ADF/Cofilin: a functional node in cell biology
Open accessAbstract
Recent findings have significantly expanded our understanding of the regulation of actin-depolymerizing factor (ADF)/cofilin proteins and the profound multifaceted impact that these well-established regulators of actin dynamics have on cell biology. In this review we discuss new aspects of previously documented regulation, such as phosphorylation, but also cover novel recently established modes of regulation and functions of ADF (also known as destrin)/cofilin. We now understand that their activity responds to a vast array of inputs far greater than previously appreciated and that these proteins not only feed back to the crucially important dynamics of actin, but also to apoptosis cascades, phospholipid metabolism, and gene expression. We argue that this ability to respond to physiological changes by modulating those same changes makes the ADF/cofilin protein family a homeostatic regulator or 'functional node' in cell biology.
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The diffusion of WT and S3A cofilin, but not S3E cofilin, in the resting state was significantly impeded by their binding to F-actins.
“These findings suggest that the diffusion of WT or S3A cofilin, but not S3E cofilin, was significantly impeded by their binding to F-actins1326.”
From State-dependent diffusion of actin-depolymerizing factor/cofilin underlies the enlargement and shrinkage of dendritic spines (2016) · cites this paper as [13]
The ‘Phosphorylation of Ser3’ section states that Ser3 phosphorylation inhibits cofilin binding to F-actin, and the pH-regulation section identifies S3A as a mutant that cannot be inactivated by phosphorylation (page numbers unavailable). These passages support the proposed binding distinction, but the paper does not report diffusion measurements or the claimed significant difference among WT, S3A and S3E cofilin in resting cells. (LLM, conf=0.83)
Experimental — accuracy not yet measuredCofilin is a highly abundant actin-regulatory protein that binds to and alters the physical properties of F-actin.
“Cofilin is a highly abundant actin-regulatory protein, which binds to and alters the physical properties of F-actin1314.”
From State-dependent diffusion of actin-depolymerizing factor/cofilin underlies the enlargement and shrinkage of dendritic spines (2016) · cites this paper as [13]
The Modulation of actin dynamics section says cofilin regulates actin filaments and, when bound at high ratios, stabilizes F-actin in a twisted form. The Distribution section calls cofilin-1 the most ubiquitous form, but does not establish that cofilin is highly abundant; ubiquity is not the same as abundance. Page numbers are unavailable in our copy. (LLM, conf=0.83)
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Cites
Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
Ridley, A. J. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.08.006 · Cited by 1,180 · see citing works
Proteins of the ADF/Cofilin Family: Essential Regulators of Actin Dynamics
Bamburg, J. R. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.185 · Cited by 1,015 · see citing works
Self-citationRate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments.
Pollard, T. D. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2747 · Cited by 893 · see citing works
Andrianantoandro, E., & Pollard, T. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.006 · Cited by 710 · see citing works
Crystal Structure of Arp2/3 Complex
Robinson, R. C., Turbedsky, K., Kaiser, D. A., Marchand, J.-B., Higgs, H. N., Choe, S., & Pollard, T. D. (2001) · Science · doi:10.1126/science.1066333 · Cited by 540 · see citing works
Ginsberg, M. H., Partridge, A. W., & Shattil, S. J. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.08.010 · Cited by 415 · see citing works
Kuhn, J. R., & Pollard, T. D. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.047399 · Cited by 399 · see citing works
Minamide, L. S., Striegl, A. M., Boyle, J. A., Meberg, P. J., & Bamburg, J. R. (2000) · Nature Cell Biology · doi:10.1038/35023579 · Cited by 394 · see citing works
Self-citationHotulainen, P., Paunola, E., Vartiainen, M. K., & Lappalainen, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0555 · Cited by 384 · see citing works
Oser, M. G., Yamaguchi, H., Mader, C. C., Bravo‐Cordero, J. J., Arias, M., Chen, X., DesMarais, V. M., van Rheenen, J., Koleske, A. J., & Condeelis, J. S. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200812176 · Cited by 369 · see citing works
Lim kinases, regulators of actin dynamics
Bernard, O. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.11.011 · Cited by 344 · see citing works
Cofilin phosphatases and regulation of actin dynamics
Huang, T. Y., DerMardirossian, C. M., & Bokoch, G. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.11.005 · Cited by 339 · see citing works
Mechanism of Interaction of Acanthamoeba Actophorin (ADF/Cofilin) with Actin Filaments
Blanchoin, L., & Pollard, T. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15538 · Cited by 335 · see citing works
Ins and outs of ADF/cofilin activity and regulation
Van Troys, M., Huyck, L., Leyman, S., Dhaese, S., Vandekerkhove, J., & Ampe, C. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.04.001 · Cited by 329 · see citing works
Mitochondrial translocation of cofilin is an early step in apoptosis induction
Chua, B. T., Volbracht, C., Tan, K. O., Li, R., Yu, V. C. K., & Li, P. (2003) · Nature Cell Biology · doi:10.1038/ncb1070 · Cited by 315 · see citing works
Yoder, A., Yu, D., Dong, L., Iyer, S. R., Xu, X., Kelly, J., Liu, J., Wang, W., Vorster, P. J., Agulto, L., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.036 · Cited by 297 · see citing works
Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
Hawkins, M., Pope, B. J., Maciver, S. K., & Weeds, A. G. (1993) · Biochemistry · doi:10.1021/bi00089a014 · Cited by 277 · see citing works
Structural Plasticity in Actin and Tubulin Polymer Dynamics
Kueh, H. Y., & Mitchison, T. J. (2009) · Science · doi:10.1126/science.1168823 · Cited by 270 · see citing works
Sequential Regulation of DOCK2 Dynamics by Two Phospholipids During Neutrophil Chemotaxis
Nishikimi, A., Fukuhara, H., Su, W., Hongu, T., Takasuga, S., Mihara, H., Cao, Q., Sanematsu, F., Kanai, M., Hasegawa, H., et al. (2009) · Science · doi:10.1126/science.1170179 · Cited by 268 · see citing works
pH control of actin polymerization by cofilin.
Yonezawa, N., Nishida, E., & Sakai, H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38580-0 · Cited by 261 · see citing works
How is actin polymerization nucleated in vivo?
Condeelis, J. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02008-6 · Cited by 258 · see citing works
Coronin 1B Coordinates Arp2/3 Complex and Cofilin Activities at the Leading Edge
Cai, L., Marshall, T. W., Uetrecht, A. C., Schafer, D. A., & Bear, J. E. (2007) · Cell · doi:10.1016/j.cell.2007.01.031 · Cited by 244 · see citing works
Specification of Actin Filament Function and Molecular Composition by Tropomyosin Isoforms
Bryce, N. S., Schevzov, G., Ferguson, V., Percival, J. M., Lin, J. J., Matsumura, F., Bamburg, J. R., Jeffrey, P. L., Hardeman, E. C., Gunning, P. W., et al. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-04-0244 · Cited by 242 · see citing works
Self-citationOxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
Klamt, F., Zdanov, S., Levine, R. L., Pariser, A. C., Zhang, Y., Zhang, B., Yu, L., Veenstra, T. D., & Shacter, E. B. (2009) · Nature Cell Biology · doi:10.1038/ncb1968 · Cited by 241 · see citing works
Eiseler, T., Döppler, H. R., Yan, I. K., Kitatani, K., Mizuno, K., & Störz, P. (2009) · Nature Cell Biology · doi:10.1038/ncb1861 · Cited by 240 · see citing works
Gurniak, C. B., Perlas, E., & Witke, W. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.11.010 · Cited by 230 · see citing works
A GTPase-independent Mechanism of p21-activated Kinase Activation
Bokoch, G., Reilly, A. M., Daniels, R. H., King, C. C., Olivera, A., Spiegel, S., & Knaus, U. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.14.8137 · Cited by 212 · see citing works
Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover
Moriyama, K., & Yahara, I. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.8.1591 · Cited by 211 · see citing works
Ono, S. (2003) · Biochemistry · doi:10.1021/bi034600x · Cited by 211 · see citing works
Cofilin Dissociates Arp2/3 Complex and Branches from Actin Filaments
Chan, C., Beltzner, C. C., & Pollard, T. D. (2009) · Current Biology · doi:10.1016/j.cub.2009.02.060 · Cited by 203 · see citing works
Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding
Frantz, C., Barreiro, G., Dominguez, L., Chen, X., Eddy, R. J., Condeelis, J. S., Kelly, M. J. S., Jacobson, M. P., & Barber, D. L. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200804161 · Cited by 199 · see citing works
Nagata-Ohashi, K., Ohta, Y., Goto, K., Chiba, S., Mori, R., Nishita, M., Ohashi, K., Kousaka, K., Iwamatsu, A., Niwa, R., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401136 · Cited by 198 · see citing works
Balcer, H. I., Goodman, A. L., Rodal, A. A., Smith, E. M., Kugler, J., Heuser, J. E., & Goode, B. L. (2003) · Current Biology · doi:10.1016/j.cub.2003.11.051 · Cited by 193 · see citing works
Reactive Oxygen Species Regulate a Slingshot-Cofilin Activation Pathway
Kim, J., Huang, T. Y., & Bokoch, G. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-02-0131 · Cited by 188 · see citing works
Actin-binding proteins take the reins in growth cones
Pak, C. W., Flynn, K. C., & Bamburg, J. R. (2008) · Nature reviews. Neuroscience · doi:10.1038/nrn2236 · Cited by 181 · see citing works
Self-citationKueh, H. Y., Charras, G., Mitchison, T. J., & Brieher, W. M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801027 · Cited by 179 · see citing works
Human gelsolin prevents apoptosis by inhibiting apoptotic mitochondrial changes via closing VDAC
Kusano, H., Shimizu, S., Koya, R. C., Fujita, H., Kamada, S., Kuzumaki, N., & Tsujimoto, Y. (2000) · Oncogene · doi:10.1038/sj.onc.1203868 · Cited by 174 · see citing works
Oxidation of Cofilin Mediates T Cell Hyporesponsiveness under Oxidative Stress Conditions
Klemke, M., Wabnitz, G. H., Funke, F., Funk, B., Kirchgessner, H., & Samstag, Y. (2008) · Immunity · doi:10.1016/j.immuni.2008.06.016 · Cited by 162 · see citing works
Determining the differences in actin binding by human ADF and cofilin 1 1Edited by J. Karn
Yeoh, S., Pope, B. J., Mannherz, H. G., & Weeds, A. G. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5280 · Cited by 160 · see citing works
Nuclear actin and actin‐binding proteins in the regulation of transcription and gene expression
Zheng, B., Han, M., Bernier, M., & Wen, J. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06986.x · Cited by 152 · see citing works
Coronin Switches Roles in Actin Disassembly Depending on the Nucleotide State of Actin
Gandhi, M., Achard, V., Blanchoin, L., & Goode, B. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.029 · Cited by 147 · see citing works
HIV-1 Nef Interferes with Host Cell Motility by Deregulation of Cofilin
Stolp, B., Reichman‐Fried, M., Abraham, L., Pan, X., Giese, S. I., Hannemann, S., Goulimari, P., Raz, E., Grosse, R., & Fackler, O. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.06.004 · Cited by 141 · see citing works
Rosso, S. B., Bollati, F. A., Bisbal, M., Peretti, D., Sumi, T., Nakamura, T., Quiroga, S., Ferreira, A., & Cáceres, A. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-05-0328 · Cited by 135 · see citing works
Solution Structure of Human Cofilin
Pope, B. J., Zierler-Gould, K. M., Kühne, R., Weeds, A. G., & Ball, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310148200 · Cited by 135 · see citing works
SynGAP Regulates Steady-State and Activity-Dependent Phosphorylation of Cofilin
Carlisle, H. J., Manzerra, P., Marcora, E., & Kennedy, M. B. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4695-08.2008 · Cited by 128 · see citing works
Identification of an upstream regulatory pathway controlling actin-mediated apoptosis in yeast
Gourlay, C. W., & Ayscough, K. R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02337 · Cited by 127 · see citing works
Bernstein, B. W., Chen, H. A., Boyle, J. A., & Bamburg, J. R. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00066.2006 · Cited by 123 · see citing works
Self-citationPeterburs, P., Heering, J., Link, G., Pfizenmaier, K., Olayioye, M. A., & Haußer, A. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0718 · Cited by 116 · see citing works
Okada, K., Blanchoin, L., Abe, H., Chen, H., Pollard, T. D., & Bamburg, J. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203111200 · Cited by 109 · see citing works
Self-citationInteraction of epithelial ion channels with the actin-based cytoskeleton
Mazzochi, C., Benos, D. J., & Smith, P. R. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00195.2006 · Cited by 104 · see citing works
Direct stimulation of receptor‐controlled phospholipase D1 by phospho‐cofilin
Han, L., Stope, M. B., de Jesús, M. L., Weernink, P. A. O., Urban, M., Wieland, T., Rosskopf, D., Mizuno, K., Jakobs, K. H., & Schmidt, M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601852 · Cited by 99 · see citing works
Modulation of the Actin Cytoskeleton via Gelsolin Regulates Vacuolar H+-ATPase Recycling
Beaulieu, V., Silva, N. D., Pastor‐Soler, N. M., Brown, C. R., Smith, P. J., Brown, D., & Breton, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412750200 · Cited by 98 · see citing works
Gorbatyuk, V., Nosworthy, N. J., Robson, S. A., Bains, N. P. S., Maciejewski, M. W., dos Remedios, C. G., & King, G. F. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.10.007 · Cited by 97 · see citing works
Ikeda, S. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg112 · Cited by 97 · see citing works
As functional nuclear actin comes into view, is it globular, filamentous, or both?
Pederson, T. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709082 · Cited by 95 · see citing works
Alberts, P., Rudge, R. E., Irinopoulou, T., Danglot, L., Gauthier‐Rouvière, C., & Galli, T. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0643 · Cited by 94 · see citing works
Whiteman, I. T., Gervasio, O. L., Cullen, K. M., Guillemin, G. J., Jeong, E. V., Witting, P. K., Antao, S. T., Minamide, L. S., Bamburg, J. R., & Goldsbury, C. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3531-09.2009 · Cited by 92 · see citing works
Self-citationADF/Cofilin weakens lateral contacts in the actin filament 1 1Edited by P. E. Wright
McGough, A. M., & Chiu, W. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2968 · Cited by 92 · see citing works
Phagocyte cell migration is mediated by phospholipases PLD1 and PLD2
Lehman, N., Fulvio, M. D., McCray, N., Campos, I., Tabatabaian, F., & Gómez-Cambronero, J. (2006) · Blood · doi:10.1182/blood-2006-02-005959 · Cited by 91 · see citing works
Mitochondrial shuttling of CAP1 promotes actin- and cofilin-dependent apoptosis
Wang, C., Zhou, G.-L., Vedantam, S., Li, P., & Field, J. M. (2008) · Journal of Cell Science · doi:10.1242/jcs.023911 · Cited by 89 · see citing works
Huang, T. Y., Minamide, L. S., Bamburg, J. R., & Bokoch, G. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.09.017 · Cited by 89 · see citing works
Self-citationYap, C. T., Simpson, T. I., Pratt, T., Price, D. J., & Maciver, S. K. (2005) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20053 · Cited by 89 · see citing works
Abramovici, H., Mojtabaie, P., Parks, R. J., Zhong, X.-P., Koretzky, G. A., Topham, M. K., & Gee, S. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1248 · Cited by 79 · see citing works
Human Cofilin Forms Oligomers Exhibiting Actin Bundling Activity
Pfannstiel, J., Cyrklaff, M., Habermann, A., Stoeva, S., Griffiths, G. W., Shoeman, R. L., & Faulstich, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104760200 · Cited by 79 · see citing works
Regulation of actin function by protein kinase A‐mediated phosphorylation of Limk1
Nadella, K. S., Saji, M., Jacob, N. K., Pavel, E., Ringel, M. D., & Kirschner, L. S. (2009) · EMBO Reports · doi:10.1038/embor.2009.58 · Cited by 78 · see citing works
Dynamic stabilization of actin filaments
Kueh, H. Y., Brieher, W. M., & Mitchison, T. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807394105 · Cited by 72 · see citing works
Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization
Orlova, A., Shvetsov, A., Galkin, V. E., Kudryashov, D. S., Rubenstein, P. A., Egelman, E. H., & Reisler, E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407525102 · Cited by 71 · see citing works
Yoo, Y., Ho, H. J., Wang, C., & Guan, J. (2009) · Oncogene · doi:10.1038/onc.2009.319 · Cited by 70 · see citing works
Microtubule-actomyosin interactions in cortical flow and cytokinesis
Mandato, C. A., Benink, H. A., & Bement, W. M. (2000) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(200002)45:2 · Cited by 69 · see citing works
Cofilin (ADF) Affects Lateral Contacts in F-actin
Bobkov, A. A., Mühlrád, A., Shvetsov, A., Benchaar, S. A., Scoville, D., Almo, S. C., & Reisler, E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.014 · Cited by 64 · see citing works
Davis, R. C., Maloney, M. T., Minamide, L. S., Flynn, K. C., Stonebraker, M. A., & Bamburg, J. R. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1122 · Cited by 63 · see citing works
Self-citationACTIN DEPOLYMERIZING FACTOR9 controls development and gene expression in Arabidopsis
Burgos‐Rivera, B., Ruzicka, D. R., Deal, R. B., McKinney, E. C., King-Reid, L., & Meagher, R. B. (2008) · Plant Molecular Biology · doi:10.1007/s11103-008-9398-1 · Cited by 61 · see citing works
Johne, C., Matenia, D., Li, X., Timm, T., Balusamy, K., & Mandelkow, E. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-07-0730 · Cited by 60 · see citing works
Bamburg, J. R., & Bernstein, B. W. (2008) · Current Biology · doi:10.1016/j.cub.2008.02.002 · Cited by 57 · see citing works
Self-citationTropomyosin and ADF/Cofilin as Collaborators and Competitors
Kuhn, T. B., & Bamburg, J. R. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-85766-4_18 · Cited by 56 · see citing works
Self-citationGoeckeler, Z. M., & Wysolmerski, R. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503173200 · Cited by 56 · see citing works
Actopaxin Interacts with TESK1 to Regulate Cell Spreading on Fibronectin
LaLonde, D. P., Brown, M. C., Bouverat, B. P., & Turner, C. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500752200 · Cited by 53 · see citing works
Regulation of the Epithelial Na+ /H+ Exchanger Isoform by the Cytoskeleton
Szászi, K., Grinstein, S., Orlowski, J., & Kapùs, A. (2000) · Cellular Physiology and Biochemistry · doi:10.1159/000016358 · Cited by 52 · see citing works
Minamide, L. S., Painter, W. B., Schevzov, G., Gunning, P. W., & Bamburg, J. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8303 · Cited by 49 · see citing works
Self-citationCoronin 2A regulates a subset of focal-adhesion-turnover events through the cofilin pathway
Marshall, T. W., Aloor, H. L., & Bear, J. E. (2009) · Journal of Cell Science · doi:10.1242/jcs.051482 · Cited by 41 · see citing works
Inorganic phosphate regulates the binding of cofilin to actin filaments
Mühlrád, A., Pavlov, D., Peyser, Y. M., & Reisler, E. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05169.x · Cited by 36 · see citing works
Bubb, M., Baines, I., & Korn, E. D. (1998) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(1998)39:2 · Cited by 35 · see citing works
Self-citationApoptosis and autophagy in rat cerebellar granule neuron death: Role of reactive oxygen species
Maycotte, P., Guemez‐Gamboa, A., & Morán, J. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22168 · Cited by 34 · see citing works
Noda, Y., & Sasaki, S. (2007) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-007-0404-2 · Cited by 32 · see citing works
Unbalancing the Phosphatidylinositol-4,5-bisphosphate–Cofilin Interaction Impairs Cell Steering
Leyman, S., Sidani, M., Ritsma, L., Waterschoot, D., Eddy, R. J., Dewitte, D., Debeir, O., Decaestecker, C., Vandekerckhove, J. S., van Rheenen, J., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-02-0121 · Cited by 28 · see citing works
Severing of F-actin by yeast cofilin is pH-independent
Pavlov, D., Mühlrád, A., Cooper, J. A., Wear, M. A., & Reisler, E. (2006) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20142 · Cited by 24 · see citing works
Becker, B. E., & Gard, D. L. (2000) · Cell Motility and the Cytoskeleton · doi:10.1002/1097-0169(200012)47:4 · Cited by 13 · see citing works
Flagged first, then by citations
Research works printed but not linked: 7
- [23]Bamburg JR Bernstein BW 2008 ADF/cofilin Curr Biol 18 R273 R275 18397729
- [36]Goeckeler ZM Wysolmerski RB 2005 Myosin phosphatase and cofilin mediate cAMP/PKA-induced decline in endothelial cell isometric tension and myosin II RLC phosphorylation J Biol Chem 280 33083 33095 16055445
- [37]Meberg PJ 1998 Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension Cell Motil Cytoskeleton 39 172 190 9484959
- [44]Bernstein BW 2000 Intracellular pH modulation of ADF/cofilin proteins Cell Motil Cytoskeleton 47 319 336 11093252
- [57]Freeman NL Field J 2000 Mammalian homolog of the yeast cyclase associated protein, CAP/Srv2p, regulates actin filament assembly Cell Motil Cytoskeleton 45 106 120 10658207
- [63]McGough A Chiu W 1999 ADF/cofilin weakens lateral contacts in the actin filament J Mol Biol 291 513 519 10448032
- [87]Pavlov D 2006 Severing of F-actin by yeast cofilin is pH-independent Cell Motil Cytoskeleton 63 533 542 16847879 PMC2583072
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Actin Dynamics, Architecture, and Mechanics in Cell Motility
Blanchoin, L., Boujemaa‐Paterski, R., Sykes, C., & Plastino, J. (2014) · Physiological Reviews · doi:10.1152/physrev.00018.2013 · Cited by 1,468 · see citing works
Dominguez, R., & Holmes, K. C. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155359 · Cited by 1,211 · see citing works
pH sensing and regulation in cancer
Damaghi, M., Wojtkowiak, J. W., & Gillies, R. J. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00370 · Cited by 532 · see citing works
Functions of cofilin in cell locomotion and invasion
Bravo‐Cordero, J. J., Magalhães, M. A. O., Eddy, R. J., Hodgson, L., & Condeelis, J. S. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3609 · Cited by 462 · see citing works
Dynamics of the Rho-family small GTPases in actin regulation and motility
Spiering, D., & Hodgson, L. (2011) · Cell Adhesion & Migration · doi:10.4161/cam.5.2.14403 · Cited by 446 · see citing works
Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation
Mizuno, K. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2012.11.001 · Cited by 396 · see citing works
Raven, F., Van der Zee, E. A., Meerlo, P., & Havekes, R. (2018) · Sleep Medicine Reviews · doi:10.1016/j.smrv.2017.05.002 · Cited by 331 · 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
Self-citationCapping protein regulators fine-tune actin assembly dynamics
Edwards, M. A., Zwolak, A., Schafer, D. A., Sept, D., Domínguez, R., & Cooper, J. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3869 · Cited by 299 · see citing works
Update on GLUT4 Vesicle Traffic: A Cornerstone of Insulin Action
Jaldín‐Fincati, J. R., Pavarotti, M. A., Frendo‐Cumbo, S., Bilan, P. J., & Klip, A. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.05.002 · Cited by 276 · see citing works
Signaling networks of Rho GTPases in cell motility
Hanna, S. J., & El‐Sibai, M. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.04.009 · Cited by 275 · see citing works
Schmidt, M., Dekker, F. J., & Maarsingh, H. (2013) · Pharmacological Reviews · doi:10.1124/pr.110.003707 · Cited by 268 · see citing works
Wioland, H., Guichard, B., Senju, Y., Myram, S., Lappalainen, P., Jegou, A. G., & Romet‐Lemonne, G. (2017) · Current Biology · doi:10.1016/j.cub.2017.05.048 · Cited by 258 · see citing works
Nawaz, S., Sánchez, P., Schmitt, S., Snaidero, N., Mitkovski, M., Velte, C., Brückner, B., Alexopoulos, I., Czopka, T., Jung, S. Y., et al. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.05.013 · Cited by 214 · see citing works
Petrovska, I., Nüske, E., Munder, M. C., Kulasegaran, G., Malinovska, L., Kroschwald, S., Richter, D., Fahmy, K., Gibson, K. H., Verbavatz, J., et al. (2014) · eLife · doi:10.7554/elife.02409 · Cited by 248 · see citing works
Remodeling of actin filaments by ADF/cofilin proteins
Galkin, V. E., Orlova, A., Kudryashov, D. S., Solodukhin, A. S., Reisler, E., Schroeder, G. F., & Egelman, E. H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110109108 · Cited by 234 · see citing works
New mechanisms and functions of actin nucleation
Firat‐Karalar, E. N., & Welch, M. D. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.10.007 · Cited by 233 · see citing works
Growth Cone Travel in Space and Time: the Cellular Ensemble of Cytoskeleton, Adhesion, and Membrane
Vitriol, E. A., & Zheng, J. Q. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.005 · Cited by 229 · see citing works
Sommer, G., Rossa, C., Chi, A. C., Neville, B. W., & Heise, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025402 · Cited by 228 · see citing works
Analysis of turnover dynamics of the submembranous actin cortex
Fritzsche, M., Lewalle, A., Duke, T., Kruse, K., & Charras, G. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-06-0485 · Cited by 226 · see citing works
GABA promotes the competitive selection of dendritic spines by controlling local Ca2+ signaling
Hayama, T., Noguchi, J., Watanabe, S., Takahashi, N., Hayashi-Takagi, A., Ellis-Davies, G. C. R., Matsuzaki, M., & Kasai, H. (2013) · Nature Neuroscience · doi:10.1038/nn.3496 · Cited by 193 · see citing works
ADF/Cofilin-Mediated Actin Retrograde Flow Directs Neurite Formation in the Developing Brain
Flynn, K. C., Hellal, F., Neukirchen, D., Jacob, S., Tahirović, S., Dupraz, S., Stern, S., Garvalov, B. K., Gurniak, C. B., Shaw, A. E., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.09.038 · Cited by 202 · see citing works
Self-citationStructural basis for cofilin binding and actin filament disassembly
Tanaka, K., Takeda, S., Mitsuoka, K., Oda, T., Kimura-Sakiyama, C., Maéda, Y., & Narita, A. (2018) · Nature Communications · doi:10.1038/s41467-018-04290-w · Cited by 195 · see citing works
LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity
Parisiadou, L., Yu, J. H., Sgobio, C., Xie, C., Liu, G., Sun, L., Gu, X., Lin, X. Z., Crowley, N. A., Lovinger, D. M., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3636 · Cited by 201 · see citing works
Long-range self-organization of cytoskeletal myosin II filament stacks
Hu, S., Dasbiswas, K., Guo, Z., Tee, Y.-H., Thiagarajan, V., Hersen, P., Chew, T., Safran, S. A., Zaidel‐Bar, R., & Bershadsky, A. D. (2017) · Nature Cell Biology · doi:10.1038/ncb3466 · Cited by 183 · see citing works
Actin dynamics and turnover in cell motility
Rottner, K., & Stradal, T. E. B. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.07.003 · Cited by 190 · see citing works
Roles of ADF/cofilin in actin polymerization and beyond
Bamburg, J. R., & Bernstein, B. W. (2010) · F1000 Biology Reports · doi:10.3410/b2-62 · Cited by 189 · see citing works
Self-citationActin dynamics and cofilin‐actin rods in alzheimer disease
Bamburg, J. R., & Bernstein, B. W. (2016) · Cytoskeleton · doi:10.1002/cm.21282 · Cited by 181 · see citing works
Self-citationSpine dynamics in the brain, mental disorders and artificial neural networks
Kasai, H., Ziv, N. E., Okazaki, H., Yagishita, S., & Toyoizumi, T. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00467-3 · Cited by 180 · see citing works
Actin Out: Regulation of the Synaptic Cytoskeleton
Spence, E. F., & Soderling, S. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.655118 · Cited by 171 · see citing works
3D scaffolds in breast cancer research
Rijal, G., & Li, W. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2015.12.016 · Cited by 169 · see citing works
Actin kinetics shapes cortical network structure and mechanics
Fritzsche, M., Erlenkämper, C., Moeendarbary, E., Charras, G., & Kruse, K. (2016) · Science Advances · doi:10.1126/sciadv.1501337 · Cited by 170 · see citing works
Ngo, K. X., Kodera, N., Katayama, E., Ando, T., & Uyeda, T. Q. P. (2015) · eLife · doi:10.7554/elife.04806 · Cited by 168 · see citing works
Paving the Rho in cancer metastasis: Rho GTPases and beyond
Jansen, S. R., Gosens, R., Wieland, T., & Schmidt, M. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.09.002 · Cited by 169 · see citing works
Internetwork competition for monomers governs actin cytoskeleton organization
Suarez, C., & Kovar, D. R. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.106 · Cited by 164 · see citing works
Schönichen, A., Webb, B. A., Jacobson, M. P., & Barber, D. L. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-050511-102349 · Cited by 162 · see citing works
Microtubules and actin crosstalk in cell migration and division
Akhshi, T. K., Wernike, D., & Piekny, A. J. (2013) · Cytoskeleton · doi:10.1002/cm.21150 · Cited by 157 · see citing works
Review of PIP2 in Cellular Signaling, Functions and Diseases
Mandal, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218342 · Cited by 160 · see citing works
Cofilin cooperates with fascin to disassemble filopodial actin filaments
Breitsprecher, D., Koestler, S. A., Chizhov, I. V., Némethová, M., Mueller, J. O., Goode, B. L., Small, J. V., Rottner, K., & Faix, J. (2011) · Journal of Cell Science · doi:10.1242/jcs.086934 · Cited by 159 · see citing works
Poukkula, M., Kremneva, E., Serlachius, M., & Lappalainen, P. (2011) · Cytoskeleton · doi:10.1002/cm.20530 · Cited by 152 · see citing works
Multiple degradation pathways regulate versatile CIP/KIP CDK inhibitors
Starostina, N. G., & Kipreos, E. T. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.004 · Cited by 147 · see citing works
Millan, M. J. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.004 · Cited by 146 · see citing works
Yu, X., Yi, Z., Gao, Z., Qin, D., Zhai, Y., Chen, X., Ouyang, Y., Wang, Z., Zheng, P., Zhu, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms5887 · Cited by 145 · see citing works
FMNL formins boost lamellipodial force generation
Kage, F., Winterhoff, M., Dimchev, V., Mueller, J. O., Thalheim, T., Freise, A., Brühmann, S., Kollasser, J., Block, J., Dimchev, G. A., et al. (2017) · Nature Communications · doi:10.1038/ncomms14832 · Cited by 143 · see citing works
Luo, D., Wilson, J. M., Harvel, N., Liu, J., Pei, L., Huang, S., Hawthorn, L., & Shi, H. (2013) · Journal of Translational Medicine · doi:10.1186/1479-5876-11-57 · Cited by 142 · see citing works
Chen, L. Y., Rex, C. S., Babayan, A. H., Kramár, E. A., LYNCH, G. S., Gall, C. M., & Lauterborn, J. C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1077-10.2010 · Cited by 135 · see citing works
The cytoskeleton and neurite initiation
Flynn, K. C. (2013) · BioArchitecture · doi:10.4161/bioa.26259 · Cited by 137 · see citing works
Kommaddi, R. P., Das, D., Karunakaran, S., Nanguneri, S., Bapat, D., Ray, A., Shaw, E., Bennett, D. A., Nair, D., & Ravindranath, V. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.2127-17.2017 · Cited by 135 · see citing works
Redox regulation of the actin cytoskeleton and its role in the vascular system
Xu, Q., Huff, L. P., Fujii, M., & Griendling, K. K. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.03.004 · Cited by 129 · see citing works
Park, C. K., & Horton, N. C. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00602-6 · Cited by 128 · see citing works
Bamburg, J. R., Minamide, L. S., Wiggan, O., Tahtamouni, L. H., & Kuhn, T. B. (2021) · Cells · doi:10.3390/cells10102726 · Cited by 122 · see citing works
Self-citationMEDYAN: mechanochemical simulations of contraction and polarity alignment in actomyosin networks
Popov, K., Komianos, J., & Papoian, G. A. (2016) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004877 · Cited by 104 · see citing works
Zheng, K., Xiang, Y., Wang, X., Wang, Q., Zhong, M., Wang, S., Wang, X., Fan, J., Kitazato, K., & Wang, Y. (2014) · mBio · doi:10.1128/mbio.00958-13 · Cited by 118 · see citing works
Roles of cofilin in development and its mechanisms of regulation
Ohashi, K. (2015) · Development Growth & Differentiation · doi:10.1111/dgd.12213 · Cited by 118 · see citing works
Henty, J. L., Bledsoe, S. W., Khurana, P., Meagher, R. B., Day, B., Blanchoin, L., & Staiger, C. J. (2011) · The Plant Cell · doi:10.1105/tpc.111.090670 · Cited by 117 · see citing works
Common Regulatory Pathways Mediate Activity of MicroRNAs Inducing Cardiomyocyte Proliferation
Torrini, C., Cubero, R. J., Dirkx, E., Braga, L., Ali, H., Prosdocimo, G., Gutiérrez, M. I., Collesi, C., Licastro, D., Zentilin, L., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.005 · Cited by 116 · see citing works
How filopodia pull: What we know about the mechanics and dynamics of filopodia
Bornschlögl, T. (2013) · Cytoskeleton · doi:10.1002/cm.21130 · Cited by 115 · see citing works
F-actin dismantling through a redox-driven synergy between Mical and cofilin
Grintsevich, E. E., Yesilyurt, H. G., Rich, S. K., Hung, R., Terman, J. R., & Reisler, E. (2016) · Nature Cell Biology · doi:10.1038/ncb3390 · Cited by 115 · see citing works
The role of small GTPases in neuronal morphogenesis and polarity
González-Billault, C. E., Muñoz-LLancao, P., Henríquez, D. R., Wojnacki, J., Conde, C. B., & Cáceres, A. (2012) · Cytoskeleton · doi:10.1002/cm.21034 · Cited by 112 · see citing works
Cofilin-1 and Other ADF/Cofilin Superfamily Members in Human Malignant Cells
Ss, S., Еремина, Л. С., Pashintseva, N. V., Ковалев, Л. И., & Ковалева, М. А. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms18010010 · Cited by 114 · see citing works
Actin-based growth cone motility and guidance
Omotade, O. F., Pollitt, S. L., & Zheng, J. Q. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.03.001 · Cited by 110 · see citing works
Eph receptors and ephrins in neuron–astrocyte communication at synapses
Murai, K. K., & Pasquale, E. B. (2011) · Glia · doi:10.1002/glia.21226 · Cited by 109 · see citing works
Cofilin: a redox sensitive mediator of actin dynamics during T‐cell activation and migration
Samstag, Y., John, I., & Wabnitz, G. H. (2013) · Immunological Reviews · doi:10.1111/imr.12115 · Cited by 108 · see citing works
Chen, C., Krishnan, R., Zhou, E. H., Ramachandran, A., Tambe, D. T., Rajendran, K., Adam, R. M., Deng, L., & Fredberg, J. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012035 · Cited by 108 · see citing works
ADF/cofilin: a crucial regulator of synapse physiology and behavior
Rust, M. B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1941-z · Cited by 104 · see citing works
Gudheti, M. V., Curthoys, N. M., Gould, T. J., Kim, D., Gunewardene, M. S., Gabor, K. A., Gosse, J. A., Kim, C. H., Zimmerberg, J., & Hess, S. T. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.03.054 · Cited by 106 · see citing works
Zheng, Y., Xie, Y., Jiang, Y., Qu, X., & Huang, S. (2013) · The Plant Cell · doi:10.1105/tpc.113.117820 · Cited by 106 · see citing works
Chaudhry, F., Breitsprecher, D., Little, K., Sharov, G., Sokolova, O. S., & Goode, B. L. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-08-0589 · Cited by 105 · see citing works
Freeman, S. A., Lei, V. J., Dang-Lawson, M., Mizuno, K., Roskelley, C. D., & Gold, M. R. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1102233 · Cited by 103 · see citing works
Biophysics of actin filament severing by cofilin
Elam, W. A., Kang, H., & Cruz, E. M. D. L. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.062 · Cited by 102 · see citing works
Narayanan, P., Chatterton, P., Ikeda, A., Ikeda, S., Corey, D. P., Ervasti, J. M., & Perrin, B. J. (2015) · Nature Communications · doi:10.1038/ncomms7855 · Cited by 100 · see citing works
Torsional stress generated by ADF/cofilin on cross-linked actin filaments boosts their severing
Wioland, H., Jegou, A. G., & Romet‐Lemonne, G. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1812053116 · Cited by 99 · see citing works
Woo, J. A., Zhao, X., Khan, H., Penn, C., Wang, X., Joly-Amado, A., Weeber, E., Morgan, D., & Kang, D. E. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.5 · Cited by 99 · see citing works
Non-coding RNA therapeutics for cardiac regeneration
Braga, L., Ali, H., Secco, I., & Giacca, M. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa071 · Cited by 97 · see citing works
Under construction: The dynamic assembly, maintenance, and degradation of the cardiac sarcomere
Martin, T. G., & Kirk, J. A. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.08.018 · Cited by 93 · see citing works
Cofilin Nuclear-Cytoplasmic Shuttling Affects Cofilin-Actin Rod Formation During Stress
Munsie, L. N., Desmond, C. R., & Truant, R. (2012) · Journal of Cell Science · doi:10.1242/jcs.097667 · Cited by 97 · see citing works
The subcortical maternal complex: multiple functions for one biological structure?
Bebbere, D., Masala, L., Albertini, D. F., & Ledda, S. (2016) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-016-0788-z · Cited by 96 · see citing works
Actin cytoskeleton in dendritic spine development and plasticity
Lei, W., Omotade, O. F., Myers, K. R., & Zheng, J. Q. (2016) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2016.04.010 · Cited by 94 · see citing works
Septin 9 Exhibits Polymorphic Binding to F-Actin and Inhibits Myosin and Cofilin Activity
Smith, C. A., Dolat, L., Angelis, D., Forgacs, E., Spiliotis, E. T., & Galkin, V. E. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.07.026 · Cited by 94 · see citing works
A RhoA Signaling Pathway Regulates Dendritic Golgi Outpost Formation
Quassollo, G., Wojnacki, J., Salas, D. A., Gastaldi, L., Marzolo, M., Conde, C. B., Bisbal, M., Couve, A., & Cáceres, A. (2015) · Current Biology · doi:10.1016/j.cub.2015.01.075 · Cited by 93 · see citing works
Sagar, Pröls, F., Wiegreffe, C., & Scaal, M. (2015) · Development · doi:10.1242/dev.115964 · Cited by 93 · see citing works
Global site-specific neddylation profiling reveals that NEDDylated cofilin regulates actin dynamics
Vogl, A. M., Phu, L., Becerra, R., Giusti, S. A., Verschueren, E., Hinkle, T. B., Bordenave, M. D., Adrian, M., Heidersbach, A. J., Yankilevich, P., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0370-3 · Cited by 88 · see citing works
Parallel global profiling of plant TOR dynamics reveals a conserved role for LARP1 in translation
Scarpin, M. R., Leiboff, S., & Brunkard, J. O. (2020) · eLife · doi:10.7554/elife.58795 · Cited by 90 · see citing works
Xu, K., & Nagy, P. D. (2016) · PLoS Biology · doi:10.1371/journal.pbio.2000128 · Cited by 91 · see citing works
Actin filaments—A target for redox regulation
Wilson, C., Terman, J. R., González-Billault, C. E., & Ahmed, G. (2016) · Cytoskeleton · doi:10.1002/cm.21315 · Cited by 87 · see citing works
A Computational Model of YAP/TAZ Mechanosensing
Sun, M., Spill, F., & Zaman, M. H. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.04.040 · Cited by 88 · see citing works
Liu, A., Zhou, Z., Dang, R., Zhu, Y., Qi, J., He, G., Leung, C., Pak, D. T. S., Jia, Z., & Xie, W. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201509023 · Cited by 87 · see citing works
Chen, X., Chen, Y., Wang, C., Jiang, Y., Chu, X., Wu, F., Wu, Y., Cai, X., Cao, Y., Liu, Y., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202107588 · Cited by 87 · see citing works
Hung, R., & Terman, J. R. (2011) · Cytoskeleton · doi:10.1002/cm.20527 · Cited by 87 · see citing works
Thioredoxin (Trx): A redox target and modulator of cellular senescence and aging-related diseases
Yang, B., Lin, Y., Huang, Y., Shen, Y.-Q., & Chen, Q. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103032 · Cited by 90 · see citing works
Cofilin-2 Controls Actin Filament Length in Muscle Sarcomeres
Kremneva, E., Makkonen, M., Skwarek‐Maruszewska, A., Gateva, G., Michelot, A., Domínguez, R., & Lappalainen, P. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.09.002 · Cited by 86 · see citing works
Bernstein, B. W., Shaw, A. E., Minamide, L. S., Pak, C. W., & Bamburg, J. R. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6020-11.2012 · Cited by 84 · see citing works
Self-citationCofilin1-dependent actin dynamics control DRP1-mediated mitochondrial fission
Rehklau, K., Hoffmann, L., Gurniak, C. B., Ott, M., Witke, W., Scorrano, L., Culmsee, C., & Rust, M. B. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.448 · Cited by 83 · see citing works
Tang, W., Zhang, Y., Xu, W., Harden, T. K., Sondek, J., Sun, L., Li, L., & Wu, D. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.10.023 · Cited by 83 · see citing works
Alhadidi, Q., & Shah, Z. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0432-7 · Cited by 83 · see citing works
Cofilin and Vangl2 cooperate in the initiation of planar cell polarity in the mouse embryo
Mahaffey, J. P., Grego‐Bessa, J., Liem, K. F., & Anderson, K. V. (2013) · Development · doi:10.1242/dev.085316 · Cited by 82 · see citing works
Wolf, M., Zimmermann, A.-M., Görlich, A., Gurniak, C. B., Sassoé‐Pognetto, M., Friauf, E., Witke, W., & Rust, M. B. (2014) · Cerebral Cortex · doi:10.1093/cercor/bhu081 · Cited by 81 · see citing works
Involvement of the Rho–mDia1 pathway in the regulation of Golgi complex architecture and dynamics
Zilberman, Y., Alieva, N. O., Miserey‐Lenkei, S., Lichtenstein, A., Kam, Z., Sabanay, H., & Bershadsky, A. D. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-01-0007 · Cited by 80 · see citing works
Koestler, S. A., Steffen, A., Némethová, M., Winterhoff, M., Luo, N., Holleboom, J. M., Krupp, J., Jacob, S., Vinzenz, M., Schur, F. K. M., et al. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-12-0857 · Cited by 79 · see citing works
Actin Bundles Dynamics and Architecture
Rajan, S., Kudryashov, D. S., & Reisler, E. (2023) · Biomolecules · doi:10.3390/biom13030450 · Cited by 78 · see citing works
- Authors
- Bernstein, B. W., & Bamburg, J. R.
- Affiliations
- Colorado State University (US)
- Corresponding author
- Bernstein, Barbara W.
- ORCID
- Bamburg, James R.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 20
- Issue
- 4
- Pages
- 187-195
- ISSN
- 0962-8924 (ISSN-L)
- PMC
- PMC2849908
- OpenAlex
- W2082024168
- Cited by
- 704
- References
- 87
- Citations by year
- 2026: 21 · 2025: 24 · 2024: 25 · 2023: 26 · 2022: 31 · 2021: 34 · 2020: 35 · 2019: 36 · 2018: 37 · 2017: 42 · 2016: 58 · 2015: 56 · 2014: 58 · 2013: 86 · 2012: 56
- FWCI
- 6.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Alzheimer's Drug Discovery Foundation
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (NS 40371, R01NS040371)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- ADF/cofilin, destrin, actin dynamics, actin depolymerizing factor, protein phosphorylation, apoptosis, phospholipid metabolism, gene expression regulation, homeostatic regulation
- MeSH terms
- Actins, Animals, Fibroblasts, Gene Expression Regulation, HeLa Cells, Humans, Models, Molecular, Neurons, Actin Depolymerizing Factors, Destrin, Mice
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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