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Volumn 17, Issue 5, 2011, Pages 266-275

Stroke intervention pathways: NMDA receptors and beyond

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CLATHRIN; DEATH ASSOCIATED PROTEIN KINASE; MEMANTINE; MITOGEN ACTIVATED PROTEIN KINASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; NEURONAL NITRIC OXIDE SYNTHASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; POSTSYNAPTIC DENSITY PROTEIN 95; STEROL REGULATORY ELEMENT BINDING PROTEIN 1;

EID: 79955645278     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2010.12.008     Document Type: Review
Times cited : (158)

References (88)
  • 1
    • 0036330007 scopus 로고    scopus 로고
    • Toward wisdom from failure: lessons from neuroprotective stroke trials and new therapeutic directions
    • Gladstone D.J., et al. Toward wisdom from failure: lessons from neuroprotective stroke trials and new therapeutic directions. Stroke 2002, 33:2123-2136.
    • (2002) Stroke , vol.33 , pp. 2123-2136
    • Gladstone, D.J.1
  • 2
    • 0033199996 scopus 로고    scopus 로고
    • Pathobiology of ischaemic stroke: an integrated view
    • Dirnagl U., et al. Pathobiology of ischaemic stroke: an integrated view. Trends Neurosci. 1999, 22:391-397.
    • (1999) Trends Neurosci. , vol.22 , pp. 391-397
    • Dirnagl, U.1
  • 3
    • 0033600277 scopus 로고    scopus 로고
    • The changing landscape of ischaemic brain injury mechanisms
    • Lee J.M., et al. The changing landscape of ischaemic brain injury mechanisms. Nature 1999, 399:A7-14.
    • (1999) Nature , vol.399
    • Lee, J.M.1
  • 4
    • 0028872674 scopus 로고
    • Excitotoxicity and the NMDA receptor - still lethal after eight years
    • Rothman S.M., Olney J.W. Excitotoxicity and the NMDA receptor - still lethal after eight years. Trends Neurosci. 1995, 18:57-58.
    • (1995) Trends Neurosci. , vol.18 , pp. 57-58
    • Rothman, S.M.1    Olney, J.W.2
  • 5
    • 0021743001 scopus 로고
    • Blockade of N-methyl-D-aspartate receptors may protect against ischemic damage in the brain
    • Simon R.P., et al. Blockade of N-methyl-D-aspartate receptors may protect against ischemic damage in the brain. Science 1984, 226:850-852.
    • (1984) Science , vol.226 , pp. 850-852
    • Simon, R.P.1
  • 6
    • 0030901530 scopus 로고    scopus 로고
    • N-methyl-D-aspartate antagonists for stroke and head trauma
    • Wood P.L., Hawkinson J.E. N-methyl-D-aspartate antagonists for stroke and head trauma. Expert Opin. Investig. Drugs 1997, 6:389-397.
    • (1997) Expert Opin. Investig. Drugs , vol.6 , pp. 389-397
    • Wood, P.L.1    Hawkinson, J.E.2
  • 7
    • 77952363301 scopus 로고    scopus 로고
    • Glutamate receptor ion channels: structure, regulation, and function
    • Traynelis S.F., et al. Glutamate receptor ion channels: structure, regulation, and function. Pharmacol. Rev. 2010, 62:405-496.
    • (2010) Pharmacol. Rev. , vol.62 , pp. 405-496
    • Traynelis, S.F.1
  • 8
    • 39849102491 scopus 로고    scopus 로고
    • Evolution of NMDA receptor cytoplasmic interaction domains: implications for organisation of synaptic signalling complexes
    • Ryan T.J., et al. Evolution of NMDA receptor cytoplasmic interaction domains: implications for organisation of synaptic signalling complexes. BMC Neurosci. 2008, 9:6.
    • (2008) BMC Neurosci. , vol.9 , pp. 6
    • Ryan, T.J.1
  • 9
    • 77953785351 scopus 로고    scopus 로고
    • Long-term depression in the CNS
    • Collingridge G.L., et al. Long-term depression in the CNS. Nat. Rev. Neurosci. 2010, 11:459-473.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 459-473
    • Collingridge, G.L.1
  • 10
    • 0032947526 scopus 로고    scopus 로고
    • Blockade of NMDA receptors and apoptotic neurodegeneration in the developing brain
    • Ikonomidou C., et al. Blockade of NMDA receptors and apoptotic neurodegeneration in the developing brain. Science 1999, 283:70-74.
    • (1999) Science , vol.283 , pp. 70-74
    • Ikonomidou, C.1
  • 11
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton S.A., Rosenberg P.A. Excitatory amino acids as a final common pathway for neurologic disorders. N. Engl. J. Med. 1994, 330:613-622.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 12
    • 33947331063 scopus 로고    scopus 로고
    • NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo
    • Liu Y., et al. NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo. J. Neurosci. 2007, 27:2846-2857.
    • (2007) J. Neurosci. , vol.27 , pp. 2846-2857
    • Liu, Y.1
  • 13
    • 55749108180 scopus 로고    scopus 로고
    • Differential roles of NMDA receptor subtypes in ischemic neuronal cell death and ischemic tolerance
    • Chen M., et al. Differential roles of NMDA receptor subtypes in ischemic neuronal cell death and ischemic tolerance. Stroke 2008, 39:3042-3048.
    • (2008) Stroke , vol.39 , pp. 3042-3048
    • Chen, M.1
  • 14
    • 0035132869 scopus 로고    scopus 로고
    • Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons
    • Lu W., et al. Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons. Neuron 2001, 29:243-254.
    • (2001) Neuron , vol.29 , pp. 243-254
    • Lu, W.1
  • 15
    • 57349135887 scopus 로고    scopus 로고
    • Neuronal viability is controlled by a functional relation between synaptic and extrasynaptic NMDA receptors
    • Leveille F., et al. Neuronal viability is controlled by a functional relation between synaptic and extrasynaptic NMDA receptors. FASEB J. 2008, 22:4258-4271.
    • (2008) FASEB J. , vol.22 , pp. 4258-4271
    • Leveille, F.1
  • 16
    • 67649875657 scopus 로고    scopus 로고
    • Coupling diverse routes of calcium entry to mitochondrial dysfunction and glutamate excitotoxicity
    • Stanika R.I., et al. Coupling diverse routes of calcium entry to mitochondrial dysfunction and glutamate excitotoxicity. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:9854-9859.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9854-9859
    • Stanika, R.I.1
  • 17
    • 67651172947 scopus 로고    scopus 로고
    • Extrasynaptic NMDA receptors couple preferentially to excitotoxicity via calpain-mediated cleavage of STEP
    • Xu J., et al. Extrasynaptic NMDA receptors couple preferentially to excitotoxicity via calpain-mediated cleavage of STEP. J. Neurosci. 2009, 29:9330-9343.
    • (2009) J. Neurosci. , vol.29 , pp. 9330-9343
    • Xu, J.1
  • 18
    • 33846847943 scopus 로고    scopus 로고
    • Decoding NMDA receptor signaling: identification of genomic programs specifying neuronal survival and death
    • Zhang S.J., et al. Decoding NMDA receptor signaling: identification of genomic programs specifying neuronal survival and death. Neuron 2007, 53:549-562.
    • (2007) Neuron , vol.53 , pp. 549-562
    • Zhang, S.J.1
  • 19
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • Hardingham G.E., et al. Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways. Nat. Neurosci. 2002, 5:405-414.
    • (2002) Nat. Neurosci. , vol.5 , pp. 405-414
    • Hardingham, G.E.1
  • 20
    • 77956917231 scopus 로고    scopus 로고
    • Synaptic versus extrasynaptic NMDA receptor signalling: implications for neurodegenerative disorders
    • Hardingham G.E., Bading H. Synaptic versus extrasynaptic NMDA receptor signalling: implications for neurodegenerative disorders. Nat. Rev. Neurosci. 2010, 11:682-696.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 682-696
    • Hardingham, G.E.1    Bading, H.2
  • 21
    • 71549143207 scopus 로고    scopus 로고
    • Balance between synaptic versus extrasynaptic NMDA receptor activity influences inclusions and neurotoxicity of mutant huntingtin
    • Okamoto S., et al. Balance between synaptic versus extrasynaptic NMDA receptor activity influences inclusions and neurotoxicity of mutant huntingtin. Nat. Med. 2009, 15:1407-1413.
    • (2009) Nat. Med. , vol.15 , pp. 1407-1413
    • Okamoto, S.1
  • 22
    • 45749092281 scopus 로고    scopus 로고
    • Evaluation of effects of memantine on cerebral ischemia in rats
    • Aluclu M.U., et al. Evaluation of effects of memantine on cerebral ischemia in rats. Neurosciences (Riyadh) 2008, 13:113-116.
    • (2008) Neurosciences (Riyadh) , vol.13 , pp. 113-116
    • Aluclu, M.U.1
  • 23
    • 77950369012 scopus 로고    scopus 로고
    • Organization of NMDA receptors at extrasynaptic locations
    • Petralia R.S., et al. Organization of NMDA receptors at extrasynaptic locations. Neuroscience 2010, 167:68-87.
    • (2010) Neuroscience , vol.167 , pp. 68-87
    • Petralia, R.S.1
  • 24
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler R., et al. Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science 1999, 284:1845-1848.
    • (1999) Science , vol.284 , pp. 1845-1848
    • Sattler, R.1
  • 25
    • 0037174635 scopus 로고    scopus 로고
    • Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions
    • Aarts M., et al. Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions. Science 2002, 298:846-850.
    • (2002) Science , vol.298 , pp. 846-850
    • Aarts, M.1
  • 26
    • 0033600913 scopus 로고    scopus 로고
    • PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain
    • Christopherson K.S., et al. PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain. J. Biol. Chem. 1999, 274:27467-27473.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27467-27473
    • Christopherson, K.S.1
  • 27
    • 78650016701 scopus 로고    scopus 로고
    • Fashioning drugs for stroke
    • Lai T.W., Wang Y.T. Fashioning drugs for stroke. Nat. Med. 2010, 16:1376-1378.
    • (2010) Nat. Med. , vol.16 , pp. 1376-1378
    • Lai, T.W.1    Wang, Y.T.2
  • 28
    • 78649983743 scopus 로고    scopus 로고
    • Treatment of cerebral ischemia by disrupting ischemia-induced interaction of nNOS with PSD-95
    • Zhou L., et al. Treatment of cerebral ischemia by disrupting ischemia-induced interaction of nNOS with PSD-95. Nat. Med. 2010, 16:1439-1443.
    • (2010) Nat. Med. , vol.16 , pp. 1439-1443
    • Zhou, L.1
  • 29
    • 0027497936 scopus 로고
    • Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons
    • Tymianski M., et al. Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons. J. Neurosci. 1993, 13:2085-2104.
    • (1993) J. Neurosci. , vol.13 , pp. 2085-2104
    • Tymianski, M.1
  • 30
    • 0033562610 scopus 로고    scopus 로고
    • The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro
    • Tovar K.R., Westbrook G.L. The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro. J. Neurosci. 1999, 19:4180-4188.
    • (1999) J. Neurosci. , vol.19 , pp. 4180-4188
    • Tovar, K.R.1    Westbrook, G.L.2
  • 31
    • 33645010267 scopus 로고    scopus 로고
    • Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors
    • Zhou M., Baudry M. Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors. J. Neurosci. 2006, 26:2956-2963.
    • (2006) J. Neurosci. , vol.26 , pp. 2956-2963
    • Zhou, M.1    Baudry, M.2
  • 32
    • 33645061251 scopus 로고    scopus 로고
    • Traumatic mechanical injury to the hippocampus in vitro causes regional caspase-3 and calpain activation that is influenced by NMDA receptor subunit composition
    • DeRidder M.N., et al. Traumatic mechanical injury to the hippocampus in vitro causes regional caspase-3 and calpain activation that is influenced by NMDA receptor subunit composition. Neurobiol. Dis. 2006, 22:165-176.
    • (2006) Neurobiol. Dis. , vol.22 , pp. 165-176
    • DeRidder, M.N.1
  • 33
    • 77955176190 scopus 로고    scopus 로고
    • Activation of NR2A receptors induces ischemic tolerance through CREB signaling
    • Terasaki Y., et al. Activation of NR2A receptors induces ischemic tolerance through CREB signaling. J. Cereb. Blood Flow Metab. 2010, 30:1441-1449.
    • (2010) J. Cereb. Blood Flow Metab. , vol.30 , pp. 1441-1449
    • Terasaki, Y.1
  • 34
    • 74549173438 scopus 로고    scopus 로고
    • DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke
    • Tu W., et al. DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke. Cell 2010, 140:222-234.
    • (2010) Cell , vol.140 , pp. 222-234
    • Tu, W.1
  • 35
    • 18644386370 scopus 로고    scopus 로고
    • Dual regulation of NMDA receptor functions by direct protein-protein interactions with the dopamine D1 receptor
    • Lee F.J., et al. Dual regulation of NMDA receptor functions by direct protein-protein interactions with the dopamine D1 receptor. Cell 2002, 111:219-230.
    • (2002) Cell , vol.111 , pp. 219-230
    • Lee, F.J.1
  • 36
    • 70350365279 scopus 로고    scopus 로고
    • Kidins220/ARMS downregulation by excitotoxic activation of NMDARs reveals its involvement in neuronal survival and death pathways
    • Lopez-Menendez C., et al. Kidins220/ARMS downregulation by excitotoxic activation of NMDARs reveals its involvement in neuronal survival and death pathways. J. Cell Sci. 2009, 122:3554-3565.
    • (2009) J. Cell Sci. , vol.122 , pp. 3554-3565
    • Lopez-Menendez, C.1
  • 37
    • 74549206659 scopus 로고    scopus 로고
    • Blocking the deadly effects of the NMDA receptor in stroke
    • Martin H.G., Wang Y.T. Blocking the deadly effects of the NMDA receptor in stroke. Cell 2010, 140:174-176.
    • (2010) Cell , vol.140 , pp. 174-176
    • Martin, H.G.1    Wang, Y.T.2
  • 38
    • 32544450453 scopus 로고    scopus 로고
    • Relating NMDA receptor function to receptor subunit composition: limitations of the pharmacological approach
    • Neyton J., Paoletti P. Relating NMDA receptor function to receptor subunit composition: limitations of the pharmacological approach. J. Neurosci. 2006, 26:1331-1333.
    • (2006) J. Neurosci. , vol.26 , pp. 1331-1333
    • Neyton, J.1    Paoletti, P.2
  • 39
    • 0028979586 scopus 로고
    • Ifenprodil inhibition of the 5-hydroxytryptamine3 receptor
    • McCool B.A., Lovinger D.M. Ifenprodil inhibition of the 5-hydroxytryptamine3 receptor. Neuropharmacology 1995, 34:621-629.
    • (1995) Neuropharmacology , vol.34 , pp. 621-629
    • McCool, B.A.1    Lovinger, D.M.2
  • 40
    • 34547228856 scopus 로고    scopus 로고
    • Excitotoxicity in vitro by NR2A- and NR2B-containing NMDA receptors
    • von Engelhardt J., et al. Excitotoxicity in vitro by NR2A- and NR2B-containing NMDA receptors. Neuropharmacology 2007, 53:10-17.
    • (2007) Neuropharmacology , vol.53 , pp. 10-17
    • von Engelhardt, J.1
  • 41
    • 58149476292 scopus 로고    scopus 로고
    • In developing hippocampal neurons NR2B-containing N-methyl-D-aspartate receptors (NMDARs) can mediate signaling to neuronal survival and synaptic potentiation, as well as neuronal death
    • Martel M.A., et al. In developing hippocampal neurons NR2B-containing N-methyl-D-aspartate receptors (NMDARs) can mediate signaling to neuronal survival and synaptic potentiation, as well as neuronal death. Neuroscience 2009, 158:334-343.
    • (2009) Neuroscience , vol.158 , pp. 334-343
    • Martel, M.A.1
  • 42
    • 35348900781 scopus 로고    scopus 로고
    • Extrasynaptic and synaptic NMDA receptors form stable and uniform pools in rat hippocampal slices
    • Harris A.Z., Pettit D.L. Extrasynaptic and synaptic NMDA receptors form stable and uniform pools in rat hippocampal slices. J. Physiol. 2007, 584:509-519.
    • (2007) J. Physiol. , vol.584 , pp. 509-519
    • Harris, A.Z.1    Pettit, D.L.2
  • 43
    • 0034688312 scopus 로고    scopus 로고
    • Glutamate release in severe brain ischaemia is mainly by reversed uptake
    • Rossi D.J., et al. Glutamate release in severe brain ischaemia is mainly by reversed uptake. Nature 2000, 403:316-321.
    • (2000) Nature , vol.403 , pp. 316-321
    • Rossi, D.J.1
  • 44
    • 69549118534 scopus 로고    scopus 로고
    • Disruption of nNOS-PSD95 protein-protein interaction inhibits acute thermal hyperalgesia and chronic mechanical allodynia in rodents
    • Florio S.K., et al. Disruption of nNOS-PSD95 protein-protein interaction inhibits acute thermal hyperalgesia and chronic mechanical allodynia in rodents. Br. J. Pharmacol. 2009, 158:494-506.
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 494-506
    • Florio, S.K.1
  • 45
    • 33846004477 scopus 로고    scopus 로고
    • PTEN enters the nuclear age
    • Baker S.J. PTEN enters the nuclear age. Cell 2007, 128:25-28.
    • (2007) Cell , vol.128 , pp. 25-28
    • Baker, S.J.1
  • 46
    • 11144356390 scopus 로고    scopus 로고
    • Dual neuroprotective signaling mediated by downregulating two distinct phosphatase activities of PTEN
    • Ning K., et al. Dual neuroprotective signaling mediated by downregulating two distinct phosphatase activities of PTEN. J. Neurosci. 2004, 24:4052-4060.
    • (2004) J. Neurosci. , vol.24 , pp. 4052-4060
    • Ning, K.1
  • 47
    • 33846457396 scopus 로고    scopus 로고
    • Critical role of PTEN in the coupling between PI3K/Akt and JNK1/2 signaling in ischemic brain injury
    • Zhang Q.G., et al. Critical role of PTEN in the coupling between PI3K/Akt and JNK1/2 signaling in ischemic brain injury. FEBS Lett. 2007, 581:495-505.
    • (2007) FEBS Lett. , vol.581 , pp. 495-505
    • Zhang, Q.G.1
  • 48
    • 0041825308 scopus 로고    scopus 로고
    • PTEN regulates Akt kinase activity in hippocampal neurons and increases their sensitivity to glutamate and apoptosis
    • Gary D.S., Mattson M.P. PTEN regulates Akt kinase activity in hippocampal neurons and increases their sensitivity to glutamate and apoptosis. Neuromol. Med. 2002, 2:261-269.
    • (2002) Neuromol. Med. , vol.2 , pp. 261-269
    • Gary, D.S.1    Mattson, M.P.2
  • 49
    • 77349112413 scopus 로고    scopus 로고
    • Neuroprotection by baicalein in ischemic brain injury involves PTEN/AKT pathway
    • Liu C., et al. Neuroprotection by baicalein in ischemic brain injury involves PTEN/AKT pathway. J. Neurochem. 2010, 112:1500-1512.
    • (2010) J. Neurochem. , vol.112 , pp. 1500-1512
    • Liu, C.1
  • 50
    • 69549126148 scopus 로고    scopus 로고
    • The protective effect of early hypothermia on PTEN phosphorylation correlates with free radical inhibition in rat stroke
    • Lee S.M., et al. The protective effect of early hypothermia on PTEN phosphorylation correlates with free radical inhibition in rat stroke. J. Cereb. Blood Flow Metab. 2009, 29:1589-1600.
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , pp. 1589-1600
    • Lee, S.M.1
  • 51
    • 79955643761 scopus 로고    scopus 로고
    • PTEN nuclear translocation induced by NMDAR activation enhances neuronal death
    • Program No. 149.5. 2009. Neuroscience Meeting Planner. Chicago, IL: Society for Neuroscience, 2009. Online
    • Zhang, S. et al. (2009) PTEN nuclear translocation induced by NMDAR activation enhances neuronal death. Program No. 149.5. 2009. Neuroscience Meeting Planner. Chicago, IL: Society for Neuroscience, 2009. Online.
    • (2009)
    • Zhang, S.1
  • 52
    • 77955850746 scopus 로고    scopus 로고
    • PTEN is recruited to the postsynaptic terminal for NMDA receptor-dependent long-term depression
    • Jurado S., et al. PTEN is recruited to the postsynaptic terminal for NMDA receptor-dependent long-term depression. EMBO J. 2010, 29:2827-2840.
    • (2010) EMBO J. , vol.29 , pp. 2827-2840
    • Jurado, S.1
  • 53
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: structure, function, and beyond
    • Bialik S., Kimchi A. The death-associated protein kinases: structure, function, and beyond. Annu. Rev. Biochem. 2006, 75:189-210.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 54
    • 0029015969 scopus 로고
    • Delayed antagonism of calpain reduces excitotoxicity in cultured neurons
    • (discussion 1267)
    • Brorson J.R., et al. Delayed antagonism of calpain reduces excitotoxicity in cultured neurons. Stroke 1995, 26:1259-1266. (discussion 1267).
    • (1995) Stroke , vol.26 , pp. 1259-1266
    • Brorson, J.R.1
  • 55
    • 55949091941 scopus 로고    scopus 로고
    • A novel calpain inhibitor, ((1S)-1((((1S)-1-benzyl-3-cyclopropylamino-2,3-di-oxopropyl)amino)carbonyl)-3-methylbutyl) carbamic acid 5-methoxy-3-oxapentyl ester, protects neuronal cells from cerebral ischemia-induced damage in mice
    • Koumura A., et al. A novel calpain inhibitor, ((1S)-1((((1S)-1-benzyl-3-cyclopropylamino-2,3-di-oxopropyl)amino)carbonyl)-3-methylbutyl) carbamic acid 5-methoxy-3-oxapentyl ester, protects neuronal cells from cerebral ischemia-induced damage in mice. Neuroscience 2008, 157:309-318.
    • (2008) Neuroscience , vol.157 , pp. 309-318
    • Koumura, A.1
  • 56
    • 71549138847 scopus 로고    scopus 로고
    • Role of NMDA receptor-dependent activation of SREBP1 in excitotoxic and ischemic neuronal injuries
    • Taghibiglou C., et al. Role of NMDA receptor-dependent activation of SREBP1 in excitotoxic and ischemic neuronal injuries. Nat. Med. 2009, 15:1399-1406.
    • (2009) Nat. Med. , vol.15 , pp. 1399-1406
    • Taghibiglou, C.1
  • 57
    • 33846502748 scopus 로고    scopus 로고
    • Calpain-mediated mGluR1alpha truncation: a key step in excitotoxicity
    • Xu W., et al. Calpain-mediated mGluR1alpha truncation: a key step in excitotoxicity. Neuron 2007, 53:399-412.
    • (2007) Neuron , vol.53 , pp. 399-412
    • Xu, W.1
  • 58
    • 0034682414 scopus 로고    scopus 로고
    • Neurotoxicity induces cleavage of p35 to p25 by calpain
    • Lee M.S., et al. Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature 2000, 405:360-364.
    • (2000) Nature , vol.405 , pp. 360-364
    • Lee, M.S.1
  • 59
    • 19544367458 scopus 로고    scopus 로고
    • Differential roles of NR2A- and NR2B-containing NMDA receptors in Ras-ERK signaling and AMPA receptor trafficking
    • Kim M.J., et al. Differential roles of NR2A- and NR2B-containing NMDA receptors in Ras-ERK signaling and AMPA receptor trafficking. Neuron 2005, 46:745-760.
    • (2005) Neuron , vol.46 , pp. 745-760
    • Kim, M.J.1
  • 60
    • 33645105536 scopus 로고    scopus 로고
    • Subunit dependencies of N-methyl-D-aspartate (NMDA) receptor-induced alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor internalization
    • Tigaret C.M., et al. Subunit dependencies of N-methyl-D-aspartate (NMDA) receptor-induced alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor internalization. Mol. Pharmacol. 2006, 69:1251-1259.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1251-1259
    • Tigaret, C.M.1
  • 61
    • 77953271477 scopus 로고    scopus 로고
    • Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization
    • Li Z., et al. Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization. Cell 2010, 141:859-871.
    • (2010) Cell , vol.141 , pp. 859-871
    • Li, Z.1
  • 62
    • 4744345382 scopus 로고    scopus 로고
    • Alpha-Amino-3-hydroxy-5-methylisoxazole-4-propionic acid subtype glutamate receptor (AMPAR) endocytosis is essential for N-methyl-D-aspartate-induced neuronal apoptosis
    • Wang Y., et al. alpha-Amino-3-hydroxy-5-methylisoxazole-4-propionic acid subtype glutamate receptor (AMPAR) endocytosis is essential for N-methyl-D-aspartate-induced neuronal apoptosis. J. Biol. Chem. 2004, 279:41267-41270.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41267-41270
    • Wang, Y.1
  • 63
    • 12144288368 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of GluR2 is required for insulin-stimulated AMPA receptor endocytosis and LTD
    • Ahmadian G., et al. Tyrosine phosphorylation of GluR2 is required for insulin-stimulated AMPA receptor endocytosis and LTD. EMBO J. 2004, 23:1040-1050.
    • (2004) EMBO J. , vol.23 , pp. 1040-1050
    • Ahmadian, G.1
  • 64
    • 0036326058 scopus 로고    scopus 로고
    • Arrestin: roles in the life and death of retinal neurons
    • Dolph P.J. Arrestin: roles in the life and death of retinal neurons. Neuroscientist 2002, 8:347-355.
    • (2002) Neuroscientist , vol.8 , pp. 347-355
    • Dolph, P.J.1
  • 65
    • 0034711397 scopus 로고    scopus 로고
    • Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3
    • McDonald P.H., et al. Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. Science 2000, 290:1574-1577.
    • (2000) Science , vol.290 , pp. 1574-1577
    • McDonald, P.H.1
  • 66
    • 3242700615 scopus 로고    scopus 로고
    • Expression of Ca(2+)-permeable AMPA receptor channels primes cell death in transient forebrain ischemia
    • Liu S., et al. Expression of Ca(2+)-permeable AMPA receptor channels primes cell death in transient forebrain ischemia. Neuron 2004, 43:43-55.
    • (2004) Neuron , vol.43 , pp. 43-55
    • Liu, S.1
  • 67
    • 24744431841 scopus 로고    scopus 로고
    • Blockade of calcium-permeable AMPA receptors protects hippocampal neurons against global ischemia-induced death
    • Noh K.-M., et al. Blockade of calcium-permeable AMPA receptors protects hippocampal neurons against global ischemia-induced death. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:12230-12235.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12230-12235
    • Noh, K.-M.1
  • 68
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions
    • Pearson G., et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr. Rev. 2001, 22:153-183.
    • (2001) Endocr. Rev. , vol.22 , pp. 153-183
    • Pearson, G.1
  • 69
    • 13444311622 scopus 로고    scopus 로고
    • Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK
    • Chen C.-H., et al. Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK. EMBO 2005, 24:294-304.
    • (2005) EMBO , vol.24 , pp. 294-304
    • Chen, C.-H.1
  • 70
    • 70350571696 scopus 로고    scopus 로고
    • NMDA receptors are involved in upstream of the spinal JNK activation in morphine antinociceptive tolerance
    • Guo R.X., et al. NMDA receptors are involved in upstream of the spinal JNK activation in morphine antinociceptive tolerance. Neurosci. Lett. 2009, 467:95-99.
    • (2009) Neurosci. Lett. , vol.467 , pp. 95-99
    • Guo, R.X.1
  • 71
    • 12144271690 scopus 로고    scopus 로고
    • The PSD95-nNOS interface: a target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death
    • Cao J., et al. The PSD95-nNOS interface: a target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death. J. Cell Biol. 2005, 168:117-126.
    • (2005) J. Cell Biol. , vol.168 , pp. 117-126
    • Cao, J.1
  • 72
    • 54849439830 scopus 로고    scopus 로고
    • Specific targeting of pro-death NMDA receptor signals with differing reliance on the NR2B PDZ ligand
    • Soriano F.X., et al. Specific targeting of pro-death NMDA receptor signals with differing reliance on the NR2B PDZ ligand. J. Neurosci. 2008, 28:10696-10710.
    • (2008) J. Neurosci. , vol.28 , pp. 10696-10710
    • Soriano, F.X.1
  • 73
    • 0030741894 scopus 로고    scopus 로고
    • Activation and involvement of p38 mitogen-activated protein kinase in glutamate-induced apoptosis in rat cerebellar granule cells
    • Kawasaki H., et al. Activation and involvement of p38 mitogen-activated protein kinase in glutamate-induced apoptosis in rat cerebellar granule cells. J. Biol. Chem. 1997, 272:18518-18521.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18518-18521
    • Kawasaki, H.1
  • 74
    • 0037188746 scopus 로고    scopus 로고
    • The selective p38 inhibitor SB-239063 protects primary neurons from mild to moderate excitotoxic injury
    • Legos J.J., et al. The selective p38 inhibitor SB-239063 protects primary neurons from mild to moderate excitotoxic injury. Eur. J. Pharmacol. 2002, 447:37-42.
    • (2002) Eur. J. Pharmacol. , vol.447 , pp. 37-42
    • Legos, J.J.1
  • 75
    • 0035124607 scopus 로고    scopus 로고
    • Inhibition of p38 mitogen-activated protein kinase provides neuroprotection in cerebral focal ischemia
    • Barone F.C., et al. Inhibition of p38 mitogen-activated protein kinase provides neuroprotection in cerebral focal ischemia. Med. Res. Rev. 2001, 21:129-145.
    • (2001) Med. Res. Rev. , vol.21 , pp. 129-145
    • Barone, F.C.1
  • 76
    • 0141724805 scopus 로고    scopus 로고
    • A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia
    • Borsello T., et al. A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia. Nat. Med. 2003, 9:1180-1186.
    • (2003) Nat. Med. , vol.9 , pp. 1180-1186
    • Borsello, T.1
  • 77
    • 3042694907 scopus 로고    scopus 로고
    • D-JNKI1, a cell-penetrating c-Jun-N-terminal kinase inhibitor, protects against cell death in severe cerebral ischemia
    • Hirt L., et al. D-JNKI1, a cell-penetrating c-Jun-N-terminal kinase inhibitor, protects against cell death in severe cerebral ischemia. Stroke 2004, 35:1738-1743.
    • (2004) Stroke , vol.35 , pp. 1738-1743
    • Hirt, L.1
  • 78
    • 40949113125 scopus 로고    scopus 로고
    • D-JNKi, a peptide inhibitor of c-Jun N-terminal kinase, promotes functional recovery after transient focal cerebral ischemia in rats
    • Esneault E., et al. D-JNKi, a peptide inhibitor of c-Jun N-terminal kinase, promotes functional recovery after transient focal cerebral ischemia in rats. Neuroscience 2008, 152:308-320.
    • (2008) Neuroscience , vol.152 , pp. 308-320
    • Esneault, E.1
  • 79
    • 30344473341 scopus 로고    scopus 로고
    • Protein sensors for membrane sterols
    • Goldstein J.L., et al. Protein sensors for membrane sterols. Cell 2006, 124:35-46.
    • (2006) Cell , vol.124 , pp. 35-46
    • Goldstein, J.L.1
  • 80
    • 33646812935 scopus 로고    scopus 로고
    • Lipids and lipidomics in brain injury and diseases
    • Adibhatla R.M., et al. Lipids and lipidomics in brain injury and diseases. AAPS J. 2006, 8:E314-321.
    • (2006) AAPS J. , vol.8
    • Adibhatla, R.M.1
  • 81
    • 0026771449 scopus 로고
    • Ischemic brain damage: focus on lipids and lipid mediators
    • Siesjo B.K., Katsura K. Ischemic brain damage: focus on lipids and lipid mediators. Adv. Exp. Med. Biol. 1992, 318:41-56.
    • (1992) Adv. Exp. Med. Biol. , vol.318 , pp. 41-56
    • Siesjo, B.K.1    Katsura, K.2
  • 82
    • 0037067449 scopus 로고    scopus 로고
    • Role of sterol regulatory element binding proteins in the regulation of Galpha(i2) expression in cultured atrial cells
    • Park H.J., et al. Role of sterol regulatory element binding proteins in the regulation of Galpha(i2) expression in cultured atrial cells. Circ. Res. 2002, 91:32-37.
    • (2002) Circ. Res. , vol.91 , pp. 32-37
    • Park, H.J.1
  • 83
    • 38149016990 scopus 로고    scopus 로고
    • Parasympathetic response in chick myocytes and mouse heart is controlled by SREBP
    • Park H.J., et al. Parasympathetic response in chick myocytes and mouse heart is controlled by SREBP. J. Clin. Invest. 2008, 118:259-271.
    • (2008) J. Clin. Invest. , vol.118 , pp. 259-271
    • Park, H.J.1
  • 84
    • 0031914497 scopus 로고    scopus 로고
    • The problem of assessing effective neuroprotection in experimental cerebral ischemia
    • Corbett D., Nurse S. The problem of assessing effective neuroprotection in experimental cerebral ischemia. Prog. Neurobiol. 1998, 54:531-548.
    • (1998) Prog. Neurobiol. , vol.54 , pp. 531-548
    • Corbett, D.1    Nurse, S.2
  • 85
    • 0035814418 scopus 로고    scopus 로고
    • Aptiganel hydrochloride in acute ischemic stroke: a randomized controlled trial
    • Albers G.W., et al. Aptiganel hydrochloride in acute ischemic stroke: a randomized controlled trial. JAMA 2001, 286:2673-2682.
    • (2001) JAMA , vol.286 , pp. 2673-2682
    • Albers, G.W.1
  • 86
    • 0035137210 scopus 로고    scopus 로고
    • Glycine antagonist (GV150526) in acute stroke: a multicentre, double-blind placebo-controlled phase II trial
    • Lees K.R., et al. Glycine antagonist (GV150526) in acute stroke: a multicentre, double-blind placebo-controlled phase II trial. Cerebrovasc. Dis. 2001, 11:20-29.
    • (2001) Cerebrovasc. Dis. , vol.11 , pp. 20-29
    • Lees, K.R.1
  • 87
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho K.O., et al. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 1992, 9:929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1
  • 88
    • 35548946698 scopus 로고    scopus 로고
    • DAP kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress
    • Eisenberg-Lerner A., Kimchi A. DAP kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress. Cell Death Differ. 2007, 14:1908-1915.
    • (2007) Cell Death Differ. , vol.14 , pp. 1908-1915
    • Eisenberg-Lerner, A.1    Kimchi, A.2


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