De Novo Mutations in Protein Kinase Genes CAMK2A and CAMK2B Cause Intellectual Disability
Open accessAbstract
Calcium/calmodulin-dependent protein kinase II (CAMK2) is one of the first proteins shown to be essential for normal learning and synaptic plasticity in mice, but its requirement for human brain development has not yet been established. Through a multi-center collaborative study based on a whole-exome sequencing approach, we identified 19 exceedingly rare de novo CAMK2A or CAMK2B variants in 24 unrelated individuals with intellectual disability. Variants were assessed for their effect on CAMK2 function and on neuronal migration. For both CAMK2A and CAMK2B, we identified mutations that decreased or increased CAMK2 auto-phosphorylation at Thr286/Thr287. We further found that all mutations affecting auto-phosphorylation also affected neuronal migration, highlighting the importance of tightly regulated CAMK2 auto-phosphorylation in neuronal function and neurodevelopment. Our data establish the importance of CAMK2A and CAMK2B and their auto-phosphorylation in human brain function and expand the phenotypic spectrum of the disorders caused by variants in key players of the glutamatergic signaling pathway.
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Several dozen human mutations in CaMKII have been identified, and their molecular characteristics support many of the biochemical behaviors of CaMKII described above.
“Several dozen human mutations in CaMKII have been identified, and their molecular characteristics support many of the biochemical behaviors of CaMKII described above.”
From Synaptic memory and CaMKII (2023) · cites this paper as [429]
The Distribution of the Variants section reports 19 distinct CAMK2A or CAMK2B variants in 24 people, not several dozen distinct mutations. The Mutations in CAMK2 section reports that variants alter autophosphorylation, supporting the point that their molecular characteristics bear on CaMKII biochemical behavior. The cited paper therefore supports the substance of the biochemical point but not the stated count. (LLM, conf=0.88)
Experimental — accuracy not yet measuredMany CaMKII mutations decrease interactions between the kinase surface and the autoinhibitory segment previously shown to increase basal activity that is normally quite low.
“Many of the mutations decrease interactions between the kinase surface and the autoinhibitory segment previously shown to increase basal activity that is normally quite low.”
From Synaptic memory and CaMKII (2023) · cites this paper as [429]
The Discussion (page unavailable) identifies several CAMK2A variants as gain-of-function mutations, and the neuronal-function section reports increased activity for three CAMK2B variants. But our copy does not say that many mutations decrease interactions between the kinase surface and autoinhibitory segment, or establish the claimed normally low basal activity. Its mutation results also include reduced activity. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThese mutations increase autophosphorylation of T286 (or T287 in some isoforms) that further increases constitutive activity.
“These in turn increase autophosphorylation of T286 (or T287 in some isoforms) that further increases constitutive activity (429, 430).”
From Synaptic memory and CaMKII (2023) · cites this paper as [429]
The “Mutations in CAMK2” section reports increased Thr286 autophosphorylation for two CAMK2A variants, and the Discussion says Thr286 autophosphorylation makes CAMK2A autonomously active (page numbers unavailable). But the paper describes heterogeneous effects: other variants reduce phosphorylation, and the constitutively active Thr286Pro variant cannot be phosphorylated at Thr286. The claim therefore overgeneralizes the mechanism to these mutations as a group. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe human CaMKII mutations were found by exome sequencing of infants with mild to severe developmental and intellectual disabilities.
“The mutations were found by exome sequencing of infants with mild to severe developmental and intellectual disabilities.”
From Synaptic memory and CaMKII (2023) · cites this paper as [429]
The Whole-Exome Sequencing Strategy section describes exome sequencing of affected individuals, and the phenotypic characterization in Distribution of the Variants in CAMK2A and CAMK2B reports mild to severe intellectual disability in all 24. The paper does not describe the group as infants: its clinical observations include children assessed after age five. The sections returned by our copy have no page numbers. (LLM, conf=0.87)
Experimental — accuracy not yet measuredNone of the human CaMKII mutations blocks generation of constitutive activity comparable to the experimental Thr286A mutation that would enable a test of Thr286 phosphorylation and constitutive CaMKII activity in human memory.
“However, none blocks generation of constitutive activity, comparable to the experimental Thr286A mutation, that would enable a test of Thr286 phosphorylation and constitutive CaMKII activity in human memory (428–430).”
From Synaptic memory and CaMKII (2023) · cites this paper as [429]
The Discussion reports that the human CAMK2A Thr286Pro variant blocks Thr286 autophosphorylation yet renders the protein constitutively active; the neuronal-function section contrasts it with the experimental phospho-dead Thr286Ala mutant. This supports the distinction between those two mutations, but the paper does not establish that no human CaMKII mutation blocks constitutive activity or assess whether a mutation could test its role in human memory. (LLM, conf=0.84)
Experimental — accuracy not yet measured
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Cites
I-TASSER server for protein 3D structure prediction
Zhang, Y. (2008) · BMC Bioinformatics · doi:10.1186/1471-2105-9-40 · Cited by 5,124 · see citing works
Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968 · see citing works
Glutamate Receptor Ion Channels: Structure, Regulation, and Function
Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., Hansen, K. B., Yuan, H., Myers, S. J., & Dingledine, R. (2010) · Pharmacological Reviews · doi:10.1124/pr.109.002451 · Cited by 3,568 · see citing works
The contribution of de novo coding mutations to autism spectrum disorder
Iossifov, I., O’Roak, B. J., Sanders, S. J., Ronemus, M., Krumm, N., Levy, D., Stessman, H. A., Witherspoon, K. T., Vives, L., Patterson, K. E., et al. (2014) · Nature · doi:10.1038/nature13908 · Cited by 2,585 · see citing works
Self-citationNMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease
Paoletti, P., Bellone, C., & Zhou, Q. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3504 · Cited by 2,523 · see citing works
DECIPHER: Database of Chromosomal Imbalance and Phenotype in Humans Using Ensembl Resources
Firth, H. V., Richards, S. M., Bevan, A. P., Clayton, S., Corpas, M., Rajan, D., Vooren, S. V., Moreau, Y., Pettett, R. M., & Carter, N. P. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.03.010 · Cited by 1,990 · see citing works
Clinical Whole-Exome Sequencing for the Diagnosis of Mendelian Disorders
Yang, Y.-P., Muzny, D., Reid, J., Bainbridge, M., Willis, A., Ward, P., Braxton, A. A., Beuten, J., Xia, F., Niu, Z., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1306555 · Cited by 1,926 · see citing works
Self-citationThe molecular basis of CaMKII function in synaptic and behavioural memory
Lisman, J., Schulman, H., & Cline, H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn753 · Cited by 1,860 · see citing works
Control of memory formation through regulated expression of a CaMKII transgene
Mayford, M., Bach, M. E., Huang, Y.-Y., Wang, L., Hawkins, R. D., & Kandel, E. R. (1996) · Science · doi:10.1126/science.274.5293.1678 · Cited by 1,550 · see citing works
Diagnostic exome sequencing in persons with severe intellectual disability
de Ligt, J., Willemsen, M. H., van Bon, B. W. M., Kleefstra, T., Yntema, H. G., Kroes, T., Vulto-van Silfhout, A. T., Koolen, D. A., de Vries, P., Gilissen, C., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1206524 · Cited by 1,546 · see citing works
Self-citationGeneMatcher: a matching tool for connecting investigators with an interest in the same gene.
Sobreira, N., Schiettecatte, F., Valle, D., & Hamosh, A. (2015) · Human Mutation · doi:10.1002/humu.22844 · Cited by 1,529 · see citing works
Prevalence and architecture of de novo mutations in developmental disorders
Study, D. D. D. (2017) · Nature · doi:10.1038/nature21062 · Cited by 1,480 · see citing works
Deficient Hippocampal Long-Term Potentiation in α-Calcium-Calmodulin Kinase II Mutant Mice
Silva, A. J., Stevens, C. F., Tonegawa, S., & Wang, Y. (1992) · Science · doi:10.1126/science.1378648 · Cited by 1,472 · see citing works
Impaired Spatial Learning in α-Calcium-Calmodulin Kinase II Mutant Mice
Silva, A. J., Paylor, R. E., Wehner, J. M., & Tonegawa, S. (1992) · Science · doi:10.1126/science.1321493 · Cited by 1,351 · see citing works
Banker, G. A., & Goslin, K. (1998) · Cited by 1,290 · see citing works
Multiplex Targeted Sequencing Identifies Recurrently Mutated Genes in Autism Spectrum Disorders
O’Roak, B. J., Vives, L., Fu, W., Egertson, J. D., Stanaway, I. B., Phelps, I. G., Carvill, G., Kumar, A., Lee, C., Ankenman, K., et al. (2012) · Science · doi:10.1126/science.1227764 · Cited by 1,240 · see citing works
Self-citationNMDA receptor trafficking in synaptic plasticity and neuropsychiatric disorders
Lau, C. G., & Zukin, R. S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2153 · Cited by 1,159 · see citing works
Mechanisms 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 · see citing works
Large-scale discovery of novel genetic causes of developmental disorders
Study, T. D. D. D. (2015) · Nature · doi:10.1038/nature14135 · Cited by 1,124 · see citing works
Autophosphorylation at Thr <sup>286</sup> of the α Calcium-Calmodulin Kinase II in LTP and Learning
Giese, K. P., Fedorov, N. B., Filipkowski, R. K., & Silva, A. J. (1998) · Science · doi:10.1126/science.279.5352.870 · Cited by 1,055 · see citing works
Clinical application of whole-exome sequencing across clinical indications
Retterer, K., Juusola, J., Cho, M. T., Vitazka, P., Millan, F., Gibellini, F., Vertino-Bell, A., Smaoui, N., Neidich, J., Monaghan, K. G., et al. (2015) · Genetics in Medicine · doi:10.1038/gim.2015.148 · Cited by 1,036 · see citing works
Self-citationEfficient Gene Transfer into the Embryonic Mouse Brain Using in Vivo Electroporation
Saito, T., & Nakatsuji, N. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0439 · Cited by 770 · see citing works
Tabata, H., & Nakajima, K. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00016-1 · Cited by 705 · see citing works
Shen, K., & Meyer, T. (1999) · Science · doi:10.1126/science.284.5411.162 · Cited by 673 · see citing works
Regional distribution of type II Ca2+/calmodulin-dependent protein kinase in rat brain
Erondu, N., & Kennedy, M. (1985) · The Journal of Neuroscience · doi:10.1523/jneurosci.05-12-03270.1985 · Cited by 630 · see citing works
Mayford, M. R., Wang, J., Kandel, E. R., & O’Dell, T. J. (1995) · Cell · doi:10.1016/0092-8674(95)90009-8 · Cited by 525 · see citing works
Endele, S., Rosenberger, G., Geider, K., Popp, B., Tamer, C., Stefanova, I., Milh, M., Kortüm, F., Fritsch, A., Pientka, F. K., et al. (2010) · Nature Genetics · doi:10.1038/ng.677 · Cited by 499 · see citing works
Self-citationHagman, K. D. F., Shahmirzadi, L., El‐Khechen, D., Powis, Z., Chao, E., Davis, B. T., Baxter, R. M., Zeng, W., Mroske, C., Parra, M. C., et al. (2014) · Genetics in Medicine · doi:10.1038/gim.2014.154 · Cited by 469 · see citing works
Self-citationLesca, G., Rudolf, G., Bruneau, N., Lozovaya, N., Labalme, A., Boutry‐Kryza, N., Salmi, M., Tsintsadze, T. S., Addis, L., Motte, J. E., et al. (2013) · Nature Genetics · doi:10.1038/ng.2726 · Cited by 433 · see citing works
Self-citationMutations in GRIN2A cause idiopathic focal epilepsy with rolandic spikes
Lemke, J. R., Lal, D., Reinthaler, E. M., Steiner, I., Nothnagel, M., Alber, M., Geider, K., Laube, B., Schwake, M., Finsterwalder, K., et al. (2013) · Nature Genetics · doi:10.1038/ng.2728 · Cited by 428 · see citing works
Self-citationMony, L., Kew, J. N. C., Gunthorpe, M. J., & Paoletti, P. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00304.x · Cited by 404 · see citing works
GRIN2A mutations cause epilepsy-aphasia spectrum disorders
Carvill, G. L., Regan, B. M., Yendle, S. C., O’Roak, B. J., Lozovaya, N., Bruneau, N., Burnashev, N., Khan, A., Cook, J., Geraghty, E., et al. (2013) · Nature Genetics · doi:10.1038/ng.2727 · Cited by 375 · see citing works
Self-citationCaMKII: Claiming Center Stage in Postsynaptic Function and Organization
Hell, J. W. (2014) · Neuron · doi:10.1016/j.neuron.2013.12.024 · Cited by 351 · see citing works
Shen, K., Teruel, M. N., Subramanian, K., & Meyer, T. (1998) · Neuron · doi:10.1016/s0896-6273(00)80569-3 · Cited by 350 · see citing works
Hamdan, F. F., Gauthier, J., Araki, Y., Lin, D.-T., Yoshizawa, Y., Higashi, K., Park, A.-R., Spiegelman, D., Dobrzeniecka, S., Piton, A., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.02.001 · Cited by 349 · see citing works
Translational control in synaptic plasticity and cognitive dysfunction
Buffington, S. A., Huang, W., & Costa-Mattioli, M. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014100 · Cited by 348 · see citing works
Mutations in SWI/SNF chromatin remodeling complex gene ARID1B cause Coffin-Siris syndrome
Santen, G. W. E., Aten, E., Sun, Y., Almomani, R., Gilissen, C., Nielsen, M., Kant, S. G., Snoeck, I. N., Peeters, E. A. J., Hilhorst-Hofstee, Y., et al. (2012) · Nature Genetics · doi:10.1038/ng.2217 · Cited by 347 · see citing works
Self-citationInhibitory Autophosphorylation of CaMKII Controls PSD Association, Plasticity, and Learning
Elgersma, Y., Fedorov, N. B., Ikonen, S., Choi, E. S., Elgersma, M., Carvalho, O. M., Giese, K. P., & Silva, A. J. (2002) · Neuron · doi:10.1016/s0896-6273(02)01007-3 · Cited by 290 · see citing works
Chen, C., Rainnie, D. G., Greene, R. W., & Tonegawa, S. (1994) · Science · doi:10.1126/science.7939668 · Cited by 286 · see citing works
van Woerden, G. M., Harris, K. D., Hojjati, M. R., Gustin, R. M., Qiu, S., de Avila Freire, R., Jiang, Y.-H., Elgersma, Y., & Weeber, E. J. (2007) · Nature Neuroscience · doi:10.1038/nn1845 · Cited by 281 · see citing works
Targeting of calcium/calmodulin-dependent protein kinase II
Colbran, R. J. (2004) · Biochemical Journal · doi:10.1042/bj20031547 · Cited by 241 · see citing works
GRIN2B mutations in west syndrome and intellectual disability with focal epilepsy
Lemke, J. R., Hendrickx, R., Geider, K., Laube, B., Schwake, M., Harvey, R. J., James, V. M., Pepler, A., Steiner, I., Hörtnagel, K., et al. (2013) · Annals of Neurology · doi:10.1002/ana.24073 · Cited by 212 · see citing works
Bainbridge, M. N., Wang, M., Wu, Y., Newsham, I., Muzny, D. M., Jefferies, J. L., Albert, T. J., Burgess, D. L., & Gibbs, R. A. (2011) · Genome biology · doi:10.1186/gb-2011-12-7-r68 · Cited by 201 · see citing works
Li, D., Yuan, H., Ortiz-Gonzalez, X. R., Marsh, E. D., Tian, L., McCormick, E. M., Kosobucki, G. J., Chen, W., Schulien, A. J., Chiavacci, R. M., et al. (2016) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.07.013 · Cited by 176 · see citing works
Rare variants in neuronal excitability genes influence risk for bipolar disorder
Ament, S. A., Szelinger, S., Glusman, G., Ashworth, J. R., Hou, L., Akula, N., Shekhtman, T., Badner, J. A., Brunkow, M. E., Mauldin, D. E., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1424958112 · Cited by 175 · see citing works
Calmodulin kinases: essential regulators in health and disease
Takemoto‐Kimura, S., Suzuki, K., Horigane, S., Kamijo, S., Inoue, M., Sakamoto, M., Fujii, H., & Bito, H. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14020 · Cited by 171 · see citing works
Bayer, K. U., Löhler, J., Schulman, H., & Harbers, K. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00131-x · Cited by 167 · see citing works
Traynelis, J. L., Silk, M. A., Wang, Q., Berkovic, S. F., Liu, L., Ascher, D. B., Balding, D. J., & Petrovski, S. (2017) · Genome Research · doi:10.1101/gr.226589.117 · Cited by 166 · see citing works
Self-citationSynaptic plasticity in health and disease: introduction and overview
Bliss, T., Collingridge, G. L., & Morris, R. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2013.0129 · Cited by 154 · see citing works
Yamagata, Y., Kobayashi, S., Umeda, T., Inoue, A., Sakagami, H., Fukaya, M., Watanabe, M., Hatanaka, N., Totsuka, M., Yagi, T., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0707-09.2009 · Cited by 146 · see citing works
βCaMKII controls the direction of plasticity at parallel fiber–Purkinje cell synapses
van Woerden, G. M., Hoebeek, F. E., Gao, Z., Nagaraja, R. Y., Hoogenraad, C. C., Kushner, S. A., Hansel, C., Zeeuw, C. I. D., & Elgersma, Y. (2009) · Nature Neuroscience · doi:10.1038/nn.2329 · Cited by 132 · see citing works
Self-citationWu, Y., Arai, A., Rumbaugh, G., Srivastava, A. K., TURNER, G. M., Hayashi, T., Suzuki, É., Jiang, Y., Zhang, L., Rodriguez, J. D., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708699104 · Cited by 129 · see citing works
Stephenson, J. R., Wang, X., Perfitt, T. L., Parrish, W. P., Shonesy, B. C., Marks, C. R., Mortlock, D. P., Nakagawa, T., Sutcliffe, J. S., & Colbran, R. J. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2068-16.2017 · Cited by 127 · see citing works
Borgesius, N. Z., van Woerden, G. M., Buitendijk, G. H. S., Keijzer, N., Jaarsma, D., Hoogenraad, C. C., & Elgersma, Y. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5105-10.2011 · Cited by 124 · see citing works
Self-citationInterpreting de novo Variation in Human Disease Using denovolyzeR
Ware, J. S., Samocha, K. E., Homsy, J. G., & Daly, M. J. (2015) · Current Protocols in Human Genetics · doi:10.1002/0471142905.hg0725s87 · Cited by 117 · see citing works
The NMDA receptor complex: a multifunctional machine at the glutamatergic synapse
Fan, X., Jin, W. Y., & Wang, Y. T. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00160 · Cited by 117 · see citing works
De Novo Mutations in CHAMP1 Cause Intellectual Disability with Severe Speech Impairment
Hempel, M., Cremer, K., Ockeloen, C. W., Lichtenbelt, K. D., Herkert, J. C., Denecke, J., Haack, T. B., Zink, A. M., Becker, J., Wohlleber, E., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.08.003 · Cited by 99 · see citing works
Self-citationSmith, M. K., Colbran, R. J., Brickey, D. A., & Soderling, T. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46011-5 · Cited by 95 · see citing works
Barkus, C., Sanderson, D. J., Rawlins, J. N. P., Walton, M. E., Harrison, P. J., & Bannerman, D. M. (2014) · Molecular Psychiatry · doi:10.1038/mp.2014.91 · Cited by 94 · see citing works
Grant, S. G. N., & Silva, A. J. (1994) · Trends in Neurosciences · doi:10.1016/0166-2236(94)90077-9 · Cited by 80 · see citing works
Hoffman, L., Farley, M. M., & Waxham, M. N. (2013) · Biochemistry · doi:10.1021/bi3016586 · Cited by 76 · see citing works
Philips, A. K., Sirén, A., Avela, K., Somer, M., Peippo, M. M., Ahvenainen, M., Doagu, F., Arvio, M., Kääriäinen, H., Esch, H. V., et al. (2014) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-9-49 · Cited by 76 · see citing works
The CaMKII/GluN2B Protein Interaction Maintains Synaptic Strength
Barcomb, K., Hell, J. W., Benke, T. A., & Bayer, K. U. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.734822 · Cited by 76 · see citing works
In Utero Electroporation as a Tool For Genetic Manipulation In Vivo to Study Psychiatric Disorders
Taniguchi, Y., Young‐Pearse, T. L., Sawa, A., & Kamiya, A. (2011) · The Neuroscientist · doi:10.1177/1073858411399925 · Cited by 62 · see citing works
Impact of clinical exomes in neurodevelopmental and neurometabolic disorders
Evers, C., Staufner, C., Granzow, M., Paramasivam, N., Hinderhofer, K., Kaufmann, L. T., Fischer, C., Thiel, C., Opladen, T., Kotzaeridou, U., et al. (2017) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2017.06.014 · Cited by 59 · see citing works
Self-citationAssociation of genetic variants of GRIN2B with autism
Pan, Y., Chen, J., Guo, H., Ou, J., Peng, Y., Liu, Q., Shen, Y., Shi, L., Liu, Y., Xiong, Z., et al. (2015) · Scientific Reports · doi:10.1038/srep08296 · Cited by 56 · see citing works
Interplay of enzymatic and structural functions of Ca MKII in long‐term potentiation
Kim, K., Saneyoshi, T., Hosokawa, T., Okamoto, K., & Hayashi, Y. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13672 · Cited by 51 · see citing works
Isidor, B., Küry, S., Rosenfeld, J. A., Besnard, T., Schmitt, S., Joss, S. K., Davies, S. J., Lebel, R. R., Henderson, A., Schaaf, C. P., et al. (2016) · Human Mutation · doi:10.1002/humu.22952 · Cited by 49 · see citing works
Self-citationGeneration and Behavior Characterization of CaMKIIβ Knockout Mice
Bachstetter, A. D., Webster, S. J., Tu, T., Goulding, D. S., Haiech, J., Watterson, D. M., & Eldik, L. J. V. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105191 · Cited by 47 · see citing works
Temporal and Region-Specific Requirements of αCaMKII in Spatial and Contextual Learning
Achterberg, K. G., Buitendijk, G. H. S., Kool, M. J., Goorden, S. M. I., Post, L., Slump, D. E., Silva, A. J., van Woerden, G. M., Kushner, S. A., & Elgersma, Y. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.0640-14.2014 · Cited by 44 · see citing works
Self-citationThe role of GluA1 in central nervous system disorders
Zhang, J., & Abdullah, J. M. (2013) · Reviews in the Neurosciences · doi:10.1515/revneuro-2013-0021 · Cited by 40 · see citing works
Nesbitt, A. I., Bhoj, E. J. K., Gibson, K. M., Yu, Z., Denenberg, E. H., Sarmady, M., Tischler, T., Cao, K., Dubbs, H. A., Zackai, E. H., et al. (2015) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.37221 · Cited by 33 · see citing works
Self-citationKool, M. J., van de Bree, J. E., Bodde, H. E., Elgersma, Y., & van Woerden, G. M. (2016) · Scientific Reports · doi:10.1038/srep26989 · Cited by 31 · see citing works
Self-citationClinical heterogeneity associated with KCNA1 mutations include cataplexy and nonataxic presentations
Brownstein, C. A., Beggs, A. H., Rodan, L. H., Shi, J., Towne, M. C., Pelletier, R. C., Cao, S., Rosenberg, P. A., Urion, D. K., Picker, J. D., et al. (2015) · Neurogenetics · doi:10.1007/s10048-015-0460-2 · Cited by 27 · see citing works
Self-citationVincent, M., Collet, C., Verloès, A., Lambert, L., Herlin, C., Blanchet, C., Sanchez, E., Drunat, S., Vigneron, J., Laplanche, J., et al. (2013) · European Journal of Human Genetics · doi:10.1038/ejhg.2013.98 · Cited by 27 · see citing works
Self-citationYang, Y., Li, W., Zhang, H., Ge, Y., Wang, X., Ding, M., Jiang, T., & Lv, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125925 · Cited by 25 · see citing works
Self-citationThe role of GRIN2B in Tourette syndrome: Results from a transmission disequilibrium study
Che, F., Zhang, Y., Wang, G., Heng, X., Liu, S., & Du, Y. (2015) · Journal of Affective Disorders · doi:10.1016/j.jad.2015.07.036 · Cited by 15 · see citing works
Clinical exome sequencing – Norwegian findings
Holla, Ø. L., Busk, Ø. L., Tveten, K., Hilmarsen, H. T., Strand, L., Høyer, H., Bakken, A., Skjelbred, C. F., & Braathen, G. J. (2015) · Tidsskrift for Den norske legeforening · doi:10.4045/tidsskr.14.1442 · Cited by 8 · see citing works
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- Web Resources 1000 Genomes, http://www.internationalgenome.org/ CADD, http://cadd.gs.washington.edu/ ClinVar, https://www.ncbi.nlm.nih.gov/clinvar/ Clustal Omega, https://www.ebi.ac.uk/Tools/msa/clustalo/ dbSNP, https://www.ncbi.nlm.nih.gov/projects/SNP/ DECIPHER, https://decipher.sanger.ac.uk/ DiscovEHR, http://www.discovehrshare.com/ European Genome-phenome Archive (EGA), https://www.ebi.ac. uk/ega/studies/EGAS00001000775 ExAC Browser, http://exac.broadinstitute.org/ GATK, https://software.broadinstitute.org/gatk/ GenBank, https://www.ncbi.nlm.nih.gov/genbank/ GeneMatcher, https://genematcher.org/ Genic Intolerance, http://genic-intolerance.org/ gnomAD Browser, http://gnomad.broadinstitute.org/ GoNL (Genomes of the Netherlands), http://www.nlgenome.nl/ search/ GTEx Portal, https://www.gtexportal.org/home/ HBT -Human Brain Transcriptome, http://hbatlas.org/
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Sorted by citations
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Forrest, M. P., Parnell, E., & Penzes, P. (2018) · Nature Reviews Neuroscience · doi:10.1038/nrn.2018.16 · Cited by 464 · see citing works
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Yasuda, R., Hayashi, Y., & Hell, J. W. (2022) · Nature Reviews Neuroscience · doi:10.1038/s41583-022-00624-2 · Cited by 431 · see citing works
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Salpietro, V., Dixon, C. L., Guo, H., Bello, O. D., Vandrovcová, J., Efthymiou, S., Maroofian, R., Heimer, G., Bürglen, L., Valence, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10910-w · Cited by 247 · see citing works
Self-citationNicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
“These in turn increase autophosphorylation of T286 (or T287 in some isoforms) that further increases constitutive activity (429, 430).”
BackgroundChemin, J., Siquier-Pernet, K., Nicouleau, M., Barcia, G., Ahmad, A., Medina-Cano, D., Hanein, S., Altin, N., Hubert, L., Bôle‐Feysot, C., et al. (2018) · Brain · doi:10.1093/brain/awy145 · Cited by 106 · see citing works
Hayashi, Y. (2022) · Neuroscience Research · doi:10.1016/j.neures.2021.08.001 · Cited by 102 · see citing works
The Role of Calmodulin in Tumor Cell Migration, Invasiveness, and Metastasis
Villalobo, A., & Berchtold, M. W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030765 · Cited by 97 · see citing works
Bhattacharyya, M., Karandur, D., & Kuriyan, J. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a035147 · Cited by 95 · see citing works
Liu, W., Liao, X., Yang, Y., Lin, H., Yeong, J. P.-S., Zhou, X., Shi, X., & Liu, J. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac219 · Cited by 89 · see citing works
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Baker, S. W., Murrell, J. R., Nesbitt, A. I., Pechter, K. B., Balciuniene, J., Zhao, X., Yu, Z., Denenberg, E. H., DeChene, E. T., Wilkens, A., et al. (2018) · Journal of Molecular Diagnostics · doi:10.1016/j.jmoldx.2018.07.008 · Cited by 88 · see citing works
Self-citationAkita, T., Aoto, K., Kato, M., Shiina, M., Mutoh, H., Nakashima, M., Kuki, I., Okazaki, S., Magara, S., Shiihara, T., et al. (2018) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.528 · Cited by 87 · see citing works
Ostrander, B., Butterfield, R. J., Pedersen, B. S., Farrell, A., Layer, R. M., Ward, A. N., Miller, C., DiSera, T., Filloux, F. M., Candee, M. S., et al. (2018) · npj Genomic Medicine · doi:10.1038/s41525-018-0061-8 · Cited by 87 · see citing works
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Self-citationWang, Z.-J., Zhong, P., Ma, K., Seo, J.-S., Yang, F., Hu, Z., Zhang, F., Lin, L., Wang, J., Liu, T., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0351-2 · Cited by 82 · see citing works
Chia, P. H., Zhong, F. L., Niwa, S., Bonnard, C., Utami, K. H., Zeng, R., Lee, H., Eskin, A., Nelson, S. F., Xie, W. H., et al. (2018) · eLife · doi:10.7554/elife.32451 · Cited by 71 · see citing works
Li, J., Gao, K., Yan, H., XiangWei, W., Liu, N., Wang, T., Han, X., Lin, Z., Xie, H., Wang, J., et al. (2019) · Gene · doi:10.1016/j.gene.2019.03.037 · Cited by 71 · see citing works
Pandya, N. J., Wang, C., Costa, V., Lopatta, P., Meier, S., Zampeta, F. I., Punt, A. M., Mientjes, E., Grossen, P., Distler, T., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100360 · Cited by 71 · see citing works
Self-citationTakata, A., Nakashima, M., Saitsu, H., Mizuguchi, T., Mitsuhashi, S., Takahashi, Y., Okamoto, N., Osaka, H., Nakamura, K., Tohyama, J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10482-9 · Cited by 70 · see citing works
Schmitz‐Abe, K., Li, Q., Rosen, S. M., Nori, N., Madden, J. A., Genetti, C. A., Wojcik, M. H., Ponnaluri, S., Gubbels, C. S., Picker, J. D., et al. (2019) · European Journal of Human Genetics · doi:10.1038/s41431-019-0401-x · Cited by 68 · see citing works
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Shimasaki, C., Frye, R. E., Trifiletti, R., Cooperstock, M., Kaplan, G., Melamed, I., Greenberg, R., Katz, A., Fier, E., Kem, D., et al. (2020) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2019.577138 · Cited by 61 · see citing works
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van Woerden, G. M., Bos, M., de Konink, C., Distel, B., Trezza, R. A., Shur, N. E., Baranano, K. W., Mahida, S., Chassevent, A., Schreiber, A., et al. (2021) · Human Mutation · doi:10.1002/humu.24176 · Cited by 55 · see citing works
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Roberts, J. A., Varma, V. R., An, Y., Varma, S., Candia, J., Fantoni, G., Tiwari, V., Anerillas, C., Williamson, A., Saito, A., et al. (2021) · Science Advances · doi:10.1126/sciadv.abi8178 · Cited by 49 · see citing works
Mohanan, A. G., Gunasekaran, S., Jacob, R. S., & Omkumar, R. V. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.855752 · Cited by 57 · see citing works
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Serrano, G. E., Walker, J. E., Tremblay, C., Piras, I. S., Huentelman, M. J., Belden, C. M., Goldfarb, D., Shprecher, D., Atri, A., Adler, C. H., et al. (2022) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlac056 · Cited by 44 · see citing works
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Liaci, C., Camera, M., Caslini, G., Rando, S., Contino, S., Romano, V., & Merlo, G. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116167 · Cited by 39 · see citing works
Proietti Onori, M., Koopal, B., Everman, D. B., Worthington, J. D., Jones, J. R., Ploeg, M. A., Mientjes, E., van Bon, B. W., Kleefstra, T., Schulman, H., et al. (2018) · Human Mutation · doi:10.1002/humu.23647 · Cited by 39 · see citing works
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Liu, Z., Tan, S., Zhou, L., Chen, L., Liu, M., Wang, W., Tang, Y., Yang, Q., Chi, S., Jiang, P., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01225-2 · Cited by 34 · see citing works
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Nourbakhsh, K., & Yadav, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.624648 · Cited by 30 · see citing works
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Cao, Y., Ling-Ling, W., Li, X., Yuan, Y.-L., Zhao, W., Qi, J., Zhao, X.-Y., Ward, N., & Wang, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010111 · Cited by 31 · see citing works
Zheng, Q., Zhang, H., Zhao, H., Chen, Y., Yang, H., Li, T., Cai, Q., Chen, Y., Wang, Y., Zhang, M., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.12.005 · Cited by 29 · see citing works
Muraleva, N. A., Kolosova, N. G., & Stefanova, N. A. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.01.017 · Cited by 29 · see citing works
Wu, L.-Y., Zeeshan, M., Dang, Y., Zhang, Y., Liang, L.-X., Huang, J.-W., Zhou, J.-X., Guo, L.-H., Fan, Y.-Y., Sun, M.-K., et al. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.164838 · Cited by 28 · see citing works
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Peng, J., Tseng, R.-H., Shih, T., & Hsieh, S. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.10.017 · Cited by 25 · see citing works
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Li, T., Feng, X., Zhang, N., Chen, J., Zhang, Y., Yang, H., Peng, S., Ma, R., Liu, Q., Gan, S., et al. (2024) · Genes · doi:10.3390/genes15121637 · Cited by 24 · see citing works
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Betancur, C., & Buxbaum, J. D. (2020) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2020.05.036 · Cited by 24 · see citing works
Pizzo, L., Lasser, M. C., Yusuff, T., Jensen, M., Ingraham, P., Huber, E., Singh, M. D., Monahan, C., Iyer, J. S., Desai, I., et al. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009112 · Cited by 24 · see citing works
Dzinovic, I., Winkelmann, J., & Zech, M. (2022) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2022.08.019 · Cited by 24 · see citing works
Zhen, H., Deng, H., Song, Q., Zheng, M., Yuan, Z., Cao, Z., Pang, Q., & Zhao, B. (2020) · The FASEB Journal · doi:10.1096/fj.201903040rr · Cited by 22 · see citing works
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Alkelai, A., Greenbaum, L., Docherty, A. R., Shabalin, A. A., Povysil, G., Malakar, A., Hughes, D., Delaney, S. L., Peabody, E. P., McNamara, J., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01383-9 · Cited by 22 · see citing works
Zech, M., Lam, D. D., Weber, S., Berutti, R., Poláková, K., Havránková, P., Fečíková, A., Strom, T. M., Růžička, E., Jech, R., et al. (2018) · Molecular Case Studies · doi:10.1101/mcs.a003293 · Cited by 22 · see citing works
Lee, Y., Hwang, S., Lee, S., Yang, J.-E., Kwak, J., Seo, H., Ahn, H. M., Lee, Y., Kim, J., Lim, C., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9061886 · Cited by 21 · see citing works
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Brown, C. N., Cook, S. G., Allen, H. F., Crosby, K. C., Singh, T., Coultrap, S. J., & Bayer, K. U. (2021) · iScience · doi:10.1016/j.isci.2021.103184 · Cited by 28 · see citing works
HDAC3 of dorsal hippocampus induces postoperative cognitive dysfunction in aged mice
Li, Y., Hao, J., Gao, Y., Yang, X., Shen, X., Wang, H.-Y., Sun, N., & Gao, C. (2022) · Behavioural Brain Research · doi:10.1016/j.bbr.2022.114002 · Cited by 21 · see citing works
Rudolf, G., de Bellescize, J., Martin, A. D. S., Arzimanoglou, A. A., Hirsch, M. P. V., Labalme, A., Boulay, C., Simonet, T., Boland, A., Deleuze, J., et al. (2020) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2020.05.003 · Cited by 21 · see citing works
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Koire, A. M., Buchovecky, C., Katsonis, P., Kim, Y. W., Wilson, S. J., & Lichtarge, O. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abc1739 · Cited by 22 · see citing works
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Barone, I., Hawks-Mayer, H., & Lipton, J. O. (2019) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2019.01.011 · Cited by 21 · see citing works
Pellikaan, K., van Woerden, G. M., Kleinendorst, L., Rosenberg, A. G. W., Horsthemke, B., Grosser, C., van Zutven, L. J. C. M., van Rossum, E. F. C., van der Lely, A. J., Resnick, J. L., et al. (2021) · Genes · doi:10.3390/genes12060875 · Cited by 19 · see citing works
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Wei, C., Sun, M., Sun, X., Meng, H., Li, Q., Gao, K., Yue, W., Wang, L., Zhang, D., & Li, J. (2021) · Neuroscience Bulletin · doi:10.1007/s12264-021-00804-7 · Cited by 19 · see citing works
Rizzi, S., Spagnoli, C., Salerno, G. G., Frattini, D., Caraffi, S. G., Trimarchi, G., Moratti, C., Pascarella, R., Garavelli, L., & Fusco, C. (2020) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61803 · Cited by 19 · see citing works
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Tian, Y., Shehata, M. A., Gauger, S. J., Veronesi, C., Hamborg, L., Thiesen, L., Bruus‐Jensen, J., Royssen, J. S., Leurs, U., Larsen, A. S. G., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00805 · Cited by 16 · see citing works
Rosenberg, A. G. W., Pater, M. R. A., Pellikaan, K., Davidse, K., Kattentidt‐Mouravieva, A. A., Kersseboom, R., Bos‐Roubos, A. G., van Eeghen, A. M., Veen-Roelofs, J. M. C., van der Meulen, J. J., et al. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10225457 · Cited by 19 · see citing works
Fernandes‐Junior, S. A., Oliveira, L. M., Czeisler, C. M., Mo, X. M., Roy, S., Somogyi, Á., Zhang, L., Moreira, T. S., Otero, J. J., & Takakura, A. C. T. (2020) · Brain Pathology · doi:10.1111/bpa.12868 · Cited by 16 · see citing works
Medyanik, A. D., Anisimova, P. E., Kustova, A. O., Tarabykin, V. S., & Kondakova, E. V. (2025) · Biomolecules · doi:10.3390/biom15010133 · Cited by 15 · see citing works
Gold, N. B., Li, D., Chassevent, A., Kaiser, F. J., Parenti, I., Strom, T. M., Ramos, F. J., Puisac, B., Pié, J., McWalter, K. M., et al. (2020) · Clinical Genetics · doi:10.1111/cge.13851 · Cited by 15 · see citing works
Self-citationGavrilovici, C., Jiang, Y., Kiroski, I., Sterley, T.-L., Vandal, M., Bains, J. S., Park, S. K., Rho, J. M., Teskey, G. C., & Nguyen, M. D. (2021) · Cerebral Cortex Communications · doi:10.1093/texcom/tgaa096 · Cited by 15 · see citing works
Sim, K. H., & Lee, Y. J. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.132503 · Cited by 15 · see citing works
Dwyer, B. K., Veenma, D. C. M., Chang, K., Schulman, H., & van Woerden, G. M. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.794008 · Cited by 15 · see citing works
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Zheng, J. J., Zhang, W., Liu, L., & Yap, M. K. H. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1109735 · Cited by 14 · see citing works
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Murano, T., Nakajima, R., Nakao, A., Hirata, N., Amemori, S., Murakami, A., Kamitani, Y., Yamamoto, J., & Miyakawa, T. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106830119 · Cited by 13 · see citing works
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Fell, C. W., & Nagy, V. (2021) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.12.003 · Cited by 14 · see citing works
Tian, Y., Shehata, M. A., Gauger, S. J., Ng, C. K. L., Solbak, S. M. Ø., Thiesen, L., Bruus‐Jensen, J., Krall, J., Bundgaard, C., Gibson, K. M., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02177 · Cited by 13 · see citing works
Borghi, R., Trivisano, M., Specchio, N., Tartaglia, M., & Compagnucci, C. (2023) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2023.105299 · Cited by 12 · see citing works
Zsolnai, A., Csókás, A., Szabó, L., Patkó, L., Csányi, S., Márton, M., Lakatos, E. A., Anton, I., Deutsch, F., & Heltai, M. (2022) · Mammalian Biology · doi:10.1007/s42991-021-00212-4 · Cited by 12 · see citing works
Netrin‐G2 dysfunction causes a Rett‐like phenotype with areflexia
Heimer, G., van Woerden, G. M., Barel, O., Marek‐Yagel, D., Kol, N., Munting, J. B., Borghei, M., Atawneh, O., Nissenkorn, A., Rechavi, G., et al. (2019) · Human Mutation · doi:10.1002/humu.23945 · Cited by 12 · see citing works
Self-citationKim, K.-R., Jeong, H., Kim, Y., Lee, S. Y., Kim, Y., Kim, H.-J., Lee, S., Cho, H., Kang, J.-S., & Ho, W. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00645-4 · Cited by 11 · see citing works
Association of CaMK2A and MeCP2 signaling pathways with cognitive ability in adolescents
Lee, L., Su, M., Huang, H.-Y., Cho, Y., Yeh, T., & Chang, C. (2021) · Molecular Brain · doi:10.1186/s13041-021-00858-8 · Cited by 11 · see citing works
Molecular Diagnostic Outcomes from 700 Cases
Murrell, J. R., Nesbitt, A. M. I., Baker, S. W., Pechter, K. B., Balciuniene, J., Zhao, X., Denenberg, E. H., DeChene, E. T., Wu, C., Jayaraman, P., et al. (2022) · Journal of Molecular Diagnostics · doi:10.1016/j.jmoldx.2021.12.002 · Cited by 11 · see citing works
Self-citationFeatherstone, R. E., Shimada, T., Crown, L. M., Melnychenko, O., Yi, J., Matsumoto, M., Tajinda, K., Mihara, T., Adachi, M., & Siegel, S. J. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.07.023 · Cited by 19 · see citing works
Liu, S., Lian, M., Fang, J., Zhai, J., Shen, X., & Wang, R. (2018) · Europe PMC (PubMed Central) · Cited by 10 · see citing works
Lecoquierre, F., Punt, A. M., Ebstein, F., Wallaard, I., Verhagen, R. F. M., Studencka‐Turski, M., Duffourd, Y., Moutton, S., Mau-Them, F. T., Philippe, C., et al. (2024) · Genetics in Medicine · doi:10.1016/j.gim.2024.101119 · Cited by 9 · see citing works
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 · see citing works
Rigter, P. M. F., Wallaard, I., Jolfaei, M. A., Kingma, J., Post, L. C., Elgersma, M., Elgersma, Y., & van Woerden, G. M. (2022) · iScience · doi:10.1016/j.isci.2022.105303 · Cited by 10 · see citing works
Self-citationKong, L., Yang, H., Yang, J., Jiang, L., Xu, B., Yang, T., & Liu, W. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.117835 · Cited by 9 · see citing works
Chang, W.-L., Tegang, K., Samuels, B. A., Saxe, M., Wichmann, J., David, D. J. P., Mendez‐David, I., Augustin, A., Fischer, H., Golling, S., et al. (2024) · Biological Psychiatry Global Open Science · doi:10.1016/j.bpsgos.2024.100419 · Cited by 8 · see citing works
Conformational spread drives the evolution of the calcium–calmodulin protein kinase II
Khan, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-12090-y · Cited by 8 · see citing works
Genetic and clinical landscape of childhood cerebellar hypoplasia and atrophy
Sakamoto, M., Iwama, K., Sasaki, M., Ishiyama, A., Komaki, H., SAITO, T. K., Takeshita, E., Shimizu‐Motohashi, Y., Haginoya, K., Kobayashi, T., et al. (2022) · Genetics in Medicine · doi:10.1016/j.gim.2022.08.007 · Cited by 8 · see citing works
Malik, M. A., Saqib, M. A. N., Mientjes, E., Acharya, A., Alam, M. R., Wallaard, I., Schrauwen, I., Bamshad, M. J., Santos‐Cortez, R. L. P., Elgersma, Y., et al. (2023) · European Journal of Human Genetics · doi:10.1038/s41431-023-01475-w · Cited by 8 · see citing works
Self-citationConformational coupling by trans-phosphorylation in calcium calmodulin dependent kinase II
Pandini, A., Schulman, H., & Khan, S. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006796 · Cited by 7 · see citing works
A familial case of CAMK2B mutation with variable expressivity
Heiman, P., Drewes, S., & Ghaloul‐Gonzalez, L. (2021) · SAGE Open Medical Case Reports · doi:10.1177/2050313x21990982 · Cited by 8 · see citing works
Luo, Y., Yang, Y., Zhang, M., & Fan, N. (2022) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2022.577998 · Cited by 7 · see citing works
Self-citation
- Authors
- Küry, S., van Woerden, G. M., Besnard, T., Proietti Onori, M., Latypova, X., Towne, M. C., Cho, M. T., Prescott, T. E., Ploeg, M. A., Sanders, S., Stessman, H. A. F., Pujol, A., Distel, B., Robak, L. A., Bernstein, J. A., Denommé-Pichon, A.-S., Lesca, G., Sellars, E. A., Berg, J., Carré, W., Busk, Ø. L., van Bon, B. W. M., Waugh, J. L., Deardorff, M., Hoganson, G. E., Bosanko, K. B., Johnson, D. S., Dabir, T., Holla, Ø. L., Sarkar, A., Tveten, K., de Bellescize, J., Braathen, G. J., Terhal, P. A., Grange, D. K., van Haeringen, A., Lam, C., Mirzaa, G., Burton, J., Bhoj, E. J., Douglas, J., Santani, A. B., Nesbitt, A. I., Helbig, K. L., Andrews, M. V., Begtrup, A., Tang, S., van Gassen, K. L. I., Juusola, J., Foss, K., Enns, G. M., Moog, U., Hinderhofer, K., Paramasivam, N., Lincoln, S., Kusako, B. H., Lindenbaum, P., Charpentier, E., Nowak, C. B., Cherot, E., Simonet, T., Ruivenkamp, C. A. L., Hahn, S., Brownstein, C. A., Xia, F., Schmitt, S., Deb, W., Bonneau, D., Nizon, M., Quinquis, D., Chelly, J., Rudolf, G., Sanlaville, D., Parent, P., Gilbert-Dussardier, B., Toutain, A., Sutton, V. R., Thies, J., Peart-Vissers, L. E. L. M., Boisseau, P., Vincent, M., Grabrucker, A. M., Dubourg, C., Tan, W.-H., Verbeek, N. E., Granzow, M., Santen, G. W. E., Shendure, J., Isidor, B., Pasquier, L., Redon, R., Yang, Y., State, M. W., Kleefstra, T., Cogné, B., Petrovski, S., Retterer, K., Eichler, E. E., Rosenfeld, J. A., Agrawal, P. B., Bézieau, S., Odent, S., Elgersma, Y., & Mercier, S.
- Affiliations
- Centre Hospitalier Universitaire de Nantes (FR)
- Boston Children's Hospital (US)
- Telemark Hospital (NO)
- Erasmus MC (NL)
- University of California, San Francisco (US)
- Creighton University (US)
- Institució Catalana de Recerca i Estudis Avançats (ES)
- Baylor College of Medicine (US)
- Stanford Medicine (US)
- Centre National de la Recherche Scientifique (FR)
- Arkansas Children's Hospital (US)
- University of Dundee (GB)
- Centre Hospitalier Universitaire de Rennes (FR)
- Children's Hospital of Philadelphia (US)
- University of Illinois Chicago (US)
- Sheffield Children's Hospital (GB)
- Belfast Health and Social Care Trust (GB)
- Nottingham University Hospitals NHS Trust (GB)
- University Medical Center Utrecht (NL)
- Washington University in St. Louis (US)
- Seattle Children's Hospital (US)
- Ambry Genetics (United States) (US)
- Seattle Children's Research Institute (US)
- Heidelberg University (DE)
- German Cancer Research Center (DE)
- Hospices Civils de Lyon (FR)
- Leiden University Medical Center (NL)
- Centre Hospitalier Régional Universitaire de Brest (FR)
- Centre Hospitalier Universitaire de Tours (FR)
- Baylor Genetics (US)
- University of Limerick (IE)
- Howard Hughes Medical Institute (US)
- Radboud University Nijmegen (NL)
- The Royal Melbourne Hospital (AU)
- Corresponding author
- Küry, Sébastien
- Elgersma, Ype
- ORCID
- Küry, Sébastien
- Besnard, Thomas
- Latypova, Xénia
- Towne, Meghan C.
- Cho, Megan T.
- Prescott, Trine E.
- Sanders, Stephan
- Stessman, Holly A.F.
- Pujol, Aurora
- Distel, Ben
- Robak, Laurie A.
- Bernstein, Jonathan A.
- Lesca, Gaëtan
- Sellars, Elizabeth A.
- Berg, Jonathan
- Carré, Wilfrid
- Busk, Øyvind Løvold
- Waugh, Jeff L.
- Deardorff, Matthew
- Johnson, Diana S.
- Holla, Øystein Lunde
- Tveten, Kristian
- Braathen, Geir J.
- Terhal, Paulien A.
- Grange, Dorothy K.
- Lam, Christina
- Mirzaa, Ghayda
- Bhoj, Elizabeth J.
- Santani, Avni B.
- Nesbitt, Addie I.
- Helbig, Katherine L.
- Andrews, Marisa V.
- Begtrup, Amber
- Tang, Sha
- Juusola, Jane
- Foss, Kimberly
- Enns, Gregory M.
- Moog, Ute
- Hinderhofer, Katrin
- Paramasivam, Nagarajan
- Lindenbaum, Pierre
- Ruivenkamp, Claudia A.L.
- Xia, Fan
- Schmitt, Sébastien
- Deb, Wallid
- Bonneau, Dominique
- Nizon, Mathilde
- Chelly, Jamel
- Rudolf, Gabrielle
- Sanlaville, Damien
- Toutain, Annick
- Sutton, Vernon R.
- Thies, Jenny
- Vincent, Marie
- Grabrucker, Andreas M.
- Dubourg, Christèle
- Tan, Wen-Hann
- Santen, Gijs W.E.
- Shendure, Jay
- Isidor, Bertrand
- Pasquier, Laurent
- Redon, Richard
- Yang, Yaping
- State, Matthew W.
- Kleefstra, Tjitske
- Cogné, Benjamin
- Petrovski, Slavé
- Retterer, Kyle
- Eichler, Evan E.
- Rosenfeld, Jill A.
- Agrawal, Pankaj B.
- Odent, Sylvie
- Elgersma, Ype
- Mercier, Sandra
- Venue
- The American Journal of Human Genetics
- Publisher
- Elsevier BV
- Published
- 2017-11
- Volume
- 101
- Issue
- 5
- Pages
- 768-788
- ISSN
- 0002-9297 (ISSN-L)
- PMC
- PMC5673671
- OpenAlex
- W2766852890
- Cited by
- 185
- References
- 78
- Citations by year
- 2026: 15 · 2025: 22 · 2024: 25 · 2023: 18 · 2022: 29 · 2021: 29 · 2020: 21 · 2019: 15 · 2018: 11
- FWCI
- 8.53
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The American Journal of Human Genetics (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (publishedVersion)
- Leiden Repository (Leiden University) (submittedVersion)
- Radboud Repository (Radboud University) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- HAL (submittedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- eScholarship (California Digital Library) (submittedVersion)
- Pure Amsterdam UMC (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Funders
- National Institute of Mental Health (R01MH101221)
- National Institute of Neurological Disorders and Stroke (K08NS092898)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR068429)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (U19HD077671)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Down syndrome and intellectual disability research
- Keywords
- CAMK2A, CAMK2B, calcium/calmodulin-dependent protein kinase II, de novo mutations, intellectual disability, autophosphorylation, neuronal migration, brain development, glutamatergic signaling, synaptic plasticity, rare variants
- MeSH terms
- Animals, Brain, Cell Line, Female, Humans, Male, Intellectual Disability, Mice, Inbred C57BL, Mutation, Neurons, Phosphorylation, Signal Transduction, Glutamic Acid, Mice, Calcium-Calmodulin-Dependent Protein Kinase Type 2, HEK293 Cells, Exome
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