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Volumn 100, Issue 10, 2011, Pages 2450-2456

Kinesin walks the line: Single motors observed by atomic force microscopy

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EID: 79959681283     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.04.015     Document Type: Article
Times cited : (34)

References (43)
  • 2
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R. D., and R. A. Milligan. 2000. The way things move: looking under the hood of molecular motor proteins. Science. 288:88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 3
    • 79951971261 scopus 로고    scopus 로고
    • Moving into the cell: Single-molecule studies of molecular motors in complex environments
    • Veigel, C., and C. F. Schmidt. 2011. Moving into the cell: single-molecule studies of molecular motors in complex environments. Nat. Rev. Mol. Cell Biol. 12:163-176.
    • (2011) Nat. Rev. Mol. Cell. Biol. , vol.12 , pp. 163-176
    • Veigel, C.1    Schmidt, C.F.2
  • 4
    • 0025934829 scopus 로고
    • A model for kinesin movement from nanometer-level movements of kinesin and cytoplasmic dynein and force measurements
    • Kuo, S. C., J. Gelles, ..., M. P. Sheetz. 1991. A model for kinesin movement from nanometer-level movements of kinesin and cytoplasmic dynein and force measurements. J. Cell Sci. Suppl. 14:135-138.
    • (1991) J. Cell. Sci. Suppl. , vol.14 , pp. 135-138
    • Kuo, S.C.1    Gelles, J.2    Sheetz, M.P.3
  • 5
    • 0027211908 scopus 로고
    • Kinesin follows the microtubule's protofilament axis
    • DOI 10.1083/jcb.121.5.1083
    • Ray, S., E. Meyhöfer, ..., J. Howard. 1993. Kinesin follows the microtubule's protofilament axis. J. Cell Biol. 121:1083-1093. (Pubitemid 23154269)
    • (1993) Journal of Cell Biology , vol.121 , Issue.5 , pp. 1083-1093
    • Ray, S.1    Meyhofer, E.2    Milligan, R.A.3    Howard, J.4
  • 6
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • DOI 10.1038/41111
    • Schnitzer, M. J., and S. M. Block. 1997. Kinesin hydrolyses one ATP per 8-nm step. Nature. 388:386-390. (Pubitemid 27334818)
    • (1997) Nature , vol.388 , Issue.6640 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 7
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • DOI 10.1038/365721a0
    • Svoboda, K., C. F. Schmidt, ..., S. M. Block. 1993. Direct observation of kinesin stepping by optical trapping interferometry. Nature. 365:721-727. (Pubitemid 23339876)
    • (1993) Nature , vol.365 , Issue.6448 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 10
    • 0036469037 scopus 로고    scopus 로고
    • Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements
    • DOI 10.1126/science.1063089
    • Hua, W., J. Chung, and J. Gelles. 2002. Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements. Science. 295:844-848. (Pubitemid 34118363)
    • (2002) Science , vol.295 , Issue.5556 , pp. 844-848
    • Hua, W.1    Chung, J.2    Gelles, J.3
  • 11
    • 0345257160 scopus 로고    scopus 로고
    • Alternate fast and slow stepping of a heterodimeric kinesin molecule
    • DOI 10.1038/ncb1067
    • Kaseda, K., H. Higuchi, and K. Hirose. 2003. Alternate fast and slow stepping of a heterodimeric kinesin molecule. Nat. Cell Biol. 5:1079-1082. (Pubitemid 37509114)
    • (2003) Nature Cell Biology , vol.5 , Issue.12 , pp. 1079-1082
    • Kaseda, K.1    Higuchi, H.2    Hirose, K.3
  • 12
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin Moves by an Asymmetric Hand-Over-Hand Mechanism
    • DOI 10.1126/science.1092985
    • Asbury, C. L., A. N. Fehr, and S. M. Block. 2003. Kinesin moves by an asymmetric hand-over-hand mechanism. Science. 302:2130-2134. (Pubitemid 38017947)
    • (2003) Science , vol.302 , Issue.5653 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 13
    • 34147188510 scopus 로고    scopus 로고
    • An ATP gate controls tubulin binding by the tethered head of kinesin-1
    • DOI 10.1126/science.1136985
    • Alonso, M. C., D. R. Drummond, ..., R. A. Cross. 2007. An ATP gate controls tubulin binding by the tethered head of kinesin-1. Science. 316:120-123. (Pubitemid 46559532)
    • (2007) Science , vol.316 , Issue.5821 , pp. 120-123
    • Alonso, M.C.1    Drummond, D.R.2    Kain, S.3    Hoeng, J.4    Amos, L.5    Cross, R.A.6
  • 14
    • 65249096643 scopus 로고    scopus 로고
    • A mobile kinesin-head intermediate during the ATP-waiting state
    • Asenjo, A. B., and H. Sosa. 2009. A mobile kinesin-head intermediate during the ATP-waiting state. Proc. Natl. Acad. Sci. USA. 106:5657-5662.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5657-5662
    • Asenjo, A.B.1    Sosa, H.2
  • 15
    • 36749068925 scopus 로고    scopus 로고
    • How kinesin waits between steps
    • DOI 10.1038/nature06346, PII NATURE06346
    • Mori, T., R. D. Vale, and M. Tomishige. 2007. How kinesin waits between steps. Nature. 450:750-754. (Pubitemid 350207692)
    • (2007) Nature , vol.450 , Issue.7170 , pp. 750-754
    • Mori, T.1    Vale, R.D.2    Tomishige, M.3
  • 16
    • 0942279641 scopus 로고    scopus 로고
    • Kinesin walks handover-hand
    • Yildiz, A., M. Tomishige, ..., P. R. Selvin. 2004. Kinesin walks handover-hand. Science. 303:676-678.
    • (2004) Science , vol.303 , pp. 676-678
    • Yildiz, A.1    Tomishige, M.2    Selvin, P.R.3
  • 18
    • 0141507035 scopus 로고    scopus 로고
    • Configuration of the two kinesin motor domains during ATP hydrolysis
    • DOI 10.1038/nsb984
    • Asenjo, A. B., N. Krohn, and H. Sosa. 2003. Configuration of the two kinesin motor domains during ATP hydrolysis. Nat. Struct. Biol. 10:836-842. (Pubitemid 37187656)
    • (2003) Nature Structural Biology , vol.10 , Issue.10 , pp. 836-842
    • Asenjo, A.B.1    Krohn, N.2    Sosa, H.3
  • 20
    • 85044686436 scopus 로고
    • Analysis of high resolution recordings of motor movement
    • Block, S. M., and K. Svoboda. 1995. Analysis of high resolution recordings of motor movement. Biophys. J. 68:2305S-2395S.
    • (1995) Biophys. J. , vol.68
    • Block, S.M.1    Svoboda, K.2
  • 22
    • 38549168383 scopus 로고    scopus 로고
    • Kinesin steps do not alternate in size
    • DOI 10.1529/biophysj.107.126839
    • Fehr, A. N., C. L. Asbury, and S. M. Block. 2008. Kinesin steps do not alternate in size. Biophys. J. 94:L20-L22. (Pubitemid 351162441)
    • (2008) Biophysical Journal , vol.94 , Issue.3
    • Fehr, A.N.1    Asbury, C.L.2    Block, S.M.3
  • 23
    • 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 , pp. 68-71
    • Giessibl, F.J.1
  • 24
    • 0001361115 scopus 로고
    • True atomic resolution by atomic force microscopy through repulsive and attractive forces
    • Ohnesorge, F., and G. Binnig. 1993. True atomic resolution by atomic force microscopy through repulsive and attractive forces. Science. 260:1451-1456.
    • (1993) Science , vol.260 , pp. 1451-1456
    • Ohnesorge, F.1    Binnig, G.2
  • 25
    • 0031930529 scopus 로고    scopus 로고
    • Thermal noise limitations on micromechanical experiments
    • DOI 10.1007/s002490050113
    • Gittes, F., and C. F. Schmidt. 1998. Thermal noise limitations on micromechanical experiments. Eur. Biophys. J. Biophys. Lett. 27:75-81. (Pubitemid 28105808)
    • (1998) European Biophysics Journal , vol.27 , Issue.1 , pp. 75-81
    • Gittes, F.1    Schmidt, C.F.2
  • 27
    • 0345276566 scopus 로고    scopus 로고
    • A high-speed atomic force microscope for studying biological macromolecules in action
    • Ando, T., N. Kodera, ..., Y. Y. Toyoshima. 2003. A high-speed atomic force microscope for studying biological macromolecules in action. ChemPhysChem. 4:1196-1202.
    • (2003) ChemPhysChem , vol.4 , pp. 1196-1202
    • Ando, T.1    Kodera, N.2    Toyoshima, Y.Y.3
  • 28
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin V by high-speed atomic force microscopy
    • Kodera, N., D. Yamamoto, ..., T. Ando. 2010. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature. 468:72-76.
    • (2010) Nature , vol.468 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ando, T.3
  • 29
    • 4143107868 scopus 로고    scopus 로고
    • Resolving the molecular structure of microtubules under physiological conditions with scanning force microscopy
    • Schaap, I. A. T., P. J. de Pablo, and C. F. Schmidt. 2004. Resolving the molecular structure of microtubules under physiological conditions with scanning force microscopy. Eur. Biophys. J. 33:462-467. (Pubitemid 39094940)
    • (2004) European Biophysics Journal , vol.33 , Issue.5 , pp. 462-467
    • Schaap, I.A.T.1    De Pablo, P.J.2    Schmidt, C.F.3
  • 32
    • 0029980479 scopus 로고    scopus 로고
    • Characterization of the biophysical and motility properties of kinesin from the fungus Neurospora crassa
    • DOI 10.1074/jbc.271.13.7516
    • Steinberg, G., and M. Schliwa. 1996. Characterization of the biophysical and motility properties of kinesin from the fungus Neurospora crassa. J. Biol. Chem. 271:7516-7521. (Pubitemid 26107026)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.13 , pp. 7516-7521
    • Steinberg, G.1    Schliwa, M.2
  • 33
    • 33746784797 scopus 로고    scopus 로고
    • Elastic response, buckling, and instability of microtubules under radial indentation
    • DOI 10.1529/biophysj.105.077826
    • Schaap, I. A., C. Carrasco, ..., C. F. Schmidt. 2006. Elastic response, buckling, and instability of microtubules under radial indentation. Biophys. J. 91:1521-1531. (Pubitemid 44174269)
    • (2006) Biophysical Journal , vol.91 , Issue.4 , pp. 1521-1531
    • Schaap, I.A.T.1    Carrasco, C.2    De Pablo, P.J.3    MacKintosh, F.C.4    Schmidt, C.F.5
  • 35
    • 33645499298 scopus 로고    scopus 로고
    • Scanning probe acceleration microscopy (SPAM) in fluids: Mapping mechanical properties of surfacesatthe nanoscale
    • Legleiter, J., M. Park, ..., T. Kowalewski. 2006. Scanning probe acceleration microscopy (SPAM) in fluids: mapping mechanical properties of surfacesatthe nanoscale. Proc. Natl. Acad. Sci. USA. 103:4813-4818.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4813-4818
    • Legleiter, J.1    Park, M.2    Kowalewski, T.3
  • 36
    • 34047109564 scopus 로고    scopus 로고
    • WSXM: A software for scanning probe microscopy and a tool for nanotechnology
    • Horcas, I., R. Fernández, ..., A. M. Baro. 2007. WSXM: a software for scanning probe microscopy and a tool for nanotechnology. Rev. Sci. Instrum. 78:013705.
    • (2007) Rev. Sci. Instrum. , vol.78 , pp. 013705
    • Horcas, I.1    Fernández, R.2    Baro, A.M.3
  • 37
    • 0035951471 scopus 로고    scopus 로고
    • Nucleotide-dependent single- to double-headed binding of kinesin
    • DOI 10.1126/science.291.5504.667
    • Kawaguchi, K., and S. Ishiwata. 2001. Nucleotide-dependent single-to double-headed binding of kinesin. Science. 291:667-669. (Pubitemid 32150428)
    • (2001) Science , vol.291 , Issue.5504 , pp. 667-669
    • Kawaguchi, K.1    Ishiwata, S.2
  • 38
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • DOI 10.1038/16219
    • Merkel, R., P. Nassoy, ..., E. Evans. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature. 397:50-53. (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
  • 40
    • 34249008806 scopus 로고    scopus 로고
    • Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules
    • DOI 10.1016/j.jsb.2006.11.010, PII S1047847706003777
    • Schaap, I. A., B. Hoffmann, ..., C. F. Schmidt. 2007. Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules. J. Struct. Biol. 158:282-292. (Pubitemid 46779032)
    • (2007) Journal of Structural Biology , vol.158 , Issue.3 , pp. 282-292
    • Schaap, I.A.T.1    Hoffmann, B.2    Carrasco, C.3    Merkel, R.4    Schmidt, C.F.5
  • 41
    • 51549097934 scopus 로고    scopus 로고
    • Intramolecular strain coordinates kinesin stepping behavior along microtubules
    • Yildiz, A., M. Tomishige, ..., R. D. Vale. 2008. Intramolecular strain coordinates kinesin stepping behavior along microtubules. Cell. 134:1030-1041.
    • (2008) Cell. , vol.134 , pp. 1030-1041
    • Yildiz, A.1    Tomishige, M.2    Vale, R.D.3
  • 42
    • 0033534629 scopus 로고    scopus 로고
    • High-resolution model of the microtubule
    • DOI 10.1016/S0092-8674(00)80961-7
    • Nogales, E., M. Whittaker, ..., K. H. Downing. 1999. High-resolution model of the microtubule. Cell. 96:79-88. (Pubitemid 29044155)
    • (1999) Cell , vol.96 , Issue.1 , pp. 79-88
    • Nogales, E.1    Whittaker, M.2    Milligan, R.A.3    Downing, K.H.4
  • 43
    • 69949092035 scopus 로고    scopus 로고
    • Direct observation of the binding state of the kinesin head to the microtubule
    • Guydosh, N. R., and S. M. Block. 2009. Direct observation of the binding state of the kinesin head to the microtubule. Nature. 461:125-128.
    • (2009) Nature , vol.461 , pp. 125-128
    • Guydosh, N.R.1    Block, S.M.2


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