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Volumn 8, Issue 5, 2013, Pages

New Model of Action for Mood Stabilizers: Phosphoproteome from Rat Pre-Frontal Cortex Synaptoneurosomal Preparations

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN CYTOPLASMIC 1; ALPHA INTERNEXIN; LITHIUM CHLORIDE; MYOSIN HEAVY CHAIN; MYOSIN HEAVY CHAIN 1; MYOSIN HEAVY CHAIN 2; MYOSIN HEAVY CHAIN 6; NEUROFILAMENT PROTEIN; PALIPERIDONE; TUBULIN; TUBULIN ALPHA 1B CHAIN; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG; VALPROIC ACID;

EID: 84877728682     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052147     Document Type: Article
Times cited : (27)

References (95)
  • 1
    • 0024349489 scopus 로고
    • [Ultrastructure of the synapses of the anterior limbic cortex in schizophrenia]
    • Uranova NA, Aganova EA, (1989) [Ultrastructure of the synapses of the anterior limbic cortex in schizophrenia]. Zh Nevropatol Psikhiatr Im S S Korsakova 89: 56-59.
    • (1989) Zh Nevropatol Psikhiatr Im S S Korsakova , vol.89 , pp. 56-59
    • Uranova, N.A.1    Aganova, E.A.2
  • 2
    • 0031781878 scopus 로고    scopus 로고
    • Superoxide, neuroleptics and the ubiquinone and cytochrome b5 reductases in brain and lymphocytes from normals and schizophrenic patients
    • Whatley SA, Curti D, Das Gupta F, Ferrier IN, Jones S, et al. (1998) Superoxide, neuroleptics and the ubiquinone and cytochrome b5 reductases in brain and lymphocytes from normals and schizophrenic patients. Mol Psychiatry 3: 227-237.
    • (1998) Mol Psychiatry , vol.3 , pp. 227-237
    • Whatley, S.A.1    Curti, D.2    Das Gupta, F.3    Ferrier, I.N.4    Jones, S.5
  • 4
    • 0035280535 scopus 로고    scopus 로고
    • Evidence for a mitochondrial oxidative phosphorylation defect in brains from patients with schizophrenia
    • Maurer I, Zierz S, Moller H, (2001) Evidence for a mitochondrial oxidative phosphorylation defect in brains from patients with schizophrenia. Schizophr Res 48: 125-136.
    • (2001) Schizophr Res , vol.48 , pp. 125-136
    • Maurer, I.1    Zierz, S.2    Moller, H.3
  • 5
    • 57049143140 scopus 로고    scopus 로고
    • Mitochondria in neuroplasticity and neurological disorders
    • Mattson MP, Gleichmann M, Cheng A, (2008) Mitochondria in neuroplasticity and neurological disorders. Neuron 60: 748-766.
    • (2008) Neuron , vol.60 , pp. 748-766
    • Mattson, M.P.1    Gleichmann, M.2    Cheng, A.3
  • 6
    • 51449105218 scopus 로고    scopus 로고
    • Paliperidone as a mood stabilizer: a pre-frontal cortex synaptoneurosomal proteomics comparison with lithium and valproic acid after chronic treatment reveals similarities in protein expression
    • Corena-McLeod MdelP, Oliveros A, Charlesworth C, Madden B, Liang YQ, et al. (2008) Paliperidone as a mood stabilizer: a pre-frontal cortex synaptoneurosomal proteomics comparison with lithium and valproic acid after chronic treatment reveals similarities in protein expression. Brain Res 1233: 8-19.
    • (2008) Brain Res , vol.1233 , pp. 8-19
    • Corena-McLeod, M.P.1    Oliveros, A.2    Charlesworth, C.3    Madden, B.4    Liang, Y.Q.5
  • 7
    • 0035987486 scopus 로고    scopus 로고
    • Proteomics analysis of the neurodegeneration in the brain of tau transgenic mice
    • Tilleman K, Van den Haute C, Geerts H, van Leuven F, Esmans EL, et al. (2002) Proteomics analysis of the neurodegeneration in the brain of tau transgenic mice. Proteomics 2: 656-665.
    • (2002) Proteomics , vol.2 , pp. 656-665
    • Tilleman, K.1    Van den Haute, C.2    Geerts, H.3    van Leuven, F.4    Esmans, E.L.5
  • 8
    • 33749531024 scopus 로고    scopus 로고
    • Rapid isolation of synaptoneurosomes and postsynaptic densities from adult mouse hippocampus
    • Villasana LE, Klann E, Tejada-Simon MV, (2006) Rapid isolation of synaptoneurosomes and postsynaptic densities from adult mouse hippocampus. J Neurosci Methods 158: 30-36.
    • (2006) J Neurosci Methods , vol.158 , pp. 30-36
    • Villasana, L.E.1    Klann, E.2    Tejada-Simon, M.V.3
  • 9
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A, Nesvizhskii AI, Kolker E, Aebersold R, (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 74: 5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 10
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii AI, Keller A, Kolker E, Aebersold R, (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75: 4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 11
    • 77951610387 scopus 로고    scopus 로고
    • Cell adhesion, the backbone of the synapse: "vertebrate" and "invertebrate" perspectives
    • Giagtzoglou N, Ly CV, Bellen HJ, (2009) Cell adhesion, the backbone of the synapse: "vertebrate" and "invertebrate" perspectives. Cold Spring Harb Perspect Biol 1: a003079.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Giagtzoglou, N.1    Ly, C.V.2    Bellen, H.J.3
  • 12
    • 0025885699 scopus 로고
    • Abnormal expression of two microtubule-associated proteins (MAP2 and MAP5) in specific subfields of the hippocampal formation in schizophrenia
    • Arnold SE, Lee VM, Gur RE, Trojanowski JQ, (1991) Abnormal expression of two microtubule-associated proteins (MAP2 and MAP5) in specific subfields of the hippocampal formation in schizophrenia. Proc Natl Acad Sci U S A 88: 10850-10854.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10850-10854
    • Arnold, S.E.1    Lee, V.M.2    Gur, R.E.3    Trojanowski, J.Q.4
  • 14
    • 11444259754 scopus 로고    scopus 로고
    • The neuronal cytoskeleton as a potential therapeutical target in neurodegenerative diseases and schizophrenia
    • Benitez-King G, Ramirez-Rodriguez G, Ortiz L, Meza I, (2004) The neuronal cytoskeleton as a potential therapeutical target in neurodegenerative diseases and schizophrenia. Curr Drug Targets CNS Neurol Disord 3: 515-533.
    • (2004) Curr Drug Targets CNS Neurol Disord , vol.3 , pp. 515-533
    • Benitez-King, G.1    Ramirez-Rodriguez, G.2    Ortiz, L.3    Meza, I.4
  • 15
    • 67650726655 scopus 로고    scopus 로고
    • 2-D DIGE analysis implicates cytoskeletal abnormalities in psychiatric disease
    • English JA, Dicker P, Focking M, Dunn MJ, Cotter DR, (2009) 2-D DIGE analysis implicates cytoskeletal abnormalities in psychiatric disease. Proteomics 9: 3368-3382.
    • (2009) Proteomics , vol.9 , pp. 3368-3382
    • English, J.A.1    Dicker, P.2    Focking, M.3    Dunn, M.J.4    Cotter, D.R.5
  • 16
    • 73449132598 scopus 로고    scopus 로고
    • Neural cytoskeleton capabilities for learning and memory
    • Priel A, Tuszynski JA, Woolf NJ, (2010) Neural cytoskeleton capabilities for learning and memory. J Biol Phys 36: 3-21.
    • (2010) J Biol Phys , vol.36 , pp. 3-21
    • Priel, A.1    Tuszynski, J.A.2    Woolf, N.J.3
  • 17
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck PJ, Saxton WM, (2005) The axonal transport of mitochondria. J Cell Sci 118: 5411-5419.
    • (2005) J Cell Sci , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 18
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris RL, Hollenbeck PJ, (1995) Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J Cell Biol 131: 1315-1326.
    • (1995) J Cell Biol , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 19
    • 0033611672 scopus 로고    scopus 로고
    • Presynaptic mitochondria and the temporal pattern of neurotransmitter release
    • Brodin L, Bakeeva L, Shupliakov O, (1999) Presynaptic mitochondria and the temporal pattern of neurotransmitter release. Philos Trans R Soc Lond B Biol Sci 354: 365-372.
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 365-372
    • Brodin, L.1    Bakeeva, L.2    Shupliakov, O.3
  • 20
    • 8144230701 scopus 로고    scopus 로고
    • The architecture of the active zone in the presynaptic nerve terminal
    • Zhai RG, Bellen HJ, (2004) The architecture of the active zone in the presynaptic nerve terminal. Physiology (Bethesda) 19: 262-270.
    • (2004) Physiology (Bethesda) , vol.19 , pp. 262-270
    • Zhai, R.G.1    Bellen, H.J.2
  • 21
    • 0020550407 scopus 로고
    • Cytoplasmic organization in cerebellar dendritic spines
    • Landis DM, Reese TS, (1983) Cytoplasmic organization in cerebellar dendritic spines. J Cell Biol 97: 1169-1178.
    • (1983) J Cell Biol , vol.97 , pp. 1169-1178
    • Landis, D.M.1    Reese, T.S.2
  • 22
    • 0024595352 scopus 로고
    • The cytoskeletal architecture of the presynaptic terminal and molecular structure of synapsin 1
    • Hirokawa N, Sobue K, Kanda K, Harada A, Yorifuji H, (1989) The cytoskeletal architecture of the presynaptic terminal and molecular structure of synapsin 1. J Cell Biol 108: 111-126.
    • (1989) J Cell Biol , vol.108 , pp. 111-126
    • Hirokawa, N.1    Sobue, K.2    Kanda, K.3    Harada, A.4    Yorifuji, H.5
  • 23
    • 0028708598 scopus 로고
    • Synapsin I, an actin-binding protein regulating synaptic vesicle traffic in the nerve terminal
    • Greengard P, Benfenati F, Valtorta F, (1994) Synapsin I, an actin-binding protein regulating synaptic vesicle traffic in the nerve terminal. Adv Second Messenger Phosphoprotein Res 29: 31-45.
    • (1994) Adv Second Messenger Phosphoprotein Res , vol.29 , pp. 31-45
    • Greengard, P.1    Benfenati, F.2    Valtorta, F.3
  • 24
    • 0028837664 scopus 로고
    • Mapping of synapsin II (SYN2) genes to human chromosome 3p and mouse chromosome 6 band F
    • Li X, Rosahl TW, Sudhof TC, Francke U, (1995) Mapping of synapsin II (SYN2) genes to human chromosome 3p and mouse chromosome 6 band F. Cytogenet Cell Genet 71: 301-305.
    • (1995) Cytogenet Cell Genet , vol.71 , pp. 301-305
    • Li, X.1    Rosahl, T.W.2    Sudhof, T.C.3    Francke, U.4
  • 27
    • 0031776815 scopus 로고    scopus 로고
    • Interaction of synapsin I with actin and SSVs: differential regulation by calmodulin
    • Nicol S, Rahman D, Chan KM, Baines AJ, (1998) Interaction of synapsin I with actin and SSVs: differential regulation by calmodulin. Biochem Soc Trans 26: S110.
    • (1998) Biochem Soc Trans , vol.26
    • Nicol, S.1    Rahman, D.2    Chan, K.M.3    Baines, A.J.4
  • 28
    • 0033681170 scopus 로고    scopus 로고
    • Actin-dependent regulation of neurotransmitter release at central synapses
    • Morales M, Colicos MA, Goda Y, (2000) Actin-dependent regulation of neurotransmitter release at central synapses. Neuron 27: 539-550.
    • (2000) Neuron , vol.27 , pp. 539-550
    • Morales, M.1    Colicos, M.A.2    Goda, Y.3
  • 29
    • 0035977120 scopus 로고    scopus 로고
    • Remodeling of synaptic actin induced by photoconductive stimulation
    • Colicos MA, Collins BE, Sailor MJ, Goda Y, (2001) Remodeling of synaptic actin induced by photoconductive stimulation. Cell 107: 605-616.
    • (2001) Cell , vol.107 , pp. 605-616
    • Colicos, M.A.1    Collins, B.E.2    Sailor, M.J.3    Goda, Y.4
  • 30
    • 0037317392 scopus 로고    scopus 로고
    • Actin has a molecular scaffolding, not propulsive, role in presynaptic function
    • Sankaranarayanan S, Atluri PP, Ryan TA, (2003) Actin has a molecular scaffolding, not propulsive, role in presynaptic function. Nat Neurosci 6: 127-135.
    • (2003) Nat Neurosci , vol.6 , pp. 127-135
    • Sankaranarayanan, S.1    Atluri, P.P.2    Ryan, T.A.3
  • 31
    • 17944375149 scopus 로고    scopus 로고
    • The presynaptic particle web: ultrastructure, composition, dissolution, and reconstitution
    • Phillips GR, Huang JK, Wang Y, Tanaka H, Shapiro L, et al. (2001) The presynaptic particle web: ultrastructure, composition, dissolution, and reconstitution. Neuron 32: 63-77.
    • (2001) Neuron , vol.32 , pp. 63-77
    • Phillips, G.R.1    Huang, J.K.2    Wang, Y.3    Tanaka, H.4    Shapiro, L.5
  • 32
    • 0038360854 scopus 로고    scopus 로고
    • Colocalization of synapsin and actin during synaptic vesicle recycling
    • Bloom O, Evergren E, Tomilin N, Kjaerulff O, Low P, et al. (2003) Colocalization of synapsin and actin during synaptic vesicle recycling. J Cell Biol 161: 737-747.
    • (2003) J Cell Biol , vol.161 , pp. 737-747
    • Bloom, O.1    Evergren, E.2    Tomilin, N.3    Kjaerulff, O.4    Low, P.5
  • 33
    • 0037103032 scopus 로고    scopus 로고
    • Developmentally regulated changes in cellular compartmentation and synaptic distribution of actin in hippocampal neurons
    • Zhang W, Benson DL, (2002) Developmentally regulated changes in cellular compartmentation and synaptic distribution of actin in hippocampal neurons. J Neurosci Res 69: 427-436.
    • (2002) J Neurosci Res , vol.69 , pp. 427-436
    • Zhang, W.1    Benson, D.L.2
  • 34
    • 23244440196 scopus 로고    scopus 로고
    • The actin cytoskeleton: integrating form and function at the synapse
    • Dillon C, Goda Y, (2005) The actin cytoskeleton: integrating form and function at the synapse. Annu Rev Neurosci 28: 25-55.
    • (2005) Annu Rev Neurosci , vol.28 , pp. 25-55
    • Dillon, C.1    Goda, Y.2
  • 35
    • 84860288600 scopus 로고    scopus 로고
    • Structural plasticity of hippocampal mossy fiber synapses as revealed by high-pressure freezing
    • Zhao S, Studer D, Chai X, Graber W, Brose N, et al. (2012) Structural plasticity of hippocampal mossy fiber synapses as revealed by high-pressure freezing. J Comp Neurol.
    • (2012) J Comp Neurol
    • Zhao, S.1    Studer, D.2    Chai, X.3    Graber, W.4    Brose, N.5
  • 36
    • 0026093409 scopus 로고
    • Cytoplasmic architecture of the axon terminal: filamentous strands specifically associated with synaptic vesicles
    • Gotow T, Miyaguchi K, Hashimoto PH, (1991) Cytoplasmic architecture of the axon terminal: filamentous strands specifically associated with synaptic vesicles. Neuroscience 40: 587-598.
    • (1991) Neuroscience , vol.40 , pp. 587-598
    • Gotow, T.1    Miyaguchi, K.2    Hashimoto, P.H.3
  • 38
    • 0019872276 scopus 로고
    • Multiple tubulin forms are expressed by a single neurone
    • Gozes I, Sweadner KJ, (1981) Multiple tubulin forms are expressed by a single neurone. Nature 294: 477-480.
    • (1981) Nature , vol.294 , pp. 477-480
    • Gozes, I.1    Sweadner, K.J.2
  • 39
    • 17944371887 scopus 로고    scopus 로고
    • Mapping susceptibility genes for bipolar disorder: a pharmacogenetic approach based on excellent response to lithium
    • Turecki G, Grof P, Grof E, D'Souza V, Lebuis L, et al. (2001) Mapping susceptibility genes for bipolar disorder: a pharmacogenetic approach based on excellent response to lithium. Mol Psychiatry 6: 570-578.
    • (2001) Mol Psychiatry , vol.6 , pp. 570-578
    • Turecki, G.1    Grof, P.2    Grof, E.3    D'Souza, V.4    Lebuis, L.5
  • 40
    • 64149094887 scopus 로고    scopus 로고
    • Calcineurin and cytoskeleton in low-frequency depression
    • Silverman-Gavrila LB, Charlton MP, (2009) Calcineurin and cytoskeleton in low-frequency depression. J Neurochem 109: 716-732.
    • (2009) J Neurochem , vol.109 , pp. 716-732
    • Silverman-Gavrila, L.B.1    Charlton, M.P.2
  • 41
    • 58149352395 scopus 로고    scopus 로고
    • The proteome of the presynaptic active zone: from docked synaptic vesicles to adhesion molecules and maxi-channels
    • Morciano M, Beckhaus T, Karas M, Zimmermann H, Volknandt W, (2009) The proteome of the presynaptic active zone: from docked synaptic vesicles to adhesion molecules and maxi-channels. J Neurochem 108: 662-675.
    • (2009) J Neurochem , vol.108 , pp. 662-675
    • Morciano, M.1    Beckhaus, T.2    Karas, M.3    Zimmermann, H.4    Volknandt, W.5
  • 42
    • 79955005373 scopus 로고    scopus 로고
    • A role for V-ATPase subunits in synaptic vesicle fusion?
    • El Far O, Seagar M, (2011) A role for V-ATPase subunits in synaptic vesicle fusion? J Neurochem 117: 603-612.
    • (2011) J Neurochem , vol.117 , pp. 603-612
    • El Far, O.1    Seagar, M.2
  • 43
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof TC, (2004) The synaptic vesicle cycle. Annu Rev Neurosci 27: 509-547.
    • (2004) Annu Rev Neurosci , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 44
    • 0347382415 scopus 로고    scopus 로고
    • Specific sorting of the a1 isoform of the V-H+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane
    • Morel N, Dedieu JC, Philippe JM, (2003) Specific sorting of the a1 isoform of the V-H+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane. J Cell Sci 116: 4751-4762.
    • (2003) J Cell Sci , vol.116 , pp. 4751-4762
    • Morel, N.1    Dedieu, J.C.2    Philippe, J.M.3
  • 45
    • 78650236557 scopus 로고    scopus 로고
    • Vesicular ATPase inserted into the plasma membrane of motor terminals by exocytosis alkalinizes cytosolic pH and facilitates endocytosis
    • Zhang Z, Nguyen KT, Barrett EF, David G, (2010) Vesicular ATPase inserted into the plasma membrane of motor terminals by exocytosis alkalinizes cytosolic pH and facilitates endocytosis. Neuron 68: 1097-1108.
    • (2010) Neuron , vol.68 , pp. 1097-1108
    • Zhang, Z.1    Nguyen, K.T.2    Barrett, E.F.3    David, G.4
  • 46
    • 0018477516 scopus 로고
    • Acute effects of lithium on central dopamine and serotonin activity reflected by inhibition of prolactin and growth hormone secretion in the rat
    • Smythe GA, Brandstater JF, Lazarus L, (1979) Acute effects of lithium on central dopamine and serotonin activity reflected by inhibition of prolactin and growth hormone secretion in the rat. Aust J Biol Sci 32: 329-334.
    • (1979) Aust J Biol Sci , vol.32 , pp. 329-334
    • Smythe, G.A.1    Brandstater, J.F.2    Lazarus, L.3
  • 47
    • 79952032110 scopus 로고    scopus 로고
    • The physiology, signaling, and pharmacology of dopamine receptors
    • Beaulieu JM, Gainetdinov RR, (2011) The physiology, signaling, and pharmacology of dopamine receptors. Pharmacol Rev 63: 182-217.
    • (2011) Pharmacol Rev , vol.63 , pp. 182-217
    • Beaulieu, J.M.1    Gainetdinov, R.R.2
  • 49
    • 79955479720 scopus 로고    scopus 로고
    • Regulation of axonal mitochondrial transport and its impact on synaptic transmission
    • Cai Q, Davis ML, Sheng ZH, (2011) Regulation of axonal mitochondrial transport and its impact on synaptic transmission. Neurosci Res 70: 9-15.
    • (2011) Neurosci Res , vol.70 , pp. 9-15
    • Cai, Q.1    Davis, M.L.2    Sheng, Z.H.3
  • 50
    • 35448970057 scopus 로고    scopus 로고
    • Serotonin stimulates mitochondrial transport in hippocampal neurons
    • Chen S, Owens GC, Crossin KL, Edelman DB, (2007) Serotonin stimulates mitochondrial transport in hippocampal neurons. Mol Cell Neurosci 36: 472-483.
    • (2007) Mol Cell Neurosci , vol.36 , pp. 472-483
    • Chen, S.1    Owens, G.C.2    Crossin, K.L.3    Edelman, D.B.4
  • 51
    • 50949084911 scopus 로고    scopus 로고
    • Dopamine inhibits mitochondrial motility in hippocampal neurons
    • Chen S, Owens GC, Edelman DB, (2008) Dopamine inhibits mitochondrial motility in hippocampal neurons. PLoS One 3: e2804.
    • (2008) PLoS One , vol.3
    • Chen, S.1    Owens, G.C.2    Edelman, D.B.3
  • 52
    • 80355148462 scopus 로고    scopus 로고
    • Neuromodulation and mitochondrial transport: live imaging in hippocampal neurons over long durations
    • Edelman DB, Owens GC, Chen S, (2011) Neuromodulation and mitochondrial transport: live imaging in hippocampal neurons over long durations. J Vis Exp.
    • (2011) J Vis Exp
    • Edelman, D.B.1    Owens, G.C.2    Chen, S.3
  • 53
    • 0020394540 scopus 로고
    • Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity
    • Fifkova E, Delay RJ, (1982) Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity. J Cell Biol 95: 345-350.
    • (1982) J Cell Biol , vol.95 , pp. 345-350
    • Fifkova, E.1    Delay, R.J.2
  • 55
    • 0022119267 scopus 로고
    • Immunocytochemical localization of actin in dendritic spines of the cerebral cortex using colloidal gold as a probe
    • Cohen RS, Chung SK, Pfaff DW, (1985) Immunocytochemical localization of actin in dendritic spines of the cerebral cortex using colloidal gold as a probe. Cell Mol Neurobiol 5: 271-284.
    • (1985) Cell Mol Neurobiol , vol.5 , pp. 271-284
    • Cohen, R.S.1    Chung, S.K.2    Pfaff, D.W.3
  • 56
    • 56449084433 scopus 로고    scopus 로고
    • Prominent synaptic and metabolic abnormalities revealed by proteomic analysis of the dorsolateral prefrontal cortex in schizophrenia and bipolar disorder
    • Pennington K, Beasley CL, Dicker P, Fagan A, English J, et al. (2008) Prominent synaptic and metabolic abnormalities revealed by proteomic analysis of the dorsolateral prefrontal cortex in schizophrenia and bipolar disorder. Mol Psychiatry 13: 1102-1117.
    • (2008) Mol Psychiatry , vol.13 , pp. 1102-1117
    • Pennington, K.1    Beasley, C.L.2    Dicker, P.3    Fagan, A.4    English, J.5
  • 57
    • 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, 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
  • 58
    • 0842269066 scopus 로고    scopus 로고
    • Myosin-dependent transport in neurons
    • Bridgman PC, (2004) Myosin-dependent transport in neurons. J Neurobiol 58: 164-174.
    • (2004) J Neurobiol , vol.58 , pp. 164-174
    • Bridgman, P.C.1
  • 59
    • 0020326774 scopus 로고
    • Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method
    • Hirokawa N, (1982) Cross-linker system between neurofilaments, microtubules, and membranous organelles in frog axons revealed by the quick-freeze, deep-etching method. J Cell Biol 94: 129-142.
    • (1982) J Cell Biol , vol.94 , pp. 129-142
    • Hirokawa, N.1
  • 60
    • 0024456931 scopus 로고
    • Studies on the interaction between mitochondria and the cytoskeleton
    • Linden M, Nelson BD, Loncar D, Leterrier JF, (1989) Studies on the interaction between mitochondria and the cytoskeleton. J Bioenerg Biomembr 21: 507-518.
    • (1989) J Bioenerg Biomembr , vol.21 , pp. 507-518
    • Linden, M.1    Nelson, B.D.2    Loncar, D.3    Leterrier, J.F.4
  • 61
    • 0028107194 scopus 로고
    • Interactions between brain mitochondria and cytoskeleton: evidence for specialized outer membrane domains involved in the association of cytoskeleton-associated proteins to mitochondria in situ and in vitro
    • Leterrier JF, Rusakov DA, Nelson BD, Linden M, (1994) Interactions between brain mitochondria and cytoskeleton: evidence for specialized outer membrane domains involved in the association of cytoskeleton-associated proteins to mitochondria in situ and in vitro. Microsc Res Tech 27: 233-261.
    • (1994) Microsc Res Tech , vol.27 , pp. 233-261
    • Leterrier, J.F.1    Rusakov, D.A.2    Nelson, B.D.3    Linden, M.4
  • 63
    • 37749053855 scopus 로고    scopus 로고
    • Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation
    • Kang JS, Tian JH, Pan PY, Zald P, Li C, et al. (2008) Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation. Cell 132: 137-148.
    • (2008) Cell , vol.132 , pp. 137-148
    • Kang, J.S.1    Tian, J.H.2    Pan, P.Y.3    Zald, P.4    Li, C.5
  • 64
    • 0032780959 scopus 로고    scopus 로고
    • Chloromethyl-X-rosamine (MitoTracker Red) photosensitises mitochondria and induces apoptosis in intact human cells
    • Minamikawa T, Sriratana A, Williams DA, Bowser DN, Hill JS, et al. (1999) Chloromethyl-X-rosamine (MitoTracker Red) photosensitises mitochondria and induces apoptosis in intact human cells. J Cell Sci 112 (Pt 14):: 2419-2430.
    • (1999) J Cell Sci , vol.112 , Issue.Pt 14 , pp. 2419-2430
    • Minamikawa, T.1    Sriratana, A.2    Williams, D.A.3    Bowser, D.N.4    Hill, J.S.5
  • 65
    • 0035863594 scopus 로고    scopus 로고
    • MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants
    • Buckman JF, Hernandez H, Kress GJ, Votyakova TV, Pal S, et al. (2001) MitoTracker labeling in primary neuronal and astrocytic cultures: influence of mitochondrial membrane potential and oxidants. J Neurosci Methods 104: 165-176.
    • (2001) J Neurosci Methods , vol.104 , pp. 165-176
    • Buckman, J.F.1    Hernandez, H.2    Kress, G.J.3    Votyakova, T.V.4    Pal, S.5
  • 66
    • 33645843025 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial movement in forebrain neurons associated with disruption of mitochondrial membrane potential
    • Rintoul GL, Bennett VJ, Papaconstandinou NA, Reynolds IJ, (2006) Nitric oxide inhibits mitochondrial movement in forebrain neurons associated with disruption of mitochondrial membrane potential. J Neurochem 97: 800-806.
    • (2006) J Neurochem , vol.97 , pp. 800-806
    • Rintoul, G.L.1    Bennett, V.J.2    Papaconstandinou, N.A.3    Reynolds, I.J.4
  • 67
    • 0019480519 scopus 로고
    • Monitoring of relative mitochondrial membrane potential in living cells by fluorescence microscopy
    • Johnson LV, Walsh ML, Bockus BJ, Chen LB, (1981) Monitoring of relative mitochondrial membrane potential in living cells by fluorescence microscopy. J Cell Biol 88: 526-535.
    • (1981) J Cell Biol , vol.88 , pp. 526-535
    • Johnson, L.V.1    Walsh, M.L.2    Bockus, B.J.3    Chen, L.B.4
  • 68
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • Miller KE, Sheetz MP, (2004) Axonal mitochondrial transport and potential are correlated. J Cell Sci 117: 2791-2804.
    • (2004) J Cell Sci , vol.117 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 69
    • 77955351652 scopus 로고    scopus 로고
    • New insights into the role of mitochondria in aging: mitochondrial dynamics and more
    • Seo AY, Joseph AM, Dutta D, Hwang JC, Aris JP, et al. (2010) New insights into the role of mitochondria in aging: mitochondrial dynamics and more. J Cell Sci 123: 2533-2542.
    • (2010) J Cell Sci , vol.123 , pp. 2533-2542
    • Seo, A.Y.1    Joseph, A.M.2    Dutta, D.3    Hwang, J.C.4    Aris, J.P.5
  • 70
    • 0027210387 scopus 로고
    • The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth
    • Morris RL, Hollenbeck PJ, (1993) The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth. J Cell Sci 104 (Pt 3):: 917-927.
    • (1993) J Cell Sci , vol.104 , Issue.Pt 3 , pp. 917-927
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 71
    • 0002185678 scopus 로고    scopus 로고
    • The pattern and mechanism of mitochondrial transport in axons
    • Hollenbeck PJ, (1996) The pattern and mechanism of mitochondrial transport in axons. Front Biosci 1: d91-102.
    • (1996) Front Biosci , vol.1
    • Hollenbeck, P.J.1
  • 72
    • 3343021928 scopus 로고    scopus 로고
    • Nerve growth factor signaling regulates motility and docking of axonal mitochondria
    • Chada SR, Hollenbeck PJ, (2004) Nerve growth factor signaling regulates motility and docking of axonal mitochondria. Curr Biol 14: 1272-1276.
    • (2004) Curr Biol , vol.14 , pp. 1272-1276
    • Chada, S.R.1    Hollenbeck, P.J.2
  • 73
    • 0041819756 scopus 로고    scopus 로고
    • Glutamate decreases mitochondrial size and movement in primary forebrain neurons
    • Rintoul GL, Filiano AJ, Brocard JB, Kress GJ, Reynolds IJ, (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
  • 74
    • 0021057839 scopus 로고
    • Inhibition of oxidative phosphorylation in hepatic and cerebral mitochondria of sodium valproate-treated rats
    • Rumbach L, Warter JM, Rendon A, Marescaux C, Micheletti G, et al. (1983) Inhibition of oxidative phosphorylation in hepatic and cerebral mitochondria of sodium valproate-treated rats. J Neurol Sci 61: 417-423.
    • (1983) J Neurol Sci , vol.61 , pp. 417-423
    • Rumbach, L.1    Warter, J.M.2    Rendon, A.3    Marescaux, C.4    Micheletti, G.5
  • 75
    • 0034054736 scopus 로고    scopus 로고
    • Disease-specific alterations in frontal cortex brain proteins in schizophrenia, bipolar disorder, and major depressive disorder. The Stanley Neuropathology Consortium
    • Johnston-Wilson NL, Sims CD, Hofmann JP, Anderson L, Shore AD, et al. (2000) Disease-specific alterations in frontal cortex brain proteins in schizophrenia, bipolar disorder, and major depressive disorder. The Stanley Neuropathology Consortium. Mol Psychiatry 5: 142-149.
    • (2000) Mol Psychiatry , vol.5 , pp. 142-149
    • Johnston-Wilson, N.L.1    Sims, C.D.2    Hofmann, J.P.3    Anderson, L.4    Shore, A.D.5
  • 76
    • 0038576291 scopus 로고    scopus 로고
    • Proteome analysis reveals phosphorylation of ATP synthase beta -subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes
    • Hojlund K, Wrzesinski K, Larsen PM, Fey SJ, Roepstorff P, et al. (2003) Proteome analysis reveals phosphorylation of ATP synthase beta-subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes. J Biol Chem 278: 10436-10442.
    • (2003) J Biol Chem , vol.278 , pp. 10436-10442
    • Hojlund, K.1    Wrzesinski, K.2    Larsen, P.M.3    Fey, S.J.4    Roepstorff, P.5
  • 77
    • 77950028099 scopus 로고    scopus 로고
    • Endoxifen is a new potent inhibitor of PKC: a potential therapeutic agent for bipolar disorder
    • Ali SM, Ahmad A, Shahabuddin S, Ahmad MU, Sheikh S, et al. (2010) Endoxifen is a new potent inhibitor of PKC: a potential therapeutic agent for bipolar disorder. Bioorg Med Chem Lett 20: 2665-2667.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 2665-2667
    • Ali, S.M.1    Ahmad, A.2    Shahabuddin, S.3    Ahmad, M.U.4    Sheikh, S.5
  • 78
    • 74849097142 scopus 로고    scopus 로고
    • SNAP-25 is a target of protein kinase C phosphorylation critical to NMDA receptor trafficking
    • Lau CG, Takayasu Y, Rodenas-Ruano A, Paternain AV, Lerma J, et al. (2010) SNAP-25 is a target of protein kinase C phosphorylation critical to NMDA receptor trafficking. J Neurosci 30: 242-254.
    • (2010) J Neurosci , vol.30 , pp. 242-254
    • Lau, C.G.1    Takayasu, Y.2    Rodenas-Ruano, A.3    Paternain, A.V.4    Lerma, J.5
  • 79
    • 0037826928 scopus 로고    scopus 로고
    • Differential regulation by stimulants of neocortical expression of mrt1, arc, and homer1a mRNA in the rats treated with repeated methamphetamine
    • Fujiyama K, Kajii Y, Hiraoka S, Nishikawa T, (2003) Differential regulation by stimulants of neocortical expression of mrt1, arc, and homer1a mRNA in the rats treated with repeated methamphetamine. Synapse 49: 143-149.
    • (2003) Synapse , vol.49 , pp. 143-149
    • Fujiyama, K.1    Kajii, Y.2    Hiraoka, S.3    Nishikawa, T.4
  • 80
    • 33645729901 scopus 로고    scopus 로고
    • Association of a polymorphism in the Homer1 gene with cocaine dependence in an African American population
    • Dahl JP, Kampman KM, Oslin DW, Weller AE, Lohoff FW, et al. (2005) Association of a polymorphism in the Homer1 gene with cocaine dependence in an African American population. Psychiatr Genet 15: 277-283.
    • (2005) Psychiatr Genet , vol.15 , pp. 277-283
    • Dahl, J.P.1    Kampman, K.M.2    Oslin, D.W.3    Weller, A.E.4    Lohoff, F.W.5
  • 81
    • 0029847068 scopus 로고    scopus 로고
    • Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly
    • Bornslaeger EA, Corcoran CM, Stappenbeck TS, Green KJ, (1996) Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly. J Cell Biol 134: 985-1001.
    • (1996) J Cell Biol , vol.134 , pp. 985-1001
    • Bornslaeger, E.A.1    Corcoran, C.M.2    Stappenbeck, T.S.3    Green, K.J.4
  • 82
    • 0028028177 scopus 로고
    • Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks
    • Stappenbeck TS, Lamb JA, Corcoran CM, Green KJ, (1994) Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks. J Biol Chem 269: 29351-29354.
    • (1994) J Biol Chem , vol.269 , pp. 29351-29354
    • Stappenbeck, T.S.1    Lamb, J.A.2    Corcoran, C.M.3    Green, K.J.4
  • 83
    • 35548999252 scopus 로고    scopus 로고
    • Protocadherin family: diversity, structure, and function
    • Morishita H, Yagi T, (2007) Protocadherin family: diversity, structure, and function. Curr Opin Cell Biol 19: 584-592.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 584-592
    • Morishita, H.1    Yagi, T.2
  • 84
    • 33845727992 scopus 로고    scopus 로고
    • The cadherin superfamily in neuronal connections and interactions
    • Takeichi M, (2007) The cadherin superfamily in neuronal connections and interactions. Nat Rev Neurosci 8: 11-20.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 11-20
    • Takeichi, M.1
  • 85
    • 50549097328 scopus 로고    scopus 로고
    • Cadherins and catenins at synapses: roles in synaptogenesis and synaptic plasticity
    • Arikkath J, Reichardt LF, (2008) Cadherins and catenins at synapses: roles in synaptogenesis and synaptic plasticity. Trends Neurosci 31: 487-494.
    • (2008) Trends Neurosci , vol.31 , pp. 487-494
    • Arikkath, J.1    Reichardt, L.F.2
  • 86
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V, a versatile motor for short-range vesicle transport
    • Langford GM, (2002) Myosin-V, a versatile motor for short-range vesicle transport. Traffic 3: 859-865.
    • (2002) Traffic , vol.3 , pp. 859-865
    • Langford, G.M.1
  • 87
    • 0029848373 scopus 로고    scopus 로고
    • Mitochondrial involvement in schizophrenia and other functional psychoses
    • Whatley SA, Curti D, Marchbanks RM, (1996) Mitochondrial involvement in schizophrenia and other functional psychoses. Neurochem Res 21 (9):: 995-1004.
    • (1996) Neurochem Res , vol.21 , Issue.9 , pp. 995-1004
    • Whatley, S.A.1    Curti, D.2    Marchbanks, R.M.3
  • 88
    • 0032775671 scopus 로고    scopus 로고
    • Mitochondrial function is differentially altered in the basal ganglia of chronic schizophrenics
    • Prince JA, Blennow K, Gottfries CG, Karlsson I, Oreland L, (1999) Mitochondrial function is differentially altered in the basal ganglia of chronic schizophrenics. Neuropsychopharmacology 21 (3):: 372-379.
    • (1999) Neuropsychopharmacology , vol.21 , Issue.3 , pp. 372-379
    • Prince, J.A.1    Blennow, K.2    Gottfries, C.G.3    Karlsson, I.4    Oreland, L.5
  • 89
    • 0001582283 scopus 로고    scopus 로고
    • Increased mitochondrial complex I activity in platelets of schizophrenic patients
    • Ben-Shachar D, Zuk R, Gazawi H, Reshef A, Sheinkman A, et al. (1999) Increased mitochondrial complex I activity in platelets of schizophrenic patients. Int J Neuropsychopharmacol 2 (4):: 245-253.
    • (1999) Int J Neuropsychopharmacol , vol.2 , Issue.4 , pp. 245-253
    • Ben-Shachar, D.1    Zuk, R.2    Gazawi, H.3    Reshef, A.4    Sheinkman, A.5
  • 90
    • 0036902639 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in schizophrenia: a possible linkage to dopamine
    • Ben-Shachar D, (2002) Mitochondrial dysfunction in schizophrenia: a possible linkage to dopamine. J Neurochem 83 (6):: 1241-1251.
    • (2002) J Neurochem , vol.83 , Issue.6 , pp. 1241-1251
    • Ben-Shachar, D.1
  • 91
    • 12744278205 scopus 로고    scopus 로고
    • Altered expression of mitochondria-related genes in postmortem brains of patients with bipolar disorder or schizophrenia, as revealed by large-scale DNA microarray analysis
    • Iwamoto K, Bundo M, Kato T, (2005) Altered expression of mitochondria-related genes in postmortem brains of patients with bipolar disorder or schizophrenia, as revealed by large-scale DNA microarray analysis. Human Molecular Genetics 14 (2):: 241-253.
    • (2005) Human Molecular Genetics , vol.14 , Issue.2 , pp. 241-253
    • Iwamoto, K.1    Bundo, M.2    Kato, T.3
  • 92
    • 0017135957 scopus 로고
    • Lithium orotate, carbonate and chloride: pharmacokinetics, polyuria in rats
    • Smith DF, (1976) Lithium orotate, carbonate and chloride: pharmacokinetics, polyuria in rats. Br J Pharmacol 56 (4):: 399-402.
    • (1976) Br J Pharmacol , vol.56 , Issue.4 , pp. 399-402
    • Smith, D.F.1
  • 93
    • 33749370570 scopus 로고    scopus 로고
    • Effects of lithium and valproate on amphetamine-induced oxidative stress generation in an animal model of mania
    • Frey BN, Valvassori SS, Réus GZ, Martins MR, Petronilho FC, et al. (2006) Effects of lithium and valproate on amphetamine-induced oxidative stress generation in an animal model of mania. J Phsychiatry Neurosci 31 (5):: 326-32.
    • (2006) J Phsychiatry Neurosci , vol.31 , Issue.5 , pp. 326-332
    • Frey, B.N.1    Valvassori, S.S.2    Réus, G.Z.3    Martins, M.R.4    Petronilho, F.C.5
  • 94
    • 77956417240 scopus 로고    scopus 로고
    • Differential effects of antipsychotic and antidepressant drugs on neurogenic regions in rats
    • Nasrallah HA, Hopkins T, Pixley SK, (2010) Differential effects of antipsychotic and antidepressant drugs on neurogenic regions in rats. Brain Res 1354: 23-29.
    • (2010) Brain Res , vol.1354 , pp. 23-29
    • Nasrallah, H.A.1    Hopkins, T.2    Pixley, S.K.3
  • 95
    • 0038662761 scopus 로고    scopus 로고
    • Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo
    • Fukazawa Y, Saitoh Y, Ozawa F, Ohta Y, Mizuno K, et al. (2003) Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo. Neuron 38: 447-460.
    • (2003) Neuron , vol.38 , pp. 447-460
    • Fukazawa, Y.1    Saitoh, Y.2    Ozawa, F.3    Ohta, Y.4    Mizuno, K.5


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