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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 501–600 of 746
Lu, Y., Lin, Y., Wen, Z., Chen, Y., Chen, S.-A., & Chen, Y. (2016) · Clinical Science · doi:10.1042/cs20150593 · Cited by 12
Structural analysis suggests that renin is released by compound exocytosis
Steppan, D., Zügner, A., Rachel, R., & Kurtz, A. (2012) · Kidney International · doi:10.1038/ki.2012.392 · Cited by 12
Grolig, F., Moch, J., Schneider, A., & Galland, P. (2014) · Plant biology · doi:10.1111/plb.12065 · Cited by 12
Examination of the olefin–olefin ring closing metathesis to prepare Latrunculin B
She, J., Lampe, J. W., Polianski, A. B., & Watson, P. S. (2008) · Tetrahedron Letters · doi:10.1016/j.tetlet.2008.10.144 · Cited by 12
Stark, M., Raz, S., & Assaraf, Y. G. (2021) · Journal of Proteomics · doi:10.1016/j.jprot.2021.104169 · Cited by 12
Fortemaison, N., Blancquaert, S., Dumont, J. E., Maenhaut, C., Aktories, K., Roger, P. P., & Dremier, S. (2005) · Endocrinology · doi:10.1210/en.2005-0329 · Cited by 12
Responding to directional cues: a tale of two cells [biochemical signaling pathways]
Paliwal, S., Ma, L., Krishnan, J., Levchenko, A., & Iglesias, P. A. (2004) · IEEE Control Systems · doi:10.1109/mcs.2004.1316655 · Cited by 12
Mierswa, S. C., Wheeler, E. E., Apsey, A. N., Jeon, O., Alsberg, E., & Leach, J. K. (2025) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.37928 · Cited by 11
Lusthaus, J. A., & Goldberg, I. (2016) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2016.1223042 · Cited by 11
Luton, F. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)04029-2 · Cited by 11
Ko, M. K., Kim, E. K., González, J. M., & Tan, J. C. H. (2016) · Scientific Reports · doi:10.1038/srep21492 · Cited by 11
Gravisensing: Ionic responses, cytoskeleton and amyloplast behavior
Allen, N. S., Chattaraj, P., Collings, D. A., & Johannes, E. (2003) · Advances in Space Research · doi:10.1016/s0273-1177(03)90404-2 · Cited by 11
Mini-dystrophin efficiently incorporates into the dystrophin protein complex in living cells
Draviam, R. A., Wang, B., Li, J., Xiao, X., & Watkins, S. C. (2006) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-006-9055-8 · Cited by 11
Recent heterocyclic compounds from marine invertebrates: Structure and synthesis
Kashman, Y., Rudi, A., & Pappo, D. (2007) · Pure and Applied Chemistry · doi:10.1351/pac200779040491 · Cited by 11
Self-citationEffect of H-7 and Lat-B on Retinal Physiology
Kiland, J. A., Miller, C. L., Kim, C. B. Y., Hoeve, J. N. V., Gabelt, B. T., Peterson, J. A., Nork, T. M., & Kaufman, P. L. P. (2006) · Current Eye Research · doi:10.1080/02713680600672185 · Cited by 11
Villanueva, M. A., Arzápalo‐Castañeda, G., & Castillo-Medina, R. E. (2014) · Canadian Journal of Microbiology · doi:10.1139/cjm-2014-0325 · Cited by 11
Khalifa, S. I., Ahmed, S. A., Mesbah, M. K., Youssef, D. T. A., & Hamann, M. T. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2005.12.028 · Cited by 11
Hypotonic stimulation of the Na+ active transport in frog skeletal muscle: role of the cytoskeleton
Venosa, R. A. (2003) · The Journal of Physiology · doi:10.1111/j.1469-7793.2003.00451.x · Cited by 11
Rearrangement and opening of the macrolide of latrunculin B
Blasberger, D., Green, D., Carmeli, S., Spector, I., & Kashman, Y. (1987) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)95756-3 · Cited by 11
Self-citationHormone-stimulated calcium release is inhibited by cytoskeleton-disrupting toxins in AR4-2J cells
Bozem, M., Kuhlmann, S., Blum, R., Feick, P., & Schulz, I. (2000) · Cell Calcium · doi:10.1054/ceca.2000.0133 · Cited by 11
Ibl, V., & Stöger, E. (2014) · Plants · doi:10.3390/plants3030442 · Cited by 10
Wooster, M. K., Voigt, O., Erpenbeck, D., Wörheide, G., & Berumen, M. L. (2019) · Coral reefs of the world · doi:10.1007/978-3-030-05802-9_6 · Cited by 11
Dynamic coalescence of yeast Heat Shock Protein genes bypasses the requirement for actin
Rubio, L. S., & Gross, D. S. (2023) · Genetics · doi:10.1093/genetics/iyad006 · Cited by 10
Bideau, L., Ramirez, Z. A. V., Baduel, L., Basso, M., Gilardi‐Hebenstreit, P., Ribes, V., Vervoort, M., & Gazave, E. (2024) · Development · doi:10.1242/dev.202452 · Cited by 10
Divergent Approach to Building a Latrunculin Family Derived Hybrid Macrocyclic Toolbox
Aeluri, M., Dasari, B., & Arya, P. (2015) · Organic Letters · doi:10.1021/ol503465p · Cited by 10
Natural Products from Tongan Marine Organisms
Taufa, T., Subramani, R., Northcote, P. T., & Keyzers, R. A. (2021) · Molecules · doi:10.3390/molecules26154534 · Cited by 10
Rich-Robinson, J., Russell, A. R., Mancini, E., & Das, M. E. (2021) · Journal of Cell Science · doi:10.1242/jcs.259291 · Cited by 10
The effects of actomyosin disruptors on the mechanical integrity of the avian crystalline lens.
Won, G.-J., Fudge, D. S., & Choh, V. (2015) · Europe PMC (PubMed Central) · Cited by 10
The Cytoskeleton as a Target in Cell Toxicity
Hargreaves, A. J. (1997) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60273-8 · Cited by 9
Contribution of F-Actin to Barrier Properties of the Blood-Joint Pathway
Poli, A., COLEMAN, P. J., Mason, R. M., & Levick, J. R. (2002) · Microcirculation · doi:10.1038/sj.mn.7800149 · Cited by 10
Effects of the F-actin inhibitor latrunculin A on the budding yeast Saccharomyces cerevisiae
Kopecká, M., Kawamoto, S., & Yamaguchi, M. (2015) · Microbiology · doi:10.1099/mic.0.000091 · Cited by 10
Small molecules that regulate zymosan phagocytosis of macrophage through deactivation of Rho GTPases
Bang, J. S., Kim, Y. J., Song, J., Yoo, J., Lee, S., Lee, M. J., Min, H., Hwang, K. W., & Min, K. H. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.06.043 · Cited by 10
Kudrimoti, S., Ahmed, S. A., Daga, P. R., Wahba, A. E., Khalifa, S. I., Doerksen, R. J., & Hamann, M. T. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.09.012 · Cited by 10
Oda, H., Suzuki, H., Sakai, K., Kitahara, S., Patrick, M. S., Azuma, Y., Sugi, K., Kitamura, T., Kaye, J., & Shirai, M. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.1005585 · Cited by 11
Role of Actin-Bundling Protein Sac6 in Growth of Cryptococcus neoformans at Low Oxygen Concentration
Chang, Y. C., Lamichhane, A. K., & Kwon-Chung, K. J. (2012) · Eukaryotic Cell · doi:10.1128/ec.00120-12 · Cited by 11
Islam, T. (2008) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20281 · Cited by 10
Inhibition of actin polymerization by marine toxin pectenotoxin-2
Hori, M., Yazama, F., Matsuura, Y., Yoshimoto, R., Kaneda, T., Yasumoto, T., Ozaki, H., & Karaki, H. (2017) · Journal of Veterinary Medical Science · doi:10.1292/jvms.17-0654 · Cited by 10
Geeraert, V., Dupont, J. L., Grant, N. J., Huvet, C., Chasserot‐Golaz, S., Janoshazi, A. K., Procksch, O., & de Barry, J. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00267-2 · Cited by 10
Mechanisms of axoneme and centriole elimination in Naegleria gruberi
Woglar, A., Busso, C., García, G. G.-J., Douma, F., Croisier, M., Knott, G. W., & Gönczy, P. (2024) · EMBO Reports · doi:10.1038/s44319-024-00329-w · Cited by 9
Shi, X., Duan, F., Lin, L., Xu, Q., Xu, T., & Zhang, R. (2019) · Journal of Cell Science · doi:10.1242/jcs.228023 · Cited by 10
Antitumor Effects of Sea Hare-Derived Compounds in Cancer
Kigoshi, H., & Kita, M. (2014) · Springer eBooks · doi:10.1007/978-3-319-07145-9_33 · Cited by 9
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Villanueva, H. E., & Setzer, W. N. (2010) · Records of Natural Products · Cited by 9
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Unzue, A., Cribiù, R., Hoffman, M. M., Knehans, T., Lafleur, K., Caflisch, A., & Nevado, C. (2018) · Chemical Science · doi:10.1039/c7sc04286h · Cited by 9
Turning the Actin Nucleating Compound Miuraenamide into Nucleation Inhibitors
Wang, S., Meixner, M., Yu, L., Zhuo, L., Karmann, L., Kazmaier, U., Vollmar, A. M., Antes, I., & Stefan Zahler, A. (2021) · ACS Omega · doi:10.1021/acsomega.1c02838 · Cited by 9
Latrunculin-A causes mydriasis and cycloplegia in the cynomolgus monkey.
Peterson, J. A., Tian, B., Geiger, B., & Kaufman, P. L. (1999) · PubMed · Cited by 9
Niedenberger, B. A., Chappell, V. A., Otey, C. A., & Geyer, C. B. (2014) · Reproduction · doi:10.1530/rep-14-0147 · Cited by 8
Detecting material state changes in the nucleolus by label-free digital holographic microscopy
Zorbas, C., Soenmez, A., Léger, J., Vleeschouwer, C. D., & Lafontaine, D. L. J. (2024) · EMBO Reports · doi:10.1038/s44319-024-00134-5 · Cited by 9
Actin and myosin dynamics are independent duringDrosophilaembryonic wound repair
Kobb, A. B., Rothenberg, K. E., & Fernández‐González, R. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-11-0703 · Cited by 9
Effect of cytoskeleton inhibitors on deadhesion kinetics of HepG2 cells on biomimetic surface.
Feng, Z.-Q., Chen, B., Tang, S.-C., Liao, K., Chen, W.-N., & Chan, V. (2010) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2009.08.010 · Cited by 7
Septin 6 localizes to microtubules in neuronal dendrites
Moon, I. S., Lee, H., & Walikonis, R. S. (2012) · Cytotechnology · doi:10.1007/s10616-012-9477-7 · Cited by 8
Altered impedance during pigment aggregation inXenopus laevis melanophores
Immerstrand, C., Jager, E. W. H., Magnusson, K., Sundqvist, T., Lundström, I., Inganäs, O., & Peterson, K. H. (2003) · Medical & Biological Engineering & Computing · doi:10.1007/bf02348443 · Cited by 8
Echovirus 11 infection induces dramatic changes in the actin cytoskeleton of polarized Caco-2 cells
Sobo, K., Stuart, A. D., Rubbia‐Brandt, L., Brown, T. D. K., & McKee, T. (2011) · Journal of General Virology · doi:10.1099/vir.0.037697-0 · Cited by 8
Díaz, E.-M., Vicente‐Manzanares, M., Legaz, M.-E., & Vicente, C. (2015) · Acta Physiologiae Plantarum · doi:10.1007/s11738-015-2007-4 · Cited by 8
Zhang, H., Colyvas, K., Patrick, J. W., & Offler, C. E. (2017) · Journal of Experimental Botany · doi:10.1093/jxb/erx315 · Cited by 8
Investigating HCMV entry into host cells by STEM tomography
Abdellatif, M. E. A., Sinzger, C., & Walther, P. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.10.007 · Cited by 8
Pollard, T. D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38062-5_11 · Cited by 8
Synthetic studies related to latrunculin. Synthesis of tetrahydropyranylthiazolidin-2-one systems
Kashman, Y., Lidor, R., Blasberger, D., & Carmeli, S. (1986) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)84260-4 · Cited by 8
Self-citationMu, B., Rutkowski, D. M., Grenci, G., Vavylonis, D., & Zhang, D. (2025) · BMC Biology · doi:10.1186/s12915-025-02309-5 · Cited by 7
Guan, Q., Chen, R., Tian, Z., Zhang, P., Liu, L., Cheng, M., Zeng, Y., Wu, D., Zhou, M., & 窦红静 (2025) · Nano Research · doi:10.26599/nr.2025.94907906 · Cited by 7
do Rosário, C. F., Zhang, Y., Stadnicki, J., Ross, J. L., & Wadsworth, P. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-02-0049 · Cited by 7
Digital holographic imaging of dynamic cytoskeleton changes
Schnekenburger, J., Bredebusch, I., Domschke, W., Kemper, B., Langehanenberg, P., & von Bally, G. (2007) · Medical Laser Application · doi:10.1016/j.mla.2007.09.008 · Cited by 7
Gholam, M. F., Ko, B. S., Ghazi, Z. M., Hoover, R. S., & Alli, A. A. (2021) · Biology · doi:10.3390/biology10121335 · Cited by 7
Myosin V facilitates polarised E‐cadherin secretion
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Actin-Interacting Amphidinolides: Syntheses and Mechanisms of Action of Amphidinolides X, J, and K
Costa, A. M. (2023) · Molecules · doi:10.3390/molecules28135249 · Cited by 7
White, P., Luo, G., & Chen, J. (2002) · Clinical Physiology and Functional Imaging · doi:10.1046/j.1475-097x.2002.00437.x · Cited by 7
Brusés, J. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062435 · Cited by 7
Matsuoka, S., Ishii, Y., Nakao, A., Abe, M., Ohtsuji, N., Momose, S., Jin, H., Arase, H., Sugimoto, K., Nakauchi, Y., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0150496 · Cited by 7
Okuda, K., Sekida, S., Hasebe, A., Iwabuchi, M., Kamiya, M., & Hishinuma, T. (2016) · Phycological Research · doi:10.1111/pre.12139 · Cited by 7
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Zhou, C., Huang, L., Shi, D., & Jiang, J. (2017) · Molecular Reproduction and Development · doi:10.1002/mrd.22878 · Cited by 7
González-Gutiérrez, A. G., Verdín, J., & Rodríguez‐Garay, B. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00384 · Cited by 7
The mitotic exit network regulates the spatiotemporal activity of Cdc42 to maintain cell size
Gihana, G. M., Cross-Najafi, A. A., & Lacefield, S. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202001016 · Cited by 7
Lynn, K. S., Easley, K. F., Martinez, F. J., Reed, R. C., Schlingmann, B., & Koval, M. H. (2021) · Tissue Barriers · doi:10.1080/21688370.2021.1929786 · Cited by 7
Kopecká, M. (2015) · Chemotherapy · doi:10.1159/000437134 · Cited by 7
Localization of Gts1p in cortical actin patches of yeast and its possible role in endocytosis
Yaguchi, S.-I., Shen, H., & Tsurugi, K. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.02.005 · Cited by 7
Latrunculin a is a potent inducer of aggregation of polymorphonuclear leukocytes
de Oliveira, C. A., Chedraoui-Silva, S., & Mantovani, B. (1997) · Life Sciences · doi:10.1016/s0024-3205(97)00435-9 · Cited by 7
West, V. C., Owen, K. E., Inguito, K. L., Ebron, K. M. M., Reiner, T. N., Mirack, C. E., Le, C. H., Marqueti, R. D. C., Snipes, S., Mousavizadeh, R., et al. (2024) · Cytoskeleton · doi:10.1002/cm.21962 · Cited by 7
Gaikani, H. K., Smith, A. M., Lee, A. Y., Giaever, G. N., & Nislow, C. (2021) · Frontiers in Fungal Biology · doi:10.3389/ffunb.2021.683414 · Cited by 6
Higa, T., & Tanaka, J. (1996) · Studies in natural products chemistry · doi:10.1016/s1572-5995(96)80015-9 · Cited by 6
Asadi, F., Michalski, D., & Karagiannis, J. (2016) · G3 Genes Genomes Genetics · doi:10.1534/g3.116.032664 · Cited by 6
Viruses That Exploit Actin-Based Motility for Their Replication and Spread
Marzook, N. B., & Newsome, T. P. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_41 · Cited by 9
Tomatis, V. M., Josh, P. F., Papadopulos, A., Gormal, R. S., Lanoue, V., Martin, S., & Meunier, F. A. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.07.005 · Cited by 6
Kowal, A. S., & Chisholm, R. L. (2011) · Eukaryotic Cell · doi:10.1128/ec.00221-10 · Cited by 8
F‐actin cytoskeleton and the fate of organelles in chromaffin cells
Villanueva, J., Giménez-Molina, Y., Viniegra, S., & Gutiérrez, L. M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13560 · Cited by 6
Braet, F., Soon, L., Vekemans, K., Thordarson, P., & Spector, I. (2008) · Springer eBooks · doi:10.1007/978-0-387-71749-4_3 · Cited by 6
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Kemper, B., & Schnekenburger, J. (2011) · doi:10.1002/9783527634286.ch8 · Cited by 6
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Kopecká, M., Yamaguchi, M., & Kawamoto, S. (2014) · Chemotherapy · doi:10.1159/000377619 · Cited by 5
Курилова, Л. С., Krutetskaya, Z. I., Lebedev, O. E., Krutetskaya, N. I., & Антонов, В. Г. (2012) · Cell and Tissue Biology · doi:10.1134/s1990519x12030066 · Cited by 5
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Prabha Devi Ravichandran, S. (2013) · Oceanography Open Access · doi:10.4172/2332-2632.1000112 · Cited by 5
Holzinger, A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1661-1_9 · Cited by 5
Structure‐Activity Studies of Truncated Latrunculin Analogues with Antimalarial Activity
Varghese, S., Rahmani, R., Drew, D. R., Beeson, J. G., Baum, J., Smith, B. J., & Baell, J. B. (2020) · ChemMedChem · doi:10.1002/cmdc.202000399 · Cited by 5
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Galli, M. G., Diani, L., Quadri, R., Nespoli, A., Galati, E., Panigada, D., Plevani, P., & Muzi-Falconi, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.625717 · Cited by 5
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Jun, J. H., Javed, S., Ndi, C. N., & Hanson, P. R. (2015) · Topics in heterocyclic chemistry · doi:10.1007/7081_2015_162 · Cited by 5
Lu, Y., Chen, Y., Lin, Y., Chen, Y., & Chen, Y. (2020) · Journal of Arrhythmia · doi:10.1002/joa3.12391 · Cited by 5
High-throughput multimodal optofluidic biophysical imaging cytometry
Lee, T. R., Cheung, E. H. Y., Lee, K. C. M., Siu, D. M. D., Lo, M. C. K., Lam, E. Y. M., Goswami, R., Girardo, S., Kim, K., Reichel, F., et al. (2025) · Lab on a Chip · doi:10.1039/d5lc00381d · Cited by 4
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Català-Castro, F., Bonilla-Quintana, M., Sanfeliu-Cerdán, N., Rangamani, P., & Krieg, M. (2025) · Nature Physics · doi:10.1038/s41567-025-03037-x · Cited by 4
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Wahl‐Schott, C., Freichel, M., Hennis, K., Philippaert, K., Ottenheijm, R., Tsvilovskyy, V., & Varbanov, H. (2023) · Handbook of experimental pharmacology · doi:10.1007/164_2023_637 · Cited by 5
Hu, Q., Zhao, Y., Sun, W., Ou, Z., Duan, W., Qiu, Z., Ge, Y., Tang, D., Chen, T., Cheng, X., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107942 · Cited by 4
Evidence for Brassinosteroid-Mediated PAT During Germination of Spathoglottis plicata (Orchidaceae)
Novak, S. D., Kalbakji, N., Upthegrove, K. C., Neher, W., Jones, J. H., & de Leon, J. A. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01215 · Cited by 4
Christophersen, C. (1985) · The Alkaloids. Chemistry and physiology · doi:10.1016/s0099-9598(08)60037-1 · Cited by 4
Involvement of lipid rafts and cellular actin in AcMNPV GP64 distribution and virus budding
Haines, F. J., Griffiths, C. M., Possee, R. D., Hawes, C. R., & King, L. A. (2009) · Virologica Sinica · doi:10.1007/s12250-009-3055-y · Cited by 4
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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