메뉴 건너뛰기




Volumn 587, Issue 8, 2013, Pages 997-1007

Molecular machines directly observed by high-speed atomic force microscopy

Author keywords

Atomic force microscopy; Bioimaging; Dynamic process; High speed AFM; Molecular machine; Structure dynamic

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIORHODOPSIN; MYOSIN V; PROTEIN DERIVATIVE;

EID: 84876016907     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.12.024     Document Type: Review
Times cited : (22)

References (100)
  • 1
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • C. Joo, H. Balci, Y. Ishitsuka, C. Buranachai, and T. Ha Advances in single-molecule fluorescence methods for molecular biology Annu. Rev. Biochem. 77 2008 51 76
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 2
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • B. Huang, M. Bates, and X. Zhuang Super-resolution fluorescence microscopy Annu. Rev. Biochem. 78 2009 993 1016
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 7
    • 54149113310 scopus 로고    scopus 로고
    • High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes
    • T. Ando, T. Uchihashi, and T. Fukuma High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes Prog. Surf. Sci. 83 2008 337 437
    • (2008) Prog. Surf. Sci. , vol.83 , pp. 337-437
    • Ando, T.1    Uchihashi, T.2    Fukuma, T.3
  • 8
    • 84855981532 scopus 로고    scopus 로고
    • High-speed atomic force microscopy coming of age
    • 27 pp
    • T. Ando High-speed atomic force microscopy coming of age Nanotechnology 23 2012 062001 27 pp
    • (2012) Nanotechnology , vol.23 , pp. 062001
    • Ando, T.1
  • 9
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin v by high-speed atomic force microscopy
    • N. Kodera, D. Yamamoto, R. Ishikawa, and T. Ando Video imaging of walking myosin V by high-speed atomic force microscopy Nature 468 2010 72 76
    • (2010) Nature , vol.468 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 10
    • 77749324964 scopus 로고    scopus 로고
    • High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin
    • M. Shibata, H. Yamashita, T. Uchihashi, H. Kandori, and T. Ando High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin Nat. Nanotechnol. 5 2010 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
  • 11
    • 79955510966 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy
    • M. Shibata, T. Uchihashi, H. Yamashita, H. Kandori, and T. Ando Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy Angew. Chem.; Int. Ed. 50 2011 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
  • 13
    • 0027610690 scopus 로고
    • Fractured polymer/silica fiber surface studied by tapping mode atomic force microscopy
    • Q. Zhong, D. Inniss, K. Kjoller, and V.B. Elings Fractured polymer/silica fiber surface studied by tapping mode atomic force microscopy Surf. Sci. 290 1993 L688 L692
    • (1993) Surf. Sci. , vol.290
    • Zhong, Q.1    Inniss, D.2    Kjoller, K.3    Elings, V.B.4
  • 15
    • 0141680600 scopus 로고    scopus 로고
    • Batch fabrication of sharpened silicon nitride tips
    • M. Kitazawa, K. Shiotani, and A. Toda Batch fabrication of sharpened silicon nitride tips Jpn. J. Appl. Phys. 42 2003 4844 4847
    • (2003) Jpn. J. Appl. Phys. , vol.42 , pp. 4844-4847
    • Kitazawa, M.1    Shiotani, K.2    Toda, A.3
  • 16
    • 18744378027 scopus 로고    scopus 로고
    • Active damping of the scanner for high-speed atomic force microscopy
    • 5 pp
    • N. Kodera, H. Yamashita, and T. Ando Active damping of the scanner for high-speed atomic force microscopy Rev. Sci. Instrum. 76 2005 053708 5 pp
    • (2005) Rev. Sci. Instrum. , vol.76 , pp. 053708
    • Kodera, N.1    Yamashita, H.2    Ando, T.3
  • 17
    • 33947508241 scopus 로고    scopus 로고
    • Dynamic proportional-integral-differential controller for high-speed atomic force microscopy
    • 7 pp
    • N. Kodera, M. Sakashita, and T. Ando Dynamic proportional-integral- differential controller for high-speed atomic force microscopy Rev. Sci. Instrum. 77 2006 083704 7 pp
    • (2006) Rev. Sci. Instrum. , vol.77 , pp. 083704
    • Kodera, N.1    Sakashita, M.2    Ando, T.3
  • 18
    • 84865814021 scopus 로고    scopus 로고
    • Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy
    • T. Uchihashi, N. Kodera, and T. Ando Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy Nat. Protoc. 7 2012 1193 1206
    • (2012) Nat. Protoc. , vol.7 , pp. 1193-1206
    • Uchihashi, T.1    Kodera, N.2    Ando, T.3
  • 20
    • 51349093802 scopus 로고    scopus 로고
    • Anisotropic diffusion of point defects in two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy
    • 9 pp
    • D. Yamamoto, T. Uchihashi, N. Kodera, and T. Ando Anisotropic diffusion of point defects in two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy Nanotechnology 19 2008 384009 9 pp
    • (2008) Nanotechnology , vol.19 , pp. 384009
    • Yamamoto, D.1    Uchihashi, T.2    Kodera, N.3    Ando, T.4
  • 21
  • 23
    • 80155209619 scopus 로고    scopus 로고
    • Protein-DNA interactions in high speed AFM: Single molecule diffusion analysis of human RAD54
    • H. Sanchez, Y. Suzuki, M. Yokokawa, K. Takeyasu, and C. Wyman Protein-DNA interactions in high speed AFM: single molecule diffusion analysis of human RAD54 Integr. Biol. 3 2011 1127 1134
    • (2011) Integr. Biol. , vol.3 , pp. 1127-1134
    • Sanchez, H.1    Suzuki, Y.2    Yokokawa, M.3    Takeyasu, K.4    Wyman, C.5
  • 24
    • 77958178581 scopus 로고    scopus 로고
    • Experimental evidence for membrane-mediated protein-protein interaction
    • I. Casuso, P. Sens, F. Rico, and S. Scheuring Experimental evidence for membrane-mediated protein-protein interaction Biophys. J. 99 2010 L47 L49
    • (2010) Biophys. J. , vol.99
    • Casuso, I.1    Sens, P.2    Rico, F.3    Scheuring, S.4
  • 25
    • 70349586142 scopus 로고    scopus 로고
    • High-resolution high-speed contact mode atomic force microscopy movies of purple membrane
    • I. Casuso, N. Kodera, Ch. Le Grimellec, T. Ando, and S. Scheuring High-resolution high-speed contact mode atomic force microscopy movies of purple membrane Biophys. J. 97 2009 1354 1361
    • (2009) Biophys. J. , vol.97 , pp. 1354-1361
    • Casuso, I.1    Kodera, N.2    Le Grimellec, Ch.3    Ando, T.4    Scheuring, S.5
  • 27
    • 70449103203 scopus 로고    scopus 로고
    • Streptavidin 2D crystal substrates for visualizing biomolecular processes by atomic force microscopy
    • D. Yamamoto, N. Nagura, S. Omote, M. Taniguchi, and T. Ando Streptavidin 2D crystal substrates for visualizing biomolecular processes by atomic force microscopy Biophys. J. 97 2009 2358 2367
    • (2009) Biophys. J. , vol.97 , pp. 2358-2367
    • Yamamoto, D.1    Nagura, N.2    Omote, S.3    Taniguchi, M.4    Ando, T.5
  • 28
    • 33749339997 scopus 로고    scopus 로고
    • Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational chnages of GroEL
    • M. Yokokawa, C. Wada, T. Ando, N. Sakai, A. Yagi, S.H. Yoshimura, and K. Takeyasu Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational chnages of GroEL EMBO J. 25 2006 4567 4576
    • (2006) EMBO J. , vol.25 , pp. 4567-4576
    • Yokokawa, M.1    Wada, C.2    Ando, T.3    Sakai, N.4    Yagi, A.5    Yoshimura, S.H.6    Takeyasu, K.7
  • 31
    • 73649106924 scopus 로고    scopus 로고
    • High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase i on crystalline cellulose
    • K. Igarashi, A. Koivula, M. Wada, S. Kimura, M. Penttilä, and M. Samejima High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose J. Biol. Chem. 284 2009 36186 36190
    • (2009) J. Biol. Chem. , vol.284 , pp. 36186-36190
    • Igarashi, K.1    Koivula, A.2    Wada, M.3    Kimura, S.4    Penttilä, M.5    Samejima, M.6
  • 33
    • 70449416758 scopus 로고    scopus 로고
    • Single-molecule dynamics of the DNA-EcoRII protein complexes revealed with high-speed atomic force microscopy
    • J.L. Gilmore, Y. Suzuki, G. Tamulaitis, V. Siksnys, K. Takeyasu, and Y.L. Lyubchenko Single-molecule dynamics of the DNA-EcoRII protein complexes revealed with high-speed atomic force microscopy Biochemistry 48 2009 10492 10498
    • (2009) Biochemistry , vol.48 , pp. 10492-10498
    • Gilmore, J.L.1    Suzuki, Y.2    Tamulaitis, G.3    Siksnys, V.4    Takeyasu, K.5    Lyubchenko, Y.L.6
  • 34
    • 84055217526 scopus 로고    scopus 로고
    • Visual analysis of concerted cleavage by type IIF restriction enzyme SfiI in subsecond time region
    • Y. Suzuki, J.L. Gilmore, S.H. Yoshimura, R.M. Henderson, Y.L. Lyubchenko, and K. Takeyasu Visual analysis of concerted cleavage by type IIF restriction enzyme SfiI in subsecond time region Biophys. J. 101 2011 2992 2998
    • (2011) Biophys. J. , vol.101 , pp. 2992-2998
    • Suzuki, Y.1    Gilmore, J.L.2    Yoshimura, S.H.3    Henderson, R.M.4    Lyubchenko, Y.L.5    Takeyasu, K.6
  • 35
    • 78649282278 scopus 로고    scopus 로고
    • Visualization of dynamic conformational switching of the G-quadruplex in a DNA nanostructure
    • Y. Sannohe, M. Endo, Y. Katsuda, K. Hidaka, and H. Sugiyama Visualization of dynamic conformational switching of the G-quadruplex in a DNA nanostructure J. Am. Chem. Soc. 132 2010 16311 16313
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 16311-16313
    • Sannohe, Y.1    Endo, M.2    Katsuda, Y.3    Hidaka, K.4    Sugiyama, H.5
  • 37
    • 79952753539 scopus 로고    scopus 로고
    • Direct AFM observation of an opening event of a DNA cuboid constructed via a prism structure
    • M. Endo, K. Hidaka, and H. Sugiyama Direct AFM observation of an opening event of a DNA cuboid constructed via a prism structure Org. Biomol. Chem. 9 2011 2075 2077
    • (2011) Org. Biomol. Chem. , vol.9 , pp. 2075-2077
    • Endo, M.1    Hidaka, K.2    Sugiyama, H.3
  • 38
    • 76149143416 scopus 로고    scopus 로고
    • Regulation of DNA methylation using different tensions of double strands constructed in a defined DNA nanostructure
    • M. Endo, Y. Katsuda, K. Hidaka, and H. Sugiyama Regulation of DNA methylation using different tensions of double strands constructed in a defined DNA nanostructure J. Am. Chem. Soc. 132 2010 1592 1597
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1592-1597
    • Endo, M.1    Katsuda, Y.2    Hidaka, K.3    Sugiyama, H.4
  • 40
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • R. Phillips, T. Ursell, P. Wiggins, and P. Sens Emerging roles for lipids in shaping membrane-protein function Nature 459 2009 379 385
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 43
    • 0034616649 scopus 로고    scopus 로고
    • Direct observation of processive movement by individual myosin v molecules
    • T. Sakamoto, I. Amitani, E. Yokota, and T. Ando Direct observation of processive movement by individual myosin V molecules Biochem. Biophys. Res. Commun. 272 2000 586 590
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 586-590
    • Sakamoto, T.1    Amitani, I.2    Yokota, E.3    Ando, T.4
  • 44
    • 0037832404 scopus 로고    scopus 로고
    • Myosin v walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • A. Yildiz, J.N. Forkey, S.A. McKinney, T. Ha, Y.E. Goldman, and P.R. Selvin Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization Science 300 2003 2061 2065
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 45
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin v by single-molecule fluorescence polarization
    • J.N. Forkey, M.E. Quinlan, M.A. Shaw, J.E.T. Corrier, and Y.E. Goldman Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization Nature 422 2003 399 404
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrier, J.E.T.4    Goldman, Y.E.5
  • 46
    • 17844385071 scopus 로고    scopus 로고
    • Differential labeling of myosin v heads with quantum dots allows direct visualization of hand-over-hand processivity
    • D.M. Warshaw, G.G. Kennedy, S.S. Work, E.B. Krementsova, S. Beck, and K.M. Trybus Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity Biophys. J. 88 2005 L30 L32
    • (2005) Biophys. J. , vol.88
    • Warshaw, D.M.1    Kennedy, G.G.2    Work, S.S.3    Krementsova, E.B.4    Beck, S.5    Trybus, K.M.6
  • 47
    • 51349088578 scopus 로고    scopus 로고
    • Direct observation of the mechanochemical coupling in myosin Va during processive movement
    • T. Sakamoto, M.R. Webb, E. Forgacs, H.D. White, and J.R. Sellers Direct observation of the mechanochemical coupling in myosin Va during processive movement Nature 455 2008 128 132
    • (2008) Nature , vol.455 , pp. 128-132
    • Sakamoto, T.1    Webb, M.R.2    Forgacs, E.3    White, H.D.4    Sellers, J.R.5
  • 50
    • 0036469037 scopus 로고    scopus 로고
    • Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements
    • W. Hua, J. Chung, and J. Gelles Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements Science 295 2002 844 848
    • (2002) Science , vol.295 , pp. 844-848
    • Hua, W.1    Chung, J.2    Gelles, J.3
  • 51
    • 33846476143 scopus 로고    scopus 로고
    • The diffusive search mechanism of processive myosin class-V motor involves directional steps along actin subunits
    • T. Okada, H. Tanaka, A. Hikikoshi Iwane, K. Kitamura, M. Ikebe, and T. Yanagida The diffusive search mechanism of processive myosin class-V motor involves directional steps along actin subunits Biochem. Biophys. Res. Commun. 354 2007 379 384
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 379-384
    • Okada, T.1    Tanaka, H.2    Hikikoshi Iwane, A.3    Kitamura, K.4    Ikebe, M.5    Yanagida, T.6
  • 52
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • H.E. Huxley The mechanism of muscular contraction Science 164 1969 1356 1366
    • (1969) Science , vol.164 , pp. 1356-1366
    • Huxley, H.E.1
  • 54
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • M.A. Geeves, and K.C. Holmes Structural mechanism of muscle contraction Annu. Rev. Biochem. 68 1999 687 728
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 55
    • 0023161165 scopus 로고
    • Kinetics of the actomyosin ATPase in muscle fibers
    • Y.E. Goldman Kinetics of the actomyosin ATPase in muscle fibers Annu. Rev. Physiol. 49 1987 637 654
    • (1987) Annu. Rev. Physiol. , vol.49 , pp. 637-654
    • Goldman, Y.E.1
  • 57
    • 4544232738 scopus 로고    scopus 로고
    • A model of myosin v processivity
    • S.S. Rosenfeld, and H.L. Sweeney A model of myosin V processivity J. Biol. Chem. 279 2004 40100 40111
    • (2004) J. Biol. Chem. , vol.279 , pp. 40100-40111
    • Rosenfeld, S.S.1    Sweeney, H.L.2
  • 58
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • C. Veigel, S. Schmitz, F. Wang, and J.R. Sellers Load-dependent kinetics of myosin-V can explain its high processivity Nat. Cell Biol. 7 2005 861 869
    • (2005) Nat. Cell Biol. , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 60
    • 25444437003 scopus 로고    scopus 로고
    • A force-dependent state controls the coordination of processive myosin v
    • T.J. Purcell, H.L. Sweeney, and J.A. Spudich A force-dependent state controls the coordination of processive myosin V Proc. Natl. Acad. Sci. USA 102 2005 13873 13878
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13873-13878
    • Purcell, T.J.1    Sweeney, H.L.2    Spudich, J.A.3
  • 63
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • C.A. Smith, and I. Rayment X-ray structure of the magnesium(II) ·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution Biochemistry 35 1996 5404 5417
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 64
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • R. Dominguez, Y. Freyzon, K.M. Trybus, and C. Cohen Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state Cell 94 1998 559 571
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 66
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin v structures delineate essential features of chemo-mechanical transduction
    • P.-D. Coureux, H.L. Sweeney, and A. Houdusse Three myosin V structures delineate essential features of chemo-mechanical transduction EMBO J. 23 2004 4527 4537
    • (2004) EMBO J. , vol.23 , pp. 4527-4537
    • Coureux, P.-D.1    Sweeney, H.L.2    Houdusse, A.3
  • 68
    • 67650334401 scopus 로고    scopus 로고
    • Site-directed spectroscopic probes of actomyosin structural dynamics
    • D.D. Thomas, D. Kast, and V.L. Korman Site-directed spectroscopic probes of actomyosin structural dynamics Annu. Rev. Biophys. 38 2009 347 369
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 347-369
    • Thomas, D.D.1    Kast, D.2    Korman, V.L.3
  • 70
    • 0030992359 scopus 로고    scopus 로고
    • Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin
    • H. Nakajima, Y. Kunioka, K. Nakano, K. Shimizu, M. Seto, and T. Ando Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin Biochem. Biophys. Res. Commun. 234 1997 178 182
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 178-182
    • Nakajima, H.1    Kunioka, Y.2    Nakano, K.3    Shimizu, K.4    Seto, M.5    Ando, T.6
  • 72
    • 0034702770 scopus 로고    scopus 로고
    • Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy
    • C. Yuan, A. Chen, P. Kolb, and V.T. Moy Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy Biochemistry 39 2000 10219 10223
    • (2000) Biochemistry , vol.39 , pp. 10219-10223
    • Yuan, C.1    Chen, A.2    Kolb, P.3    Moy, V.T.4
  • 73
    • 0029984843 scopus 로고    scopus 로고
    • Strength and lifetime of the bond between actin and skeletal muscle α-actinin studied with an optical trapping technique
    • H. Miyata, R. Yasuda, and K. Kinosita Jr. Strength and lifetime of the bond between actin and skeletal muscle α-actinin studied with an optical trapping technique Biochim. Biophys. Acta 1290 1996 83 88
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 83-88
    • Miyata, H.1    Yasuda, R.2    Kinosita, Jr.K.3
  • 74
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • R.A. Milligan Protein-protein interactions in the rigor actomyosin complex Proc. Natl. Acad. Sci. USA 93 1996 21 26
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 77
    • 0020491305 scopus 로고
    • 1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model
    • 1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model J. Biol. Chem. 257 1982 12030 12038
    • (1982) J. Biol. Chem. , vol.257 , pp. 12030-12038
    • Gresser, M.J.1    Myers, J.A.2    Boyer, P.D.3
  • 79
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps Cell 93 1998 1117 1124
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita, Jr.K.3    Yoshida, M.4
  • 81
    • 0032547899 scopus 로고    scopus 로고
    • 1 motor of ATP synthase
    • 1 motor of ATP synthase Nature 396 1998 279 282
    • (1998) Nature , vol.396 , pp. 279-282
    • Wang, H.1    Oster, G.2
  • 87
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • U. Haupts, J. Tittor, and D. Oesterhelt Closing in on bacteriorhodopsin: progress in understanding the molecule Annu. Rev. Biophys. Biomol. Struct. 28 1999 367 399
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 88
  • 91
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 Angstroms: Insights into color tuning and transducer interaction
    • H. Luecke, B. Schobert, J.K. Lanyi, E.N. Spudich, and J.L. Spudich Crystal structure of sensory rhodopsin II at 2.4 Angstroms: insights into color tuning and transducer interaction Science 293 2001 1499 1503
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 93
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • S. Subramaniam, and R. Henderson Molecular mechanism of vectorial proton translocation by bacteriorhodopsin Nature 406 2000 653 657
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 94
    • 0024317089 scopus 로고
    • Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • H. Otto, T. Marti, M. Holz, T. Mogi, M. Lindau, H.G. Khorana, and M.P. Heyn Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin Proc. Natl. Acad. Sci. USA 86 1989 9228 9232
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9228-9232
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 96
    • 0029886089 scopus 로고    scopus 로고
    • A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: Part of the F helix tilts in the M to N transition
    • J. Vonck A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition Biochemistry 35 1996 5870 5878
    • (1996) Biochemistry , vol.35 , pp. 5870-5878
    • Vonck, J.1
  • 97
    • 0029086922 scopus 로고
    • M-decay in the bacteriorhodopsin photocycle: Effect of cooperativity and pH
    • A.Y. Komrakov, and A.D. Kaulen M-decay in the bacteriorhodopsin photocycle: effect of cooperativity and pH Biophys. Chem. 56 1995 113 119
    • (1995) Biophys. Chem. , vol.56 , pp. 113-119
    • Komrakov, A.Y.1    Kaulen, A.D.2
  • 98
    • 0027177539 scopus 로고    scopus 로고
    • Dimeric-like kinetic cooperativity of the bacteriorhodopsin molecules in purple membranes
    • Z. Tokaji Dimeric-like kinetic cooperativity of the bacteriorhodopsin molecules in purple membranes Biophys. J. 65 1997 1130 1134
    • (1997) Biophys. J. , vol.65 , pp. 1130-1134
    • Tokaji, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.