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Volumn 288, Issue 25, 2013, Pages 18588-18598

Snapshots of ispinesib-induced conformational changes in the mitotic kinesin eg5

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC SITES; CONFORMATIONAL CHANGE; KEY REGULATORS; MITOTIC KINESIN EG5; SMALL MOLECULE INHIBITOR;

EID: 84880052495     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.462648     Document Type: Article
Times cited : (28)

References (33)
  • 1
    • 77957887591 scopus 로고    scopus 로고
    • Kinesins at a glance
    • Endow, S. A., Kull, F. J., and Liu, H. (2010) Kinesins at a glance. J. Cell Sci. 123, 3420-3424
    • (2010) J. Cell Sci. , vol.123 , pp. 3420-3424
    • Endow, S.A.1    Kull, F.J.2    Liu, H.3
  • 2
    • 0035816597 scopus 로고    scopus 로고
    • Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker
    • Turner, J., Anderson, R., Guo, J., Beraud, C., Fletterick, R., and Sakowicz, R. (2001) Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. J. Biol. Chem. 276, 25496-25502
    • (2001) J. Biol. Chem. , vol.276 , pp. 25496-25502
    • Turner, J.1    Anderson, R.2    Guo, J.3    Beraud, C.4    Fletterick, R.5    Sakowicz, R.6
  • 4
    • 74149091292 scopus 로고    scopus 로고
    • Mutations in the human kinesin Eg5 that confer resistance to monastrol and S-trityl-L-cysteine in tumor derived cell lines
    • Tcherniuk, S., van Lis, R., Kozielski, F., and Skoufias, D. A. (2010) Mutations in the human kinesin Eg5 that confer resistance to monastrol and S-trityl-L-cysteine in tumor derived cell lines. Biochem. Pharmacol. 79, 864-872
    • (2010) Biochem. Pharmacol. , vol.79 , pp. 864-872
    • Tcherniuk, S.1    Van Lis, R.2    Kozielski, F.3    Skoufias, D.A.4
  • 5
    • 77952977790 scopus 로고    scopus 로고
    • The conserved L5 loop establishes the pre-powerstroke conformation of the kinesin-5 motor, eg5
    • Larson, A. G., Naber, N., Cooke, R., Pate, E., and Rice, S. E. (2010) The conserved L5 loop establishes the pre-powerstroke conformation of the kinesin-5 motor, eg5. Biophys. J. 98, 2619-2627
    • (2010) Biophys. J. , vol.98 , pp. 2619-2627
    • Larson, A.G.1    Naber, N.2    Cooke, R.3    Pate, E.4    Rice, S.E.5
  • 7
    • 33747624954 scopus 로고    scopus 로고
    • Allosteric inhibition of kinesin-5 modulates its processive directional motility
    • DOI 10.1038/nchembio812f, PII NCHEMBIO812
    • Kwok, B. H., Kapitein, L. C., Kim, J. H., Peterman, E. J., Schmidt, C. F., and Kapoor, T. M. (2006) Allosteric inhibition of kinesin-5 modulates its processive directional motility. Nat. Chem. Biol. 2, 480-485 (Pubitemid 44266310)
    • (2006) Nature Chemical Biology , vol.2 , Issue.9 , pp. 480-485
    • Kwok, B.H.1    Kapitein, L.C.2    Kim, J.H.3    Peterman, E.J.G.4    Schmidt, C.F.5    Kapoor, T.M.6
  • 8
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer, T. U., Kapoor, T. M., Haggarty, S. J., King, R. W., Schreiber, S. L., and Mitchison, T. J. (1999) Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 286, 971-974
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1    Kapoor, T.M.2    Haggarty, S.J.3    King, R.W.4    Schreiber, S.L.5    Mitchison, T.J.6
  • 10
    • 33646358250 scopus 로고    scopus 로고
    • Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol
    • Maliga, Z., and Mitchison, T. J. (2006) Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol. BMC Chem. Biol. 6, 2
    • (2006) BMC Chem. Biol. , vol.6 , pp. 2
    • Maliga, Z.1    Mitchison, T.J.2
  • 11
    • 3242771433 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the human kinetochore protein CENP-E
    • DOI 10.1016/j.jmb.2004.05.053, PII S0022283604005960
    • Garcia-Saez, I., Yen, T., Wade, R. H., and Kozielski, F. (2004) Crystal structure of the motor domain of the human kinetochore-associated protein CENP-E. J. Mol. Biol. 340, 1107-1116 (Pubitemid 38968704)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.5 , pp. 1107-1116
    • Garcia-Saez, I.1    Yen, T.2    Wade, R.H.3    Kozielski, F.4
  • 15
    • 79955627902 scopus 로고    scopus 로고
    • Aphase I study of ispinesib, a kinesin spindle protein inhibitor, administered weekly for three consecutive weeks of a 28-day cycle in patients with solid tumors
    • Burris, H. A., 3rd, Jones, S. F., Williams, D. D., Kathman, S. J., Hodge, J. P., Pandite, L., Ho, P. T., Boerner, S. A., and Lorusso, P. (2011)Aphase I study of ispinesib, a kinesin spindle protein inhibitor, administered weekly for three consecutive weeks of a 28-day cycle in patients with solid tumors. Invest. New Drugs 29, 467-472
    • (2011) Invest. New Drugs , vol.29 , pp. 467-472
    • Burris III, H.A.1    Jones, S.F.2    Williams, D.D.3    Kathman, S.J.4    Hodge, J.P.5    Pandite, L.6    Ho, P.T.7    Boerner, S.A.8    Lorusso, P.9
  • 17
    • 27444445780 scopus 로고    scopus 로고
    • Docking and rolling, a model of how the mitotic motor Eg5 works
    • DOI 10.1074/jbc.M506561200
    • Rosenfeld, S. S., Xing, J., Jefferson, G. M., and King, P. H. (2005) Docking and rolling, a model of how the mitotic motor Eg5 works. J. Biol. Chem. 280, 35684-35695 (Pubitemid 41532761)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35684-35695
    • Rosenfeld, S.S.1    Xing, J.2    Jefferson, G.M.3    King, P.H.4
  • 18
    • 29244476067 scopus 로고    scopus 로고
    • ATPase mechanism of Eg5 in the absence of microtubules: Insight into microtubule activation and allosteric inhibition by monastrol
    • DOI 10.1021/bi051724w
    • Cochran, J. C., and Gilbert, S. P. (2005) ATPase mechanism of Eg5 in the absence of microtubules. Insight into microtubule activation and allosteric inhibition by monastrol. Biochemistry 44, 16633-16648 (Pubitemid 41832044)
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16633-16648
    • Cochran, J.C.1    Gilbert, S.P.2
  • 19
    • 77949318844 scopus 로고    scopus 로고
    • ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism
    • Parke, C. L., Wojcik, E. J., Kim, S., and Worthylake, D. K. (2010) ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism. J. Biol. Chem. 285, 5859-5867
    • (2010) J. Biol. Chem. , vol.285 , pp. 5859-5867
    • Parke, C.L.1    Wojcik, E.J.2    Kim, S.3    Worthylake, D.K.4
  • 20
    • 72449183762 scopus 로고    scopus 로고
    • An allosteric transition trapped in an intermediate state of a new kinesininhibitor complex
    • Kaan, H. Y., Ulaganathan, V., Hackney, D. D., and Kozielski, F. (2010) An allosteric transition trapped in an intermediate state of a new kinesininhibitor complex. Biochem. J. 425, 55-60
    • (2010) Biochem. J. , vol.425 , pp. 55-60
    • Kaan, H.Y.1    Ulaganathan, V.2    Hackney, D.D.3    Kozielski, F.4
  • 21
    • 0035955690 scopus 로고    scopus 로고
    • ATP reorients the neck linker of kinesin in two sequential steps
    • Rosenfeld, S. S., Jefferson, G. M., and King, P. H. (2001) ATP reorients the neck linker of kinesin in two sequential steps. J. Biol. Chem. 276, 40167-40174
    • (2001) J. Biol. Chem. , vol.276 , pp. 40167-40174
    • Rosenfeld, S.S.1    Jefferson, G.M.2    King, P.H.3
  • 22
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer
    • Dale, R. E., Eisinger, J., and Blumberg, W. E. (1979) The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys. J. 26, 161-193
    • (1979) Biophys. J. , vol.26 , pp. 161-193
    • Dale, R.E.1    Eisinger, J.2    Blumberg, W.E.3
  • 33
    • 0020484811 scopus 로고
    • Transient kinetics of adenosine 5'-diphosphate and adenosine 5'-(β,γ-imidotriphosphate) binding to subfragment 1 and acto-subfragment 1
    • Trybus, K. M., and Taylor, E. W. (1982) Transient kinetics of adenosine 5'-diphosphate and adenosine 5'-(β,γ-imidotriphosphate) binding to subfragment 1 and acto-subfragment 1. Biochemistry 21, 1284-1294
    • (1982) Biochemistry , vol.21 , pp. 1284-1294
    • Trybus, K.M.1    Taylor, E.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.