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Volumn 17, Issue 1, 2005, Pages 12-19

Dissecting cell biology with chemical scalpels

Author keywords

[No Author keywords available]

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BLEBBISTATIN; BORTEZOMIB; BREFELDIN A; DIMINUTOL; ENZYME INHIBITOR; EPOXOMICIN; EXO 1; EXO 2; HESPERADIN; LACTACYSTIN; LEPTOMYCIN B; MG 115; MONASTROL; MYOSEVERIN; N [4 [6 METHOXY 7 (3 MORPHOLINOPROPOXY) 4 QUINAZOLINYLAMINO]PHENYL]BENZAMIDE; NUTLIN; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN INHIBITOR; PROTEOLYSIS TARGETING CHIMERIC MOLECULE; PURVALANOL; SORTIN; SULFONAMIDE; TRAPOXIN; TUBACIN; UBISTATIN; UNCLASSIFIED DRUG; WISKOSTATIN;

EID: 12344324701     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.12.004     Document Type: Review
Times cited : (6)

References (48)
  • 1
    • 0028505040 scopus 로고
    • Towards a pharmacological genetics
    • T.J. Mitchison Towards a pharmacological genetics Chem Biol 1 1994 3 6
    • (1994) Chem Biol , vol.1 , pp. 3-6
    • Mitchison, T.J.1
  • 3
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • M.A. Jordan, and L. Wilson Microtubules as a target for anticancer drugs Nat Rev Cancer 4 2004 253 265
    • (2004) Nat Rev Cancer , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 4
    • 0036909567 scopus 로고    scopus 로고
    • Small molecules, big impact: A history of chemical inhibitors and the cytoskeleton
    • J.R. Peterson, and T.J. Mitchison Small molecules, big impact: a history of chemical inhibitors and the cytoskeleton Chem Biol 9 2002 1275 1285
    • (2002) Chem Biol , vol.9 , pp. 1275-1285
    • Peterson, J.R.1    Mitchison, T.J.2
  • 5
    • 0035845540 scopus 로고    scopus 로고
    • A chemical inhibitor of N-WASP reveals a new mechanism for targeting protein interactions
    • J.R. Peterson, R.S. Lokey, T.J. Mitchison, and M.W. Kirschner A chemical inhibitor of N-WASP reveals a new mechanism for targeting protein interactions Proc Natl Acad Sci USA 98 2001 10624 10629
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10624-10629
    • Peterson, J.R.1    Lokey, R.S.2    Mitchison, T.J.3    Kirschner, M.W.4
  • 6
    • 3543015540 scopus 로고    scopus 로고
    • Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation
    • J.R. Peterson, L.C. Bickford, D. Morgan, A.S. Kim, O. Ouerfelli, M.W. Kirschner, and M.K. Rosen Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation Nat Struct Mol Biol 11 2004 747 755 A forward chemical genetic screen identifies a synthetic molecule that inhibits actin assembly in extracts. NMR studies demonstrate how the molecule stabilizes N-WASP in an autoinhibited conformation.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 747-755
    • Peterson, J.R.1    Bickford, L.C.2    Morgan, D.3    Kim, A.S.4    Ouerfelli, O.5    Kirschner, M.W.6    Rosen, M.K.7
  • 8
    • 0036233469 scopus 로고    scopus 로고
    • Inhibition and reversal of myogenic differentiation by purine-based microtubule assembly inhibitors
    • O.D. Perez, Y.T. Chang, G. Rosania, D. Sutherlin, and P.G. Schultz Inhibition and reversal of myogenic differentiation by purine-based microtubule assembly inhibitors Chem Biol 9 2002 475 483
    • (2002) Chem Biol , vol.9 , pp. 475-483
    • Perez, O.D.1    Chang, Y.T.2    Rosania, G.3    Sutherlin, D.4    Schultz, P.G.5
  • 10
    • 1142306148 scopus 로고    scopus 로고
    • Identification of a novel protein regulating microtubule stability through a chemical approach
    • S.M. Wignall, N.S. Gray, Y.T. Chang, L. Juarez, R. Jacob, A. Burlingame, P.G. Schultz, and R. Heald Identification of a novel protein regulating microtubule stability through a chemical approach Chem Biol 11 2004 135 146 This paper describes a forward chemical genetic screen for inhibitors of mitotic spindle assembly and identifies the quinone oxidoreductase NQO1 as a potential novel modulator of microtubule dynamics.
    • (2004) Chem Biol , vol.11 , pp. 135-146
    • Wignall, S.M.1    Gray, N.S.2    Chang, Y.T.3    Juarez, L.4    Jacob, R.5    Burlingame, A.6    Schultz, P.G.7    Heald, R.8
  • 11
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • C.M. Grozinger, and S.L. Schreiber Deacetylase enzymes: biological functions and the use of small-molecule inhibitors Chem Biol 9 2002 3 16
    • (2002) Chem Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 12
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin a and cyclic tetrapeptide antibiotics including trapoxin
    • R. Furumai, Y. Komatsu, N. Nishino, S. Khochbin, M. Yoshida, and S. Horinouchi Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin Proc Natl Acad Sci USA 98 2001 87 92
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 15
    • 0037448671 scopus 로고    scopus 로고
    • Cell biology: Tubulin acetylation and cell motility
    • A. Palazzo, B. Ackerman, and G.G. Gundersen Cell biology: tubulin acetylation and cell motility Nature 421 2003 230
    • (2003) Nature , vol.421 , pp. 230
    • Palazzo, A.1    Ackerman, B.2    Gundersen, G.G.3
  • 16
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • S.J. Haggarty, K.M. Koeller, J.C. Wong, C.M. Grozinger, and S.L. Schreiber Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation Proc Natl Acad Sci USA 100 2003 4389 4394 This paper describes the discovery of tubacin as a specific inhibitor of HDAC6. Tubacin inhibits tubulin deacetylation while not affecting histone acetylation levels or gene expression significantly.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 17
    • 0038522853 scopus 로고    scopus 로고
    • Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays
    • S.J. Haggarty, K.M. Koeller, J.C. Wong, R.A. Butcher, and S.L. Schreiber Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays Chem Biol 10 2003 383 396
    • (2003) Chem Biol , vol.10 , pp. 383-396
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Butcher, R.A.4    Schreiber, S.L.5
  • 18
    • 0037562075 scopus 로고    scopus 로고
    • Chemical genetic modifier screens: Small molecule trichostatin suppressors as probes of intracellular histone and tubulin acetylation
    • K.M. Koeller, S.J. Haggarty, B.D. Perkins, I. Leykin, J.C. Wong, M.C. Kao, and S.L. Schreiber Chemical genetic modifier screens: small molecule trichostatin suppressors as probes of intracellular histone and tubulin acetylation Chem Biol 10 2003 397 410
    • (2003) Chem Biol , vol.10 , pp. 397-410
    • Koeller, K.M.1    Haggarty, S.J.2    Perkins, B.D.3    Leykin, I.4    Wong, J.C.5    Kao, M.C.6    Schreiber, S.L.7
  • 19
    • 0038274087 scopus 로고    scopus 로고
    • Structural biasing elements for in-cell histone deacetylase paralog selectivity
    • J.C. Wong, R. Hong, and S.L. Schreiber Structural biasing elements for in-cell histone deacetylase paralog selectivity J Am Chem Soc 125 2003 5586 5587
    • (2003) J Am Chem Soc , vol.125 , pp. 5586-5587
    • Wong, J.C.1    Hong, R.2    Schreiber, S.L.3
  • 20
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • T.U. Mayer, T.M. Kapoor, S.J. Haggarty, R.W. King, S.L. Schreiber, and T.J. Mitchison Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen Science 286 1999 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
  • 21
    • 0034605123 scopus 로고    scopus 로고
    • Probing spindle assembly mechanisms with monastrol, a small molecule inhibitor of the mitotic kinesin, Eg5
    • T.M. Kapoor, T.U. Mayer, M.L. Coughlin, and T.J. Mitchison Probing spindle assembly mechanisms with monastrol, a small molecule inhibitor of the mitotic kinesin, Eg5 J Cell Biol 150 2000 975 988
    • (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
  • 22
    • 0036752261 scopus 로고    scopus 로고
    • Evidence that monastrol is an allosteric inhibitor of the mitotic kinesin Eg5
    • Z. Maliga, T.M. Kapoor, and T.J. Mitchison Evidence that monastrol is an allosteric inhibitor of the mitotic kinesin Eg5 Chem Biol 9 2002 989 996
    • (2002) Chem Biol , vol.9 , pp. 989-996
    • Maliga, Z.1    Kapoor, T.M.2    Mitchison, T.J.3
  • 23
    • 0042679490 scopus 로고    scopus 로고
    • Determining the position of the cell division plane
    • J.C. Canman, L.A. Cameron, P.S. Maddox, A. Straight, J.S. Tirnauer, T.J. Mitchison, G. Fang, T.M. Kapoor, and E.D. Salmon Determining the position of the cell division plane Nature 424 2003 1074 1078 By overriding the spindle checkpoint in monastrol-treated cells, this study demonstrates the ability of mammalian cells to undergo cytokinesis without forming a bipolar spindle.
    • (2003) Nature , vol.424 , pp. 1074-1078
    • Canman, J.C.1    Cameron, L.A.2    Maddox, P.S.3    Straight, A.4    Tirnauer, J.S.5    Mitchison, T.J.6    Fang, G.7    Kapoor, T.M.8    Salmon, E.D.9
  • 25
    • 1542399869 scopus 로고    scopus 로고
    • Correcting improper chromosome-spindle attachments during cell division
    • M.A. Lampson, K. Renduchitala, A. Khodjakov, and T.M. Kapoor Correcting improper chromosome-spindle attachments during cell division Nat Cell Biol 6 2004 232 237 An excellent application of chemical tools, this work uses multiple inhibitors to demonstrate the role of Aurora kinase in correcting attachment of mal-oriented chromosomes.
    • (2004) Nat Cell Biol , vol.6 , pp. 232-237
    • Lampson, M.A.1    Renduchitala, K.2    Khodjakov, A.3    Kapoor, T.M.4
  • 26
    • 0013057087 scopus 로고    scopus 로고
    • Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores
    • C. Ditchfield, V.L. Johnson, A. Tighe, R. Ellston, C. Haworth, T. Johnson, A. Mortlock, N. Keen, and S.S. Taylor Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores J Cell Biol 161 2003 267 280 This paper characterizes ZM447439 as an inhibitor of Aurora kinase and demonstrates a potential requirement for Aurora B in BubR1 regulation.
    • (2003) J Cell Biol , vol.161 , pp. 267-280
    • Ditchfield, C.1    Johnson, V.L.2    Tighe, A.3    Ellston, R.4    Haworth, C.5    Johnson, T.6    Mortlock, A.7    Keen, N.8    Taylor, S.S.9
  • 28
    • 0036178929 scopus 로고    scopus 로고
    • Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections
    • T.U. Tanaka, N. Rachidi, C. Janke, G. Pereira, M. Galova, E. Schiebel, M.J. Stark, and K. Nasmyth Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections Cell 108 2002 317 329
    • (2002) Cell , vol.108 , pp. 317-329
    • Tanaka, T.U.1    Rachidi, N.2    Janke, C.3    Pereira, G.4    Galova, M.5    Schiebel, E.6    Stark, M.J.7    Nasmyth, K.8
  • 29
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor
    • A.F. Straight, A. Cheung, J. Limouze, I. Chen, N.J. Westwood, J.R. Sellers, and T.J. Mitchison Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor Science 299 2003 1743 1747 This paper describes the discovery of blebbistatin as a specific inhibitor of nonmuscle myosin II.
    • (2003) Science , vol.299 , pp. 1743-1747
    • Straight, A.F.1    Cheung, A.2    Limouze, J.3    Chen, I.4    Westwood, N.J.5    Sellers, J.R.6    Mitchison, T.J.7
  • 31
    • 2042544799 scopus 로고    scopus 로고
    • Myosin-II-dependent cortical movement is required for centrosome separation and positioning during mitotic spindle assembly
    • J. Rosenblatt, L.P. Cramer, B. Baum, and K.M. McGee Myosin-II-dependent cortical movement is required for centrosome separation and positioning during mitotic spindle assembly Cell 117 2004 361 372 Blebbistatin is used along with biochemical and genetic techniques to demonstrate that myosin II is required for proper assembly of the mitotic spindle.
    • (2004) Cell , vol.117 , pp. 361-372
    • Rosenblatt, J.1    Cramer, L.P.2    Baum, B.3    McGee, K.M.4
  • 34
    • 0033574449 scopus 로고    scopus 로고
    • Brefeldin A: The advantage of being uncompetitive
    • P. Chardin, and F. McCormick Brefeldin A: the advantage of being uncompetitive Cell 97 1999 153 155
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2
  • 35
    • 0347747970 scopus 로고    scopus 로고
    • A chemical genetic screen identifies inhibitors of regulated nuclear export of a Forkhead transcription factor in PTEN-deficient tumor cells
    • T.R. Kau, F. Schroeder, S. Ramaswamy, C.L. Wojciechowski, J.J. Zhao, T.M. Roberts, J. Clardy, W.R. Sellers, and P.A. Silver A chemical genetic screen identifies inhibitors of regulated nuclear export of a Forkhead transcription factor in PTEN-deficient tumor cells Cancer Cell 4 2003 463 476 An extensive screen for small molecules affecting the localization of FOXO1a identifies many inhibitors of nuclear export and PI3-kinase signaling, including molecules that implicate calmodulin as a novel regulator of FOX1Oa localization.
    • (2003) Cancer Cell , vol.4 , pp. 463-476
    • Kau, T.R.1    Schroeder, F.2    Ramaswamy, S.3    Wojciechowski, C.L.4    Zhao, J.J.5    Roberts, T.M.6    Clardy, J.7    Sellers, W.R.8    Silver, P.A.9
  • 37
    • 4344571004 scopus 로고    scopus 로고
    • Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells
    • Y. Feng, A.P. Jadhav, C. Rodighiero, Y. Fujinaga, T. Kirchhausen, and W.I. Lencer Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells EMBO Rep 5 2004 596 601 Exo2 is used as a tool to demonstrate that cholera toxin can be transported from the plasma membrane to the endoplasmic reticulum in the absence of a functional Golgi apparatus.
    • (2004) EMBO Rep , vol.5 , pp. 596-601
    • Feng, Y.1    Jadhav, A.P.2    Rodighiero, C.3    Fujinaga, Y.4    Kirchhausen, T.5    Lencer, W.I.6
  • 39
    • 3042552336 scopus 로고    scopus 로고
    • Sorting inhibitors (sortins): Chemical compounds to study vacuolar sorting in Arabidopsis
    • J. Zouhar, G.R. Hicks, and N.V. Raikhel Sorting inhibitors (sortins): chemical compounds to study vacuolar sorting in Arabidopsis Proc Natl Acad Sci USA 101 2004 9497 9501
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9497-9501
    • Zouhar, J.1    Hicks, G.R.2    Raikhel, N.V.3
  • 40
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • C.M. Pickart Back to the future with ubiquitin Cell 116 2004 181 190
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 41
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • A.F. Kisselev, and A.L. Goldberg Proteasome inhibitors: from research tools to drug candidates Chem Biol 8 2001 739 758
    • (2001) Chem Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 42
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • J. Adams The proteasome: a suitable antineoplastic target Nat Rev Cancer 4 2004 349 360
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 43
    • 6044271376 scopus 로고    scopus 로고
    • Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain
    • R. Verma, N.R. Peters, M. D'Onofrio, G.P. Tochtrop, K.M. Sakamoto, R. Varadan, M. Zhang, P. Coffino, D. Fushman, and R.J. Deshaies Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain Science 306 2004 117 120 This forward chemical genetic screen in Xenopus extracts identifies new inhibitors of cell cycle progression, including ubistatin, which binds specifically to lysine 48-linked ubiquitin chains, disrupting recognition and subsequent destruction by the proteasome.
    • (2004) Science , vol.306 , pp. 117-120
    • Verma, R.1    Peters, N.R.2    D'Onofrio, M.3    Tochtrop, G.P.4    Sakamoto, K.M.5    Varadan, R.6    Zhang, M.7    Coffino, P.8    Fushman, D.9    Deshaies, R.J.10
  • 45
    • 0035902475 scopus 로고    scopus 로고
    • Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F-box complex for ubiquitination and degradation
    • K.M. Sakamoto, K.B. Kim, A. Kumagai, F. Mercurio, C.M. Crews, and R.J. Deshaies Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F-box complex for ubiquitination and degradation Proc Natl Acad Sci USA 98 2001 8554 8559
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8554-8559
    • Sakamoto, K.M.1    Kim, K.B.2    Kumagai, A.3    Mercurio, F.4    Crews, C.M.5    Deshaies, R.J.6
  • 48


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