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Volumn 288, Issue 17, 2013, Pages 12353-12365

A calcineurin docking motif (LXVP) in dynamin-related protein 1 contributes to mitochondrial fragmentation and ischemic neuronal injury

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY PRECIPITATION; DEPHOSPHORYLATIONS; ISCHEMIC STROKES; ISOTHERMAL TITRATION CALORIMETRY; MITOCHONDRIAL FRAGMENTATION; MITOCHONDRIAL PROTEIN; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN KINASE;

EID: 84876942158     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.459677     Document Type: Article
Times cited : (62)

References (73)
  • 1
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li, Z., Okamoto, K., Hayashi, Y., and Sheng, M. (2004) The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 119, 873-887
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 3
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes, L. C., Di Benedetto, G., and Scorrano, L. (2011) During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat Cell Biol. 13, 589-598
    • (2011) Nat Cell Biol. , vol.13 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 4
    • 80155137546 scopus 로고    scopus 로고
    • PKA/AKAP1 and PP2A/Bβ2 regulate neuronal morphogenesis via Drp1 phosphorylation and mitochondrial bioenergetics
    • Dickey, A. S., and Strack, S. (2011) PKA/AKAP1 and PP2A/Bβ2 regulate neuronal morphogenesis via Drp1 phosphorylation and mitochondrial bioenergetics. J. Neurosci. 31, 15716-15726
    • (2011) J. Neurosci. , vol.31 , pp. 15716-15726
    • Dickey, A.S.1    Strack, S.2
  • 8
    • 77951096150 scopus 로고    scopus 로고
    • Mitochondrial dynamics, fusion, fission, movement, and mitophagy, in neurodegenerative diseases
    • Chen, H., and Chan, D. C. (2009) Mitochondrial dynamics, fusion, fission, movement, and mitophagy, in neurodegenerative diseases. Hum. Mol. Genet. 18, R169-R176
    • (2009) Hum. Mol. Genet. , vol.18
    • Chen, H.1    Chan, D.C.2
  • 10
    • 84872686195 scopus 로고    scopus 로고
    • Cell signaling and mitochondrial dynamics. Implications for neuronal function and neurodegenerative disease
    • Wilson, T. J., Slupe, A. M., and Strack, S. (2013) Cell signaling and mitochondrial dynamics. Implications for neuronal function and neurodegenerative disease. Neurobiol. Dis. 51, 13-26
    • (2013) Neurobiol. Dis. , vol.51 , pp. 13-26
    • Wilson, T.J.1    Slupe, A.M.2    Strack, S.3
  • 11
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs, J. T., and Strack, S. (2007) Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBORep. 8, 939-944
    • (2007) EMBORep. , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 12
    • 34547611925 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
    • Chang, C. R., and Blackstone, C. (2007) Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J. Biol. Chem. 282, 21583-21587
    • (2007) J. Biol. Chem. , vol.282 , pp. 21583-21587
    • Chang, C.R.1    Blackstone, C.2
  • 14
    • 84858434492 scopus 로고    scopus 로고
    • Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain
    • Strack, S., and Cribbs, J. T. (2012) Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain. J. Biol. Chem. 287, 10990-11001
    • (2012) J. Biol. Chem. , vol.287 , pp. 10990-11001
    • Strack, S.1    Cribbs, J.T.2
  • 16
    • 84872782873 scopus 로고    scopus 로고
    • N-terminal phosphorylation of protein phosphatase 2A/Bβ32 regulates translocation to mitochondria, dynamin-related protein 1 dephosphorylation, and neuronal survival
    • Merrill, R. A., Slupe, A. M., and Strack, S. (2013) N-terminal phosphorylation of protein phosphatase 2A/Bβ32 regulates translocation to mitochondria, dynamin-related protein 1 dephosphorylation, and neuronal survival. FEBS J. 280, 662-673
    • (2013) FEBS J. , vol.280 , pp. 662-673
    • Merrill, R.A.1    Slupe, A.M.2    Strack, S.3
  • 17
    • 60249095382 scopus 로고    scopus 로고
    • The spinocerebellar ataxia 12 gene product and protein phosphatase 2A regulatory subunit Bβ32 antagonizes neuronal survival by promoting mitochondrial fission
    • Dagda, R. K., Merrill, R. A., Cribbs, J. T., Chen, Y., Hell, J. W., Usachev, Y. M., and Strack, S. (2008) The spinocerebellar ataxia 12 gene product and protein phosphatase 2A regulatory subunit Bβ32 antagonizes neuronal survival by promoting mitochondrial fission. J. Biol. Chem. 283, 36241-36248
    • (2008) J. Biol. Chem. , vol.283 , pp. 36241-36248
    • Dagda, R.K.1    Merrill, R.A.2    Cribbs, J.T.3    Chen, Y.4    Hell, J.W.5    Usachev, Y.M.6    Strack, S.7
  • 18
    • 78651232227 scopus 로고    scopus 로고
    • MiR-499 regulates mitochondrial dynamics by targeting calcineurin and dynamin-related protein-1
    • Wang, J. X., Jiao, J. Q., Li, Q., Long, B., Wang, K., Liu, J. P., Li, Y. R., and Li, P. F. (2011) miR-499 regulates mitochondrial dynamics by targeting calcineurin and dynamin-related protein-1. Nat. Med. 17, 71-78
    • (2011) Nat. Med. , vol.17 , pp. 71-78
    • Wang, J.X.1    Jiao, J.Q.2    Li, Q.3    Long, B.4    Wang, K.5    Liu, J.P.6    Li, Y.R.7    Li, P.F.8
  • 20
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin. Form and function
    • Rusnak, F., and Mertz, P. (2000) Calcineurin. Form and function. Physiol. Rev. 80, 1483-1521
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 21
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulinstimulated protein phosphatase, calcineurin
    • Klee, C. B., Ren, H., and Wang, X. (1998) Regulation of the calmodulinstimulated protein phosphatase, calcineurin. J. Biol. Chem. 273, 13367-13370
    • (1998) J. Biol. Chem. , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 23
    • 79551474570 scopus 로고    scopus 로고
    • Recognition of β-calcineurin by the domains of calmodulin. Thermodynamic and structure evidence for distinct roles
    • O'Donnell, S. E., Yu, L., Fowler, C. A., and Shea, M. A. (2011) Recognition of β-calcineurin by the domains of calmodulin. Thermodynamic and structure evidence for distinct roles. Proteins Struct. Funct. Bioinformat. 79, 765-786
    • (2011) Proteins Struct. Funct. Bioinformat. , vol.79 , pp. 765-786
    • O'Donnell, S.E.1    Yu, L.2    Fowler, C.A.3    Shea, M.A.4
  • 25
    • 77449110096 scopus 로고    scopus 로고
    • Cracking the phosphatase code. Docking interactions determine substrate specificity
    • Roy, J., and Cyert, M. S. (2009) Cracking the phosphatase code. Docking interactions determine substrate specificity. Sci. Signal 2, re9
    • (2009) Sci. Signal , vol.2
    • Roy, J.1    Cyert, M.S.2
  • 26
    • 0030574021 scopus 로고    scopus 로고
    • Calcineurin and mitochondrial function in glutamate-induced neuronal cell death
    • Ankarcrona, M., Dypbukt, J. M., Orrenius, S., and Nicotera, P. (1996) Calcineurin and mitochondrial function in glutamate-induced neuronal cell death. FEBS Lett. 394, 321-324
    • (1996) FEBS Lett. , vol.394 , pp. 321-324
    • Ankarcrona, M.1    Dypbukt, J.M.2    Orrenius, S.3    Nicotera, P.4
  • 29
    • 30644461158 scopus 로고    scopus 로고
    • Calcium-and metabolic state-dependent modulation of the voltage-dependent Kv2.1 channel regulates neuronal excitability in response to ischemia
    • Misonou, H., Mohapatra, D. P., Menegola, M., and Trimmer, J. S. (2005) Calcium-and metabolic state-dependent modulation of the voltage-dependent Kv2.1 channel regulates neuronal excitability in response to ischemia. J. Neurosci. 25, 11184-11193
    • (2005) J. Neurosci. , vol.25 , pp. 11184-11193
    • Misonou, H.1    Mohapatra, D.P.2    Menegola, M.3    Trimmer, J.S.4
  • 30
    • 0031912196 scopus 로고    scopus 로고
    • N-Methyl-D-aspartate receptor desensitisation is neuroprotective by inhibiting glutamate-induced apoptotic-like death
    • Wood, A. M., and Bristow, D. R. (1998) N-Methyl-D-aspartate receptor desensitisation is neuroprotective by inhibiting glutamate-induced apoptotic-like death. J. Neurochem. 70, 677-687
    • (1998) J. Neurochem. , vol.70 , pp. 677-687
    • Wood, A.M.1    Bristow, D.R.2
  • 31
    • 28444487509 scopus 로고    scopus 로고
    • Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death
    • Arnoult, D., Rismanchi, N., Grodet, A., Roberts, R. G., Seeburg, D. P., Estaquier, J., Sheng, M., and Blackstone, C. (2005) Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death. Curr. Biol. 15, 2112-2118
    • (2005) Curr. Biol. , vol.15 , pp. 2112-2118
    • Arnoult, D.1    Rismanchi, N.2    Grodet, A.3    Roberts, R.G.4    Seeburg, D.P.5    Estaquier, J.6    Sheng, M.7    Blackstone, C.8
  • 34
    • 0022970569 scopus 로고
    • Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity
    • Blumenthal, D. K., Takio, K., Hansen, R. S., and Krebs, E. G. (1986) Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity. J. Biol. Chem. 261, 8140-8145
    • (1986) J. Biol. Chem. , vol.261 , pp. 8140-8145
    • Blumenthal, D.K.1    Takio, K.2    Hansen, R.S.3    Krebs, E.G.4
  • 35
    • 66349086505 scopus 로고    scopus 로고
    • Domain architecture of the regulators of calcineurin (RCANs) and identification of a divergent RCAN in yeast
    • Mehta, S., Li, H, Hogan, P. G., and Cunningham, K. W. (2009) Domain architecture of the regulators of calcineurin (RCANs) and identification of a divergent RCAN in yeast. Mol. Cell Biol. 29, 2777-2793
    • (2009) Mol. Cell Biol. , vol.29 , pp. 2777-2793
    • Mehta, S.1    Li, H.2    Hogan, P.G.3    Cunningham, K.W.4
  • 36
    • 0032584656 scopus 로고    scopus 로고
    • SAP97 is associated with the α-amino-3-hydroxy-5-methylisoxazole-4- propionic acid receptor GluR1 subunit
    • Leonard, A. S., Davare, M. A., Horne, M. C., Garner, C. C, and Hell, J. W. (1998) SAP97 is associated with the α-amino-3-hydroxy-5- methylisoxazole-4-propionic acid receptor GluR1 subunit. J. Biol. Chem. 273, 19518-19524
    • (1998) J. Biol. Chem. , vol.273 , pp. 19518-19524
    • Leonard, A.S.1    Davare, M.A.2    Horne, M.C.3    Garner, C.C.4    Hell, J.W.5
  • 37
    • 11144247943 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 phosphorylates serine 31 of tyrosine hydroxylase and regulates its stability
    • Moy, L. Y., and Tsai, L. H. (2004) Cyclin-dependent kinase 5 phosphorylates serine 31 of tyrosine hydroxylase and regulates its stability. J. Biol. Chem. 279, 54487-54493
    • (2004) J. Biol. Chem. , vol.279 , pp. 54487-54493
    • Moy, L.Y.1    Tsai, L.H.2
  • 38
    • 0030890757 scopus 로고    scopus 로고
    • Overexpression and purification of human calcineurin α from Escherichia coli and assessment of catalytic functions of residues surrounding the binuclear metal center
    • Mondragon, A., Griffith, E. C., Sun, L., Xiong, F., Armstrong, C, and Liu, J. O. (1997) Overexpression and purification of human calcineurin α from Escherichia coli and assessment of catalytic functions of residues surrounding the binuclear metal center. Biochemistry 36, 4934-4942
    • (1997) Biochemistry , vol.36 , pp. 4934-4942
    • Mondragon, A.1    Griffith, E.C.2    Sun, L.3    Xiong, F.4    Armstrong, C.5    Liu, J.O.6
  • 39
    • 0028927330 scopus 로고
    • 2+ binding to calmodulin. Proteolytic susceptibility of E31 and E87 indicates interdomain interactions
    • 2+ binding to calmodulin. Proteolytic susceptibility of E31 and E87 indicates interdomain interactions. Biochemistry 34, 1179-1196
    • (1995) Biochemistry , vol.34 , pp. 1179-1196
    • Pedigo, S.1    Shea, M.A.2
  • 40
    • 77957707285 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatase assays
    • McAvoy, T., and Nairn, A. C (2010) Serine/threonine protein phosphatase assays. Curr. Protoc. Mol. Bol. 92, 18.18.1-18.18.11
    • (2010) Curr. Protoc. Mol. Bol. , vol.92 , pp. 18181-181811
    • McAvoy, T.1    Nairn, A.C.2
  • 41
    • 79961135005 scopus 로고    scopus 로고
    • R Development Core Team, R Foundation for Statistical Computing, Vienna, Austria
    • R Development Core Team (2011) R: A Language and Environment for Statistical Computing, R Foundation for Statistical Computing, Vienna, Austria
    • (2011) R: A Language and Environment for Statistical Computing
  • 42
    • 0016291269 scopus 로고
    • Statistical quality control and routine data processing for radioimmunoassays and immunoradiometric assays
    • Rodbard, D. (1974) Statistical quality control and routine data processing for radioimmunoassays and immunoradiometric assays. Clin. Chem. 20, 1255-1270
    • (1974) Clin. Chem. , vol.20 , pp. 1255-1270
    • Rodbard, D.1
  • 43
    • 65449187907 scopus 로고    scopus 로고
    • Functional characterization of phosphorylation sites in dynamin-related protein 1
    • Cribbs, J. T., and Strack, S. (2009) Functional characterization of phosphorylation sites in dynamin-related protein 1. Methods Enzymol. 457, 231-253
    • (2009) Methods Enzymol. , vol.457 , pp. 231-253
    • Cribbs, J.T.1    Strack, S.2
  • 44
    • 79953019314 scopus 로고    scopus 로고
    • The mitochondrial inner membrane GTPase, optic atrophy 1 (Opa1), restores mitochondrial morphology and promotes neuronal survival following excitotoxicity
    • Jahani-Asl, A., Pilon-Larose, K., Xu, W., MacLaurin, J. G., Park, D. S., McBride, H. M., and Slack, R. S. (2011) The mitochondrial inner membrane GTPase, optic atrophy 1 (Opa1), restores mitochondrial morphology and promotes neuronal survival following excitotoxicity. J. Biol. Chem. 286, 4772-4782
    • (2011) J. Biol. Chem. , vol.286 , pp. 4772-4782
    • Jahani-Asl, A.1    Pilon-Larose, K.2    Xu, W.3    MacLaurin, J.G.4    Park, D.S.5    McBride, H.M.6    Slack, R.S.7
  • 46
    • 77953854247 scopus 로고    scopus 로고
    • Drp1 dephosphorylation in ATP depletion-induced mitochondrial injury and tubular cell apoptosis
    • Cho, S.-G., Du, Q., Huang, S., and Dong, Z. (2010) Drp1 dephosphorylation in ATP depletion-induced mitochondrial injury and tubular cell apoptosis. Am. J. Physiol. Renal Physiol. 299, F199-F206
    • (2010) Am. J. Physiol. Renal Physiol. , vol.299
    • Cho, S.-G.1    Du, Q.2    Huang, S.3    Dong, Z.4
  • 47
    • 63149106832 scopus 로고    scopus 로고
    • Differential cell death regulation between adult-unloaded and aged rat soleus muscle
    • Ogata, T., Machida, S., Oishi, Y., Higuchi, M., and Muraoka, I. (2009) Differential cell death regulation between adult-unloaded and aged rat soleus muscle. Mech. Ageing Dev. 130, 328-336
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 328-336
    • Ogata, T.1    Machida, S.2    Oishi, Y.3    Higuchi, M.4    Muraoka, I.5
  • 48
    • 79151468994 scopus 로고    scopus 로고
    • Interaction of calcineurin with substrates and targeting proteins
    • Li, H., Rao, A., and Hogan, P. G. (2011) Interaction of calcineurin with substrates and targeting proteins. Trends Cell Biol. 21, 91-103
    • (2011) Trends Cell Biol. , vol.21 , pp. 91-103
    • Li, H.1    Rao, A.2    Hogan, P.G.3
  • 50
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • Taguchi, N., Ishihara, N, Jofuku, A., Oka, T., and Mihara, K. (2007) Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J. Biol. Chem. 282, 11521-11529
    • (2007) J. Biol. Chem. , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 51
    • 82755163057 scopus 로고    scopus 로고
    • Determinants for substrate specificity of protein phosphatase 2A
    • Slupe, A. M., Merrill, R. A., and Strack, S. (2011) Determinants for substrate specificity of protein phosphatase 2A. Enzyme Res. 2011, 398751
    • (2011) Enzyme Res. , vol.2011 , pp. 398751
    • Slupe, A.M.1    Merrill, R.A.2    Strack, S.3
  • 53
    • 0037421222 scopus 로고    scopus 로고
    • Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy
    • Oliveria, S. F., Gomez, L. L., and DellAcqua, M. L. (2003) Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy. J. Cell Biol. 160, 101-112
    • (2003) J. Cell Biol. , vol.160 , pp. 101-112
    • Oliveria, S.F.1    Gomez, L.L.2    DellAcqua, M.L.3
  • 56
    • 67449164361 scopus 로고    scopus 로고
    • KSR2 is a calcineurin substrate that promotes ERK cascade activation in response to calcium signals
    • Dougherty, M. K., Ritt, D. A., Zhou, M., Specht, S. I., Monson, D. M., Veenstra, T. D., and Morrison, D. K. (2009) KSR2 is a calcineurin substrate that promotes ERK cascade activation in response to calcium signals. Mol. Cell 34, 652-662
    • (2009) Mol. Cell , vol.34 , pp. 652-662
    • Dougherty, M.K.1    Ritt, D.A.2    Zhou, M.3    Specht, S.I.4    Monson, D.M.5    Veenstra, T.D.6    Morrison, D.K.7
  • 59
    • 0027937489 scopus 로고
    • Immunophilins mediate the neuroprotective effects of FK506 in focal cerebral ischaemia
    • Sharkey, J., and Butcher, S. P. (1994) Immunophilins mediate the neuroprotective effects of FK506 in focal cerebral ischaemia. Nature 371, 336-339
    • (1994) Nature , vol.371 , pp. 336-339
    • Sharkey, J.1    Butcher, S.P.2
  • 60
    • 0033019790 scopus 로고    scopus 로고
    • Calcineurin inhibitors FK506 and SDZ ASM 981 alleviate the outcomeoffocal cerebral ischemic/reperfusion injury
    • Bochelen, D., Rudin, M., and Sauter, A. (1999) Calcineurin inhibitors FK506 and SDZ ASM 981 alleviate the outcomeoffocal cerebral ischemic/reperfusion injury. J. Pharmacol. Exp. Ther. 288, 653-659
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 653-659
    • Bochelen, D.1    Rudin, M.2    Sauter, A.3
  • 61
    • 0037424434 scopus 로고    scopus 로고
    • Neuroprotective action of tacrolimus (FK506) in focal and global cerebral ischemia in rodents. Dose dependency, therapeutic time window and long-term efficacy
    • Furuichi, Y., Katsuta, K., Maeda, M., Ueyama, N., Moriguchi, A., Matsuoka, N., Goto, T., and Yanagihara, T. (2003) Neuroprotective action of tacrolimus (FK506) in focal and global cerebral ischemia in rodents. Dose dependency, therapeutic time window and long-term efficacy. Brain Res. 965, 137-145
    • (2003) Brain Res. , vol.965 , pp. 137-145
    • Furuichi, Y.1    Katsuta, K.2    Maeda, M.3    Ueyama, N.4    Moriguchi, A.5    Matsuoka, N.6    Goto, T.7    Yanagihara, T.8
  • 62
    • 0141994812 scopus 로고    scopus 로고
    • Tacrolimus, a potential neuroprotective agent, ameliorates ischemic brain damage and neurologic deficits after focal cerebral ischemia in nonhuman primates
    • Furuichi, Y., Maeda, M., Moriguchi, A., Sawamoto, T., Kawamura, A., Matsuoka, N., Mutoh, S., and Yanagihara, T. (2003) Tacrolimus, a potential neuroprotective agent, ameliorates ischemic brain damage and neurologic deficits after focal cerebral ischemia in nonhuman primates. J. Cereb. Blood Flow Metab. 23, 1183-1194
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 1183-1194
    • Furuichi, Y.1    Maeda, M.2    Moriguchi, A.3    Sawamoto, T.4    Kawamura, A.5    Matsuoka, N.6    Mutoh, S.7    Yanagihara, T.8
  • 63
    • 33847360523 scopus 로고    scopus 로고
    • Therapeutic time window of tacrolimus (FK506) in a nonhuman primate stroke model. Comparison with tissue plasminogen activator
    • Furuichi, Y., Maeda, M., Matsuoka, N., Mutoh, S., and Yanagihara, T. (2007) Therapeutic time window of tacrolimus (FK506) in a nonhuman primate stroke model. Comparison with tissue plasminogen activator. Exp. Neurol. 204, 138-146
    • (2007) Exp. Neurol. , vol.204 , pp. 138-146
    • Furuichi, Y.1    Maeda, M.2    Matsuoka, N.3    Mutoh, S.4    Yanagihara, T.5
  • 66
    • 0041819756 scopus 로고    scopus 로고
    • Glutamate decreases mitochondrial size and movement in primary forebrain neurons
    • Rintoul, G. L., Filiano, A. J., Brocard, J. B., Kress, G. J., and Reynolds, I. J. (2003) Glutamate decreases mitochondrial size and movement in primary forebrain neurons. J. Neurosci. 23, 7881-7888
    • (2003) J. Neurosci. , vol.23 , pp. 7881-7888
    • Rintoul, G.L.1    Filiano, A.J.2    Brocard, J.B.3    Kress, G.J.4    Reynolds, I.J.5
  • 67
    • 33846022729 scopus 로고    scopus 로고
    • Calcium-dependent spontaneously reversible remodeling of brain mitochondria
    • Shalbuyeva, N., Brustovetsky, T., Bolshakov, A., and Brustovetsky, N. (2006) Calcium-dependent spontaneously reversible remodeling of brain mitochondria. J. Biol. Chem. 281, 37547-37558
    • (2006) J. Biol. Chem. , vol.281 , pp. 37547-37558
    • Shalbuyeva, N.1    Brustovetsky, T.2    Bolshakov, A.3    Brustovetsky, N.4
  • 68
    • 77956511129 scopus 로고    scopus 로고
    • Different pathways lead to mitochondrial fragmentation during apoptotic and excitotoxic cell death in primary neurons
    • Young, K. W., Pinon, L. G., Bampton, E. T., and Nicotera, P. (2010) Different pathways lead to mitochondrial fragmentation during apoptotic and excitotoxic cell death in primary neurons. J. Biochem. Mol. Toxicol. 24, 335-341
    • (2010) J. Biochem. Mol. Toxicol. , vol.24 , pp. 335-341
    • Young, K.W.1    Pinon, L.G.2    Bampton, E.T.3    Nicotera, P.4
  • 69
    • 3042595335 scopus 로고    scopus 로고
    • Excitotoxic calcium overload in a subpopulation of mitochondria triggers delayed death in hippocampal neurons
    • Pivovarova, N. B., Nguyen, H. V., Winters, C. A., Brantner, C. A., Smith, C. L., and Andrews, S. B. (2004) Excitotoxic calcium overload in a subpopulation of mitochondria triggers delayed death in hippocampal neurons. J. Neurosci. 24, 5611-5622
    • (2004) J. Neurosci. , vol.24 , pp. 5611-5622
    • Pivovarova, N.B.1    Nguyen, H.V.2    Winters, C.A.3    Brantner, C.A.4    Smith, C.L.5    Andrews, S.B.6
  • 72
    • 84862786010 scopus 로고    scopus 로고
    • Dynamic changes of mitochondrial fusion and fission proteins after transient cerebral ischemia in mice
    • Liu, W., Tian, F., Kurata, T., Morimoto, N., and Abe, K. (2012) Dynamic changes of mitochondrial fusion and fission proteins after transient cerebral ischemia in mice. J. Neurosci. Res. 90, 1183-1189
    • (2012) J. Neurosci. Res. , vol.90 , pp. 1183-1189
    • Liu, W.1    Tian, F.2    Kurata, T.3    Morimoto, N.4    Abe, K.5
  • 73
    • 57649178442 scopus 로고    scopus 로고
    • Oxidative stress and energy crises in neuronal dysfunction
    • Nicholls, D. G. (2008) Oxidative stress and energy crises in neuronal dysfunction. Ann. NY. Acad. Sci. 1147, 53-60
    • (2008) Ann. NY. Acad. Sci. , vol.1147 , pp. 53-60
    • Nicholls, D.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.