Cited by 173Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsCellular Mechanics and Interactions

The DOI matches its Crossref record; 101 of the 102 references it cites were found in a registry or an index.

ADF/Cofilin-Actin Rods in Neurodegenerative Diseases

Open access

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.·2010·Current Alzheimer Research

DOI 10.2174/156720510791050902PMC PMC4458070

Open this paper in CoChat — free account

Abstract

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

Crossref · 10.2174/156720510791050902

Cites

101 of 101 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366
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
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
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
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
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
Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
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
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group.
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
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,153
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 1,722
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
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

Show all 102 references

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

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 1,547
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 241
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
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 209
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
Self-citation
The 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 169
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
Actin‐depolymerizing factor homology domain: A conserved fold performing diverse roles in cytoskeletal dynamics
Poukkula, M., Kremneva, E., Serlachius, M., & Lappalainen, P. (2011) · Cytoskeleton · doi:10.1002/cm.20530 · Cited by 152
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
Linking deregulation of non-coding RNA to the core pathophysiology of Alzheimer’s disease: An integrative review
Millan, M. J. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.004 · Cited by 151
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
Aβ mediates F-actin disassembly in dendritic spines leading to cognitive deficits in Alzheimer's disease
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
Cofilin under control of β-arrestin-2 in NMDA-dependent dendritic spine plasticity, long-term depression (LTD), and learning
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 135
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 121
Epidermal Growth Factor Receptor-PI3K Signaling Controls Cofilin Activity To Facilitate Herpes Simplex Virus 1 Entry into Neuronal Cells
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
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
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 128
Nuclear Actin: From Discovery to Function
Kelpsch, D. J., & Tootle, T. L. (2018) · The Anatomical Record · doi:10.1002/ar.23959 · Cited by 99
Amyloid beta dimers/trimers potently induce cofilin-actin rods that are inhibited by maintaining cofilin-phosphorylation
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 102
Self-citation
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
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
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 97
Incorporation of Cofilin into Rods Depends on Disulfide Intermolecular Bonds: Implications for Actin Regulation and Neurodegenerative Disease
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
Self-citation
Binucleate 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 61
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 69
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 70
Amyloid-β and Proinflammatory Cytokines Utilize a Prion Protein-Dependent Pathway to Activate NADPH Oxidase and Induce Cofilin-Actin Rods in Hippocampal Neurons
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 69
Self-citation
Cofilin 1-Mediated Biphasic F-Actin Dynamics of Neuronal Cells Affect Herpes Simplex Virus 1 Infection and Replication
Xiang, 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
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 66
The multiple sclerosis drug fingolimod (FTY720) stimulates neuronal gene expression, axonal growth and regeneration
Anastasiadou, S., & Knöll, B. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.03.012 · Cited by 61
Remodeling of the Actin/Spectrin Membrane-associated Periodic Skeleton, Growth Cone Collapse and F-Actin Decrease during Axonal Degeneration
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
Palmitoylation of LIM Kinase-1 ensures spine-specific actin polymerization and morphological plasticity
George, J., Soares, C., Montersino, A., Béïque, J.-C., & Thomas, G. M. (2015) · eLife · doi:10.7554/elife.06327 · Cited by 61
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
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
Self-citation
LIM 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 57
Cytoskeletal dysregulation and neurodegenerative disease: Formation, monitoring, and inhibition of cofilin-actin rods
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
Branching out in different directions: Emerging cellular functions for the Arp2/3 complex and WASP-family actin nucleation factors
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
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 53
Anti-proliferative effect of 23,24-dihydrocucurbitacin F on human prostate cancer cells through induction of actin aggregation and cofilin-actin rod formation
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
The role of the cofilin-actin rod stress response in neurodegenerative diseases uncovers potential new drug targets
Munsie, L. N., & Truant, R. (2012) · BioArchitecture · doi:10.4161/bioa.22549 · Cited by 49
The Transcription Factor Serum Response Factor Stimulates Axon Regeneration through Cytoplasmic Localization and Cofilin Interaction
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
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 50
Improvement of Spatial Memory Disorder and Hippocampal Damage by Exposure to Electromagnetic Fields in an Alzheimer’s Disease Rat Model
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 51
Cytoskeletal Proteins and Alzheimer’s Disease Pathogenesis: Focusing on the Interplay with Tau Pathology
Jiang, G., Xie, G., Li, X., & Xiong, J. (2025) · Biomolecules · doi:10.3390/biom15060831 · Cited by 48
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
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
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
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 45
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
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
Up‐regulation and activation of the P2Y2 nucleotide receptor mediate neurite extension in IL ‐1β‐treated mouse primary cortical neurons
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 41
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
Microdomains in Forebrain Spines: an Ultrastructural Perspective
Rácz, B., & Weinberg, R. J. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8345-y · Cited by 41
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
HIV Associated Neurodegenerative Disorders: A New Perspective on the Role of Lipid Rafts in Gp120-Mediated Neurotoxicity
Smith, L. K., Kuhn, T. B., Chen, J. C., & Bamburg, J. R. (2018) · Current HIV Research · doi:10.2174/1570162x16666181003144740 · Cited by 36
Self-citation
Current and future applications of induced pluripotent stem cell-based models to study pathological proteins in neurodegenerative disorders
Jacquet, A. D. R., Denis, H. L., Cicchetti, F., & Alpaugh, M. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00999-7 · Cited by 36
Photodynamic sensitizers modulate cytoskeleton structural dynamics in neuronal cells
Dubey, T., & Chinnathambi, S. (2021) · Cytoskeleton · doi:10.1002/cm.21655 · Cited by 36
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 37
Partial Amelioration of Synaptic and Cognitive Deficits by Inhibiting Cofilin Dephosphorylation in an Animal Model of Alzheimer’s Disease
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 36
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 37
Self-citation
Cofilin/Actin Rod Formation by Dysregulation of Cofilin-1 Activity as a Central Initial Step in Neurodegeneration
Schönhofen, 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 34
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 35
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 34
The decreased exclusion of nuclear eccDNA: From molecular and subcellular levels to human aging and age-related diseases
Qiu, G., Zheng, X., Fu, M., Huang, C., & Yang, X. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101306 · Cited by 31
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 29
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 33
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
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 32
Rapid Changes in Phospho-MAP/Tau Epitopes during Neuronal Stress: Cofilin-Actin Rods Primarily Recruit Microtubule Binding Domain Epitopes
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 29
Self-citation
Tianma modulates proteins with various neuro-regenerative modalities in differentiated human neuronal SH-SY5Y cells
Ramachandran, 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
Di-Tyrosine Cross-Link Decreases the Collisional Cross-Section of Aβ Peptide Dimers and Trimers in the Gas Phase: An Ion Mobility Study
Sitkiewicz, E., Olędzki, J., Poznański, J. T., & Dadlez, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100200 · Cited by 26
Identification of two novel synaptic γ-secretase associated proteins that affect amyloid β-peptide levels without altering Notch processing
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
Formation of cofilin-actin rods following cucurbitacin-B-induced actin aggregation depends on slingshot homolog 1-mediated cofilin hyperactivation
Zhang, Y.-T., Ouyang, D., Xu, L., Zha, Q., & He, X. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24587 · Cited by 26
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
Regulation of the Postsynaptic Compartment of Excitatory Synapses by the Actin Cytoskeleton in Health and Its Disruption in Disease
Stefen, H., Chaichim, C., Power, J., & Fath, T. (2016) · Neural Plasticity · doi:10.1155/2016/2371970 · Cited by 30
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
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
Under the umbrella of depression and Alzheimer’s disease physiopathology: Can cannabinoids be a dual-pleiotropic therapy?
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 31
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
Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease
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
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
The Multifaceted Role of Cofilin in Neurodegeneration and Stroke: Insights into Pathogenesis and Targeting as a Therapy
Shehjar, F., Almarghalani, D. A., Mahajan, R., Hasan, S. A.-M., & Shah, Z. A. (2024) · Cells · doi:10.3390/cells13020188 · Cited by 22
Potential crosstalk between cofilin-1 and EGFR pathways in cisplatin resistance of non-small-cell lung cancer
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 23
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
Decelerated neurodegeneration after intravitreal injection of α-synuclein antibodies in a glaucoma animal model
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 25
Xanthoceraside prevented synaptic loss and reversed learning-memory deficits in APP/PS1 transgenic mice
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
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
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-citation
Differential proteomic and genomic profiling of mouse striatal cell model of Huntington's disease and control; probable implications to the disease biology
Choudhury, K. R., Das, S., & Bhattacharyya, N. P. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.11.007 · Cited by 19
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
Aggregatibacter actinomycetemcomitans leukotoxin (LtxA; Leukothera) induces cofilin dephosphorylation and actin depolymerization during killing of malignant monocytes
Kaur, M., & Kachlany, S. C. (2014) · Microbiology · doi:10.1099/mic.0.082347-0 · Cited by 18
Dysregulation of LIMK‐1/cofilin‐1 pathway: A possible basis for alteration of neuronal morphology in experimental cerebral malaria
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 20
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
Fe65: A Scaffolding Protein of Actin Regulators
Augustin, V., & Kins, S. (2021) · Cells · doi:10.3390/cells10071599 · Cited by 18
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 17
Aggregated Alpha-Synuclein Inclusions within the Nucleus Predict Impending Neuronal Cell Death in a Mouse Model of Parkinsonism
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 16
Sporadic C reutzfeldt– J akob disease subtype‐specific alterations of the brain proteome: Impact on R ab3a recycling
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
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
Self-citation
Actin-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
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

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)
ORCID: Bamburg, J.R.
Goldsbury, C.
Maloney, M.T.
Whiteman, I.
Wiggan, O.
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)
DOI: 10.2174/156720510791050902
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: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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

ADF/Cofilin-Actin Rods in Neurodegenerative Diseases

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks