus 로고    scopus 로고
    • Nanopore unitary permeability measured by electrochemical and optical single transporter recording
    • DOI 10.1529/biophysj.104.058255
    • Hemmler R, Böse G, Wagner R and Peters R 2005 Nanopore unitary permeability measured by electrochemical and optical single transporter recording Biophys. J. 88 4000-7 (Pubitemid 40991112)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 4000-4007
    • Hemmler, R.1    Bose, G.2    Wagner, R.3    Peters, R.4
  • 184
    • 0037131473 scopus 로고    scopus 로고
    • Membrane-suspended nanocompartments based on ordered pores in alumina
    • Hennesthal C, Drexler J and Steinem C 2002 Membrane-suspended nanocompartments based on ordered pores in alumina ChemPhysChem 3 885-9
    • (2002) ChemPhysChem , vol.3 , Issue.10 , pp. 885-889
    • Hennesthal, C.1    Drexler, J.2    Steinem, C.3
  • 185
    • 0034705976 scopus 로고    scopus 로고
    • Pore-spanning lipid bilayers visualized by scanning force microscopy [8]
    • DOI 10.1021/ja000940j
    • Hennesthal C and Steinem C 2000 Pore-spanning lipid bilayers visualized by scanning force microscopy J. Am. Chem. Soc. 122 8085-6 (Pubitemid 30659436)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.33 , pp. 8085-8086
    • Hennesthal, C.1    Steinem, C.2
  • 186
  • 187
    • 33845985288 scopus 로고    scopus 로고
    • Fabrication and functionalization of nanochannels by electron-beam- induced silicon oxide deposition
    • DOI 10.1021/la061321c
    • Danelon C, Santschi C, Brugger J and Vogel H 2006 Fabrication and functionalization of nanochannels by electron-beam-induced silicon oxide deposition Langmuir 22 10711-5 (Pubitemid 46051757)
    • (2006) Langmuir , vol.22 , Issue.25 , pp. 10711-10715
    • Danelon, C.1    Santschi, C.2    Brugger, J.3    Vogel, H.4
  • 189
    • 1142298535 scopus 로고    scopus 로고
    • Impedance Analysis and Single-Channel Recordings on Nano-Black Lipid Membranes Based on Porous Alumina
    • Romer W and Steinem C 2004 Impedance analysis and single-channel recordings on nano-black lipid membranes based on porous alumina Biophys. J. 86 955-65 (Pubitemid 38209540)
    • (2004) Biophysical Journal , vol.86 , Issue.2 , pp. 955-965
    • Romer, W.1    Steinem, C.2
  • 190
    • 33748461428 scopus 로고    scopus 로고
    • Channel activity of OmpF monitored in nano-BLMs
    • DOI 10.1529/biophysj.106.083592
    • Schmitt E K, Vrouenraets M and Steinem C 2006 Channel activity of OmpF monitored in nano-BLMs Biophys. J. 91 2163-71 (Pubitemid 44352399)
    • (2006) Biophysical Journal , vol.91 , Issue.6 , pp. 2163-2171
    • Schmitt, E.K.1    Vrouenraets, M.2    Steinem, C.3
  • 191
    • 67649354952 scopus 로고    scopus 로고
    • Three-beam interference lithography: Upgrading a Lloyd's interferometer for single-exposure hexagonal patterning
    • De Boor J, Geyer N, Gösele U and Schmidt V 2009 Three-beam interference lithography: upgrading a Lloyd's interferometer for single-exposure hexagonal patterning Opt. Lett. 34 1783-5
    • (2009) Opt. Lett. , vol.34 , Issue.12 , pp. 1783-1785
    • De Boor, J.1    Geyer, N.2    Gösele, U.3    Schmidt, V.4
  • 192
    • 67651227175 scopus 로고    scopus 로고
    • Nanomechanical characterization of phospholipid bilayer islands on flat and porous substrates: A force spectroscopy study
    • Nussio M R, Oncins G, Ridelis I, Szili E, Shapter J G, Sanz F and Voelcker N H 2009 Nanomechanical characterization of phospholipid bilayer islands on flat and porous substrates: a force spectroscopy study J. Phys. Chem. B 113 10339-47
    • (2009) J. Phys. Chem. , vol.113 , Issue.30 , pp. 10339-10347
    • Nussio, M.R.1    Oncins, G.2    Ridelis, I.3    Szili, E.4    Shapter, J.G.5    Sanz, F.6    Voelcker, N.H.7
  • 193
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • DOI 10.1146/annurev.biophys.36.040306.132640
    • Kedrov A, Janovjak H, Sapra K T and Muller D J 2007 Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy Annu. Rev. Biophys. Biomol. Struct. 36 233-60 (Pubitemid 46998118)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Muller, D.J.4
  • 195
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E, Döbeli H and Schacher A 1987 New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues J. Chromatogr. A 411 177-84
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Döbeli, H.2    Schacher, A.3
  • 197
    • 20744442150 scopus 로고    scopus 로고
    • Antigen binding forces of single antilysozyme Fv fragments explored by atomic force microscopy
    • DOI 10.1021/la050162e
    • Berquand A, Xia N, Castner D G, Clare B H, Abbott N L, Dupres V, Adriaensen Y and Dufrene Y F 2005 Antigen binding forces of single antilysozyme Fv fragments explored by atomic force microscopy Langmuir 21 5517-23 (Pubitemid 40850639)
    • (2005) Langmuir , vol.21 , Issue.12 , pp. 5517-5523
    • Berquand, A.1    Xia, N.2    Castner, D.G.3    Clare, B.H.4    Abbott, N.L.5    Dupres, V.6    Adriaensen, Y.7    Dufrene, Y.F.8
  • 199
    • 0034598522 scopus 로고    scopus 로고
    • How strong is the coordination bond between a histidine tag and Ni- nitrilotriacetate? An experiment of mechanochemistry on single molecules
    • DOI 10.1002/(SICI)1521-3773(20000103)39:1<215::AID-ANIE215>3.0. CO;2-R
    • Conti M, Falini G and Samor B 2000 How strong is the coordination bond between a histidine tag and Ni - nitrilotriacetate? An experiment of mechanochemistry on single molecules Angew. Chem. Int. Edn Engl. 39 215-8 (Pubitemid 30265721)
    • (2000) Angewandte Chemie - International Edition , vol.39 , Issue.1 , pp. 215-218
    • Conti, M.1    Falini, G.2    Samori, B.3
  • 200
    • 0034093896 scopus 로고    scopus 로고
    • A metal-chelating microscopy tip as a new toolbox for single-molecule experiments by atomic force microscopy
    • Schmitt L, Ludwig M, Gaub H E and Tampe R 2000 A metal-chelating microscopy tip as a new toolbox for single-molecule experiments by atomic force microscopy Biophys. J. 78 3275-85 (Pubitemid 30396955)
    • (2000) Biophysical Journal , vol.78 , Issue.6 , pp. 3275-3285
    • Schmitt, L.1    Ludwig, M.2    Gaub, H.E.3    Tampe, R.4
  • 202
    • 38349101056 scopus 로고    scopus 로고
    • 6 bond is strong enough for AFM single-molecular recognition studies
    • 6 bond is strong enough for AFM single-molecular recognition studies J. Mol. Recognit. 20 490-4
    • (2007) J. Mol. Recognit. , vol.20 , Issue.6 , pp. 490-494
    • Verbelen, C.1    Gruber, H.J.2    Dufrne, Y.F.3
  • 203
    • 70350036095 scopus 로고    scopus 로고
    • One beta hairpin after the other: Exploring mechanical unfolding pathways of the transmembrane beta-barrel protein OmpG
    • Sapra K T, Damaghi M, Koster S, Yildiz O, Kuhlbrandt W and Muller D J 2009 One beta hairpin after the other: exploring mechanical unfolding pathways of the transmembrane beta-barrel protein OmpG Angew. Chem. Int. Edn Engl. 48 8306-8
    • (2009) Angew. Chem. Int. Edn Engl. , vol.48 , Issue.44 , pp. 8306-8308
    • Sapra, K.T.1    Damaghi, M.2    Koster, S.3    Yildiz, O.4    Kuhlbrandt, W.5    Muller, D.J.6
  • 204
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin biotin interactions with atomic-force microscopy
    • Lee G U, Kidwell D A and Colton R J 1994 Sensing discrete streptavidin biotin interactions with atomic-force microscopy Langmuir 10 354-7
    • (1994) Langmuir , vol.10 , Issue.2 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 205
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-adhesion molecules
    • DOI 10.1038/nature01605
    • Marshall B T, Long M, Piper J W, Yago T, Mcever R P and Zhu C 2003 Direct observation of catch bonds involving cell-adhesion molecules Nature 423 190-3 (Pubitemid 36569544)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 190-193
    • Marshall, B.T.1    Long, M.2    Piper, J.W.3    Yago, T.4    McEver, R.P.5    Zhu, C.6
  • 206
    • 30644476474 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the digoxigenin-antibody complex
    • DOI 10.1016/j.febslet.2005.12.052, PII S0014579305015358
    • Neuert G, Albrecht C, Pamir E and Gaub H E 2006 Dynamic force spectroscopy of the digoxigenin-antibody complex FEBS Lett. 580 505-9 (Pubitemid 43089679)
    • (2006) FEBS Letters , vol.580 , Issue.2 , pp. 505-509
    • Neuert, G.1    Albrecht, C.2    Pamir, E.3    Gaub, H.E.4
  • 207
    • 38349157027 scopus 로고    scopus 로고
    • Atomic force microscopy imaging and single molecule recognition force spectroscopy of coat proteins on the surface of Bacillus subtilis spore
    • Tang J, Krajcikova D, Zhu R, Ebner A, Cutting S, Gruber H J, Barak I and Hinterdorfer P 2007 Atomic force microscopy imaging and single molecule recognition force spectroscopy of coat proteins on the surface of Bacillus subtilis spore J. Mol. Recognit. 20 483-9
    • (2007) J. Mol. Recognit. , vol.20 , Issue.6 , pp. 483-489
    • Tang, J.1    Krajcikova, D.2    Zhu, R.3    Ebner, A.4    Cutting, S.5    Gruber, H.J.6    Barak, I.7    Hinterdorfer, P.8
  • 208
    • 0038458807 scopus 로고    scopus 로고
    • Integrins induce expression of monocyte chemoattractant protein-1 via focal adhesion kinase in mesangial cells
    • DOI 10.1046/j.1523-1755.2003.00122.x
    • Watanabe Y, Tamura M, Osajima A, Anai H, Kabashima N, Serino R and Nakashima Y 2003 Integrins induce expression of monocyte chemoattractant protein-1 via focal adhesion kinase in mesangial cells Kidney Int. 64 431-40 (Pubitemid 36871914)
    • (2003) Kidney International , vol.64 , Issue.2 , pp. 431-440
    • Watanabe, Y.1    Tamura, M.2    Osajima, A.3    Anai, H.4    Kabashima, N.5    Serino, R.6    Nakashima, Y.7
  • 209
    • 0014028723 scopus 로고
    • Interaction of concanavalin a, a phytohemagglutinin, with model substrates
    • Goldstein I J and Iyer R N 1966 Interaction of concanavalin a, a phytohemagglutinin, with model substrates Biochim. Biophys. Acta Gen. Subj. 121 197-200
    • (1966) Biochim. Biophys. Acta Gen. Subj. , vol.121 , Issue.1 , pp. 197-200
    • Goldstein, I.J.1    Iyer, R.N.2
  • 210
    • 27144462660 scopus 로고    scopus 로고
    • Measuring cell adhesion forces of primary gastrulating cells from zebrafish using atomic force microscopy
    • DOI 10.1242/jcs.02547
    • Puech P H, Taubenberger A, Ulrich F, Krieg M, Muller D J and Heisenberg C P 2005 Measuring cell adhesion forces of primary gastrulating cells from zebrafish using atomic force microscopy J. Cell Sci. 118 4199-206 (Pubitemid 41488957)
    • (2005) Journal of Cell Science , vol.118 , Issue.18 , pp. 4199-4206
    • Puech, P.-H.1    Taubenberger, A.2    Ulrich, F.3    Krieg, M.4    Muller, D.J.5    Heisenberg, C.-P.6
  • 211
    • 0038159325 scopus 로고    scopus 로고
    • Contributions of molecular binding events and cellular compliance to the modulation of leukocyte adhesion
    • DOI 10.1242/jcs.00465
    • Wojcikiewicz E P, Zhang X, Chen A and Moy V T 2003 Contributions of molecular binding events and cellular compliance to the modulation of leukocyte adhesion J. Cell Sci. 116 2531-9 (Pubitemid 36790134)
    • (2003) Journal of Cell Science , vol.116 , Issue.12 , pp. 2531-2539
    • Wojcikiewicz, E.P.1    Zhang, X.2    Chen, A.3    Moy, V.T.4
  • 212
    • 77954286695 scopus 로고    scopus 로고
    • Quantifying cellular adhesion to extracellular matrix components by single-cell force spectroscopy
    • Friedrichs J, Helenius J and Muller D J 2010 Quantifying cellular adhesion to extracellular matrix components by single-cell force spectroscopy Nature Protoc. 5 1353-61
    • (2010) Nature Protoc. , vol.5 , Issue.7 , pp. 1353-1361
    • Friedrichs, J.1    Helenius, J.2    Muller, D.J.3
  • 213
    • 65249143274 scopus 로고    scopus 로고
    • Nanoimprinted thin films of reactive, azlactone-containing polymers: Combining methods for the topographic patterning of cell substrates with opportunities for facile post-fabrication chemical functionalization
    • Fredin N J, Broderick A H, Buck M E and Lynn D M 2009 Nanoimprinted thin films of reactive, azlactone-containing polymers: combining methods for the topographic patterning of cell substrates with opportunities for facile post-fabrication chemical functionalization Biomacromolecules 10 994-1003
    • (2009) Biomacromolecules , vol.10 , Issue.4 , pp. 994-1003
    • Fredin, N.J.1    Broderick, A.H.2    Buck, M.E.3    Lynn, D.M.4
  • 215
    • 34347215533 scopus 로고    scopus 로고
    • Molecular engineering of cellular environments: Cell adhesion to nano-digital surfaces
    • Spatz J P and Geiger B 2007 Molecular engineering of cellular environments: cell adhesion to nano-digital surfaces Methods Cell Biol. 83 89-111
    • (2007) Methods Cell Biol. , vol.83 , pp. 89-111
    • Spatz, J.P.1    Geiger, B.2
  • 216
    • 77950645792 scopus 로고    scopus 로고
    • Stimulated single-cell force spectroscopy to quantify cell adhesion receptor crosstalk
    • Friedrichs J, Helenius J and Muller D J 2010 Stimulated single-cell force spectroscopy to quantify cell adhesion receptor crosstalk Proteomics 10 1455-62
    • (2010) Proteomics , vol.10 , Issue.7 , pp. 1455-1462
    • Friedrichs, J.1    Helenius, J.2    Muller, D.J.3
  • 217
    • 0037391134 scopus 로고    scopus 로고
    • Membrane protein structural biology: The high throughput challenge
    • DOI 10.1016/S1047-8477(03)00045-5
    • Loll P J 2003 Membrane protein structural biology: the high throughput challenge J. Struct. Biol. 142 144-53 (Pubitemid 36457896)
    • (2003) Journal of Structural Biology , vol.142 , Issue.1 , pp. 144-153
    • Loll, P.J.1
  • 218
    • 76649137521 scopus 로고    scopus 로고
    • Development of key technologies for high-throughput cell-free protein production with the extract from wheat embryos
    • New York: Academic
    • Takai K, Sawasaki T and Endo Y 2008 Development of key technologies for high-throughput cell-free protein production with the extract from wheat embryos Advances in Protein Chemistry and Structural Biology (New York: Academic) chapter 2, pp 53-84
    • (2008) Advances in Protein Chemistry and Structural Biology
    • Takai, K.1    Sawasaki, T.2    Endo, Y.3
  • 222
    • 46249098051 scopus 로고    scopus 로고
    • Receptor-receptor interactions within receptor mosaics. Impact on neuropsychopharmacology
    • Fuxe K et al 2008 Receptor-receptor interactions within receptor mosaics. Impact on neuropsychopharmacology Brain Res. Rev. 58 415-52
    • (2008) Brain Res. Rev. , vol.58 , Issue.2 , pp. 415-452
    • Fuxe, K.1
  • 224
    • 34548677192 scopus 로고    scopus 로고
    • Heterogeneity and complexity of native brain nicotinic receptors
    • DOI 10.1016/j.bcp.2007.05.023, PII S0006295207003346
    • Gotti C, Moretti M, Gaimarri A, Zanardi A, Clementi F and Zoli M 2007 Heterogeneity and complexity of native brain nicotinic receptors Biochem. Pharmacol. 74 1102-11 (Pubitemid 47432651)
    • (2007) Biochemical Pharmacology , vol.74 , Issue.8 , pp. 1102-1111
    • Gotti, C.1    Moretti, M.2    Gaimarri, A.3    Zanardi, A.4    Clementi, F.5    Zoli, M.6
  • 225
    • 72449123327 scopus 로고    scopus 로고
    • Opioid-receptor-heteromer-specific trafficking and pharmacology
    • van Rijn R M, Whistler J L and Waldhoer M 2010 Opioid-receptor-heteromer- specific trafficking and pharmacology Curr. Opin. Pharmacol. 10 73-9
    • (2010) Curr. Opin. Pharmacol. , vol.10 , Issue.1 , pp. 73-79
    • Van Rijn, R.M.1    Whistler, J.L.2    Waldhoer, M.3
  • 226
    • 0031458238 scopus 로고    scopus 로고
    • Ligand conduction and the gated-pore mechanism of transmembrane transport
    • DOI 10.1016/S0304-4157(97)00007-5, PII S0304415797000075
    • West I C 1997 Ligand conduction and the gated-pore mechanism of transmembrane transport Biochim. Biophys. Acta Rev. Biomembr. 1331 213-34 (Pubitemid 28015515)
    • (1997) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1331 , Issue.3 , pp. 213-234
    • West, I.C.1
  • 227
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • Law C J, Maloney P C and Wang D-N 2008 Ins and outs of major facilitator superfamily antiporters Annu. Rev. Microbiol. 62 289-305
    • (2008) Annu. Rev. Microbiol. , vol.62 , Issue.1 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.-N.3
  • 228
    • 34548853133 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporter proteins
    • DOI 10.1016/j.sbi.2007.07.003, PII S0959440X07001029
    • Hollenstein K, Dawson R J P and Locher K P 2007 Structure and mechanism of ABC transporter proteins Curr. Opin. Struct. Biol. 17 412-8 (Pubitemid 47451766)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.4 , pp. 412-418
    • Hollenstein, K.1    Dawson, R.J.2    Locher, K.P.3
  • 231
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: Biophysics fills the gap
    • Harris A L 2001 Emerging issues of connexin channels: biophysics fills the gap Q. Rev. Biophys. 34 325-472 (Pubitemid 34123306)
    • (2001) Quarterly Reviews of Biophysics , vol.34 , Issue.3 , pp. 325-472
    • Harris, A.L.1
  • 232
    • 33747623998 scopus 로고    scopus 로고
    • Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
    • DOI 10.1038/sj.emboj.7601237, PII 7601237
    • Yildiz, Vinothkumar K R, Goswami P and Kühlbrandt W 2006 Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation EMBO J. 25 3702-13 (Pubitemid 44264880)
    • (2006) EMBO Journal , vol.25 , Issue.15 , pp. 3702-3713
    • Yildiz, O.1    Vinothkumar, K.R.2    Goswami, P.3    Kuhlbrandt, W.4
  • 235
    • 0033582948 scopus 로고    scopus 로고
    • Site-directed spin-labeling reveals the orientation of the amino acid side-chains in the E-F loop of bacteriorhodopsin
    • DOI 10.1006/jmbi.1998.2593
    • Pfeiffer M, Rink T, Gerwert K, Oesterhelt D and Steinhoff H J 1999 Site-directed spin-labeling reveals the orientation of the amino acid side-chains in the E-F loop of bacteriorhodopsin J. Mol. Biol. 287 163-71 (Pubitemid 29134804)
    • (1999) Journal of Molecular Biology , vol.287 , Issue.1 , pp. 163-171
    • Pfeiffer, M.1    Rink, T.2    Gerwert, K.3    Oesterhelt, D.4    Steinhoff, H.-J.5
  • 238
  • 240
    • 0033568641 scopus 로고    scopus 로고
    • High resolution AFM topographs of the Escherichia coli water channel aquaporin Z
    • DOI 10.1093/emboj/18.18.4981
    • Scheuring S, Ringler P, Borgnia M, Stahlberg H, Muller D J, Agre P and Engel A 1999 High resolution AFM topographs of the Escherichia coli water channel aquaporin Z EMBO J. 18 4981-7 (Pubitemid 29443800)
    • (1999) EMBO Journal , vol.18 , Issue.18 , pp. 4981-4987
    • Scheuring, S.1    Ringler, P.2    Borgnia, M.3    Stahlberg, H.4    Muller, D.J.5    Agre, P.6    Engel, A.7
  • 241
    • 0026095474 scopus 로고
    • Atomic force microscopy and dissection of gap junctions
    • Hoh J H, Lal R, John S A, Revel J-P and Arnsdorf M F 1991 Atomic force microscopy and dissection of gap junctions Science 253 1405-8 (Pubitemid 21917291)
    • (1991) Science , vol.253 , Issue.5026 , pp. 1405-1408
    • Hoh, J.H.1    Lal, R.2    John, S.A.3    Revel, J.-P.4    Arnsdorf, M.F.5
  • 242
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert F A, Henn C and Engel A 1995 Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy Science 268 92-4
    • (1995) Science , vol.268 , Issue.5207 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 243
    • 0031563799 scopus 로고    scopus 로고
    • Photosystem I of Synechococcus elongatus at 4 A resolution: Comprehensive structure analysis
    • DOI 10.1006/jmbi.1997.1269
    • Schubert W D, Klukas O, Krauss N, Saenger W, Fromme P and Witt H T 1997 Photosystem I of Synechococcus elongatus at 4 resolution: comprehensive structure analysis J. Mol. Biol. 272 741-69 (Pubitemid 27448191)
    • (1997) Journal of Molecular Biology , vol.272 , Issue.5 , pp. 741-769
    • Schubert, W.-D.1    Klukas, O.2    Krauss, N.3    Saenger, W.4    Fromme, P.5    Witt, H.T.6
  • 245
    • 61449279992 scopus 로고    scopus 로고
    • Structural function of MIP/aquaporin 0 in the eye lens; Genetic defects lead to congenital inherited cataracts
    • Berlin: Springer
    • Chepelinsky A B 2009 Structural function of MIP/aquaporin 0 in the eye lens; genetic defects lead to congenital inherited cataracts Aquaporins ed E Beitz (Berlin: Springer) pp 265-97
    • (2009) Aquaporins , vol.190 , pp. 265-297
    • Chepelinsky, A.B.1
  • 246
    • 0032546752 scopus 로고    scopus 로고
    • Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
    • DOI 10.1006/jmbi.1998.1796
    • Hasler L, Walz T, Tittmann P, Gross H, Kistler J and Engel A 1998 Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution J. Mol. Biol. 279 855-64 (Pubitemid 28284700)
    • (1998) Journal of Molecular Biology , vol.279 , Issue.4 , pp. 855-864
    • Hasler, L.1    Walz, T.2    Tittmann, P.3    Gross, H.4    Kistler, J.5    Engel, A.6
  • 247
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • DOI 10.1038/nature02503
    • Gonen T, Sliz P, Kistler J, Cheng Y and Walz T 2004 Aquaporin-0 membrane junctions reveal the structure of a closed water pore Nature 429 193-7 (Pubitemid 38656196)
    • (2004) Nature , vol.429 , Issue.6988 , pp. 193-197
    • Gonen, T.1    Silz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 248
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • DOI 10.1038/nature04321
    • Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison S C and Walz T 2005 Lipid-protein interactions in double-layered two-dimensional AQP0 crystals Nature 438 633-8 (Pubitemid 41740568)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 633-638
    • Gonen, T.1    Cheng, Y.2    Sliz, P.3    Hiroaki, Y.4    Fujiyoshi, Y.5    Harrison, S.C.6    Walz, T.7
  • 249
    • 35548930792 scopus 로고    scopus 로고
    • Gap junction channel structure in the early 21st century: Facts and fantasies
    • DOI 10.1016/j.ceb.2007.09.001, PII S0955067407001238, Cell to Cell Contact and Extracellular Matrix
    • Yeager M and Harris A L 2007 Gap junction channel structure in the early 21st century: facts and fantasies Curr. Opin. Cell Biol. 19 521-8 (Pubitemid 350016852)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 521-528
    • Yeager, M.1    Harris, A.L.2
  • 250
    • 20444397355 scopus 로고    scopus 로고
    • Structural organization of gap junction channels
    • DOI 10.1016/j.bbamem.2005.04.001, PII S0005273605000878
    • Sosinsky G E and Nicholson B J 2005 Structural organization of gap junction channels Biochim. Biophys. Acta Biomembr. 1711 99-125 (Pubitemid 40799287)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1711 , Issue.SPEC. ISS. , pp. 99-125
    • Sosinsky, G.E.1    Nicholson, B.J.2
  • 251
    • 34247863710 scopus 로고    scopus 로고
    • Aminosulfonate modulated pH-induced conformational changes in connexin26 hemichannels
    • DOI 10.1074/jbc.M609317200
    • Yu J, Bippes C A, Hand G M, Muller D J and Sosinsky G E 2007 Aminosulfonate modulated pH-induced conformational changes in connexin26 hemichannels J. Biol. Chem. 282 8895-904 (Pubitemid 47093512)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.12 , pp. 8895-8904
    • Yu, J.1    Bippes, C.A.2    Hand, G.M.3    Muller, D.J.4    Sosinsky, G.E.5
  • 253
    • 56049124076 scopus 로고    scopus 로고
    • Physiological relevance of GPCR oligomerization and its impact on drug discovery
    • Panetta R and Greenwood M T 2008 Physiological relevance of GPCR oligomerization and its impact on drug discovery Drug Discov. Today 13 1059-66
    • (2008) Drug Discov. Today , vol.13 , Issue.23-24 , pp. 1059-1066
    • Panetta, R.1    Greenwood, M.T.2
  • 254
    • 70249099233 scopus 로고    scopus 로고
    • Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease
    • Mo W and Zhang J-T 2009 Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease Expert Opin. Drug Metab. Toxicol. 5 1049-63
    • (2009) Expert Opin. Drug Metab. Toxicol. , vol.5 , Issue.9 , pp. 1049-1063
    • Mo, W.1    Zhang, J.-T.2
  • 257
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers
    • DOI 10.1006/jmbi.1997.1535
    • Czajkowsky D M, Sheng S and Shao Z 1998 Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers J. Mol. Biol. 276 325-30 (Pubitemid 28085322)
    • (1998) Journal of Molecular Biology , vol.276 , Issue.2 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 258
    • 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 1995 Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids J. Mol. Biol. 248 507-12
    • (1995) J. Mol. Biol. , vol.248 , Issue.3 , pp. 507-512
    • Mou, J.1    Yang, J.2    Shao, Z.3
  • 263
    • 27644486110 scopus 로고    scopus 로고
    • 11 ring stoichiometry in the sodium F-ATP synthase
    • DOI 10.1111/j.1742-4658.2005.04940.x
    • Meier T, Yu J, Raschle T, Henzen F, Dimroth P and Muller D J 2005 Structural evidence for a constant c11 ring stoichiometry in the sodium F-ATP synthase FEBS J. 272 5474-83 (Pubitemid 41579409)
    • (2005) FEBS Journal , vol.272 , Issue.21 , pp. 5474-5483
    • Meier, T.1    Yu, J.2    Raschle, T.3    Henzen, F.4    Dimroth, P.5    Muller, D.J.6
  • 266
    • 64649086247 scopus 로고    scopus 로고
    • The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region
    • Matthies D, Preiss L, Klyszejko A L, Muller D J, Cook G M, Vonck J and Meier T 2009 The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region J. Mol. Biol. 388 611-8
    • (2009) J. Mol. Biol. , vol.388 , Issue.3 , pp. 611-618
    • Matthies, D.1    Preiss, L.2    Klyszejko, A.L.3    Muller, D.J.4    Cook, G.M.5    Vonck, J.6    Meier, T.7
  • 267
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy
    • Muller D J, Schabert F A, Büldt G and Engel A 1995 Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy Biophys. J. 68 1681-6
    • (1995) Biophys. J. , vol.68 , Issue.5 , pp. 1681-1686
    • Muller, D.J.1    Schabert, F.A.2    Büldt, G.3    Engel, A.4
  • 268
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • DOI 10.1016/S0959-440X(98)80128-0
    • Oesterhelt D 1998 The structure and mechanism of the family of retinal proteins from halophilic archaea Curr. Opin. Struct. Biol. 8 489-500 (Pubitemid 28409960)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.4 , pp. 489-500
    • Oesterhelt, D.1
  • 270
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi V K and Girvin M E 1999 Structural changes linked to proton translocation by subunit c of the ATP synthase Nature 402 263-8 (Pubitemid 129516255)
    • (1999) Nature , vol.402 , Issue.6759 , pp. 263-268
    • Rastogi, V.K.1    Girbvin, M.E.2
  • 272
    • 0035929328 scopus 로고    scopus 로고
    • The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids
    • DOI 10.1016/S0014-5793(01)02837-X, PII S001457930102837X
    • Meier T, Matthey U, Henzen F, Dimroth P and Muller D J 2001 The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids FEBS Lett. 505 353-6 (Pubitemid 32905476)
    • (2001) FEBS Letters , vol.505 , Issue.3 , pp. 353-356
    • Meier, T.1    Matthey, U.2    Henzen, F.3    Dimroth, P.4    Muller, D.J.5
  • 274
    • 77956185067 scopus 로고    scopus 로고
    • High resolution imaging of surface patterns of single bacterial cells
    • Greif D, Wesner D, Regtmeier J and Anselmetti D 2010 High resolution imaging of surface patterns of single bacterial cells Ultramicroscopy 110 1290-6
    • (2010) Ultramicroscopy , vol.110 , Issue.10 , pp. 1290-1296
    • Greif, D.1    Wesner, D.2    Regtmeier, J.3    Anselmetti, D.4
  • 275
    • 0032816166 scopus 로고    scopus 로고
    • Atomic force microscopy imaging of living cells: Progress, problems and prospects
    • You H X and Yu L 1999 Atomic force microscopy imaging of living cells: progress, problems and prospects Methods Cell Sci. 21 1-17 (Pubitemid 29373957)
    • (1999) Methods in Cell Science , vol.21 , Issue.1 , pp. 1-17
    • You, H.X.1    Yu, L.2
  • 276
    • 77956184435 scopus 로고    scopus 로고
    • Microbial nanoscopy: A closer look at microbial cell surfaces
    • Dupres V, Alsteens D, Andre G and Dufríne Y F 2010 Microbial nanoscopy: a closer look at microbial cell surfaces Trends Microbiol. 18 397-405
    • (2010) Trends Microbiol. , vol.18 , Issue.9 , pp. 397-405
    • Dupres, V.1    Alsteens, D.2    Andre, G.3    Dufríne, Y.F.4
  • 277
    • 0025663353 scopus 로고
    • Imaging the membrane protein bacteriorhodopsin with the atomic force microscope
    • Butt H J, Downing K H and Hansma P K 1990 Imaging the membrane protein bacteriorhodopsin with the atomic force microscope Biophys. J. 58 1473-80
    • (1990) Biophys. J. , vol.58 , Issue.6 , pp. 1473-1480
    • Butt, H.J.1    Downing, K.H.2    Hansma, P.K.3
  • 281
    • 1942468189 scopus 로고    scopus 로고
    • The G protein-coupled receptor rhodopsin in the native membrane
    • DOI 10.1016/S0014-5793(04)00194-2, PII S0014579304001942
    • Fotiadis D, Liang Y, Filipek S, Saperstein D A, Engel A and Palczewski K 2004 The G protein-coupled receptor rhodopsin in the native membrane FEBS Lett. 564 281-8 (Pubitemid 38520934)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 281-288
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 284
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • Scheuring S and Sturgis J N 2005 Chromatic adaptation of photosynthetic membranes Science 309 484-7
    • (2005) Science , vol.309 , Issue.5733 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 285
    • 0347717833 scopus 로고    scopus 로고
    • Structural Analysis of the Reaction Center Light-harvesting Complex I Photosynthetic Core Complex of Rhodospirillum rubrum Using Atomic Force Microscopy
    • DOI 10.1074/jbc.M310382200
    • Fotiadis D, Qian P, Philippsen A, Bullough P A, Engel A and Hunter C N 2004 Structural analysis of the reaction center light-harvesting complex I photosynthetic core complex of Rhodospirillum rubrum using atomic force microscopy J. Biol. Chem. 279 2063-8 (Pubitemid 38084478)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 2063-2068
    • Fotiadis, D.1    Qian, P.2    Philippsen, A.3    Bullough, P.A.4    Engel, A.5    Hunter, C.N.6
  • 286
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S J and Nicolson G L 1972 The fluid mosaic model of the structure of cell membranes Science 175 720-31
    • (1972) Science , vol.175 , Issue.4023 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 287
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • DOI 10.1038/nature04394
    • Engelman D M 2005 Membranes are more mosaic than fluid Nature 438 578-80 (Pubitemid 41740560)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 578-580
    • Engelman, D.M.1
  • 288
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D and Simons K 2010 Lipid rafts as a membrane-organizing principle Science 327 46-50
    • (2010) Science , vol.327 , Issue.5961 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 289
    • 0026082909 scopus 로고
    • Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae
    • Zinser E, Sperka-Gottlieb C D, Fasch E V, Kohlwein S D, Paltauf F and Daum G 1991 Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae J. Bacteriol. 173 2026-34
    • (1991) J. Bacteriol. , vol.173 , pp. 2026-2034
    • Zinser, E.1    Sperka-Gottlieb, C.D.2    Fasch, E.V.3    Kohlwein, S.D.4    Paltauf, F.5    Daum, G.6
  • 290
    • 33847328318 scopus 로고    scopus 로고
    • Modulation of lateral diffusion in the plasma membrane by protein density
    • Frick M, Schmidt K and Nichols B J 2007 Modulation of lateral diffusion in the plasma membrane by protein density Curr. Biol. 17 462-7
    • (2007) Curr. Biol. , vol.17 , Issue.5 , pp. 462-467
    • Frick, M.1    Schmidt, K.2    Nichols, B.J.3
  • 292
    • 33645294105 scopus 로고    scopus 로고
    • Fluorescence correlation studies of lipid domains in model membranes (review)
    • Kahya N and Schwille P 2006 Fluorescence correlation studies of lipid domains in model membranes (review) Mol. Membr. Biol. 23 29-39
    • (2006) Mol. Membr. Biol. , vol.23 , Issue.1 , pp. 29-39
    • Kahya, N.1    Schwille, P.2
  • 293
    • 33746303104 scopus 로고    scopus 로고
    • Methods to measure the lateral diffusion of membrane lipids and proteins
    • DOI 10.1016/j.ymeth.2006.05.008, PII S1046202306000788
    • Chen Y, Lagerholm B C, Yang B and Jacobson K 2006 Methods to measure the lateral diffusion of membrane lipids and proteins Methods 39 147-53 (Pubitemid 44107712)
    • (2006) Methods , vol.39 , Issue.2 , pp. 147-153
    • Chen, Y.1    Lagerholm, B.C.2    Yang, B.3    Jacobson, K.4
  • 294
    • 58149456901 scopus 로고    scopus 로고
    • Synaptic receptor trafficking: The lateral point of view
    • Jaskolski F and Henley J M 2009 Synaptic receptor trafficking: the lateral point of view Neuroscience 158 19-24
    • (2009) Neuroscience , vol.158 , Issue.1 , pp. 19-24
    • Jaskolski, F.1    Henley, J.M.2
  • 296
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single biomolecules
    • Weiss S 1999 Fluorescence spectroscopy of single biomolecules Science 283 1676-83
    • (1999) Science , vol.283 , Issue.5408 , pp. 1676-1683
    • Weiss, S.1
  • 297
    • 41149164202 scopus 로고    scopus 로고
    • Strategies to prepare and characterize native membrane proteins and protein membranes by AFM
    • Muller D J and Engel A 2008 Strategies to prepare and characterize native membrane proteins and protein membranes by AFM Curr. Opin. Colloid Interface Sci. 13 338-50
    • (2008) Curr. Opin. Colloid Interface Sci. , vol.13 , Issue.5 , pp. 338-350
    • Muller, D.J.1    Engel, A.2
  • 298
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A and Muller D J 2000 Observing single biomolecules at work with the atomic force microscope Nature Struct. Biol. 7 715-8
    • (2000) Nature Struct. Biol. , vol.7 , Issue.9 , pp. 715-718
    • Engel, A.1    Muller, D.J.2
  • 299
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy
    • Muller D J, Baumeister W and Engel A 1996 Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy J. Bacteriol. 178 3025-30 (Pubitemid 26000136)
    • (1996) Journal of Bacteriology , vol.178 , Issue.11 , pp. 3025-3030
    • Muller, D.J.1    Baumeister, W.2    Engel, A.3
  • 300
    • 0036828872 scopus 로고    scopus 로고
    • PH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding
    • DOI 10.1074/jbc.M206804200
    • Andersen C, Schiffler B, Charbit A and Benz R 2002 pH-induced collapse of the extracellular loops closes Escherichia coli maltoporin and allows the study of asymmetric sugar binding J. Biol. Chem. 277 41318-25 (Pubitemid 35257431)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41318-41325
    • Andersen, C.1    Schiffler, B.2    Charbit, A.3    Benz, R.4
  • 301
    • 77949316155 scopus 로고    scopus 로고
    • PH-induced conformational change of the β-barrel-forming protein OmpG reconstituted into native E. coli lipids
    • Mari S A, Koster S, Bippes C A, Yildiz O, Kuhlbrandt W and Muller D J 2010 pH-induced conformational change of the β-barrel-forming protein OmpG reconstituted into native E. coli lipids J. Mol. Biol. 396 610-6
    • (2010) J. Mol. Biol. , vol.396 , Issue.3 , pp. 610-616
    • Mari, S.A.1    Koster, S.2    Bippes, C.A.3    Yildiz, O.4    Kuhlbrandt, W.5    Muller, D.J.6
  • 303
    • 0043281578 scopus 로고    scopus 로고
    • The role of connexins in human disease
    • DOI 10.1097/01.AUD.0000079801.55588.13
    • Chang E H, Van Camp G and Smith R J 2003 The role of connexins in human disease Ear Hear. 24 314-23 (Pubitemid 37022143)
    • (2003) Ear and Hearing , vol.24 , Issue.4 , pp. 314-323
    • Chang, E.H.1    Van Camp, G.2    Smith, R.J.H.3
  • 304
    • 0031991524 scopus 로고    scopus 로고
    • Gap junctions in health and disease
    • Dermietzel R and Hofstädter F 1998 Gap junctions in health and disease Virchows Arch. 432 177-86
    • (1998) Virchows Arch. , vol.432 , Issue.2 , pp. 177-186
    • Dermietzel, R.1    Hofstädter, F.2
  • 305
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriorhodopsin
    • Muller D J, Büldt G and Engel A 1995 Force-induced conformational change of bacteriorhodopsin J. Mol. Biol. 249 239-43
    • (1995) J. Mol. Biol. , vol.249 , Issue.2 , pp. 239-243
    • Muller, D.J.1    Büldt, G.2    Engel, A.3
  • 307
    • 21144452622 scopus 로고    scopus 로고
    • Assessment of insulated conductive cantilevers for biology and electrochemistry
    • DOI 10.1088/0957-4484/16/8/001, PII S0957448405952550
    • Frederix P L T M, Gullo M R, Akiyama T, Tonin A, Rooij N F D, Staufer U and Engel A 2005 Assessment of insulated conductive cantilevers for biology and electrochemistry Nanotechnology 16 997-1005 (Pubitemid 40878592)
    • (2005) Nanotechnology , vol.16 , Issue.8 , pp. 997-1005
    • Frederix, P.L.T.M.1    Gullo, M.R.2    Akiyama, T.3    Tonin, A.4    De Rooij, N.F.5    Staufer, U.6    Engel, A.7
  • 308
    • 0141753133 scopus 로고    scopus 로고
    • Unfolding pathways of native bacteriorhodopsin depend on temperature
    • DOI 10.1093/emboj/cdg509
    • Janovjak H, Kessler M, Oesterhelt D, Gaub H and Muller D J 2003 Unfolding pathways of native bacteriorhodopsin depend on temperature EMBO J. 22 5220-9 (Pubitemid 37222041)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 5220-5229
    • Janovjak, H.1    Kessler, M.2    Oesterhelt, D.3    Gaub, H.4    Muller, D.J.5
  • 309
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy
    • Muller D J, Kessler M, Oesterhelt F, Möller C, Oesterhelt D and Gaub H 2002 Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy Biophys. J. 83 3578-88 (Pubitemid 36041975)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3578-3588
    • Muller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Moller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 310
    • 23744506838 scopus 로고    scopus 로고
    • Locating ligand binding and activation of a single antiporter
    • DOI 10.1038/sj.embor.7400455
    • Kedrov A, Krieg M, Ziegler C, Kuhlbrandt W and Muller D J 2005 Locating ligand binding and activation of a single antiporter EMBO Rep. 6 668-74 (Pubitemid 41122436)
    • (2005) EMBO Reports , vol.6 , Issue.7 , pp. 668-674
    • Kedrov, A.1    Krieg, M.2    Ziegler, C.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 311
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • DOI 10.1016/j.jmb.2005.10.080, PII S0022283605013653
    • Sapra K T, Besir H, Oesterhelt D and Muller D J 2006 Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy J. Mol. Biol. 355 640-50 (Pubitemid 41817625)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.4 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Muller, D.J.4
  • 313
    • 28844490188 scopus 로고    scopus 로고
    • Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli
    • DOI 10.1016/j.jmb.2005.10.028, PII S0022283605012593
    • Kedrov A, Janovjak H, Ziegler C, Kuhlbrandt W and Muller D J 2006 Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli J. Mol. Biol. 355 2-8 (Pubitemid 41774134)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.1 , pp. 2-8
    • Kedrov, A.1    Janovjak, H.2    Ziegler, C.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 314
    • 33344474603 scopus 로고    scopus 로고
    • Bacteriorhodopsin folds into the membrane against an external force
    • DOI 10.1016/j.jmb.2005.12.065, PII S0022283605016414
    • Kessler M, Gottschalk K E, Janovjak H, Muller D J and Gaub H E 2006 Bacteriorhodopsin folds into the membrane against an external force J. Mol. Biol. 357 644-54 (Pubitemid 43290762)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.2 , pp. 644-654
    • Kessler, M.1    Gottschalk, K.E.2    Janovjak, H.3    Muller, D.J.4    Gaub, H.E.5
  • 315
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • DOI 10.1038/387308a0
    • Tskhovrebova L, Trinick J, Sleep J A and Simmons R M 1997 Elasticity and unfolding of single molecules of the giant muscle protein titin Nature 387 308-12 (Pubitemid 27220769)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 316
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • DOI 10.1126/science.276.5315.1112
    • Kellermayer M S S Z, Smith S B, Granzier H L and Bustamante C 1997 Folding-unfolding transitions in single titin molecules characterized with laser tweezers Science 276 1112-6 (Pubitemid 27218119)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 317
    • 0034665438 scopus 로고    scopus 로고
    • Force spectroscopy of molecular systems - Single molecule spectroscopy of polymers and biomolecules
    • Janshoff A, Neitzert M, Oberdörfer Y and Fuchs H 2000 Force spectroscopy of molecular systems - single molecule spectroscopy of polymers and biomolecules Angew. Chem. Int. Edn Engl. 39 3212-37
    • (2000) Angew. Chem. Int. Edn Engl. , vol.39 , pp. 3212-3237
    • Janshoff, A.1    Neitzert, M.2    Oberdörfer, Y.3    Fuchs, H.4
  • 318
    • 67650632375 scopus 로고    scopus 로고
    • Substrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter
    • Bippes C A, Zeltina A, Casagrande F, Ratera M, Palacin M, Muller D J and Fotiadis D 2009 Substrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter J. Biol. Chem. 284 18651-63
    • (2009) J. Biol. Chem. , vol.284 , Issue.28 , pp. 18651-18663
    • Bippes, C.A.1    Zeltina, A.2    Casagrande, F.3    Ratera, M.4    Palacin, M.5    Muller, D.J.6    Fotiadis, D.7
  • 320
    • 78650087374 scopus 로고    scopus 로고
    • Conservation of molecular interactions stabilizing bovine and mouse rhodopsin
    • Kawamura S, Colozo A T, Muller D J and Park P S H 2010 Conservation of molecular interactions stabilizing bovine and mouse rhodopsin Biochemistry 49 10412-20
    • (2010) Biochemistry , vol.49 , Issue.49 , pp. 10412-10420
    • Kawamura, S.1    Colozo, A.T.2    Muller, D.J.3    Park, P.S.H.4
  • 321
    • 33748467970 scopus 로고    scopus 로고
    • Differentiating Ligand and Inhibitor Interactions of a Single Antiporter
    • DOI 10.1016/j.jmb.2006.07.049, PII S0022283606008977
    • Kedrov A, Ziegler C and Muller D J 2006 Differentiating ligand and inhibitor interactions of a single antiporter J. Mol. Biol. 362 925-32 (Pubitemid 44353514)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.5 , pp. 925-932
    • Kedrov, A.1    Ziegler, C.2    Muller, D.J.3
  • 322
    • 73449133713 scopus 로고    scopus 로고
    • Probing the interactions of carboxy-atractyloside and atractyloside with the yeast mitochondrial ADP/ATP carrier
    • Kedrov A, Hellawell A M, Klosin A, Broadhurst R B, Kunji E R S and Müller D J 2010 Probing the interactions of carboxy-atractyloside and atractyloside with the yeast mitochondrial ADP/ATP carrier Structure 18 39-46
    • (2010) Structure , vol.18 , Issue.1 , pp. 39-46
    • Kedrov, A.1    Hellawell, A.M.2    Klosin, A.3    Broadhurst, R.B.4    Kunji, E.R.S.5    Müller, D.J.6
  • 323
    • 2342646040 scopus 로고    scopus 로고
    • Probing the energy landscape of the membrane protein bacteriorhodopsin
    • DOI 10.1016/j.str.2004.03.016, PII S096921260400098X
    • Janovjak H, Struckmeier J, Hubain M, Kedrov A, Kessler M and Muller D J 2004 Probing the energy landscape of the membrane protein bacteriorhodopsin Structure 12 871-9 (Pubitemid 38595775)
    • (2004) Structure , vol.12 , Issue.5 , pp. 871-879
    • Janovjak, H.1    Struckmeier, J.2    Hubain, M.3    Kedrov, A.4    Kessler, M.5    Muller, D.J.6
  • 324
    • 39049092605 scopus 로고    scopus 로고
    • Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways
    • Sapra K T, Balasubramanian G P, Labudde D, Bowie J U and Muller D J 2008 Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways J. Mol. Biol. 376 1076-90
    • (2008) J. Mol. Biol. , vol.376 , Issue.4 , pp. 1076-1090
    • Sapra, K.T.1    Balasubramanian, G.P.2    Labudde, D.3    Bowie, J.U.4    Muller, D.J.5
  • 325
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C B 1973 Principles that govern the folding of protein chains Science 181 223-30
    • (1973) Science , vol.181 , Issue.4096 , pp. 223-230
    • Anfinsen, C.B.1
  • 327
    • 47749083052 scopus 로고    scopus 로고
    • From the first protein structures to our current knowledge of protein folding: Delights and scepticisms
    • Fersht A R 2008 From the first protein structures to our current knowledge of protein folding: delights and scepticisms Nature Rev. Mol. Cell Biol. 9 650-4
    • (2008) Nature Rev. Mol. Cell Biol. , vol.9 , Issue.8 , pp. 650-654
    • Fersht, A.R.1
  • 328
    • 39149104002 scopus 로고    scopus 로고
    • Combining experiment and simulation in protein folding: Closing the gap for small model systems
    • Schaeffer R D, Fersht A and Daggett V 2008 Combining experiment and simulation in protein folding: closing the gap for small model systems Curr. Opin. Struct. Biol. 18 4-9
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , Issue.1 , pp. 4-9
    • Schaeffer, R.D.1    Fersht, A.2    Daggett, V.3
  • 330
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of α-helical integral membrane proteins
    • DOI 10.1021/cr0404388
    • MacKenzie K R 2006 Folding and stability of α-helical integral membrane proteins Chem. Rev. 106 1931-77 (Pubitemid 43792787)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1931-1977
    • MacKenzie, K.R.1
  • 332
    • 23044510444 scopus 로고    scopus 로고
    • Transmembrane helices before, during, and after insertion
    • DOI 10.1016/j.sbi.2005.07.004, PII S0959440X05001260, Membranes/Engineering and Desing
    • White S H and von Heijne G 2005 Transmembrane helices before, during, and after insertion Curr. Opin. Struct. Biol. 15 378-86 (Pubitemid 41073827)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.4 , pp. 378-386
    • White, S.H.1    Von Heijne, G.2
  • 335
    • 0034734237 scopus 로고    scopus 로고
    • Unravelling the folding of bacteriorhodopsin
    • Booth P J 2000 Unravelling the folding of bacteriorhodopsin Biochim. Biophys. Acta Bioenerg. 1460 4-14
    • (2000) Biochim. Biophys. Acta Bioenerg. , vol.1460 , Issue.1 , pp. 4-14
    • Booth, P.J.1
  • 336
    • 7044247850 scopus 로고    scopus 로고
    • Folding and assembly of β-barrel membrane proteins
    • DOI 10.1016/j.bbamem.2004.06.011, PII S0005273604001646, Lipid-Protein Interactions
    • Tamm L K, Hong H and Liang B 2004 Folding and assembly of β-barrel membrane proteins Biochim. Biophys. Acta Biomembr. 1666 250-63 (Pubitemid 39425208)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 250-263
    • Tamm, L.K.1    Hong, H.2    Liang, B.3
  • 338
    • 0036401862 scopus 로고    scopus 로고
    • The expanded denatured state: An ensemble of conformations trapped in a locally encoded topological space
    • DOI 10.1016/S0065-3233(02)62003-0
    • Shortle D 2002 The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space Adv. Protein Chem. 62 1-23 (Pubitemid 35204866)
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 1-23
    • Shortle, D.1
  • 339
    • 0037031261 scopus 로고    scopus 로고
    • Effects of topology and excluded volume on protein denatured state conformational properties
    • DOI 10.1021/bi0259249
    • Smith C R, Mateljevic N and Bowler B E 2002 Effects of topology and excluded volume on protein denatured state conformational properties Biochemistry 41 10173-81 (Pubitemid 34839763)
    • (2002) Biochemistry , vol.41 , Issue.31 , pp. 10173-10181
    • Smith, C.R.1    Mateljevic, N.2    Bowler, B.E.3
  • 340
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy model (with applications to protein folding)
    • Bryngelson J D and Wolynes P G 1989 Intermediates and barrier crossing in a random energy model (with applications to protein folding) J. Phys. Chem. 93 6902-15
    • (1989) J. Phys. Chem. , vol.93 , Issue.19 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 342
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar S G and Wolynes P G 1991 The energy landscapes and motions of proteins Science 254 1598-603 (Pubitemid 21917496)
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 344
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • DOI 10.1038/nature06522, PII NATURE06522
    • Henzler-Wildman K and Kern D 2007 Dynamic personalities of proteins Nature 450 964-72 (Pubitemid 350273626)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 345
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • DOI 10.1111/j.1742-4658.2005.05021.x
    • Jahn T R and Radford SE 2005 The yin and yang of protein folding FEBS J. 272 5962-70 (Pubitemid 41713688)
    • (2005) FEBS Journal , vol.272 , Issue.23 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 346
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • DOI 10.1038/nature05959, PII NATURE05959
    • Frederick K K, Marlow M S, Valentine K G and Wand A J 2007 Conformational entropy in molecular recognition by proteins Nature 448 325-9 (Pubitemid 47080342)
    • (2007) Nature , vol.448 , Issue.7151 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 347
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • DOI 10.1126/science.1130258
    • Boehr D D, McElheny D, Dyson H J and Wright P E 2006 The dynamic energy landscape of dihydrofolate reductase catalysis Science 313 1638-42 (Pubitemid 44414038)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wrightt, P.E.4
  • 348
    • 0034696766 scopus 로고    scopus 로고
    • Transition-state ensemble in enzyme catalysis: Possibility, reality, or necessity?
    • DOI 10.1006/jtbi.2000.1097
    • Ma B, Kumar S, Tsai C-J, Hu Z and Nussinov R 2000 Transition-state ensemble in enzyme catalysis: possibility, reality, or necessity? J. Theor. Biol. 203 383-97 (Pubitemid 30662934)
    • (2000) Journal of Theoretical Biology , vol.203 , Issue.4 , pp. 383-397
    • Ma, B.1    Kumar, S.2    Tsai, C.-J.3    Hu, Z.4    Nussinov, R.5
  • 349
    • 40449118071 scopus 로고    scopus 로고
    • Mechanical properties of bovine rhodopsin and bacteriorhodopsin: Possible roles in folding and function
    • DOI 10.1021/la702299z
    • Sapra K T, Park P S H, Palczewski K and Muller D J 2008 Mechanical properties of bovine rhodopsin and bacteriorhodopsin: possible roles in folding and function Langmuir 24 1330-7 (Pubitemid 351345853)
    • (2008) Langmuir , vol.24 , Issue.4 , pp. 1330-1337
    • Sapra, K.T.1    Park, P.S.-H.2    Palczewski, K.3    Muller, D.J.4
  • 350
    • 37549016432 scopus 로고    scopus 로고
    • Examining the dynamic energy landscape of an antiporter upon inhibitor binding
    • Kedrov A, Appel M, Baumann H, Ziegler C and Muller D J 2008 Examining the dynamic energy landscape of an antiporter upon inhibitor binding J. Mol. Biol. 375 1258-66
    • (2008) J. Mol. Biol. , vol.375 , Issue.5 , pp. 1258-1266
    • Kedrov, A.1    Appel, M.2    Baumann, H.3    Ziegler, C.4    Muller, D.J.5
  • 351
    • 9744250110 scopus 로고    scopus 로고
    • Strength of integration of transmembrane α-helical peptides in lipid bilayers as determined by atomic force spectroscopy
    • DOI 10.1021/bi048372y
    • Ganchev D N, Rijkers D T S, Snel M M E, Killian J A and De Kruijff B 2004 Strength of integration of transmembrane α-helical peptides in lipid bilayers as determined by atomic force spectroscopy Biochemistry 43 14987-93 (Pubitemid 39587475)
    • (2004) Biochemistry , vol.43 , Issue.47 , pp. 14987-14993
    • Ganchev, D.N.1    Rijkers, D.T.S.2    Snel, M.M.E.3    Killian, J.A.4    De Kruijff, B.5
  • 353
    • 5244245983 scopus 로고
    • A correlation of reaction rates
    • Hammond G S 1955 A correlation of reaction rates J. Am. Chem. Soc. 77 334-8
    • (1955) J. Am. Chem. Soc. , vol.77 , Issue.2 , pp. 334-338
    • Hammond, G.S.1
  • 356
    • 38349086420 scopus 로고    scopus 로고
    • Energy landscape roughness of the streptavidin-biotin interaction
    • Rico F and Moy V T 2007 Energy landscape roughness of the streptavidin-biotin interaction J. Mol. Recognit. 20 495-501
    • (2007) J. Mol. Recognit. , vol.20 , Issue.6 , pp. 495-501
    • Rico, F.1    Moy, V.T.2
  • 357
    • 20044395620 scopus 로고    scopus 로고
    • Direct measurement of protein energy landscape roughness
    • DOI 10.1038/sj.embor.7400403
    • Nevo R, Brumfeld V, Kapon R, Hinterdorfer P and Reich Z 2005 Direct measurement of protein energy landscape roughness EMBO Rep. 6 482-6 (Pubitemid 40767083)
    • (2005) EMBO Reports , vol.6 , Issue.5 , pp. 482-486
    • Nevo, R.1    Brumfeld, V.2    Kapon, R.3    Hinterdorfer, P.4    Reich, Z.5
  • 358
    • 77950021500 scopus 로고    scopus 로고
    • PH-dependent interactions guide the folding and gate the transmembrane pore of the β-barrel membrane protein OmpG
    • Damaghi M, Bippes C, Koster S, Yildiz O, Mari S A, Kuhlbrandt W and Muller D J 2010 pH-dependent interactions guide the folding and gate the transmembrane pore of the β-barrel membrane protein OmpG J. Mol. Biol. 397 878-82
    • (2010) J. Mol. Biol. , vol.397 , Issue.4 , pp. 878-882
    • Damaghi, M.1    Bippes, C.2    Koster, S.3    Yildiz, O.4    Mari, S.A.5    Kuhlbrandt, W.6    Muller, D.J.7
  • 359
    • 0023658628 scopus 로고
    • PH dependence of bacteriorhodopsin thermal unfolding
    • Brouillette C G, Muccio D D and Finney T K 1987 pH dependence of bacteriorhodopsin thermal unfolding Biochemistry 26 7431-8
    • (1987) Biochemistry , vol.26 , Issue.23 , pp. 7431-7438
    • Brouillette, C.G.1    Muccio, D.D.2    Finney, T.K.3
  • 360
    • 0033524486 scopus 로고    scopus 로고
    • Glucose-induced thermal stabilization of the native conformation of GLUT 1
    • DOI 10.1021/bi981893z
    • Epand R F, Epand R M and Jung C Y 1999 Glucose-induced thermal stabilization of the native conformation of GLUT 1 Biochemistry 38 454-8 (Pubitemid 29035716)
    • (1999) Biochemistry , vol.38 , Issue.1 , pp. 454-458
    • Epand, R.F.1    Epand, R.M.2    Jung, C.Y.3
  • 361
    • 0035909103 scopus 로고    scopus 로고
    • Thermal destabilization of rhodopsin and opsin by proteolytic cleavage in bovine rod outer segment disk membranes
    • DOI 10.1021/bi0100539
    • Landin J S, Katragadda M and Albert A D 2001 Thermal destabilization of rhodopsin and opsin by proteolytic cleavage in bovine rod outer segment disk membranes Biochemistry 40 11176-83 (Pubitemid 32847986)
    • (2001) Biochemistry , vol.40 , Issue.37 , pp. 11176-11183
    • Landin, J.S.1    Katragadda, M.2    Albert, A.D.3
  • 362
    • 0025129186 scopus 로고
    • Thermal stability of membrane-reconstituted yeast cytochrome c oxidase
    • DOI 10.1021/bi00455a028
    • Morin P E, Diggs D and Freire E 1990 Thermal stability of membrane-reconstituted yeast cytochrome c oxidase Biochemistry 29 781-8 (Pubitemid 20041964)
    • (1990) Biochemistry , vol.29 , Issue.3 , pp. 781-788
    • Morin, P.E.1    Diggs, D.2    Freire, E.3
  • 363
    • 0029032977 scopus 로고
    • A pathway for the thermal destabilization of bacteriorhodopsin
    • Taneva S G, Caaveiro J M, Muga A and Gõi F M 1995 A pathway for the thermal destabilization of bacteriorhodopsin FEBS Lett. 367 297-300
    • (1995) FEBS Lett. , vol.367 , Issue.3 , pp. 297-300
    • Taneva, S.G.1    Caaveiro, J.M.2    Muga, A.3    Gõi, F.M.4
  • 364
    • 0029112313 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia T and Freire E 1995 Forces and factors that contribute to the structural stability of membrane proteins Biochim. Biophys. Acta Rev. Biomembr. 1241 295-322
    • (1995) Biochim. Biophys. Acta Rev. Biomembr. , vol.1241 , pp. 295-322
    • Haltia, T.1    Freire, E.2
  • 365
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • DOI 10.1021/bi963095j
    • Lau F W and Bowie J U 1997 A method for assessing the stability of a membrane protein Biochemistry 36 5884-92 (Pubitemid 27214941)
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 366
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • London E and Khorana H G 1982 Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures J. Biol. Chem. 257 7003-11
    • (1982) J. Biol. Chem. , vol.257 , pp. 7003-7011
    • London, E.1    Khorana, H.G.2
  • 368
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang K S, Bayley H, Liao M J, London E and Khorana H G 1981 Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments J. Biol. Chem. 256 3802-9
    • (1981) J. Biol. Chem. , vol.256 , pp. 3802-3809
    • Huang, K.S.1    Bayley, H.2    Liao, M.J.3    London, E.4    Khorana, H.G.5
  • 371
    • 15944387765 scopus 로고    scopus 로고
    • Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling
    • DOI 10.1016/j.tips.2005.02.009
    • Klein-Seetharaman J 2005 Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling Trends Pharmacol. Sci. 26 183-9 (Pubitemid 40432653)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.4 , pp. 183-189
    • Klein-Seetharaman, J.1
  • 374
    • 0017172010 scopus 로고
    • Binding of radioactively labeled carboxyatractyloside, atractyloside and bongkrekic acid to the ADP translocator of potato mitochondria
    • Vignais P V, Douce R, Lauquin G J M and Vignais P M 1976 Binding of radioactively labeled carboxyatractyloside, atractyloside and bongkrekic acid to the ADP translocator of potato mitochondria Biochim. Biophys. Acta Bioenerg. 440 688-96
    • (1976) Biochim. Biophys. Acta Bioenerg. , vol.440 , Issue.3 , pp. 688-696
    • Vignais, P.V.1    Douce, R.2    Lauquin, G.J.M.3    Vignais, P.M.4
  • 375
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • DOI 10.1016/j.tips.2007.06.003, PII S0165614707001459, Allosterism and Collateral Efficacy
    • Kobilka B K and Deupi X 2007 Conformational complexity of G-protein-coupled receptors Trends Pharmacol. Sci. 28 397-406 (Pubitemid 47087966)
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.8 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 376
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai C J, Kumar S, Ma B and Nussinov R 1999 Folding funnels, binding funnels, and protein function Protein Sci. 8 1181-90 (Pubitemid 29264948)
    • (1999) Protein Science , vol.8 , Issue.6 , pp. 1181-1190
    • Tsai, C.-J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 377
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R O 1992 Integrins: versatility, modulation, and signaling in cell adhesion Cell 69 11-25
    • (1992) Cell , vol.69 , Issue.1 , pp. 11-25
    • Hynes, R.O.1
  • 378
    • 77956143566 scopus 로고    scopus 로고
    • New insights into the dynamics of cell adhesions
    • Costa P and Parsons M 2010 New insights into the dynamics of cell adhesions Int. Rev. Cell Molec. Biol. 283 57-91
    • (2010) Int. Rev. Cell Molec. Biol. , vol.283 , pp. 57-91
    • Costa, P.1    Parsons, M.2
  • 380
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger B, Bershadsky A, Pankov R and Yamada K M 2001 Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk Nature Rev. Mol. Cell Biol. 2 793-805
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , Issue.11 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 381
    • 29244433026 scopus 로고    scopus 로고
    • Analyzing focal adhesion structure by atomic force microscopy
    • DOI 10.1242/jcs.02653
    • Franz C M and Muller D J 2005 Analyzing focal adhesion structure by atomic force microscopy J. Cell Sci. 118 5315-23 (Pubitemid 41819593)
    • (2005) Journal of Cell Science , vol.118 , Issue.22 , pp. 5315-5323
    • Franz, C.M.1    Muller, D.J.2
  • 382
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
    • Grashoff C et al 2010 Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics Nature 466 263-6
    • (2010) Nature , vol.466 , Issue.7303 , pp. 263-266
    • Grashoff, C.1
  • 383
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • DOI 10.1038/nmeth.1208, PII NMETH.1208
    • Roy R, Hohng S and Ha T 2008 A practical guide to single-molecule FRET Nature Methods 5 507-16 (Pubitemid 351761757)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 384
    • 56749104130 scopus 로고    scopus 로고
    • Fluorescent probes for super-resolution imaging in living cells
    • Fernandez-Suarez M and Ting A Y 2008 Fluorescent probes for super-resolution imaging in living cells Nature Rev. Mol. Cell Biol. 9 929-43
    • (2008) Nature Rev. Mol. Cell Biol. , vol.9 , Issue.12 , pp. 929-943
    • Fernandez-Suarez, M.1    Ting, A.Y.2
  • 385
    • 34249945258 scopus 로고    scopus 로고
    • Far-field optical nanoscopy
    • DOI 10.1126/science.1137395
    • Hell S W 2007 Far-field optical nanoscopy Science 316 1153-8 (Pubitemid 46877470)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1153-1158
    • Hell, S.W.1


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