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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.
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“Phosphorylation of S1303 in heterologous cells enhances NMDAR current (127, 128)”
From Synaptic memory and CaMKII (2023) · cites this paper as [128]
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“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]
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N-Methyl-D-Aspartate Receptor Signaling-Protein Kinases Crosstalk in Cerebral Ischemia
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“kinase 1 uncoupling agents Early research indicated that cerebral ischemia could induce the recruitment of death- associated protein kinase 1 (DAPK1) into GluN2B- containing NMDA receptors via binding to the GluN2B Cterminal tail (Tu et al., 2010).”
BackgroundJiang, W., Zhang, P., Yang, P. H., Kang, N., Liu, J., Aihemaiti, Y., & Tu, H. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100222 · Cited by 17
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“Finally, Tat-NR2B that can block the binding between DAPK1 and NR2B was used in TBI mice, and the results indicate that TBI-induced dysfunction was mitigated while normal synapse function was not affected.”
BackgroundMethodResultInfluentialLiao, W., Wen, Y., Yang, S., Duan, Y., & Liu, Z. (2023) · Medicine · doi:10.1097/md.0000000000035490 · Cited by 15
Roles of microRNA-124 in traumatic brain injury: a comprehensive review
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Pituitary Adenylate Cyclase-Activating Polypeptide: A Potent Therapeutic Agent in Oxidative Stress
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“NMDA receptors that contain GluN2B subunits induce apoptosis and reduce CREB pathways via intracellular signaling pathways and caspase 3 activity [58,59].”
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“Furthermore, suppressing DAPK1 attenuates the GluN2B-containing NMDAR-mediated Ca2+ increase and protects neurons from excitotoxic damage [39,73].”
BackgroundDifferential roles of GluN2A- and GluN2B-containing NMDA receptors in neuronal survival and death.
Lujan, B., Liu, X., & Wan, Q. (2012) · PubMed Central · Cited by 15
Wang, Y., Yang, Y., Chen, L., Xiong, W., Song, L., Li, B., Zhou, T., Pei, L., Shiying, Y., Yao, S., et al. (2020) · Anesthesiology · doi:10.1097/aln.0000000000003464 · Cited by 15
“Death-associated protein kinase 1 (DAPK1) is a proapoptotic Ca/calmodulin–regulated serine/threonine kinase involving in the regulation of both apoptosis and necrosis.(7,8) It was originally described as a positive regulator of interferon-γ–mediated cell death.”
BackgroundTargeting the dysfunction of glutamate receptors for the development of novel antidepressants
Xia, C., He, J., Du, L., Yan, Y., Lian, W., Xu, J., & Zhang, W. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107875 · Cited by 15
Self-citationToll-Like Receptor 4 Signaling in Neurons Mediates Cerebral Ischemia/Reperfusion Injury
Liu, L., Xu, T., Zhao, Z., Zhang, N., Li, J., & Chen, D. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03122-9 · Cited by 14
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MethodRapamycin Alleviates Neuronal Injury and Modulates Microglial Activation After Cerebral Ischemia
Zhang, Y., Li, D., Gao, H., Zhao, H., Zhang, S., & Li, T. (2024) · Molecular Neurobiology · doi:10.1007/s12035-023-03904-9 · Cited by 13
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miR-124 Alleviates Ischemic Stroke-Induced Neuronal Death by Targeting DAPK1 in Mice
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The α2δ-1-NMDA receptor complex and its potential as a therapeutic target for ischemic stroke
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BackgroundDu, Y., Gao, F., Sun, H., Wu, C., Zhu, G., & Zhu, M. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115855 · Cited by 14
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GluN2B S1303 phosphorylation by CaMKII or DAPK1: No indication for involvement in ischemia or LTP
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Regulation of DAPK1 by Natural Products: An Important Target in Treatment of Stroke
Noori, T., Shirooie, S., Sureda, A., Sobarzo‐Sánchez, E., Dehpour, A. R., Saldías, M., & Akkol, E. K. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03628-7 · Cited by 13
“In addition, the ability of DAPK1 to induce neuronal cell death associated with ceramide-induced apoptosis, ischemia, and glutamate toxicity has been demonstrated [44].”
BackgroundGluA1 Degradation by Autophagy Contributes to Circadian Rhythm Effects on Cerebral Ischemia Injury
Lu, H., Wang, Y., Fan, H., Wang, Y., Fan, S., Hu, S., Shen, H., Li, H., Xue, Q., Ni, J., et al. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1914-22.2023 · Cited by 15
Blockade and knock-out of CALHM1 channels attenuate ischemic brain damage
Cisneros-Mejorado, A., Gottlieb, M., Ruiz, A., Chara, J. C., Pérez‐Samartín, A., Marambaud, P., & Matute, C. (2017) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x17713587 · Cited by 13
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“For example, the phosphorylation of NR2B at S1303 site can increase the opening rate of NMDAR and aggravate the neuronal death caused by ischemia (Tu et al., 2010).”
BackgroundLarsen, M. E., Buonarati, O. R., Qian, H., Hell, J. W., & Bayer, K. U. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104706 · Cited by 13
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“This is consistent with previous findings that showed synaptic CaMKII accumulation after cLTD stimuli is normally suppressed by synaptic DAPK1.”
BackgroundInfluentialWon, J., Lee, S., Khan, Z. A., Choi, J., Lee, T. H., & Hong, Y. (2023) · Brain Research · doi:10.1016/j.brainres.2023.148588 · Cited by 12
Yan, J., & Bading, H. (2023) · Pharmaceuticals · doi:10.3390/ph16081085 · Cited by 12
“Similar to PSD95, the interruption of the GluN2B-DAPK1 interaction via an interfering peptide or via the genetic deletion of DAPK1 provided protection against brain damage in ischemic stroke [101].”
BackgroundInfluentialCausal Association of Iron Status With Functional Outcome After Ischemic Stroke
He, Q., Wang, W., Xu, D., Xiong, Y., You, C., Tao, C., & Ma, L. (2023) · Stroke · doi:10.1161/strokeaha.123.044930 · Cited by 12
“43 ATf could reduce the Tf (transferrin)/TfR-mediated reactive oxygen species-4-hydroxynonenal and remit brain damage.”
BackgroundDevelopment of NMDAR Antagonists with Reduced Neurotoxic Side Effects: a Study on GK11
Vandame, D., Ulmann, L., Teigell, M., Prieto-Cappellini, M., Vignon, J., Privat, A., Perez‐Polo, R. J., Nešić, O., & Hirbec, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081004 · Cited by 12
“On the other hand, it has been shown that certain prodeath pathways are preferentially activated by extrasynaptic NMDARs [11] [12].”
BackgroundWang, X., He, X., Li, T., Shu, Y., Qi, S., & Luan, G. (2017) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2017.5311 · Cited by 12
Sprouty1 regulates neuritogenesis and survival of cortical neurons
Gu, X., Su, X., Jia, C., Lin, L., Liu, S., Zhang, P., Wang, X., & Jiang, X. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.27949 · Cited by 10
Zhang, Z., Wang, Y., Yan, S., Du, F., & Yan, S. S. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.07.019 · Cited by 12
“More specifically, overactivation of the N-methyl D- aspartate receptor subunit 2B (NR2B) causes intracellular Ca2+ overload and recruits several molecules, such as phosphatase and tensin homologs deleted on chromosome TEN (PTEN) (Zhang et al., 2013) and death-associated protein kinase 1 (DAPK1) (Tu et al., 2010) that…”
BackgroundInfluentialLu, K. P., & Zhou, X. Z. (2024) · Science Signaling · doi:10.1126/scisignal.adi8743 · Cited by 12
“Because DAPK1 is activated in stroke ( 254 , 255 ), these results suggest that stroke induces cis phospho-Thr 231 tau through the DAPK1-mediated inhibition of Pin1, thereby driving progressive neurode-generation in VCID ( 44 ).”
BackgroundDeGregorio‐Rocasolano, N., Guirao, V., Ponce, J., Melià-Sorolla, M., Aliena‐Valero, A., García-Serran, A., Salom, J. B., Dávalos, A., Martı́, O., & Gasull, T. (2020) · Antioxidants · doi:10.3390/antiox9121202 · Cited by 11
“As direct antagonism of NMDAR has been revealed to be poorly tolerated in the clinical arena so far, other therapeutic strategies have been postulated to prevent the association of the NMDAR with intracellular protein signaling transducers networking for excitotoxicity.”
BackgroundMethodInfluentialYou, M., Lee, W. K., Jin, M., Song, D. E., Cheng, S.-Y., Kim, T. Y., Kim, W. B., Jeon, M. J., & Kim, W. G. (2021) · Cells · doi:10.3390/cells10112994 · Cited by 11
“DAPK1 plays an important role in apoptosis, autophagy, the immune response, ischemic injury of the brain, and neurodegenerative disease [8,9].”
BackgroundLi, R., Zhi, S., Lan, G., Chen, X., Zheng, X., Hu, L., Wang, L., Zhang, T., Lee, T. H., Rao, S., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076542 · Cited by 11
“In addition, DAPK1 modulates brain damage via the NMDA receptor or alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptor by ischemia and inhibition of DAPK1 activity, which contributes to neuroprotective effects in a mouse model of ischemia [15,28,36,37].”
BackgroundThe Good and Bad Sides of NAAG
Khacho, P., Wang, B., & Bergeron, R. (2016) · Advances in pharmacology · doi:10.1016/bs.apha.2016.01.003 · Cited by 10
“Moreover, preventing the interaction between DAPK1 and NMDA receptors protected neurons against in vitro oxygen-glucose deprivation and in vivo ischemic injury (Tu et al., 2010).”
InfluentialLu, F., Shao, G., Wang, Y., Guan, S., Burlingame, A. L., Liu, X., Liang, X., Knox, R. N., Ferriero, D. M., & Jiang, X. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.10.005 · Cited by 11
“Besides the kinases that were validated by co-IP (CaMKIIα and β, PKCα, β and γ, p38α MAP kinase and Src kinase), reported GluN2B interactions in adult stroke or transient ischemia model, such as with death-associated protein kinase 1 (DAPK1) (Tu et al., 2010), with phosphoinositide 3- kinase (PI3K) subunit p85 (Takagi…”
Williams, S., Hossain, M., Mishra, S., Gonzalez-Martinez, J. A., Najm, I., & Ghosh, C. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1415-z · Cited by 11
“Similarly, oxygen-glucose deprivation can increase the association of DAPK with N-methyl-D-aspartate receptors, which amplifies their activity and induces toxic calcium influx into neuronal cells [40].”
BackgroundTRPC6 expression in neurons is differentially regulated by NR2A‐ and NR2B‐containing NMDA receptors
Qu, Z., Wang, Y., Li, X., Wu, L., & Wang, Y. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14215 · Cited by 11
Future Perspectives of NMDAR in CNS Disorders
Capó, T., Rebassa, J. B., Raïch, I., Lillo, J., Badia, P., Navarro, G., & Reyes‐Resina, I. (2025) · Molecules · doi:10.3390/molecules30040877 · Cited by 12
“The final goal of these emerging therapeutics is to selectively enhance neuroprotective signaling complex activity [139,140] and/or inhibit neurodegenerative signaling complex pathways [141,142] without affecting other NMDAR-associated signaling processes.”
Lee, G. S., Zhang, J., Wu, Y., & Zhou, Y. (2021) · PLoS ONE · doi:10.1371/journal.pone.0261791 · Cited by 11
COVID-19-induced neurological symptoms: focus on the role of metal ions
Zhang, Y., Ren, K., Luo, X., & Peng, J. (2023) · Inflammopharmacology · doi:10.1007/s10787-023-01176-2 · Cited by 10
Li, H., Luo, X.-B., Xu, Y., & Hou, X. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190207 · Cited by 10
“Although the roles of NMDA receptor GluN2A and GluN2B subunits in neuronal signaling remain to be inconsistent [45–47], both GluN2A and GluN2B subunits contribute to A (cid:2) - or brain ischemia-induced excitotoxicity [20, 43, 48].”
Discovery and Optimization of Isoliquiritigenin as a Death-Associated Protein Kinase 1 Inhibitor
Yokoyama, T., Hisatomi, K., Oshima, S., Tanaka, I., Okada, T., & Toyooka, N. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116836 · Cited by 9
Mechanisms of Transsynaptic Degeneration in the Aging Brain
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“3) [67, 68].”
BackgroundMolecular level activation insights from a NR2A/NR2B agonist
Tou, W. I., Chang, S.-S., Wu, D., Lai, T. W., Wang, Y. T., Hsu, C. Y., & Chen, C. Y. (2013) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2013.787371 · Cited by 9
“In contrast, the NR2B receptors are the primary cause of neuronal death following cerebral ischemia (Tu et al., 2010; Zhou et al., 2010), with NR2B antagonism the efficacy of NMDAR blockers in experimental studies.”
BackgroundInfluentialNeuroprotective strategies for NMDAR-mediated excitotoxicity in Huntington’s Disease
Girling, K., & Wang, Y. T. (2016) · Frontiers in Biology · doi:10.1007/s11515-016-1425-z · Cited by 9
E2-25K SUMOylation inhibits proteasome for cell death during cerebral ischemia/reperfusion
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“Tu et al. 36 reported that DAPK1 directly bound to N-methyl-D-aspartate (NMDA) receptor NR2B subunits at Ser-1303, resulting in increased NR1/NR2B receptor channel conductance and calcium influx in a stroke mouse model.”
BackgroundBueschke, N., Amaral‐Silva, L., Hu, M., Alvarez, A., & Santin, J. M. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0502-23.2024 · Cited by 10
Gao, X., Wang, H., Pollok, K. E., Chen, J., & Cohen‐Gadol, A. (2015) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2015.03.044 · Cited by 9
“Active DAPK1 is recruited to bind and phosphorylate NR2B at S1303 [15].”
BackgroundInfluentialWang, K., Tan, X., Ding, K.-M., Feng, X.-Z., Zhao, Y.-Y., Zhu, W., Li, G.-H., & Li, S. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107236 · Cited by 8
Mechanism of DAPK1 for Regulating Cancer Stem Cells in Thyroid Cancer
You, M. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46070422 · Cited by 8
“DAPK1 can directly phosphorylate Ser350 in NDRG2, and the NDRG2 domain can specifically bind to DAPK1 through the ROC-COR domain [12].”
BackgroundInfluentialLin, J., Callender, J. A., Mayfield, J. E., McClatchy, D. B., Ojeda-Juárez, D., Pourhamzeh, M., Soldau, K., Kurt, T. D., Danque, G. A., Khuu, H., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci186432 · Cited by 8
“GluN2B is phosphorylated at S1303 by the CaM kinase family members CaMKII or death-associated protein kinase 1 (DAPK1) (45, 47–49), or by PKC (50).”
InfluentialThe ERK signaling pathway in cerebral ischemic stroke: Mechanism and therapeutic significance
Yin, X., Chang, J., Yang, L., Jia, L.-Y., Han, J., Chen, L., Cao, J., Chen, X., Xie, N., Lin, Y., et al. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2026.119058 · Cited by 8
Kim, D., Morikawa, S., Nakagawa, T., Okano, H., & Kase, Y. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115177 · Cited by 8
“( Tu et al., 2010) Here, we have summarized the development of therapies targeting DAPK1 (Table 1).”
ITPRIP promotes glioma progression by linking MYL9 to DAPK1 inhibition
Cao, C., He, K., Li, S., Ge, Q., Liu, L., Zhang, Z., Zhang, H., Wang, X., Sun, X., & Ding, L. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110062 · Cited by 8
Postsynaptic signaling at glutamatergic synapses as therapeutic targets
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Death-associated protein kinase 1: a double-edged sword in health and disease
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Stability of an anti-stroke peptide: Driving forces and kinetics in chemical degradation
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Protection of blood-brain barrier by endothelial DAPK1 deletion after stroke
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Young DAPK1 knockout mice have altered presynaptic function
Goodell, D. J., Tullis, J. E., & Bayer, K. U. (2021) · Journal of Neurophysiology · doi:10.1152/jn.00055.2021 · Cited by 7
Li, L., Zhang, B., Tang, X., Yu, Q., He, A., Lu, Y., & Li, X. (2022) · Cell Insight · doi:10.1016/j.cellin.2022.100060 · Cited by 7
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Targeting NMDA receptor signaling for therapeutic intervention in brain disorders
Chen, H., Dong, Y., Wu, Y. J., & Yi, F. (2022) · Reviews in the Neurosciences · doi:10.1515/revneuro-2022-0096 · Cited by 7
Chu, M.-C., Lee, J.-Y., Lee, H., Chu, K.-W., Wu, H.-F., Lee, C. J., Lin, C., Tang, C., & Lin, H. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.03.111 · Cited by 7
Brain Ischemia and Reperfusion
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Self-citationTargeting selective autophagy in CNS disorders by small-molecule compounds
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“Additionally, phosphorylation of death-associated protein kinase 1 (DAPK1) and phospho-inositide 3-kinase (PI3K) p85 subunit is enhanced in the early stages after HI, indicating that well-characterized kinases may phosphorylate GluN2B at one or more specific sites [34, 35].”
Salek, A. B., Claeboe, E. T., Bansal, R., Berbari, N. F., & Baucum, A. J. (2023) · Synapse · doi:10.1002/syn.22264 · Cited by 6
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Zeng, Z., Wang, D., Gaur, U., Rifang, L., Wang, H., & Zheng, W. (2017) · Oncotarget · doi:10.18632/oncotarget.18625 · Cited by 6
Chimeric Peptide Tat-HA-NR2B9c Improves Regenerative Repair after Transient Global Ischemia
Zhou, H.-H., Zhang, L., Zhang, H., Zhang, J., & Ge, W. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00509 · Cited by 6
“A prominent organizing protein is PSD-95, which binds both N-Methyl-d-aspartate receptors (NMDARs) and neuronal nitric oxide synthase (nNOS) at excitatory synapses (7, 8).”
BackgroundChang, Y., Pan, W., & Wang, S. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177654 · Cited by 5
Xiao, R., Wang, Q., Peng, J., Hu, X., Chen, M., & Xia, Y. (2025) · Experimental Brain Research · doi:10.1007/s00221-025-07127-3 · Cited by 5
“However, the interaction between DAPK1 and the NMDA NR2B subunit mediates stroke-induced brain injury (Tu et al. 2010).”
Neuroprotectants Targeting NMDA Receptor Signaling
Vetiska, S., & Tymianski, M. (2014) · Springer eBooks · doi:10.1007/978-1-4614-5836-4_168 · Cited by 5
Cholesterol and Fat Metabolism in Alzheimer’s Disease
Taghibiglou, C., & Khalaj, S. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802810-0.00009-x · Cited by 5
A Novel Neuroprotection Target With Distinct Regulation in Stroke and Alzheimer’s Disease
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Metadata
- 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 › Clinical Neurology › 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
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