DAPK1 Interaction with NMDA Receptor NR2B Subunits Mediates Brain Damage in Stroke
Open accessAbstract
N-methyl-D-aspartate (NMDA) receptors constitute a major subtype of glutamate receptors at extrasynaptic sites that link multiple intracellular catabolic processes responsible for irreversible neuronal death. Here, we report that cerebral ischemia recruits death-associated protein kinase 1 (DAPK1) into the NMDA receptor NR2B protein complex in the cortex of adult mice. DAPK1 directly binds with the NMDA receptor NR2B C-terminal tail consisting of amino acid 1292-1304 (NR2B(CT)). A constitutively active DAPK1 phosphorylates NR2B subunit at Ser-1303 and in turn enhances the NR1/NR2B receptor channel conductance. Genetic deletion of DAPK1 or administration of NR2B(CT) that uncouples an activated DAPK1 from an NMDA receptor NR2B subunit in vivo in mice blocks injurious Ca(2+) influx through NMDA receptor channels at extrasynaptic sites and protects neurons against cerebral ischemic insults. Thus, DAPK1 physically and functionally interacts with the NMDA receptor NR2B subunit at extrasynaptic sites and this interaction acts as a central mediator for stroke damage.
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
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?
Phosphorylation of S1303 in heterologous cells enhances NMDAR current.
“Phosphorylation of S1303 in heterologous cells enhances NMDAR current (127, 128)”
From Synaptic memory and CaMKII (2023) · cites this paper as [128]
DAPK1 is a calcium-dependent serine/threonine kinase highly expressed in the cortex in Alzheimer's disease, after ischemic damage, and in physiological ageing where it may play a role in the decay of learning and memory.
“DAPK1 (FC = 1.08, p = 0.05) is a calcium-dependent serine/threonine kinase that is highly expressed in the cortex in AD [167], after ischemic damage [154], and in physiological ageing where it has been suggested to play a role in the decay of learning and memory with age [51].”
From Early onset senescence and cognitive impairment in a murine model of repeated mTBI (2021) · cites this paper as [154]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The 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
Mechanisms, challenges and opportunities in stroke
Lo, E. H., Dalkara, T., & Moskowitz, M. A. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1106 · Cited by 1,783 · see citing works
Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
Hardingham, G. E., Fukunaga, Y., & Bading, H. (2002) · Nature Neuroscience · doi:10.1038/nn835 · Cited by 1,686 · see citing works
Blockade of N -Methyl-D-Aspartate Receptors May Protect Against Ischemic Damage in the Brain
Simon, R. P., Swan, J. H., Griffiths, T., & Meldrum, B. S. (1984) · Science · doi:10.1126/science.6093256 · Cited by 1,682 · see citing works
Ca 2+ -Induced Apoptosis Through Calcineurin Dephosphorylation of BAD
Wang, H., Pathan, N., Ethell, I. M., Krajewski, S., Yamaguchi, Y., Shibasaki, F., McKeon, F., Bobo, T., Franke, T. F., & Reed, J. C. (1999) · Science · doi:10.1126/science.284.5412.339 · Cited by 1,132 · see citing works
Glutamate release in severe brain ischaemia is mainly by reversed uptake
Rossi, D. J., Oshima, T., & Attwell, D. (2000) · Nature · doi:10.1038/35002090 · Cited by 1,128 · see citing works
Treatment of Ischemic Brain Damage by Perturbing NMDA Receptor- PSD-95 Protein Interactions
Aarts, M., Liu, Y., Liu, L.-D., Besshoh, S., Arundine, M., Gurd, J. W., Wang, Y.-T., Salter, M., & Tymianski, M. (2002) · Science · doi:10.1126/science.1072873 · Cited by 1,048 · see citing works
Xiong, Z., Zhu, X., Chu, X., Minami, M., Hey, J. G., Wei, W., MacDonald, J. F., Wemmie, J. A., Price, M. P., Welsh, M. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.08.026 · Cited by 1,026 · see citing works
Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond
Lipton, S. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1958 · Cited by 909 · see citing works
S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
Uehara, T., Nakamura, T., Yao, D., Shi, Z., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., & Lipton, S. A. (2006) · Nature · doi:10.1038/nature04782 · Cited by 908 · see citing works
The Neurobiology of Slow Synaptic Transmission
Greengard, P. (2001) · Science · doi:10.1126/science.294.5544.1024 · Cited by 865 · see citing works
Tovar, K. R., & Westbrook, G. L. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-10-04180.1999 · Cited by 786 · see citing works
A Key Role for TRPM7 Channels in Anoxic Neuronal Death
Aarts, M. M., Iihara, K., Wei, W.-L., Xiong, Z.-G., Arundine, M., Cerwinski, W., MacDonald, J. F., & Tymianski, M. (2003) · Cell · doi:10.1016/s0092-8674(03)01017-1 · Cited by 784 · see citing works
Src kinases: a hub for NMDA receptor regulation
Salter, M. W., & Kalia, L. V. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1368 · Cited by 777 · see citing works
Liu, Y., Wong, T. P., Aarts, M., Rooyakkers, A., Liu, L., Lai, T. W., Wu, D. C., Lu, J., Tymianski, M., Craig, A. M., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0116-07.2007 · Cited by 773 · see citing works
Excitatory glycine receptors containing the NR3 family of NMDA receptor subunits
Chatterton, J. E., Awobuluyi, M., Premkumar, L. S., Takahashi, H., Talantova, M. V., Shin, Y., Cui, J., Tu, S., Sevarino, K. A., Nakanishi, N., et al. (2002) · Nature · doi:10.1038/nature715 · Cited by 695 · see citing works
Kinouchi, H., Epstein, C. J., Mizui, T., Carlson, E. J., Chen, S. F., & Chan, P. H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11158 · Cited by 589 · see citing works
Synaptic Strength Regulated by Palmitate Cycling on PSD-95
El-Husseini, A., Schnell, E., Dakoji, S., Sweeney, N. T., Zhou, Q., Prange, O., Gauthier-Campbell, C., Aguilera-Moreno, A., Nicoll, R. A., & Bredt, D. S. (2002) · Cell · doi:10.1016/s0092-8674(02)00683-9 · Cited by 569 · see citing works
The GluR2 (GluR-B) hypothesis: Ca2+-permeable AMPA receptors in neurological disorders
Pellegrini-Giampietro, D. E. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01100-4 · Cited by 548 · see citing works
Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia
Krajewski, S., Krajewska, M., Ellerby, L., Welsh, K., Xie, Z., Deveraux, Q. L., Salvesen, G. S., Bredesen, D. E., Rosenthal, R. E., Fiskum, G. M., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5752 · Cited by 542 · see citing works
Cleavage of the Plasma Membrane Na+/Ca2+ Exchanger in Excitotoxicity
Bano, D., Young, K. W., Guérin, C. J., Feuvre, R. A. L., Rothwell, N. J., Naldini, L., Rizzuto, R., Carafoli, E., & Nicotera, P. (2005) · Cell · doi:10.1016/j.cell.2004.11.049 · Cited by 532 · see citing works
Modulation of NMDA Receptor- Dependent Calcium Influx and Gene Expression Through EphB Receptors
Takasu, M. A., Dalva, M. B., Zigmond, R. E., & Greenberg, M. E. (2002) · Science · doi:10.1126/science.1065983 · Cited by 497 · see citing works
Cellular Origin of Ischemia‐Induced Glutamate Release from Brain Tissue In Vivo and In Vitro
Drejer, J., Benveniste, H., Diemer, N. H., & Schousboe, A. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb05486.x · Cited by 463 · see citing works
Importance of the Intracellular Domain of NR2 Subunits for NMDA Receptor Function In Vivo
Sprengel, R., Suchanek, B., Amico, C., Brusa, R., Burnashev, N., Rozov, A. V., Hvalby, Ø., Jensen, V., Paulsen, O., Andersen, P. N., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)80921-6 · Cited by 460 · see citing works
CREB Couples Neurotrophin Signals to Survival Messages
Finkbeiner, S. M. (2000) · Neuron · doi:10.1016/s0896-6273(00)80866-1 · Cited by 454 · see citing works
The Death-Associated Protein Kinases: Structure, Function, and Beyond
Bialik, S., & Kimchi, A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142615 · Cited by 441 · see citing works
The structure and function of glutamate receptor ion channels
Madden, D. R. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn725 · Cited by 381 · see citing works
Eliasson, M. J. L., Huang, Z., Ferrante, R. J., Sasamata, M., Molliver, M. E., Snyder, S. H., & Moskowitz, M. A. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-14-05910.1999 · Cited by 366 · see citing works
Mitochondria in Neurodegeneration: Acute Ischemia and Chronic Neurodegenerative Diseases
Fiskum, G. M., Murphy, A. N., & Beal, M. F. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199904000-00001 · Cited by 351 · see citing works
Omkumar, R. V., Kiely, M. J., Rosenstein, A. J., Min, K.-T., & Kennedy, M. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31670 · Cited by 304 · see citing works
Synaptic and Extrasynaptic NMDA Receptor NR2 Subunits in Cultured Hippocampal Neurons
Thomas, C. G., Miller, A., & Westbrook, G. L. (2005) · Journal of Neurophysiology · doi:10.1152/jn.00771.2005 · Cited by 286 · see citing works
Cdk5 activation induces hippocampal CA1 cell death by directly phosphorylating NMDA receptors
Wang, J., Liu, S., Fu, Y., Wang, J. H.-C., & Lu, Y. (2003) · Nature Neuroscience · doi:10.1038/nn1119 · Cited by 270 · see citing works
Self-citationMabuchi, T., Kitagawa, K., Kuwabara, K., 高沢健一郎, Ohtsuki, T., Xia, Z., Storm, D. R., Yanagihara, T., Hori, M., & Matsumoto, M. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-23-09204.2001 · Cited by 265 · see citing works
Krupp, J., Vissel, B., Thomas, C. G., Heinemann, S. F., & Westbrook, G. L. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-04-01165.1999 · Cited by 237 · see citing works
Fridovich, I. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-333640-8.50016-2 · Cited by 235 · see citing works
Peng, P. L., Zhong, X., Tu, W., Soundarapandian, M. M., Molner, P., Zhu, D., Lau, L. W., Liu, S., Liu, F., & Lu, Y. (2006) · Neuron · doi:10.1016/j.neuron.2006.01.025 · Cited by 232 · see citing works
Self-citationPetersen, J. D., Chen, X., Vinadé, L., Döṣemeci, A., Lisman, J. E., & Reese, T. S. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-35-11270.2003 · Cited by 211 · see citing works
Liu, S., Lau, L. W., Wei, J., Zhu, D., Zou, S., Sun, H.-S., Fu, Y., Liu, F., & Lu, Y. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.017 · Cited by 208 · see citing works
Self-citationBrickley, S. G., Misra, C., Mok, M. H. S., Mishina, M., & Cull-Candy, S. G. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-12-04958.2003 · Cited by 161 · see citing works
Shohat-Ophir, G., Spivak-Kroizman, T. R., Cohen, O., Bialik, S., Shani, G., Berissi, H., Eisenstein, M., & Kimchi, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105133200 · Cited by 153 · see citing works
Selective Activation Induced Cleavage of the NR2B Subunit by Calpain
Simpkins, K. L., Guttmann, R. P., Dong, Y., Chen, Z., Sokol, S. A., Neumar, R. W., & Lynch, D. R. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-36-11322.2003 · Cited by 146 · see citing works
Wang, J., Liu, S., Haditsch, U., Tu, W., Cochrane, K., Ahmadian, G., Tran, L., Paw, J., Wang, Y., Mansuy, I. M., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-03-00826.2003 · Cited by 137 · see citing works
Self-citationPoststroke neuronal rescue and synaptogenesis mediated in vivo by protein kinase C in adult brains
Sun, M., Hongpaisan, J., Nelson, T. J., & Alkon, D. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805952105 · Cited by 117 · see citing works
Ischemia-Induced Neuronal Damage: A Role for Calcium/Calmodulin-Dependent Protein Kinase II
Waxham, M. N., Grotta, J. C., Silva, A. J., Strong, R., & Aronowski, J. A. (1996) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199601000-00001 · Cited by 102 · see citing works
Marshall, J. J., Dolan, B. M., Garcia, E. P., Sathe, S., Tang, X., Mao, Z., & Blair, L. A. C. (2003) · Neuron · doi:10.1016/s0896-6273(03)00496-3 · Cited by 102 · see citing works
Regulation of c-Src Activity in Glutamate-induced Neurodegeneration
Khanna, S., Roy, S., Park, H., & Sen, C. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611269200 · Cited by 64 · see citing works
A Protein Kinase Associated with Apoptosis and Tumor Suppression
Velentza, A. V., Schumacher, A. M., Weiss, C. H., Egli, M., & Watterson, D. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104273200 · Cited by 63 · see citing works
Gardoni, F., Bellone, C., Viviani, B., Marinovich, M., Meli, E., Pellegrini-Giampietro, D. E., Cattabeni, F., & Luca, M. D. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02141.x · Cited by 50 · see citing works
Calcium/calmodulin-dependent protein kinase II activity in focal ischemia with reperfusion in rats.
Hanson, S., Grotta, J. C., Waxham, M. N., Aronowski, J. A., & Ostrow, P. T. (1994) · Stroke · doi:10.1161/01.str.25.2.466 · Cited by 46 · see citing works
Schumacher, A. M., Schavocky, J. P., Velentza, A. V., Mirzoeva, S., & Watterson, D. M. (2004) · Biochemistry · doi:10.1021/bi049589v · Cited by 46 · see citing works
Learning More About NMDA Receptor Regulation
Ghosh, A. (2002) · Science · doi:10.1126/science.1069391 · Cited by 34 · see citing works
Structure and enzymology of a death-associated protein kinase
Eldik, L. J. V. (2002) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(02)02049-7 · Cited by 13 · see citing works
Flagged first, then by citations
2 of the 54 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
NMDA 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
The Science of Stroke: Mechanisms in Search of Treatments
Moskowitz, M. A., Lo, E. H., & Iadecola, C. (2010) · Neuron · doi:10.1016/j.neuron.2010.07.002 · Cited by 1,930 · see citing works
Synaptic versus extrasynaptic NMDA receptor signalling: implications for neurodegenerative disorders
Hardingham, G. E., & Bading, H. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2911 · Cited by 1,644 · see citing works
Excitotoxicity and stroke: Identifying novel targets for neuroprotection
Lai, T. W., Zhang, S., & Wang, Y. T. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.11.006 · Cited by 1,106 · see citing works
Mechanisms of neuronal cell death in ischemic stroke and their therapeutic implications
Tuo, Q., Zhang, S., & Lei, P. (2021) · Medicinal Research Reviews · doi:10.1002/med.21817 · Cited by 747 · see citing works
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686 · see citing works
Neuronal injuries in cerebral infarction and ischemic stroke: From mechanisms to treatment (Review)
Zhao, Y., Zhang, X., Chen, X., & Wei, Y. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.5070 · Cited by 648 · see citing works
Pathogenic mechanisms following ischemic stroke
Khoshnam, S. E., Winlow, W., Farzaneh, M., Farbood, Y., & Moghaddam, H. F. (2017) · Neurological Sciences · doi:10.1007/s10072-017-2938-1 · Cited by 618 · see citing works
Extrasynaptic NMDA Receptor Involvement in Central Nervous System Disorders
Parsons, M. P., & Raymond, L. A. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.030 · Cited by 555 · see citing works
Synapses and Alzheimer's Disease
Sheng, M., Sabatini, B. L., & Sudhof, T. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005777 · Cited by 436 · see citing works
Excitotoxicity, calcium and mitochondria: a triad in synaptic neurodegeneration
Verma, M., Lizama, B. N., & Chu, C. T. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-021-00278-7 · Cited by 451 · see citing works
Cell Death Pathways in Ischemic Stroke and Targeted Pharmacotherapy
Datta, A., Sarmah, D., Mounica, L., Kaur, H., Kesharwani, R., Verma, G., Veeresh, P., Kotian, V., Kalia, K., Borah, A., et al. (2020) · Translational Stroke Research · doi:10.1007/s12975-020-00806-z · Cited by 328 · see citing works
Raymond, L. A., André, V. M., Cepeda, C., Gladding, C. M., Milnerwood, A. J., & Levine, M. S. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.08.052 · Cited by 319 · see citing works
Microglial displacement of inhibitory synapses provides neuroprotection in the adult brain
Chen, Z., Jalabi, W., Hu, W., Park, H.-J., Gale, J. T., Kidd, G. J., Bernatowicz, R., Gossman, Z. C., Chen, J. T., Dutta, R., et al. (2014) · Nature Communications · doi:10.1038/ncomms5486 · Cited by 319 · see citing works
Targeting NMDA receptors in stroke: new hope in neuroprotection
Wu, Q. J., & Tymianski, M. (2018) · Molecular Brain · doi:10.1186/s13041-018-0357-8 · Cited by 320 · see citing works
NMDA receptors in nervous system diseases
Zhou, Q., & Sheng, M. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.03.030 · Cited by 293 · see citing works
METTL3-mediated m6A modification is required for cerebellar development
Wang, C.-X., Cui, G.-S., Liu, X., Xu, K., Wang, M., Zhang, X.-X., Jiang, L.-Y., Li, A., Yang, Y., Lai, W.-Y., et al. (2018) · PLOS Biology · doi:10.1371/journal.pbio.2004880 · Cited by 291 · see citing works
Self-citationNeuronal Death Mechanisms and Therapeutic Strategy in Ischemic Stroke
Mao, R., Zong, N., Hu, Y., Chen, Y., & Xu, Y. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00859-0 · Cited by 289 · see citing works
Self-citationInfluence of GluN2 subunit identity on NMDA receptor function
Wyllie, D. J. A., Livesey, M. R., & Hardingham, G. E. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.01.016 · Cited by 260 · see citing works
Welsbie, D. S., Yang, Z., Ge, Y., Mitchell, K. L., Zhou, X., Martin, S. E., Berlinicke, C. A., Hackler, L., Fuller, J., Fu, J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211284110 · Cited by 247 · see citing works
Glutamate excitotoxicity: Potential therapeutic target for ischemic stroke.
Shen, Z., Xiang, M., Chen, C., Ding, F., Wang, Y., Shang, C., Xin, L., Zhang, Y., & Cui, X.-N. (2022) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2022.113125 · Cited by 211 · see citing works
Molecular mechanisms of ischemia and glutamate excitotoxicity
Neves, D., Salazar, I. L., Almeida, R. D., & Silva, R. M. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121814 · Cited by 219 · see citing works
Rapid and reversible knockdown of endogenous proteins by peptide-directed lysosomal degradation
Fan, X., Wu, J., Lu, J., Wang, J., & Wang, Y. T. (2014) · Nature Neuroscience · doi:10.1038/nn.3637 · Cited by 213 · see citing works
Death Associated Protein Kinase 1 (DAPK1): A Regulator of Apoptosis and Autophagy
Singh, P., Ravanan, P., & Talwar, P. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00046 · Cited by 215 · see citing works
Neuronal networks provide rapid neuroprotection against spreading toxicity
Samson, A. J., Robertson, G. R., Zagnoni, M., & Connolly, C. N. (2016) · Scientific Reports · doi:10.1038/srep33746 · Cited by 218 · see citing works
Mechanisms of specificity in neuronal activity-regulated gene transcription
Lyons, M. R., & West, A. E. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.05.003 · Cited by 199 · see citing works
Excitotoxicity: Still Hammering the Ischemic Brain in 2020
Choi, D. W. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.579953 · Cited by 198 · see citing works
Mechanisms underlying NMDA receptor synaptic/extrasynaptic distribution and function
Gladding, C. M., & Raymond, L. A. (2011) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2011.05.001 · Cited by 197 · see citing works
Neuroprotection in stroke: the importance of collaboration and reproducibility
Neuhaus, A. A., Couch, Y., Hadley, G., & Buchan, A. M. (2017) · Brain · doi:10.1093/brain/awx126 · Cited by 193 · see citing works
Karpova, A., Mikhaylova, M., Bera, S., Bär, J., Reddy, P. P., Behnisch, T., Rankovic, V., Spilker, C., Bethge, P., Şahin, J., et al. (2013) · Cell · doi:10.1016/j.cell.2013.02.002 · Cited by 194 · see citing works
Mitochondria: hub of injury responses in the developing brain
Hagberg, H., Mallard, C. E., Rousset, C. I., & Thornton, C. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70261-8 · Cited by 194 · see citing works
Lee, T. H., Chen, C.-H., Suizu, F., Huang, P., Schiene-Fischer, C., Daum, S., Zhang, Y. J., Goate, A., Chen, R.-H., Zhou, X. Z., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.005 · Cited by 183 · see citing works
Yang, Y., Shu, X., Liu, D., Shang, Y., Wu, Y., Pei, L., Xu, X., Tian, Q., Zhang, J., Qian, K., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.02.003 · Cited by 178 · see citing works
Self-citationStroke intervention pathways: NMDA receptors and beyond
Lai, T. W., Shyu, W., & Wang, Y. T. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.12.008 · Cited by 177 · see citing works
Hackos, D. H., Lupardus, P. J., Grand, T., Chen, Y., Wang, T.-M., Reynen, P. H., Gustafson, A. E., Wallweber, H. J. A., Volgraf, M., Sellers, B. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.016 · Cited by 174 · see citing works
Self-citationThe Subtype of GluN2 C-terminal Domain Determines the Response to Excitotoxic Insults
Martel, M., Ryan, T. J., Bell, K. F. S., Fowler, J. H., McMahon, A., Al-Mubarak, B. R., Komiyama, N. H., Horsburgh, K. J., Kind, P. C., Grant, S. G. N., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.021 · Cited by 176 · see citing works
Kocsis, B. (2012) · Biological Psychiatry · doi:10.1016/j.biopsych.2011.10.002 · Cited by 159 · see citing works
Liu, S., Zhang, N., Guo, Y., Zhao, R., Shi, T., Feng, S., Wang, S.-Q., Yang, Q., Li, X., Wu, Y., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5828-11.2012 · Cited by 161 · see citing works
Self-citationBading, H. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20161673 · Cited by 156 · see citing works
Emerging Roles of microRNAs in Ischemic Stroke: As Possible Therapeutic Agents
Khoshnam, S. E., Winlow, W., Farbood, Y., Moghaddam, H. F., & Farzaneh, M. (2017) · Journal of Stroke · doi:10.5853/jos.2016.01368 · Cited by 156 · see citing works
Regulation of NMDA glutamate receptor functions by the GluN2 subunits
Vieira, M., Yong, X. L. H., Roche, K. W., & Anggono, V. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14970 · Cited by 151 · see citing works
“DAPK1 directly interacts with the GluN2B CTD in a region that overlaps with the CaMKII-binding site (Tu et al., 2010).”
BackgroundRole of NMDA Receptor-Mediated Glutamatergic Signaling in Chronic and Acute Neuropathologies
Carvajal, F. J., Mattison, H. A., & Cerpa, W. F. (2016) · Neural Plasticity · doi:10.1155/2016/2701526 · Cited by 150 · see citing works
Zhou, X., Ding, Q., Chen, Z., Yun, H., & Wang, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482000 · Cited by 148 · see citing works
Coultrap, S. J., Vest, R. S., Ashpole, N. M., Hudmon, A., & Bayer, K. U. (2011) · Acta Pharmacologica Sinica · doi:10.1038/aps.2011.68 · Cited by 145 · see citing works
An Increase in Synaptic NMDA Receptors in the Insular Cortex Contributes to Neuropathic Pain
Qiu, S., Chen, T., Koga, K., Guo, Y., Xu, H., Song, Q., Wang, J., Descalzi, G., Kaang, B., Luo, J., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2003778 · Cited by 147 · see citing works
Yang, X., Yao, C., Tian, T., Li, X., Yan, H., Wu, J., Li, H., Pei, L., Liu, D., Tian, Q., et al. (2018) · Molecular Psychiatry · doi:10.1038/mp.2016.151 · Cited by 136 · see citing works
Self-citationLong noncoding RNA MEG3 activation of p53 mediates ischemic neuronal death in stroke
Yan, H., Yuan, J., Gao, L., Rao, J., & Hu, J. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.09.017 · Cited by 142 · see citing works
Emerging mechanisms of disrupted cellular signaling in brain ischemia
Tymianski, M. (2011) · Nature Neuroscience · doi:10.1038/nn.2951 · Cited by 131 · see citing works
Kaufman, A. M., Milnerwood, A. J., Sepers, M. D., Coquinco, A., She, K., Wang, L., Lee, H., Craig, A. M., Cynader, M. S., & Raymond, L. A. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4129-11.2012 · Cited by 131 · see citing works
Extrasynaptic glutamate release through cystine/glutamate antiporter contributes to ischemic damage
Soria, F. N., Pérez‐Samartín, A., Martín, A., Gona, K. B., Llop, J., Szczupak, B., Chara, J. C., Matute, C., & Domercq, M. (2014) · Journal of Clinical Investigation · doi:10.1172/jci71886 · Cited by 129 · see citing works
Nicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
“Phosphorylation of S1303 in heterologous cells enhances NMDAR current (127, 128) and reduces desensitization of GluN2B-containing receptors (129).”
BackgroundLuo, Y., Zhou, Y.-Q., Xiao, W., Liang, Z., Dai, J., Weng, X., & Wu, X. (2014) · Brain Research · doi:10.1016/j.brainres.2014.12.005 · Cited by 125 · see citing works
Su, Y., Deng, M., Xiong, W., Xie, A., Guo, J., Liang, Z., Hu, B., Chen, J., Zhu, X., Man, H., et al. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.12.008 · Cited by 123 · see citing works
Self-citationEmerging Therapies in Traumatic Brain Injury
Jackson, T. C., Ferguson, N. M., Carlson, S. W., Simon, D. W., Brockman, E., Ji, J., Bayır, H., Poloyac, S. M., Wagner, A. K., Kline, A. E., et al. (2015) · Seminars in Neurology · doi:10.1055/s-0035-1544237 · Cited by 123 · see citing works
DAPK1–p53 Interaction Converges Necrotic and Apoptotic Pathways of Ischemic Neuronal Death
Pei, L., Shang, Y., Jin, H., Wang, S., Wei, N., Yan, H., Wu, Y., Yao, C., Wang, X., Zhu, L., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5119-13.2014 · Cited by 122 · see citing works
Self-citationZhu, H., Yan, H., Tang, N., Li, X., Pang, P., Li, H., Chen, W., Guo, Y. A., Shu, S., Cai, Y., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01943-0 · Cited by 119 · see citing works
Self-citationThe DAPK family: a structure–function analysis
Shiloh, R., Bialik, S., & Kimchi, A. (2014) · Apoptosis · doi:10.1007/s10495-013-0924-5 · Cited by 112 · 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
Báez, M. V., Cercato, M. C., & Jerusalinsky, D. A. (2018) · Neural Plasticity · doi:10.1155/2018/5093048 · Cited by 117 · see citing works
Death‐associated protein kinase (DAPK) family modulators: Current and future therapeutic outcomes
Farag, A. K., & Roh, E. J. (2018) · Medicinal Research Reviews · doi:10.1002/med.21518 · Cited by 115 · see citing works
The Role of Excitotoxic Programmed Necrosis in Acute Brain Injury
Fujikawa, D. G. (2015) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2015.03.004 · Cited by 110 · see citing works
Perinatal brain damage: The term infant
Hagberg, H., Edwards, A. D., & Groenendaal, F. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.09.011 · Cited by 109 · see citing works
Misplaced NMDA receptors in epileptogenesis contribute to excitotoxicity
Frasca, A., Aalbers, M. W., Frigerio, F., Fiordaliso, F., Salio, M., Gobbi, M., Cagnotto, A., Gardoni, F., Battaglia, G. S., Hoogland, G., et al. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.04.024 · Cited by 104 · see citing works
Uncoupling DAPK1 from NMDA receptor GluN2B subunit exerts rapid antidepressant-like effects
Li, S.-X., Han, Y., Xu, L., Yuan, K., Zhang, R.-X., Sun, C.-Y., Xu, D.-F., Yuan, M., Deng, J.-H., Meng, S.-Q., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.85 · Cited by 100 · see citing works
Verma, M., Wills, Z. P., & Chu, C. T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00523 · Cited by 98 · see citing works
Kim, B. M., You, M.-H., Chen, C.-H., Lee, S., Hong, Y., Hong, Y., Kimchi, A., Zhou, X. Z., & Lee, T. H. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.216 · Cited by 98 · see citing works
Imbalance of neurotrophin receptor isoforms TrkB-FL/TrkB-T1 induces neuronal death in excitotoxicity
Vidaurre, Ó. G., Gascón, S., Deogracias, R., Sobrado, M., Cuadrado, E., Montaner, J., Rodríguez‐Peña, A., & Díaz‐Guerra, M. (2012) · Cell Death and Disease · doi:10.1038/cddis.2011.143 · Cited by 98 · see citing works
Mira, R. G., & Cerpa, W. F. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00924-0 · Cited by 96 · see citing works
NMDARs in Cell Survival and Death: Implications in Stroke Pathogenesis and Treatment
Ge, Y., Chen, W., Axerio-Cilies, P., & Wang, Y. T. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.03.001 · Cited by 96 · see citing works
IQGAP1 Regulates NR2A Signaling, Spine Density, and Cognitive Processes
Gao, C., Frausto, S. F., Guedea, A. L., Tronson, N. C., Jovasevic, V., Leaderbrand, K., Corcoran, K. A., Guzmán, Y. F., Swanson, G. T., & Radulović, J. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.1300-11.2011 · Cited by 96 · see citing works
Frega, M., Pasquale, V., Tedesco, M., Marcoli, M., Contestabile, A., Nanni, M., Bonzano, L., Maura, G., & Chiappalone, M. (2011) · Neurotoxicology and Teratology · doi:10.1016/j.ntt.2011.08.001 · Cited by 93 · see citing works
MicroRNA-9 Mediates the Cell Apoptosis by Targeting Bcl2l11 in Ischemic Stroke
Wei, N., Xiao, L., Xue, R., Zhang, D., Zhou, J., Ren, H., Guo, S., & Xu, J. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9605-4 · Cited by 93 · see citing works
Wei, R., Zhang, L., Hu, W., Wu, J., & Zhang, W. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.01.009 · Cited by 93 · see citing works
Self-citationFan, J., Gladding, C. M., Wang, L., Zhang, L. Y. J., Kaufman, A. M., Milnerwood, A. J., & Raymond, L. A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.019 · Cited by 94 · see citing works
Poly-Arginine and Arginine-Rich Peptides are Neuroprotective in Stroke Models
Meloni, B. P., Brookes, L. M., Clark, V. W., Cross, J. L., Edwards, A. B., Anderton, R. S., Hopkins, R. M., Hoffmann, K., & Knuckey, N. W. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.11 · Cited by 91 · see citing works
Benarroch, E. E. (2011) · Neurology · doi:10.1212/wnl.0b013e31821b7cc9 · Cited by 90 · see citing works
Critical Role of Increased PTEN Nuclear Translocation in Excitotoxic and Ischemic Neuronal Injuries
Zhang, S., Taghibiglou, C., Girling, K., Dong, Z., Lin, S., Lee, W., Shyu, W., & Wang, Y. T. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5661-12.2013 · Cited by 88 · see citing works
DAPK1 Mediates LTD by Making CaMKII/GluN2B Binding LTP Specific
Goodell, D. J., Zaegel, V., Coultrap, S. J., Hell, J. W., & Bayer, K. U. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.068 · Cited by 88 · see citing works
Kim, N., Chen, D., Zhou, X. Z., & Lee, T. H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133131 · Cited by 87 · see citing works
Meloni, B. P., Milani, D., Edwards, A. B., Anderton, R. S., Doig, R. O., Fitzgerald, M., Palmer, T. N., & Knuckey, N. W. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.06.002 · Cited by 87 · see citing works
Genomic and epigenetic profiles of gastric cancer: Potential diagnostic and therapeutic applications
Yamashita, K., Sakuramoto, S., & Watanabe, M. (2010) · Surgery Today · doi:10.1007/s00595-010-4370-5 · Cited by 86 · see citing works
Discovery and development of NA-1 for the treatment of acute ischemic stroke
Ballarin, B., & Tymianski, M. (2018) · Acta Pharmacologica Sinica · doi:10.1038/aps.2018.5 · Cited by 86 · see citing works
Meloni, B. P., Mastaglia, F. L., & Knuckey, N. W. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00108 · Cited by 85 · see citing works
Li, X., Chen, W., Pan, K., Li, H., Pang, P., Guo, Y., Shu, S., Cai, Y., Pei, L., Liu, D., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0207-0 · Cited by 83 · see citing works
Self-citationPaul, S., & Connor, J. A. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06835.x · Cited by 85 · see citing works
DAPK1 Signaling Pathways in Stroke: from Mechanisms to Therapies
Wang, S., Shi, X.-D., Li, H., Pang, P., Pei, L., Shen, H., & Lu, Y. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0008-y · Cited by 83 · see citing works
Self-citationDAPK activates MARK1/2 to regulate microtubule assembly, neuronal differentiation, and tau toxicity
Wu, P.-R., Tsai, P.-I., Chen, G., Chou, H.-J., Huang, Y.-P., Chen, Y. H., Lin, M.-Y., Kimchi, A., Chien, C.-T., & Chen, R.-H. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.2 · Cited by 82 · see citing works
Self-citationYokoyama, T., Kosaka, Y., & Mizuguchi, M. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00893 · Cited by 83 · see citing works
The Emergence of NMDA Receptor Metabotropic Function: Insights from Imaging
Doré, K., Aow, J., & Malinow, R. (2016) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2016.00020 · Cited by 80 · see citing works
Wang, J., Liu, F., Yang, F., Wang, Y., Qi, X., Li, Y., Hu, Q., Zhu, M. X., & Xu, T. (2020) · Nature Communications · doi:10.1038/s41467-019-13873-0 · Cited by 81 · see citing works
DeGregorio‐Rocasolano, N., Martı́, O., Ponce, J., Castelló‐Ruiz, M., Millán, M., Guirao, V., García‐Yébenes, I., Salom, J. B., Ramos‐Cabrer, P., Alborch, E., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.026 · Cited by 80 · see citing works
Bhattacharya, S., Khatri, A., Swanger, S. A., DiRaddo, J. O., Yi, F., Hansen, K. B., Yuan, H., & Traynelis, S. F. (2018) · Neuron · doi:10.1016/j.neuron.2018.06.010 · Cited by 77 · see citing works
Wang, P., Cui, Y., Liu, Y., Li, Z., Bai, H., Zhao, Y., & Chang, Y. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102475 · Cited by 77 · see citing works
Modes of Neuronal Calcium Entry and Homeostasis following Cerebral Ischemia
Cross, J. L., Meloni, B. P., Bakker, A. J., Lee, S., & Knuckey, N. (2010) · Stroke Research and Treatment · doi:10.4061/2010/316862 · Cited by 77 · see citing works
Balu, D. T., Pantazopoulos, H., Huang, C. C., Muszynski, K., Harvey, T. L., Uno, Y., Rorabaugh, J. M., Galloway, C. R., Botz-Zapp, C. A., Berretta, S., et al. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104511 · Cited by 77 · see citing works
Levin‐Salomon, V., Bialik, S., & Kimchi, A. (2013) · APOPTOSIS · doi:10.1007/s10495-013-0918-3 · Cited by 76 · see citing works
Insights into the neuropathology of cerebral ischemia and its mechanisms
Ahad, M. A., Kumaran, K. R., Tiang, N., Mansor, N. I., Effendy, M. A., Damodaran, T. K., Lingam, K., Wahab, H. A., Nordin, N., Liao, P. H., et al. (2020) · Reviews in the Neurosciences · doi:10.1515/revneuro-2019-0099 · Cited by 75 · see citing works
Wang, J., Li, X., Song, Y., Su, Q., Xiaohalati, X., Yang, W., Xu, L., Cai, B., Wang, G., Wang, Z., et al. (2020) · Bioactive Materials · doi:10.1016/j.bioactmat.2020.12.017 · Cited by 74 · see citing works
A Novel Mechanism of Spine Damages in Stroke via DAPK1 and Tau
Pei, L., Wang, S., Jin, H., Bi, L., Wei, N., Yan, H., Yang, X., Yao, C., Xu, M., Shu, S., et al. (2015) · Cerebral Cortex · doi:10.1093/cercor/bhv096 · Cited by 74 · see citing works
Self-citation
- Authors
- Tu, W., Xu, X., Peng, L., Zhong, X., Zhang, W., Soundarapandian, M. M., Belal, C., Wang, M., Jia, N., Zhang, W., Lew, F., Chan, S. L., Chen, Y., & Lu, Y.
- Affiliations
- University of Central Florida (US)
- Louisiana State University (US)
- Wright State University (US)
- Corresponding author
- Lu, Youming
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 140
- Issue
- 2
- Pages
- 222-234
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2820131
- OpenAlex
- W2112215250
- Cited by
- 493
- References
- 54
- Citations by year
- 2026: 15 · 2025: 27 · 2024: 24 · 2023: 37 · 2022: 28 · 2021: 38 · 2020: 35 · 2019: 24 · 2018: 35 · 2017: 45 · 2016: 35 · 2015: 20 · 2014: 35 · 2013: 34 · 2012: 21
- FWCI
- 12.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Commons - East Tennessee State University (East Tennessee State University) (submittedVersion)
- Journal of International Crisis and Risk Communication Research (submittedVersion)
- Funders
- National Institute on Aging (R01AG033282YL, R01AG033282)
- National Institute of Neurological Disorders and Stroke (R01NS5051383YL, R01NS051383)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Epidemiology › Acute Ischemic Stroke Management
- Keywords
- DAPK1, NMDA receptor, NR2B subunit, cerebral ischemia, stroke, extrasynaptic NMDA receptors, neuronal cell death, calcium influx, protein phosphorylation, neuroprotection
- MeSH terms
- Animals, Brain, Brain Ischemia, Neurons, Peptides, Recombinant Proteins, Receptors, N-Methyl-D-Aspartate, Cell Death, Calcium-Calmodulin-Dependent Protein Kinases, Stroke, Apoptosis Regulatory Proteins, Mice, tat Gene Products, Human Immunodeficiency Virus, Death-Associated Protein Kinases
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