메뉴 건너뛰기




Volumn 23, Issue 4, 2012, Pages 510-515

Atomic force microscopy for the study of membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

AFM; ATOMIC FORCE MICROSCOPE (AFM); BIOLOGICAL PROCESS; CELL-CELL COMMUNICATIONS; CONFORMATIONAL CHANGE; MEMBRANE PROTEINS; MOLECULAR TRANSPORT; NATIVE ENVIRONMENT; NATIVE MEMBRANES; SINGLE MOLECULE LEVEL; SUBNANOMETER RESOLUTION; SUPRAMOLECULAR ORGANIZATIONS;

EID: 84864808515     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2011.11.032     Document Type: Review
Times cited : (39)

References (40)
  • 1
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens T.J., Arkin I.T. Do more complex organisms have a greater proportion of membrane proteins in their genomes?. Proteins 2000, 39:417-420.
    • (2000) Proteins , vol.39 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 2
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 1998, 7:1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 3
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressure in membranes
    • Marsh D. Lateral pressure in membranes. Biochim Biophys Acta 1996, 1286:183-223.
    • (1996) Biochim Biophys Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 6
    • 48649106769 scopus 로고    scopus 로고
    • AFM: a nanotool in membrane biology
    • Müller D.J. AFM: a nanotool in membrane biology. Biochemistry 2008, 47:7986-7998.
    • (2008) Biochemistry , vol.47 , pp. 7986-7998
    • Müller, D.J.1
  • 7
    • 58849147969 scopus 로고    scopus 로고
    • Atomic force microscopy of biological membranes
    • Frederix P.L., Bosshart P.D., Engel A. Atomic force microscopy of biological membranes. Biophys J 2009, 96:329-338.
    • (2009) Biophys J , vol.96 , pp. 329-338
    • Frederix, P.L.1    Bosshart, P.D.2    Engel, A.3
  • 8
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A., Müller D.J. Observing single biomolecules at work with the atomic force microscope. Nat Struct Biol 2000, 7:715-718.
    • (2000) Nat Struct Biol , vol.7 , pp. 715-718
    • Engel, A.1    Müller, D.J.2
  • 9
    • 38449087324 scopus 로고    scopus 로고
    • Atomic force microscopy and spectroscopy of native membrane proteins
    • Müller D.J., Engel A. Atomic force microscopy and spectroscopy of native membrane proteins. Nat Protoc 2007, 2:2191-2197.
    • (2007) Nat Protoc , vol.2 , pp. 2191-2197
    • Müller, D.J.1    Engel, A.2
  • 10
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope
    • Müller D.J., Fotiadis D., Scheuring S., Müller S.A., Engel A. Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope. Biophys J 1999, 76:1101-1111.
    • (1999) Biophys J , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 11
    • 80054842999 scopus 로고    scopus 로고
    • Recognizing and avoiding artifacts in atomic force microscopy imaging
    • Canale C., Torre B., Ricci D., Braga P.C. Recognizing and avoiding artifacts in atomic force microscopy imaging. Methods Mol Biol 2011, 736:31-43.
    • (2011) Methods Mol Biol , vol.736 , pp. 31-43
    • Canale, C.1    Torre, B.2    Ricci, D.3    Braga, P.C.4
  • 13
    • 0028020713 scopus 로고
    • Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy
    • Schabert F.A., Engel A. Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy. Biophys J 1994, 67:2394-2403.
    • (1994) Biophys J , vol.67 , pp. 2394-2403
    • Schabert, F.A.1    Engel, A.2
  • 15
    • 0034698003 scopus 로고    scopus 로고
    • Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence
    • Fotiadis D., Hasler L., Müller D.J., Stahlberg H., Kistler J., Engel A. Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence. J Mol Biol 2000, 300:779-789.
    • (2000) J Mol Biol , vol.300 , pp. 779-789
    • Fotiadis, D.1    Hasler, L.2    Müller, D.J.3    Stahlberg, H.4    Kistler, J.5    Engel, A.6
  • 20
    • 34248215318 scopus 로고    scopus 로고
    • Visual rhodopsin sees the light: structure and mechanism of G protein signaling
    • Ridge K.D., Palczewski K. Visual rhodopsin sees the light: structure and mechanism of G protein signaling. J Biol Chem 2007, 282:9297-9301.
    • (2007) J Biol Chem , vol.282 , pp. 9297-9301
    • Ridge, K.D.1    Palczewski, K.2
  • 21
    • 77953384365 scopus 로고    scopus 로고
    • Complexes between photoactivated rhodopsin and transducin: progress and questions
    • Jastrzebska B., Tsybovsky Y., Palczewski K. Complexes between photoactivated rhodopsin and transducin: progress and questions. Biochem J 2010, 428:1-10.
    • (2010) Biochem J , vol.428 , pp. 1-10
    • Jastrzebska, B.1    Tsybovsky, Y.2    Palczewski, K.3
  • 22
    • 34249696578 scopus 로고    scopus 로고
    • The supramolecular assemblies of voltage-dependent anion channels in the native membrane
    • Hoogenboom B.W., Suda K., Engel A., Fotiadis D. The supramolecular assemblies of voltage-dependent anion channels in the native membrane. J Mol Biol 2007, 370:246-255.
    • (2007) J Mol Biol , vol.370 , pp. 246-255
    • Hoogenboom, B.W.1    Suda, K.2    Engel, A.3    Fotiadis, D.4
  • 25
    • 51349159635 scopus 로고    scopus 로고
    • Potential of interferometric cantilever detection and its application for SFM/AFM in liquids
    • Hoogenboom B.W., Frederix P.L., Fotiadis D., Hug H.J., Engel A. Potential of interferometric cantilever detection and its application for SFM/AFM in liquids. Nanotechnology 2008, 19:384019.
    • (2008) Nanotechnology , vol.19 , pp. 384019
    • Hoogenboom, B.W.1    Frederix, P.L.2    Fotiadis, D.3    Hug, H.J.4    Engel, A.5
  • 28
    • 37849002062 scopus 로고    scopus 로고
    • Probing the organization of photosystem II in photosynthetic membranes by atomic force microscopy
    • Kirchhoff H., Lenhert S., Buchel C., Chi L., Nield J. Probing the organization of photosystem II in photosynthetic membranes by atomic force microscopy. Biochemistry 2008, 47:431-440.
    • (2008) Biochemistry , vol.47 , pp. 431-440
    • Kirchhoff, H.1    Lenhert, S.2    Buchel, C.3    Chi, L.4    Nield, J.5
  • 29
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • Müller D.J., Engel A. Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J Mol Biol 1999, 285:1347-1351.
    • (1999) J Mol Biol , vol.285 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 30
    • 77949316155 scopus 로고    scopus 로고
    • PH-induced conformational change of the beta-barrel-forming protein OmpG reconstituted into native E. coli lipids
    • Mari S.A., Koster S., Bippes C.A., Yildiz O., Kühlbrandt W., Müller D.J. pH-induced conformational change of the beta-barrel-forming protein OmpG reconstituted into native E. coli lipids. J Mol Biol 2010, 396:610-616.
    • (2010) J Mol Biol , vol.396 , pp. 610-616
    • Mari, S.A.1    Koster, S.2    Bippes, C.A.3    Yildiz, O.4    Kühlbrandt, W.5    Müller, D.J.6
  • 31
    • 0037099393 scopus 로고    scopus 로고
    • Conformational changes in surface structures of isolated Connexin26 gap junctions
    • Müller D.J., Hand G.M., Engel A., Sosinsky G. Conformational changes in surface structures of isolated Connexin26 gap junctions. EMBO J 2002, 21:3598-3607.
    • (2002) EMBO J , vol.21 , pp. 3598-3607
    • Müller, D.J.1    Hand, G.M.2    Engel, A.3    Sosinsky, G.4
  • 32
    • 34247863710 scopus 로고    scopus 로고
    • Aminosulfonate modulated pH-induced conformational changes in connexin26 hemichannels
    • Yu J., Bippes C.A., Hand G.M., Müller D.J., Sosinsky G.E. Aminosulfonate modulated pH-induced conformational changes in connexin26 hemichannels. J Biol Chem 2007, 282:8895-8904.
    • (2007) J Biol Chem , vol.282 , pp. 8895-8904
    • Yu, J.1    Bippes, C.A.2    Hand, G.M.3    Müller, D.J.4    Sosinsky, G.E.5
  • 36
  • 38
    • 80052720714 scopus 로고    scopus 로고
    • High-speed atomic force microscopy and biomolecular processes
    • Uchihashi T., Ando T. High-speed atomic force microscopy and biomolecular processes. Methods Mol Biol 2011, 736:285-300.
    • (2011) Methods Mol Biol , vol.736 , pp. 285-300
    • Uchihashi, T.1    Ando, T.2
  • 39
    • 79955510966 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy
    • Shibata M., Uchihashi T., Yamashita H., Kandori H., Ando T. Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy. Angew Chem Int Ed 2011, 50:4410-4413.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 4410-4413
    • Shibata, M.1    Uchihashi, T.2    Yamashita, H.3    Kandori, H.4    Ando, T.5
  • 40
    • 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., Ando T. High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin. Nat Nanotechnol 2010, 5:208-212.
    • (2010) Nat Nanotechnol , vol.5 , pp. 208-212
    • Shibata, M.1    Yamashita, H.2    Uchihashi, T.3    Kandori, H.4    Ando, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.