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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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“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]
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“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]
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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 1,215
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
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 890
Andrianantoandro, E., & Pollard, T. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.006 · Cited by 710
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
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
Kuhn, J. R., & Pollard, T. D. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.047399 · Cited by 399
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
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
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
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Sorted by citations
Items 301–400 of 702
Dimethyloxalylglycine Promotes Bone Marrow Mesenchymal Stem Cell Osteogenesis via Rho/ROCK Signaling
Zhang, L., Jiang, G., Zhao, X., & Gong, Y. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000447843 · Cited by 25
Alhadidi, Q., Nash, K. M., Alaqel, S. I., Sayeed, M. S. B., & Shah, Z. A. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.04.036 · Cited by 25
N-terminal α-amino SUMOylation of cofilin-1 is critical for its regulation of actin depolymerization
Weng, W., Gu, X., Yang, Y., Zhang, Q., Deng, Q., Zhou, J., Cheng, J., Zhu, M. X., Feng, J., Huang, O., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41520-2 · Cited by 24
Ma, X., España‐Serrano, L., Kim, W.-J., Purayil, H. T., Nie, Z., & Daaka, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.511360 · Cited by 25
Choi, C., Patel, H., & Barber, D. L. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-12-1058 · Cited by 24
Wang, R., Wang, X., Wu, J., Ni, B., Wen, L.-B., Huang, L. P., Liao, Y., Tong, G., Ding, C., & Mao, X. (2016) · Virus Research · doi:10.1016/j.virusres.2016.09.005 · Cited by 24
Wu, Y., Zhu, Y., Zhang, Q., Xie, H., Yu, K., Xu, G.-J., & Li, S. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.313048 · Cited by 24
Leonard, A., Marando, C. M., Rahman, A., & Fazal, F. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00071.2013 · Cited by 24
Endosomal Actin Remodeling by Coronin-1A Controls Lipoprotein Uptake and Degradation in Macrophages
Hölttä‐Vuori, M., Vainio, S., Kauppi, M., Eck, M. V., Jokitalo, E., & Ikonen, E. (2012) · Circulation Research · doi:10.1161/circresaha.111.256842 · Cited by 24
Lang, A. E., Qu, Z., Schwan, C., Silván, U., Unger, A., Schoenenberger, C., Aktories, K., & Mannherz, H. G. (2016) · Cellular Microbiology · doi:10.1111/cmi.12636 · Cited by 24
Alhadidi, Q., Sayeed, M. S. B., & Shah, Z. A. (2017) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527316666170117115040 · Cited by 27
Characterization of Sarcocystis fayeri's actin‐depolymerizing factor as a toxin that causes diarrhea
Irikura, D., Saito, M., Sugita‐Konishi, Y., Ohnishi, T., Sugiyama, K., Watanabe, M., Yamazaki, A., Izumiyama, S., Sato, H., Kimura, Y., et al. (2017) · Genes to Cells · doi:10.1111/gtc.12515 · Cited by 24
Differential proteomic and phenotypic behaviour of papillary and anaplastic thyroid cell lines
Musso, R., Cara, G. D., Albanese, N. N., Marabeti, M. R., Cancemi, P., Martini, D., Orsini, E., Giordano, C. S. D. S., & Pucci‐Minafra, I. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.01.023 · Cited by 24
Insulin Receptor Substrate-4 Binds to Slingshot-1 Phosphatase and Promotes Cofilin Dephosphorylation
Homma, Y., Kanno, S., Sasaki, K., Nishita, M., Yasui, A., Asano, T., Ohashi, K., & Mizuno, K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.565945 · Cited by 24
Zafar, S., Younas, N., Sheikh, N., Tahir, W., Shafiq, M., Schmitz, M., Ferrer, I., Andréoletti, O., & Zerr, I. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0589-0 · Cited by 24
Deficiency of the clock gene Bmal1 affects neural progenitor cell migration
Ali, A. A. H., Schwarz‐Herzke, B., Mir, S., Sahlender, B., Victor, M. B., Görg, B., Schmuck, M. R., Dach, K., Fritsche, E., Kremer, A., et al. (2018) · Brain Structure and Function · doi:10.1007/s00429-018-1775-1 · Cited by 24
Investigation of adipocyte proteome during the differentiation of brown preadipocytes
Kamal, A. H. M., Kim, W. K., Cho, K., Park, A., Min, J., Han, B., Park, S. G., Lee, S. C., & Bae, K. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.10.005 · Cited by 23
BMPR-2 gates activity-dependent stabilization of primary dendrites during mitral cell remodeling
Aihara, S., Fujimoto, S., Sakaguchi, R., & Imai, T. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109276 · Cited by 25
Nguyen, M. T., & Lee, W. (2022) · Cells · doi:10.3390/cells11132030 · Cited by 23
Wen, R., Zhou, L., Jiang, S., Fan, H., Zheng, K., Yu, Y., Gao, X., Hao, L., Lou, Z., Yu, G., et al. (2023) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2023.03.067 · Cited by 23
Cazzaro, S., Woo, J. A., Wang, X., Liu, T., Rego, S., Kee, T. R., Koh, Y., Vázquez‐Rosa, E., Pieper, A. A., & Kang, D. E. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217128120 · Cited by 23
RNA interference of cofilin in Chinese hamster ovary cells improves recombinant protein productivity
Hammond, S., & Lee, K. H. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23322 · Cited by 24
Zeidan, A., Gan, X. T., Thomas, A., & Karmazyn, M. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1832-2 · Cited by 23
Actin - a biosensor that determines cell fate in yeasts
Smethurst, D. G. J., Dawes, I. W., & Gourlay, C. W. (2013) · FEMS Yeast Research · doi:10.1111/1567-1364.12119 · Cited by 23
Kumar, S. P., Chandy, M. L., Shanavas, M., Khan, S., & Veerabhadrappa, S. K. (2016) · Journal of Oral and Maxillofacial Surgery Medicine and Pathology · doi:10.1016/j.ajoms.2016.01.006 · Cited by 23
MIEN1 drives breast tumor cell migration by regulating cytoskeletal-focal adhesion dynamics
Kpetemey, M., Chaudhary, P., Treuren, T. V., & Vishwanatha, J. K. (2016) · Oncotarget · doi:10.18632/oncotarget.10798 · Cited by 23
Filamin A is required for spindle migration and asymmetric division in mouse oocytes
Wang, H., Guo, J., Lin, Z., Namgoong, S., Oh, J. S., & Kim, N. (2017) · The FASEB Journal · doi:10.1096/fj.201700056r · Cited by 23
Han, X., Yu, R., Ji, L., Zhen, D., Tao, S., Li, S., Sun, Y., Huang, L., Feng, Z., Li, X., et al. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07726.x · Cited by 23
Oliveira, M. M., Mohamed, M. S., Elder, M. K., Banegas-Morales, K., Mamcarz, M., Lu, E. H., Golhan, E. N., Navrange, N., Chatterjee, S., Abel, T. G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2023.113670 · Cited by 28
Zhuang, T.-T., Pan, C., Chen, J., Han, F., Zhu, X.-L., Xu, H., & Lu, Y.-P. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.09.006 · Cited by 24
Sensing α‐Synuclein From the Outside via the Prion Protein: Implications for Neurodegeneration
Brás, I. C., Lopes, L. V., & Outeiro, T. F. (2018) · Movement Disorders · doi:10.1002/mds.27478 · Cited by 24
SSH1 impedes SQSTM1/p62 flux and MAPT/Tau clearance independent of CFL (cofilin) activation
Fang, C. C., Woo, J. A., Liu, T., Zhao, X., Cazzaro, S., Yan, Y., Matlack, J. K., Kee, T. R., LePochat, P., & Kang, D. E. (2020) · Autophagy · doi:10.1080/15548627.2020.1816663 · Cited by 22
Functional Role of Non-Muscle Myosin II in Microglia: An Updated Review
Porro, C., Pennella, A., Panaro, M. A., & Trotta, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136687 · Cited by 20
Yang, V. W. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00008-6 · Cited by 24
Shehjar, F., Almarghalani, D. A., Mahajan, R., Hasan, S. A.-M., & Shah, Z. A. (2024) · Cells · doi:10.3390/cells13020188 · Cited by 22
Pathogenic microbes manipulate cofilin activity to subvert actin cytoskeleton
Zheng, K., Kitazato, K., Wang, Y., & He, Z. (2015) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2015.1010139 · Cited by 23
Simard, J. P., Reynolds, D. N., Kraguljac, A. P., Smith, G. S. T., & Mosser, D. D. (2011) · Journal of Cell Science · doi:10.1242/jcs.081745 · Cited by 22
Cara, G. D., Marengo, G., Albanese, N. N., Marabeti, M. R., Musso, R., Cancemi, P., & Pucci‐Minafra, I. (2013) · PubMed · Cited by 22
Regulation of actin filament turnover by cofilin-1 and cytoplasmic tropomyosin isoforms
Ostrowska, Z., Robaszkiewicz, K., & Moraczewska, J. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.09.019 · Cited by 22
Cytoskeleton actin-binding proteins in clinical behavior of pituitary tumors
Mantovani, G., Treppiedi, D., Giardino, E., Catalano, R., Mangili, F., VERCESI, P., Arosio, M., Spada, A., & Peverelli, E. (2018) · Endocrine Related Cancer · doi:10.1530/erc-18-0442 · Cited by 22
Role of Actin Cytoskeleton During Mammalian Sperm Acrosomal Exocytosis
Romarowski, A., Luque, G. M., Spina, F. A. L., Krapf, D., & Buffone, M. G. (2016) · Advances in anatomy, embryology and cell biology · doi:10.1007/978-3-319-30567-7_7 · Cited by 22
Alam, M. N., Yu, J. Q., Beale, P. J., & Huq, F. (2019) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520619666191021112042 · Cited by 21
Ling, H. Y., Ji, X., Lei, Y., Jia, Y., Liu, F., Xia, H., Tan, H., Zeng, X., Yi, L., He, J., et al. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.4968 · Cited by 21
Zhang, L., Fu, R., Duan, D., Li, Z., Li, B., Ming, Y., Li, L., Ni, R., & Chen, J. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.656184 · Cited by 21
Morris, K. J., Ihnatovych, I., Ionetz, E., Reed, J., Braundmeier, A. G., & Straková, Z. (2011) · Reproductive Sciences · doi:10.1177/1933719111401663 · Cited by 21
Harrison, A., Dubois, L. G., John‐Williams, L. S., Moseley, M. A., Hardison, R. L., Heimlich, D. R., Stoddard, A., Kerschner, J. E., Justice, S. S., Thompson, J. W., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.052498 · Cited by 21
Roy-Zokan, E. M., Dyer, K. A., & Meagher, R. B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145917 · Cited by 21
Zhou, C., Wang, Y., Pan, D., Sun, Y., & Cao, J. (2016) · Food Research International · doi:10.1016/j.foodres.2016.10.032 · Cited by 21
Yehl, J., Kudryashova, E., Reisler, E., Kudryashov, D. S., & Polenova, T. E. (2017) · Scientific Reports · doi:10.1038/srep44506 · Cited by 21
Islam, S. U., Ahmed, M. B., Lee, S. J., Shehzad, A., Sonn, J. K., Kwon, O., & Lee, Y. S. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.05.018 · Cited by 21
Olshina, M. A., Wong, W., & Baum, J. (2012) · IUBMB Life · doi:10.1002/iub.1014 · Cited by 21
JunB Mediates Basal- and TGFβ1-Induced Smooth Muscle Cell Contractility
Ramachandran, A., Gangopadhyay, S. S., Krishnan, R., Ranpura, S. A., Rajendran, K., Ram‐Mohan, S., Mulone, M. D., Gong, E. M.-L., & Adam, R. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053430 · Cited by 21
The role of reactive oxygen species in the regulation of the blood-brain barrier
Shuvalova, M. L., Dmitrieva, A., Belousov, V. V., & Nosov, G. (2024) · Tissue Barriers · doi:10.1080/21688370.2024.2361202 · Cited by 21
Cofilin promotes tau pathology in Alzheimer’s disease
Yan, M., Tang, L., Dai, L., Lei, C., Xiong, M., Zhang, X., He, M., Tian, Y., Xiong, J., Ke, W., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112138 · Cited by 20
Koga, R., Sugita, Y., Noda, T., Yanagi, Y., & Ohno, S. (2015) · Journal of Virology · doi:10.1128/jvi.01819-15 · Cited by 20
Durst, S., Nick, P., & Maisch, J. (2013) · Journal of Plant Physiology · doi:10.1016/j.jplph.2013.03.002 · Cited by 20
P53 in acute respiratory distress syndrome
Barabutis, N. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03629-1 · Cited by 20
Wang, X., Zou, S., Ren, T., Zhao, L., Yu, L., Li, X.-Y., Yan, X., & Zhang, L. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.4901 · Cited by 20
Ono, S., Nomura, K., Hitosugi, S., Tu, D. K., Lee, J. A., Baillie, D. L., & Ono, K. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-12-0934 · Cited by 20
Thapsigargin Induces Apoptosis by Impairing Cytoskeleton Dynamics in Human Lung Adenocarcinoma Cells
Wang, F., Liu, D., Xu, H., Li, Y., Wang, W., Liu, B., & Zhang, L.-Y. (2014) · The Scientific World JOURNAL · doi:10.1155/2014/619050 · Cited by 20
Sudnitsyna, M. V., Seit‐Nebi, A. S., & Gusev, N. B. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.03.010 · Cited by 20
A Genetically Encoded Reporter for Real-Time Imaging of Cofilin-Actin Rods in Living Neurons
Mi, J., Shaw, A. E., Pak, C. W., Walsh, K. P., Minamide, L. S., Bernstein, B. W., Kuhn, T. B., & Bamburg, J. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083609 · Cited by 20
Self-citationCao, F., Zhou, Z., Pan, X., Leung, C., Xie, W., Collingridge, G. L., & Jia, Z. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.08.017 · Cited by 21
Lewińska, A., Klukowska‐Rötzler, J., Deręgowska, A., Adamczyk‐Grochala, J., & Wnuk, M. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101163 · Cited by 20
Sun, Y., Zhong, M.-M., Li, Y., Zhang, R., Su, L., Xia, G., & Wang, H. (2021) · Molecular Plant Pathology · doi:10.1111/mpp.13137 · Cited by 19
Wang, Q., Xu, Y., Zhao, S., Jiang, Y., Yi, R., Guo, Y., & Huang, S. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002073 · Cited by 19
Thiopurines Induce Oxidative Stress in T‐Lymphocytes: A Proteomic Approach
Misdaq, M., Ziegler, S., von Ahsen, N., Oellerich, M., & Asif, A. R. (2015) · Mediators of Inflammation · doi:10.1155/2015/434825 · Cited by 19
Zhang, Y., Fu, R., Liu, Y., Li, J., Zhang, H., Hu, X., Chen, Y., Liu, X. B., Li, Y., Li, P., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7994 · Cited by 19
Tropomodulin isoforms utilize specific binding functions to modulate dendrite development
Gray, K. T., Suchowerska, A. K., Bland, T., Colpan, M., Wayman, G. A., Fath, T., & Kostyukova, A. S. (2016) · Cytoskeleton · doi:10.1002/cm.21304 · Cited by 19
Lin, C., Yen, S., Chang, H.-T., Chen, S., Lai, S.-L., Liu, Y., Chan, T., Liao, W.-L., & Lee, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015331 · Cited by 19
Novel functions for ADF/cofilin in excitatory synapses - lessons from gene-targeted mice
Rust, M. B. (2015) · Communicative & Integrative Biology · doi:10.1080/19420889.2015.1114194 · Cited by 18
Ciotti, S., Sgarra, R., Sgorbissa, A., Penzo, C., Tomasella, A., Casarsa, F., Benedetti, F. M., Berti, F., Manfioletti, G., & Brancolini, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0259-1 · Cited by 18
Lee, M., Hwang, Y., Yoon, J., Sun, J., Harned, A., Nagashima, K., & Daar, I. O. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201811147 · Cited by 19
Nguyen, M. T., Won, Y. H., Kwon, T. W., & Lee, W. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.02.021 · Cited by 18
Heng, N., Zhao, Z.-X., Guo, Y. X., Gao, S., Cai, D.-L., Fu, B.-F., Sheng, X., Wang, X., Xing, K., Xiao, L., et al. (2022) · Poultry Science · doi:10.1016/j.psj.2022.102051 · Cited by 18
Almarghalani, D. A., Sha, X., Mrak, R. E., & Shah, Z. A. (2023) · Cells · doi:10.3390/cells12081153 · Cited by 17
Doxorubicin-induced F-actin reorganization in cofilin-1 (nonmuscle) down-regulated CHO AA8 cells.
Grzanka, D., Marszałek, A., Gagat, M., Izdebska, M., Gackowska, L., & Grzanka, A. (2010) · Folia Histochemica et Cytobiologica · doi:10.2478/v10042-010-0072-5 · Cited by 17
Shen, X., Li, C.-C., Aponte, A. M., Shen, R., Billings, E. M., Moss, J., & Vaughan, M. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211877109 · Cited by 18
Han, F., Xu, H., Shen, J.-X., Pan, C., Yu, Z.-H., Chen, J.-J., Zhu, X.-L., Cai, Y.-F., & Lu, Y.-P. (2020) · Acta Neurobiologiae Experimentalis · doi:10.21307/ane-2020-021 · Cited by 18
Ferri, S. L., Hildebrand, P. F., Way, S. E., & Flanagan‐Cato, L. M. (2014) · Hormones and Behavior · doi:10.1016/j.yhbeh.2014.06.016 · Cited by 20
p210 bcr‐abl induces amoeboid motility by recruiting ADF/destrin through RhoA/ROCK1
Rochelle, T., Daubon, T., Troys, M. V., Harnois, T., Waterschoot, D., Ampè, C., Roy, L., Bourmeyster, N., & Constantin, B. (2012) · The FASEB Journal · doi:10.1096/fj.12-205112 · Cited by 18
Hsieh, Y., Hsu, W., Yang, S., Liu, C., Lu, K., Wang, P., & Lin, R.-C. (2021) · Pharmaceuticals · doi:10.3390/ph14030260 · Cited by 18
Yan, M., Meng, L., Dai, L., Zhang, X., Chen, G., Zheng, Y., Zha, Y., Zeng, Y., & Zhang, Z. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.06.101 · Cited by 18
RanBP9 overexpression accelerates loss of dendritic spines in a mouse model of Alzheimer's disease
Wang, R., Palavicini, J. P., Wang, H., Maiti, P., Bianchi, E., Xu, S., Lloyd, B. N., Dawson-Scully, K. D., Kang, D. E., & Lakshmana, M. K. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.029 · Cited by 17
Liu, C., Seeley‐Fallen, M. K., Miller, H. E., Upadhyaya, A., & Song, W. (2013) · Frontiers in Biology · doi:10.1007/s11515-013-1272-0 · Cited by 19
Lauterborn, J. C., Kramár, E. A., Rice, J. D., Babayan, A. H., Cox, C. D., Karsten, C. A., Gall, C. M., & LYNCH, G. S. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw088 · Cited by 17
Pathogenic Mechanisms of Actin Cross-Linking Toxins: Peeling Away the Layers
Kudryashova, E., Heisler, D. B., & Kudryashov, D. S. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_22 · Cited by 17
Amyloid fibrils induce dysfunction of hippocampal glutamatergic silent synapses
Bie, B., Wu, J., Foss, J. F., & Naguib, M. (2018) · Hippocampus · doi:10.1002/hipo.22955 · Cited by 18
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Metadata
- 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
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