The DOI matches its Crossref record; 71 of the 71 references it cites were found in a registry or an index.
Aβ mediates F-actin disassembly in dendritic spines leading to cognitive deficits in Alzheimer's disease
Open accessAbstract
Dendritic spine loss is recognized as an early feature of Alzheimer's disease (AD), but the underlying mechanisms are poorly understood. Dendritic spine structure is defined by filamentous actin (F-actin) and we observed depolymerization of synaptosomal F-actin accompanied by increased globular-actin (G-actin) at as early as 1 month of age in a mouse model of AD (APPswe/PS1ΔE9, male mice). This led to recall deficit after contextual fear conditioning (cFC) at 2 months of age in APPswe/PS1ΔE9 male mice, which could be reversed by the actin-polymerizing agent jasplakinolide. Further, the F-actin-depolymerizing agent latrunculin induced recall deficit after cFC in WT mice, indicating the importance of maintaining F-/G-actin equilibrium for optimal behavioral response. Using direct stochastic optical reconstruction microscopy (dSTORM), we show that F-actin depolymerization in spines leads to a breakdown of the nano-organization of outwardly radiating F-actin rods in cortical neurons from APPswe/PS1ΔE9 mice. Our results demonstrate that synaptic dysfunction seen as F-actin disassembly occurs very early, before onset of pathological hallmarks in AD mice, and contributes to behavioral dysfunction, indicating that depolymerization of F-actin is causal and not consequent to decreased spine density. Further, we observed decreased synaptosomal F-actin levels in postmortem brain from mild cognitive impairment and AD patients compared with subjects with normal cognition. F-actin decrease correlated inversely with increasing AD pathology (Braak score, Aβ load, and tangle density) and directly with performance in episodic and working memory tasks, suggesting its role in human disease pathogenesis and progression. SIGNIFICANCE STATEMENT Synaptic dysfunction underlies cognitive deficits in Alzheimer's disease (AD). The cytoskeletal protein actin plays a critical role in maintaining structure and function of synapses. Using cultured neurons and an AD mouse model, we show for the first time that filamentous actin (F-actin) is lost selectively from synapses early in the disease process, long before the onset of classical AD pathology. We also demonstrate that loss of synaptic F-actin contributes directly to memory deficits. Loss of synaptosomal F-actin in human postmortem tissue correlates directly with decreased performance in memory test and inversely with AD pathology. Our data highlight that synaptic cytoarchitectural changes occur early in AD and they may be targeted for the development of therapeutics.
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 cited source says what the claim attributes to it.
In the citing paper
“Moreover, even low levels of Aβ can facilitate synaptic F-actin depolymerization and impair dendritic spines at very early stages of the pathology in an APP/presenilin 1 transgenic mouse model (64).”
From Deletion of Abi3 gene locus exacerbates neuropathological features of Alzheimer’s disease in a mouse model of Aβ amyloidosis (2021) · cites this paper as [64]
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
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“Dendritic spines undergo synaptic-activitydependent modifications such as enlargement and shrinkage/ elimination during LTP (Bosch et al., 2014) or LTD, respectively, and correlate with memory deficits in animal models (Holcomb et al., 1998; Lesné et al., 2006; Shankar et al., 2008).”
BackgroundRetractedThe Mouse Brain in Stereotaxic Coordinates
Paxinos, G. (2001) · Cited by 12,859
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
Rust, M., Bates, M., & Zhuang, X. (2006) · Nature Methods · doi:10.1038/nmeth929 · Cited by 7,823
Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396
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
An unbiased detector of curvilinear structures
Steger, C. T. (1998) · IEEE Transactions on Pattern Analysis and Machine Intelligence · doi:10.1109/34.659930 · Cited by 1,436
Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386
Actin, Spectrin, and Associated Proteins Form a Periodic Cytoskeletal Structure in Axons
Xu, K., Zhong, G., & Zhuang, X. (2012) · Science · doi:10.1126/science.1232251 · Cited by 1,269
Direct stochastic optical reconstruction microscopy with standard fluorescent probes
van de Linde, S., Löschberger, A., Klein, T., Heidbreder, M., Wolter, S., Heilemann, M., & Sauer, M. (2011) · Nature Protocols · doi:10.1038/nprot.2011.336 · Cited by 1,104
Natural history of mild cognitive impairment in older persons
Bennett, D. A., Wilson, R. S., Schneider, J. A., Evans, D. A., Beckett, L. A., Aggarwal, N. T., Barnes, L. L., Fox, J. H., & Bach, J. (2002) · Neurology · doi:10.1212/wnl.59.2.198 · Cited by 1,037
Self-citationProteins 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
Biomarker Modeling of Alzheimer’s Disease
Jack, C. R., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.12.003 · Cited by 1,002
Okamoto, K.-I., Nagai, T., Miyawaki, A., & Hayashi, Y. (2004) · Nature Neuroscience · doi:10.1038/nn1311 · Cited by 854
Individual differences in rates of change in cognitive abilities of older persons.
Wilson, R. S., Beckett, L. A., Barnes, L. L., Schneider, J. A., Bach, J., Evans, D. A., & Bennett, D. A. (2002) · Psychology and Aging · doi:10.1037/0882-7974.17.2.179 · Cited by 842
Self-citationActin in dendritic spines: connecting dynamics to function
Hotulainen, P., & Hoogenraad, C. C. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003008 · Cited by 815
Kilgore, M., Miller, C. A., Fass, D. M., Hennig, K. M., Haggarty, S. J., Sweatt, J. D., & Rumbaugh, G. (2010) · Neuropsychopharmacology · doi:10.1038/npp.2009.197 · Cited by 727
ADF/Cofilin: a functional node in cell biology
Bernstein, B. W., & Bamburg, J. R. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.001 · Cited by 704
A trans-synaptic nanocolumn aligns neurotransmitter release to receptors
Tang, A.-H., Chen, H., Li, T. P., Metzbower, S. R., MacGillavry, H. D., & Blanpied, T. A. (2016) · Nature · doi:10.1038/nature19058 · Cited by 677 · cited 1×
“We then performed dSTORM (Rust et al., 2006; van de Linde et al., 2011; Tang et al., 2016) of F-actin at mushroom spine heads (as indicated by morphology and presence of Homer1 puncta) in WT neurons and APP/PS1 neurons actin is arranged as radiating structures from the base of the spine head (Fig.”
MethodCulturing pyramidal neurons from the early postnatal mouse hippocampus and cortex
Beaudoin, G. M. J., Lee, S.-H., Singh, D., Yuan, Y., Ng, Y., Reichardt, L. F., & Arikkath, J. (2012) · Nature Protocols · doi:10.1038/nprot.2012.099 · Cited by 675
Overview and Findings from the Religious Orders Study
Bennett, D. A., Schneider, J. A., Arvanitakis, Z., & Wilson, R. S. (2012) · Current Alzheimer Research · doi:10.2174/156720512801322573 · Cited by 656
Self-citationFibrilTool, an ImageJ plug-in to quantify fibrillar structures in raw microscopy images
Boudaoud, A., Burian, A., Borowska-Wykręt, D., Uyttewaal, M., Wrzalik, R., Kwiatkowska, D., & Hamant, O. (2014) · Nature Protocols · doi:10.1038/nprot.2014.024 · Cited by 647
Structural and Molecular Remodeling of Dendritic Spine Substructures during Long-Term Potentiation
Bosch, M., Castro, J., Saneyoshi, T., Matsuno, H., Sur, M., & Hayashi, Y. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.021 · Cited by 637
Nair, D., Hosy, E., Petersen, J. D., Constals, A., Giannone, G., Choquet, D., & Sibarita, J.-B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2381-12.2013 · Cited by 617
Self-citationFibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches
Tsai, J., Grutzendler, J., Duff, K., & Gan, W.-B. (2004) · Nature Neuroscience · doi:10.1038/nn1335 · Cited by 561
Spires, T. L., Meyer-Luehmann, M., Stern, E. A., McLean, P. J., Skoch, J., Nguyen, P. T., Bacskai, B. J., & Hyman, B. T. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1879-05.2005 · Cited by 550 · cited 2×
“, 2007) and in postmortem brains from AD patients (Tsai et al., 2004; Spires et al., 2005; SpiresJones et al., 2007).”
BackgroundMild cognitive impairment is related to Alzheimer disease pathology and cerebral infarctions
Bennett, D. A., Schneider, J. A., Bienias, J. L., Evans, D. A., & Wilson, R. S. (2005) · Neurology · doi:10.1212/01.wnl.0000152982.47274.9e · Cited by 537
Self-citationBennett, D. A., Schneider, J. A., Wilson, R. S., Bienias, J. L., & Arnold, S. E. (2004) · Archives of Neurology · doi:10.1001/archneur.61.3.378 · Cited by 526
Self-citationRapid turnover of actin in dendritic spines and its regulation by activity
Star, E. N., Kwiatkowski, D. J., & Murthy, V. N. (2002) · Nature Neuroscience · doi:10.1038/nn811 · Cited by 481
The actin cytoskeleton: integrating form and function at the synapse
Dillon, C., & Goda, Y. (2005) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.28.061604.135757 · Cited by 447
Bennett, D. A., Schneider, J. A., Aggarwal, N. T., Arvanitakis, Z., Shah, R. C., Kelly, J. F., Fox, J. H., Cochran, E. J., Arends, D., Treinkman, A., et al. (2006) · Neuroepidemiology · doi:10.1159/000096129 · Cited by 411
Self-citationKorobova, F., & Svitkina, T. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0596 · Cited by 399
Hotulainen, P., Paunola, E., Vartiainen, M. K., & Lappalainen, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0555 · Cited by 384
Stain-Free technology as a normalization tool in Western blot analysis
Gürtler, A., Kunz, N., Gomolka, M., Hornhardt, S., Friedl, A. A., McDonald, K., Kohn, J. E., & Posch, A. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.10.010 · Cited by 369
Wu, H.-Y., Hudry, E., Hashimoto, T., Kuchibhotla, K., Rozkalne, A., Fan, Z., Spires-Jones, T., Xie, H., Arbel-Ornath, M., Grosskreutz, C. L., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4456-09.2010 · Cited by 367
Hotulainen, P., Llano, O., Smirnov, S., Tanhuanpää, K., Faix, J., Rivera, C., & Lappalainen, P. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200809046 · Cited by 360
Stain-Free total protein staining is a superior loading control to β-actin for Western blots
Gilda, J. E., & Gomes, A. V. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.05.027 · Cited by 349
ADF/cofilin-mediated actin dynamics regulate AMPA receptor trafficking during synaptic plasticity
Gu, J., Lee, C. W., Fan, Y., Komlos, D., Tang, X., Sun, C., Yu, K., Hartzell, H. C., Chen, G., Bamburg, J. R., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2634 · Cited by 344
Okamoto, K.-I., Narayanan, R., Lee, S. H., Murata, K., & Hayashi, Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701656104 · Cited by 328
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
mTORC2 controls actin polymerization required for consolidation of long-term memory
Huang, W., Zhu, P. J., Zhang, S., Zhou, H., Stoica, L., Galiano, M., Krnjević, K., Roman, G., & Costa-Mattioli, M. (2013) · Nature Neuroscience · doi:10.1038/nn.3351 · Cited by 307
Frost, N. A., Shroff, H., Kong, H., Betzig, E., & Blanpied, T. A. (2010) · Neuron · doi:10.1016/j.neuron.2010.05.026 · Cited by 275
Post-translational modification and regulation of actin
Terman, J. R., & Kashina, A. S. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.10.009 · Cited by 232
Wavelet analysis for single molecule localization microscopy
Izeddin, I., Boulanger, J., Racine, V., Specht, C. G., Kechkar, A., Nair, D. K., Triller, A., Choquet, D., Dahan, M., & Sibarita, J. (2012) · Optics Express · doi:10.1364/oe.20.002081 · Cited by 227
Self-citationDendritic Spine Pathology in Neurodegenerative Diseases
Herms, J., & Dorostkar, M. M. (2016) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044216 · Cited by 201 · cited 3×
“Synaptic dysfunction seen as loss of dendritic spines in mouse models of AD (Wu et al., 2010; Herms and Dorostkar, 2016) and that observed as decreased glucose utilization (FDG-PET imaging) in human subjects precedes the overt appearance of behavioral/cognitive dysfunction (Jack and Holtzman, 2013; Jack et al.”
BackgroundRivero‐Gutiérrez, B., Anzola, A., Martínez‐Augustin, O., & de Medina, F. S. (2014) · Analytical Biochemistry · doi:10.1016/j.ab.2014.08.027 · Cited by 197
Impaired Spine Stability Underlies Plaque-Related Spine Loss in an Alzheimer's Disease Mouse Model
Spires-Jones, T. L., Meyer-Luehmann, M., Osetek, J. D., Jones, P. B., Stern, E. A., Bacskai, B. J., & Hyman, B. T. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070055 · Cited by 189
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
Blanpied, T. A., & Ehlers, M. (2004) · Biological Psychiatry · doi:10.1016/j.biopsych.2003.10.006 · Cited by 187
Heredia, L., Helguera, P. R., de Olmos, S., Kedikian, G., Vigo, F. S., LaFerla, F. M., Staufenbiel, M., de Olmos, J. S., Busciglio, J. A., Cáceres, A., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.5567-05.2006 · Cited by 184
Actin dynamics and cofilin‐actin rods in alzheimer disease
Bamburg, J. R., & Bernstein, B. W. (2016) · Cytoskeleton · doi:10.1002/cm.21282 · Cited by 181
Volianskis, A., Køstner, R., Mølgaard, M., Hass, S., & Jensen, M. S. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.08.005 · Cited by 179
ADF/Cofilin-Actin Rods in Neurodegenerative Diseases
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., et al. (2010) · Current Alzheimer Research · doi:10.2174/156720510791050902 · Cited by 173
SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics
Hung, R., Spaeth, C. S., Yesilyurt, H. G., & Terman, J. R. (2013) · Nature Cell Biology · doi:10.1038/ncb2871 · Cited by 155
Synaptic Mitochondrial Pathology in Alzheimer's Disease
Du, H., Guo, L., & Yan, S. S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4277 · Cited by 154
Chazeau, A., Mehidi, A., Nair, D. K., Gautier, J. J., Leduc, C., Chamma, I., Kage, F., Kechkar, A., Thoumine, O. R., Rottner, K., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488837 · Cited by 147
Self-citationComparison of Stain-Free gels with traditional immunoblot loading control methodology
Colella, A. D., Chegeni, N., Tea, M. N., Gibbins, I. L., Williams, K. A., & Chataway, T. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.08.015 · Cited by 138
Calpain Activation in Alzheimer's Model Mice Is an Artifact of APP and Presenilin Overexpression
Saito, T., Matsuba, Y., Yamazaki, N., Hashimoto, S., & Saido, T. C. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.1907-16.2016 · Cited by 121
Western Blotting Using In-Gel Protein Labeling as a Normalization Control: Stain-Free Technology
Gilda, J. E., & Gomes, A. V. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2550-6_27 · Cited by 101
Woo, J. A., Zhao, X., Khan, H., Penn, C., Wang, X., Joly-Amado, A., Weeber, E., Morgan, D., & Kang, D. E. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.5 · Cited by 99
Ahmad, F., Singh, K. P., Das, D., Gowaikar, R., Shaw, E., Ramachandran, A., Rupanagudi, K. V., Kommaddi, R. P., Bennett, D. A., & Ravindranath, V. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6860 · Cited by 99
Self-citationLiu, D.-S., Pan, X.-D., Zhang, J., Shen, H., Collins, N. C., Cole, A. M., Koster, K. P., Ben Aissa, M., Dai, X.-M., Zhou, M., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0002-2 · Cited by 99
Hippocampal Drebrin Loss in Mild Cognitive Impairment
Counts, S., He, B., Nadeem, M., Wuu, J., Scheff, S. W., & Mufson, E. J. (2012) · Neurodegenerative Diseases · doi:10.1159/000333122 · Cited by 88
Cummings, D. M., Liu, W., Portelius, E., Bayram, S., Yasvoina, M. V., Ho, H., Smits, H., Ali, S. S., Steinberg, R., Pegasiou, C.-M., et al. (2015) · Brain · doi:10.1093/brain/awv127 · Cited by 84
Automatic Dendritic Spine Quantification from Confocal Data with Neurolucida 360
Dickstein, D. L., Dickstein, D. R., Janssen, W. G. M., Hof, P. R., Glaser, J. R., Rodriguez, A., O'Connor, N., Angstman, P. J., & Tappan, S. J. (2016) · Current Protocols in Neuroscience · doi:10.1002/cpns.16 · Cited by 78
Nanguneri, S., Flottmann, B., Horstmann, H., Heilemann, M., & Kuner, T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038098 · Cited by 74
Self-citationInactivation of brain Cofilin-1 by age, Alzheimer's disease and γ-secretase
Barone, E., Mosser, S., & Fraering, P. C. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.10.004 · Cited by 63
Bonardi, C., de Pulford, F., Jennings, D. J., & Pardon, M. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.03.041 · Cited by 62
SuReSim: simulating localization microscopy experiments from ground truth models
Venkataramani, V., Herrmannsdörfer, F., Heilemann, M., & Kuner, T. (2016) · Nature Methods · doi:10.1038/nmeth.3775 · Cited by 61
Mendoza‐Naranjo, A., Contreras-Vallejos, E., Henríquez, D. R., Carola Otth, L., Bamburg, J. R., Maccioni, R. B., & González-Billault, C. E. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-101575 · Cited by 51
Efimova, N., Korobova, F., Stankewich, M. C., Moberly, A. H., Stolz, D. B., Wang, J., Kashina, A., Ma, M., & Svitkina, T. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.3520-16.2017 · Cited by 50
Flagged first, then by citations
Cited by
Sorted by citations
Religious Orders Study and Rush Memory and Aging Project
Bennett, D. A., Buchman, A. S., Boyle, P. A., Barnes, L. L., Wilson, R. S., & Schneider, J. A. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179939 · Cited by 1,260
Self-citationDejanovic, B., Huntley, M. A., De Mazière, A., Meilandt, W. J., Wu, T., Srinivasan, K., Jiang, Z., Gandham, V., Friedman, B. A., Ngu, H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.014 · Cited by 517
Neuroprotective Effects of Quercetin in Alzheimer’s Disease
Khan, H. Z., Ullah, H., Aschner, M., Cheang, W. S., & Akkol, E. K. (2019) · Biomolecules · doi:10.3390/biom10010059 · Cited by 563
Amyloid Beta in Aging and Alzheimer’s Disease
Sehar, U., Rawat, P., Reddy, A. P., Kopel, J. J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112924 · Cited by 409
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
Metadata
- Authors
- Kommaddi, R. P., Das, D., Karunakaran, S., Nanguneri, S., Bapat, D., Ray, A., Shaw, E., Bennett, D. A., Nair, D., & Ravindranath, V.
- Affiliations
- Indian Institute of Science Bangalore (IN)
- Rush University Medical Center (US)
- Corresponding author
- Ravindranath, Vijayalakshmi
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2017-12-15
- Volume
- 38
- Issue
- 5
- Pages
- 1085-1099
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC5792472
- OpenAlex
- W2774657197
- Cited by
- 135
- References
- 71
- Citations by year
- 2026: 3 · 2025: 22 · 2024: 13 · 2023: 16 · 2022: 13 · 2021: 25 · 2020: 17 · 2019: 20 · 2018: 6
- FWCI
- 8.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- NOT FOUND REPOSITORY (Indian Institute of Science Bangalore) (acceptedVersion)
- Funders
- Tata Trusts
- Science and Engineering Research Board (PDF/2016/003226)
- National Institute on Aging (R01AG017917, R01AG015819, P30AG010161, RF1AG015819)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta, F-actin depolymerization, dendritic spines, actin cytoskeleton, synaptic dysfunction, APPswe/PS1ΔE9 mice, contextual fear conditioning, memory impairment, jasplakinolide, latrunculin, actin polymerization, postmortem brain, working memory
- MeSH terms
- Actins, Aging, Alzheimer Disease, Animals, Autopsy, Cognition Disorders, Conditioning, Classical, Fear, Female, Humans, Male, Mice, Inbred C57BL, Mice, Transgenic, Mental Recall, Synaptosomes, Amyloid beta-Peptides, Dendritic Spines, Actin Depolymerizing Factors, Mice, Cognitive Dysfunction, Primary Cell Culture
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
