메뉴 건너뛰기




Volumn 62, Issue 6, 2013, Pages 836-842

Lectin from Canavalia brasiliensis (ConBr) protects hippocampal slices against glutamate neurotoxicity in a manner dependent of PI3K/Akt pathway

Author keywords

ConBr; Glutamate; Lectin; Neuroprotection; NMDA; PI3K Akt

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; CONCANAVALIN BR; GLUTAMIC ACID; LECTIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 10; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE 9; MITOGEN ACTIVATED PROTEIN KINASE P38; NEUROPROTECTIVE AGENT; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE 1; UNCLASSIFIED DRUG;

EID: 84875071937     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2013.02.020     Document Type: Article
Times cited : (16)

References (67)
  • 4
    • 0024411948 scopus 로고
    • Has immunoblotting replaced electroimmunoprecipitation? Examples from the analysis of autoantigens and transglutaminase-induced polymers of the human erythrocyte membrane
    • O.J. Bjerrum, and N.H. Heegaard Has immunoblotting replaced electroimmunoprecipitation? Examples from the analysis of autoantigens and transglutaminase-induced polymers of the human erythrocyte membrane J. Chromatogr. 470 1989 351 367
    • (1989) J. Chromatogr. , vol.470 , pp. 351-367
    • Bjerrum, O.J.1    Heegaard, N.H.2
  • 5
    • 0031771515 scopus 로고    scopus 로고
    • Presynaptic inhibition by concavalin A: Are alpha-latrotoxin receptors involved in action potential-dependent transmitter release?
    • S. Boehm, and S. Huck Presynaptic inhibition by concavalin A: are alpha-latrotoxin receptors involved in action potential-dependent transmitter release? J. Neurochem. 71 1998 2421 2430
    • (1998) J. Neurochem. , vol.71 , pp. 2421-2430
    • Boehm, S.1    Huck, S.2
  • 6
  • 7
    • 0029153913 scopus 로고
    • Apoptosis and necrosis: Two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures
    • E. Bonfoco, D. Krainc, M.D. Ankrakrona, P. Nicotera, and S.A. Lipton Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures Proc. Natl. Acad. Sci. USA 92 1995 7162 7166
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7162-7166
    • Bonfoco, E.1    Krainc, D.2    Ankrakrona, M.D.3    Nicotera, P.4    Lipton, S.A.5
  • 8
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signaling: A hard AKT to follow
    • D.P. Brazil, and B.A. Hemmings Ten years of protein kinase B signaling: a hard AKT to follow Trends Biochem. Sci. 26 2001 657 664
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 9
    • 2342565881 scopus 로고    scopus 로고
    • Advances in protein kinase B signalling: AKTion on multiple fronts
    • D.P. Brazil, Z.Z. Yang, and B.A. Hemmings Advances in protein kinase B signalling: AKTion on multiple fronts Trends Biochem. Sci. 29 2004 23 42
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 23-42
    • Brazil, D.P.1    Yang, Z.Z.2    Hemmings, B.A.3
  • 10
    • 0034991896 scopus 로고    scopus 로고
    • Revisiting proteus: Do minor changes in lectin structure matter in biological activity? Lessons from and potential biotechnological uses of the diocleinae subtribe lectins
    • B.S. Cavada, T. Barbosa, S. Arruda, T.B. Grangeiro, and M. Barral-Netto Revisiting proteus: do minor changes in lectin structure matter in biological activity? Lessons from and potential biotechnological uses of the diocleinae subtribe lectins Curr. Protein Pept. Sci. 2 2001 1 13
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 1-13
    • Cavada, B.S.1    Barbosa, T.2    Arruda, S.3    Grangeiro, T.B.4    Barral-Netto, M.5
  • 11
    • 12344262306 scopus 로고    scopus 로고
    • Characterization of serotonin transporter in blood lymphocytes of rats. Modulation by in vivo administration of mitogens
    • N. Cedeño, M. Urbina, F. Obregón, and L. Lima Characterization of serotonin transporter in blood lymphocytes of rats. Modulation by in vivo administration of mitogens J. Neuroimmunol. 159 2005 31 40
    • (2005) J. Neuroimmunol. , vol.159 , pp. 31-40
    • Cedeño, N.1    Urbina, M.2    Obregón, F.3    Lima, L.4
  • 13
    • 0023137252 scopus 로고
    • Ionic dependence of glutamate neurotoxicity
    • D.W. Choi Ionic dependence of glutamate neurotoxicity J. Neurosci. 7 1987 369 379
    • (1987) J. Neurosci. , vol.7 , pp. 369-379
    • Choi, D.W.1
  • 14
    • 0026497926 scopus 로고
    • Excitotoxic cell death
    • D.W. Choi Excitotoxic cell death J. Neurobiol. 23 1992 1261 1276
    • (1992) J. Neurobiol. , vol.23 , pp. 1261-1276
    • Choi, D.W.1
  • 15
    • 33846785187 scopus 로고    scopus 로고
    • Deactivation of Akt and STAT3 signaling promotes apoptosis, inhibits proliferation, and enhances the sensitivity of hepatocellular carcinoma cells to an anticancer agent
    • S.R. Choudhari, M.A. Khan, G. Harris, D. Picker, G.S. Jacob, T. Block, and K. Shailubhai Deactivation of Akt and STAT3 signaling promotes apoptosis, inhibits proliferation, and enhances the sensitivity of hepatocellular carcinoma cells to an anticancer agent Atiprimod Mol. Cancer Ther. 6 2007 112 121
    • (2007) Atiprimod Mol. Cancer Ther. , vol.6 , pp. 112-121
    • Choudhari, S.R.1    Khan, M.A.2    Harris, G.3    Picker, D.4    Jacob, G.S.5    Block, T.6    Shailubhai, K.7
  • 17
    • 82955196366 scopus 로고    scopus 로고
    • GSK-3 as a target for lithium-induced neuroprotection against excitotoxicity in neuronal cultures and animal models of ischemic stroke
    • D.M. Chuang, Z. Wang, and C.T. Chiu GSK-3 as a target for lithium-induced neuroprotection against excitotoxicity in neuronal cultures and animal models of ischemic stroke Front. Mol. Neurosci. 4 2011 15
    • (2011) Front. Mol. Neurosci. , vol.4 , pp. 15
    • Chuang, D.M.1    Wang, Z.2    Chiu, C.T.3
  • 18
    • 0031745290 scopus 로고    scopus 로고
    • Identification of lectin-purified neural glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA receptor subunits: Conservation of glycosylation at the synapse
    • R.A. Clark, J.W. Gurd, N. Bissoon, N. Tricaud, E. Molnar, S.E. Zamze, R.A. Dwek, R.A. McIlhinney, and D.R. Wing Identification of lectin-purified neural glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA receptor subunits: conservation of glycosylation at the synapse J. Neurochem. 70 1998 2594 2605
    • (1998) J. Neurochem. , vol.70 , pp. 2594-2605
    • Clark, R.A.1    Gurd, J.W.2    Bissoon, N.3    Tricaud, N.4    Molnar, E.5    Zamze, S.E.6    Dwek, R.A.7    McIlhinney, R.A.8    Wing, D.R.9
  • 21
    • 79955585812 scopus 로고    scopus 로고
    • + channels, phosphatidilinositol-3 kinase/protein kinase B pathway activation and glutamate uptake
    • + channels, phosphatidilinositol-3 kinase/protein kinase B pathway activation and glutamate uptake Neuroscience 183 2011 212 220
    • (2011) Neuroscience , vol.183 , pp. 212-220
    • Dal-Cim, T.1    Martins, W.C.2    Santos, A.R.3    Tasca, C.I.4
  • 22
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation-potential for therapeutics and diagnostics
    • D.H. Dube, and C.R. Bertozzi Glycans in cancer and inflammation-potential for therapeutics and diagnostics Nat. Rev. Drug Discovery 4 2005 477 488
    • (2005) Nat. Rev. Drug Discovery , vol.4 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 23
    • 21444460273 scopus 로고    scopus 로고
    • Glycans and glycan-binding proteins in brain: Galectin-1-induced expression of neurotrophic factors in astocytes
    • T. Endo Glycans and glycan-binding proteins in brain: galectin-1-induced expression of neurotrophic factors in astocytes Curr. Drug Targets 6 2005 427 436
    • (2005) Curr. Drug Targets , vol.6 , pp. 427-436
    • Endo, T.1
  • 24
    • 0030729835 scopus 로고    scopus 로고
    • N-Glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation
    • I. Everts, C. Villmann, and M. Hollmann N-Glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation Mol. Pharmacol. 52 1997 861 873
    • (1997) Mol. Pharmacol. , vol.52 , pp. 861-873
    • Everts, I.1    Villmann, C.2    Hollmann, M.3
  • 25
    • 33645313464 scopus 로고    scopus 로고
    • Concanavalin-A reports agonist-induced conformational changes in the intact GluR6 kainate receptor
    • A.M. Fay, and D. Bowie Concanavalin-A reports agonist-induced conformational changes in the intact GluR6 kainate receptor J. Physiol. 572 2006 201 213
    • (2006) J. Physiol. , vol.572 , pp. 201-213
    • Fay, A.M.1    Bowie, D.2
  • 26
    • 79952008246 scopus 로고    scopus 로고
    • A glycobiology review: Carbohydrates, lectins and implications in cancer therapeutics
    • H. Ghazarian, B. Idoni, and S.B. Pooenheimer A glycobiology review: carbohydrates, lectins and implications in cancer therapeutics Elsevier 113 2010 236 247
    • (2010) Elsevier , vol.113 , pp. 236-247
    • Ghazarian, H.1    Idoni, B.2    Pooenheimer, S.B.3
  • 27
    • 84860210195 scopus 로고    scopus 로고
    • Basic pharmacology of NMDA receptors
    • X. Gonda Basic pharmacology of NMDA receptors Curr. Pharm. Des. 18 2012 1558 1567
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 1558-1567
    • Gonda, X.1
  • 28
    • 0035798093 scopus 로고    scopus 로고
    • The neurobiology of slow synaptic transmission
    • P. Greengard The neurobiology of slow synaptic transmission Science 294 2001 1024 1030
    • (2001) Science , vol.294 , pp. 1024-1030
    • Greengard, P.1
  • 30
    • 1542328927 scopus 로고    scopus 로고
    • Structure, regulation and function of PKB/AKT-A major therapeutic target
    • M. Hanada, J. Feng, and B.A. Hemmings Structure, regulation and function of PKB/AKT-a major therapeutic target Biochim. Biophys. Acta 1697 2004 3 16
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 3-16
    • Hanada, M.1    Feng, J.2    Hemmings, B.A.3
  • 31
    • 84555187316 scopus 로고    scopus 로고
    • Cadmium increases HIF-1 and VEGF expression through ROS, ERK, and AKT signaling pathways and induces malignant transformation of human bronchial epithelial cells
    • Y. Jing, L.Z. Liu, Y. Jiang, Y. Zhu, N.L. Guo, J. Barnett, Y. Rojanasakul, F. Agani, and B.H. Jiang Cadmium increases HIF-1 and VEGF expression through ROS, ERK, and AKT signaling pathways and induces malignant transformation of human bronchial epithelial cells Toxicol. Sci. 125 2012 10 19
    • (2012) Toxicol. Sci. , vol.125 , pp. 10-19
    • Jing, Y.1    Liu, L.Z.2    Jiang, Y.3    Zhu, Y.4    Guo, N.L.5    Barnett, J.6    Rojanasakul, Y.7    Agani, F.8    Jiang, B.H.9
  • 32
    • 14544300519 scopus 로고    scopus 로고
    • A positive role of the PI3K/Akt signaling pathway in PC12 cell differentiation
    • Y. Kim, R. Seger, C.V. Suresh babu, S.Y. Hwang, and Y.S. Yoo A positive role of the PI3K/Akt signaling pathway in PC12 cell differentiation Mol. Cells 18 2004 353 359
    • (2004) Mol. Cells , vol.18 , pp. 353-359
    • Kim, Y.1    Seger, R.2    Suresh Babu, C.V.3    Hwang, S.Y.4    Yoo, Y.S.5
  • 33
    • 76749088358 scopus 로고    scopus 로고
    • Pathological roles of MAPK signaling pathways in human diseases
    • E.K. Kim, and E.J. Choi Pathological roles of MAPK signaling pathways in human diseases Biochim. Biophys. Acta 1802 2010 396 405
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 396-405
    • Kim, E.K.1    Choi, E.J.2
  • 34
    • 77955570062 scopus 로고    scopus 로고
    • Glutamate receptors, neurotoxicity an neurodegeneration
    • A. Lau, and M. Tymianski Glutamate receptors, neurotoxicity an neurodegeneration Pflugers Arch. 460 2010 525 542
    • (2010) Pflugers Arch. , vol.460 , pp. 525-542
    • Lau, A.1    Tymianski, M.2
  • 35
    • 84863376097 scopus 로고    scopus 로고
    • Ghrelin protects spinal cord motoneurons against chronic glutamate excitotoxicity by inhibiting microglial activation
    • S. Lee, Y. Kim, E. Li, and S. Park Ghrelin protects spinal cord motoneurons against chronic glutamate excitotoxicity by inhibiting microglial activation Korean J. Physiol. Pharmacol. 16 2012 43 48
    • (2012) Korean J. Physiol. Pharmacol. , vol.16 , pp. 43-48
    • Lee, S.1    Kim, Y.2    Li, E.3    Park, S.4
  • 36
    • 0025805779 scopus 로고
    • Concanavalin A: A tool to investigate neuronal plasticity
    • S.S. Lin, and I.B. Levitan Concanavalin A: a tool to investigate neuronal plasticity Trends Neurosci. 14 1991 273 277
    • (1991) Trends Neurosci. , vol.14 , pp. 273-277
    • Lin, S.S.1    Levitan, I.B.2
  • 37
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) reduction
    • Y. Liu, D.A. Peterson, H. Kimura, and D. Schubert Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction J. Neurochem. 69 1997 581 593
    • (1997) J. Neurochem. , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 38
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • F.T. Liu, and G.A. Rabinovich Galectins as modulators of tumour progression Nat. Rev. Cancer 5 2005 29 41
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 39
    • 21644437580 scopus 로고    scopus 로고
    • Differential effect of plant lectins on mast cells of different origins on the histamine release induced by plant lectins
    • F.C. Lopes, B.S. Cavada, V.P. Pinto, A.H. Sampaio, and J.C. Gomes Differential effect of plant lectins on mast cells of different origins on the histamine release induced by plant lectins Braz. J. Med. Biol. Res. 38 2005 935 941
    • (2005) Braz. J. Med. Biol. Res. , vol.38 , pp. 935-941
    • Lopes, F.C.1    Cavada, B.S.2    Pinto, V.P.3    Sampaio, A.H.4    Gomes, J.C.5
  • 40
    • 0036179194 scopus 로고    scopus 로고
    • Excitotoxicity: Perspectives based on NMDA receptor subtypes
    • D.R. Lynch, and R.P. Guttmann Excitotoxicity: perspectives based on NMDA receptor subtypes J. Pharmacol. Exp. Ther. 300 2002 717 723
    • (2002) J. Pharmacol. Exp. Ther. , vol.300 , pp. 717-723
    • Lynch, D.R.1    Guttmann, R.P.2
  • 41
    • 0024383915 scopus 로고
    • Carbohydrate and glycoprotein specificity of two endogenous cerebellar lectins
    • P. Marschal, A. Reeber, J.R. Neeser, G. Vincendon, and J.P. Zanetta Carbohydrate and glycoprotein specificity of two endogenous cerebellar lectins Biochimie 71 1989 645 653
    • (1989) Biochimie , vol.71 , pp. 645-653
    • Marschal, P.1    Reeber, A.2    Neeser, J.R.3    Vincendon, G.4    Zanetta, J.P.5
  • 42
    • 0344457344 scopus 로고    scopus 로고
    • Glycosylation of proteins during a critical time window is necessary for the maintenance of long-term potentiation in the hippocampal CA1 region
    • H. Matthies Jr., J. Kretlow, H. Matthies, K.H. Smalla, S. Staak, and M. Krug Glycosylation of proteins during a critical time window is necessary for the maintenance of long-term potentiation in the hippocampal CA1 region Neuroscience 91 1999 75 183
    • (1999) Neuroscience , vol.91 , pp. 75-183
    • Matthies, Jr.H.1    Kretlow, J.2    Matthies, H.3    Smalla, K.H.4    Staak, S.5    Krug, M.6
  • 43
    • 0034065936 scopus 로고    scopus 로고
    • Glutamate as a neurotransmitter in the brain: Review of physiology and pathology
    • B.S. Meldrum Glutamate as a neurotransmitter in the brain: review of physiology and pathology J. Nutr. 130 2000 1007 1015
    • (2000) J. Nutr. , vol.130 , pp. 1007-1015
    • Meldrum, B.S.1
  • 44
    • 50649090457 scopus 로고    scopus 로고
    • GMP prevents excitotoxicity mediated by NMDA receptor activation but not by reversal activity of glutamate transporters in rat hippocampal slices
    • S. Molz, T. Dal-Cim, H. Decker, and C.I. Tasca GMP prevents excitotoxicity mediated by NMDA receptor activation but not by reversal activity of glutamate transporters in rat hippocampal slices Brain Res. 22 2008 113 120
    • (2008) Brain Res. , vol.22 , pp. 113-120
    • Molz, S.1    Dal-Cim, T.2    Decker, H.3    Tasca, C.I.4
  • 45
    • 36948998562 scopus 로고    scopus 로고
    • Glutamate induced toxicity in hippocampal slices involves apoptotic features and-p38MAPK signaling
    • S. Molz, H. Decker, T. Dal-Cim, C. Cremonez, F.M. Cordova, R.B. Leal, and C.I. Tasca Glutamate induced toxicity in hippocampal slices involves apoptotic features and-p38MAPK signaling Neurochem. Res. 33 2008 27 36
    • (2008) Neurochem. Res. , vol.33 , pp. 27-36
    • Molz, S.1    Decker, H.2    Dal-Cim, T.3    Cremonez, C.4    Cordova, F.M.5    Leal, R.B.6    Tasca, C.I.7
  • 46
    • 79960049379 scopus 로고    scopus 로고
    • Neuroprotective effect of guanosine against glutamate-induced cell death in rat hippocampal slices is mediated by the phosphatidylinositol-3 kinase/Akt/glycogen synthase kinase 3β pathway activation and inducible nitric oxide synthase inhibition
    • S. Molz, T. Dal-Cim, J. Budni, M.D. Martín-de-Saavedra, J. Egea, A. Romero, L. del Barrio, A.L. Rodrigues, M.G. López, and C.I. Tasca Neuroprotective effect of guanosine against glutamate-induced cell death in rat hippocampal slices is mediated by the phosphatidylinositol-3 kinase/Akt/glycogen synthase kinase 3β pathway activation and inducible nitric oxide synthase inhibition J. Neurosci. Res. 89 2011 1400 1408
    • (2011) J. Neurosci. Res. , vol.89 , pp. 1400-1408
    • Molz, S.1    Dal-Cim, T.2    Budni, J.3    Martín-De-Saavedra, M.D.4    Egea, J.5    Romero, A.6    Del Barrio, L.7    Rodrigues, A.L.8    López, M.G.9    Tasca, C.I.10
  • 47
    • 0000926728 scopus 로고
    • Lectin from Canavalia brasiliensis: Isolation, charaterizatin and behavior during germination
    • R.A. Moreira, and B.S. Cavada Lectin from Canavalia brasiliensis: isolation, charaterizatin and behavior during germination Biol. Plant. (Praha) 26 1984 113 120
    • (1984) Biol. Plant. (Praha) , vol.26 , pp. 113-120
    • Moreira, R.A.1    Cavada, B.S.2
  • 48
    • 0027715150 scopus 로고
    • Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A
    • K.M. Partin, D.K. Patneau, C.A. Winters, M.L. Mayer, and A. Buonanno Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A Neuron 11 1993 1069 1082
    • (1993) Neuron , vol.11 , pp. 1069-1082
    • Partin, K.M.1    Patneau, D.K.2    Winters, C.A.3    Mayer, M.L.4    Buonanno, A.5
  • 49
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • G.L. Peterson A simplification of the protein assay method of Lowry et al. which is more generally applicable Anal. Biochem. 83 1977 346 356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 51
    • 78650699630 scopus 로고    scopus 로고
    • Galectin-1 attenuates astrogliosis-associated injuries and improves recovery of rats following focal cerebral ischemia
    • W.S. Qu, Y.H. Wang, J.F. Ma, D.S. Tian, Q. Zhang, D.J. Pan, Z.Y. Yu, M.J. Xie, J.P. Wang, and W. Wang Galectin-1 attenuates astrogliosis-associated injuries and improves recovery of rats following focal cerebral ischemia J. Neurochem. 116 2011 217 226
    • (2011) J. Neurochem. , vol.116 , pp. 217-226
    • Qu, W.S.1    Wang, Y.H.2    Ma, J.F.3    Tian, D.S.4    Zhang, Q.5    Pan, D.J.6    Yu, Z.Y.7    Xie, M.J.8    Wang, J.P.9    Wang, W.10
  • 52
    • 0014050604 scopus 로고
    • Electron microscope observations on the carbohydrate-rich cell coat present at the surface of cells in the rat
    • A. Rambourg, and C.P. Leblond Electron microscope observations on the carbohydrate-rich cell coat present at the surface of cells in the rat J. Cell Biol. 32 1967 27 53
    • (1967) J. Cell Biol. , vol.32 , pp. 27-53
    • Rambourg, A.1    Leblond, C.P.2
  • 53
    • 0029847118 scopus 로고    scopus 로고
    • Excitotoxicity hypothesis
    • J.D. Rothstein Excitotoxicity hypothesis Neurology 47 4 Suppl. 2 1996 19 25
    • (1996) Neurology , vol.47 , Issue.4 SUPPL. 2 , pp. 19-25
    • Rothstein, J.D.1
  • 55
    • 0030995894 scopus 로고    scopus 로고
    • The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A
    • J. Sanz-Aparicio, J. Hermoso, T.B. Grangeiro, J.J. Calvete, and B.S. Cavada The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A FEBS Lett. 405 1997 114 118
    • (1997) FEBS Lett. , vol.405 , pp. 114-118
    • Sanz-Aparicio, J.1    Hermoso, J.2    Grangeiro, T.B.3    Calvete, J.J.4    Cavada, B.S.5
  • 56
    • 84887024919 scopus 로고
    • Concanavalin A reduces habituation in the tectum of the frog
    • W.J. Scherer, and S.B. Udin Concanavalin A reduces habituation in the tectum of the frog Brain Res. 405 1994 114 118
    • (1994) Brain Res. , vol.405 , pp. 114-118
    • Scherer, W.J.1    Udin, S.B.2
  • 57
    • 0030957325 scopus 로고    scopus 로고
    • Glutamate, but not dopamine, stimulates stress-activated protein kinase and AP-1-mediated transcription in striatal neurons
    • M.A. Schwarzschild, R.L. Cole, and S.E. Hyman Glutamate, but not dopamine, stimulates stress-activated protein kinase and AP-1-mediated transcription in striatal neurons J. Neurosci. 17 1997 3455 3466
    • (1997) J. Neurosci. , vol.17 , pp. 3455-3466
    • Schwarzschild, M.A.1    Cole, R.L.2    Hyman, S.E.3
  • 58
    • 84864871552 scopus 로고    scopus 로고
    • Hydrogen peroxide attenuates the prosurvival signaling of insulin-like growth factor-1 through two pathways
    • C. Sun, D. Wang, and W. Zheng Hydrogen peroxide attenuates the prosurvival signaling of insulin-like growth factor-1 through two pathways Neuroreport 23 2012 768 773
    • (2012) Neuroreport , vol.23 , pp. 768-773
    • Sun, C.1    Wang, D.2    Zheng, W.3
  • 59
    • 2942550646 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in synaptic plasticity and memory
    • J.D. Sweatt Mitogen-activated protein kinases in synaptic plasticity and memory Curr. Opin. Neurobiol. 14 2004 1 7
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 1-7
    • Sweatt, J.D.1
  • 60
    • 1342289413 scopus 로고    scopus 로고
    • MAPK cascade signalling and synaptic plasticity
    • G.M. Thomas, and R.L. Huganir MAPK cascade signalling and synaptic plasticity Nat. Rev. Neurosci. 5 2004 173 183
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 173-183
    • Thomas, G.M.1    Huganir, R.L.2
  • 61
    • 33748295795 scopus 로고    scopus 로고
    • Insulin signaling in the central nervous system: Learning to survive
    • L.P. Van der Heide, G.M. Ramakers, and M.P. Smidt Insulin signaling in the central nervous system: learning to survive Prog. Neurobiol. 79 2006 205 221
    • (2006) Prog. Neurobiol. , vol.79 , pp. 205-221
    • Van Der Heide, L.P.1    Ramakers, G.M.2    Smidt, M.P.3
  • 62
    • 2342469986 scopus 로고    scopus 로고
    • Neurodegenerative and physiological actions of c-Jun N-terminal kinases in the mammalian brain
    • V. Waetzig, and T. Herdegen Neurodegenerative and physiological actions of c-Jun N-terminal kinases in the mammalian brain Neurosci. Lett. 6 361 2004 64 67
    • (2004) Neurosci. Lett. , vol.6 , Issue.361 , pp. 64-67
    • Waetzig, V.1    Herdegen, T.2
  • 64
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • W. Wong, and J.D. Scott AKAP signalling complexes: focal points in space and time Nat. Rev. Mol. Cell Biol. 5 2004 959 970
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 959-970
    • Wong, W.1    Scott, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.