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.
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“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]
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Cites
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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 1,547
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
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GAP-43 and BASP1 in Axon Regeneration: Implications for the Treatment of Neurodegenerative Diseases
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Roles of ADF/cofilin in actin polymerization and beyond
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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
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