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 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.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
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.
Citations
Cites
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
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
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
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
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
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
Items 101–173 of 173
Gα13 Contributes to LPS-Induced Morphological Alterations and Affects Migration of Microglia
Bettegazzi, B., Bellani, S., Cattaneo, S., Codazzi, F., Grohovaz, F., & Zacchetti, D. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02553-0 · Cited by 13
Cerebral Ischemia-Reperfusion Is Associated With Upregulation of Cofilin-1 in the Motor Cortex
Xu, M., Yin, L.-M., Cheng, A.-F., Zhang, Y., Zhang, D., Tao, M.-M., Deng, Y.-Y., Ge, L.-B., & Shan, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.634347 · Cited by 12
Kaushik, V., Brünnert, D., Hanschmann, E.-M., Sharma, P. K., Anand, B. G., Kar, K., Kateriya, S., & Goyal, P. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.07.013 · Cited by 12
Proline-rich transmembrane protein 2 (PRRT2) regulates the actin cytoskeleton during synaptogenesis
Savino, E., Cervigni, R. I., Povolo, M., Stefanetti, A., Ferrante, D., Valente, P., Corradi, A. M., Benfenati, F., Guarnieri, F. C., & Valtorta, F. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03073-w · Cited by 12
Verma, H., Kaur, S., Kaur, S., Gangwar, P., Dhiman, M., & Mantha, A. K. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04053-3 · Cited by 11
Fighting the Cause of Alzheimer’s and GNE Myopathy
Devi, S., Yadav, R., Chanana, P., & Arya, R. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00669 · Cited by 12
Nikitina, E. A., Медведева, А. В., Герасименко, М. С., Проников, В. С., Сурма, С. В., Щеголев, Б. Ф., & Savvateeva-Popova, E. V. (2018) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-018-0632-2 · Cited by 11
Wille, C., Eiseler, T., Langenberger, S.-T., Richter, J., Mizuno, K., Radermacher, P., Knippschild, U., Huber-Lang, M. S., Seufferlein, T. T. W., & Paschke, S. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.4a0617-251rr · Cited by 11
Behroozi, Z., Askarpour, H., & Baghcheghi, Y. (2026) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823261415807 · Cited by 10
Gallo, G. (2024) · Molecular Neurobiology · doi:10.1007/s12035-023-03879-7 · Cited by 15
Karayel‐Basar, M., Uras, I., Kiris, İ., Şahin, B., Akgün, E., & Baykal, A. T. (2022) · Molecular Omics · doi:10.1039/d1mo00440a · Cited by 10
De novoactin polymerization is required for model Hirano body formation inDictyostelium
Dong, Y., Shahid-Salles, S., Sherling, D., Fechheimer, N., Iyer, N., Wells, L., Fechheimer, M., & Furukawa, R. (2016) · Biology Open · doi:10.1242/bio.014944 · Cited by 10
RABV induces biphasic actin cytoskeletal rearrangement through Rac1 activity modulation
Liu, X., Xu, J., Zhang, M., Wang, H., Guo, X., Zhao, M., Duan, M., Guan, Z., & Guo, Y. (2024) · Journal of Virology · doi:10.1128/jvi.00606-24 · Cited by 9
Kim, Y., Lee, H.-K., Park, K., Ismail, T., Lee, H., Ryu, H., Cho, D., Kwon, T. K., Park, T. J., Kwon, T., et al. (2024) · Molecules and Cells · doi:10.1016/j.mocell.2024.100076 · Cited by 9
Pathak, S., Parkar, H., Tripathi, S., & Kale, A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.591579 · Cited by 9
Cytokine profile and glial activation following brachial plexus roots avulsion injury in mice
Zhong, K., Li, Y., Tang, Y., Yu, G., Zilundu, P. L. M., Wang, Y., Zhou, Y., Xu, X., Fu, R., & Zhou, L. (2021) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2021.577517 · Cited by 9
Ishikawa-Ankerhold, H. C., Kurzbach, S. C., Kinali, A. S., & Müller‐Taubenberger, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.742310 · Cited by 9
Abdellatif, M. E. A., Hipp, L., Plessner, M., Walther, P., & Knöll, B. (2019) · Histochemistry and Cell Biology · doi:10.1007/s00418-019-01795-3 · Cited by 9
Identification and functional characterization of Cofilin-1 as a new member of antimicrobial protein
Li, Y., Gong, Y., Chen, Y., Qu, B., & Zhang, S. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104281 · Cited by 9
Kukalev, A., Ng, Y., Ju, L., Saidi, A., Lane, S., Mondragon, A., Dormann, D., Walker, S. E., Grey, W. E., Ho, P. W., et al. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw354 · Cited by 8
Xiao, Y., Ma, H., Wan, P., Qin, D., Wang, X., Zhang, X., Xiang, Y., Liu, W., Chen, J., Yi, Z., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.759886 · Cited by 9
Dual role of cofilin in APP trafficking and amyloid‐β clearance
Liu, T., Woo, J. A., Yan, Y., LePochat, P., Bukhari, M. Z., & Kang, D. E. (2019) · The FASEB Journal · doi:10.1096/fj.201901268r · Cited by 10
Salem, F. B., Bunner, W., Prabhu, V. V., Kuyateh, A.-B., O’Bryant, C. T., Murashov, A. K., Szatmari, E. M., & Hughes, R. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012427 · Cited by 10
SRF deletion results in earlier disease onset in a mouse model of amyotrophic lateral sclerosis
Song, J., Dikwella, N., Sinske, D., Roselli, F., & Knöll, B. (2023) · JCI Insight · doi:10.1172/jci.insight.167694 · Cited by 8
Andrade, T. A., Fahel, J. S., de Souza, J. M., Terra, A. C. U., Souza, D. G., Costa, V. V., Teixeira, M. M., Bloise, E., & Ribeiro, F. M. (2022) · ASN NEURO · doi:10.1177/17590914221121257 · Cited by 8
Sui, H. X., Zhan, L., Niu, X., Liang, L., & Li, X. (2017) · Neuropeptides · doi:10.1016/j.npep.2017.03.001 · Cited by 8
Automated spatio-temporal analysis of dendritic spines and related protein dynamics
On, V., Zahedi, A., Ethell, I. M., & Bhanu, B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182958 · Cited by 7
Mitochondria and the Actin Cytoskeleton in Neurodegeneration
Tuli, S., Patel, P., Shethji, A., & Gau, D. M. (2026) · Cytoskeleton · doi:10.1002/cm.70095 · Cited by 7
Genetic admixture drives climate adaptation in the bank vole
Horníková, M., Lanier, H. C., Marková, S., Escalante, M. A., Searle, J. B., & Kotlı́k, P. (2024) · Communications Biology · doi:10.1038/s42003-024-06549-z · Cited by 7
Ghia, E. M., Widhopf, G. F., Rassenti, L. Z., & Kipps, T. J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.0902875 · Cited by 6
Ojeda, V., Robles‐Valero, J., Barreira, M., & Bustelo, X. R. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-01-0052 · Cited by 6
Microscopy basics and the study of actin–actin-binding protein interactions
Thomasson, M. S., & Macnaughtan, M. A. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.09.008 · Cited by 5
Focus on ADF/Cofilin: Beyond Actin Cytoskeletal Regulation
Tsai, C.-H., & Lee, Y. (2012) · ISRN Cell Biology · doi:10.5402/2012/597876 · Cited by 5
Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos
Biel, N., Figard, L., & Sokac, A. M. (2020) · Journal of Visualized Experiments · doi:10.3791/61297 · Cited by 4
Cheng, L. Z., Chen, H., Li, C., Cui, X., & Xu, Y. (2018) · Neuroreport · doi:10.1097/wnr.0000000000001162 · Cited by 4
An astrocyte-derived cytokine TIMP-1 restores synaptic plasticity in an Alzheimer’s disease modelPreprint
Sarkar, S., Gharami, K., Paidi, R. K., Srikumar, B. N., & Biswas, S. C. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.18.533245 · Cited by 4
Kim, S. W., Hong, I. K., Kim, M., Song, Y. S., & Kim, K. (2021) · Cells · doi:10.3390/cells10123567 · Cited by 3
Cao, T. H. M., Le, A. P. H., Tran, T. T., Huynh, V. K., Pham, B. H., Le, T., Nguyen, Q. L., Tran, T. C., Tong, T. M., Than, T. H. N., et al. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1308610 · Cited by 3
Bioenergetic and excitotoxic determinants of cofilactin rod formation
Mai, N., Wu, L., Uruk, G., Mocanu, E., & Swanson, R. A. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16065 · Cited by 3
Cytoskeletal Elements in Neurotoxicity*
Pyle, S. J., & Reuhl, K. R. (2010) · Elsevier eBooks · doi:10.1016/b978-0-08-046884-6.01306-3 · Cited by 3
Assignment of functional impact on genetic data in two mouse models of affective disorders
Widner-Andrä, R. (2012) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.14380 · Cited by 2
Jury-Garfe, N., You, Y.-W., Martínez, P., Redding-Ochoa, J., Karahan, H., Johnson, T., Zhang, J., Kim, J., Troncoso, J., & Lasagna-Reeves, C. A. (2023) · bioRxiv · doi:10.1101/2023.07.27.550884 · Cited by 2
Azargoonjahromi, A., Eivazi, M., Nasiri, H., Tarhriz, V., Payandeh, Z., & Initiative, A. D. N. (2025) · Journal of Molecular Neuroscience · doi:10.1007/s12031-025-02333-8 · Cited by 2
Cofilin Regulates Filopodial Structure and Flexibility in Neuronal Growth ConesPreprint
Hylton, R. K., Heebner, J. E., Grillo, M. A., & Swulius, M. T. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.17.460569 · Cited by 2
Hippocampal Cofilin and CFL1 gene variants are linked to Alcohol Use Disorder phenotypes
Salamian, A., Pagano, R., Skonieczna, E., Kalinichenko, L. S., Puchalska, M., Ünlü, G. Y., Gajewska‐Woźniak, O., Kruashvili, L. B., Grochowicz, M., Wojtaś, B., et al. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-03226-3 · Cited by 3
Cofilin hyperphosphorylation triggers TDP-43 pathology in sporadic amyotrophic lateral sclerosis
Jagaraj, C. J., Saravanabavan, S., Parakh, S., Jayakumar, M., Kashani, S. A., Shadfar, S., Mehta, P. M., Gautam, S., Farzana, F., Suchowerska, A. K., et al. (2026) · Brain · doi:10.1093/brain/awag096 · Cited by 1
A Method to Regulate Cofilin Transport Using Optogenetics and Live Video Analysis
Zahedi, A., On, V., & Ethell, I. M. (2015) · Computational biology · doi:10.1007/978-3-319-23724-4_15 · Cited by 1
On, V., Zahedi, A., Ethell, I. M., & Bhanu, B. (2016) · Proceedings - International Conference on Pattern Recognition/Proceedings/International Conference on Pattern Recognition · doi:10.1109/icpr.2016.7899936 · Cited by 1
Actin Polymerization: A Cellular Perspective for Motility
Pathak, S., Tripathi, S., Gauba, R., Dantu, S. C., & Kale, A. (2019) · Springer eBooks · doi:10.1007/978-981-13-7450-0_1 · Cited by 1
A high affinity Sybody blocks Cofilin-1 binding to F-actin in vitro and in cancer cells
Paraschiakos, T., Li, J., Scholz, J., Han, S.-J., Deckers, M., Pogenberg, V., Faix, J., & Windhorst, S. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116866 · Cited by 1
Madineni, A. (2013) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 1
Molecular fingerprints in the hippocampus of alcohol seeking during withdrawalPreprint
Pagano, R., Salamian, A., Skonieczna, E., Wojtaś, B., Gielniewski, B., Harda, Z., Cały, A., Havekes, R., Abel, T. G., & Radwańska, K. (2023) · Research Square · doi:10.1101/2023.08.24.554622 · Cited by 1
Stress-induced changes in gene transcriptions and translations related to Alzheimer’s disease
Sántha, P. (2014) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.2358
Molinar‐Inglis, O. (2015) · KiltHub Repository · doi:10.1184/r1/6714359
Salem, F. B., Prabhu, V. V., Kuyateh, A.-B., Bunner, W. P., Murashov, A. K., Szatmari, E. M., & Hughes, R. M. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/857706
Kaushik, V., Hanschmann, E.-M., Brünnert, D., Prerna, K., Anand, B. G., Sharma, P. K., Kar, K., & Goyal, P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.27.470221
Cytoskeletal Elements in Neurotoxicity
Pyle, S. J., & Meberg, P. J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.65380-1
Ellis, R. E. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733663076.793550458
Jagaraj, C. J., Mehta, P. M., Parakh, S., Shadfar, S., Jamali, S., Suchowerska, A. K., Sultana, J., Fath, T., & Atkin, J. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.28.555209 · Cited by 1
Davies, D., Arthur, A. T., Aitken, H., Crossett, B., & Goldsbury, C. S. (2024) · Biology Open · doi:10.1242/bio.060067
Self-citationMann, N., Surabhi, K. S., Sharp, J. F., Phipps, M., Becton, M., Hill, J., Roberts, D., Szatmari, E. M., & Hughes, R. M. (2025) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2025.1543199
Stringhi, R., Pelucchi, S., D’Andrea, L., Greca, F. L., Zianni, E., Targa, L., Mosconi, C., Vandermeulen, L., Ascagni, M., Speciani, M. C., et al. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.12.023
Additional file 1 of Synaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Figshare · doi:10.6084/m9.figshare.16599510
Neuronal growth regulator 1 modulates actin dynamics to control intracellular GLUT4 trafficking
Yun, S.-Y., & Lee, S. (2026) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00084.2026
Influence of a destabilizing factor, cofilin, on the mechanics of actin networks
Kopec, M. (2023) · theses.fr (ABES) · doi:10.70675/7fe0c472z1e47z412cz8dc5zc3b6b6b9ad88
Transsynaptic complex dysfunction in the hippocampus of Alzheimer’s disease patients
Hindle, A., Chen, Y., Yin, X., Mańczak, M., Decourt, B., & Neugebauer, V. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1837327
Structure and assembly of microfilaments
Tishkova, M. V., Golozubova, T. A., Artemov, A. V., Reushev, V. A., Константинович, Т. К., Fonin, A. V., Uversky, V. N., & Kuznetsova, I. М. (2026) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00092-5
Stephens, M. C., Han, R. I., Perez, A. M., Chester, H., de Haro, M., Ali, A., Hammett, A., Dere, R., Al‐Ramahi, I., & Botas, J. (2026) · Autophagy · doi:10.1080/15548627.2026.2752745
Huntingtin Nuclear Localization: Current Insights into Mechanism and Regulation
Desmond, C. R. (2012) · MacSphere (McMaster University) · doi:10.71548/9066
Metadata
- 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
- 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
