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Volumn 435, Issue 7040, 2005, Pages 308-312

Mechanics of the kinesin step

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CELLS; DATABASE SYSTEMS; MOLECULAR BIOLOGY;

EID: 19644377414     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03528     Document Type: Article
Times cited : (628)

References (35)
  • 1
    • 0345257160 scopus 로고    scopus 로고
    • Alternate fast and slow stepping of a heterodimeric kinesin molecule
    • Kaseda, K., Higuchi, H. & Hirose, K. Alternate fast and slow stepping of a heterodimeric kinesin molecule. Nature Cell Biol. 5, 1079-1082 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 1079-1082
    • Kaseda, K.1    Higuchi, H.2    Hirose, K.3
  • 2
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • Asbury, C. L., Fehr, A. N. & Block, S. M. Kinesin moves by an asymmetric hand-over-hand mechanism. Science 302, 2130-2134 (2003).
    • (2003) Science , vol.302 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 4
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda, K., Schmidt, C. F., Schnapp, B. J. & Block, S. M. Direct observation of kinesin stepping by optical trapping interferometry. Nature 365, 721-727 (1993).
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 5
    • 0030824684 scopus 로고    scopus 로고
    • Mechanics of single kinesin molecules measured by optical trapping nanometry
    • Kojima, H., Muto, E., Higuchi, H. & Yanagida, T. Mechanics of single kinesin molecules measured by optical trapping nanometry. Biophys. J. 73, 2012-2022 (1997).
    • (1997) Biophys. J. , vol.73 , pp. 2012-2022
    • Kojima, H.1    Muto, E.2    Higuchi, H.3    Yanagida, T.4
  • 6
    • 0029877798 scopus 로고    scopus 로고
    • Detection of sub-8-nm movements of kinesin by high-resolution optical-trap microscopy
    • Coppin, C. M., Finer, J. T., Spudich, J. A. & Vale, R. D. Detection of sub-8-nm movements of kinesin by high-resolution optical-trap microscopy. Proc. Natl Acad. Sci. USA 93, 1913-1917 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1913-1917
    • Coppin, C.M.1    Finer, J.T.2    Spudich, J.A.3    Vale, R.D.4
  • 7
    • 0035069744 scopus 로고    scopus 로고
    • Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules
    • Nishiyama, M., Muto, E., Inoue, Y., Yanagida, T. & Higuchi, H. Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules. Nature Cell Biol. 3, 425-428 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 425-428
    • Nishiyama, M.1    Muto, E.2    Inoue, Y.3    Yanagida, T.4    Higuchi, H.5
  • 8
    • 0030844286 scopus 로고    scopus 로고
    • Coupling of kinesin steps to ATP hydrolysis
    • Hua, W., Young, E. C., Fleming, M. L. & Gelles, J. Coupling of kinesin steps to ATP hydrolysis. Nature 388, 390-393 (1997).
    • (1997) Nature , vol.388 , pp. 390-393
    • Hua, W.1    Young, E.C.2    Fleming, M.L.3    Gelles, J.4
  • 9
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • Schnitzer, M. J. & Block, S. M. Kinesin hydrolyses one ATP per 8-nm step. Nature 388, 386-390 (1997).
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 10
    • 0033525190 scopus 로고    scopus 로고
    • Kinesin takes one 8-nm step for each ATP that it hydrolyzes
    • Coy, D. L., Wagenbach, M. & Howard, J. Kinesin takes one 8-nm step for each ATP that it hydrolyzes. J. Biol. Chem. 274, 3667-3671 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3667-3671
    • Coy, D.L.1    Wagenbach, M.2    Howard, J.3
  • 11
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • Visscher, K., Schnitzer, M. J. & Block, S. M. Single kinesin molecules studied with a molecular force clamp. Nature 400, 184-189 (1999).
    • (1999) Nature , vol.400 , pp. 184-189
    • Visscher, K.1    Schnitzer, M.J.2    Block, S.M.3
  • 12
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney, D. D. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl Acad. Sci. USA 91, 6865-6869 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 13
    • 3242776257 scopus 로고    scopus 로고
    • The kinetic mechanism of kinesin
    • Cross, R. A. The kinetic mechanism of kinesin. Trends Biochem. Sci. 29, 301-309 (2004).
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 301-309
    • Cross, R.A.1
  • 14
    • 1142286682 scopus 로고    scopus 로고
    • Molecular engineering of a backwards-moving myosin motor
    • Tsiavaliaris, G., Fujita-Becker, S. & Manstein, D. J. Molecular engineering of a backwards-moving myosin motor. Nature 427, 558-561 (2004).
    • (2004) Nature , vol.427 , pp. 558-561
    • Tsiavaliaris, G.1    Fujita-Becker, S.2    Manstein, D.J.3
  • 15
    • 11144353812 scopus 로고    scopus 로고
    • The myosin motor in muscle generates a smaller and slower working stroke at higher load
    • Reconditi, M. et al. The myosin motor in muscle generates a smaller and slower working stroke at higher load. Nature 428, 578-581 (2004).
    • (2004) Nature , vol.428 , pp. 578-581
    • Reconditi, M.1
  • 16
    • 0033576727 scopus 로고    scopus 로고
    • A structural change in the kinesin motor protein that drives motility
    • Rice, S. et al. A structural change in the kinesin motor protein that drives motility. Nature 402, 778-784 (1999).
    • (1999) Nature , vol.402 , pp. 778-784
    • Rice, S.1
  • 17
    • 0036798857 scopus 로고    scopus 로고
    • Chemomechanical coupling of the forward and backward steps of single kinesin molecules
    • Nishiyama, M., Higuchi, H. & Yanagida, T. Chemomechanical coupling of the forward and backward steps of single kinesin molecules. Nature Cell Biol. 4, 790-797 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 790-797
    • Nishiyama, M.1    Higuchi, H.2    Yanagida, T.3
  • 18
    • 0041522803 scopus 로고    scopus 로고
    • Processivity of the single-headed kinesin KIF1A through biased binding to tubulin
    • Okada, Y., Higuchi, H. & Hirokawa, N. Processivity of the single-headed kinesin KIF1A through biased binding to tubulin. Nature 424, 574-577 (2003)
    • (2003) Nature , vol.424 , pp. 574-577
    • Okada, Y.1    Higuchi, H.2    Hirokawa, N.3
  • 19
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block, S. M., Goldstein, L. S. & Schnapp, B. J. Bead movement by single kinesin molecules studied with optical tweezers. Nature 348, 348-352 (1990).
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.2    Schnapp, B.J.3
  • 20
    • 0028145209 scopus 로고
    • The force exerted by a single kinesin molecule against a viscous load
    • Hunt, A. J., Gittes, F. & Howard, J. The force exerted by a single kinesin molecule against a viscous load. Biophys. J. 67, 766-781 (1994).
    • (1994) Biophys. J. , vol.67 , pp. 766-781
    • Hunt, A.J.1    Gittes, F.2    Howard, J.3
  • 21
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • Svoboda, K. & Block, S. M. Force and velocity measured for single kinesin molecules. Cell 77, 773-784 (1994).
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 22
    • 0034674337 scopus 로고    scopus 로고
    • Temperature dependence of force, velocity, and processivity of single kinesin molecules
    • Kawaguchi, K. & Ishiwata, S. Temperature dependence of force, velocity, and processivity of single kinesin molecules. Biochem. Biophys. Res. Commun. 272, 895-899 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 895-899
    • Kawaguchi, K.1    Ishiwata, S.2
  • 23
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion limit of chemical reactions
    • Kramers, H. A. Brownian motion in a field of force and the diffusion limit of chemical reactions. Physica 7, 284-304 (1940).
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 24
    • 0142122076 scopus 로고    scopus 로고
    • Single molecule processes on the stepwise movement of ATP-driven molecular motors
    • Nishiyama, M., Higuchi, H., Ishii, Y., Taniguchi, Y. & Yanagida, T. Single molecule processes on the stepwise movement of ATP-driven molecular motors. Biosystems 71, 145-156 (2003).
    • (2003) Biosystems , vol.71 , pp. 145-156
    • Nishiyama, M.1    Higuchi, H.2    Ishii, Y.3    Taniguchi, Y.4    Yanagida, T.5
  • 27
    • 0029795642 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules
    • Hirose, K., Lockhart, A., Cross, R. A. & Amos, L. A. Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules. Proc. Natl Acad. Sci. USA 93, 9539-9544 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9539-9544
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 28
    • 0035146785 scopus 로고    scopus 로고
    • Conformational changes during kinesin motility
    • Schief, W. R. & Howard, J. Conformational changes during kinesin motility, Curr. Opin. Cell Biol. 13, 19-28 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 19-28
    • Schief, W.R.1    Howard, J.2
  • 29
    • 0037342516 scopus 로고    scopus 로고
    • Thermodynamic properties of the Kinesin neck-region docking to the catalytic core
    • Rice, S. et al. Thermodynamic properties of the Kinesin neck-region docking to the catalytic core. Biophys. J. 84, 1844-1854 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 1844-1854
    • Rice, S.1
  • 31
    • 0034934257 scopus 로고    scopus 로고
    • Simple mechanochemistry describes the dynamics of kinesin molecules
    • Fisher, M. E. & Kolomeisky, A. B. Simple mechanochemistry describes the dynamics of kinesin molecules. Proc. Natl Acad. Sci. USA 98, 7748-7753 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7748-7753
    • Fisher, M.E.1    Kolomeisky, A.B.2
  • 32
  • 34
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7, 257-318 (1957).
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 257-318
    • Huxley, A.F.1
  • 35
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F. & Simmons, R. M. Proposed mechanism of force generation in striated muscle. Nature 233, 533-538 (1971).
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.