ADF/Cofilin-Actin Rods in Neurodegenerative Diseases
Open accessAbstract
Dephosphorylation (activation) of cofilin, an actin binding protein, is stimulated by initiators of neuronal dysfunction and degeneration including oxidative stress, excitotoxic glutamate, ischemia, and soluble forms of beta-amyloid peptide (Abeta). Hyperactive cofilin forms rod-shaped cofilin-saturated actin filament bundles (rods). Other proteins are recruited to rods but are not necessary for rod formation. Neuronal cytoplasmic rods accumulate within neurites where they disrupt synaptic function and are a likely cause of synaptic loss without neuronal loss, as occurs early in dementias. Different rod-inducing stimuli target distinct neuronal populations within the hippocampus. Rods form rapidly, often in tandem arrays, in response to stress. They accumulate phosphorylated tau that immunostains for epitopes present in "striated neuropil threads," characteristic of tau pathology in Alzheimer disease (AD) brain. Thus, rods might aid in further tau modifications or assembly into paired helical filaments, the major component of neurofibrillary tangles (NFTs). Rods can occlude neurites and block vesicle transport. Some rod-inducing treatments cause an increase in secreted Abeta. Thus rods may mediate the loss of synapses, production of excess Abeta, and formation of NFTs, all of the pathological hallmarks of AD. Cofilin-actin rods also form within the nucleus of heat-shocked neurons and are cleared from cells expressing wild type huntingtin protein but not in cells expressing mutant or silenced huntingtin, suggesting a role for nuclear rods in Huntington disease (HD). As an early event in the neurodegenerative cascade, rod formation is an ideal target for therapeutic intervention that might be useful in treatment of many different neurological diseases.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
CFL1 is one of the main components of actin/cofilin rods, which are insoluble aggregates that lead to neurodysfunction.
“CFL1 is one of the main components of actin/cofilin rods, which are insoluble aggregates that lead to neurodysfunction [4, 101].”
From Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease (2024) · cites this paper as [4]
The “Isolation and characterization of rods” section identifies cofilin-1 as a core rod component, and “Cofilin-actin rods form in neurites and block vesicular transport and distal synaptic activity” links rods to neuronal dysfunction (page numbers unavailable). The copy describes rods as aggregated actin filaments but does not establish that they are insoluble; it says isolated rods are not stable in non-ionic detergents. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366 · see citing works
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works
Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172 · see citing works
Shah, M. A., Datson, N. A., Srinidhi, L., Stanton, V. P., MacDonald, M. E., Allard, M. W., Youngman, S., Am, F., Mott, R., Draths, K., et al. (1993) · Cell · Cited by 3,055 · see citing works
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,106 · see citing works
Atomic model of the actin filament
Holmes, K. C., Popp, D., Gebhard, W., & Kabsch, W. (1990) · Nature · doi:10.1038/347044a0 · Cited by 1,696 · see citing works
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,677 · see citing works
Axonopathy and Transport Deficits Early in the Pathogenesis of Alzheimer’s Disease
Stokin, G. B., Lillo, C., Falzone, T. L., Brusch, R. G., Rockenstein, E., Mount, S. L., Raman, R., Davies, P., Masliah, E., Williams, D. S., et al. (2005) · Science · doi:10.1126/science.1105681 · Cited by 1,214 · see citing works
Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
Ehehalt, R., Keller, P., Haass, C., Thiele, C., & Simons, K. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207113 · Cited by 1,103 · see citing works
Requirement for Hippocampal CA3 NMDA Receptors in Associative Memory Recall
Nakazawa, K., Quirk, M. C., Chitwood, R. A., Watanabe, M., Yeckel, M. F., Sun, L. D., Kato, A., Carr, C. A., Johnston, D., Wilson, M. A., et al. (2002) · Science · doi:10.1126/science.1071795 · Cited by 1,090 · 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-citationAugustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998 · see citing works
Dentate gyrus NMDA receptors mediate rapid pattern separation in the hippocampal network
McHugh, T. J., Jones, M. W., Quinn, J. J., Balthasar, N., Coppari, R., Elmquist, J. K., Lowell, B. B., Fanselow, M. S., Wilson, M. A., & Tonegawa, S. (2007) · Science · doi:10.1126/science.1140263 · Cited by 958 · see citing works
Cofilin Changes the Twist of F-Actin: Implications for Actin Filament Dynamics and Cellular Function
McGough, A. M., Pope, B. J., Chiu, W., & Weeds, A. G. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.4.771 · Cited by 762 · 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
Niwa, R., Nagata-Ohashi, K., Takeichi, M., Mizuno, K., & Uemura, T. (2002) · Cell · doi:10.1016/s0092-8674(01)00638-9 · Cited by 694 · see citing works
Fratelli, M., Demol, H., Puype, M., Casagrande, S., Eberini, I., Salmona, M., Bonetto, V., Mengozzi, M., Duffieux, F., Miclet, E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052592699 · Cited by 556 · see citing works
Mutant huntingtin impairs axonal trafficking in mammalian neurons in vivo and in vitro
Trushina, E., Dyer, R. B., Badger, J. D., Ure, D., Eide, L., Tran, D. D., Vrieze, B. T., Legendre-Guillemin, V., McPherson, P. S., Mandavilli, B. S., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8195-8209.2004 · Cited by 520 · see citing works
Transgenic inhibition of synaptic transmission reveals role of CA3 output in hippocampal learning
Nakashiba, T., Young, J. Z., McHugh, T. J., Buhl, D. L., & Tonegawa, S. (2008) · Science · doi:10.1126/science.1151120 · Cited by 492 · see citing works
Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
Fulga, T. A., Elson-Schwab, I., Khurana, V., Steinhilb, M. L., Spires, T. L., Hyman, B. T., & Feany, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1528 · Cited by 452 · see citing works
Welch, W. J., & Suhan, J. P. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.4.1198 · Cited by 430 · see citing works
Morris, R. G. M. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04888.x · Cited by 398 · 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-citationSynaptic pathology in Alzheimer's disease: a review of ultrastructural studies
Scheff, S. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.08.002 · Cited by 391 · see citing works
Synaptic and neuritic alterations during the progression of Alzheimer's disease
Masliah, E., Mallory, M., Hansen, L., Richard, D., Alford, M., & Terry, R. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90121-x · Cited by 370 · 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
Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
Gohla, A., Birkenfeld, J., & Bokoch, G. (2004) · Nature Cell Biology · doi:10.1038/ncb1201 · Cited by 327 · see citing works
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
Parkinson's disease and pesticides: a toxicological perspective
Hatcher, J. M., Pennell, K. D., & MILLER, G. (2008) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.03.007 · Cited by 319 · see citing works
Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease
Zhao, L., Ma, Q.-L., Calon, F., Harris-White, M. E., Yang, F., Lim, G. P., Morihara, T., Ubeda, O. J., Ambegaokar, S., Hansen, J. E., et al. (2006) · Nature Neuroscience · doi:10.1038/nn1630 · Cited by 317 · see citing works
Interplay between components of a novel LIM kinase–slingshot phosphatase complex regulates cofilin
Soosairajah, J., Maiti, S., Wiggan, O., Sarmiere, P. D., Moussi, N., Šarčević, B., Sampath, R., Bamburg, J. R., & Bernard, O. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600543 · Cited by 301 · see citing works
Self-citationActin-ATP Hydrolysis Is a Major Energy Drain for Neurons
Bernstein, B. W., & Bamburg, J. R. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-01-00002.2003 · Cited by 293 · see citing works
Self-citationADF/cofilin and actin dynamics in disease
Bamburg, J. R., & Wiggan, O. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02404-2 · Cited by 287 · see citing works
Self-citationCofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells.
Nishida, E., Iida, K., Yonezawa, N., Koyasu, S., Yahara, I., & Sakai, H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5262 · Cited by 275 · see citing works
Cdc42 regulates cofilin during the establishment of neuronal polarity.
Garvalov, B. K., Flynn, K. C., Neukirchen, D., Meyn, L., Teusch, N., Wu, X., Brakebusch, C., Bamburg, J. R., & Bradke, F. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3322-07.2007 · Cited by 262 · see citing works
Self-citationEssential functions and actin‐binding surfaces of yeast cofilin revealed by systematic mutagenesis
Lappalainen, P., Fedorov, E. V., Fedorov, A. A., Almo, S. C., & Drubin, D. G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5520 · Cited by 257 · see citing works
Calcium Signal-induced Cofilin Dephosphorylation Is Mediated by Slingshot via Calcineurin
Wang, Y., Shibasaki, F., & Mizuno, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411494200 · Cited by 253 · see citing works
Fukui, H., & Moraes, C. T. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.02.008 · Cited by 248 · see citing works
The ADF Homology (ADF-H) Domain: A Highly Exploited Actin-binding Module
Lappalainen, P., Kessels, M. M., Cope, M. J. T. V., & Drubin, D. G. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.8.1951 · Cited by 215 · see citing works
ADF/Cofilin Controls Cell Polarity during Fibroblast Migration
Dawe, H. R., Minamide, L. S., Bamburg, J. R., & Cramer, L. P. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00040-x · Cited by 189 · see citing works
Self-citationReactive 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
Huntingtin contains a highly conserved nuclear export signal
Xia, J. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg156 · Cited by 175 · see citing works
Structure of the actin-depolymerizing factor homology domain in complex with actin
Paavilainen, V. O., Oksanen, E., Goldman, A., & Lappalainen, P. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803100 · Cited by 169 · see citing works
Cytoskeletal pathologies of Alzheimer disease
Bamburg, J. R., & Bloom, G. S. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20388 · Cited by 168 · see citing works
Self-citationNuclear 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
Mechanism of Actin Polymerization in Cellular ATP Depletion
Atkinson, S. J., Hosford, M., & Molitoris, B. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306973200 · Cited by 148 · see citing works
Growth cone‐like waves transport actin and promote axonogenesis and neurite branching
Flynn, K. C., Pak, C. W., Shaw, A. E., Bradke, F., & Bamburg, J. R. (2009) · Developmental Neurobiology · doi:10.1002/dneu.20734 · Cited by 143 · see citing works
Self-citationIntranuclear actin bundles induced by dimethyl sulfoxide in interphase nucleus of Dictyostelium.
Fukui, Y. (1978) · The Journal of Cell Biology · doi:10.1083/jcb.76.1.146 · Cited by 135 · see citing works
Maloney, M. T., Minamide, L. S., Kinley, A. W., Boyle, J. A., & Bamburg, J. R. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3711-05.2005 · Cited by 131 · see citing works
Self-citationReversible translocation of cytoplasmic actin into the nucleus caused by dimethyl sulfoxide.
Sanger, J. W., Sanger, J. M., Kreis, T. E., & Jockusch, B. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.9.5268 · Cited by 125 · see citing works
Gehler, S., Shaw, A. E., Sarmiere, P. D., Bamburg, J. R., & Letourneau, P. C. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2836-04.2004 · Cited by 124 · see citing works
Self-citationDephosphorylation of Cofilin Accompanies Heat Shock-induced Nuclear Accumulation of Cofilin
Ohta, Y., Nishida, E., Sakai, H., & Miyamoto, E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71598-6 · Cited by 124 · 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 122 · see citing works
Self-citationUncoupling actin filament fragmentation by cofilin from increased subunit turnover
Pope, B. J., Gonsior, S. M., Yeoh, S., McGough, A. M., & Weeds, A. G. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3688 · Cited by 117 · see citing works
Maciver, S. K., & Weeds, A. G. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00552-4 · Cited by 116 · see citing works
Cofilin-mediated neurodegeneration in alzheimer’s disease and other amyloidopathies
Maloney, M. T., & Bamburg, J. R. (2007) · Molecular Neurobiology · doi:10.1007/bf02700622 · Cited by 112 · see citing works
Self-citationChapter 21 Glutamate toxicity in chronic neurodegenerative disease
Lancelot, E., & Beal, M. F. (1998) · Progress in brain research · doi:10.1016/s0079-6123(08)60446-x · Cited by 110 · see citing works
Damage of cellular functions by trifluoperazine, a calmodulin-specific drug
Osborn, M., & Weber, K. (1980) · Experimental Cell Research · doi:10.1016/0014-4827(80)90033-6 · Cited by 110 · see citing works
Matsuzaki, F., Matsumoto, S., Yahara, I., Yonezawa, N., Nishida, E., & Sakai, H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37996-1 · Cited by 102 · see citing works
Iida, K., Matsumoto, S., & Yahara, I. (1992) · Cell Structure and Function · doi:10.1247/csf.17.39 · Cited by 102 · see citing works
Masurovsky, E. B., Benitez, H. H., Kim, S. U., & Murray, M. R. (1970) · The Journal of Cell Biology · doi:10.1083/jcb.44.1.172 · Cited by 102 · see citing works
Costimulatory signals for human T-cell activation induce nuclear translocation of pp19/cofilin.
Samstag, Y., Eckerskorn, C., Wesselborg, S., Henning, S. W., Wallich, R., & Meuer, S. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4494 · Cited by 95 · see citing works
Cytoplasmic Localization and Nuclear Transport of Cofilin in Cultured Myotubes
Abe, H., Nagaoka, R., & Obinata, T. (1993) · Experimental Cell Research · doi:10.1006/excr.1993.1113 · Cited by 93 · 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-citationHeat shock induction of intranuclear actin rods in cultured mammalian cells
Iida, K., Iida, H., & Yahara, I. (1986) · Experimental Cell Research · doi:10.1016/0014-4827(86)90545-8 · Cited by 91 · 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-citationOsborn, M., & Weber, K. K. (1980) · Experimental Cell Research · doi:10.1016/0014-4827(80)90335-3 · Cited by 85 · see citing works
Chen, T., Gehler, S., Shaw, A. E., Bamburg, J. R., & Letourneau, P. C. (2005) · Journal of Neurobiology · doi:10.1002/neu.20204 · Cited by 84 · see citing works
Self-citationChen, H., Bernstein, B. W., Sneider, J. M., Boyle, J. A., Minamide, L. S., & Bamburg, J. R. (2004) · Biochemistry · doi:10.1021/bi049797n · Cited by 83 · see citing works
Self-citationAbe, H., Endo, T., Yamamoto, K., & Obinata, T. (1990) · Biochemistry · doi:10.1021/bi00484a010 · Cited by 82 · 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
Isolation and Characterization of Cytoplasmic Cofilin-Actin Rods
Minamide, L. S., Maiti, S., Boyle, J. A., Davis, R. C., Coppinger, J. A., Bao, Y., Huang, T. Y., Yates, J. R., Bokoch, G., & Bamburg, J. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063768 · Cited by 79 · see citing works
Self-citationThe dentate gyrus in Alzheimer's disease
Ohm, T. G. (2007) · Progress in brain research · doi:10.1016/s0079-6123(07)63039-8 · Cited by 78 · see citing works
Novel Method to Quantify Neuropil Threads in Brains from Elders With or Without Cognitive Impairment
Mitchell, T. W., Nissanov, J., Han, L.-Y., Mufson, E. J., Schneider, J. A., Cochran, E. J., Bennett, D. A., Lee, V. M.-Y., Trojanowski, J. Q., & Arnold, S. E. (2000) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540004801206 · Cited by 78 · see citing works
Jang, D., Han, J., Lee, S., Lee, Y., Park, H., Lee, S., Kim, H., & Kaang, B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507675102 · Cited by 77 · see citing works
Ressad, F., Didry, D., Égile, C., Pantaloni, D., & Carlier, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20970 · Cited by 72 · see citing works
Histological Changes Induced in Sympathetic, Motor and Sensory Nerve Cells by Functional Activity
Mann, G. (1895) · The American Journal of Psychology · doi:10.2307/1411204 · Cited by 71 · see citing works
Intranuclear rods and sheets in rat cochlear nucleus
Feldman, M. L., & Peters, A. (1972) · Journal of Neurocytology · doi:10.1007/bf01099179 · Cited by 69 · see citing works
Fukui, Y., & Katsumaru, H. (1980) · The Journal of Cell Biology · doi:10.1083/jcb.84.1.131 · Cited by 65 · see citing works
Deterioration threshold of synaptic morphology in aging and senile dementia of Alzheimer's type.
Bertoni–Freddari, C., Fattoretti, P., Casoli, T., Caselli, U., & Meier-Ruge, W. A. (1996) · PubMed · Cited by 64 · see citing works
Seite, R., Leonetti, J., Vuillet, J., & Vio, M. (1977) · Brain Research · doi:10.1016/0006-8993(77)90862-9 · 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-citationNucleocytoplasmic trafficking and transcription effects of huntingtin in Huntington's disease
Truant, R., Atwal, R. S., & Burtnik, A. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.11.004 · Cited by 59 · see citing works
Truant, R., Atwal, R. S., & Burtnik, A. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-181 · Cited by 55 · see citing works
Saito, T., Lamy, F., Roger, P. P., Lecocq, R., & Dumont, J. E. (1994) · Experimental Cell Research · doi:10.1006/excr.1994.1117 · Cited by 54 · see citing works
Mann, G. (1894) · Europe PMC (PubMed Central) · Cited by 51 · see citing works
Kamal, J. K. A., Benchaar, S. A., Takamoto, K., Reisler, E., & Chance, M. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611283104 · Cited by 44 · see citing works
Goldsbury, C. S., Whiteman, I. T., Jeong, E. V., & Lim, Y. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00423.x · Cited by 43 · see citing works
Self-citationShaw, A. E., Minamide, L. S., Bill, C. L., Funk, J. D., Maiti, S., & Bamburg, J. R. (2004) · Electrophoresis · doi:10.1002/elps.200406017 · Cited by 40 · see citing works
Self-citation̈te, R. S., Mei, N., & Vuillet-Luciani, J. (1973) · Brain Research · doi:10.1016/0006-8993(73)90744-0 · Cited by 38 · see citing works
Mapping the Cofilin Binding Site on Yeast G-Actin by Chemical Cross-Linking
Grintsevich, E. E., Benchaar, S. A., Warshaviak, D. T., Boontheung, P., Halgand, F., Whitelegge, J. P., Faull, K. F., Loo, R. R. O., Sept, D., Loo, J. A., et al. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.12.073 · Cited by 38 · see citing works
Striation is the characteristic neuritic abnormality in Alzheimer disease
Velasco, M. E., Smith, M. A., Siedlak, S. L., Nunomura, A., & Perry, G. L. (1998) · Brain Research · doi:10.1016/s0006-8993(98)01034-8 · Cited by 32 · see citing works
Giannakopoulos, P., von Gunten, A., Kövari, E., Gold, G., Herrmann, F. R., Hof, P. R., & Bouras, C. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2007.00827.x · Cited by 31 · see citing works
Glutamic acid and Alzheimer's disease.
Arias, C., Becerra-Garcı́a, F., & Tapia, R. (1998) · PubMed · Cited by 30 · see citing works
Actin paracrystal induction by forskolin and by db-cAMP in CHO cells
Osborn, M., & Weber, K. K. (1984) · Experimental Cell Research · doi:10.1016/0014-4827(84)90584-6 · Cited by 28 · see citing works
Homma, K., Niino, Y., Hotta, K., & Oka, K. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.10.001 · Cited by 26 · see citing works
Mills, R. G., Minamide, L. S., Yuan, A., Bamburg, J. R., & Bray, J. J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031225.x · Cited by 26 · see citing works
Self-citationThomas, R. S., Liddell, J. E., Murphy, L. S., Pache, D. M., & Kidd, E. J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-10406 · Cited by 21 · see citing works
ADF/Cofilin, Actin Dynamics, and Disease
Maloney, M. T., Kinley, A. W., Pak, C. W., & Bamburg, J. R. (2008) · Springer eBooks · doi:10.1007/978-0-387-71749-4_6 · Cited by 10 · see citing works
Self-citation
Flagged first, then by citations
1 of the 102 references couldn’t be matched to a known paper.
Research works printed but not linked: 5
- [6]Lancelot E Beal MF Glutamate toxicity in chronic neurodegenerative disease Prog Brain Res 116 331 347 1998 9932386
- [25]Minamide LS Maiti S Boyle JA Davis RC Coppinger JA Bao Y Huang TY Yates J Bokoch GM Bamburg JR Isolationand characterization of cofilin-actin rods from stressed cells J Biol Chem 12 17 Epub ahead of print 2009 PMC2820773 20022956
- [58]Whiteman IT Gervasio OL Cullen KM Guillemin GJ Jeong EV Wittig PK Activated ADF/cofilin sequesters phosphorylated microtubule-associated protein during the assembly of Alzheimer-like neuronal cytoskeletal striations J Neurosci 29 12994 13005 2009 19828813 PMC2821881
- [78]Matsuzaki F Matsumoto S Yahara I Yonezawa N Nishida E Sakai H Cloning and characterization of porcine brain cofilin cDNA J Biol Chem 263 11564 11568 1988 3403546
- [84]Truant R Atwal R Burtnik A Hypothesis: Huntingtin may function in membrane association and vesicular trafficking Biochem Cell Biol 84 912 917 2006 17215878
Cited by
Sorted by citations
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
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
Cellular functions of the ADF/cofilin family at a glance
Kanellos, G., & Frame, M. C. (2016) · Journal of Cell Science · doi:10.1242/jcs.187849 · Cited by 223 · see citing works
GAP-43 and BASP1 in Axon Regeneration: Implications for the Treatment of Neurodegenerative Diseases
Chung, D., Shum, A. K., & Caraveo, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.567537 · Cited by 198 · 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-citationThe role of aberrant mitochondrial bioenergetics in diabetic neuropathy
Chowdhury, S. R., Smith, D. R., & Fernyhough, P. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.016 · Cited by 166 · see citing works
Global treadmilling coordinates actin turnover and controls the size of actin networks
Carlier, M., & Shekhar, S. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.172 · Cited by 148 · see citing works
Poukkula, M., Kremneva, E., Serlachius, M., & Lappalainen, P. (2011) · Cytoskeleton · doi:10.1002/cm.20530 · Cited by 152 · see citing works
Near-Atomic Resolution for One State of F-Actin
Galkin, V. E., Orlova, A., Vos, M. R. J., Schroeder, G. F., & Egelman, E. H. (2014) · Structure · doi:10.1016/j.str.2014.11.006 · Cited by 146 · see citing works
Millan, M. J. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.004 · Cited by 146 · see citing works
Mechanisms of protein toxicity in neurodegenerative diseases
Chung, C. G., Lee, H., & Lee, S. B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2854-4 · Cited by 142 · 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
Pontrello, C. G., Sun, M., Lin, A. Y., Fiacco, T. A., DeFea, K., & Ethell, I. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118803109 · Cited by 130 · see citing works
Epigenetically regulated microRNAs in Alzheimer's disease
van den Hove, D., Kompotis, K., Lardenoije, R., Kenis, G., Mill, J. S., Steinbusch, H. W. M., Lesch, K., Fitzsimons, C. P., Strooper, B. D., & Rutten, B. P. F. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.10.082 · Cited by 119 · 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
Actin, actin-binding proteins, and actin-related proteins in the nucleus
Kristó, I., Bajusz, I., Bajusz, C., Borkúti, P., & Vilmos, P. (2016) · Histochemistry and Cell Biology · doi:10.1007/s00418-015-1400-9 · Cited by 116 · see citing works
Synaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 117 · see citing works
Nuclear Actin: From Discovery to Function
Kelpsch, D. J., & Tootle, T. L. (2018) · The Anatomical Record · doi:10.1002/ar.23959 · Cited by 99 · see citing works
Davis, R. C., Marsden, I. T., Maloney, M. T., Minamide, L. S., Podlisny, M. B., Selkoe, D. J., & Bamburg, J. R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-10 · Cited by 97 · see citing works
Self-citationCofilin 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
Cucurbitacin B and cancer intervention: Chemistry, biology and mechanisms (Review)
Garg, S., Kaul, S. C., & Wadhwa, R. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4203 · Cited by 95 · see citing works
In Pursuit of Healthy Aging: Effects of Nutrition on Brain Function
Melzer, T. M., Manosso, L. M., Yau, S., Gil‐Mohapel, J., & Brocardo, P. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22095026 · Cited by 90 · 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-citationBinucleate germ cells in Caenorhabditis elegans are removed by physiological apoptosis
Raiders, S. A., Eastwood, M. D., Bacher, M. C., & Priess, J. R. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007417 · Cited by 73 · see citing works
Activated cofilin exacerbates tau pathology by impairing tau-mediated microtubule dynamics
Woo, J. A., Liu, T., Fang, C. C., Cazzaro, S., Kee, T. R., LePochat, P., Yrigoin, K., Penn, C., Zhao, X., Wang, X., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0359-9 · Cited by 68 · see citing works
Cofilin, a Master Node Regulating Cytoskeletal Pathogenesis in Alzheimer’s Disease
Kang, D. E., & Woo, J. A. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190585 · Cited by 67 · see citing works
Walsh, K. P., Minamide, L. S., Kane, S. J., Shaw, A. E., Brown, D. R., Pulford, B. E., Zabel, M. D., Lambeth, J. D., Kuhn, T. B., & Bamburg, J. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095995 · Cited by 65 · see citing works
Self-citationXiang, Y., Zheng, K., Ju, H., Wang, S., Pei, Y., Ding, W., Chen, Z., Wang, Q.-L., Qiu, X., Zhong, M., et al. (2012) · Journal of Virology · doi:10.1128/jvi.00609-12 · Cited by 64 · see citing works
The epigenetic dimension of Alzheimer's disease: causal, consequence, or curiosity?
Millan, M. J. (2014) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2014.16.3/mmillan · Cited by 63 · see citing works
Anastasiadou, S., & Knöll, B. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.03.012 · Cited by 63 · see citing works
Unsain, N., Bordenave, M. D., Martínez, G. F., Jalil, S., von Bilderling, C., Barabas, F. M., Masullo, L. A., Johnstone, A. D., Barker, P. A., Bisbal, M., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-21232-0 · Cited by 66 · see citing works
George, J., Soares, C., Montersino, A., Béïque, J.-C., & Thomas, G. M. (2015) · eLife · doi:10.7554/elife.06327 · Cited by 58 · see citing works
Cofilin as a Promising Therapeutic Target for Ischemic and Hemorrhagic Stroke
Alhadidi, Q., Sayeed, M. S. B., & Shah, Z. A. (2015) · Translational Stroke Research · doi:10.1007/s12975-015-0438-2 · Cited by 57 · see citing works
Serum Response Factor (SRF)-cofilin-actin signaling axis modulates mitochondrial dynamics
Beck, H., Flynn, K. C., Lindenberg, K. S., Schwarz, H., Bradke, F., Giovanni, S. D., & Knöll, B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208141109 · Cited by 56 · see citing works
Self-citationLIM kinase mediates estrogen action on the actin depolymerization factor Cofilin
Yuen, G. S., McEwen, B. S., & Akama, K. T. (2010) · Brain Research · doi:10.1016/j.brainres.2010.07.067 · Cited by 54 · see citing works
Wurz, A. I., Schulz, A. M., O’Bryant, C. T., Sharp, J. F., & Hughes, R. M. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.982074 · Cited by 53 · see citing works
Campellone, K. G., Lebek, N. M., & King, V. L. (2023) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2023.151301 · Cited by 50 · see citing works
The Actin Depolymerizing Factor (ADF)/Cofilin Signaling Pathway and DNA Damage Responses in Cancer
Chang, C., Leu, J., & Lee, Y. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16024095 · Cited by 50 · see citing works
Ren, S., Ouyang, D., Saltis, M., Xu, L., Zha, Q., Cai, J., & He, X. (2012) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-012-1921-z · Cited by 50 · see citing works
Munsie, L. N., & Truant, R. (2012) · BioArchitecture · doi:10.4161/bioa.22549 · Cited by 49 · see citing works
Stern, S., Haverkamp, S., Sinske, D., Tedeschi, A., Naumann, U., Giovanni, S. D., Kochanek, S., Nordheim, A., & Knöll, B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3029-13.2013 · Cited by 49 · see citing works
Amyloid precursor proteins are protective in Drosophila models of progressive neurodegeneration
Wentzell, J. S., Bolkan, B. J., Carmine-Simmen, K., Swanson, T. L., Musashe, D. T., & Kretzschmar, D. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.047 · Cited by 48 · see citing works
Liu, X., Zuo, H., Wang, D., Peng, R., Song, T., Wang, S., Xu, X., Gao, Y., Li, Y., Wang, S., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126963 · Cited by 47 · see citing works
Jiang, G., Xie, G., Li, X., & Xiong, J. (2025) · Biomolecules · doi:10.3390/biom15060831 · Cited by 45 · see citing works
Role of synucleins in traumatic brain injury — An experimental in vitro and in vivo study in mice
Surgucheva, I. G., He, S., Rich, M. C., Sharma, R., Ninkina, N. N., Stahel, P. F., & Surguchov, A. P. (2014) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2014.10.005 · Cited by 45 · see citing works
Actin(g) on mitochondria – a role for cofilin1 in neuronal cell death pathways
Hoffmann, L., Rust, M. B., & Culmsee, C. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0120 · Cited by 45 · see citing works
Cofilactin filaments regulate filopodial structure and dynamics in neuronal growth cones
Hylton, R. K., Heebner, J. E., Grillo, M. A., & Swulius, M. T. (2022) · Nature Communications · doi:10.1038/s41467-022-30116-x · Cited by 45 · see citing works
Aβ Influences Cytoskeletal Signaling Cascades with Consequences to Alzheimer’s Disease
Henriques, A. G., Oliveira, J. M., Carvalho, L., & Silva, O. A. B. D. C. E. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8913-4 · Cited by 43 · see citing works
Synaptic actin stabilization protein loss in Down syndrome and Alzheimer disease
Lauterborn, J. C., Cox, C. D., Chan, S. W., Vanderklish, P. W., Lynch, G., & Gall, C. M. (2020) · Brain Pathology · doi:10.1111/bpa.12779 · Cited by 43 · see citing works
Arabidopsis actin-depolymerizing factors (ADFs) 1 and 9 display antagonist activities
Tholl, S., Moreau, F., Hoffmann, C., Arumugam, K., Dieterle, M., Moes, D., Neumann, K., Steinmetz, A. A., & Thomas, C. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.019 · Cited by 41 · see citing works
Peterson, T. S., Thebeau, C. N., Ajit, D., Camden, J. M., Woods, L. T., Wood, W. G., Petris, M. J., Sun, G. Y., Erb, L., & Weisman, G. A. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12252 · Cited by 40 · see citing works
Muscle lim protein isoform negatively regulates striated muscle actin dynamics and differentiation
Vafiadaki, E., Arvanitis, D. A., Papalouka, V., Terzis, G. D., Roumeliotis, T. I., Spengos, K. M., Garbis, S. D., Manta, P., Kranias, E. G., & Sanoudou, D. (2014) · FEBS Journal · doi:10.1111/febs.12859 · Cited by 38 · see citing works
Microdomains in Forebrain Spines: an Ultrastructural Perspective
Rácz, B., & Weinberg, R. J. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8345-y · Cited by 37 · see citing works
Brain ischemic insult induces cofilin rod formation leading to synaptic dysfunction in neurons
Shu, L., Chen, B., Chen, B., Xu, H., Wang, G., Huang, Y., Zhao, Y., Gong, H., Jiang, M., Chen, L., et al. (2018) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x18785567 · Cited by 37 · see citing works
Smith, L. K., Kuhn, T. B., Chen, J. C., & Bamburg, J. R. (2018) · Current HIV Research · doi:10.2174/1570162x16666181003144740 · Cited by 36 · see citing works
Self-citationJacquet, A. D. R., Denis, H. L., Cicchetti, F., & Alpaugh, M. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00999-7 · Cited by 35 · see citing works
Photodynamic sensitizers modulate cytoskeleton structural dynamics in neuronal cells
Dubey, T., & Chinnathambi, S. (2021) · Cytoskeleton · doi:10.1002/cm.21655 · Cited by 36 · see citing works
INF2-mediated actin filament reorganization confers intrinsic resilience to neuronal ischemic injury
Calabrese, B., Jones, S. L., Shiraishi‐Yamaguchi, Y., Lingelbach, M., Manor, U., Svitkina, T., Higgs, H. N., Shih, A. Y., & Halpain, S. (2022) · Nature Communications · doi:10.1038/s41467-022-33268-y · Cited by 36 · see citing works
Deng, Y., Wei, J., Cheng, J., Zhong, P., Zhe, X., Liu, A., Lin, L., Chen, S., & Yan, Z. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160167 · Cited by 35 · see citing works
Cofilin-actin rod formation in neuronal processes after brain ischemia
Won, S. J., Minnella, A. M., Wu, L., Eun, C. H., Rome, E., Shaw, A. E., Herson, P. S., Bamburg, J. R., & Swanson, R. A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0198709 · Cited by 33 · see citing works
Self-citationSchönhofen, P., de Medeiros, L. M., Chatain, C. P., Bristot, I. J., & Klamt, F. (2014) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557514666140506161458 · Cited by 33 · see citing works
Accumulation of F-actin drives brain aging and limits healthspan in Drosophila
Schmid, E. T., Schinaman, J. M., Liu-Abramowicz, N., Williams, K. S., & Walker, D. W. (2024) · Nature Communications · doi:10.1038/s41467-024-53389-w · Cited by 34 · see citing works
Functional Diversity of Actin Cytoskeleton in Neurons and its Regulation by Tropomyosin
Schevzov, G., Curthoys, N. M., Gunning, P. W., & Fath, T. (2012) · International review of cytology · doi:10.1016/b978-0-12-394309-5.00002-x · Cited by 32 · see citing works
Qiu, G., Zheng, X., Fu, M., Huang, C., & Yang, X. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101306 · Cited by 31 · see citing works
Direct Visualization of Actin Filaments and Actin-Binding Proteins in Neuronal Cells
Jung, M., Kim, D., & Mun, J. Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.588556 · Cited by 30 · see citing works
Critical Roles of Dual-Specificity Phosphatases in Neuronal Proteostasis and Neurological Diseases
Bhore, N., Wang, B., Chen, Y.-W., & Liao, Y. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091963 · Cited by 30 · see citing works
Cofilin-Mediated Actin Stress Response Is Maladaptive in Heat-Stressed Embryos
Figard, L., Zheng, L., Biel, N., Xue, Z., Seede, H., Coleman, S., Golding, I., & Sokac, A. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.092 · Cited by 29 · see citing works
Toward High Spatially Resolved Proteomics Using Expansion Microscopy
Drelich, L., Aboulouard, S., Franck, J., Salzet, M., Fournier, I., & Wisztorski, M. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c05372 · Cited by 29 · see citing works
Whiteman, I. T., Minamide, L. S., Goh, D. L., Bamburg, J. R., & Goldsbury, C. S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020878 · Cited by 28 · see citing works
Self-citationRamachandran, U., Manavalan, A., Sundaramurthi, H., Sze, S. K., Feng, Z. W., Hu, J., & Heese, K. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.03.012 · Cited by 27 · see citing works
Sitkiewicz, E., Olędzki, J., Poznański, J. T., & Dadlez, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100200 · Cited by 27 · see citing works
Frykman, S., Teranishi, Y., Hur, J., Matton, A., Yamamoto, N. G., Ankarcrona, M., Nishimura, T., Winblad, B. G., Bogdanović, N., Schedin‐Weiss, S., et al. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.03.016 · Cited by 27 · see citing works
Zhang, Y.-T., Ouyang, D., Xu, L., Zha, Q., & He, X. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24587 · Cited by 26 · see citing works
Regulation of actin filament assembly and disassembly in growth cone motility and axon guidance
Schneider, F., Metz, I., & Rust, M. B. (2022) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2022.10.019 · Cited by 26 · see citing works
Stefen, H., Chaichim, C., Power, J., & Fath, T. (2016) · Neural Plasticity · doi:10.1155/2016/2371970 · Cited by 26 · see citing works
The Effects of Disease Models of Nuclear Actin Polymerization on the Nucleus
Serebryannyy, L., Yuen, M., Parilla, M., Cooper, S. T., & de Lanerolle, P. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00454 · Cited by 26 · see citing works
The role of actin cytoskeleton CFL1 and ADF/cofilin superfamily in inflammatory response
Xing, J., Wang, Y., Peng, A., Li, J., Niu, X., & Zhang, K. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1408287 · Cited by 24 · see citing works
Fonseca, C., Ettcheto, M., Bicker, J., Fernandes, M. J., Falcão, A. C., Camins, A., & Fortuna, A. C. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101998 · Cited by 26 · see citing works
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 · see citing works
Jury-Garfe, N., Redding-Ochoa, J., You, Y., Martínez, P., Karahan, H., Chimal-Juárez, E., Johnson, T. S., Zhang, J., Resnick, S., Kim, J., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02775-1 · Cited by 22 · see citing works
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 22 · see citing works
Shehjar, F., Almarghalani, D. A., Mahajan, R., Hasan, S. A.-M., & Shah, Z. A. (2024) · Cells · doi:10.3390/cells13020188 · Cited by 22 · see citing works
Müller, C. B., Bastiani, M. A. D., Becker, M. W., França, F. S., Branco, M. A., Castro, M. A. A., & Klamt, F. (2015) · Oncotarget · doi:10.18632/oncotarget.3471 · Cited by 22 · see citing works
In vivo and in vitro effects of vortioxetine on molecules associated with neuroplasticity
Kugathasan, P., Waller, J. A., Westrich, L., Abdourahman, A., Tamm, J. A., Pehrson, A. L., Dale, E., Gulinello, M. E., Sánchez, C., & Li, Y. (2016) · Journal of Psychopharmacology · doi:10.1177/0269881116667710 · Cited by 22 · see citing works
Teister, J., Anders, F., Gehrke-Beck, S., Funke, S., von Pein, H., Prokosch, V., Pfeiffer, N., & Grus, F. H. (2017) · Scientific Reports · doi:10.1038/s41598-017-06702-1 · Cited by 22 · see citing works
Jin, G., Zhu, L., Liu, P., Xu, Q., Qi, Y. A., Zhou, X., Xu, J., Ji, X., Chi, T., & Zou, L. (2019) · The Journal of Physiological Sciences · doi:10.1007/s12576-019-00664-x · Cited by 22 · see citing works
HIV-associated neurodegeneration: exploitation of the neuronal cytoskeleton
Wenzel, E. D., Avdoshina, V., & Mocchetti, I. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-019-00737-y · Cited by 21 · see citing works
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 · see citing works
Self-citationChoudhury, K. R., Das, S., & Bhattacharyya, N. P. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.11.007 · Cited by 19 · see citing works
Nuclear actin: ancient clue to evolution in eukaryotes?
Bajusz, C., Borkúti, P., Kristó, I., Kovács, Z., Abonyi, C., & Vilmos, P. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1693-6 · Cited by 19 · see citing works
Kaur, M., & Kachlany, S. C. (2014) · Microbiology · doi:10.1099/mic.0.082347-0 · Cited by 18 · see citing works
Simhadri, P. K., Malwade, R., Ravisankar, V., Nakka, V. P., Kuppusamy, G., & Babu, P. P. (2017) · Annals of Neurology · doi:10.1002/ana.25028 · Cited by 18 · see citing works
Role of Rho-associated kinases and their inhibitor fasudil in neurodegenerative diseases
Ye, Q., Li, X., Gao, W. Q., Gao, J., Zheng, L., Zhang, M., Yang, F., & Li, H. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1481983 · Cited by 17 · see citing works
Fe65: A Scaffolding Protein of Actin Regulators
Augustin, V., & Kins, S. (2021) · Cells · doi:10.3390/cells10071599 · Cited by 18 · see citing works
Cofilin 2 in Serum as a Novel Biomarker for Alzheimer’s Disease in Han Chinese
Sun, Y., Liang, L., Dong, M., Li, C., Liu, Z., & Gao, H. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00214 · Cited by 16 · see citing works
Weston, L. J., Bowman, A. M., Osterberg, V. R., Meshul, C. K., Woltjer, R. L., & Unni, V. K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315294 · Cited by 15 · see citing works
Gawinecka, J., Cardone, F., Asif, A. R., Pascalis, A. D., Wemheuer, W. M., Schulz‐Schaeffer, W., Pocchiari, M., & Zerr, I. (2012) · PROTEOMICS · doi:10.1002/pmic.201200201 · Cited by 15 · see citing works
Cofilactin rod formation mediates inflammation-induced neurite degeneration
Uruk, G., Mocanu, E., Shaw, A. E., Bamburg, J. R., & Swanson, R. A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113914 · Cited by 14 · see citing works
Self-citationActin-Interacting Protein 1 Contributes to Intranuclear Rod Assembly in Dictyostelium discoideum
Ishikawa-Ankerhold, H. C., Daszkiewicz, W., Schleicher, M., & Müller‐Taubenberger, A. (2017) · Scientific Reports · doi:10.1038/srep40310 · Cited by 14 · see citing works
Chronophin coordinates cell leading edge dynamics by controlling active cofilin levels
Delorme, V., Seo, J., Gohla, A., Fowler, B. J., Bohl, B. P., & DerMardirossian, C. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510945112 · Cited by 14 · see citing works
- Authors
- Bamburg, J. R., Bernstein, B. W., Davis, R. C., Flynn, K. C., Goldsbury, C., Jensen, J. R., Maloney, M. T., Marsden, I. T., Minamide, L. S., Pak, C. W., Shaw, A. E., Whiteman, I., & Wiggan, O.
- Affiliations
- Colorado State University (US)
- Max Planck Society (DE)
- The University of Sydney (AU)
- Stanford Medicine (US)
- Venue
- Current Alzheimer Research
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2010-05-01
- Volume
- 7
- Issue
- 3
- Pages
- 241-250
- ISSN
- 1567-2050 (ISSN-L)
- PMC
- PMC4458070
- OpenAlex
- W2009511852
- Cited by
- 173
- References
- 102
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 13 · 2023: 9 · 2022: 7 · 2021: 17 · 2020: 7 · 2019: 12 · 2018: 14 · 2017: 11 · 2016: 12 · 2015: 10 · 2014: 12 · 2013: 9 · 2012: 18
- FWCI
- 7.80
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Alzheimer Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Alzheimer's Drug Discovery Foundation
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (NS43115, NS 40371, R01NS040371, T32NS043115)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- cofilin, neurodegenerative diseases, Alzheimer's disease, Huntington's disease, tau phosphorylation, neurofibrillary tangles, amyloid-beta, oxidative stress, excitotoxicity, ischemia, synaptic loss, hippocampus, heat shock, huntingtin, actin cytoskeleton
- MeSH terms
- Alzheimer Disease, Animals, Inclusion Bodies, Humans, Huntington Disease, Actin Cytoskeleton, Neurons, Neurofibrillary Tangles, Oxidative Stress, Neurodegenerative Diseases, Cofilin 1
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 ›
Are you an author, or do you see a problem with this page? Request a review
