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Volumn 130, Issue 3, 2014, Pages 455-466

The voltage-gated calcium channel blocker lomerizine is neuroprotective in motor neurons expressing mutant SOD1, but not TDP-43

Author keywords

amyotrophic lateral sclerosis; FUS; lomerizine; SOD1; TDP 43; voltage gated calcium channel

Indexed keywords

CALCIUM ION; COPPER ZINC SUPEROXIDE DISMUTASE; FUSED IN SARCOMA PROTEIN; GLUTAMIC ACID; LOMERIZINE; MUTANT PROTEIN; TAR DNA BINDING PROTEIN;

EID: 84904565950     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.12738     Document Type: Article
Times cited : (15)

References (65)
  • 1
    • 53049105819 scopus 로고    scopus 로고
    • ALS drug development: Reflections from the past and a way forward
    • Aggarwal S., and, Cudkowicz M., (2008) ALS drug development: reflections from the past and a way forward. Neurotherapeutics 5, 516-527.
    • (2008) Neurotherapeutics , vol.5 , pp. 516-527
    • Aggarwal, S.1    Cudkowicz, M.2
  • 3
    • 0027946813 scopus 로고
    • The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis
    • Alexianu M. E., Ho B.-K., Mohamed A. H., La Bella V., Smith R. G., and, Appel S. H., (1994) The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis. Ann. Neurol. 36, 846-858.
    • (1994) Ann. Neurol. , vol.36 , pp. 846-858
    • Alexianu, M.E.1    Ho, B.-K.2    Mohamed, A.H.3    La Bella, V.4    Smith, R.G.5    Appel, S.H.6
  • 5
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T., Hasegawa M., Akiyama H., et al,. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351, 602-611.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3
  • 6
    • 84872719753 scopus 로고    scopus 로고
    • Calcium channel agonists protect against neuromuscular dysfunction in a genetic model of TDP-43 mutation in ALS
    • Armstrong G. A., and, Drapeau P., (2013) Calcium channel agonists protect against neuromuscular dysfunction in a genetic model of TDP-43 mutation in ALS. J. Neurosci. 33, 1741-1752.
    • (2013) J. Neurosci. , vol.33 , pp. 1741-1752
    • Armstrong, G.A.1    Drapeau, P.2
  • 7
    • 0028920258 scopus 로고
    • Metabolism of lomerizine hydrochloride in rats
    • Awata N., Sakai T., Satomi O., and, Kawashima T., (1995) Metabolism of lomerizine hydrochloride in rats. Yakugaku Zasshi 115, 120-129.
    • (1995) Yakugaku Zasshi , vol.115 , pp. 120-129
    • Awata, N.1    Sakai, T.2    Satomi, O.3    Kawashima, T.4
  • 8
    • 33749989045 scopus 로고    scopus 로고
    • Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis
    • Batulan Z., Taylor D. M., Aarons R. J., Minotti S., Doroudchi M. M., Nalbantoglu J., and, Durham H. D., (2006) Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis. Neurobiol. Dis. 24, 213-225.
    • (2006) Neurobiol. Dis. , vol.24 , pp. 213-225
    • Batulan, Z.1    Taylor, D.M.2    Aarons, R.J.3    Minotti, S.4    Doroudchi, M.M.5    Nalbantoglu, J.6    Durham, H.D.7
  • 9
    • 0034763566 scopus 로고    scopus 로고
    • Parvalbumin overexpression alters immune-mediated increases in intracellular calcium, and delays disease onset in a transgenic model of familial amyotrophic lateral sclerosis
    • Beers D. R., Ho B. K., Siklos L., et al,. (2001) Parvalbumin overexpression alters immune-mediated increases in intracellular calcium, and delays disease onset in a transgenic model of familial amyotrophic lateral sclerosis. J. Neurochem. 79, 499-509.
    • (2001) J. Neurochem. , vol.79 , pp. 499-509
    • Beers, D.R.1    Ho, B.K.2    Siklos, L.3
  • 10
    • 0028097839 scopus 로고
    • A controlled trial of riluzole in amyotrophic lateral sclerosis
    • ALS-Riluzole Study Group.
    • Bensimon G., Lacomblez L., and, Meininger V., and ALS-Riluzole Study Group (1994) A controlled trial of riluzole in amyotrophic lateral sclerosis. N. Engl. J. Med. 330, 585-591.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 585-591
    • Bensimon, G.1    Lacomblez, L.2    Meininger, V.3
  • 12
    • 34247499892 scopus 로고    scopus 로고
    • Mitochondrial dynamics in the regulation of neuronal cell death
    • Cheung E. C., McBride H. M., and, Slack R. S., (2007) Mitochondrial dynamics in the regulation of neuronal cell death. Apoptosis 12, 979-992.
    • (2007) Apoptosis , vol.12 , pp. 979-992
    • Cheung, E.C.1    McBride, H.M.2    Slack, R.S.3
  • 13
    • 34047131622 scopus 로고    scopus 로고
    • 2+ determine motoneuron vulnerability in rat spinal cord in vivo
    • 2+ determine motoneuron vulnerability in rat spinal cord in vivo. Neuropharmacology 52, 1219-1228.
    • (2007) Neuropharmacology , vol.52 , pp. 1219-1228
    • Corona, J.C.1    Tapia, R.2
  • 14
    • 35548991459 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-linked SOD1 mutants perturb fast axonal transport to reduce axonal mitochondria content
    • De Vos K. J., Chapman A. L., Tennant M. E., et al,. (2007) Familial amyotrophic lateral sclerosis-linked SOD1 mutants perturb fast axonal transport to reduce axonal mitochondria content. Hum. Mol. Genet. 16, 2720-2728.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2720-2728
    • De Vos, K.J.1    Chapman, A.L.2    Tennant, M.E.3
  • 16
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham H. D., Roy J., Dong L., and, Figlewicz D. A., (1997) Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56, 523-530.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 17
    • 0028819581 scopus 로고
    • Parvalbumin is a marker of ALS-resistant motor neurons
    • Elliott J. L., and, Snider W. D., (1995) Parvalbumin is a marker of ALS-resistant motor neurons. NeuroReport 6, 449-452.
    • (1995) NeuroReport , vol.6 , pp. 449-452
    • Elliott, J.L.1    Snider, W.D.2
  • 18
    • 0041421277 scopus 로고    scopus 로고
    • Glutamate carboxypeptidase II inhibition protects motor neurons from death in familial amyotrophic lateral sclerosis models
    • Ghadge G. D., Slusher B. S., Bodner A., et al,. (2003) Glutamate carboxypeptidase II inhibition protects motor neurons from death in familial amyotrophic lateral sclerosis models. Proc. Natl Acad. Sci. USA 100, 9554-9559.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9554-9559
    • Ghadge, G.D.1    Slusher, B.S.2    Bodner, A.3
  • 20
    • 79958204001 scopus 로고    scopus 로고
    • The L-type channel antagonist isradipine is neuroprotective in a mouse model of Parkinson's disease
    • Ilijic E., Guzman J. N., and, Surmeier D. J., (2011) The L-type channel antagonist isradipine is neuroprotective in a mouse model of Parkinson's disease. Neurobiol. Dis. 43, 364-371.
    • (2011) Neurobiol. Dis. , vol.43 , pp. 364-371
    • Ilijic, E.1    Guzman, J.N.2    Surmeier, D.J.3
  • 21
    • 34249804780 scopus 로고    scopus 로고
    • Do the effects of long-term lomerizine administration differ with age?
    • Imai N., Konishi T., Serizawa M., and, Okabe T., (2007) Do the effects of long-term lomerizine administration differ with age? Intern. Med. 46, 683-684.
    • (2007) Intern. Med. , vol.46 , pp. 683-684
    • Imai, N.1    Konishi, T.2    Serizawa, M.3    Okabe, T.4
  • 23
    • 79957935715 scopus 로고    scopus 로고
    • Neuroprotection by lomerizine, a prophylactic drug for migraine, against hydrogen peroxide-induced hippocampal neurotoxicity
    • Ishii M., Iizuka R., Kiuchi Y., Mori Y., and, Shimizu S., (2011) Neuroprotection by lomerizine, a prophylactic drug for migraine, against hydrogen peroxide-induced hippocampal neurotoxicity. Mol. Cell. Biochem. 358, 1-11.
    • (2011) Mol. Cell. Biochem. , vol.358 , pp. 1-11
    • Ishii, M.1    Iizuka, R.2    Kiuchi, Y.3    Mori, Y.4    Shimizu, S.5
  • 26
    • 0028888575 scopus 로고
    • Localization of neurocalcin-like immunoreactivity in rat cranial motoneurons and spinal cord interneurons
    • Junttila T., Koistinaho J., Reichardt L., Hidaka H., Okazaki K., and, Pelto-Huikko M., (1995) Localization of neurocalcin-like immunoreactivity in rat cranial motoneurons and spinal cord interneurons. Neurosci. Lett. 183, 100-103.
    • (1995) Neurosci. Lett. , vol.183 , pp. 100-103
    • Junttila, T.1    Koistinaho, J.2    Reichardt, L.3    Hidaka, H.4    Okazaki, K.5    Pelto-Huikko, M.6
  • 27
    • 77950360176 scopus 로고    scopus 로고
    • Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo
    • Kabashi E., Lin L., Tradewell M. L., et al,. (2010) Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo. Hum. Mol. Genet. 19, 671-683.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 671-683
    • Kabashi, E.1    Lin, L.2    Tradewell, M.L.3
  • 28
    • 0038673599 scopus 로고    scopus 로고
    • Human spinal motoneurons express low relative abundance of GluR2 mRNA: An implication for excitotoxicity in ALS
    • Kawahara Y., Kwak S., Sun H., Ito K., Hashida H., Aizawa H., Jeong S. Y., and, Kanazawa I., (2003) Human spinal motoneurons express low relative abundance of GluR2 mRNA: an implication for excitotoxicity in ALS. J. Neurochem. 85, 680-689.
    • (2003) J. Neurochem. , vol.85 , pp. 680-689
    • Kawahara, Y.1    Kwak, S.2    Sun, H.3    Ito, K.4    Hashida, H.5    Aizawa, H.6    Jeong, S.Y.7    Kanazawa, I.8
  • 29
    • 0037381851 scopus 로고    scopus 로고
    • Efficient three-drug cocktail for disease induced by mutant superoxide dismutase
    • Kriz J., Gowing G., and, Julien J. P., (2003) Efficient three-drug cocktail for disease induced by mutant superoxide dismutase. Ann. Neurol. 53, 429-436.
    • (2003) Ann. Neurol. , vol.53 , pp. 429-436
    • Kriz, J.1    Gowing, G.2    Julien, J.P.3
  • 30
    • 0032731637 scopus 로고    scopus 로고
    • ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis
    • Kruman I. I., Pedersen W. A., Springer J. E., and, Mattson M. P., (1999) ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis. Exp. Neurol. 160, 28-39.
    • (1999) Exp. Neurol. , vol.160 , pp. 28-39
    • Kruman, I.I.1    Pedersen, W.A.2    Springer, J.E.3    Mattson, M.P.4
  • 32
    • 15844431408 scopus 로고    scopus 로고
    • Increased persistent Na+ current and its effect on excitability in motoneurones cultured from mutant SOD1 mice
    • Kuo J. J., Siddique T., Fu R., and, Heckman C. J., (2005) Increased persistent Na+ current and its effect on excitability in motoneurones cultured from mutant SOD1 mice. J. Physiol. 563, 843-854.
    • (2005) J. Physiol. , vol.563 , pp. 843-854
    • Kuo, J.J.1    Siddique, T.2    Fu, R.3    Heckman, C.J.4
  • 33
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski T. J., Jr, Bosco D. A., Leclerc A. L., et al,. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323, 1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, Jr.T.J.1    Bosco, D.A.2    Leclerc, A.L.3
  • 34
    • 0032528992 scopus 로고    scopus 로고
    • Endogenous calcium buffering in motoneurones of the nucleus hypoglossus from mouse
    • Lips M. B., and, Keller B. U., (1998) Endogenous calcium buffering in motoneurones of the nucleus hypoglossus from mouse. J. Physiol. 511 (Pt 1), 105-117.
    • (1998) J. Physiol. , vol.511 , Issue.PART 1 , pp. 105-117
    • Lips, M.B.1    Keller, B.U.2
  • 35
    • 68949163080 scopus 로고    scopus 로고
    • Ca2 + -dependent regulation of mitochondrial dynamics by the Miro-Milton complex
    • Liu X., and, Hajnoczky G., (2009) Ca2 + -dependent regulation of mitochondrial dynamics by the Miro-Milton complex. Int. J. Biochem. Cell Biol. 41, 1972-1976.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1972-1976
    • Liu, X.1    Hajnoczky, G.2
  • 36
    • 70449417623 scopus 로고    scopus 로고
    • Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities
    • Magrane J., Hervias I., Henning M. S., Damiano M., Kawamata H., and, Manfredi G., (2009) Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities. Hum. Mol. Genet. 18, 4552-4564.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4552-4564
    • Magrane, J.1    Hervias, I.2    Henning, M.S.3    Damiano, M.4    Kawamata, H.5    Manfredi, G.6
  • 37
    • 84855931735 scopus 로고    scopus 로고
    • Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons
    • Magrane J., Sahawneh M. A., Przedborski S., Estevez A. G., and, Manfredi G., (2012) Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons. J. Neurosci. 32, 229-242.
    • (2012) J. Neurosci. , vol.32 , pp. 229-242
    • Magrane, J.1    Sahawneh, M.A.2    Przedborski, S.3    Estevez, A.G.4    Manfredi, G.5
  • 40
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M., Sampathu D. M., Kwong L. K., et al,. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 41
    • 0142226957 scopus 로고    scopus 로고
    • Alpha-amino-3-hydroxy-5-methyl-isoxazole-4-propionate receptors in spinal cord motor neurons are altered in transgenic mice overexpressing human Cu, Zn superoxide dismutase (Gly(93)->Ala) mutation
    • Pieri M., Gaetti C., Spalloni A., Cavalcanti S., Mercuri N., Bernardi G., Longone P., and, Zona C., (2003) alpha-amino-3-hydroxy-5-methyl-isoxazole-4- propionate receptors in spinal cord motor neurons are altered in transgenic mice overexpressing human Cu, Zn superoxide dismutase (Gly(93)->Ala) mutation. Neuroscience 122, 47-58.
    • (2003) Neuroscience , vol.122 , pp. 47-58
    • Pieri, M.1    Gaetti, C.2    Spalloni, A.3    Cavalcanti, S.4    Mercuri, N.5    Bernardi, G.6    Longone, P.7    Zona, C.8
  • 42
    • 0028947555 scopus 로고
    • Brainstem motoneuron pools that are selectively resistant in amyotrophic lateral sclerosis are preferentially enriched in parvalbumin: Evidence from monkey brainstem for a calcium-mediated mechanism in sporadic ALS
    • Reiner A., Medina L., Figueredo-Cardenas G., and, Anfinson S., (1995) Brainstem motoneuron pools that are selectively resistant in amyotrophic lateral sclerosis are preferentially enriched in parvalbumin: evidence from monkey brainstem for a calcium-mediated mechanism in sporadic ALS. Exp. Neurol. 131, 239-250.
    • (1995) Exp. Neurol. , vol.131 , pp. 239-250
    • Reiner, A.1    Medina, L.2    Figueredo-Cardenas, G.3    Anfinson, S.4
  • 43
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D. R., Siddique T., Patterson D., et al,. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 44
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein J. D., Van Kammen M., Levey A. I., Martin L. J., and, Kuncl R. W., (1995) Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann. Neurol. 38, 73-84.
    • (1995) Ann. Neurol. , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3    Martin, L.J.4    Kuncl, R.W.5
  • 45
    • 0032402093 scopus 로고    scopus 로고
    • Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms
    • Roy J., Minotti S., Dong L., Figlewicz D. A., and, Durham H. D., (1998) Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms. J. Neurosci. 18, 9673-9684.
    • (1998) J. Neurosci. , vol.18 , pp. 9673-9684
    • Roy, J.1    Minotti, S.2    Dong, L.3    Figlewicz, D.A.4    Durham, H.D.5
  • 47
    • 0030026832 scopus 로고    scopus 로고
    • Ultrastructural evidence for altered calcium in motor nerve terminals in amyotropic lateral sclerosis
    • Siklos L., Engelhardt J., Harati Y., Smith R. G., Joo F., and, Appel S. H., (1996) Ultrastructural evidence for altered calcium in motor nerve terminals in amyotropic lateral sclerosis. Ann. Neurol. 39, 203-216.
    • (1996) Ann. Neurol. , vol.39 , pp. 203-216
    • Siklos, L.1    Engelhardt, J.2    Harati, Y.3    Smith, R.G.4    Joo, F.5    Appel, S.H.6
  • 50
    • 84872683148 scopus 로고    scopus 로고
    • Mutant SOD1(G93A) triggers mitochondrial fragmentation in spinal cord motor neurons: Neuroprotection by SIRT3 and PGC-1alpha
    • Song W., Song Y., Kincaid B., Bossy B., and, Bossy-Wetzel E., (2012) Mutant SOD1(G93A) triggers mitochondrial fragmentation in spinal cord motor neurons: neuroprotection by SIRT3 and PGC-1alpha. Neurobiol. Dis. 51, 72-81.
    • (2012) Neurobiol. Dis. , vol.51 , pp. 72-81
    • Song, W.1    Song, Y.2    Kincaid, B.3    Bossy, B.4    Bossy-Wetzel, E.5
  • 51
    • 0032752054 scopus 로고    scopus 로고
    • Reduction of GluR2 RNA editing, a molecular change that increases calcium influx through AMPA receptors, selective in the spinal ventral gray of patients with amyotrophic lateral sclerosis
    • Takuma H., Kwak S., Yoshizawa T., and, Kanazawa I., (1999) Reduction of GluR2 RNA editing, a molecular change that increases calcium influx through AMPA receptors, selective in the spinal ventral gray of patients with amyotrophic lateral sclerosis. Ann. Neurol. 46, 806-815.
    • (1999) Ann. Neurol. , vol.46 , pp. 806-815
    • Takuma, H.1    Kwak, S.2    Yoshizawa, T.3    Kanazawa, I.4
  • 52
    • 5444222849 scopus 로고    scopus 로고
    • Calcium-permeable AMPA receptors promote misfolding of mutant SOD1 protein and development of amyotrophic lateral sclerosis in a transgenic mouse model
    • Tateno M., Sadakata H., Tanaka M., et al,. (2004) Calcium-permeable AMPA receptors promote misfolding of mutant SOD1 protein and development of amyotrophic lateral sclerosis in a transgenic mouse model. Hum. Mol. Genet. 13, 2183-2196.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2183-2196
    • Tateno, M.1    Sadakata, H.2    Tanaka, M.3
  • 53
    • 30344437262 scopus 로고    scopus 로고
    • Glutamate AMPA receptors change in motor neurons of SOD1G93A transgenic mice and their inhibition by a noncompetitive antagonist ameliorates the progression of amytrophic lateral sclerosis-like disease
    • Tortarolo M., Grignaschi G., Calvaresi N., et al,. (2006) Glutamate AMPA receptors change in motor neurons of SOD1G93A transgenic mice and their inhibition by a noncompetitive antagonist ameliorates the progression of amytrophic lateral sclerosis-like disease. J. Neurosci. Res. 83, 134-146.
    • (2006) J. Neurosci. Res. , vol.83 , pp. 134-146
    • Tortarolo, M.1    Grignaschi, G.2    Calvaresi, N.3
  • 54
    • 77957558614 scopus 로고    scopus 로고
    • Calpastatin reduces toxicity of SOD1G93A in a culture model of amyotrophic lateral sclerosis
    • Tradewell M. L., and, Durham H. D., (2010) Calpastatin reduces toxicity of SOD1G93A in a culture model of amyotrophic lateral sclerosis. NeuroReport 21, 976-979.
    • (2010) NeuroReport , vol.21 , pp. 976-979
    • Tradewell, M.L.1    Durham, H.D.2
  • 55
    • 79954633016 scopus 로고    scopus 로고
    • Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: Mechanistic relationship and differential sensitivity to intervention
    • Tradewell M. L., Cooper L., Minotti S., and, Durham H. D., (2011) Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: mechanistic relationship and differential sensitivity to intervention. Neurobiol. Dis. 42, 265-275.
    • (2011) Neurobiol. Dis. , vol.42 , pp. 265-275
    • Tradewell, M.L.1    Cooper, L.2    Minotti, S.3    Durham, H.D.4
  • 56
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • Tradewell M. L., Yu Z., Tibshirani M., Boulanger M.-C., Durham H. D., and, Richard S., (2012) Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum. Mol. Genet. 21, 136-149.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.-C.4    Durham, H.D.5    Richard, S.6
  • 58
    • 0037986558 scopus 로고    scopus 로고
    • The AMPA receptor antagonist NBQX prolongs survival in a transgenic mouse model of amyotrophic lateral sclerosis
    • Van Damme P., Leyssen M., Callewaert G., Robberecht W., and, Van Den B. L., (2003) The AMPA receptor antagonist NBQX prolongs survival in a transgenic mouse model of amyotrophic lateral sclerosis. Neurosci. Lett. 343, 81-84.
    • (2003) Neurosci. Lett. , vol.343 , pp. 81-84
    • Van Damme, P.1    Leyssen, M.2    Callewaert, G.3    Robberecht, W.4    Van Den, B.L.5
  • 59
    • 22244460463 scopus 로고    scopus 로고
    • GluR2 deficiency accelerates motor neuron degeneration in a mouse model of amyotrophic lateral sclerosis
    • Van Damme P., Braeken D., Callewaert G., Robberecht W., and, Van Den B. L., (2005) GluR2 deficiency accelerates motor neuron degeneration in a mouse model of amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 64, 605-612.
    • (2005) J. Neuropathol. Exp. Neurol. , vol.64 , pp. 605-612
    • Van Damme, P.1    Braeken, D.2    Callewaert, G.3    Robberecht, W.4    Van Den, B.L.5
  • 60
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C., Rogelj B., Hortobagyi T., et al,. (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323, 1208-1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3
  • 61
    • 41649086378 scopus 로고    scopus 로고
    • Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria
    • Vande Velde C., Miller T. M., Cashman N. R., and, Cleveland D. W., (2008) Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria. Proc. Natl. Acad. Sci. USA 105, 4022-4027.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4022-4027
    • Vande Velde, C.1    Miller, T.M.2    Cashman, N.R.3    Cleveland, D.W.4
  • 63
    • 0033993642 scopus 로고    scopus 로고
    • AMPA receptor calcium permeability, GluR2 expression, and selective motoneuron vulnerability
    • Vandenberghe W., Robberecht W., and, Brorson J. R., (2000) AMPA receptor calcium permeability, GluR2 expression, and selective motoneuron vulnerability. J. Neurosci. 20, 123-132.
    • (2000) J. Neurosci. , vol.20 , pp. 123-132
    • Vandenberghe, W.1    Robberecht, W.2    Brorson, J.R.3
  • 64
    • 0030789347 scopus 로고    scopus 로고
    • Calcium-permeable α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors: A molecular determinant of selective vulnerability in amyotrophic lateral sclerosis
    • Williams T. L., Day N. C., Ince P. G., Kamboj R. K., and, Shaw P. J., (1997) Calcium-permeable α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors: a molecular determinant of selective vulnerability in amyotrophic lateral sclerosis. Ann. Neurol. 42, 200-207.
    • (1997) Ann. Neurol. , vol.42 , pp. 200-207
    • Williams, T.L.1    Day, N.C.2    Ince, P.G.3    Kamboj, R.K.4    Shaw, P.J.5
  • 65
    • 79954608945 scopus 로고    scopus 로고
    • Emerging targets and treatments in amyotrophic lateral sclerosis
    • Zinman L., and, Cudkowicz M., (2011) Emerging targets and treatments in amyotrophic lateral sclerosis. Lancet Neurol. 10, 481-490.
    • (2011) Lancet Neurol. , vol.10 , pp. 481-490
    • Zinman, L.1    Cudkowicz, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.