The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Rapid Dispersion of SynGAP from Synaptic Spines Triggers AMPA Receptor Insertion and Spine Enlargement during LTP
Open accessAbstract
SynGAP is a Ras-GTPase activating protein highly enriched at excitatory synapses in the brain. Previous studies have shown that CaMKII and the RAS-ERK pathway are critical for several forms of synaptic plasticity including LTP. NMDA receptor-dependent calcium influx has been shown to regulate the RAS-ERK pathway and downstream events that result in AMPA receptor synaptic accumulation, spine enlargement, and synaptic strengthening during LTP. However, the cellular mechanisms whereby calcium influx and CaMKII control Ras activity remain elusive. Using live-imaging techniques, we have found that SynGAP is rapidly dispersed from spines upon LTP induction in hippocampal neurons, and this dispersion depends on phosphorylation of SynGAP by CaMKII. Moreover, the degree of acute dispersion predicts the maintenance of spine enlargement. Thus, the synaptic dispersion of SynGAP by CaMKII phosphorylation during LTP represents a key signaling component that transduces CaMKII activity to small G protein-mediated spine enlargement, AMPA receptor synaptic incorporation, and synaptic potentiation.
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
“To test this, we induced long-term potentiation via APV withdrawal and glycine stimulation19 which resulted in an increase in PSD-95 localization density within NCs, the percentage of PSD-95 NCs enriched with RIM1/2, and the enrichment index of PSD-95 NCs (Fig. 4a–c, Extended Data Fig. 10m).”
From A trans-synaptic nanocolumn aligns neurotransmitter release to receptors (2016) · cites this paper as [19]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“we induced long-term potentiation via APV withdrawal and glycine stimulation19”
From A trans-synaptic nanocolumn aligns neurotransmitter release to receptors (2016) · cites this paper as [19]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Several mechanisms should be considered, including indirect effects on synaptic features such as activity, which regulates the targeting of SYNGAP1 through its phosphorylation by Ca2+/calmodulin-dependent protein kinase II (CAMK2).54”
From Synaptic neoteny of human cortical neurons requires species-specific balancing of SRGAP2-SYNGAP1 cross-inhibition (2024) · cites this paper as [54]
The cited source says what the claim attributes to it.
In the citing paper
“Imaging studies have reported that this phosphorylation triggers movement of SynGAP out of the PSD (304, 305)”
From Synaptic memory and CaMKII (2023) · cites this paper as [304]
The cited source says what the claim attributes to it.
In the citing paper
“Furthermore, knockdown of SynGAP results in the accumulation of synaptic AMPARs, which occludes chemLTP (304).”
From Synaptic memory and CaMKII (2023) · cites this paper as [304]
The cited source says what the claim attributes to it.
In the citing paper
“and this dispersal is required for chemLTP (304).”
From Synaptic memory and CaMKII (2023) · cites this paper as [304]
The cited source says what the claim attributes to it.
In the citing paper
“CaMKII phosphorylates SynGAP and decreases its binding to PSD-95 (302, 304).”
From Synaptic memory and CaMKII (2023) · cites this paper as [304]
In the citing paper
“Synaptic GTPase activating protein 1 (SynGAP1) is a Ras-GTPase activating protein localized in the PSD in glutamatergic neurons [66, 197] and involved in dendritic spine maturation, glutamate receptor trafficking and synaptic function [11].”
From Autism spectrum disorder: neuropathology and animal models (2017) · cites this paper as [11]
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
Structural basis of long-term potentiation in single dendritic spines
Matsuzaki, M., Honkura, N., Ellis-Davies, G. C. R., & Kasai, H. (2004) · Nature · doi:10.1038/nature02617 · Cited by 2,483
GEFs and GAPs: Critical Elements in the Control of Small G Proteins
Bos, J. L., Rehmann, H., & Wittinghofer, A. (2007) · Cell · doi:10.1016/j.cell.2007.05.018 · Cited by 1,903
Matsuzaki, M., Ellis-Davies, G. C. R., Nemoto, T., Miyashita, Y., Iino, M., & Kasai, H. (2001) · Nature Neuroscience · doi:10.1038/nn736 · Cited by 1,563
MAPK cascade signalling and synaptic plasticity
Thomas, G. M., & Huganir, R. L. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1346 · Cited by 1,454
Self-citationMechanisms of CaMKII action in long-term potentiation
Lisman, J., Yasuda, R., & Raghavachari, S. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3192 · Cited by 1,134
Synaptic AMPA receptor plasticity and behavior
Kessels, H. W., & Malinow, R. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.015 · Cited by 993
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
Self-citationAMPARs and Synaptic Plasticity: The Last 25 Years
Huganir, R. L., & Nicoll, R. A. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.025 · Cited by 968
Self-citationLu, W.-Y., Man, H., Ju, W. H., Trimble, W. S., MacDonald, J. F., & Wang, Y. T. (2001) · Neuron · doi:10.1016/s0896-6273(01)00194-5 · Cited by 935
Ras and Rap control AMPA receptor trafficking during synaptic plasticity
Zhu, J. J., Qin, Y., Zhao, M., Van Aelst, L., & Malinow, R. (2002) · Cell · doi:10.1016/s0092-8674(02)00897-8 · Cited by 769
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–270 of 270
Stamenković, V., Harsh, F. M., Kniffen, B., Rumbaugh, G., & Smith, S. E. P. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101614 · Cited by 3
Li, Z., Han, Y., Meng-Yao, W., Jian, L., Shi, J., Xi, Z., & Yuhong, W. (2020) · Digital Chinese Medicine · doi:10.1016/j.dcmed.2020.06.003 · Cited by 3
P-Rex2 mediation of synaptic plasticity contributes to bone cancer pain
Fu, Q., Huang, X., Wan, S., Li, Y., Li, X., Su, S., Xu, X., & Wu, Y. (2022) · Molecular Pain · doi:10.1177/17448069221076460 · Cited by 3
Mapping proteomic composition of excitatory postsynaptic sites in the cerebellar cortex
Robinson, K., Delhaye, M., & Craig, A. M. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1381534 · Cited by 3
MicroRNA‐138‐5p suppresses excitatory synaptic strength at the cerebellar input layer
Delvendahl, I., Daswani, R., Winterer, J., Germain, P., Uhr, N. M., Schratt, G., & Müller, M. (2025) · The Journal of Physiology · doi:10.1113/jp288019 · Cited by 3
Neuronal Stress and Its Hormetic Aspects
Hofbrucker-MacKenzie, S. A., Sivaprakasam, I., Ji, Y., Kessels, M. M., & Qualmann, B. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-814253-0.00015-2 · Cited by 4
Liquid Phase Transition in the Postsynaptic Density?
Kennedy, M. B., & Mastro, T. L. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.11.005 · Cited by 3
Piconewton‐Scale Analysis of Ras‐BRaf Signal Transduction with Single‐Molecule Force Spectroscopy
Lim, C., Wen, C., Sheng, Y., Wang, G., Zhou, Z., Wang, S., Zhang, H., Ye, A., & Zhu, J. (2017) · Small · doi:10.1002/smll.201701972 · Cited by 3
SYNGAP1 deficiency disrupts neoteny in human cortical neurons in vivoPreprint
Vermaercke, B., Iwata, R., Weirda, K., Boubakar, L., Rodríguez, P., Ditkowska, M., Bonin, V., & Vanderhaeghen, P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.14.524054 · Cited by 3
Mayer, A., Derua, R., Spahn, E., Verbinnen, I., Zhang, Y., Wadzinski, B. E., Swingle, M. R., Honkanen, R. E., Janssens, V., & Xia, H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.18.599485 · Cited by 3
Sichlinger, L., Reilly, M. B., Arora, S., Zhang, S., Marotta, N., Rodríguez-Acevedo, K. L., Hooks, M., Czarnecki, K. S., Winter, J. J., Waxman, E. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.28.685100 · Cited by 3
Self-citationAryal, S., Geng, C., Yin, M. A., Kwon, M. J., Farsi, Z., Goble, N., Asan, A. S., Brenner, K. S., Shepard, N., Geller, A., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117436 · Cited by 7
Wang, X., Tian, Y.-N., Chen, C., & Peng, J. (2023) · PubMed Central · doi:10.7499/j.issn.1008-8830.2301054 · Cited by 2
Shifting rules in a brain disorder
Choquet, D. (2024) · Science · doi:10.1126/science.adn8707 · Cited by 2
Synaptic Physiology Depends on Electrical Forces and Liquid–Liquid Phase Separation
McCaig, C. (2025) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/978-3-031-68827-0_17 · Cited by 2
Syngap +/− CA1 Pyramidal Neurons Exhibit Upregulated Translation of Long MRNAs Associated with LTP
Singh, A., Rizzi, M., Seo, S. S., & Osterweil, E. K. (2025) · eNeuro · doi:10.1523/eneuro.0086-25.2025 · Cited by 2
CaMKII: A Master Functional and Structural Molecule in Synaptic Plasticity and Memory
Sanhueza, M., & Fernandez, G. (2015) · Springer eBooks · doi:10.1007/978-3-319-24364-1_3 · Cited by 2
Dynamin forms liquid-like condensates at synapses to support ultrafast endocytosisPreprint
Imoto, Y., Ma, Y., Itoh, K., Blumrich, E., Matsubayashi, H. T., Liu, J., Wu, B., Cousin, M. A., Ha, T., Inoue, T., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.01.494432 · Cited by 1
Gao, Y., Trn, M., Shonai, D., Zhao, J., Soderblom, E. J., Garcia-Moreno, S. A., Gersbach, C. A., Wetsel, W. C., Dawson, G., Velmeshev, D., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.06.511211 · Cited by 2
Bartol, T. M., Ordyan, M., B, T. J. S. A., Rangamani, P., & Kennedy, M. B. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.02.578696 · Cited by 2
Jiang, J. P., Rust, R., Flores, I., Feng, Y., Nouri, P., Clementel, V. A., Arya, A., Basirattalab, A., Yang, I. Y., Manousopoulou, A., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.24.707848 · Cited by 3
Modeling phase separation dynamics of SynGAP and PSD-95 in postsynaptic densitiesPreprint
Sakly, S., & Smith, G. D. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.23.740312 · Cited by 1
AMPA receptors in synaptic plasticity and learning and memory
Kim, K., & Park, M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00056-0 · Cited by 1
IQSEC2/BRAG1 may modulate postsynaptic density assembly through Ca2+-induced phase separation
Bai, G., Huang, R., Nan, X., Zhuang, M., Wu, M., Lian, Y., Cai, Q., Tian, H.-L., Lu, Y., Li, H., et al. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202503076 · Cited by 1
Self-citationVisualizing Postsynaptic Density in Excitatory Synapses with Electron Tomography
Sun, R., & Zhou, Q. (2026) · Advances in neurobiology · doi:10.1007/978-3-032-12594-1_10 · Cited by 2
CDKL5 modulates the plasticity of excitatory synapses via liquid–liquid phase separation
Li, M., Zhu, Z., Li, D., Wang, J., Zhang, M., Xu, Q.-W., Zhang, Y., Zhu, Y., Zhu, J., & Xiong, Z. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2511123123 · Cited by 2
Self-citationLim, S., Shin, S., Lee, N.-Y., Min, S. S., Kim, N.-S., Lee, D. Y., & Lee, J.-R. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.06.071 · Cited by 1
Bernardo, D. (2024) · Springer eBooks · doi:10.1007/978-3-031-62945-7_29 · Cited by 1
Neuronal ARHGAP8 controls synapse structure and AMPA receptor-mediated synaptic transmission
Schmidt, J., Inácio, Â. S., Ferreira, J. S., Serrenho, D., Socodato, R., Beltrão, N., Ribeiro, L. F., Pinheiro, P. S., Relvas, J. B., & Carvalho, A. L. (2026) · Communications Biology · doi:10.1038/s42003-026-09884-5 · Cited by 1
How CBP/Shank3 Guards Rap and H-Ras
Chowdhury, D., & Hell, J. W. (2020) · Structure · doi:10.1016/j.str.2020.02.003 · Cited by 1
Demystifying neuroscience laboratory techniques used to investigate single-gene disorders
Mizen, L. A. M., & Stanfield, A. C. (2020) · BJPsych Advances · doi:10.1192/bja.2020.30 · Cited by 1
Groß, C. (2022) · Epiliepsy currents/Epilepsy currents · doi:10.1177/15357597221111686 · Cited by 1
Hyperexcitability and translational phenotypes in a preclinical model of SYNGAP1 mutationsPreprint
Silverman, J. L., Fenton, T., Haouchine, O. Y., Hallam, E., Smith, E., Jackson, K. C., Rahbarian, D., Canales, C. P., Adhikari, A., Nord, A. S., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-3246655/v1 · Cited by 1
Singh, A. K., Joshi, I., Reddy, N. M. N., Purushotham, S. S., Eswaramoorthy, M., Vasudevan, M., Banerjee, S., Clement, J. P., & Kundu, T. K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.03.574003 · Cited by 1
Francavilla, R., Chattopadhyaya, B., Kamda, J. L. D., Jadhav, V., Kourrich, S., Michaud, J. L., & Cristo, G. D. (2024) · eLife · doi:10.7554/elife.97100.2 · Cited by 1
Walkup, W. G., Mastro, T. L., Schenker, L. T., Vielmetter, J., Hu, R., Iancu, A., Reghunathan, M., Bannon, B. D., & Mary, B. K. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/058016
Roles of CaMKII in Learning and Memory ☆
Stephenson, J. R., & Colbran, R. J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809324-5.21106-1
BDNF-Induced Intracellular Signaling
Gomes, J. R., Lobo, A. C., Duarte, C. B., & Grãos, M. (2017) · Neuromethods · doi:10.1007/7657_2017_6
Mizen, L. A. M. (2018) · ERA
Translational regulation of Syngap1 by FMRP modulates NMDAR mediated signallingPreprint
Paul, A., Nawalpuri, B., Sateesh, S., Muddashetty, R. S., & Clement, J. P. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/345058
Kılınç, M., Creson, T. K., Rojas, C., Maity, S., Le, A. A., Lauterborn, J. C., Wilkinson, B., Hartel, N. G., Graham, N. A., Reich, A. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.18.911487
Self-citationINVESTIGATING THE ROLE OF VASCULAR ACTIVATION IN ALZHEIMER’S DISEASE-RELATED NEUROINFLAMMATION
Iannucci, J. (2020) · Digital Commons - URI (University of Rhode Island) · doi:10.23860/iannucci-jaclyn-2020
Exciting inhibition: Local regulation of synapse formation and plasticity
Kruijssen, D. L. H. (2020) · Utrecht University Repository (Utrecht University) · doi:10.33540/296
PD-1 in hippocampal neurons regulates excitability, synaptic plasticity, and cognitionPreprint
Zhao, J., Bang, S., McGinnis, A., Furutani, K., Jiang, C.-Y., Roberts, A., Donnelly, C., He, Q., Ko, M.-C., Wang, H.-C., et al. (2021) · bioRxiv · doi:10.1101/2021.07.13.451894
Sala, C. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734207936.793553923
Zhao, M., & Kwon, S. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.27.509690
Li, Z. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0099-23.2023
CaMKII mechanisms in plasticity, learning and memory: Approaches and concepts
Bayer, K. U., Brown, C. N., & Giese, K.-P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00057-2
Novel Approaches for Treating Pediatric Psychiatric Disorders
Sabetfakhri, N. P., & Cook, E. H. (2025) · Oxford University Press eBooks · doi:10.1093/med/9780197640654.003.0068
CDKL5 modulates structural plasticity of excitatory synapses via liquid-liquid phase separationPreprint
Li, M., Zhu, Z., Li, D., Wang, J., Zhang, M., Zhu, Y., Zhu, J., & Xiong, Z. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.16.643581
Self-citationAcharya, S., Tsunoyama, T. A., Hoffmann, C., Aguilar, P. G., Meshcheryakova, I., Nakamura-Norimoto, A., Mastro, T. L., Walkup, W. G., Fujiwara, T. K., Kennedy, M. B., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.22.649955
Francavilla, R., Chattopadhyaya, B., Kamda, J. L. D., Jadhav, V., Kourrich, S., Michaud, J. L., & Cristo, G. D. (2025) · eLife · doi:10.7554/elife.97100.3
Single-cell long-read sequencing of the experience-induced transcriptomePreprint
Cavalier, S., Hook, P. W., Huganir, R. L., & Timp, W. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.12.674885
Self-citationEpigenetic regulation of SYNGAP1 in alcohol use disorder in whole blood and saliva
Edelmann, S., Kummer, C., Pasche, S., Zimmermann, M., & Nieratschker, V. (2025) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2025.1661760
Pentosidine modification of neuronal proteins induces dendritic spine enlargement in vitro
Ozawa, A., Toriumi, K., Shimada, T., Endo, A., Tomita, T., Munesue, S., Tomita, Y., Takagi, H., Parida, I. S., Miyashita, M., et al. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.153032
Samowitz, P. N., Radnai, L., Vaissière, T., Michaelson, S. D., Rojas, C. J., Mitchell, R., Kılınç, M., Edwards, A. W., Shumate, J., Hawkins, R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65971-x
Deurloo, M. H. S., Eide, S., Turlova, E., Li, Q., Spijker, S., Sun, H.-S., Groffen, A. J. A., & Feng, Z.-P. (2024) · Figshare · doi:10.6084/m9.figshare.26670456
Deurloo, M. H. S., Eide, S., Turlova, E., Li, Q., Spijker, S., Sun, H.-S., Groffen, A. J. A., & Feng, Z.-P. (2024) · Figshare · doi:10.6084/m9.figshare.26670453
Pathophysiology of the FMRP-R138Q Fragile X Syndrome missense mutation in mice
Chato-Astrain, I. (2025) · theses.fr (ABES) · doi:10.70675/ce8d1ccfz4554z4c55z8782z624e392f72a1
Hiền, B. T. T., Trung, D. M., Điềm, P. T., Nguyet, B. T. M., Quyên, V. T., & Nguyen, N. V. (2026) · Foods and raw materials · doi:10.21603/2308-4057-2027-1-704
Local translational repression and retention of SynGAP1 during synaptic plasticityPreprint
Livingstone, R. W., & Donlin-Asp, P. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.29.719691
Calcium-dependent synaptic proteomics reveals EGFR signaling at active synapsesPreprint
Yong, A. J. H., Jan, Y. N., Osés-Prieto, J. A., Cheng, T., Chen, C., Domke, L., Zubia, M. V., Koroknay, A., Simms, J. A., Burlingame, A. L., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.20.726457
Ginzburg, S., Khaliulin, I., Kartawy, M., Hamoudi, W., & Amal, H. (2026) · Scientific Reports · doi:10.1038/s41598-026-57345-0
The Synaptic Clock: SynGAP1 as a Molecular Timer of Postsynaptic Density Consolidation
Cao, Z., Jia, Y., Zhang, Z., Xue, H., Yu, H. D., Li, X., & Luo, P. (2026) · Biomolecules · doi:10.3390/biom16060876
Btbd11 regulates glutamatergic synapse organization in GABAergic inhibitory interneuronsPreprint
Brady, M., Zhang, S., Levy, A. D., Schamber, P., Hartman, H., Blanpied, T. A., & Bygrave, A. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.22.733761
Félix, A. J., Brown, B. L., Marotta, N., Gessner, M. J., Houserova, M., Huerta-Ocampo, I., Wilson, T., Randell, R., Dawicki-McKenna, J. M., Reinhardt, D., et al. (2026) · Molecular Psychiatry · doi:10.1038/s41380-026-03698-x · Cited by 6
Ali, A. E., Liljeblad, A., Lehtonen, J. V., Komiyama, N. H., & Postila, P. A. (2026) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2026.100162
Autism: epidemiology, genetics, molecular mechanisms, clinical features, diagnosis, and management
Fan, R., Wang, Y., & Miao, T. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00613-2
Metadata
- Authors
- Araki, Y., Zeng, M., Zhang, M., & Huganir, R. L.
- Affiliations
- Howard Hughes Medical Institute (US)
- Hong Kong University of Science and Technology (HK)
- Corresponding author
- Huganir, Richard L.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2015-01
- Volume
- 85
- Issue
- 1
- Pages
- 173-189
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4428669
- OpenAlex
- W1993505652
- Cited by
- 271
- References
- 57
- Citations by year
- 2026: 18 · 2025: 31 · 2024: 36 · 2023: 22 · 2022: 23 · 2021: 15 · 2020: 31 · 2019: 20 · 2018: 29 · 2017: 19 · 2016: 18 · 2015: 9
- FWCI
- 11.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of Mental Health (MH64856, R01MH064856)
- National Institute of Neurological Disorders and Stroke (R01NS036715, NS036715, R37NS036715)
- 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 › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- SynGAP, CaMKII, long-term potentiation, Ras/ERK pathway, synaptic plasticity, hippocampal neurons, small GTPases, synaptic potentiation
- MeSH terms
- Animals, Calcium, Hippocampus, Neuronal Plasticity, Neurons, Phosphorylation, Signal Transduction, Receptors, N-Methyl-D-Aspartate, Long-Term Potentiation, Receptors, AMPA, ras Proteins, GTPase-Activating Proteins, MAP Kinase Signaling System, Long-Term Synaptic Depression, Dendritic Spines, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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
