The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Interaction with the NMDA receptor locks CaMKII in an active conformation
Abstract
Calcium- and calmodulin-dependent protein kinase II (CaMKII) and glutamate receptors are integrally involved in forms of synaptic plasticity that may underlie learning and memory. In the simplest model for long-term potentiation, CaMKII is activated by Ca2+ influx through NMDA (N-methyl-D-aspartate) receptors and then potentiates synaptic efficacy by inducing synaptic insertion and increased single-channel conductance of AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) receptors. Here we show that regulated CaMKII interaction with two sites on the NMDA receptor subunit NR2B provides a mechanism for the glutamate-induced translocation of the kinase to the synapse in hippocampal neurons. This interaction can lead to additional forms of potentiation by: facilitated CaMKII response to synaptic Ca2+; suppression of inhibitory autophosphorylation of CaMKII; and, most notably, direct generation of sustained Ca2+/calmodulin (CaM)-independent (autonomous) kinase activity by a mechanism that is independent of the phosphorylation state. Furthermore, the interaction leads to trapping of CaM that may reduce down-regulation of NMDA receptor activity. CaMKII-NR2B interaction may be prototypical for direct activation of a kinase by its targeting protein.
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In the citing paper
“This binding directly generates Ca2+-independent autonomous CaMKII activity”
From LTP expression mediated by autonomous activity of GluN2B-bound CaMKII (2024) · cites this paper as [13]
In the citing paper
“A second mechanism proposed for generating autonomy involves binding of the GluN2B subunit of the NMDAR to the kinase surface groove in place of the autoinhibitory domain that allows for autonomous activity without autophosphorylation (78).”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“The CTD peptide may act like a wedge between the kinase and its regulatory segment, propping the enzyme in an open active conformation that persists as long as the CTD peptide is bound, even after Ca2+/CaM dissociates (FIGURE 2B6) (78).”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“Ca2+/CaM was then removed and when the CaMKII-CTD complex was assayed with substrate and ATP it was found to be autonomously active (78).”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“A similar finding was made with T286A, the phosphonull mutant, i.e., the CTD peptide induced constitutive activity without T286P.”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“A third approach takes advantage of a point mutation of CaMKII (I205K), which prevents binding to GluN2B but otherwise reported to function normally (78)”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“This translocation involves the binding of CaMKII to the NMDAR (78, 125, 144, 221–224).”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“In the binding study, no autophosphorylation is necessary; the transient CaMKII-GluN2B complex transitions into a persistent form that remains constitutively active.”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“In contrast, the CaMKII-GluN2B CTD interaction and constitutive activity appeared to transition to a stable interaction that was almost as persistent with T286A as with phosphorylated T286.”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“In both cases addition of Ca2+/CaM in the absence of ATP or with the T286A mutant was sufficient for the LLPS or complex formation.”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“The first step involves Ca2+/CaM peeling away the autoinhibitory segment from the kinase domain. This results in the phosphorylation of T286 and also the binding of CaMKII to GluN2B even without prior autophosphorylation, both of which maintain CaMKII in an active state (64, 78, 119–121, 221).”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“As long as Ca2+/CaM is present, binding and phase separation are maintained even with a phosphonull mutant of T286 (T286A) (78, 169, 323, 377) or with a kinase-dead mutant of CaMKII (169, 323, 378, 379), although the binding of CaMKII to GluN2B is modestly enhanced by T286 phosphorylation (378).”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
In the citing paper
“First, a biochemical study demonstrated that in the absence of added ATP, and with sufficient time, the binding of CaMKII to GluN2B persists after the removal of Ca2+/CaM (78).”
From Synaptic memory and CaMKII (2023) · cites this paper as [78]
Citations
Cites
Long-Term Potentiation--A Decade of Progress?
Malenka, R. C., & Nicoll, A. R. A. (1999) · Science · doi:10.1126/science.285.5435.1870 · Cited by 2,729
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
Sensitivity of CaM Kinase II to the Frequency of Ca 2+ Oscillations
De Koninck, P., & Schulman, H. (1998) · Science · doi:10.1126/science.279.5348.227 · Cited by 1,269
Self-citationDerkach, V., Barria, A., & Soderling, T. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3269 · Cited by 842
Shen, K., & Meyer, T. (1999) · Science · doi:10.1126/science.284.5411.162 · Cited by 673
Calmodulin Trapping by Calcium-Calmodulin-Dependent Protein Kinase
Meyer, T., Hanson, P. I., Stryer, L., & Schulman, H. (1992) · Science · doi:10.1126/science.256.5060.1199 · Cited by 637
Self-citationA Synaptic Ras-GTPase Activating Protein (p135 SynGAP) Inhibited by CaM Kinase II
Chen, H.-J., Rojas-Soto, M., Oguni, A., & Kennedy, M. B. (1998) · Neuron · doi:10.1016/s0896-6273(00)80471-7 · Cited by 590
Inactivation of NMDA Receptors by Direct Interaction of Calmodulin with the NR1 Subunit
Ehlers, M., Zhang, S., Bernhardt, J., & Huganir, R. L. (1996) · Cell · doi:10.1016/s0092-8674(00)81052-1 · Cited by 537
Hanson, P. I., Meyer, T., Stryer, L., & Schulman, H. (1994) · Neuron · doi:10.1016/0896-6273(94)90306-9 · Cited by 500
Self-citationRegulation of NMDA channel function by endogenous Ca2+-dependent phosphatase
Lieberman, D. N., & Mody, I. (1994) · Nature · doi:10.1038/369235a0 · Cited by 480
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The Function of CaM Kinase II in Synaptic Plasticity and Spine Formation
Fukunaga, K., Shioda, N., & Miyamoto, E. (2009) · Springer eBooks · doi:10.1007/978-0-387-30370-3_9 · Cited by 12
Lisman, J. E., & Hell, J. W. (2008) · Springer eBooks · doi:10.1007/978-0-387-77232-5_17 · Cited by 12
Self-citationDavis-Reyes, B. D., Campbell, V. M., Land, M. A., Chapman, H. L., Stafford, S. J., & Anastasio, N. C. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.07.007 · Cited by 12
Tullis, J. E., & Bayer, K. U. (2023) · iScience · doi:10.1016/j.isci.2023.106723 · Cited by 12
Self-citationOtmakhov, N., Gorbacheva, E. V., Regmi, S., Yasuda, R., Hudmon, A., & Lisman, J. E. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120881 · Cited by 12
Developmental distribution of CaM kinase II in the antennal lobe of the sphinx moth Manduca sexta
Lohr, C., Bergstein, S., & Hirnet, D. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0249-6 · Cited by 13
Delineating and Understanding Cerebellar Neuroprotective Pathways
Wu, X., Jiang, X., Marini, A. M., & Lipsky, R. H. (2005) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2005.tb00009.x · Cited by 12
Taha, S. A., & Stryker, M. P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508185102 · Cited by 12
Moody, T. D., Watabe, A. M., Indersmitten, T., Komiyama, N. H., Grant, S. G. N., & O’Dell, T. J. (2011) · Learning & Memory · doi:10.1101/lm.2045311 · Cited by 12
CaMKIIα as a Promising Drug Target for Ischemic Grey Matter
Griem‐Krey, N., Clarkson, A. N., & Wellendorph, P. (2022) · Brain Sciences · doi:10.3390/brainsci12121639 · Cited by 11
Xu, P., Cui, D., Jin, M., & Sun, L. (2024) · Journal of Neurorestoratology · doi:10.1016/j.jnrt.2024.100094 · Cited by 12
Zhuang, Z., Wu, H.-Y., Song, Y.-Y., Li, L., Cui, X., Yang, J., Xu, X.-Q., & Cui, W. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.981190 · Cited by 12
Griem‐Krey, N., Klein, A. B., Clausen, B. H., Namini, M. R., Nielsen, P. V., Bhuiyan, M. H., Nagaraja, R. Y., Silva, T. M. D., Sobey, C. G., Cheng, H., et al. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231167920 · Cited by 11
CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to induce mitotic checkpoint in glioma
Chuah, Y. H., Tay, E. X. Y., Grinchuk, O. V., Yoon, J., Feng, J., Kannan, S., Robert, M., Jakhar, R., Liang, Y., Lee, B. W. L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01192-3 · Cited by 11
NMDA receptors on zebrafish M authner cells require CaMKII‐α for normal development
Roy, B., Ferdous, J., & Ali, D. W. (2014) · Developmental Neurobiology · doi:10.1002/dneu.22214 · Cited by 11
The Roles of Calmodulin and CaMKII in Cx36 Plasticity
Zoidl, G., & Spray, D. C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094473 · Cited by 11
Zheng, N., Gui, Z., Liu, X., Wu, Y., Wang, H., Cai, A., Wu, J., Li, X., Kaewborisuth, C., Zhang, Z., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04362-6 · Cited by 10
Behroozi, Z., Askarpour, H., & Baghcheghi, Y. (2026) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823261415807 · Cited by 10
Sadat‐Shirazi, M., Ahmadian-Moghadam, H., Khalifeh, S., Zadeh‐Tehrani, S. N., Farahmandfar, M., & Zarrindast, M. (2018) · Behavioural Brain Research · doi:10.1016/j.bbr.2018.11.010 · Cited by 10
Kim, S., Sohn, S., & Choe, E. S. (2022) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyac034 · Cited by 10
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Pitcher, G. M., Kalia, L. V., Liu, X. J., Salter, M. W., & Dong, Y. (2008) · Frontiers in neuroscience · doi:10.1201/9781420044157.ch7 · Cited by 10
Nguyen, T. A., Puhl, H. L., Hines, K. G., Liput, D. J., & Vogel, S. S. (2022) · Nature Communications · doi:10.1038/s41467-022-33795-8 · Cited by 10
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Medina, I. (2007) · Science s STKE · doi:10.1126/stke.3862007pe23 · Cited by 10
Long-Term Potentiation and Memory
(2012) · Springer eBooks · doi:10.1007/springerreference_169302 · Cited by 10
Mapping fear memory consolidation and extinction-specific expression of JunB
Radwańska, K., Pereira, G. S., Ziółkowska, M., Łukasiewicz, K., & Giese, K.-P. (2015) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2015.08.007 · Cited by 10
Earl, D. E., Das, P., Gunning, W. T., & Tietz, E. I. (2012) · Neural Plasticity · doi:10.1155/2012/405926 · Cited by 9
She, K., Rose, J. K., & Craig, A. M. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.08.001 · Cited by 9
Saneyoshi, T. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.01.018 · Cited by 9
Kv4.2 block of long-term potentiation is partially dependent on synaptic NMDA receptor remodeling
Jung, S., Eun, S., Kim, J., & Hoffman, D. A. (2010) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2010.09.012 · Cited by 9
NMDA Receptors in Astroglia: Chronology, Controversies, and Contradictions from a Complex Molecule
Balderas, P. M. D. O., & GonzálezHernández, J. (2018) · InTech eBooks · doi:10.5772/intechopen.72975 · Cited by 12
Brown, C. N., Rumian, N. L., Tullis, J. E., Coultrap, S. J., & Bayer, K. U. (2022) · iScience · doi:10.1016/j.isci.2022.104368 · Cited by 9
Self-citationFujii, H., Kidokoro, H., Kondo, Y., Kawaguchi, M., Horigane, S., Natsume, J., Takemoto‐Kimura, S., & Bito, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.970031 · Cited by 8
Chen, Y., Liu, S., Jacobi, A. A., Jeng, G., Ulrich, J. D., Stein, I. S., Patriarchi, T., & Hell, J. W. (2024) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2024.1291262 · Cited by 9
Self-citationBartol, T. M., Ordyan, M., B, T. J. S. A., Rangamani, P., & Kennedy, M. B. (2025) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2025.1547948 · Cited by 8
Ahern, B. M., Sebastian, A. H., Levitan, B. M., Goh, J. Z., Andres, D., & Satin, J. (2021) · The Journal of General Physiology · doi:10.1085/jgp.202012854 · Cited by 8
Reeves, S. R., Carter, E. S., Guo, S. Z., & Gozal, D. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00249.2005 · Cited by 8
Zhao, M., Zeng, L., Zhou, Y., Yang, C. H., Sheng, R., Liu, X., Wen, W., Yang, S., Zhang, S., & Xu, S. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c12077 · Cited by 7
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Zhu, S., Shen, Z., Wu, X., & Zhang, M. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2025.102975 · Cited by 7
Hoffman, L., Li, L., Alexov, E., Sanabria, H., & Waxham, M. N. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00028 · Cited by 7
Alla, J. A., Langer, A., Wolf, S., Fu, X., Rageh, M. A., & Quitterer, U. (2023) · Nature Cardiovascular Research · doi:10.1038/s44161-023-00351-6 · Cited by 7
Heidarinejad, M., Nakamura, H., & Inoue, T. (2018) · Neuroscience Research · doi:10.1016/j.neures.2018.01.003 · Cited by 7
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Pandini, A., Schulman, H., & Khan, S. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006796 · Cited by 7
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Fernández‐Espejo, E. (2006) · Revista de Neurología · doi:10.33588/rn.4303.2005644 · Cited by 7
Yamagata, Y., & Obata, K. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02753.x · Cited by 7
Georgiev, D. D., Taniura, H., Kambe, Y., & Yoneda, Y. (2008) · Biomedical Reviews · doi:10.14748/bmr.v19.57 · Cited by 7
Expression and phosphorylation of δ-CaM kinase II in cultured Alzheimer fibroblasts
Cavazzin, C., Bonvicini, C., Nocera, A., Racchi, M., Kasahara, J., Tardito, D., Gennarelli, M., Govoni, S. M., Racagni, G., & Popoli, M. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.12.003 · Cited by 7
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Deurloo, M., Eide, S., Turlova, E., Li, Q., Spijker, S., Sun, H., Groffen, A. J. A., & Feng, Z. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01193-w · Cited by 7
Activation is only the beginning: mechanisms that tune kinase substrate specificity
Clark, L. K., & Cullati, S. N. (2025) · Biochemical Society Transactions · doi:10.1042/bst20241420 · Cited by 7
CaMKII mechanisms that promote pathological LTP impairments
Larsen, M. E., Rumian, N. L., Quillinan, N., & Bayer, K. U. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2024.102961 · Cited by 6
Self-citationFiumelli, H., Herrera‐López, G., Lemtiri‐Chlieh, F., Mottier, L., Girgis, J., Benadiba, C., Jourdain, P., Carrano, N., Mahmood, H., Ooi, A., et al. (2026) · The Journal of Physiology · doi:10.1113/jp288960 · Cited by 7
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Stein, I. S., & Hell, J. W. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.105 · Cited by 6
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Bussey, C. T., & Erickson, J. (2017) · Current Opinion in Physiology · doi:10.1016/j.cophys.2017.07.003 · Cited by 6
Castro-Rodrigues, A. F., Zhao, Y., Fonseca, F., Gabant, G., Cadène, M., Robertson, G. A., & Morais-Cabral, J. H. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.10.015 · Cited by 6
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Kennedy, M. B. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00075-9 · Cited by 6
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Kantamneni, S. (2016) · Springer eBooks · doi:10.1007/978-3-319-46044-4_7 · Cited by 6
Interaction of peptide substrate outside the active site influences catalysis by CaMKII
Praseeda, M., Mayadevi, M., & Omkumar, R. V. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.019 · Cited by 6
Petralia, R. S., & Wenthold, R. J. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-055-3_2 · Cited by 7
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Tang, L., Liu, F., Sun, X., Yang, J., Liu, Y., Pan, X., Hao, L., Lou, F., & Su, J. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04160-7 · Cited by 5
Ahmadi, S., Amiri, S., Rafieenia, F., & Rostamzadeh, J. (2013) · Europe PMC (PubMed Central) · Cited by 5
Mehrotra, S., Pierce, M. L., Dravid, S. M., & Murray, T. F. (2022) · Marine Drugs · doi:10.3390/md20090559 · Cited by 5
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Berchtold, M. W., & Villalobo, A. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167583 · Cited by 7
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Villaamil, V. M., Gallego, G. A., Caínzos, I. S., Valladares‐Ayerbes, M., & Aparicio, L. M. A. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13066561 · Cited by 5
Nisanov, R., Schelbaum, E., Morris, D., & Ranaldi, R. (2020) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2020.107299 · Cited by 5
Fujii, H., & Bito, H. (2022) · Neuroscience Research · doi:10.1016/j.neures.2022.04.004 · Cited by 6
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Stratton, M. M. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2216529119 · Cited by 5
Cheriyan, J., Mohanan, A. G., Kurup, P. K., Mayadevi, M., & Omkumar, R. V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045064 · Cited by 5
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Pelkey, K. A., & McBain, C. J. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-055-3_5 · Cited by 5
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Takahashi, E., Niimi, K., & Itakura, C. (2009) · Journal of Molecular Neuroscience · doi:10.1007/s12031-009-9216-5 · Cited by 5
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Chen, X. D., Xiao, J., Fu, H., Zhang, Y., Li, Y., Yang, H., Gao, W., & Li, B. (2022) · Toxicology in Vitro · doi:10.1016/j.tiv.2022.105455 · Cited by 4
Induction of LTP mechanisms in dually innervated dendritic spines
Tullis, J. E., & Bayer, K. U. (2024) · Scientific Reports · doi:10.1038/s41598-024-66871-8 · Cited by 4
Self-citationYuan, X., Li, W., Yuan, Y., Zhu, X., Meng, Y., Wu, Q., Qi, Y., & Zhang, P. (2024) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2024.110296 · Cited by 5
The Role of the Postsynaptic Density and the Spine Cytoskeleton in Synaptic Plasticity
Marcora, E. M., Carlisle, H. J., & Kennedy, M. B. (2008) · Elsevier eBooks · doi:10.1016/b978-012370509-9.00036-x · Cited by 4
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Maduka, U. P., White, S. R., Joiner, M.-L. A., Hell, J. W., & Hammond, D. L. (2020) · Brain Research · doi:10.1016/j.brainres.2020.147154 · Cited by 4
Self-citationMayadevi, M., Kesavan, L., Priya, S. D. S., John, S., & Omkumar, R. V. (2016) · PLoS ONE · doi:10.1371/journal.pone.0162011 · Cited by 4
Subunit-Specific NMDA Receptor Trafficking to Synapses
Barría, A. (2007) · Elsevier eBooks · doi:10.1016/b978-012369437-9/50015-3 · Cited by 4
Cellular Functions of Calcium Channel Subtypes
Piedras-Renterı́a, E. S., Mermelstein, P. G., & Pitt, G. S. (2004) · Springer eBooks · doi:10.1007/978-1-4419-9254-3_7 · Cited by 4
Granulocyte-macrophage colony-stimulating factor
Structure, C., Heit, B., Jones, G., Knight, D., Joseph, M., Gill, M. J., Brown, C., Kubes, P., Brown, C., Power, C., et al. (1989) · Reactions Weekly · doi:10.1007/bf03284025 · Cited by 4
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Chen, S., Cai, Q., Peng, H., Yang, Y., Wu, Z., & Zhang, M. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116723 · Cited by 3
Liu, X., Wang, Y., Yang, P., Yang, C., Chen, S. F., Wen, C., Wong, L. E., & Chang, S. (2026) · Nature Communications · doi:10.1038/s41467-026-72234-w · Cited by 3
Kulasiri, D., Liang, J., He, Y., & Samarasinghe, S. (2017) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2017.02.003 · Cited by 3
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de Andrés, R., Martínez‐Blanco, E., & Díez-Guerra, F. J. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04598-3 · Cited by 3
Schulman, H. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397179-1.00004-x · Cited by 3
Self-citationVézina-Audette, R., Tremblay, M. R., & Carbonetto, S. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.11.006 · Cited by 3
Kang, J., Wei, X., Liu, J., Wong‐Riley, M. T. T., Ju, G., & Liu, Y. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12297 · Cited by 3
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Strack, S., & Hell, J. W. (2008) · Springer eBooks · doi:10.1007/978-0-387-77232-5_16 · Cited by 3
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Self-citation
Metadata
- Authors
- Bayer, K.-U., De Koninck, P., Leonard, A. S., Hell, J. W., & Schulman, H.
- Affiliations
- Stanford Medicine (US)
- University of Iowa (US)
- Corresponding author
- Bayer, K.-Ulrich
- Venue
- Nature
- Published
- 2001-06
- Volume
- 411
- Issue
- 6839
- Pages
- 801-805
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2007393704
- Cited by
- 732
- References
- 30
- Citations by year
- 2026: 12 · 2025: 23 · 2024: 28 · 2023: 23 · 2022: 28 · 2021: 28 · 2020: 30 · 2019: 21 · 2018: 26 · 2017: 27 · 2016: 18 · 2015: 23 · 2014: 42 · 2013: 25 · 2012: 37
- FWCI
- 12.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- 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
- CaMKII, NMDA receptor, NR2B subunit, kinase activation, synaptic plasticity, long-term potentiation, autophosphorylation, hippocampal neurons, glutamate signaling
- MeSH terms
- Animals, Calcium, Calmodulin, Cell Line, Enzyme Activation, Hippocampus, Neurons, Phosphorylation, Protein Binding, Protein Conformation, Recombinant Fusion Proteins, Receptors, N-Methyl-D-Aspartate, Calcium-Calmodulin-Dependent Protein Kinases, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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