Latrunculins: Novel Marine Toxins That Disrupt Microfilament Organization in Cultured Cells

Mechanism of action of cytochalasin B on actin

MacLean-Fletcher, S. (1980) · Cell · doi:10.1016/0092-8674(80)90619-4 · Cited by 755 · see citing works

Nonmuscle Contractile Proteins: The Role of Actin and Myosin in Cell Motility and Shape Determination

Clarke, M., & Spudich, J. A. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.004053 · Cited by 504 · see citing works

Actin-binding proteins—regulators of cell architecture and motility

Weeds, A. G. (1982) · Nature · doi:10.1038/296811a0 · Cited by 467 · see citing works

Cytoplasmic fibrils in living cultured cells

Buckley, I. K., & Porter, K. R. (1967) · PROTOPLASMA · doi:10.1007/bf01666538 · Cited by 353 · see citing works

Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro

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 · see citing works

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 · see citing works

Substoichiometric concentrations of cytochalasin D inhibit actin polymerization. Additional evidence for an F-actin treadmill.

Brenner, S. L., & Korn, E. D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86660-7 · Cited by 266 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Cytoplasmic contractile proteins.

Pollard, T. D. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.3.156s · Cited by 197 · see citing works

Ionic currents in cultured mouse neuroblastoma cells under voltage‐clamp conditions.

Moolenaar, W. H., & Spector, I. (1978) · The Journal of Physiology · doi:10.1113/jphysiol.1978.sp012303 · Cited by 175 · see citing works

Latrunculin, a new 2-thiazolidinone macrolide from the marine sponge

Kashman, Y., Groweiss, A., & Shmueli, U. (1980) · Tetrahedron Letters · doi:10.1016/0040-4039(80)80255-3 · Cited by 164 · see citing works

Excitable Cells in Tissue Culture

(1981) · Springer eBooks · doi:10.1007/978-1-4684-3803-1 · Cited by 143 · see citing works

Actin polymerization induced by a motility-related high-affinity cytochalasin binding complex from human erythrocyte membrane

Lin, D. C., & Lin, S. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.5.2345 · Cited by 120 · see citing works

Aggregation of microtubule initiation sites preceding neurite outgrowth in mouse neuroblastoma cells

Spiegelman, B. M., Lopata, M. A., & Kirschner, M. W. (1979) · Cell · doi:10.1016/0092-8674(79)90003-5 · Cited by 116 · see citing works

Multiple sites for the initiation of microtubule assembly in mammalian cells

Spiegelman, B. M., Lopata, M. A., & Kirschner, M. W. (1979) · Cell · doi:10.1016/0092-8674(79)90002-3 · Cited by 99 · see citing works

Isolation of a new toxin from the sponge Latrunculia magnifica in the Gulf of Aquaba (Red Sea)

N�eman, I., Fishelson, L., & Kashman, Y. (1975) · Marine Biology · doi:10.1007/bf00390634 · Cited by 53 · see citing works

Motility.

Allen, R. D. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.3.148s · Cited by 44 · see citing works

Changes in intracellular organization of tubulin and actin in N-18 neuroblastoma cells during the process of axon extension induced by serum deprivation

Marchisio, P. C., Osborn, M., & Weber, K. K. (1978) · Brain Research · doi:10.1016/0006-8993(78)91019-3 · Cited by 32 · see citing works

The intracellular organization of actin and tubulin in cultured C-1300 mouse neuroblastoma cells (clone NB41A3)

Marchisio, P. C., Osborn, M., & Weber, K. K. (1978) · Journal of Neurocytology · doi:10.1007/bf01260890 · Cited by 25 · see citing works

Pyrrolidinyl‐Spirooxindole Natural Products as Inspirations for the Development of Potential Therapeutic Agents

Galliford, C. V., & Scheidt, K. A. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200701342 · Cited by 2,431 · see citing works

Drug-Induced Changes of Cytoskeletal Structure and Mechanics in Fibroblasts: An Atomic Force Microscopy Study

Rotsch, C., & Radmacher, M. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76614-8 · Cited by 972 · see citing works

Inhibition of actin polymerization by latrunculin A

Coué, M., Brenner, S. L., Spector, I., & Korn, E. D. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81513-2 · Cited by 824 · see citing works

Divergent Signals and Cytoskeletal Assemblies Regulate Self-Organizing Polarity in Neutrophils

Xu, J., Wang, F., Keymeulen, A. V., Herzmark, P., Straight, A. F., Kelly, K., Takuwa, Y., Sugimoto, N., Mitchison, T. J., & Bourne, H. R. (2003) · Cell · doi:10.1016/s0092-8674(03)00555-5 · Cited by 687 · see citing works

Ultrafast endocytosis at mouse hippocampal synapses

Watanabe, S., Rost, B. R., Camacho-Pérez, M., Davis, M. W., Söhl-Kielczynski, B., Rosenmund, C., & Jorgensen, E. M. (2013) · Nature · doi:10.1038/nature12809 · Cited by 607 · see citing works

Dynamin and the Actin Cytoskeleton Cooperatively Regulate Plasma Membrane Invagination by BAR and F-BAR Proteins

Itoh, T., Erdmann, K. S., Roux, A., Habermann, B. H., Werner, H. B., & Camilli, P. V. D. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.11.005 · Cited by 585 · see citing works

Latrunculins—novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D

Spector, I., Shochet, N. R., Blasberger, D., & Kashman, Y. (1989) · Cell Motility · doi:10.1002/cm.970130302 · Cited by 580 · see citing works

Early steps in cold sensing by plant cells: the role of actin cytoskeleton and membrane fluidity

Örvar, B. L., Sangwan, V., Omann, F., & Dhindsa, R. S. (2000) · The Plant Journal · doi:10.1046/j.1365-313x.2000.00845.x · Cited by 574 · see citing works

Natürliche Pyrrolidinylspirooxindole als Vorlagen für die Entwicklung medizinischer Wirkstoffe

Galliford, C. V., & Scheidt, K. A. (2007) · Angewandte Chemie · doi:10.1002/ange.200701342 · Cited by 524 · see citing works

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

Morton, W. M., Ayscough, K. R., & McLaughlin, P. J. (2000) · Nature Cell Biology · doi:10.1038/35014075 · Cited by 523 · see citing works

Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils

Wang, F., Herzmark, P., Weiner, O. D., Srinivasan, S., Servant, G., & Bourne, H. R. (2002) · Nature Cell Biology · doi:10.1038/ncb810 · Cited by 471 · see citing works

Actin and serum response factor transduce physical cues from the microenvironment to regulate epidermal stem cell fate decisions

Connelly, J. T., Gautrot, J. E., Trappmann, B., Tan, D. W., Donati, G., Huck, W. T. S., & Watt, F. M. (2010) · Nature Cell Biology · doi:10.1038/ncb2074 · Cited by 442 · see citing works

Force measurements in E-cadherin–mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42

Chu, Y., Thomas, W. A., Eder, O., Pincet, F., Perez, É., Thiery, J. P., & Dufour, S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403043 · Cited by 419 · see citing works

Latrunculin B Has Different Effects on Pollen Germination and Tube Growth

Gibbon, B. C., Kovar, D. R., & Staiger, C. J. (1999) · The Plant Cell · doi:10.1105/tpc.11.12.2349 · Cited by 416 · see citing works

Molecular Ordering of the Initial Signaling Events of CD95

Algeciras-Schimnich, A., Shen, L., Barnhart, B. C., Murmann, A. E., Burkhardt, J. K., & Peter, M. E. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.207-220.2002 · Cited by 393 · see citing works

A Role of Actin Filament in Synaptic Transmission and Long-Term Potentiation

Kim, C.-H., & Lisman, J. E. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-11-04314.1999 · Cited by 386 · see citing works

Zebrafish vasa RNA but Not Its Protein Is a Component of the Germ Plasm and Segregates Asymmetrically before Germline Specification

Knaut, H., Pelegri, F. J., Bohmann, K., Schwarz, H., & Nüsslein‐Volhard, C. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.4.875 · Cited by 387 · see citing works

Investigation of living pancreas tumor cells by digital holographic microscopy

Kemper, B., Carl, D. D., Schnekenburger, J., Bredebusch, I., Schäfer, M. M., Domschke, W., & von Bally, G. (2006) · Journal of Biomedical Optics · doi:10.1117/1.2204609 · Cited by 364 · see citing works

ADF/cofilin-mediated actin dynamics regulate AMPA receptor trafficking during synaptic plasticity

Gu, J., Lee, C. W., Fan, Y., Komlos, D., Tang, X., Sun, C., Yu, K., Hartzell, H. C., Chen, G., Bamburg, J. R., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2634 · Cited by 325 · see citing works

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

Spector, I., Braet, F., Shochet, N. R., & Bubb, M. (1999) · Microscopy Research and Technique · doi:10.1002/(sici)1097-0029(19991001)47:1 · Cited by 324 · see citing works

GPI-anchored receptor clusters transiently recruit Lyn and Gα for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1

Suzuki, K. G. N., Fujiwara, T. K., Sanematsu, F., Iino, R., Edidin, M. A., & Kusumi, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609174 · Cited by 309 · see citing works

Small Molecules, Big Impact

Peterson, J. R., & Mitchison, T. J. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00284-3 · Cited by 307 · see citing works

Actin Depolymerization Disrupts Tight Junctions via Caveolae-mediated Endocytosis

Shen, L., & Turner, J. R. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-12-1089 · Cited by 302 · see citing works

A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells

Feric, M., & Brangwynne, C. P. (2013) · Nature Cell Biology · doi:10.1038/ncb2830 · Cited by 294 · see citing works

Physical confinement alters tumor cell adhesion and migration phenotypes

Balzer, E. M., Tong, Z., Paul, C. D., Hung, W., Stroka, K. M., Boggs, A. E., Martin, S. S., & Κωνσταντόπουλος, Κ. (2012) · The FASEB Journal · doi:10.1096/fj.12-211441 · Cited by 282 · see citing works

Subcellular compartment targeting of layered double hydroxide nanoparticles

Xu, Z. P., Niebert, M., Porazik, K., Walker, T. L., Cooper, H. M., Middelberg, A. P. J., Gray, P. P., Bartlett, P. F., & Lu, G. Q. (2008) · Journal of Controlled Release · doi:10.1016/j.jconrel.2008.05.021 · Cited by 279 · see citing works

A Library of Spirooxindoles Based on a Stereoselective Three-Component Coupling Reaction

LO, M. M. ‐., Neumann, C. S., Nagayama, S., Perlstein, E. O., & Schreiber, S. L. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045089d · Cited by 276 · see citing works

Actin-Latrunculin A Structure and Function

Yarmola, E. G., Somasundaram, T., Boring, T. A., Spector, I., & Bubb, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004253200 · Cited by 268 · see citing works

Rapid Hop Diffusion of a G-Protein-Coupled Receptor in the Plasma Membrane as Revealed by Single-Molecule Techniques

Suzuki, K. G. N., Ritchie, K. P., Kajikawa, E., Fujiwara, T. K., & Kusumi, A. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.048538 · Cited by 269 · see citing works

Integrin‐mediated adhesion orients the spindle parallel to the substratum in an EB1‐ and myosin X‐dependent manner

Toyoshima, F., & Nishida, E. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601599 · Cited by 264 · see citing works

Subcellular Trafficking of the Arabidopsis Auxin Influx Carrier AUX1 Uses a Novel Pathway Distinct from PIN1

Kleine‐Vehn, J., Dhonukshe, P., Swarup, R., Bennett, M. J., & Friml, J. (2006) · The Plant Cell · doi:10.1105/tpc.106.042770 · Cited by 262 · see citing works

MLCK-dependent exchange and actin binding region-dependent anchoring of ZO-1 regulate tight junction barrier function

Yu, D., Marchiando, A. M., Weber, C. R., Raleigh, D. R., Wang, Y., Shen, L., & Turner, J. R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908869107 · Cited by 256 · see citing works

Distinct Roles of Synaptic and Extrasynaptic NMDA Receptors in Excitotoxicity

Sattler, R., Xiong, Z., Lu, W.-Y., MacDonald, J. F., & Tymianski, M. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00022.2000 · Cited by 247 · see citing works

Auxin transport inhibitors impair vesicle motility and actin cytoskeleton dynamics in diverse eukaryotes

Dhonukshe, P., Grigoriev, I., Fischer, R., Tominaga, M., Robinson, D. G., Hašek, J., Paciorek, T., Petrášek, J., Seifertová, D., Tejos, R., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711414105 · Cited by 245 · see citing works

Ebola Virus Enters Host Cells by Macropinocytosis and Clathrin-Mediated Endocytosis

Aleksandrowicz, P., Marzi, A., Biedenkopf, N., Beimforde, N., Becker, S., Hoenen, T., Feldmann, H., & Schnittler, H. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jir326 · Cited by 244 · see citing works

Biomedical Potential of Marine Natural Products

Ireland, C. M., Copp, B. R., Foster, M. P., McDonald, L. A., Radisky, D. C., & Swersey, J. C. (1993) · Springer eBooks · doi:10.1007/978-1-4899-2391-2_1 · Cited by 241 · see citing works

Mammary stem cells have myoepithelial cell properties

Prater, M. D., Petit, V., Russell, I. A., Giraddi, R. R., Shehata, M., Menon, S., Schulte, R., Kalajzić, I., Rath, N., Olson, M. F., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3025 · Cited by 237 · see citing works

High-Throughput Fluorescent Tagging of Full-Length Arabidopsis Gene Products in Planta

Tian, G.-W., Mohanty, A., Chary, S. N., Li, S., Paap, B. K., Drakakaki, G., Kopec, C. D., Li, J., Ehrhardt, D. W., Jackson, D. P., et al. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.040139 · Cited by 236 · see citing works

A Master Relation Defines the Nonlinear Viscoelasticity of Single Fibroblasts

Fernández, P., Pullarkat, P. A., & Ott, A. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.072215 · Cited by 235 · see citing works

AFM IMAGING AND ELASTICITY MEASUREMENTS ON LIVING RAT LIVER MACROPHAGES

Rotsch, C., Braet, F., Wisse, E., & Radmacher, M. (1997) · Cell Biology International · doi:10.1006/cbir.1997.0213 · Cited by 229 · see citing works

Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments

Maas, T., Eidenmüller, J., & Brandt, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000389200 · Cited by 226 · see citing works

Actin-myosin–based contraction is responsible for apoptotic nuclear disintegration

Croft, D. R., Coleman, M. L., Li, S., Robertson, D. M., Sullivan, T. L., Stewart, C. L., & Olson, M. F. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200409049 · Cited by 222 · see citing works

Dynamic recruitment of phospholipase Cγ at transiently immobilized GPI-anchored receptor clusters induces IP3–Ca2+ signaling: single-molecule tracking study 2

Suzuki, K. G. N., Fujiwara, T. K., Edidin, M. A., & Kusumi, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609175 · Cited by 216 · see citing works

Role of Actin Cortex in the Subplasmalemmal Transport of Secretory Granules in PC-12 Cells

Lang, T., Wacker, I. U., Wunderlich, I., Rohrbach, A., Giese, G., Soldati, T., & Almers, W. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76828-7 · Cited by 215 · see citing works

Insulin-induced actin filament remodeling colocalizes actin with phosphatidylinositol 3-kinase and GLUT4 in L6 myotubes

Khayat, Z. A., Tong, P. C. Y., Yaworsky, K., Bloch, R. J., & Klip, A. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.2.279 · Cited by 213 · see citing works

Insulin-induced cortical actin remodeling promotes GLUT4 insertion at muscle cell membrane ruffles

Tong, P. C. Y., Khayat, Z. A., Huang, C., Patel, N., Ueyama, A., & Klip, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12348 · Cited by 211 · see citing works

Small-Molecule Inhibitors of Actin Dynamics and Cell Motility

Fenteany, G., & Zhu, S. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033452348 · Cited by 208 · see citing works

The cytoskeleton in plant and fungal cell tip growth

Geitmann, A., & Emons, A. M. C. (2000) · Journal of Microscopy · doi:10.1046/j.1365-2818.2000.00702.x · Cited by 203 · see citing works

Actin-dependent cytoplasmic streaming in C. elegans oogenesis

Wolke, U., Jezuit, E. A., & Priess, J. R. (2007) · Development · doi:10.1242/dev.004952 · Cited by 200 · see citing works

Actin-targeting natural products: structures, properties and mechanisms of action

Allingham, J. S., Klenchin, V. A., & Rayment, I. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6157-9 · Cited by 196 · see citing works

An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin

Zhou, D., Mooseker, M. S., & Galán, J. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10176 · Cited by 197 · see citing works

Direct chemical evidence for sphingolipid domains in the plasma membranes of fibroblasts

Frisz, J. F., Lou, K., Klitzing, H. A., Hanafin, W. P., Lizunov, V. A., Wilson, R. L., Carpenter, K. J., Kim, R., Hutcheon, I. D., Zimmerberg, J. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216585110 · Cited by 196 · see citing works

Latrunculin B-Induced Plant Dwarfism: Plant Cell Elongation Is F-Actin-Dependent

Baluška, F., Jásik, J., Edelmann, H. G., Salajová, T., & Volkmann, D. (2001) · Developmental Biology · doi:10.1006/dbio.2000.0115 · Cited by 195 · see citing works

Interaction between Mitochondria and the Actin Cytoskeleton in Budding Yeast Requires Two Integral Mitochondrial Outer Membrane Proteins, Mmm1p and Mdm10p

Boldogh, I. R., Vojtov, N., Karmon, S. L., & Pon, L. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.6.1371 · Cited by 186 · see citing works

Functional coordination of microtubule-based and actin-based motility in melanophores

Rodionov, V., Hope, A. J., Svitkina, T., & Borisy, G. G. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70064-8 · Cited by 186 · see citing works

A Role for the Actin Cytoskeleton in the Initiation and Maintenance of Store-mediated Calcium Entry in Human Platelets

Rosado, J. A., Jenner, S., & Sage, S. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7527 · Cited by 184 · see citing works

Actin‐Binding Marine Macrolides: Total Synthesis and Biological Importance

Yeung, K. S., & Paterson, I. (2002) · Angewandte Chemie International Edition · doi:10.1002/anie.200290057 · Cited by 182 · see citing works

HSF-1–mediated cytoskeletal integrity determines thermotolerance and life span

Baird, N. A., Douglas, P. M., Simic, M., Grant, A. R., Moresco, J. J., Wolff, S., Yates, J. R., Manning, G., & Dillin, A. G. (2014) · Science · doi:10.1126/science.1253168 · Cited by 181 · see citing works

Integrin and cytoskeletal regulation of growth factor signaling to the MAP kinase pathway

Aplin, A. E., & Juliano, R. L. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.5.695 · Cited by 179 · see citing works

Membrane Lipid Rafts Are Necessary for the Maintenance of the α7 Nicotinic Acetylcholine Receptor in Somatic Spines of Ciliary Neurons

Brusés, J. L., Chauvet, N., & Rutishauser, U. S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00504.2001 · Cited by 208 · see citing works

Hem-1 Complexes Are Essential for Rac Activation, Actin Polymerization, and Myosin Regulation during Neutrophil Chemotaxis

Weiner, O. D., Rentel, M., Ott, A., Brown, G. E., Jedrychowski, M. P., Yaffe, M. B., Gygi, S. P., Cantley, L. C., Bourne, H. R., & Kirschner, M. W. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040038 · Cited by 178 · see citing works

The Symbiotic Relationship Between Drug Discovery and Organic Chemistry

Grygorenko, O. O., Volochnyuk, D. M., Ryabukhin, S. V., & Judd, D. B. (2019) · Chemistry - A European Journal · doi:10.1002/chem.201903232 · Cited by 172 · see citing works

Catalysis‐Based Total Synthesis of Latrunculin B

Fürstner, A., Souza, D. D., Rapado, L. P., & Jensen, J. T. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200352413 · Cited by 172 · see citing works

Effects of Calreticulin on Viral Cell-to-Cell Movement

Chen, M., Tian, G.-W., Gafni, Y., & Citovsky, V. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.064386 · Cited by 171 · see citing works

Analysis of Transient Behavior in Complex Trajectories: Application to Secretory Vesicle Dynamics

Huet, S., Karatekin, E., Tran, V. S., Fanget, I., Cribier, S., & Henry, J. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.080622 · Cited by 171 · see citing works

Substratum-induced differentiation of human pluripotent stem cells reveals the coactivator YAP is a potent regulator of neuronal specification

Musah, S., Wrighton, P. J., Zaltsman, Y., Zhong, X., Zorn, S., Parlato, M. B., Hsiao, C., Palecek, S. P., Chang, Q., Murphy, W. L., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415330111 · Cited by 169 · see citing works

Neutrophil polarization: Spatiotemporal dynamics of RhoA activity support a self-organizing mechanism

Wong, K., Pertz, O. C., Hahn, K. M., & Bourne, H. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600092103 · Cited by 168 · see citing works

Motor proteins regulate force interactions between microtubules and microfilaments in the axon

Ahmad, F. J., Hughey, J., Wittmann, T., Hyman, A. A., Greaser, M. L., & Baas, P. W. (2000) · Nature Cell Biology · doi:10.1038/35010544 · Cited by 167 · see citing works

Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites

Desnos, C., Schonn, J., Huet, S., Tran, V. S., El-Amraoui, A., Raposo, G., Fanget, I., Chapuis, C., Ménasché, G., Basile, G. D. S., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302157 · Cited by 168 · see citing works

To stabilize neutrophil polarity, PIP3 and Cdc42 augment RhoA activity at the back as well as signals at the front

Keymeulen, A. V., Wong, K., Knight, Z. A., Govaerts, C., Hahn, K. M., Shokat, K. M., & Bourne, H. R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604113 · Cited by 165 · see citing works

A MAP kinase-dependent actin checkpoint ensures proper spindle orientation in fission yeast

Gachet, Y., Tournier, S., Millar, J. B. A., & Hyams, J. S. (2001) · Nature · doi:10.1038/35085604 · Cited by 161 · see citing works

Three-dimensional tracking of single mRNA particles in Saccharomyces cerevisiae using a double-helix point spread function

Thompson, M. A., Casolari, J. M., Badieirostami, M., Brown, P. O., & Moerner, W. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012868107 · Cited by 160 · see citing works

The Rho GTPase Effector ROCK Regulates Cyclin A, Cyclin D1, and p27Kip1 Levels by Distinct Mechanisms

Croft, D. R., & Olson, M. F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02061-05 · Cited by 160 · see citing works

Diatom gliding is the result of an actin-myosin motility system

Poulsen, N., Spector, I., Spurck, T. P., Schultz, T. F., & Wetherbee, R. (1999) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(199909)44:1 · Cited by 160 · see citing works

Latrunculin A Accelerates Actin Filament Depolymerization in Addition to Sequestering Actin Monomers

Fujiwara, I., Zweifel, M. E., Courtemanche, N., & Pollard, T. D. (2018) · Current Biology · doi:10.1016/j.cub.2018.07.082 · Cited by 158 · see citing works

Actin filaments play a critical role in insulin-induced exocytotic recruitment but not in endocytosis of GLUT4 in isolated rat adipocytes

Omata, W., Shibata, H., Lu, L. I., Takata, K., & Kojima, I. (2000) · Biochemical Journal · doi:10.1042/bj3460321 · Cited by 157 · see citing works

Nuclear F-Actin Counteracts Nuclear Deformation and Promotes Fork Repair during Replication Stress

Lamm, N., Read, M. N., Nobis, M., Van Ly, D., Page, S. G., Masamsetti, V. P., Timpson, P., Biro, M., & Cesare, A. J. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00605-6 · Cited by 156 · see citing works

Actin depolymerization is sufficient to induce programmed cell death in self-incompatible pollen

Thomas, S. G., Huang, S., Li, S., Staiger, C. J., & Franklin‐Tong, V. E. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604011 · Cited by 155 · see citing works

Acquisition of Viral Receptor by NK Cells Through Immunological Synapse

Tabiasco, J., Vercellone, A., Meggetto, F., Hudrisier, D., Brousset, P., & Fournié, J. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.12.5993 · Cited by 151 · see citing works

Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast

Rinnerthaler, M., Büttner, S., Laun, P., Heeren, G., Felder, T. K., Klinger, H., Weinberger, M., Stolze, K., Groušl, T., Hašek, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201629109 · Cited by 151 · see citing works

Body Handedness Is Directed by Genetically Determined Cytoskeletal Dynamics in the Early Embryo

Shibazaki, Y., Shimizu, M., & Kuroda, R. (2004) · Current Biology · doi:10.1016/j.cub.2004.08.018 · Cited by 148 · see citing works

Total Synthesis of Iejimalide A−D and Assessment of the Remarkable Actin-Depolymerizing Capacity of These Polyene Macrolides

Fürstner, A., Nevado, C., Waser, M., Tremblay, M., Chevrier, C., Teplý, F., Aïssa, C., Moulin, É., & Müller, O. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072334v · Cited by 148 · see citing works

Actin cytoskeleton remodeling drives epithelial‐mesenchymal transition for hepatoma invasion and metastasis in mice

Peng, J., Bera, R., Chiou, C., Yu, M., Chen, T., Chen, C., Wang, T.-H., Chiang, W., Chai, S., Wei, Y., et al. (2017) · Hepatology · doi:10.1002/hep.29678 · Cited by 147 · see citing works

Cytoskeletal remodeling of the airway smooth muscle cell: a mechanism for adaptation to mechanical forces in the lung

Gunst, S. J., Tang, D. D., & Saez, A. M. O. (2003) · Respiratory Physiology & Neurobiology · doi:10.1016/s1569-9048(03)00144-7 · Cited by 145 · see citing works

Aberrant actin depolymerization triggers the pyrin inflammasome and autoinflammatory disease that is dependent on IL-18, not IL-1β

Kim, M. L., Chae, J. J., Park, Y. H., Nardo, D. D., Stirzaker, R. A., Ko, H., Tye, H., Cengia, L. H., DiRago, L., Metcalf, D., et al. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20142384 · Cited by 142 · see citing works

Physical interaction between peroxisomes and chloroplasts elucidated by in situ laser analysis

Oikawa, K., Matsunaga, S., Mano, S., Kondo, M., Yamada, K., Hayashi, M., Kagawa, T., Kadota, A., Sakamoto, W., Higashi, S., et al. (2015) · Nature Plants · doi:10.1038/nplants.2015.35 · Cited by 144 · see citing works

Extrinsic cues, intrinsic cues and microfilaments regulate asymmetric protein localization in Drosophila neuroblasts

Broadus, J., & Doe, C. Q. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00370-8 · Cited by 143 · see citing works

Highlights of marine invertebrate-derived biosynthetic products: Their biomedical potential and possible production by microbial associants

Radjasa, O. K., Vaske, Y. S. M., Navarro, G., Vervoort, H. C., Tenney, K., Linington, R. G., & Crews, P. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.07.017 · Cited by 141 · see citing works

Japanese Encephalitis Virus Infects Neuronal Cells through a Clathrin-Independent Endocytic Mechanism

Kalia, M., Khasa, R., Sharma, M., Nain, M., & Vrati, S. (2012) · Journal of Virology · doi:10.1128/jvi.01399-12 · Cited by 141 · see citing works

Translocation of the B Cell Antigen Receptor into Lipid Rafts Reveals a Novel Step in Signaling

Cheng, P. C., Brown, B. K., Song, W., & Pierce, S. K. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.6.3693 · Cited by 137 · see citing works

The Actin Cytoskeleton Is Required for Selective Types of Autophagy, but Not Nonspecific Autophagy, in the Yeast<i>Saccharomyces cerevisiae</i>

Reggiori, F., Monastyrska, I., Shintani, T., & Klionsky, D. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0629 · Cited by 155 · see citing works

Drosophila Cip4/Toca-1 Integrates Membrane Trafficking and Actin Dynamics through WASP and SCAR/WAVE

Fricke, R., Gohl, C., Dharmalingam, E., Grevelhörster, A., Zahedi, B., Harden, N., Kessels, M. M., Qualmann, B., & Bogdan, S. (2009) · Current Biology · doi:10.1016/j.cub.2009.07.058 · Cited by 134 · see citing works

The Actin-Driven Movement and Formation of Acetylcholine Receptor Clusters

Dai, Z., Luo, X., Xie, H. M., & Peng, H. B. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1321 · Cited by 134 · see citing works

Natural Killer Cell Inhibitory Receptors Block Actin Cytoskeleton-dependent Recruitment of 2B4 (CD244) to Lipid Rafts

Watzl, C., & Long, E. O. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020427 · Cited by 126 · see citing works

Concise and Practical Synthesis of Latrunculin A by Ring‐Closing Enyne–Yne Metathesis

Fürstner, A., & Turet, L. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500390 · Cited by 126 · see citing works

Total Syntheses of the Actin‐Binding Macrolides Latrunculin A, B, C, M, S and 16‐epi‐Latrunculin B

Fürstner, A., Souza, D. D., Turet, L., Fenster, M. D. B., Rapado, L. P., Wirtz, C., MYNOTT, R. J., & Lehmann, C. W. (2006) · Chemistry - A European Journal · doi:10.1002/chem.200601135 · Cited by 124 · see citing works

The Src Homology Domain 3 (SH3) of a Yeast Type I Myosin, Myo5p, Binds to Verprolin and Is Required for Targeting to Sites of Actin Polarization

Anderson, B. L., Boldogh, I. R., Evangelista, M., Boone, C. M., Greene, L. A., & Pon, L. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.6.1357 · Cited by 124 · see citing works

Both MHC Class II and its GPI-Anchored Form Undergo Hop Diffusion as Observed by Single-Molecule Tracking

Umemura, Y. M., Vrljic, M., Nishimura, S. Y., Fujiwara, T. K., Suzuki, K. G. N., & Kusumi, A. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.123018 · Cited by 122 · see citing works

The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast

Nakano, K., Imai, J., Arai, R., Toh‐e, A., Matsui, Y., & Mabuchi, I. (2002) · Journal of Cell Science · doi:10.1242/jcs.00150 · Cited by 118 · see citing works

Intracellular Events in the “Selective” Transport of Lipoprotein-derived Cholesteryl Esters

REAVEN, E. P., Tsai, L., & Azhar, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.27.16208 · Cited by 118 · see citing works

Latrunculins—novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D

Spector, I., Shochet, N. R., Blasberger, D., & Kashman, Y. (1989) · Cell Motility · doi:10.1002/cm.970130302 · Cited by 580 · see citing works

TOTAL SYNTHESIS OF THE LATRUNCULINS: MACROLIDE MARINE TOXINS (LATRUNCULIA MAGNIFICA)

Zibuck, R. (1986) · Scholarly Commons (University of Pennsylvania)

Latrunculin, a new 2-thiazolidinone macrolide from the marine sponge

Kashman, Y., Groweiss, A., & Shmueli, U. (1980) · Tetrahedron Letters · doi:10.1016/0040-4039(80)80255-3 · Cited by 164 · see citing works

ChemInform Abstract: Chemistry of Latrunculins A and B.

Blasberger, D., Carmely, S., Cojocaru, M., Spector, I., Shochet, N. R., & Kashman, Y. (1990) · ChemInform · doi:10.1002/chin.199011343

Marine toxins of Latrunculia magnifica

Groweiss, A., Shmueli, U., & Kashman, Y. (1983) · The Journal of Organic Chemistry · doi:10.1021/jo00168a028 · Cited by 96 · see citing works