메뉴 건너뛰기




Volumn 77, Issue 2, 1999, Pages 1003-1016

Kinetics processivity and the direction of motion of Ncd

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; KINESIN; NONCLARET DISJUNCTIONAL PROTEIN; NUCLEOTIDE; PHOSPHATE; PROTEIN; UNCLASSIFIED DRUG; VANADIC ACID;

EID: 0032804989     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76951-1     Document Type: Article
Times cited : (50)

References (38)
  • 1
    • 0028899953 scopus 로고
    • Failure of a single-headed kinesin to track parallel to microtubule protofilaments
    • Berliner, E., C. Young, K. Anderson, H. Matani, and J. Gelles. 1995. Failure of a single-headed kinesin to track parallel to microtubule protofilaments. Nature. 373:718-721.
    • (1995) Nature , vol.373 , pp. 718-721
    • Berliner, E.1    Young, C.2    Anderson, K.3    Matani, H.4    Gelles, J.5
  • 2
    • 0028098798 scopus 로고
    • Direct real time measurement of rapid inorganic phosphate release using a novel fluorescent probe
    • Brune, M., J. L. Hunter, J. E. Corrie, and M. R. Webb. 1994. Direct real time measurement of rapid inorganic phosphate release using a novel fluorescent probe. Biochemistry. 33:8262-8271.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4
  • 3
    • 0030874883 scopus 로고    scopus 로고
    • The directional preference of kinesin motors is specified by an element outside the motor catalytic domain
    • Case, R. B., D. W. Pierce, N. Hom-Booher, C. L. Hart, and R. D. Vale. 1997. The directional preference of kinesin motors is specified by an element outside the motor catalytic domain. Cell. 90:959-966.
    • (1997) Cell , vol.90 , pp. 959-966
    • Case, R.B.1    Pierce, D.W.2    Hom-Booher, N.3    Hart, C.L.4    Vale, R.D.5
  • 4
    • 0027463255 scopus 로고
    • Structural and functional domains of the Drosophila Ncd micro-tubule motor protein
    • Chandra, R., E. D. Salmon, H. P. Erickson, A. Lockhart, and S. A. Endow. 1993. Structural and functional domains of the Drosophila Ncd micro-tubule motor protein. J. Biol. Chem. 268:9005-9013.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9005-9013
    • Chandra, R.1    Salmon, E.D.2    Erickson, H.P.3    Lockhart, A.4    Endow, S.A.5
  • 5
    • 0029914906 scopus 로고    scopus 로고
    • Weak and strong states of kinesin and Ncd
    • Crevel, I. M., A. Lockhart, and R. A. Cross. 1996. Weak and strong states of kinesin and Ncd. J. Mol. Biol. 257:66-76.
    • (1996) J. Mol. Biol. , vol.257 , pp. 66-76
    • Crevel, I.M.1    Lockhart, A.2    Cross, R.A.3
  • 6
    • 0031576329 scopus 로고    scopus 로고
    • Kinetic evidence for low chemical processivity in Ncd and eg5
    • Crevel, I. M., A. Lockhart, and R. A. Cross. 1997. Kinetic evidence for low chemical processivity in Ncd and eg5. J. Mol Biol. 273:160-170.
    • (1997) J. Mol Biol. , vol.273 , pp. 160-170
    • Crevel, I.M.1    Lockhart, A.2    Cross, R.A.3
  • 7
    • 0032567442 scopus 로고    scopus 로고
    • Equilibrium binding studies of non-claret disjunction protein (Ncd) reveal cooperative inter-actions between motor domains
    • Foster, K. A., J. J. Correia, and S. P. Gilbert. 1998. Equilibrium binding studies of non-claret disjunction protein (Ncd) reveal cooperative inter-actions between motor domains. J. Biol. Chem. 273:35307-35318.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35307-35318
    • Foster, K.A.1    Correia, J.J.2    Gilbert, S.P.3
  • 8
    • 0028985886 scopus 로고
    • Pathway of processive ATP hydrolysis by kinesin
    • Gilbert, S. P., M. R. Webb, M. Brune, and K. A. Johnson. 1995. Pathway of processive ATP hydrolysis by kinesin. Nature. 373:671-676.
    • (1995) Nature , vol.373 , pp. 671-676
    • Gilbert, S.P.1    Webb, M.R.2    Brune, M.3    Johnson, K.A.4
  • 9
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert, S. P., M. L. Moyer, and K. A. Johnson. 1998. Alternating site mechanism of the kinesin ATPase. Biochemistry. 37:792-799.
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 10
    • 0032555532 scopus 로고    scopus 로고
    • Determinants of kinesin motor polarity
    • Endow, S. A., and K. W. Waligora. 1998. Determinants of kinesin motor polarity. Science. 281:1200-1202.
    • (1998) Science , vol.281 , pp. 1200-1202
    • Endow, S.A.1    Waligora, K.W.2
  • 11
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule stimulated ATP hydrolysis
    • Hackney, D. D. 1994. Evidence for alternating head catalysis by kinesin during microtubule stimulated ATP hydrolysis. Proc. Nat. Acad. Sci. USA. 91:6865-6869.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 12
    • 0029156511 scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney, D. D. 1995. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature. 377:448-450.
    • (1995) Nature , vol.377 , pp. 448-450
    • Hackney, D.D.1
  • 13
    • 0030924142 scopus 로고    scopus 로고
    • Reversal in the direction of movement of a molecular motor
    • Henningsen, U., and M. Schliva. 1997. Reversal in the direction of movement of a molecular motor. Nature. 389:93-95.
    • (1997) Nature , vol.389 , pp. 93-95
    • Henningsen, U.1    Schliva, M.2
  • 14
    • 0029795642 scopus 로고    scopus 로고
    • Three dimensional cryoelectron microscopy of dimeric kinesin and Ncd motor domains on microtulules
    • Hirose, K., A Lockhart, R. A. Cross, and L. A. Amos. 1996. Three dimensional cryoelectron microscopy of dimeric kinesin and Ncd motor domains on microtulules. Proc. Nat. Acad. Sci. USA. 93:9539-9544.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 9539-9544
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 15
    • 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., S. Sack, M. Thormahlen, A. Marx, J. Muller, H. Gross, and E. Mandelkow. 1998. 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) J. Cell Biol. , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormahlen, M.3    Marx, A.4    Muller, J.5    Gross, H.6    Mandelkow, E.7
  • 16
    • 0030844286 scopus 로고    scopus 로고
    • Coupling of kinesin steps to ATP hydrolysis
    • Hua, W., E. C. Young, M. L. Flemming, and J. Gelles. 1997. Coupling of kinesin steps to ATP hydrolysis. Nature. 388:390-393.
    • (1997) Nature , vol.388 , pp. 390-393
    • Hua, W.1    Young, E.C.2    Flemming, M.L.3    Gelles, J.4
  • 17
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptation to cellular function
    • Howard, J. 1997. Molecular motors: structural adaptation to cellular function. Nature. 389:154-158.
    • (1997) Nature , vol.389 , pp. 154-158
    • Howard, J.1
  • 18
    • 0031041380 scopus 로고    scopus 로고
    • Monomeric kinesin head domains hydrolyze multiple ATP molecules before release from a microtubule
    • Jiang, W., and D. D. Hackney. 1997. Monomeric kinesin head domains hydrolyze multiple ATP molecules before release from a microtubule. J. Biol. Chem. 272:5616-5621.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5616-5621
    • Jiang, W.1    Hackney, D.D.2
  • 20
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structure similar to myosin
    • Kull, F. J., E. P. Sablin, R. Lau, R. J. Fletterick, and R. D. Vale. 1996. Crystal structure of the kinesin motor domain reveals a structure similar to myosin. Nature. 380:550-555.
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 21
    • 0029148759 scopus 로고
    • ADP release is the rate limiting step of the MT activated ATPase of non-claret disjunctional and kinesin
    • Lockhart, A., R. A. Cross, and D. F. McKillop. 1995. ADP release is the rate limiting step of the MT activated ATPase of non-claret disjunctional and kinesin. FEBS Lett. 368:531-535.
    • (1995) FEBS Lett. , vol.368 , pp. 531-535
    • Lockhart, A.1    Cross, R.A.2    McKillop, D.F.3
  • 22
    • 0030044339 scopus 로고    scopus 로고
    • Kinetics and motility of the eg5 microtubule motor
    • Lockhart, A., and R. A. Cross. 1996. Kinetics and motility of the eg5 microtubule motor. Biochemistry. 35:2365-2373.
    • (1996) Biochemistry , vol.35 , pp. 2365-2373
    • Lockhart, A.1    Cross, R.A.2
  • 23
    • 0028210495 scopus 로고
    • Kinetic mechanism of myofibril ATPase
    • Ma, Y. Z., and E. W. Taylor. 1994. Kinetic mechanism of myofibril ATPase. Biophys. J. 66:1542-1553.
    • (1994) Biophys. J. , vol.66 , pp. 1542-1553
    • Ma, Y.Z.1    Taylor, E.W.2
  • 24
    • 0028865659 scopus 로고
    • Mechanism of microtubule kinesin ATPase
    • Ma, Y. Z., and E. W. Taylor. 1995. Mechanism of microtubule kinesin ATPase. Biochemistry. 34:13242-13251.
    • (1995) Biochemistry , vol.34 , pp. 13242-13251
    • Ma, Y.Z.1    Taylor, E.W.2
  • 25
    • 0031022509 scopus 로고    scopus 로고
    • Kinetic mechanism of a monomeric kinesin construct
    • Ma, Y. Z., and E. W. Taylor. 1997a. Kinetic mechanism of a monomeric kinesin construct. J. Biol. Chem. 272:717-723.
    • (1997) J. Biol. Chem. , vol.272 , pp. 717-723
    • Ma, Y.Z.1    Taylor, E.W.2
  • 26
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • Ma, Y. Z., and E. W. Taylor. 1997b. Interacting head mechanism of microtubule-kinesin ATPase. J. Biol. Chem. 272:724-730.
    • (1997) J. Biol. Chem. , vol.272 , pp. 724-730
    • Ma, Y.Z.1    Taylor, E.W.2
  • 27
    • 0032548491 scopus 로고    scopus 로고
    • Pathway of ATP hydrolysis by monomeric and dimeric kinesin
    • Moyer, M. L., S. P. Gilbert, and K. A. Johnson. 1998. Pathway of ATP hydrolysis by monomeric and dimeric kinesin. Biochemistry. 37: 800-813.
    • (1998) Biochemistry , vol.37 , pp. 800-813
    • Moyer, M.L.1    Gilbert, S.P.2    Johnson, K.A.3
  • 28
    • 0030695901 scopus 로고    scopus 로고
    • Kinetic mechanism of monomeric non-claret disjunctional protein
    • Pechatnikova, E., and E. W. Taylor. 1997. Kinetic mechanism of monomeric non-claret disjunctional protein. J. Biol. Chem. 272:30735-30740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30735-30740
    • Pechatnikova, E.1    Taylor, E.W.2
  • 29
    • 0032559824 scopus 로고    scopus 로고
    • Role of kinesin neck region in processive microtubule based motility
    • Romberg, L., D. W. Pierce, and R. D. Vale. 1998. Role of kinesin neck region in processive microtubule based motility. J. Cell Biol. 140: 1407-1416.
    • (1998) J. Cell Biol. , vol.140 , pp. 1407-1416
    • Romberg, L.1    Pierce, D.W.2    Vale, R.D.3
  • 32
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8 nm step
    • Schnitzer, M. J., and S. M. Block. 1997. Kinesin hydrolyses one ATP per 8 nm step. Nature. 388:386-390.
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 33
    • 0028949968 scopus 로고
    • Comparison of the motile and enzymatic properties of two microtubule minus-end-directed motors, Ncd and cytoplasmic dynein
    • Shimizu, T., Y. Y. Toyoshima, M. Edamatsu, and R. D. Vale. 1995a. Comparison of the motile and enzymatic properties of two microtubule minus-end-directed motors, Ncd and cytoplasmic dynein. Biochemistry. 34:1575-1582.
    • (1995) Biochemistry , vol.34 , pp. 1575-1582
    • Shimizu, T.1    Toyoshima, Y.Y.2    Edamatsu, M.3    Vale, R.D.4
  • 34
    • 0028838570 scopus 로고
    • Expression, purification, ATPase properties and microtubule binding properties of the Ncd motor domain
    • Shimizu, T., E Sablin, R. D. Vale, R. Fletterick, E. Pechatnikova, and E. W. Taylor. 1995b. Expression, purification, ATPase properties and microtubule binding properties of the Ncd motor domain. Biochemistry. 34: 13259-13266.
    • (1995) Biochemistry , vol.34 , pp. 13259-13266
    • Shimizu, T.1    Sablin, E.2    Vale, R.D.3    Fletterick, R.4    Pechatnikova, E.5    Taylor, E.W.6
  • 37
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale, R. D., T. Funatsu, D. W. Pierce, L. Romberg, Y. Harada, and T. Yanagida. 1996. Direct observation of single kinesin molecules moving along microtubules. Nature. 380:451-453.
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 38
    • 0032502328 scopus 로고    scopus 로고
    • One head kinesin derivatives move by a nonprocessive, low duty ratio mechanism
    • Young, E. C., H. K. Mahtani, and J. Gelles. 1998. One head kinesin derivatives move by a nonprocessive, low duty ratio mechanism. Biochemistry. 37:3467-3479.
    • (1998) Biochemistry , vol.37 , pp. 3467-3479
    • Young, E.C.1    Mahtani, H.K.2    Gelles, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.