메뉴 건너뛰기




Volumn 3, Issue 11, 2007, Pages 722-726

ATP-competitive inhibitors of the mitotic kinesin KSP that function via an allosteric mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE INHIBITOR; EG5 PROTEIN; ISPINESIB; KINESIN; KINESIN SPINDLE PROTEIN; KINESIN SPINDLE PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 35349018479     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2007.34     Document Type: Article
Times cited : (96)

References (27)
  • 1
    • 18344371892 scopus 로고    scopus 로고
    • The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks
    • Kapitein, L.C. et al. The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks. Nature 435, 114-118 (2005).
    • (2005) Nature , vol.435 , pp. 114-118
    • Kapitein, L.C.1
  • 2
    • 0034605123 scopus 로고    scopus 로고
    • Probing spindle assembly mechanisms with monastrol, a small molecule inhibitor of the mitotic kinesin, Eg5
    • Kapoor, T.M., Mayer, T.U., Coughlin, M.L. & Mitchison, T.J. Probing spindle assembly mechanisms with monastrol, a small molecule inhibitor of the mitotic kinesin, Eg5. J. Cell Biol. 150, 975-988 (2000).
    • (2000) J. Cell Biol , vol.150 , pp. 975-988
    • Kapoor, T.M.1    Mayer, T.U.2    Coughlin, M.L.3    Mitchison, T.J.4
  • 3
    • 2342563857 scopus 로고    scopus 로고
    • Antitumor activity of a kinesin inhibitor
    • Sakowicz, R. et al. Antitumor activity of a kinesin inhibitor. Cancer Res. 64, 3276-3280 (2004).
    • (2004) Cancer Res , vol.64 , pp. 3276-3280
    • Sakowicz, R.1
  • 4
    • 17144405643 scopus 로고    scopus 로고
    • Mitotic kinesins: Prospects for antimitotic drug discovery
    • Bergnes, G., Brejc, K. & Belmont, L. Mitotic kinesins: prospects for antimitotic drug discovery. Curr. Top. Med. Chem. 5, 127-145 (2005).
    • (2005) Curr. Top. Med. Chem , vol.5 , pp. 127-145
    • Bergnes, G.1    Brejc, K.2    Belmont, L.3
  • 5
    • 33846523617 scopus 로고    scopus 로고
    • Targeted anti-mitotic therapies: Can we improve on tubulin agents?
    • Jackson, J.R., Patrick, D.R., Dar, M.M. & Huang, P.S. Targeted anti-mitotic therapies: can we improve on tubulin agents? Nat. Rev. Cancer 7, 107-117 (2007).
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 107-117
    • Jackson, J.R.1    Patrick, D.R.2    Dar, M.M.3    Huang, P.S.4
  • 6
    • 5444274954 scopus 로고    scopus 로고
    • Identification of the protein binding region of S-trityl-l-cysteine, a new potent inhibitor of the mitotic kinesin Eg5
    • Brier, S., Lemaire, D., DeBonis, S., Forest, E. & Kozielski, F. Identification of the protein binding region of S-trityl-l-cysteine, a new potent inhibitor of the mitotic kinesin Eg5. Biochemistry 43, 13072-13082 (2004).
    • (2004) Biochemistry , vol.43 , pp. 13072-13082
    • Brier, S.1    Lemaire, D.2    DeBonis, S.3    Forest, E.4    Kozielski, F.5
  • 8
    • 20144388363 scopus 로고    scopus 로고
    • Kinesin spindle protein (KSP) inhibitors. Part 1: The discovery of 3,5-diaryl-4,5-dihydropyrazoles as potent and selective inhibitors of the mitotic kinesin KSP
    • Cox, C.D. et al. Kinesin spindle protein (KSP) inhibitors. Part 1: the discovery of 3,5-diaryl-4,5-dihydropyrazoles as potent and selective inhibitors of the mitotic kinesin KSP. Bioorg. Med. Chem. Lett. 15, 2041-2045 (2005).
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 2041-2045
    • Cox, C.D.1
  • 9
    • 33646175956 scopus 로고    scopus 로고
    • Kinesin spindle protein (KSP) inhibitors. Part 4: Structure-based design of 5-alkylamino-3,5-diaryl-4,5-dihydropyrazoles as potent, water-soluble inhibitors of the mitotic kinesin KSP
    • Cox, C.D. et al. Kinesin spindle protein (KSP) inhibitors. Part 4: structure-based design of 5-alkylamino-3,5-diaryl-4,5-dihydropyrazoles as potent, water-soluble inhibitors of the mitotic kinesin KSP. Bioorg. Med. Chem. Lett. 16, 3175-3179 (2006).
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , pp. 3175-3179
    • Cox, C.D.1
  • 10
    • 10044264293 scopus 로고    scopus 로고
    • Mechanism of inhibition of human KSP by monastrol: Insights from kinetic analysis and the effect of ionic strength on KSP inhibition
    • Luo, L. et al. Mechanism of inhibition of human KSP by monastrol: insights from kinetic analysis and the effect of ionic strength on KSP inhibition. Biochemistry 43, 15258-15266 (2004).
    • (2004) Biochemistry , vol.43 , pp. 15258-15266
    • Luo, L.1
  • 11
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer, T.U. et al. Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 286, 971-974 (1999).
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1
  • 12
    • 33745867225 scopus 로고    scopus 로고
    • S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression
    • Skoufias, D.A. et al. S-trityl-L-cysteine is a reversible, tight binding inhibitor of the human kinesin Eg5 that specifically blocks mitotic progression. J. Biol. Chem. 281, 17559-17569 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 17559-17569
    • Skoufias, D.A.1
  • 13
    • 10744220712 scopus 로고    scopus 로고
    • Inhibition of a mitotic motor protein: Where, how, and conformational consequences
    • Yan, Y. et al. Inhibition of a mitotic motor protein: where, how, and conformational consequences. J. Mol. Biol. 335, 547-554 (2004).
    • (2004) J. Mol. Biol , vol.335 , pp. 547-554
    • Yan, Y.1
  • 14
    • 33745246040 scopus 로고    scopus 로고
    • Molecular dissection of the inhibitor binding pocket of mitotic kinesin Eg5 reveals mutants that confer resistance to antimitotic agents
    • Brier, S., Lemaire, D., DeBonis, S., Forest, E. & Kozielski, F. Molecular dissection of the inhibitor binding pocket of mitotic kinesin Eg5 reveals mutants that confer resistance to antimitotic agents. J. Mol. Biol. 360, 360-376 (2006).
    • (2006) J. Mol. Biol , vol.360 , pp. 360-376
    • Brier, S.1    Lemaire, D.2    DeBonis, S.3    Forest, E.4    Kozielski, F.5
  • 16
    • 33646358250 scopus 로고    scopus 로고
    • Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol
    • Maliga, Z. & Mitchison, T.J. Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol. BMC Chem. Biol. 6, 2 (2006).
    • (2006) BMC Chem. Biol , vol.6 , pp. 2
    • Maliga, Z.1    Mitchison, T.J.2
  • 17
    • 34948846564 scopus 로고    scopus 로고
    • Novel ATP-competitive kinesin spindle protein inhibitors
    • published online 29 August, doi:10.1021/jm070435y
    • Parrish, C.A. et al. Novel ATP-competitive kinesin spindle protein inhibitors. J. Med. Chem. published online 29 August 2007 (doi:10.1021/jm070435y).
    • (2007) J. Med. Chem
    • Parrish, C.A.1
  • 18
    • 13244275215 scopus 로고    scopus 로고
    • A method for determining intracellular concentrations of enzyme substrates from a combination of competitive inhibition and mutagenesis studies
    • Copeland, R.A., Luo, L., Auger, K.R. & Huang, P.S. A method for determining intracellular concentrations of enzyme substrates from a combination of competitive inhibition and mutagenesis studies. Anal. Biochem. 337, 351-353 (2005).
    • (2005) Anal. Biochem , vol.337 , pp. 351-353
    • Copeland, R.A.1    Luo, L.2    Auger, K.R.3    Huang, P.S.4
  • 19
    • 33644826711 scopus 로고    scopus 로고
    • Resistance to imatinib: Mechanisms and management
    • Deininger, M. Resistance to imatinib: mechanisms and management. J. Natl. Compr. Canc. Netw. 3, 757-768 (2005).
    • (2005) J. Natl. Compr. Canc. Netw , vol.3 , pp. 757-768
    • Deininger, M.1
  • 20
    • 0036737593 scopus 로고    scopus 로고
    • The emergence of resistance to targeted cancer therapeutics
    • Mellinghoff, I.K. & Sawyers, C.L. The emergence of resistance to targeted cancer therapeutics. Pharmacogenomics 3, 603-623 (2002).
    • (2002) Pharmacogenomics , vol.3 , pp. 603-623
    • Mellinghoff, I.K.1    Sawyers, C.L.2
  • 21
    • 3442876110 scopus 로고    scopus 로고
    • KIF1A alternately uses two loops to bind microtubules
    • Nitta, R., Kikkawa, M., Okada, Y. & Hirokawa, N. KIF1A alternately uses two loops to bind microtubules. Science 305, 678-683 (2004).
    • (2004) Science , vol.305 , pp. 678-683
    • Nitta, R.1    Kikkawa, M.2    Okada, Y.3    Hirokawa, N.4
  • 22
    • 33749515974 scopus 로고    scopus 로고
    • Single-molecule observations of neck linker conformational changes in the kinesin motor protein
    • Tomishige, M., Stuurman, N. & Vale, R.D. Single-molecule observations of neck linker conformational changes in the kinesin motor protein. Nat. Struct. Mol. Biol. 13, 887-894 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 887-894
    • Tomishige, M.1    Stuurman, N.2    Vale, R.D.3
  • 23
    • 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
  • 24
    • 1542286175 scopus 로고    scopus 로고
    • A new structural state of myosin
    • Kull, F.J. & Endow, S.A. A new structural state of myosin. Trends Biochem. Sci. 29, 103-106 (2004).
    • (2004) Trends Biochem. Sci , vol.29 , pp. 103-106
    • Kull, F.J.1    Endow, S.A.2
  • 25
    • 0033081564 scopus 로고    scopus 로고
    • Resistance to non-nucleoside inhibitors of HIV-1 reverse transcriptase
    • Bacheler, L.T. Resistance to non-nucleoside inhibitors of HIV-1 reverse transcriptase. Drug Resist. Updat. 2, 56-67 (1999).
    • (1999) Drug Resist. Updat , vol.2 , pp. 56-67
    • Bacheler, L.T.1
  • 26
    • 1342325435 scopus 로고    scopus 로고
    • Defining a molecular mechanism of synergy between nucleoside and nonnucleoside AIDS drugs
    • Basavapathruni, A., Bailey, C.M. & Anderson, K.S. Defining a molecular mechanism of synergy between nucleoside and nonnucleoside AIDS drugs. J. Biol. Chem. 279, 6221-6224 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 6221-6224
    • Basavapathruni, A.1    Bailey, C.M.2    Anderson, K.S.3
  • 27
    • 0029867822 scopus 로고    scopus 로고
    • Drug combinations and effect parameters of zidovudine, stavudine, and nevirapine in standardized drug-sensitive and resistant HIV type 1 strains
    • Zhu, Q.Y., Scarborough, A., Polsky, B. & Chou, T.C. Drug combinations and effect parameters of zidovudine, stavudine, and nevirapine in standardized drug-sensitive and resistant HIV type 1 strains. AIDS Res. Hum. Retroviruses 12, 507-517 (1996).
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , pp. 507-517
    • Zhu, Q.Y.1    Scarborough, A.2    Polsky, B.3    Chou, T.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.