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Volumn 45, Issue 3, 2012, Pages 999-1009

P38 MAPK is involved in enhanced NMDA receptor-dependent excitotoxicity in YAC transgenic mouse model of Huntington disease

Author keywords

Excitotoxicity; Huntington disease; JNK; NMDA receptor; P38; PSD 95

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE P38; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2B; POLYGLUTAMINE; POSTSYNAPTIC DENSITY PROTEIN 95; STRESS ACTIVATED PROTEIN KINASE; TRANSACTIVATOR PROTEIN;

EID: 84856579300     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2011.12.019     Document Type: Article
Times cited : (69)

References (93)
  • 1
    • 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
  • 2
    • 0037130451 scopus 로고    scopus 로고
    • Subunit-specific NMDA receptor trafficking to synapses
    • Barria A., Malinow R. Subunit-specific NMDA receptor trafficking to synapses. Neuron 2002, 35:345-353.
    • (2002) Neuron , vol.35 , pp. 345-353
    • Barria, A.1    Malinow, R.2
  • 3
    • 4444302167 scopus 로고    scopus 로고
    • Deranged neuronal calcium signaling and Huntington disease
    • Bezprozvanny I., Hayden M.R. Deranged neuronal calcium signaling and Huntington disease. Biochem. Biophys. Res. Commun. 2004, 322:1310-1317.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 1310-1317
    • Bezprozvanny, I.1    Hayden, M.R.2
  • 4
    • 3142596164 scopus 로고    scopus 로고
    • Molecular pathways to neurodegeneration
    • Bossy-Wetzel E., et al. Molecular pathways to neurodegeneration. Nat. Med. 2004, 10(Suppl.):S2-S9.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Bossy-Wetzel, E.1
  • 5
    • 0028899648 scopus 로고
    • Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase
    • Boulanger L.M., et al. Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase. J. Neurosci. 1995, 15:1532-1544.
    • (1995) J. Neurosci. , vol.15 , pp. 1532-1544
    • Boulanger, L.M.1
  • 6
    • 33745079669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking and function by striatal-enriched tyrosine phosphatase (STEP)
    • Braithwaite S.P., et al. Regulation of NMDA receptor trafficking and function by striatal-enriched tyrosine phosphatase (STEP). Eur. J. Neurosci. 2006, 23:2847-2856.
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 2847-2856
    • Braithwaite, S.P.1
  • 7
    • 33746366493 scopus 로고    scopus 로고
    • Synaptic plasticity: one STEP at a time
    • Braithwaite S.P., et al. Synaptic plasticity: one STEP at a time. Trends Neurosci. 2006, 29:452-458.
    • (2006) Trends Neurosci. , vol.29 , pp. 452-458
    • Braithwaite, S.P.1
  • 8
    • 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
  • 9
    • 0036321148 scopus 로고    scopus 로고
    • Mutant huntingtin goes straight to the heart
    • Cattaneo E., Calabresi P. Mutant huntingtin goes straight to the heart. Nat. Neurosci. 2002, 5:711-712.
    • (2002) Nat. Neurosci. , vol.5 , pp. 711-712
    • Cattaneo, E.1    Calabresi, P.2
  • 10
    • 0032971311 scopus 로고    scopus 로고
    • Subtype-specific enhancement of NMDA receptor currents by mutant huntingtin
    • Chen N., et al. Subtype-specific enhancement of NMDA receptor currents by mutant huntingtin. J. Neurochem. 1999, 72:1890-1898.
    • (1999) J. Neurochem. , vol.72 , pp. 1890-1898
    • Chen, N.1
  • 11
    • 33846456236 scopus 로고    scopus 로고
    • Differential roles of NR2A- and NR2B-containing NMDA receptors in activity-dependent brain-derived neurotrophic factor gene regulation and limbic epileptogenesis
    • Chen Q., et al. Differential roles of NR2A- and NR2B-containing NMDA receptors in activity-dependent brain-derived neurotrophic factor gene regulation and limbic epileptogenesis. J. Neurosci. 2007, 27:542-552.
    • (2007) J. Neurosci. , vol.27 , pp. 542-552
    • Chen, Q.1
  • 12
    • 0034009242 scopus 로고    scopus 로고
    • Native N-methyl-d-aspartate receptors containing NR2A and NR2B subunits have pharmacologically distinct competitive antagonist binding sites
    • Christie J.M., et al. Native N-methyl-d-aspartate receptors containing NR2A and NR2B subunits have pharmacologically distinct competitive antagonist binding sites. J. Pharmacol. Exp. Ther. 2000, 292:1169-1174.
    • (2000) J. Pharmacol. Exp. Ther. , vol.292 , pp. 1169-1174
    • Christie, J.M.1
  • 13
    • 0036615741 scopus 로고    scopus 로고
    • C-Jun N-terminal protein kinase (JNK) 2/3 is specifically activated by stress, mediating c-Jun activation, in the presence of constitutive JNK1 activity in cerebellar neurons
    • Coffey E.T., et al. c-Jun N-terminal protein kinase (JNK) 2/3 is specifically activated by stress, mediating c-Jun activation, in the presence of constitutive JNK1 activity in cerebellar neurons. J. Neurosci. 2002, 22:4335-4345.
    • (2002) J. Neurosci. , vol.22 , pp. 4335-4345
    • Coffey, E.T.1
  • 14
    • 33748577363 scopus 로고    scopus 로고
    • Selective neuronal degeneration in Huntington's disease
    • Cowan C.M., Raymond L.A. Selective neuronal degeneration in Huntington's disease. Curr. Top. Dev. Biol. 2006, 75:25-71.
    • (2006) Curr. Top. Dev. Biol. , vol.75 , pp. 25-71
    • Cowan, C.M.1    Raymond, L.A.2
  • 15
    • 58149373434 scopus 로고    scopus 로고
    • Polyglutamine-modulated striatal calpain activity in YAC transgenic Huntington disease mouse model: impact on NMDA receptor function and toxicity
    • Cowan C.M., et al. Polyglutamine-modulated striatal calpain activity in YAC transgenic Huntington disease mouse model: impact on NMDA receptor function and toxicity. J. Neurosci. 2008, 28:12725-12735.
    • (2008) J. Neurosci. , vol.28 , pp. 12725-12735
    • Cowan, C.M.1
  • 16
    • 0036209793 scopus 로고    scopus 로고
    • A broad view of glutamate spillover
    • Diamond J.S. A broad view of glutamate spillover. Nat. Neurosci. 2002, 5:291-292.
    • (2002) Nat. Neurosci. , vol.5 , pp. 291-292
    • Diamond, J.S.1
  • 17
    • 77953523094 scopus 로고    scopus 로고
    • Synaptic activity and nuclear calcium signaling protect hippocampal neurons from death signal-associated nuclear translocation of FoxO3a induced by extrasynaptic N-methyl-d-aspartate receptors
    • Dick O., Bading H. Synaptic activity and nuclear calcium signaling protect hippocampal neurons from death signal-associated nuclear translocation of FoxO3a induced by extrasynaptic N-methyl-d-aspartate receptors. J. Biol. Chem. 2010, 285:19354-19361.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19354-19361
    • Dick, O.1    Bading, H.2
  • 18
    • 34147112751 scopus 로고    scopus 로고
    • Altered NMDA receptor trafficking in a yeast artificial chromosome transgenic mouse model of Huntington's disease
    • Fan M.M., et al. Altered NMDA receptor trafficking in a yeast artificial chromosome transgenic mouse model of Huntington's disease. J. Neurosci. 2007, 27:3768-3779.
    • (2007) J. Neurosci. , vol.27 , pp. 3768-3779
    • Fan, M.M.1
  • 19
    • 69749091508 scopus 로고    scopus 로고
    • Interaction of postsynaptic density protein-95 with NMDA receptors influences excitotoxicity in the yeast artificial chromosome mouse model of Huntington's disease
    • Fan J., et al. Interaction of postsynaptic density protein-95 with NMDA receptors influences excitotoxicity in the yeast artificial chromosome mouse model of Huntington's disease. J. Neurosci. 2009, 29:10928-10938.
    • (2009) J. Neurosci. , vol.29 , pp. 10928-10938
    • Fan, J.1
  • 20
    • 77958561819 scopus 로고    scopus 로고
    • N-methyl-d-aspartate receptor subunit- and neuronal-type dependence of excitotoxic signaling through post-synaptic density 95
    • Fan J., et al. N-methyl-d-aspartate receptor subunit- and neuronal-type dependence of excitotoxic signaling through post-synaptic density 95. J. Neurochem. 2010, 115:1045-1056.
    • (2010) J. Neurochem. , vol.115 , pp. 1045-1056
    • Fan, J.1
  • 21
    • 37249083913 scopus 로고    scopus 로고
    • Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease
    • Fernandes H.B., et al. Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease. J. Neurosci. 2007, 27:13614-13623.
    • (2007) J. Neurosci. , vol.27 , pp. 13614-13623
    • Fernandes, H.B.1
  • 22
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni J., Ellerby L.M. Calpain activation in Huntington's disease. J. Neurosci. 2002, 22:4842-4849.
    • (2002) J. Neurosci. , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 23
    • 2442631459 scopus 로고    scopus 로고
    • Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus
    • Gafni J., et al. Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J. Biol. Chem. 2004, 279:20211-20220.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20211-20220
    • Gafni, J.1
  • 24
    • 0034710303 scopus 로고    scopus 로고
    • P38 MAP kinase mediates bax translocation in nitric oxide-induced apoptosis in neurons
    • Ghatan S., et al. p38 MAP kinase mediates bax translocation in nitric oxide-induced apoptosis in neurons. J. Cell Biol. 2000, 150:335-347.
    • (2000) J. Cell Biol. , vol.150 , pp. 335-347
    • Ghatan, S.1
  • 25
    • 4444380899 scopus 로고    scopus 로고
    • Adenosine and glutamate extracellular concentrations and mitogen-activated protein kinases in the striatum of Huntington transgenic mice. Selective antagonism of adenosine A2A receptors reduces transmitter outflow
    • Gianfriddo M., et al. Adenosine and glutamate extracellular concentrations and mitogen-activated protein kinases in the striatum of Huntington transgenic mice. Selective antagonism of adenosine A2A receptors reduces transmitter outflow. Neurobiol. Dis. 2004, 17:77-88.
    • (2004) Neurobiol. Dis. , vol.17 , pp. 77-88
    • Gianfriddo, M.1
  • 26
    • 30744459353 scopus 로고    scopus 로고
    • Levels of mutant huntingtin influence the phenotypic severity of Huntington disease in YAC128 mouse models
    • Graham R.K., et al. Levels of mutant huntingtin influence the phenotypic severity of Huntington disease in YAC128 mouse models. Neurobiol. Dis. 2006, 21:444-455.
    • (2006) Neurobiol. Dis. , vol.21 , pp. 444-455
    • Graham, R.K.1
  • 27
    • 29044449313 scopus 로고    scopus 로고
    • N-methyl-d-aspartate (NMDA) and the regulation of mitogen-activated protein kinase (MAPK) signaling pathways: a revolving neurochemical axis for therapeutic intervention?
    • Haddad J.J. N-methyl-d-aspartate (NMDA) and the regulation of mitogen-activated protein kinase (MAPK) signaling pathways: a revolving neurochemical axis for therapeutic intervention?. Prog. Neurobiol. 2005, 77:252-282.
    • (2005) Prog. Neurobiol. , vol.77 , pp. 252-282
    • Haddad, J.J.1
  • 28
    • 33751268411 scopus 로고    scopus 로고
    • Pro-survival signalling from the NMDA receptor
    • Hardingham G.E. Pro-survival signalling from the NMDA receptor. Biochem. Soc. Trans. 2006, 34:936-938.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 936-938
    • Hardingham, G.E.1
  • 29
    • 0037301661 scopus 로고    scopus 로고
    • The Yin and Yang of NMDA receptor signalling
    • Hardingham G.E., Bading H. The Yin and Yang of NMDA receptor signalling. Trends Neurosci. 2003, 26:81-89.
    • (2003) Trends Neurosci. , vol.26 , pp. 81-89
    • Hardingham, G.E.1    Bading, H.2
  • 31
    • 63849154126 scopus 로고    scopus 로고
    • In vivo evidence for NMDA receptor-mediated excitotoxicity in a murine genetic model of Huntington disease
    • Heng M.Y., et al. In vivo evidence for NMDA receptor-mediated excitotoxicity in a murine genetic model of Huntington disease. J. Neurosci. 2009, 29:3200-3205.
    • (2009) J. Neurosci. , vol.29 , pp. 3200-3205
    • Heng, M.Y.1
  • 32
    • 0033136692 scopus 로고    scopus 로고
    • A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration
    • Hodgson J.G., et al. A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron 1999, 23:181-192.
    • (1999) Neuron , vol.23 , pp. 181-192
    • Hodgson, J.G.1
  • 33
    • 0036757263 scopus 로고    scopus 로고
    • The effect of aging on p38 signaling pathway activity in the mouse liver and in response to ROS generated by 3-nitropropionic acid
    • Hsieh C.C., Papaconstantinou J. The effect of aging on p38 signaling pathway activity in the mouse liver and in response to ROS generated by 3-nitropropionic acid. Mech. Ageing Dev. 2002, 123:1423-1435.
    • (2002) Mech. Ageing Dev. , vol.123 , pp. 1423-1435
    • Hsieh, C.C.1    Papaconstantinou, J.2
  • 34
    • 0037674756 scopus 로고    scopus 로고
    • Age-associated changes in SAPK/JNK and p38 MAPK signaling in response to the generation of ROS by 3-nitropropionic acid
    • Hsieh C.C., et al. Age-associated changes in SAPK/JNK and p38 MAPK signaling in response to the generation of ROS by 3-nitropropionic acid. Mech. Ageing Dev. 2003, 124:733-746.
    • (2003) Mech. Ageing Dev. , vol.124 , pp. 733-746
    • Hsieh, C.C.1
  • 35
    • 40849139482 scopus 로고    scopus 로고
    • Long-term potentiation inhibition by low-level N-methyl-d-aspartate receptor activation involves calcineurin, nitric oxide, and p38 mitogen-activated protein kinase
    • Izumi Y., et al. Long-term potentiation inhibition by low-level N-methyl-d-aspartate receptor activation involves calcineurin, nitric oxide, and p38 mitogen-activated protein kinase. Hippocampus 2008, 18:258-265.
    • (2008) Hippocampus , vol.18 , pp. 258-265
    • Izumi, Y.1
  • 36
    • 1542346231 scopus 로고    scopus 로고
    • Regulation of proteins affecting NMDA receptor-induced excitotoxicity in a Huntington's mouse model
    • Jarabek B.R., et al. Regulation of proteins affecting NMDA receptor-induced excitotoxicity in a Huntington's mouse model. Brain 2004, 127:505-516.
    • (2004) Brain , vol.127 , pp. 505-516
    • Jarabek, B.R.1
  • 37
    • 0031015043 scopus 로고    scopus 로고
    • Fas activation of the p38 mitogen-activated protein kinase signalling pathway requires ICE/CED-3 family proteases
    • Juo P., et al. Fas activation of the p38 mitogen-activated protein kinase signalling pathway requires ICE/CED-3 family proteases. Mol. Cell. Biol. 1997, 17:24-35.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 24-35
    • Juo, P.1
  • 38
    • 34548864370 scopus 로고    scopus 로고
    • Culturing hippocampal neurons
    • Kaech S., Banker G. Culturing hippocampal neurons. Nat. Protoc. 2006, 1:2406-2415.
    • (2006) Nat. Protoc. , vol.1 , pp. 2406-2415
    • Kaech, S.1    Banker, G.2
  • 39
    • 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
  • 40
    • 0032055396 scopus 로고    scopus 로고
    • SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family
    • Kim J.H., et al. SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family. Neuron 1998, 20:683-691.
    • (1998) Neuron , vol.20 , pp. 683-691
    • Kim, J.H.1
  • 41
    • 0036080832 scopus 로고    scopus 로고
    • Mitochondrial ROS initiate phosphorylation of p38 MAP kinase during hypoxia in cardiomyocytes
    • Kulisz A., et al. Mitochondrial ROS initiate phosphorylation of p38 MAP kinase during hypoxia in cardiomyocytes. Am. J. Physiol. Lung Cell. Mol. Physiol. 2002, 282:L1324-L1329.
    • (2002) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.282
    • Kulisz, A.1
  • 42
    • 0029068332 scopus 로고
    • NMDA receptor subunit mRNA expression by projection neurons and interneurons in rat striatum
    • Landwehrmeyer G.B., et al. NMDA receptor subunit mRNA expression by projection neurons and interneurons in rat striatum. J. Neurosci. 1995, 15:5297-5307.
    • (1995) J. Neurosci. , vol.15 , pp. 5297-5307
    • Landwehrmeyer, G.B.1
  • 43
    • 0035127907 scopus 로고    scopus 로고
    • Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo
    • Leavitt B.R., et al. Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo. Am. J. Hum. Genet. 2001, 68:313-324.
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 313-324
    • Leavitt, B.R.1
  • 44
    • 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
  • 45
    • 0033571743 scopus 로고    scopus 로고
    • Enhanced sensitivity to N-methyl-d-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease
    • Levine M.S., et al. Enhanced sensitivity to N-methyl-d-aspartate receptor activation in transgenic and knockin mouse models of Huntington's disease. J. Neurosci. Res. 1999, 58:515-532.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 515-532
    • Levine, M.S.1
  • 46
    • 0344413576 scopus 로고    scopus 로고
    • Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington disease
    • Li L., et al. Role of NR2B-type NMDA receptors in selective neurodegeneration in Huntington disease. Neurobiol. Aging 2003, 24:1113-1121.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1113-1121
    • Li, L.1
  • 47
    • 14844314896 scopus 로고    scopus 로고
    • Enhanced striatal NR2B-containing N-methyl-d-aspartate receptor-mediated synaptic currents in a mouse model of Huntington disease
    • Li L., et al. Enhanced striatal NR2B-containing N-methyl-d-aspartate receptor-mediated synaptic currents in a mouse model of Huntington disease. J. Neurophysiol. 2004, 92:2738-2746.
    • (2004) J. Neurophysiol. , vol.92 , pp. 2738-2746
    • Li, L.1
  • 48
    • 0001583878 scopus 로고    scopus 로고
    • Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin
    • Liu Y.F., et al. Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin. J. Biol. Chem. 2000, 275:19035-19040.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19035-19040
    • Liu, Y.F.1
  • 49
    • 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
  • 50
    • 84856583036 scopus 로고    scopus 로고
    • Calpain in the CNS: from synaptic function to neurotoxicity
    • Liu J., et al. Calpain in the CNS: from synaptic function to neurotoxicity. Sci. Signal. 2008, 1:re1.
    • (2008) Sci. Signal. , vol.1
    • Liu, J.1
  • 51
    • 37449011119 scopus 로고    scopus 로고
    • Corticostriatal synaptic function in mouse models of Huntington's disease: early effects of huntingtin repeat length and protein load
    • Milnerwood A.J., Raymond L.A. Corticostriatal synaptic function in mouse models of Huntington's disease: early effects of huntingtin repeat length and protein load. J. Physiol. 2007, 585:817-831.
    • (2007) J. Physiol. , vol.585 , pp. 817-831
    • Milnerwood, A.J.1    Raymond, L.A.2
  • 52
    • 74549181538 scopus 로고    scopus 로고
    • Early increase in extrasynaptic NMDA receptor signaling and expression contributes to phenotype onset in Huntington's disease mice
    • Milnerwood A.J., et al. Early increase in extrasynaptic NMDA receptor signaling and expression contributes to phenotype onset in Huntington's disease mice. Neuron 2010, 65:178-190.
    • (2010) Neuron , vol.65 , pp. 178-190
    • Milnerwood, A.J.1
  • 53
    • 0037954344 scopus 로고    scopus 로고
    • Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents
    • Munoz J.J., et al. Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents. Biochem. J. 2003, 372:193-201.
    • (2003) Biochem. J. , vol.372 , pp. 193-201
    • Munoz, J.J.1
  • 54
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa H., et al. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 1991, 108:193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1
  • 55
    • 0028857858 scopus 로고
    • Immunocytochemical localization of the striatal enriched protein tyrosine phosphatase in the rat striatum: a light and electron microscopic study with a complementary DNA-generated polyclonal antibody
    • Oyama T., et al. Immunocytochemical localization of the striatal enriched protein tyrosine phosphatase in the rat striatum: a light and electron microscopic study with a complementary DNA-generated polyclonal antibody. Neuroscience 1995, 69:869-880.
    • (1995) Neuroscience , vol.69 , pp. 869-880
    • Oyama, T.1
  • 56
    • 77953407291 scopus 로고    scopus 로고
    • The role of AMPAR trafficking mediated by neuronal pentraxins in cocaine-induced neuroadaptations
    • Pacchioni A.M., Kalivas P.W. The role of AMPAR trafficking mediated by neuronal pentraxins in cocaine-induced neuroadaptations. Mol. Cell Pharmacol. 2009, 1:183-192.
    • (2009) Mol. Cell Pharmacol. , vol.1 , pp. 183-192
    • Pacchioni, A.M.1    Kalivas, P.W.2
  • 57
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • Panov A.V., et al. Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat. Neurosci. 2002, 5:731-736.
    • (2002) Nat. Neurosci. , vol.5 , pp. 731-736
    • Panov, A.V.1
  • 58
    • 35948937549 scopus 로고    scopus 로고
    • The dichotomy of NMDA receptor signaling
    • Papadia S., Hardingham G.E. The dichotomy of NMDA receptor signaling. Neuroscientist 2007, 13:572-579.
    • (2007) Neuroscientist , vol.13 , pp. 572-579
    • Papadia, S.1    Hardingham, G.E.2
  • 59
    • 0037220735 scopus 로고    scopus 로고
    • NMDA-mediated activation of the tyrosine phosphatase STEP regulates the duration of ERK signaling
    • Paul S., et al. NMDA-mediated activation of the tyrosine phosphatase STEP regulates the duration of ERK signaling. Nat. Neurosci. 2003, 6:34-42.
    • (2003) Nat. Neurosci. , vol.6 , pp. 34-42
    • Paul, S.1
  • 60
    • 33947310301 scopus 로고    scopus 로고
    • The striatal-enriched protein tyrosine phosphatase gates long-term potentiation and fear memory in the lateral amygdala
    • Paul S., et al. The striatal-enriched protein tyrosine phosphatase gates long-term potentiation and fear memory in the lateral amygdala. Biol. Psychiatry 2007, 61:1049-1061.
    • (2007) Biol. Psychiatry , vol.61 , pp. 1049-1061
    • Paul, S.1
  • 61
    • 0037187645 scopus 로고    scopus 로고
    • Tyrosine phosphatase STEP is a tonic brake on induction of long-term potentiation
    • Pelkey K.A., et al. Tyrosine phosphatase STEP is a tonic brake on induction of long-term potentiation. Neuron 2002, 34:127-138.
    • (2002) Neuron , vol.34 , pp. 127-138
    • Pelkey, K.A.1
  • 62
    • 57449085907 scopus 로고    scopus 로고
    • Implication of the JNK pathway in a rat model of Huntington's disease
    • Perrin V., et al. Implication of the JNK pathway in a rat model of Huntington's disease. Exp. Neurol. 2009, 215:191-200.
    • (2009) Exp. Neurol. , vol.215 , pp. 191-200
    • Perrin, V.1
  • 63
    • 78649994240 scopus 로고    scopus 로고
    • NR2B-NMDA receptor mediated modulation of the tyrosine phosphatase STEP regulates glutamate induced neuronal cell death
    • Poddar R., et al. NR2B-NMDA receptor mediated modulation of the tyrosine phosphatase STEP regulates glutamate induced neuronal cell death. J. Neurochem. 2010, 115:1350-1362.
    • (2010) J. Neurochem. , vol.115 , pp. 1350-1362
    • Poddar, R.1
  • 64
    • 0034941552 scopus 로고    scopus 로고
    • Molecular determinants of NMDA receptor internalization
    • Roche K.W., et al. Molecular determinants of NMDA receptor internalization. Nat. Neurosci. 2001, 4:794-802.
    • (2001) Nat. Neurosci. , vol.4 , pp. 794-802
    • Roche, K.W.1
  • 65
    • 0033573390 scopus 로고    scopus 로고
    • Distinct synaptic and extrasynaptic NMDA receptors in developing cerebellar granule neurons
    • Rumbaugh G., Vicini S. Distinct synaptic and extrasynaptic NMDA receptors in developing cerebellar granule neurons. J. Neurosci. 1999, 19:10603-10610.
    • (1999) J. Neurosci. , vol.19 , pp. 10603-10610
    • Rumbaugh, G.1    Vicini, S.2
  • 66
    • 33645217296 scopus 로고    scopus 로고
    • SynGAP regulates synaptic strength and mitogen-activated protein kinases in cultured neurons
    • Rumbaugh G., et al. SynGAP regulates synaptic strength and mitogen-activated protein kinases in cultured neurons. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:4344-4351.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4344-4351
    • Rumbaugh, G.1
  • 67
    • 0034023864 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium-dependent excitotoxicity
    • Sattler R., Tymianski M. Molecular mechanisms of calcium-dependent excitotoxicity. J. Mol. Med. 2000, 78:3-13.
    • (2000) J. Mol. Med. , vol.78 , pp. 3-13
    • Sattler, R.1    Tymianski, M.2
  • 68
    • 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
  • 69
    • 0032851595 scopus 로고    scopus 로고
    • Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization
    • Sawa A., et al. Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization. Nat. Med. 1999, 5:1194-1198.
    • (1999) Nat. Med. , vol.5 , pp. 1194-1198
    • Sawa, A.1
  • 70
    • 34547843693 scopus 로고    scopus 로고
    • Intersectin enhances huntingtin aggregation and neurodegeneration through activation of c-Jun-NH2-terminal kinase
    • Scappini E., et al. Intersectin enhances huntingtin aggregation and neurodegeneration through activation of c-Jun-NH2-terminal kinase. Hum. Mol. Genet. 2007, 16:1862-1871.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1862-1871
    • Scappini, E.1
  • 71
    • 0030957325 scopus 로고    scopus 로고
    • Glutamate, but not dopamine, stimulates stress-activated protein kinase and AP-1-mediated transcription in striatal neurons
    • Schwarzschild M.A., et al. Glutamate, but not dopamine, stimulates stress-activated protein kinase and AP-1-mediated transcription in striatal neurons. J. Neurosci. 1997, 17:3455-3466.
    • (1997) J. Neurosci. , vol.17 , pp. 3455-3466
    • Schwarzschild, M.A.1
  • 72
    • 0038345688 scopus 로고    scopus 로고
    • Formation of dendritic spines in cultured striatal neurons depends on excitatory afferent activity
    • Segal M., et al. Formation of dendritic spines in cultured striatal neurons depends on excitatory afferent activity. Eur. J. Neurosci. 2003, 17:2573-2585.
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 2573-2585
    • Segal, M.1
  • 73
    • 10744227174 scopus 로고    scopus 로고
    • Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease
    • Slow E.J., et al. Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 2003, 12:1555-1567.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1555-1567
    • Slow, E.J.1
  • 74
    • 0042357138 scopus 로고    scopus 로고
    • Expression of polyglutamine-expanded huntingtin induces tyrosine phosphorylation of N-methyl-d-aspartate receptors
    • Song C., et al. Expression of polyglutamine-expanded huntingtin induces tyrosine phosphorylation of N-methyl-d-aspartate receptors. J. Biol. Chem. 2003, 278:33364-33369.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33364-33369
    • Song, C.1
  • 75
    • 35348918230 scopus 로고    scopus 로고
    • Compartmentalized NMDA receptor signalling to survival and death
    • Soriano F.X., Hardingham G.E. Compartmentalized NMDA receptor signalling to survival and death. J. Physiol. 2007, 584:381-387.
    • (2007) J. Physiol. , vol.584 , pp. 381-387
    • Soriano, F.X.1    Hardingham, G.E.2
  • 76
    • 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
  • 77
    • 8144228679 scopus 로고    scopus 로고
    • HAP1 facilitates effects of mutant huntingtin on inositol 1,4,5-trisphosphate-induced Ca release in primary culture of striatal medium spiny neurons
    • Tang T.S., et al. HAP1 facilitates effects of mutant huntingtin on inositol 1,4,5-trisphosphate-induced Ca release in primary culture of striatal medium spiny neurons. Eur. J. Neurosci. 2004, 20:1779-1787.
    • (2004) Eur. J. Neurosci. , vol.20 , pp. 1779-1787
    • Tang, T.S.1
  • 78
    • 14044264256 scopus 로고    scopus 로고
    • 2+ signaling and apoptosis of medium spiny neurons in Huntington's disease
    • 2+ signaling and apoptosis of medium spiny neurons in Huntington's disease. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:2602-2607.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2602-2607
    • Tang, T.S.1
  • 79
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 1993, 72:971-983. The Huntington's Disease Collaborative Research Group.
    • (1993) Cell , vol.72 , pp. 971-983
  • 80
    • 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
  • 81
    • 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
  • 82
    • 0038383459 scopus 로고    scopus 로고
    • Opposing roles of synaptic and extrasynaptic NMDA receptors in neuronal calcium signalling and BDNF gene regulation
    • Vanhoutte P., Bading H. Opposing roles of synaptic and extrasynaptic NMDA receptors in neuronal calcium signalling and BDNF gene regulation. Curr. Opin. Neurobiol. 2003, 13:366-371.
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 366-371
    • Vanhoutte, P.1    Bading, H.2
  • 83
    • 0031959242 scopus 로고    scopus 로고
    • Neurotransmitter regulation of MAP kinase signaling in striatal neurons in primary culture
    • Vincent S.R., et al. Neurotransmitter regulation of MAP kinase signaling in striatal neurons in primary culture. Synapse 1998, 29:29-36.
    • (1998) Synapse , vol.29 , pp. 29-36
    • Vincent, S.R.1
  • 85
    • 2542439782 scopus 로고    scopus 로고
    • Glutamate signaling to Ras-MAPK in striatal neurons: mechanisms for inducible gene expression and plasticity
    • Wang J.Q., et al. Glutamate signaling to Ras-MAPK in striatal neurons: mechanisms for inducible gene expression and plasticity. Mol. Neurobiol. 2004, 29:1-14.
    • (2004) Mol. Neurobiol. , vol.29 , pp. 1-14
    • Wang, J.Q.1
  • 86
    • 33846245536 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinases by glutamate receptors
    • Wang J.Q., et al. Regulation of mitogen-activated protein kinases by glutamate receptors. J. Neurochem. 2007, 100:1-11.
    • (2007) J. Neurochem. , vol.100 , pp. 1-11
    • Wang, J.Q.1
  • 87
    • 13544268511 scopus 로고    scopus 로고
    • N-methyl-d-aspartate receptor subtypes: multiple roles in excitotoxicity and neurological disease
    • Waxman E.A., Lynch D.R. N-methyl-d-aspartate receptor subtypes: multiple roles in excitotoxicity and neurological disease. Neuroscientist 2005, 11:37-49.
    • (2005) Neuroscientist , vol.11 , pp. 37-49
    • Waxman, E.A.1    Lynch, D.R.2
  • 88
    • 0031730811 scopus 로고    scopus 로고
    • Calpain inhibitors as potential treatment for stoke and other neurodegenerative diseases: recent trends and developments
    • Wells G.J., Bihovsky R. Calpain inhibitors as potential treatment for stoke and other neurodegenerative diseases: recent trends and developments. Exp. Opin. Ther. Pat. 1998, 8:21.
    • (1998) Exp. Opin. Ther. Pat. , vol.8 , pp. 21
    • Wells, G.J.1    Bihovsky, R.2
  • 89
    • 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
  • 90
    • 0035154912 scopus 로고    scopus 로고
    • Mutant huntingtin enhances excitotoxic cell death
    • Zeron M.M., et al. Mutant huntingtin enhances excitotoxic cell death. Mol. Cell. Neurosci. 2001, 17:41-53.
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 41-53
    • Zeron, M.M.1
  • 91
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-d-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • Zeron M.M., et al. Increased sensitivity to N-methyl-d-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron 2002, 33:849-860.
    • (2002) Neuron , vol.33 , pp. 849-860
    • Zeron, M.M.1
  • 92
    • 1642295805 scopus 로고    scopus 로고
    • Potentiation of NMDA receptor-mediated excitotoxicity linked with intrinsic apoptotic pathway in YAC transgenic mouse model of Huntington's disease
    • Zeron M.M., et al. Potentiation of NMDA receptor-mediated excitotoxicity linked with intrinsic apoptotic pathway in YAC transgenic mouse model of Huntington's disease. Mol. Cell. Neurosci. 2004, 25:469-479.
    • (2004) Mol. Cell. Neurosci. , vol.25 , pp. 469-479
    • Zeron, M.M.1
  • 93
    • 45049085513 scopus 로고    scopus 로고
    • 2+ signaling and apoptosis of striatal neurons in the YAC mouse model of Huntington's disease
    • 2+ signaling and apoptosis of striatal neurons in the YAC mouse model of Huntington's disease. Neurobiol. Dis. 2008, 31:80-88.
    • (2008) Neurobiol. Dis. , vol.31 , pp. 80-88
    • Zhang, H.1


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