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Latrunculins: Novel Marine Toxins That Disrupt Microfilament Organization in Cultured Cells
Abstract
Two toxins, latrunculins A and B, which contain a new class of 16- and 14-membered marine macrolides attached to the rare 2-thiazolidinone moiety, were purified recently from the Red Sea sponge Latrunculia magnifica. The effects of these toxins on cultured mouse neuroblastoma and fibroblast cells have been evaluated. In both types of cells, submicromolar toxin concentrations rapidly induce striking changes in cell morphology that are reversible upon removal of the toxin. Immunofluorescence studies with antibodies specific for cytoskeletal proteins reveal that the toxins cause major alterations in the organization of microfilaments without obvious effects on the organization of the microtubular system.
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“When neurons are treated with Latrunculin A, which sequesters monomeric actin (G-actin) and perturbs F-actin formation12,13, ultrafast endocytosis fails completely, with no induction of membrane pit formation5.”
From Membrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis (2023) · cites this paper as [13]
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Cites
Mechanism of action of cytochalasin B on actin
MacLean-Fletcher, S. (1980) · Cell · doi:10.1016/0092-8674(80)90619-4 · Cited by 755
Clarke, M., & Spudich, J. A. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.004053 · Cited by 504
Actin-binding proteins—regulators of cell architecture and motility
Weeds, A. G. (1982) · Nature · doi:10.1038/296811a0 · Cited by 467
Cytoplasmic fibrils in living cultured cells
Buckley, I. K., & Porter, K. R. (1967) · PROTOPLASMA · doi:10.1007/bf01666538 · Cited by 354
Yahara, I., Harada, F., Sekita, S., Yoshihira, K., & Natori, S. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.92.1.69 · Cited by 321
Cytochalasin inhibits the rate of elongation of actin filament fragments
Brown, S. S., & Spudich, J. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.83.3.657 · Cited by 297
Brenner, S. L., & Korn, E. D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86660-7 · Cited by 266
Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.
Brown, S. S., & Spudich, J. A. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.88.3.487 · Cited by 262
Cytochalasin B and the structure of actin gels
Hartwig, J. H., & Stossel, T. P. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90366-8 · Cited by 236
The distribution of actin in non-muscle cells
Goldman, R. D., Lazarides, E., Pollack, R., & Weber, K. (1975) · Experimental Cell Research · doi:10.1016/0014-4827(75)90323-7 · Cited by 221
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Research works printed but not linked: 1
- Marchisio, P. C., Tissue Culture in Neurobiology: 99 (1980).
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Items 301–400 of 746
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Charalambous, C., Gsandtner, I., Keuerleber, S., Milan‐Lobo, L., Kudlacek, O., Freissmuth, M., & Zezula, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706275200 · Cited by 43
Reggiori, F., & Klionsky, D. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03047 · Cited by 42
Terashita, Y., Wakayama, S., Yamagata, K., Li, C., Sato, E., & Wakayama, T. (2012) · Biology of Reproduction · doi:10.1095/biolreprod.111.098764 · Cited by 57
Riemann, M., Büche, C., Kassemeyer, H., & Nick, P. (2002) · PROTOPLASMA · doi:10.1007/s007090200001 · Cited by 42
Role of the actin cytoskeleton during respiratory burst in chemoattractant‐stimulated neutrophils
Bengtsson, T., Orselius, K., & Wetterö, J. (2006) · Cell Biology International · doi:10.1016/j.cellbi.2005.10.017 · Cited by 42
Annexin A1 regulates hormone exocytosis through a mechanism involving actin reorganization
McArthur, S., Yazid, S., Christian, H., Sirha, R., Flower, R. J., Buckingham, J. C., & Solito, E. (2009) · The FASEB Journal · doi:10.1096/fj.09-131391 · Cited by 42
Oren, A., Herschkovitz, A., Ben‐Dror, I., Holdengreber, V., Ben‐Shaul, Y., Seger, R., & Vardimon, L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1742 · Cited by 42
Marine Pharmacology: Bioactive Molecules from the Sea
Kaul, P. N., & Daftari, P. (1986) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.26.040186.001001 · Cited by 41
An Antiprion Effect of the Anticytoskeletal Drug Latrunculin A in Yeast
Bailleul-Winslett, P. A., Newnam, G. P., Wegrzyn, R. D., & Chernoff, Y. O. (2001) · Gene Expression · doi:10.3727/000000001783992650 · Cited by 42
Rogge, H., Artelt, N., Endlich, N., & Endlich, K. (2017) · Journal of Microscopy · doi:10.1111/jmi.12593 · Cited by 40
Chlamydia exploits filopodial capture and a macropinocytosis-like pathway for host cell entry
Ford, C., Nans, A., Boucrot, E., & Hayward, R. D. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007051 · Cited by 41
Conserved actin machinery drives microtubule-independent motility and phagocytosis in Naegleria
Velle, K., & Fritz‐Laylin, L. K. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202007158 · Cited by 41
β-Adrenergic control of sarcolemmal Ca V 1.2 abundance by small GTPase Rab proteins
del Villar, S. G., Voelker, T. L., Westhoff, M., Reddy, G. R., Spooner, H. C., Navedo, M. F., Dickson, E. J., & Dixon, R. E. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017937118 · Cited by 47
Marine natural products as inhibitors of hypoxic signaling in tumors
Nagle, D. G., & Zhou, Y. (2009) · Phytochemistry Reviews · doi:10.1007/s11101-009-9120-1 · Cited by 41
Amagata, T., Johnson, T. A., Cichewicz, R. H., Tenney, K., Mooberry, S. L., Media, J. E., Edelstein, M., Valeriote, F. A., & Crews, P. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8008585 · Cited by 41
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Prinsep, M. R. (2003) · Studies in natural products chemistry · doi:10.1016/s1572-5995(03)80151-5 · Cited by 40
Zirngibl, M., Fürnrohr, B. G., Janko, C., Munoz, L. E., Voll, R. E., Gregory, C. D., Schett, G. A., & i, M. H. (2014) · Clinical & Experimental Immunology · doi:10.1111/cei.12342 · Cited by 40
Yan, Q., Schmidt, B. F., Perkins, L. A., Naganbabu, M., Saurabh, S., Andreko, S. K., & Bruchez, M. P. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob02309a · Cited by 40
Onishi, M., Pringle, J. R., & Cross, F. R. (2015) · Genetics · doi:10.1534/genetics.115.184663 · Cited by 40
Hansjakob, A., Riederer, M., & Hildebrandt, U. (2012) · Fungal Biology · doi:10.1016/j.funbio.2012.05.006 · Cited by 40
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Napolitano, J. G., Daranas, A. H., Norte, M., & Fernández, J. J. (2009) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152009787313800 · Cited by 40
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Peterson, J. J., Orisme, W., Fellows, J., McDowell, J. H., Shelamer, C. L., Dugger, D. R., & Smith, W. C. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-0567 · Cited by 40
Yvon, A.-M. C., Gross, D. J., & Wadsworth, P. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141224198 · Cited by 42
Regulation of the mesangial cell myofibroblast phenotype by actin polymerization
Patel, K., Harding, P., Haney, L. B., & Glass, W. F. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10267 · Cited by 40
Ebrahimighaei, R., Sala‐Newby, G. B., Hudson, C. A., Kimura, T. E., Hathway, T., Hawkins, J., McNeill, M. C., Richardson, R. J., Newby, A. C., & Bond, M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119329 · Cited by 41
Ste20/GCK kinase Nak1/Orb3 polarizes the actin cytoskeleton in fission yeast during the cell cycle
Leonhard, K., & Nurse, P. (2005) · Journal of Cell Science · doi:10.1242/jcs.01690 · Cited by 39
Lyubchenko, T. A., Wurth, G. A., & Zweifach, A. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.033522 · Cited by 39
Ñeco, P., Rossetto, O., Gil, A., Montecucco, C., & Gutiérrez, L. M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01682.x · Cited by 39
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Ammar, D. A., Nguyen, P. N. B., & Forte, J. G. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.2.c407 · Cited by 39
da Costa, S. R., Okamoto, C. T., & Hamm‐Alvarez, S. F. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.07.011 · Cited by 39
Schumacher, M. M., Kelkel, M., Dicato, M. A., & Diederich, M. F. (2011) · Molecules · doi:10.3390/molecules16075629 · Cited by 38
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Gagliardi, P. A., Puliafito, A., di Blasio, L., Chianale, F., Somale, D., Seano, G., Bussolino, F., & Primo, L. (2015) · Scientific Reports · doi:10.1038/srep10206 · Cited by 38
ACTIN AND MYOSIN REGULATE PSEUDOPODIA OFPORPHYRA PULCHELLA(RHODOPHYTA) ARCHEOSPORES1
Ackland, J. C., West, J. A., & Pickett‐Heaps, J. D. (2007) · Journal of Phycology · doi:10.1111/j.1529-8817.2006.00311.x · Cited by 38
Moscatelli, A., Idilli, A., Rodighiero, S., & Caccianiga, M. (2012) · Plant biology · doi:10.1111/j.1438-8677.2011.00547.x · Cited by 38
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Zhang, Z., Denans, N., Liu, Y., Zhulyn, O., Rosenblatt, H. D., Wernig, M., & Barna, M. (2021) · Nature Cell Biology · doi:10.1038/s41556-020-00625-2 · Cited by 38
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Walsh, C. J. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2006.10.003 · Cited by 37
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Ahmed, S. A., Odde, S., Daga, P. R., Bowling, J. J., Mesbah, M. K., Youssef, D. T. A., Khalifa, S. I., Doerksen, R. J., & Hamann, M. T. (2007) · Organic Letters · doi:10.1021/ol7020675 · Cited by 37
F‐actin involvement in guinea pig sperm motility
Azamar, Y., Uribe‐Carvajal, S., & Mújica, A. (2006) · Molecular Reproduction and Development · doi:10.1002/mrd.20578 · Cited by 37
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Hermans, M. A. W., van Stigt, A. C., van de Meerendonk, S., Schrijver, B., van Daele, P. L. A., van Hagen, P. M., van Splunter, M. E., & Dik, W. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.625284 · Cited by 36
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Okka, M., Tian, B., & Kaufman, P. L. (2004) · Archives of Ophthalmology · doi:10.1001/archopht.122.10.1482 · Cited by 36
do Prado, M. P., Torres, Y. R., Berlinck, R. G. S., Desiderá, C., Sanchez, M. A., Craveiro, M. V., Hajdu, E., da Rocha, R. M., & Machado‐Santelli, G. M. (2004) · Journal of Experimental Marine Biology and Ecology · doi:10.1016/j.jembe.2004.08.008 · Cited by 36
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Sierra‐Paredes, G., Oreiro-García, T., Núñez-Rodriguez, A., Vázquez-López, A., & Sierra‐Marcuño, G. (2006) · Journal of Molecular Neuroscience · doi:10.1385/jmn:28:2:151 · Cited by 38
Paschoud, S., Yu, D., Pulimeno, P., Jond, L., Turner, J. R., & Citi, S. (2010) · Molecular Membrane Biology · doi:10.3109/09687688.2010.538937 · Cited by 36
Bogliolo, L., Murrone, O., Piccinini, M., Ariu, F., Ledda, S., Tilocca, S., & Albertini, D. F. (2014) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-014-0389-7 · Cited by 36
Rasmussen, C. A., Kaufman, P. L., Ritch, R. H., Haque, R. M., Brazzell, R. K., & Vittitow, J. L. (2014) · Translational Vision Science & Technology · doi:10.1167/tvst.3.5.1 · Cited by 35
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Viloria, K., Nasteska, D., Briant, L. J. B., Heising, S., Larner, D. P., Fine, N. H. F., Ashford, F. B., Xavier, G. D. S., Ramos, M. J., Hasib, A., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107761 · Cited by 35
Cristofanilli, M., & Akopian, A. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.114108 · Cited by 35
Nicolas, E., Chenouard, N., Olivo‐Marín, J., & Guichet, A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-04-0360 · Cited by 35
Schatten, H., Simerly, C. R., Maul, G. G., & Schatten, G. P. (1989) · Gamete Research · doi:10.1002/mrd.1120230308 · Cited by 35
Miller, K. E., Vargas-García, C. A., Singh, A., & Moseley, J. B. (2023) · Current Biology · doi:10.1016/j.cub.2023.06.054 · Cited by 31
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Bi, Y., Page, S. L. L., & Williams, J. A. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00508.2004 · Cited by 34
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van der Honing, H. S., de Ruijter, N. C. A., Emons, A. M. C., & Ketelaar, T. (2009) · New Phytologist · doi:10.1111/j.1469-8137.2009.03017.x · Cited by 34
Miki, T., Akiba, K., Iguchi, M., Danbara, H., & Okada, N. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07637.x · Cited by 34
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Li, H., Cook, J. D., Terry, M., Spitzer, N. C., & Ferrari, M. B. (2003) · Developmental Dynamics · doi:10.1002/dvdy.10428 · Cited by 34
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Aravamudhan, P., Raghunathan, K., Konopka‐Anstadt, J. L., Pathak, A., Sutherland, D. M., Carter, B. D., & Dermody, T. S. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008380 · Cited by 33
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Fumoto, S., Nishi, J., Ishii, H., Wang, X., Miyamoto, H., Yoshikawa, N., Nakashima, M., Nakamura, J., & Nishida, K. (2009) · Molecular Pharmaceutics · doi:10.1021/mp900042p · Cited by 33
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Yamada, K., Ojika, M., Kigoshi, H., & Suenaga, K. (2010) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.86.176 · Cited by 33
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DeMay, B. S., Meseroll, R. A., Occhipinti, P., & Gladfelter, A. S. (2010) · Cytoskeleton · doi:10.1002/cm.20452 · Cited by 37
Hosu, B. G., Mullen, S. F., Critser, J. K., & Forgács, G. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002787 · Cited by 33
Cox, K. H., Tate, J. J., & Cooper, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309240200 · Cited by 33
Cuchillo‐Ibáñez, I., Lejen, T., Albillos, A., Rosé, S. D., Olivares, R., Villarroya, M., Garcı́a, A. G., & Trifaró, J. M. (2004) · The Journal of Physiology · doi:10.1113/jphysiol.2004.064063 · Cited by 32
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Kaufman, P. L. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108105 · Cited by 32
Torres, C., Pérez‐Victoria, F. J., Parodi‐Talice, A., Castanys, S., & Gamarro, F. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04304.x · Cited by 32
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Nakhost, A., Kabir, N., Forscher, P., & Sossin, W. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205099200 · Cited by 32
Yang, Y., Zhao, Y., Zheng, W.-N., Zhao, Y., Zhao, S., Wang, Q., Bai, L., Zhang, T., Huang, S., Song, C., et al. (2021) · The Plant Cell · doi:10.1093/plcell/koab264 · Cited by 33
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Ehrlich, H., Łuczak, M., Ziganshin, R., Mikšı́k, I., Wysokowski, M., Simon, P., Baranowska‐Bosiacka, I., Kupnicka, P., Ereskovsky, A. V., Galli, R., et al. (2022) · Advanced Science · doi:10.1002/advs.202105059 · Cited by 30
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Gong, H., & Freddo, T. F. (2009) · Experimental Eye Research · doi:10.1016/j.exer.2009.01.015 · Cited by 31
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Okuda, R. K., & Scheuer, P. J. (1985) · Cellular and Molecular Life Sciences · doi:10.1007/bf01952094 · Cited by 31
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Schatten, H., & Schatten, G. P. (1986) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970060215 · Cited by 31
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Wurth, M. A., Schowalter, R. M., Smith, E. C., Moncman, C. L., Dutch, R., & McCann, R. O. (2010) · Virology · doi:10.1016/j.virol.2010.04.024 · Cited by 30
Still, P. C., Johnson, T. A., Theodore, C. M., Loveridge, S. T., & Crews, P. (2014) · Journal of Natural Products · doi:10.1021/np500041x · Cited by 30
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Fabian, L., & Forer, A. (2007) · PROTOPLASMA · doi:10.1007/s00709-007-0262-y · Cited by 30
Brückner, B. R., Nöding, H., Skamrahl, M., & Janshoff, A. (2018) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2018.08.010 · Cited by 28
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Aihara, E., Medina-Candelaria, N. M., Hanyu, H., Matthis, A. L., Engevik, K. A., Gurniak, C. B., Witke, W., Turner, J. R., Zhang, T., & Montrose, M. H. (2018) · Journal of Cell Science · doi:10.1242/jcs.216317 · Cited by 29
Nummela, P., Yin, M., Kielosto, M., Leaner, V. D., Birrer, M. J., & Hölttä, E. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2421 · Cited by 29
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Macejak, D. G., & Luftig, R. B. (1991) · Virus Research · doi:10.1016/0168-1702(91)90092-a · Cited by 29
Krebs, H. C. (1986) · Fortschritte der Chemie Organischer Naturstoffe/Fortschritte der Chemie organischer Naturstoffe/Progress in the chemistry of organic natural products · doi:10.1007/978-3-7091-8846-0_3 · Cited by 29
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Torrès, M., & Coates, T. D. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(99)00168-4 · Cited by 29
Hirai, H. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00938.x · Cited by 29
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Heimlicher, M. B., Bächler, M., Liu, M., Ibeneche-Nnewihe, C., Florin, E., Hoenger, A., & Brunner, D. (2019) · Journal of Cell Science · doi:10.1242/jcs.231688 · Cited by 28
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Scheffler, K., Giannini, F., Lemonnier, T., & Mogessie, B. (2022) · Journal of Cell Science · doi:10.1242/jcs.259807 · Cited by 28
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Conchonaud, F., Nicolas, S., Amoureux, M., Ménager, C., Marguet, D., Lenne, P., Rougon, G., & Matarazzo, V. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608590200 · Cited by 29
Villanueva, J., Viniegra, S., Giménez-Molina, Y., García-Martinez, V., Expósito-Romero, G., Francés, M. D. M., Garcı́a-Sancho, J., & Gutiérrez, L. M. (2014) · Journal of Cell Science · doi:10.1242/jcs.160242 · Cited by 28
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Pan, N., Jin, J., & Peng, H. B. (2012) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-012-1132-9 · Cited by 28
Grosjean, K., Der, C., Robert, F., Thomas, D., Mongrand, S., Simon-Plas, F., & Gerbeau‐Pissot, P. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/ery152 · Cited by 28
Drug discovery: Past, present and future
Kaul, P. N. (1998) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8833-2_1 · Cited by 28
Micromechanical coupling between cell surface receptors and RGD peptides
Rahman, A., Tseng, Y., & Wirtz, D. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00903-8 · Cited by 28
Smrž, D., Bandara, G., Beaven, M. A., Metcalfe, D. D., & Gilfillan, A. M. (2013) · European Journal of Immunology · doi:10.1002/eji.201243214 · Cited by 27
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Metadata
- Authors
- Spector, I., Shochet, N. R., Kashman, Y., & Groweiss, A.
- Affiliations
- National Institutes of Health (US)
- Tel Aviv University (IL)
- Venue
- Science
- Published
- 1983-02-04
- Volume
- 219
- Issue
- 4584
- Pages
- 493-495
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1984653721
- Cited by
- 750
- References
- 21
- Citations by year
- 2026: 18 · 2025: 22 · 2024: 16 · 2023: 21 · 2022: 16 · 2021: 19 · 2020: 31 · 2019: 21 · 2018: 19 · 2017: 16 · 2016: 19 · 2015: 28 · 2014: 33 · 2013: 31 · 2012: 29
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Marine Sponges and Natural Products
- Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Physical Sciences › Chemistry › Organic Chemistry › Isoquinoline Alkaloid Synthesis
- Keywords
- latrunculin, latrunculin A, latrunculin B, marine toxins, marine sponges, microfilament organization, actin cytoskeleton, macrolides, neuroblastoma cells, fibroblasts, cell morphology, microtubules
- MeSH terms
- Actins, Animals, Cells, Cultured, Cytoskeleton, Fibroblasts, Marine Toxins, Microscopy, Fluorescence, Microtubules, Neuroblastoma, Thiazoles, Bridged Bicyclo Compounds, Heterocyclic, Thiazolidines
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