The DOI matches its Crossref record; 89 of the 89 references it cites were found in a registry or an index.
AKAP Signaling Complexes in Regulation of Excitatory Synaptic Plasticity
Open accessAbstract
Plasticity at excitatory glutamatergic synapses in the central nervous system is believed to be critical for neuronal circuits to process and encode information, allowing animals to perform complex behaviors such as learning and memory. In addition, alterations in synaptic plasticity are associated with human diseases, including Alzheimer disease, epilepsy, chronic pain, drug addiction, and schizophrenia. Long-term potentiation (LTP) and depression (LTD) in the hippocampal region of the brain are two forms of synaptic plasticity that increase or decrease, respectively, the strength of synaptic transmission by postsynaptic AMPA-type glutamate receptors. Both LTP and LTD are induced by activation of NMDA-type glutamate receptors but differ in the level and duration of Ca 2+ influx through the NMDA receptor and the subsequent engagement of downstream signaling by protein kinases, including PKA, PKC, and CaMKII, and phosphatases, including PP1 and calcineurin-PP2B (CaN). This review addresses the important emerging roles of the A-kinase anchoring protein family of scaffold proteins in regulating localization of PKA and other kinases and phosphatases to postsynaptic multiprotein complexes that control NMDA and AMPA receptor function during LTP and LTD.
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
“AKAP5 anchors both PKA and CaN to GluA1 allowing for the efficient coordination of these signaling pathways during LTD (Sanderson and Dell'Acqua, 2011).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Sanderson and Dell'Acqua, 2011
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
Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968
Glutamate receptor ion channels
Mayer, M. L. (2005) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2005.05.004 · Cited by 3,655
The Glutamate Receptor Ion Channels
Dingledine, R., Borges, K., Bowie, D., & Traynelis, S. F. (1999) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01394-2 · Cited by 3,554
Hayashi, Y., Shi, S.-H., Esteban, J. A., Piccini, A., Poncer, J.-C., & Malinow, R. (2000) · Science · doi:10.1126/science.287.5461.2262 · Cited by 1,524
Addiction and the brain: The neurobiology of compulsion and its persistence
Hyman, S. E., & Malenka, R. C. (2001) · Nature reviews. Neuroscience · doi:10.1038/35094560 · Cited by 1,337
Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms
Chen, L., Chetkovich, D. M., Petralia, R. S., Sweeney, N. T., Kawasaki, Y., Wenthold, R. J., Bredt, D. S., & Nicoll, R. A. (2000) · Nature · doi:10.1038/35050030 · Cited by 1,111
Reinsertion or Degradation of AMPA Receptors Determined by Activity-Dependent Endocytic Sorting
Ehlers, M. D. (2000) · Neuron · doi:10.1016/s0896-6273(00)00129-x · Cited by 1,096
AKAP signalling complexes: focal points in space and time
Wong, W., & Scott, J. D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1527 · Cited by 1,073
Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
Barria, A., Muller, D., Derkach, V., Griffith, L. C., & Soderling, T. R. (1997) · Science · doi:10.1126/science.276.5321.2042 · Cited by 1,049
The cell biology of synaptic plasticity: AMPA receptor trafficking
Shepherd, J. D., & Huganir, R. L. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123516 · Cited by 978
Cited by
Sorted by citations
Items 101–185 of 185
AKAPS Act in a Two-Step Mechanism of Memory Acquisition
Scheunemann, L., Skroblin, P., Hundsrucker, C., Klußmann, E., Efetova, M., & Schwärzel, M. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1303-13.2013 · Cited by 17
Kähne, T., Richter, S., Kolodziej, A., Smalla, K., Pielot, R., Engler, A., Ohl, F. W., Dieterich, D. C., Seidenbecher, C. I., Tischmeyer, W., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13636 · Cited by 16
AKAP79/150 interacts with the neuronal calcium‐binding protein caldendrin
Gorny, X., Mikhaylova, M., Seeger, C., Reddy, P. P., Reißner, C., Schott, B. H., Danielson, U. H., Kreutz, M. R., & Seidenbecher, C. I. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07828.x · Cited by 17
Prikhodko, O., Freund, R. K., Sullivan, E. M., Kennedy, M. J., & Dell’Acqua, M. L. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0675-24.2024 · Cited by 16
Self-citationMcClatchy, D. B., Savas, J. N., Martínez‐Bartolomé, S., Park, S. K., Maher, P. A., Powell, S. B., & Yates, J. R. (2015) · Molecular Psychiatry · doi:10.1038/mp.2015.41 · Cited by 14
Jayakar, S. S., Pugh, P. C., Dale, Z., Starr, E. R., Cole, S., & Margiotta, J. F. (2014) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2014.08.007 · Cited by 17
He, Y., Kulasiri, D., & Samarasinghe, S. (2014) · Biosystems · doi:10.1016/j.biosystems.2014.06.005 · Cited by 15
Zhang, J., & Shapiro, M. S. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.287698 · Cited by 15
Wang, Q., Li, D., Bubula, N., Campioni, M. R., McGehee, D. S., & Vezina, P. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.02.018 · Cited by 16
PKA-RIIβ autophosphorylation modulates PKA activity and seizure phenotypes in mice
Zhang, J., Zhang, C., Chen, X., Wang, B., Ma, W., Yang, Y., Zheng, R., & Huang, Z. (2021) · Communications Biology · doi:10.1038/s42003-021-01748-4 · Cited by 15
Guercio, L. A., Hofmann, M. E., Swinford-Jackson, S. E., Sigman, J. S., Wimmer, M. E., Dell’Acqua, M. L., Schmidt, H. D., & Pierce, R. C. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2017.297 · Cited by 13
Self-citationSynaptic PSD-95 biology: from localization and interactors to N-terminus function
Alkaas, A., Kurup, P., Kanuru, S., Rommel, A. V., Singh, T., Patel, M. J., & Delgado, J. Y. (2025) · Journal of Neurophysiology · doi:10.1152/jn.00272.2025 · Cited by 16
Man, K. N. M., Bartels, P., Henderson, P. B., Kim, K., Shi, M., Zhang, M., Ho, S., Nieves‐Cintrón, M., Navedo, M. F., Horne, M. C., et al. (2023) · eLife · doi:10.7554/elife.79648 · Cited by 14
Bernstein, H., Dobrowolny, H., Schott, B. H., Gorny, X., Becker, V., Steiner, J. H., Seidenbecher, C. I., & Bogerts, B. (2013) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2012.12.020 · Cited by 13
Mirisis, A. A., Alexandrescu, A., Carew, T. J., & Kopec, A. M. (2016) · AIMS neuroscience · doi:10.3934/neuroscience.2016.3.356 · Cited by 12
Gaydukov, A. E., Tarasova, E. O., & Balezina, O. P. (2013) · Neurochemical Journal · doi:10.1134/s1819712413010030 · Cited by 12
Vezatin regulates seizures by controlling AMPAR-mediated synaptic activity
Wang, Y., Yuan, J., Yu, X., Liu, X., Tan, C., Chen, Y., & Xu, T. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04233-2 · Cited by 12
The structural basis of the G protein–coupled receptor and ion channel axis
Luo, Y., Sun, L., & Peng, Y. (2025) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2025.100165 · Cited by 12
Regulation of NMDA Receptor Signaling at Single Synapses by Human Anti-NMDA Receptor Antibodies
Dean, C. A., Metzbower, S. R., Dessain, S. K., Blanpied, T. A., & Benavides, D. R. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.940005 · Cited by 11
Tourette Syndrome Risk Genes Regulate Mitochondrial Dynamics, Structure, and Function
Clarke, R. A., Furlong, T. M., & Eapen, V. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2020.556803 · Cited by 10
Challenor, M., Doig, R. O., Fuller-Carter, P. I., Giacci, M. K., Bartlett, C. A., Wale, C. H., Cozens, G. S., Hool, L. C., Dunlop, S. A., Iyer, K. S., et al. (2015) · Biochimie · doi:10.1016/j.biochi.2015.03.008 · Cited by 11
Behroozi, Z., Askarpour, H., & Baghcheghi, Y. (2026) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823261415807 · Cited by 10
Simmons, S. C., Flerlage, W. J., Langlois, L. D., Shepard, R. D., Bouslog, C., Thomas, E. H., Gouty, K. M., Sanderson, J. L., Gouty, S., Cox, B. M., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06041-8 · Cited by 11
Self-citationInhibition of ANXA2 activity attenuates epileptic susceptibility and GluA1 phosphorylation
Ma, L., Wu, Q., Yuan, J., Wang, Y., Zhang, P., Liu, Q., Tan, D., Liang, M., & Chen, Y. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14295 · Cited by 10
Itakura, M., Watanabe, I., Sugaya, T., & Takahashi, M. (2014) · FEBS Journal · doi:10.1111/febs.12708 · Cited by 10
Huang, Y., Hu, L., Li, H., Huang, Y., Li, Y., Yang, J., Gu, J., & Xu, H. (2019) · Psychiatry Research · doi:10.1016/j.psychres.2019.112497 · Cited by 10
Proteasomal-Mediated Degradation of AKAP150 Accompanies AMPAR Endocytosis during cLTD
Cheng, W., Siedlecki‐Wullich, D., Català-Solsona, J., Fábregas, C., Fadó, R., Casals, N., Solé, M., Unzeta, M., Saura, C. A., Rodrı́guez-Álvarez, J., et al. (2020) · eNeuro · doi:10.1523/eneuro.0218-19.2020 · Cited by 10
A Role for Second Messengers in Axodendritic Neuronal Polarity
Urrutia, P. J., & González-Billault, C. (2023) · The Journal of Neuroscience · doi:10.1523/jneurosci.1065-19.2023 · Cited by 9
Bai, X., Zhang, K., Ou, C., Mu, Y., Chi, D., Zhang, J., Huang, J., Li, X., Zhang, Y., Huang, W., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108227 · Cited by 8
Protein kinase A is a functional component of focal adhesions
Kang, M., Senatore, A. J., Naughton, H., McTigue, M., Beltman, R. J., Herppich, A. A., Pflum, M. K. H., & Howe, A. K. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107234 · Cited by 9
Li, L., Sase, A., Patil, S. S., Sunyer, B., Höger, H., Smalla, K., Stork, O., & Lübec, G. (2013) · Hippocampus · doi:10.1002/hipo.22127 · Cited by 8
Seeger, C., Gorny, X., Reddy, P. P., Seidenbecher, C. I., & Danielson, U. H. (2012) · Journal of Molecular Recognition · doi:10.1002/jmr.2215 · Cited by 11
Calcium, Calpain, and Calcineurin in Low-Frequency Depression of Transmitter Release
Silverman‐Gavrila, L. B., Praver, M., Mykles, D. L., & Charlton, M. P. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3092-12.2013 · Cited by 10
Disrupting sensitization of TRPV4
Mack, K., & Fischer, M. J. M. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.03.037 · Cited by 9
How anchoring proteins shape pain
Fischer, M. J. M., & McNaughton, P. A. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.04.001 · Cited by 9
Calpain Interactions with the Protein Phosphatase Calcineurin in Neurodegeneration
Norris, C. M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9099-9_2 · Cited by 8
Biochemical Analysis of AKAP-Anchored PKA Signaling Complexes
Byrne, D. P., Omar, M. H., Kennedy, E. J., Eyers, P. A., & Scott, J. D. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2245-2_19 · Cited by 8
AMPA Receptor Antagonist NBQX Decreased Seizures by Normalization of Perineuronal Nets
Chen, W., Li, Y.-S., Gao, J., Lin, X.-Y., & Li, X. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166672 · Cited by 8
Saccà, S. C., Cutolo, C. A., & Rossi, T. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-3681-2_14 · Cited by 8
Lai, C., He, W., Yang, H., Lai, J., & Huang, S. (2025) · Neurological Research · doi:10.1080/01616412.2025.2520017 · Cited by 7
Structural Analysis of Hippocampal Kinase Signal Transduction
McClatchy, D. B., Yu, N., Martínez‐Bartolomé, S., Patel, R. R., Pelletier, A. R., Lavallée‐Adam, M., Powell, S. B., Roberto, M., & Yates, J. R. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00284 · Cited by 8
Wang, S., Xia, Z., Yang, S., Chen, W., Zhao, Y., Li, M., Tian, D., Pan, Y., Lin, X., Zhu, X., et al. (2024) · British Journal of Pharmacology · doi:10.1111/bph.16318 · Cited by 9
Light regulated SIK1 remodels the synaptic phosphoproteome to induce sleepPreprint
Taylor, L., Palumaa, T., Reardon, P. K., Walsh, S., Johnson, B., Liberatori, S., Hasan, S., Clark, K., Cohen, P., Vasudevan, S. R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.28.462159 · Cited by 8
Qiao, L., Getz, M., Gross, B., Tenner, B., Zhang, J., & Rangamani, P. (2024) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1012564 · Cited by 6
Phosphoproteome profiling of hippocampal synaptic plasticity
Lim, S., Lee, N.-Y., Ryu, J. Y., An, J. H., Lee, G. S., Min, S. S., Moon, J., & Lee, J.-R. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.07.051 · Cited by 6
Proteomic Analyses of PKA and AKAP Signaling in Cocaine Addiction
Reissner, K. J. (2012) · Neuropsychopharmacology · doi:10.1038/npp.2012.181 · Cited by 6
Modulation of Neurotransmission by the GABAB Receptor
Kantamneni, S. (2016) · Springer eBooks · doi:10.1007/978-3-319-46044-4_7 · Cited by 6
Chu, C.-C., Hu, Y.-H., Li, G.-Z., Chen, J., Zhang, N.-N., Gu, Y., Wu, S., Zhang, H., Xu, Y.-Y., Guo, H.-L., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106812 · Cited by 4
Lee, Y., Kim, H., Barker, D., Vijayvargia, R., Atwal, R. S., Specht, H., Keshishian, H., Carr, S. A., Lee, R., Kwak, S., et al. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac165 · Cited by 4
Aleebrahim‐Dehkordi, E., Jafari, A., Bala, A. A., Lagzian, A., Ghoshouni, H., Koochaki, P., Hamedanchi, N. F., Azadeh-Ghahfaroghi, S. Z., Azadikhah, F., Taei, N., et al. (2024) · The Natural Products Journal · doi:10.2174/0122103155289394240522110321 · Cited by 4
Vascular CaV1.2 channels in diabetes
Silva, E. A. P., Baudel, M. A. S. M., Hong, J., Bartels, P., Navedo, M. F., & Nieves‐Cintrón, M. (2022) · Current topics in membranes · doi:10.1016/bs.ctm.2022.09.003 · Cited by 4
Koster, K. P., Fyke, Z., Nguyen, T. T. A., Niqula, A., Noriega-González, L. Y., Woolfrey, K. M., Dell’Acqua, M. L., Cologna, S. M., & Yoshii, A. (2024) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2024.1384625 · Cited by 3
Self-citationBringing the Signal into the Nucleus
Kramer, I. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394803-8.00007-3 · Cited by 4
Wang, T., Liu, Y., Liu, X., Wei, X. P., Ding, X., Mo, L., Wang, H., Zhou, W., Xu, T., Deng, F., et al. (2018) · Neuroreport · doi:10.1097/wnr.0000000000001088 · Cited by 4
Neuroplasticity, Sensitization, and Pain
Ray, A. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1821-8_2 · Cited by 4
Role of calcineurin and ionotropic glutamate receptors in Alzheimer's disease: A systematic review
Teklemariam, A. B., Zewde, E. A., Agidew, M. M., Siyamrew, S. A., Maru, L., & Muche, Z. T. (2025) · Brain Disorders · doi:10.1016/j.dscb.2025.100218 · Cited by 3
Neuroplasticity, Sensitization, and Pain
Ray, A. (2012) · Springer eBooks · doi:10.1007/978-1-4614-1560-2_71 · Cited by 3
Highly Sensitive Chemigenetic FRET-Based Kinase BiosensorsPreprint
He, X., Zhou, D. R., Yu, H., Berriman-Rozen, Z. D., Mehta, S., Chen, Y., Frei, M. S., & Zhang, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.06.702961 · Cited by 3
Javed, E., Nayak, A. P., Jannu, A. K., Cohen, A. H., Dewes, I., Wang, R., Tang, D. D., Deshpande, D. A., & Penn, R. B. (2024) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2023-0358oc · Cited by 2
Uyhelji, H., Nicholson, S. J., Nesthus, T. E., Beckel, J. L. O., Klerman, E. B., Czeisler, C. A., Yuan, R. K., Arrona‐Palacios, A., Song, P., Ronda, J. M., et al. (2025) · BMC Genomics · doi:10.1186/s12864-025-12193-6 · Cited by 2
Hypothetical gene C18orf42 encodes a novel protein kinase A‐binding protein
Fukuda, M., & Aizawa, Y. (2015) · Genes to Cells · doi:10.1111/gtc.12217 · Cited by 2
Modulation of VGCCs by G-Protein Coupled Receptors and Their Second Messengers
Mark, M. D., Schwitalla, J. C., & Herlitze, S. (2022) · Springer eBooks · doi:10.1007/978-3-031-08881-0_7 · Cited by 2
Hu, P., Maita, I., Kwok, C., Gu, E., Gergues, M. M., Liu, J., Pang, Z. P., Swaab, D. F., Lucassen, P. J., Roepke, T. A., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/572966 · Cited by 2
Koster, K. P., Flores-Barrera, E., de la Villarmois, E. A., Nguyen, T. T. A., Niqula, A., Noriega-González, L. Y., Fyke, Z., Caballero, A., Cologna, S. M., Tseng, K. Y., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.16.473002 · Cited by 2
Thomas, R. E., Hernández, A., Benavides, D. R., Li, W., Tan, C., Umfress, A., Plattner, F., Chakraborti, A., Pozzo‐Miller, L. D., Taylor, S. S., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102245 · Cited by 2
Modulation of the Core Neural Network in Stress: The Role of Endocannabinoids and LTD
Bennett, M. R., & Lagopoulos, J. (2018) · Springer eBooks · doi:10.1007/978-3-319-91116-8_5 · Cited by 1
Neural firing rate homeostasis via inhibitory synaptic plasticity
Xue, X.-D., Wang, M., Shao, Y.-Z., & Wang, J. (2019) · Acta Physica Sinica · doi:10.7498/aps.68.20182234 · Cited by 1
Investigation Of The Molecular Mechanisms Of Synaptic Tagging And Capture
Park, J. W. (2014) · Scholarly Commons (University of Pennsylvania) · Cited by 1
Targeting AKAP79/150 in Human Disorders: An Emerging Opportunity for Future Therapies?
Chen, F., Chu, C.-C., Wu, C., Chen, F., Xu, J., Zhou, L., Fang, W. R., Lu, X., & Hu, Y. H. (2023) · Progress in Neurobiology · doi:10.60124/j.pneuro.2023.10.06
Simmons, S. C., Flerlage, W. J., Langlois, L. D., Shepard, R. D., Bouslog, C., Thomas, E. H., Gouty, K. M., Sanderson, J. L., Gouty, S., Cox, B. M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.06.570160 · Cited by 1
Self-citationOliveira‐Giacomelli, Á. (2014)
Serpa, A. (2015) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Dynamics of Scaffold Protein Tethered Signal Transduction
Greenwald, E. C. (2015) · doi:10.18130/v39p00
Neuroproteômica de abelhas e ratos para descoberta de proteínas relacionadas à aprendizagem
de Souza, J. M. F. (2017) · RIUnB Institutional Repository (University of Brasília) · doi:10.26512/2017.03.t.24057
Kohansal-Nodehi, M. (2017) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6118
Qiao, L., Getz, M., Gross, B., Tenner, B., Zhang, J., & Rangamani, P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.29.577875
Bloom, J. C., Torres, E., Pereira, S. A., Arvizu-Sanchez, L., Fontes, A. N., Joffe, H., Page, D. C., & Navarro, V. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.05.616758
Bernard, P. B., Castano, A. M., Buonarati, O. R., Camp, C. R., Hell, J. W., & Benke, T. A. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106884
del Campo, I. S. F., Cebrián-León, A., Caño, C. H.-D., Varela-Andrés, N., Plaza, I., Deogracias, R., & Merchán, M. Á. (2026) · Hearing Research · doi:10.1016/j.heares.2026.109580
McClatchy, D. B., Lane, J. E., Powell, S. B., & Yates, J. R. (2026) · Schizophrenia · doi:10.1038/s41537-026-00734-1
Pratlong, M. (2014) · theses.fr (ABES) · doi:10.70675/02dafa47zd1cfz49e6z86a9zb57e2f9d693f
Anchored kinase and phosphatase signaling networks in amyloid β-induced synaptic dysfunction
Koek, L. A., Jo, H.-N., Kennedy, M. J., & Dell’Acqua, M. L. (2026) · Molecular Pharmacology · doi:10.1016/j.molpha.2026.100141
Self-citationBloom, J. C., Torres, E., Pereira, S. A., Arvizu-Sanchez, L., Fontes, A. N., Joffe, H., Page, D. C., & Navarro, V. M. (2026) · JCI Insight · doi:10.1172/jci.insight.207270 · Cited by 1
Metadata
- Authors
- Sanderson, J. L., & Dell'Acqua, M. L.
- Affiliations
- University of Colorado Anschutz (US)
- Department of Pharmacology, University of Colorado School of Medicine, Anschutz Medical Campus, Aurora, CO, USA, Program in Neuroscience, University of Colorado School of Medicine, Anschutz Medical Campus, Aurora, CO, USA,
- Venue
- The Neuroscientist
- Publisher
- SAGE Publications
- Published
- 2011-04-15
- Volume
- 17
- Issue
- 3
- Pages
- 321-336
- ISSN
- 1073-8584 (ISSN-L)
- 1089-4098
- PMC
- PMC3126619
- OpenAlex
- W2126128061
- Cited by
- 185
- References
- 89
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 12 · 2023: 7 · 2022: 9 · 2021: 8 · 2020: 4 · 2019: 9 · 2018: 8 · 2017: 12 · 2016: 16 · 2015: 24 · 2014: 23 · 2013: 20 · 2012: 17
- FWCI
- 1.92
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Neuroscientist (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Alcohol Abuse and Alcoholism (T32AA007464)
- National Institute of Mental Health (R01MH080291)
- National Institute of Neurological Disorders and Stroke (R01NS040701)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Keywords
- A-kinase anchoring proteins, synaptic plasticity, long-term potentiation, long-term depression, NMDA receptor, AMPA receptors, calcium/calmodulin-dependent protein kinase II, protein kinase A, protein kinase C, calcineurin, scaffold proteins, hippocampus, glutamatergic synapses
- MeSH terms
- Animals, Brain, Humans, Synaptic Transmission, Neuronal Plasticity, Signal Transduction, A Kinase Anchor Proteins
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