메뉴 건너뛰기




Volumn 47, Issue 1, 1999, Pages 18-37

New anti-actin drugs in the study of the organization and function of the actin cytoskeleton

Author keywords

Halichondramides; Jasplakinolide; Latrunculin; Misakinolide; Pectenotoxin II; Swinholide A

Indexed keywords

BINDING ENERGY; PROTEINS; STRUCTURAL PROPERTIES;

EID: 0032829103     PISSN: 1059910X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0029(19991001)47:1<18::AID-JEMT3>3.0.CO;2-E     Document Type: Article
Times cited : (295)

References (105)
  • 1
    • 0028139085 scopus 로고
    • Clostridial ADP-ribosylating toxins: Effects on ATP and GTP-binding proteins
    • Aktories K. 1994. Clostridial ADP-ribosylating toxins: effects on ATP and GTP-binding proteins. Mol Cell Biochem 138:167-176.
    • (1994) Mol Cell Biochem , vol.138 , pp. 167-176
    • Aktories, K.1
  • 2
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison DW, Gelfand VI, Spector I, Craig AM. 1998. Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J Neurosci 18:2423-2436.
    • (1998) J Neurosci , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 3
    • 0033540283 scopus 로고    scopus 로고
    • The Rho GTPases have multiple effects on the actin cytoskeleton
    • Aspenstrom P. 1999. The Rho GTPases have multiple effects on the actin cytoskeleton. Exp Cell Res 246:20-25.
    • (1999) Exp Cell Res , vol.246 , pp. 20-25
    • Aspenstrom, P.1
  • 4
    • 0031604152 scopus 로고    scopus 로고
    • Use of latrunculin A, an actin monomer-binding drug
    • Ayscough K. 1998. Use of latrunculin A, an actin monomer-binding drug. Methods Enzymol 298:18-25.
    • (1998) Methods Enzymol , vol.298 , pp. 18-25
    • Ayscough, K.1
  • 5
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough KR, Stryker J, Pokala N, Sanders M, Crews P, Drubin DG. 1997. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J Cell Biol 137:399-416.
    • (1997) J Cell Biol , vol.137 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 6
    • 0032005265 scopus 로고    scopus 로고
    • Myosins: Matching functions with motors
    • Baker JP, Titus MA. 1998. Myosins: matching functions with motors. Curr Opin Cell Biol 10:80-86.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 80-86
    • Baker, J.P.1    Titus, M.A.2
  • 8
    • 0028244490 scopus 로고
    • Assessment of a method of isolation, purification, and cultivation of rat liver sinusoidal endothelial cells
    • Braet F, De Zanger R, Sasaoki T, Baekeland M, Janssens P, Smedsrød B, Wisse E. 1994. Assessment of a method of isolation, purification, and cultivation of rat liver sinusoidal endothelial cells. Lab Invest 70:944-952.
    • (1994) Lab Invest , vol.70 , pp. 944-952
    • Braet, F.1    De Zanger, R.2    Sasaoki, T.3    Baekeland, M.4    Janssens, P.5    Smedsrød, B.6    Wisse, E.7
  • 9
    • 0028890767 scopus 로고
    • Structure and dynamics of the fenestrae-associated cytoskeleton of rat liver sinusoidal endothelial cells
    • Braet F, De Zanger R, Baekeland M, Crabbé E, Van Der Smissen P, Wisse E. 1995. Structure and dynamics of the fenestrae-associated cytoskeleton of rat liver sinusoidal endothelial cells. Hepatology 21:180-189.
    • (1995) Hepatology , vol.21 , pp. 180-189
    • Braet, F.1    De Zanger, R.2    Baekeland, M.3    Crabbé, E.4    Van Der Smissen, P.5    Wisse, E.6
  • 10
    • 0029795652 scopus 로고    scopus 로고
    • Microfilament-disrupting agent latrunculin A induces an increased number of fenestrae in rat liver sinusoidal endothelial cells: Comparison with cytochalasin B
    • Braet F, De Zanger R, Jans D, Spector I, Wisse E. 1996. Microfilament-disrupting agent latrunculin A induces an increased number of fenestrae in rat liver sinusoidal endothelial cells: comparison with cytochalasin B. Hepatology 24:627-635.
    • (1996) Hepatology , vol.24 , pp. 627-635
    • Braet, F.1    De Zanger, R.2    Jans, D.3    Spector, I.4    Wisse, E.5
  • 11
    • 0032506113 scopus 로고    scopus 로고
    • A novel structure involved in the formation of liver endothelial cell fenestrae revealed by using the actin inhibitor misakinolide
    • Braet F, Spector I, De Zanger R, Wisse E. 1998a. A novel structure involved in the formation of liver endothelial cell fenestrae revealed by using the actin inhibitor misakinolide. Proc Natl Acad Sci USA 95:13635-13640.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13635-13640
    • Braet, F.1    Spector, I.2    De Zanger, R.3    Wisse, E.4
  • 12
    • 0038450993 scopus 로고    scopus 로고
    • Comparison of fixed and living liver endothelial cells by atomic force microscopy
    • Braet F, Rotsch C, Wisse E, Radmacher M. 1998b. Comparison of fixed and living liver endothelial cells by atomic force microscopy. Appl Phys A66:S575-S578.
    • (1998) Appl Phys , vol.A66
    • Braet, F.1    Rotsch, C.2    Wisse, E.3    Radmacher, M.4
  • 13
    • 0004058896 scopus 로고
    • New York: Garland. 406 p.
    • Bray D. 1992. Cell movements. New York: Garland. 406 p.
    • (1992) Cell Movements
    • Bray, D.1
  • 14
    • 0033005168 scopus 로고    scopus 로고
    • Molecular mechanisms of nonmuscle myosin-II regulation
    • Bresnick AR. 1999. Molecular mechanisms of nonmuscle myosin-II regulation. Curr Opin Cell Biol 11:26-33.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 26-33
    • Bresnick, A.R.1
  • 15
    • 0028244823 scopus 로고
    • Jaspakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin
    • Bubb MR, Senderowicz AMJ, Sausville EA, Duncan KLK, Korn ED. 1994. Jaspakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J Biol Chem 269:14869-14871.
    • (1994) J Biol Chem , vol.269 , pp. 14869-14871
    • Bubb, M.R.1    Senderowicz, A.M.J.2    Sausville, E.A.3    Duncan, K.L.K.4    Korn, E.D.5
  • 16
    • 0031615933 scopus 로고    scopus 로고
    • Use of the F-actin binding drugs, misakinolide A and swinholide A
    • Bubb MR, Spector I. 1998. Use of the F-actin binding drugs, misakinolide A and swinholide A. Methods Enzymol 298:26-32.
    • (1998) Methods Enzymol , vol.298 , pp. 26-32
    • Bubb, M.R.1    Spector, I.2
  • 17
    • 0028967310 scopus 로고
    • Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments
    • Bubb MR, Spector I, Bershadsky AD, Korn ED. 1995. Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments. J Biol Chem 270:3463-3466.
    • (1995) J Biol Chem , vol.270 , pp. 3463-3466
    • Bubb, M.R.1    Spector, I.2    Bershadsky, A.D.3    Korn, E.D.4
  • 20
    • 0032006817 scopus 로고    scopus 로고
    • Control of actin dynamics
    • Carlier MF. 1998. Control of actin dynamics. Curr Opin Cell Biol 10:45-51.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 45-51
    • Carlier, M.F.1
  • 21
    • 0025685426 scopus 로고
    • Tolytoxin and new scytophycins from 3 species of scytonema
    • Carmeli S, Moore RE, Patterson GML. 1990. Tolytoxin and new scytophycins from 3 species of scytonema. J Nat Prod 53:1533-1542.
    • (1990) J Nat Prod , vol.53 , pp. 1533-1542
    • Carmeli, S.1    Moore, R.E.2    Patterson, G.M.L.3
  • 22
    • 0021920504 scopus 로고
    • The structure of swinholide-A, a new macrolide from the marine sponge Theonella swinhoei
    • Carmely S, Kashman Y. 1985. The structure of swinholide-A, a new macrolide from the marine sponge Theonella swinhoei. Tetrahedron Lett 26:511-514.
    • (1985) Tetrahedron Lett , vol.26 , pp. 511-514
    • Carmely, S.1    Kashman, Y.2
  • 23
    • 0023199134 scopus 로고
    • Stereostructures of geodiamolide-A and geodiamolide-B, novel cyclodepsipeptides from the marine sponge Geodia sp
    • Chan WR, Tinto WF, Manchand PS, Todaro LJ. 1987. Stereostructures of geodiamolide-A and geodiamolide-B, novel cyclodepsipeptides from the marine sponge Geodia sp. J Org Chem 52:3091-3093.
    • (1987) J Org Chem , vol.52 , pp. 3091-3093
    • Chan, W.R.1    Tinto, W.F.2    Manchand, P.S.3    Todaro, L.J.4
  • 24
    • 0027333420 scopus 로고
    • Life at the leading edge: The formation of cell protrusions
    • Condeelis J. 1993. Life at the leading edge: the formation of cell protrusions. Annu Rev Cell Biol 9:411-444.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 25
    • 0023427610 scopus 로고
    • Effects of cytochalasins and phalloidin on actin
    • Cooper JA. 1987. Effects of cytochalasins and phalloidin on actin. J Cell Biol 105:1473-1478.
    • (1987) J Cell Biol , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 26
    • 0025982039 scopus 로고
    • The role of actin polymerization in cell motility
    • Cooper JA. 1991. The role of actin polymerization in cell motility. Annu Rev Physiol 53:585-605.
    • (1991) Annu Rev Physiol , vol.53 , pp. 585-605
    • Cooper, J.A.1
  • 27
    • 0030067021 scopus 로고    scopus 로고
    • Assembly of focal adhesions: Progress, paradigms, and portents
    • Craig SW, Johnson RP. 1996. Assembly of focal adhesions: progress, paradigms, and portents. Curr Opin Cell Biol 8:74-85.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 74-85
    • Craig, S.W.1    Johnson, R.P.2
  • 29
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coué M, Brenner SL, Spector I, Korn E. 1987. Inhibition of actin polymerization by latrunculin A. FEBS Lett 213:316-318.
    • (1987) FEBS Lett , vol.213 , pp. 316-318
    • Coué, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.4
  • 30
    • 4243562790 scopus 로고
    • Jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis sp
    • Crews P, Manes LV, Boehler M. 1986. Jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis sp. Tetrahedron Lett 27:2797-2800.
    • (1986) Tetrahedron Lett , vol.27 , pp. 2797-2800
    • Crews, P.1    Manes, L.V.2    Boehler, M.3
  • 31
    • 0027217080 scopus 로고
    • Three new potent cytotoxic macrolides closely related to Sphinxolide from the New Caledonian sponge Neosiphonia superstes
    • D'auria MV, Paloma LG, Minale L, Zampella A, Verbist JF, Roussakis C, Debitus C. 1993. Three new potent cytotoxic macrolides closely related to Sphinxolide from the New Caledonian sponge Neosiphonia superstes. Tetrahedron 49:8657-8664.
    • (1993) Tetrahedron , vol.49 , pp. 8657-8664
    • D'auria, M.V.1    Paloma, L.G.2    Minale, L.3    Zampella, A.4    Verbist, J.F.5    Roussakis, C.6    Debitus, C.7
  • 32
    • 0025105061 scopus 로고
    • Geodiamolides C to F, new cytotoxic cyclodepsipeptides from the marine sponge Pseudaxinyssa sp
    • deSilva ED, Andersen RJ, Allen TM. 1990. Geodiamolides C to F, new cytotoxic cyclodepsipeptides from the marine sponge Pseudaxinyssa sp. Tetrahedron Lett 31:489-492.
    • (1990) Tetrahedron Lett , vol.31 , pp. 489-492
    • DeSilva, E.D.1    Andersen, R.J.2    Allen, T.M.3
  • 33
    • 0030802568 scopus 로고    scopus 로고
    • The structure, function, and assembly of actin filament bundles
    • Furukawa R, Fechheimer M. 1997. The structure, function, and assembly of actin filament bundles. Int Rev Cytol 175:29-90.
    • (1997) Int Rev Cytol , vol.175 , pp. 29-90
    • Furukawa, R.1    Fechheimer, M.2
  • 34
    • 0024378138 scopus 로고
    • Mycalolides-A-C, hybrid macrolides of Ulapualides and Halichondramide, from a sponge of the genus Mycale
    • Fusetani N, Yasumuro K, Matsunaga S, Hashimoto K. 1989. Mycalolides-A-C, hybrid macrolides of Ulapualides and Halichondramide, from a sponge of the genus Mycale. Tetrahedron Lett 30:2809-2812.
    • (1989) Tetrahedron Lett , vol.30 , pp. 2809-2812
    • Fusetani, N.1    Yasumuro, K.2    Matsunaga, S.3    Hashimoto, K.4
  • 35
    • 0026691647 scopus 로고
    • Isolation of latrunculin-A, 6,7-epoxylatrunculin-A, fijianolide-A, and euryfuran from a new genus of the family Thorectidae
    • Gulavita NK, Gunasekera SP, Pomponi SA. 1992. Isolation of latrunculin-A, 6,7-epoxylatrunculin-A, fijianolide-A, and euryfuran from a new genus of the family Thorectidae. J Nat Prod 55:506-508.
    • (1992) J Nat Prod , vol.55 , pp. 506-508
    • Gulavita, N.K.1    Gunasekera, S.P.2    Pomponi, S.A.3
  • 36
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM. 1996. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84:345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 37
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 38
    • 0031081425 scopus 로고    scopus 로고
    • Signaling through focal adhesion kinase
    • Hanks SK, Polte TR. 1997. Signaling through focal adhesion kinase. Bioessays 19:137-145.
    • (1997) Bioessays , vol.19 , pp. 137-145
    • Hanks, S.K.1    Polte, T.R.2
  • 39
    • 0028674557 scopus 로고
    • Actin-binding proteins in cell motility
    • Hatano S. 1994. Actin-binding proteins in cell motility. Int Rev Cytol 156:199-273.
    • (1994) Int Rev Cytol , vol.156 , pp. 199-273
    • Hatano, S.1
  • 40
    • 0031042322 scopus 로고    scopus 로고
    • Actin and cell pathogenesis
    • Higley S, Way M. 1997. Actin and cell pathogenesis. Curr Opin Cell Biol 9:62-69.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 62-69
    • Higley, S.1    Way, M.2
  • 41
    • 0032054275 scopus 로고    scopus 로고
    • Interaction of invasive bacteria with host signaling pathways
    • Ireton K, Cossart P. 1998. Interaction of invasive bacteria with host signaling pathways, Curr Opin Cell Biol 10:276-283.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 276-283
    • Ireton, K.1    Cossart, P.2
  • 42
    • 0022871254 scopus 로고
    • Scytophycins, cytotoxic and antimycotic agents from the Cyanophyte Scytonema-Pseudohofmanni
    • Ishibashi M, Moore RE, Patterson GML, Xu CF, Clardy J. 1986. Scytophycins, cytotoxic and antimycotic agents from the Cyanophyte Scytonema-Pseudohofmanni. J Org Chem 51:5300-5306.
    • (1986) J Org Chem , vol.51 , pp. 5300-5306
    • Ishibashi, M.1    Moore, R.E.2    Patterson, G.M.L.3    Xu, C.F.4    Clardy, J.5
  • 43
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signaling: Component localization and mechanical coupling
    • Janmey PA. 1998. The cytoskeleton and cell signaling: component localization and mechanical coupling. Physiol Rev 78:763-781.
    • (1998) Physiol Rev , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 44
    • 0028899770 scopus 로고
    • Medical aspects of the actin cytoskeleton
    • Janmey PA, Chaponnier C. 1995. Medical aspects of the actin cytoskeleton. Curr Opin Cell Biol 7:111-117.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 111-117
    • Janmey, P.A.1    Chaponnier, C.2
  • 45
    • 0030068561 scopus 로고    scopus 로고
    • Structures and absolute configurations of the marine toxins, latrunculin A and laulimalide
    • Jefford CW, Bernardinelli G, Tanaka J, Higa T. 1996. Structures and absolute configurations of the marine toxins, latrunculin A and laulimalide. Tetrahedron Lett 37:159-162.
    • (1996) Tetrahedron Lett , vol.37 , pp. 159-162
    • Jefford, C.W.1    Bernardinelli, G.2    Tanaka, J.3    Higa, T.4
  • 46
    • 0028044834 scopus 로고
    • Signal transduction by integrins and its role in the regulation of tumor growth
    • Juliano R. 1994. Signal transduction by integrins and its role in the regulation of tumor growth. Cancer Metastasis Rev 13:25-30.
    • (1994) Cancer Metastasis Rev , vol.13 , pp. 25-30
    • Juliano, R.1
  • 47
    • 0023181048 scopus 로고
    • Dendrolasin and latrunculin A from the Fijian sponge Spongia-mycofijiensis and an associated nudibranch chromodoris-lochi
    • Kakou Y, Crews P, Bakus GJ. 1987. Dendrolasin and latrunculin A from the Fijian sponge Spongia-mycofijiensis and an associated nudibranch chromodoris-lochi. J Nat Prod 50:482-484.
    • (1987) J Nat Prod , vol.50 , pp. 482-484
    • Kakou, Y.1    Crews, P.2    Bakus, G.J.3
  • 48
    • 23744475536 scopus 로고
    • Latrunculin, a new 2-thiazolidinone macrolide from the marine sponge Latrunculia magnifica
    • Kashman Y, Groweiss A, Shmueli U. 1980. Latrunculin, a new 2-thiazolidinone macrolide from the marine sponge Latrunculia magnifica. Tetrahedron Lett 21:3629-3632.
    • (1980) Tetrahedron Lett , vol.21 , pp. 3629-3632
    • Kashman, Y.1    Groweiss, A.2    Shmueli, U.3
  • 49
    • 0023490475 scopus 로고
    • Antitumor macrodiolides isolated from a marine sponge Theonella sp: Structure revision of misakinolide A
    • Kato Y, Fusetani N, Matsunaga S, Hasimoto K, Sakai R, Higa T, Kashman Y. 1987. Antitumor macrodiolides isolated from a marine sponge Theonella sp: structure revision of misakinolide A. Tetrahedron Lett 28:6225-6228.
    • (1987) Tetrahedron Lett , vol.28 , pp. 6225-6228
    • Kato, Y.1    Fusetani, N.2    Matsunaga, S.3    Hasimoto, K.4    Sakai, R.5    Higa, T.6    Kashman, Y.7
  • 50
    • 0023275574 scopus 로고
    • Halichondramide, an antifungal macrolide from the sponge Halichondria sp
    • Kernan MR, Faulkner DJ. 1987. Halichondramide, an antifungal macrolide from the sponge Halichondria sp. Tetrahedron Lett 28:2809-2812.
    • (1987) Tetrahedron Lett , vol.28 , pp. 2809-2812
    • Kernan, M.R.1    Faulkner, D.J.2
  • 51
    • 0023751922 scopus 로고
    • Macrocyclic antifungal metabolites from the spanish dancer nudibranch Hexabranchus-sanguineus and sponges of the genus Halichondria
    • Kernan MR, Molinski TF, Faulkner DJ. 1988. Macrocyclic antifungal metabolites from the spanish dancer nudibranch Hexabranchus-sanguineus and sponges of the genus Halichondria. J Org Chem 53:5014-5020.
    • (1988) J Org Chem , vol.53 , pp. 5014-5020
    • Kernan, M.R.1    Molinski, T.F.2    Faulkner, D.J.3
  • 52
    • 0025179912 scopus 로고
    • Absolute stereostructure of swinholide A, a potent cytotoxic macrolide, from the Okinawan marine sponge Theonella swinhoei
    • Kitagawa I, Kobayashi M, Katori T, Yamashita M. 1990. Absolute stereostructure of swinholide A, a potent cytotoxic macrolide, from the Okinawan marine sponge Theonella swinhoei. J Am Chem Soc 112:3710-3712.
    • (1990) J Am Chem Soc , vol.112 , pp. 3710-3712
    • Kitagawa, I.1    Kobayashi, M.2    Katori, T.3    Yamashita, M.4
  • 53
    • 0027976864 scopus 로고
    • Marine natural products. XXXI. Structure-activity correlation of a potent cytotoxic dimeric macrolide swinholide A, from the Okinawan marine sponge Theonella swinhoei, and its isomers
    • Kobayashi M, Kawazoe K, Okamoto T, Sasaki T, Kitagawa I. 1994. Marine natural products. XXXI. Structure-activity correlation of a potent cytotoxic dimeric macrolide swinholide A, from the Okinawan marine sponge Theonella swinhoei, and its isomers. Chem Pharm Bull 42:19-26.
    • (1994) Chem Pharm Bull , vol.42 , pp. 19-26
    • Kobayashi, M.1    Kawazoe, K.2    Okamoto, T.3    Sasaki, T.4    Kitagawa, I.5
  • 54
    • 0025037109 scopus 로고
    • Marine natural products. XXII. The absolute structure of swinholide A, a potent cytotoxic dimeric macrolides from the Okinawan marine sponge Theonella swinhoei
    • Kobayashi M, Tanaka J-I, Katori T, Matsuura M, Yamashita M, Kitagawa I. 1990a. Marine natural products. XXII. The absolute structure of swinholide A, a potent cytotoxic dimeric macrolides from the Okinawan marine sponge Theonella swinhoei. Chem Pharm Bull 38:2409-2418.
    • (1990) Chem Pharm Bull , vol.38 , pp. 2409-2418
    • Kobayashi, M.1    Tanaka, J.-I.2    Katori, T.3    Matsuura, M.4    Yamashita, M.5    Kitagawa, I.6
  • 55
    • 0025674098 scopus 로고
    • Marine natural products. XXIII. Three new cytotoxic dimeric macrolides, swinholide B and C, and isoswinholide A, congeners of swinholide A, from the Okinawan marine sponge Theonella swinhoei
    • Kobayashi M, Tanaka J-I, Katori T, Kitagawa I. 1990b. Marine natural products. XXIII. Three new cytotoxic dimeric macrolides, swinholide B and C, and isoswinholide A, congeners of swinholide A, from the Okinawan marine sponge Theonella swinhoei. Chem Pharm Bull 38:2960-2966.
    • (1990) Chem Pharm Bull , vol.38 , pp. 2960-2966
    • Kobayashi, M.1    Tanaka, J.-I.2    Katori, T.3    Kitagawa, I.4
  • 56
    • 37049066945 scopus 로고
    • New congeners of bistheonellides from Okinawan marine sponges of the genus Theonella
    • Kobayashi J, Tsukamoto S, Tanabe A, Sasaki T, Ishibashi M. 1991. New congeners of bistheonellides from Okinawan marine sponges of the genus Theonella. J Chem Soc-Perkin Trans 1(10):2379-2383.
    • (1991) J Chem Soc-Perkin Trans , vol.1 , Issue.10 , pp. 2379-2383
    • Kobayashi, J.1    Tsukamoto, S.2    Tanabe, A.3    Sasaki, T.4    Ishibashi, M.5
  • 57
    • 0026569069 scopus 로고
    • The extracellular actin-scavenger system and actin toxicity
    • Lee WM, Galbraith RM. 1992. The extracellular actin-scavenger system and actin toxicity. N Engl J Med 326:1335-1341.
    • (1992) N Engl J Med , vol.326 , pp. 1335-1341
    • Lee, W.M.1    Galbraith, R.M.2
  • 58
    • 0024507924 scopus 로고
    • Further kabiramides and halichondramides, cytotoxic macrolides embracing trisoxazole from the Hexabranchus egg masses
    • Matsunaga S, Fusetani N, Hashimoto K, Keseki K, Noma M, Noguchi H, Sankawa U. 1989. Further kabiramides and halichondramides, cytotoxic macrolides embracing trisoxazole from the Hexabranchus egg masses. J Org Chem 54:1360-1363.
    • (1989) J Org Chem , vol.54 , pp. 1360-1363
    • Matsunaga, S.1    Fusetani, N.2    Hashimoto, K.3    Keseki, K.4    Noma, M.5    Noguchi, H.6    Sankawa, U.7
  • 59
    • 0032054640 scopus 로고    scopus 로고
    • F-actin-binding proteins
    • McGough A. 1998. F-actin-binding proteins. Curr Opin Struct Biol 8:166-176.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 166-176
    • McGough, A.1
  • 60
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V, Post PL, Mooseker MS. 1998. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 279:527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 61
    • 0019468104 scopus 로고
    • Membrane-associated cytoskeleton and coated vesicles in cultured hepatocytes visualized by dry-cleaving
    • Mesland DAM, Spiele H, Roos E. 1981. Membrane-associated cytoskeleton and coated vesicles in cultured hepatocytes visualized by dry-cleaving. Exp Cell Res 132:169-184.
    • (1981) Exp Cell Res , vol.132 , pp. 169-184
    • Mesland, D.A.M.1    Spiele, H.2    Roos, E.3
  • 62
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison TJ, Cramer LP. 1996. Actin-based cell motility and cell locomotion. Cell 84:371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 64
    • 0030462623 scopus 로고    scopus 로고
    • The chemical mechanism of myosin-I: Implications for actin-based motility and the evolution of the myosin family of motor proteins
    • Pollard TD, Ostap EM. 1996. The chemical mechanism of myosin-I: implications for actin-based motility and the evolution of the myosin family of motor proteins. Cell Struct Funct 21:351-356.
    • (1996) Cell Struct Funct , vol.21 , pp. 351-356
    • Pollard, T.D.1    Ostap, E.M.2
  • 67
    • 0026917533 scopus 로고
    • From molecules to cells: Imaging soft samples with the atomic force microscope
    • Radmacher M, Tillman RW, Fritz M, Gaub HE. 1992. From molecules to cells: imaging soft samples with the atomic force microscope. Science 257:1900-1905.
    • (1992) Science , vol.257 , pp. 1900-1905
    • Radmacher, M.1    Tillman, R.W.2    Fritz, M.3    Gaub, H.E.4
  • 68
    • 0026530460 scopus 로고
    • Cytochalasins induce actin polymerization in human leukocytes
    • Rao KM, Padmanabhan J, Cohen HJ. 1992. Cytochalasins induce actin polymerization in human leukocytes, Cell Motil Cytoskeleton 21:58-64.
    • (1992) Cell Motil Cytoskeleton , vol.21 , pp. 58-64
    • Rao, K.M.1    Padmanabhan, J.2    Cohen, H.J.3
  • 69
    • 0022578987 scopus 로고
    • Ulapualide-A and ulapualide-B, extraordinary antitumor macrolides from nudibranch egg masses
    • Roesener JA, Scheuer PJ. 1986. Ulapualide-A and ulapualide-B, extraordinary antitumor macrolides from nudibranch egg masses. J Am Chem Soc 108:846-847.
    • (1986) J Am Chem Soc , vol.108 , pp. 846-847
    • Roesener, J.A.1    Scheuer, P.J.2
  • 72
    • 0006244338 scopus 로고
    • Misakinolide-A, an antitumor macrolide from the marine sponge Theonella sp
    • Sakai R, Riga T, Kashman Y. 1986. Misakinolide-A, an antitumor macrolide from the marine sponge Theonella sp. Chem Lett 9:1499-1502.
    • (1986) Chem Lett , vol.9 , pp. 1499-1502
    • Sakai, R.1    Riga, T.2    Kashman, Y.3
  • 73
    • 0025731586 scopus 로고
    • Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments
    • Sampath P, Pollard TD. 1991. Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments. Biochemistry 30:1973-1980.
    • (1991) Biochemistry , vol.30 , pp. 1973-1980
    • Sampath, P.1    Pollard, T.D.2
  • 74
    • 0032556187 scopus 로고    scopus 로고
    • The chondramides: Cytostatic agents from myxobacteria acting on the actin cytoskeleton
    • Sasse F, Kunze B, Gronewold TM, Reichenbach H. 1998. The chondramides: cytostatic agents from myxobacteria acting on the actin cytoskeleton. J Natl Cancer Inst 90:1559-1563.
    • (1998) J Natl Cancer Inst , vol.90 , pp. 1559-1563
    • Sasse, F.1    Kunze, B.2    Gronewold, T.M.3    Reichenbach, H.4
  • 76
    • 0020361502 scopus 로고
    • Preferential distribution of anionic sites on the basement membrane and the albuminal aspect of the endothelium in fenestrated capillaries
    • Simionescu M, Simionescu N, Palade GE. 1982. Preferential distribution of anionic sites on the basement membrane and the albuminal aspect of the endothelium in fenestrated capillaries. J Cell Biol 95:425-434.
    • (1982) J Cell Biol , vol.95 , pp. 425-434
    • Simionescu, M.1    Simionescu, N.2    Palade, G.E.3
  • 77
    • 0021063738 scopus 로고
    • Rings of membrane sterols surround the openings of vesicles and fenestrae, in capillary endothelium
    • Simionescu N, Lupu F, Simionescu M. 1983. Rings of membrane sterols surround the openings of vesicles and fenestrae, in capillary endothelium. J Cell Biol 97:1592-1600.
    • (1983) J Cell Biol , vol.97 , pp. 1592-1600
    • Simionescu, N.1    Lupu, F.2    Simionescu, M.3
  • 78
    • 0029972233 scopus 로고    scopus 로고
    • Actin and the coordination of protrusion, attachment and retraction in cell crawling
    • Small JV, Anderson K, Rottner K. 1996. Actin and the coordination of protrusion, attachment and retraction in cell crawling. Biosci Rep 16:351-368.
    • (1996) Biosci Rep , vol.16 , pp. 351-368
    • Small, J.V.1    Anderson, K.2    Rottner, K.3
  • 79
    • 0032537991 scopus 로고    scopus 로고
    • Assembling an actin cytoskeleton for cell attachment and movement
    • Small JV, Rottner K, Kaverina I, Andersen KI. 1998. Assembling an actin cytoskeleton for cell attachment and movement. BBA-Mol Cell Res 1404:271-281.
    • (1998) BBA-Mol Cell Res , vol.1404 , pp. 271-281
    • Small, J.V.1    Rottner, K.2    Kaverina, I.3    Andersen, K.I.4
  • 81
    • 0020698663 scopus 로고
    • Latrunculins: Novel marine toxins that disrupt microfilament organization in cultured cells
    • Specter I, Shochet NR, Kashman Y, Groweiss A. 1983. Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells. Science 214:493-495.
    • (1983) Science , vol.214 , pp. 493-495
    • Specter, I.1    Shochet, N.R.2    Kashman, Y.3    Groweiss, A.4
  • 82
    • 0024360298 scopus 로고
    • Latrunculins - Novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D
    • Spector I, Shochet NR, Blasberger D, Kashman Y. 1989. Latrunculins - novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D. Cell Motil Cytoskeleton 13:127-144.
    • (1989) Cell Motil Cytoskeleton , vol.13 , pp. 127-144
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 83
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel TP. 1993. On the crawling of animal cells. Science 260:1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 84
    • 0028503567 scopus 로고
    • The machinery of cell crawling
    • Stossel TP. 1994. The machinery of cell crawling. Sci Am 271:54-63.
    • (1994) Sci Am , vol.271 , pp. 54-63
    • Stossel, T.P.1
  • 85
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M, Derry JM, Karlak B, Jiang S, Lemahieu V, Mccormick F, Francke U, Abo A. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 86
    • 0030605887 scopus 로고    scopus 로고
    • Zampanolide, a new cytotoxic macrolide from a marine sponge
    • Tanaka J, Higa T. 1996. Zampanolide, a new cytotoxic macrolide from a marine sponge. Tetrahedron Lett 37:5535-5538.
    • (1996) Tetrahedron Lett , vol.37 , pp. 5535-5538
    • Tanaka, J.1    Higa, T.2
  • 87
    • 0025689054 scopus 로고
    • Marine natural-products. 24. The absolute stereostructure of misakinolide-A, a potent cytotoxic dimeric macrolide from an Okinawan marine sponge Theonella sp
    • Tanaka J, Higa T, Kobayashi M, Kitagawa I. 1990. Marine natural-products. 24. The absolute stereostructure of misakinolide-A, a potent cytotoxic dimeric macrolide from an Okinawan marine sponge Theonella sp. Chem Pharm Bull 38:2967-2970.
    • (1990) Chem Pharm Bull , vol.38 , pp. 2967-2970
    • Tanaka, J.1    Higa, T.2    Kobayashi, M.3    Kitagawa, I.4
  • 88
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon N, Hall A. 1997. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol 9:86-92.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 89
    • 0022972488 scopus 로고
    • Histopathological studies on experimental marine toxin poisoning. 1. Ultrastructural-changes in the small-intestine and liver of suckling mice induced by dinophy-sistoxin-1 and pectenotoxin-1
    • Terao K, Ito E, Yanagi T, Yasumoto T. 1986. Histopathological studies on experimental marine toxin poisoning. 1. Ultrastructural-changes in the small-intestine and liver of suckling mice induced by dinophy-sistoxin-1 and pectenotoxin-1. Toxicon 24:1141-1151.
    • (1986) Toxicon , vol.24 , pp. 1141-1151
    • Terao, K.1    Ito, E.2    Yanagi, T.3    Yasumoto, T.4
  • 90
    • 0031004871 scopus 로고    scopus 로고
    • Misakinolide A is a marine macrolide that caps but does not sever filamentous actin
    • Terry DR, Specter I, Higa T, Bubb MR. 1997. Misakinolide A is a marine macrolide that caps but does not sever filamentous actin. J Biol Chem 272:7841-7845.
    • (1997) J Biol Chem , vol.272 , pp. 7841-7845
    • Terry, D.R.1    Specter, I.2    Higa, T.3    Bubb, M.R.4
  • 91
    • 0028065195 scopus 로고
    • Actin filament dynamics in cell motility
    • Theriot JA. 1994. Actin filament dynamics in cell motility. Adv Exp Med Biol 358:133-145.
    • (1994) Adv Exp Med Biol , vol.358 , pp. 133-145
    • Theriot, J.A.1
  • 92
    • 0026569575 scopus 로고
    • The isolation of monomeric carboxylic acid of swinholide A from the Indo-Pacific sponge, Theonella swinhei
    • Todd JS, Alvi KA, Crews P. 1992. The isolation of monomeric carboxylic acid of swinholide A from the Indo-Pacific sponge, Theonella swinhei. Tetrahedron Lett 33:441-442.
    • (1992) Tetrahedron Lett , vol.33 , pp. 441-442
    • Todd, J.S.1    Alvi, K.A.2    Crews, P.3
  • 93
    • 37049073169 scopus 로고
    • New congeners of swinholides from the Okinawan marine sponge Theonella sp
    • Tsukamoto S, Ishibashi M, Sasaki T, Kobayashi J. 1991. New congeners of swinholides from the Okinawan marine sponge Theonella sp. J Chem Soc Perkin Trans 1(12):3185-3188.
    • (1991) J Chem Soc Perkin Trans , vol.1 , Issue.12 , pp. 3185-3188
    • Tsukamoto, S.1    Ishibashi, M.2    Sasaki, T.3    Kobayashi, J.4
  • 94
    • 0032910692 scopus 로고    scopus 로고
    • Structural modules in actin-binding proteins: Towards a new classification
    • Van Troys M, Vandekerckhove J, Ampe C. 1999. Structural modules in actin-binding proteins: towards a new classification. Biochim Biophys Acta 1448:323-348.
    • (1999) Biochim Biophys Acta , vol.1448 , pp. 323-348
    • Van Troys, M.1    Vandekerckhove, J.2    Ampe, C.3
  • 95
    • 0018869639 scopus 로고
    • Phalloidin associates with microfilaments after microinjection into tissue culture cells
    • Wehland J, Osborn M, Weber K. 1980. Phalloidin associates with microfilaments after microinjection into tissue culture cells. Eur J Cell Biol 21:188-194.
    • (1980) Eur J Cell Biol , vol.21 , pp. 188-194
    • Wehland, J.1    Osborn, M.2    Weber, K.3
  • 97
    • 0025940658 scopus 로고
    • Actin polymerization in murine B lymphocytes is stimulated by cytochalasin D but not by anti-immunoglobulin
    • Wilder JA, Ashman RF. 1991. Actin polymerization in murine B lymphocytes is stimulated by cytochalasin D but not by anti-immunoglobulin, Cell Immunol 137:514-528.
    • (1991) Cell Immunol , vol.137 , pp. 514-528
    • Wilder, J.A.1    Ashman, R.F.2
  • 98
    • 0027024609 scopus 로고
    • Comparative study on the effects of cytochalasins B and D on F-actin content in different cell lines and different culture conditions
    • Wodnicka M, Pierzchalska M, Bereiter-Hahn J, Kajstura J. 1992. Comparative study on the effects of cytochalasins B and D on F-actin content in different cell lines and different culture conditions. Folia Histochem Cytobiol 30:107-112.
    • (1992) Folia Histochem Cytobiol , vol.30 , pp. 107-112
    • Wodnicka, M.1    Pierzchalska, M.2    Bereiter-Hahn, J.3    Kajstura, J.4
  • 99
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada KM, Geiger B. 1997. Molecular interactions in cell adhesion complexes. Curr Opin Cell Biol 9:76-85.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 100
    • 0027763552 scopus 로고
    • Aplyronine-A, a potent antitumor substance, and the congeners aplyronine-B and aplyronine-C isolated from the sea hare Aplysia-Kurodai
    • Yamada K, Ojika M, Ishigaki T, Yoshida Y, Ekimoto H, Arakawa M. 1993. Aplyronine-A, a potent antitumor substance, and the congeners aplyronine-B and aplyronine-C isolated from the sea hare Aplysia-Kurodai. J Am Chem Soc 115:11020-11021.
    • (1993) J Am Chem Soc , vol.115 , pp. 11020-11021
    • Yamada, K.1    Ojika, M.2    Ishigaki, T.3    Yoshida, Y.4    Ekimoto, H.5    Arakawa, M.6
  • 101
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • Yap AS, Brieher WM, Gumbiner BM. 1997. Molecular and functional analysis of cadherin-based adherens junctions. Annu Rev Cell Dev Biol 13:119-146.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 119-146
    • Yap, A.S.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 104
    • 0033058149 scopus 로고    scopus 로고
    • New jaspamide derivatives from the marine sponge Jaspis splendans collected in Vanuatu
    • Zampella A, Giannini C, Debitus C, Roussakis C, D'Auria MV. 1999. New jaspamide derivatives from the marine sponge Jaspis splendans collected in Vanuatu. J Nat Prod 62:332-334.
    • (1999) J Nat Prod , vol.62 , pp. 332-334
    • Zampella, A.1    Giannini, C.2    Debitus, C.3    Roussakis, C.4    D'Auria, M.V.5
  • 105
    • 0030777109 scopus 로고    scopus 로고
    • Microfilament depletion and circumvention of multiple drug resistance by sphinxolides
    • Zhang X, Minale L, Zampella A, Smith CD. 1997. Microfilament depletion and circumvention of multiple drug resistance by sphinxolides. Cancer Res 57:3751-3758.
    • (1997) Cancer Res , vol.57 , pp. 3751-3758
    • Zhang, X.1    Minale, L.2    Zampella, A.3    Smith, C.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.