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Volumn 10, Issue 10, 2003, Pages 836-842

Configuration of the two kinesin motor domains during ATP hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; KINESIN; NUCLEOTIDE;

EID: 0141507035     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb984     Document Type: Article
Times cited : (72)

References (28)
  • 1
    • 0033280668 scopus 로고    scopus 로고
    • The road less traveled: Emerging principles of kinesin motor utilization
    • Goldstein, L.S.B. & Philp, A.V. The road less traveled: emerging principles of kinesin motor utilization. Annu. Rev. Cell Dev. Biol. 15, 141-183 (1999).
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 141-183
    • Goldstein, L.S.B.1    Philp, A.V.2
  • 2
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard, J., Hudspeth, A.J. & Vale, R.D. Movement of microtubules by single kinesin molecules. Nature 342, 154-158 (1989).
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 3
    • 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
  • 4
    • 0035951471 scopus 로고    scopus 로고
    • Nucleotide-dependent single- to double-headed binding of kinesin
    • Kawaguchi, K. & Ishiwata, S. Nucleotide-dependent single- to double-headed binding of kinesin. Science 291, 667-669 (2001).
    • (2001) Science , vol.291 , pp. 667-669
    • Kawaguchi, K.1    Ishiwata, S.2
  • 5
    • 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
  • 6
    • 0030266603 scopus 로고    scopus 로고
    • Three-dimensional structure of functional motor proteins on microtubules
    • Arnal, I., Metoz, F., DeBonis, S. & Wade, R.H. Three-dimensional structure of functional motor proteins on microtubules. Curr. Biol. 6, 1265-1270 (1996).
    • (1996) Curr. Biol. , vol.6 , pp. 1265-1270
    • Arnal, I.1    Metoz, F.2    DeBonis, S.3    Wade, R.H.4
  • 7
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with X-ray structure and implications for motility
    • Hoenger, A. et al. Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: comparison with X-ray structure and implications for motility. J. Cell Biol. 141, 419-430 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 419-430
    • Hoenger, A.1
  • 8
    • 0034758206 scopus 로고    scopus 로고
    • Polarized fluorescence microscopy of individual and many kinesin motors bound to axonemal microtubules
    • Peterman, E.J., Sosa, H., Goldstein, L.S. & Moerner, W.E. Polarized fluorescence microscopy of individual and many kinesin motors bound to axonemal microtubules. Biophys. J. 81, 2851-2863 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 2851-2863
    • Peterman, E.J.1    Sosa, H.2    Goldstein, L.S.3    Moerner, W.E.4
  • 9
    • 0034995132 scopus 로고    scopus 로고
    • ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
    • Sosa, H., Peterman, E.J., Moerner, W.E. & Goldstein, L.S. ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy. Nat. Struct. Biol. 8, 540-544 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 540-544
    • Sosa, H.1    Peterman, E.J.2    Moerner, W.E.3    Goldstein, L.S.4
  • 10
    • 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
  • 11
    • 0031282504 scopus 로고    scopus 로고
    • Signaling mechanistics: Aluminum fluoride for molecule of the year
    • Wittinghofer, A. Signaling mechanistics: aluminum fluoride for molecule of the year. Curr. Biol. 7, R682-R685 (1997).
    • (1997) Curr. Biol. , vol.7
    • Wittinghofer, A.1
  • 12
    • 0029914906 scopus 로고    scopus 로고
    • Weak and strong states of kinesin and ncd
    • Crevel, I.M., Lockhart, A. & Cross, R.A. Weak and strong states of kinesin and ncd. J. Mol. Biol. 257, 66-76 (1996).
    • (1996) J. Mol. Biol. , vol.257 , pp. 66-76
    • Crevel, I.M.1    Lockhart, A.2    Cross, R.A.3
  • 13
    • 0343811700 scopus 로고    scopus 로고
    • A model for the microtubule-Ncd motor protein complex obtained by cryo-electron microscopy and image analysis
    • Sosa, H. et al. A model for the microtubule-Ncd motor protein complex obtained by cryo-electron microscopy and image analysis. Cell 90, 217-224 (1997).
    • (1997) Cell , vol.90 , pp. 217-224
    • Sosa, H.1
  • 14
    • 0035942761 scopus 로고    scopus 로고
    • Switch-based mechanism of kinesin motors
    • Kikkawa, M. et al. Switch-based mechanism of kinesin motors. Nature 411, 439-445 (2001).
    • (2001) Nature , vol.411 , pp. 439-445
    • Kikkawa, M.1
  • 15
    • 0031405880 scopus 로고    scopus 로고
    • X-ray structure of motor and neck domains from rat brain kinesin
    • Sack, S. et al. X-ray structure of motor and neck domains from rat brain kinesin. Biochemistry 36, 16155-16165 (1997).
    • (1997) Biochemistry , vol.36 , pp. 16155-16165
    • Sack, S.1
  • 16
    • 0031471243 scopus 로고    scopus 로고
    • The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
    • Kozielski, F. et al. The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Cell 91, 985-994 (1997).
    • (1997) Cell , vol.91 , pp. 985-994
    • Kozielski, F.1
  • 17
    • 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • Ma, Y.Z. & Taylor, E.W. Interacting head mechanism of microtubule-kinesin ATPase. J. Biol. Chem. 272, 724-730 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 724-730
    • Ma, Y.Z.1    Taylor, E.W.2
  • 21
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert, S.P., Moyer, M.L. & Johnson, K.A. Alternating site mechanism of the kinesin ATPase. Biochemistry 37, 800-813 (1998).
    • (1998) Biochemistry , vol.37 , pp. 800-813
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 22
    • 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
  • 23
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R.D. & Milligan, R.A. The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95 (2000).
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 24
    • 0141464451 scopus 로고    scopus 로고
    • Influence of the kinesin neck domain on dimerization and ATPase kinetics
    • Jiang, W., Stock, M.F., Li, X. & Hackney, D.D. Influence of the kinesin neck domain on dimerization and ATPase kinetics. Biochemistry 37, 5288-5295 (1997).
    • (1997) Biochemistry , vol.37 , pp. 5288-5295
    • Jiang, W.1    Stock, M.F.2    Li, X.3    Hackney, D.D.4
  • 25
    • 0018785964 scopus 로고
    • A latent adenosine triphosphatase form of dynein 1 from sea urchin sperm flagella
    • Gibbons, I.R. & Fronk, E. A latent adenosine triphosphatase form of dynein 1 from sea urchin sperm flagella. J. Biol. Chem. 254, 187-196 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 187-196
    • Gibbons, I.R.1    Fronk, E.2
  • 26
    • 0031615152 scopus 로고    scopus 로고
    • Assaying processive movement of kinesin by fluorescence microscopy
    • Pierce, D.W. & Vale, R.D. Assaying processive movement of kinesin by fluorescence microscopy. Methods Enzymol. 298, 154-171 (1998).
    • (1998) Methods Enzymol. , vol.298 , pp. 154-171
    • Pierce, D.W.1    Vale, R.D.2
  • 28
    • 0033615015 scopus 로고    scopus 로고
    • Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction
    • Corrie, J.E.T. et al. Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction. Nature 400, 425-430 (1999).
    • (1999) Nature , vol.400 , pp. 425-430
    • Corrie, J.E.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.