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Volumn 73, Issue 12, 2014, Pages 1166-1182

The calcium-binding protein EFhd2 modulates synapse formation in vitro and is linked to human dementia

Author keywords

Alzheimer disease; Cortical neurons; EFhd2; Frontotemporal dementia; Frontotemporal lobar degeneration; Swiprosin 1; Synapses

Indexed keywords

ADAPTOR PROTEIN; CALCIUM BINDING PROTEIN; EF HAND DOMAIN CONTAINING PROTEIN 2; MESSENGER RNA; SHORT HAIRPIN RNA; TAU PROTEIN; UNCLASSIFIED DRUG; EFHD2 PROTEIN, HUMAN;

EID: 84915767481     PISSN: 00223069     EISSN: 15546578     Source Type: Journal    
DOI: 10.1097/NEN.0000000000000138     Document Type: Article
Times cited : (26)

References (48)
  • 1
    • 84881546833 scopus 로고    scopus 로고
    • The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease
    • Crimins JL, Pooler A, Polydoro M, et al. The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease. Ageing Res Rev 2013;12:757-63
    • (2013) Ageing Res Rev , vol.12 , pp. 757-763
    • Crimins, J.L.1    Pooler, A.2    Polydoro, M.3
  • 2
    • 77957954675 scopus 로고    scopus 로고
    • Review: Disruption of the postsynaptic density in Alzheimer's disease and other neurodegenerative dementias
    • Gong Y, Lippa CF. Review: Disruption of the postsynaptic density in Alzheimer's disease and other neurodegenerative dementias. Am J Alzheimers Dis Other Demen 2010;25:547-55
    • (2010) Am J Alzheimers Dis Other Demen , vol.25 , pp. 547-555
    • Gong, Y.1    Lippa, C.F.2
  • 3
    • 0031878572 scopus 로고    scopus 로고
    • Frontotemporal dementia: Neuropil spheroids and presynaptic terminal degeneration
    • Zhou L, Miller BL, McDaniel CH, et al. Frontotemporal dementia: Neuropil spheroids and presynaptic terminal degeneration. Ann Neurol 1998;44:99-109
    • (1998) Ann Neurol , vol.44 , pp. 99-109
    • Zhou, L.1    Miller, B.L.2    McDaniel, C.H.3
  • 5
    • 84864383087 scopus 로고    scopus 로고
    • Frontotemporal dementia: Implications for understanding Alzheimer disease
    • Goedert M, Ghetti B, Spillantini MG. Frontotemporal dementia: Implications for understanding Alzheimer disease. Cold Spring Harb Perspect Med 2012;2:a006254
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. a006254
    • Goedert, M.1    Ghetti, B.2    Spillantini, M.G.3
  • 6
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediactes amyloid-b toxicity in Alzheimer's disease mouse models
    • Ittner LM. Dendritic function of tau mediactes amyloid-b toxicity in Alzheimer's disease mouse models. Cell 2010;142:387-97
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1
  • 7
    • 79551510136 scopus 로고    scopus 로고
    • Tau protein is required for amyloid A-induced impairment of hippocampal long-term potentiation
    • Shipton OA, Leitz JR, Dworzak J, et al. Tau protein is required for amyloid A-induced impairment of hippocampal long-term potentiation. J Neurosci 2011;31:1688-92
    • (2011) J Neurosci , vol.31 , pp. 1688-1692
    • Shipton, O.A.1    Leitz, J.R.2    Dworzak, J.3
  • 8
    • 35748954923 scopus 로고    scopus 로고
    • The beta-propensity of tau determines aggregation and synaptic loss in inducible mouse models of tauopathy
    • Eckermann K, Mocanu MM, Khlistunova I, et al. The beta-propensity of tau determines aggregation and synaptic loss in inducible mouse models of tauopathy. J Biol Chem 2007;282:31755-65
    • (2007) J Biol Chem , vol.282 , pp. 31755-31765
    • Eckermann, K.1    Mocanu, M.M.2    Khlistunova, I.3
  • 9
    • 0035139540 scopus 로고    scopus 로고
    • Staging of neurofibrillary degeneration caused by human tau overexpression in a unique cellular model of human tauopathy
    • Hall GF, Lee VM, Lee G, et al. Staging of neurofibrillary degeneration caused by human tau overexpression in a unique cellular model of human tauopathy. Am J Pathol 2001;158:235-46
    • (2001) Am J Pathol , vol.158 , pp. 235-246
    • Hall, G.F.1    Lee, V.M.2    Lee, G.3
  • 10
    • 84908161213 scopus 로고    scopus 로고
    • Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS
    • epub ahead of print June 8
    • Bennion Callister J, Pickering-Brown SM. Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS [epub ahead of print June 8, 2014]. Exp Neurol doi: 10.1016/j.expneurol.2014.06.001
    • (2014) Exp Neurol
    • Bennion Callister, J.1    Pickering-Brown, S.M.2
  • 11
    • 84878761125 scopus 로고    scopus 로고
    • Efhd2 is a novel amyloid protein associated to pathological tau in Alzheimer's disease
    • Ferrer-Acosta Y, Rodríguez-Cruz EN, Orange F, et al. Efhd2 is a novel amyloid protein associated to pathological tau in Alzheimer's disease. J Neurochem 2013;125:921-31
    • (2013) J Neurochem , vol.125 , pp. 921-931
    • Ferrer-Acosta, Y.1    Rodríguez-Cruz, E.N.2    Orange, F.3
  • 12
    • 45249099292 scopus 로고    scopus 로고
    • A novel calcium-binding protein is associated with tau proteins in tauopathy
    • Vega IE, Traverso EE, Ferrer-Acosta Y, et al. A novel calcium-binding protein is associated with tau proteins in tauopathy. J Neurochem 2008; 106:96-106
    • (2008) J Neurochem , vol.106 , pp. 96-106
    • Vega, I.E.1    Traverso, E.E.2    Ferrer-Acosta, Y.3
  • 13
    • 84906888245 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of EFhd2 at S74 affects its calcium binding activity
    • Vázquez-Rosa E, Rodríguez-Cruz EN, Serrano S, et al. Cdk5 phosphorylation of EFhd2 at S74 affects its calcium binding activity. Protein Sci 2014;23:1197-207
    • (2014) Protein Sci , vol.23 , pp. 1197-1207
    • Vázquez-Rosa, E.1    Rodríguez-Cruz, E.N.2    Serrano, S.3
  • 14
    • 77649134880 scopus 로고    scopus 로고
    • Prefrontal cortex shotgun proteome analysis reveals altered calcium homeostasis and immune system imbalance in schizophrenia
    • Martins-de-Souza D, Gattaz WF, Schmitt A, et al. Prefrontal cortex shotgun proteome analysis reveals altered calcium homeostasis and immune system imbalance in schizophrenia. Eur Arch Psychiatry Clin Neurosci 2009;259:151-63
    • (2009) Eur Arch Psychiatry Clin Neurosci , vol.259 , pp. 151-163
    • Martins-De-Souza, D.1    Gattaz, W.F.2    Schmitt, A.3
  • 15
    • 84870825177 scopus 로고    scopus 로고
    • Altered functional protein networks in the prefrontal cortex and amygdala of victims of suicide
    • Kekesi KA, Juhasz G, Simor A, et al. Altered functional protein networks in the prefrontal cortex and amygdala of victims of suicide. PLoS One 2012;7:e50532
    • (2012) PLoS One , vol.7 , pp. e50532
    • Kekesi, K.A.1    Juhasz, G.2    Simor, A.3
  • 16
    • 66249085542 scopus 로고    scopus 로고
    • Proteomic characterization of lipid raft proteins in amyotrophic lateral sclerosis mouse spinal cord
    • Zhai J, Strom AL, Kilty R, et al. Proteomic characterization of lipid raft proteins in amyotrophic lateral sclerosis mouse spinal cord. FEBS J 2009; 276:3308-23
    • (2009) FEBS J , vol.276 , pp. 3308-3323
    • Zhai, J.1    Strom, A.L.2    Kilty, R.3
  • 17
    • 84915784999 scopus 로고    scopus 로고
    • Swiprosin-1 expression is upregulated through protein kinase C-theta and NF-kappaB pathway in T cells
    • Kim YD, Kwon MS, Na BR, et al. Swiprosin-1 expression is upregulated through protein kinase C-theta and NF-kappaB pathway in T cells. Immune Netw 2013;13:55-62
    • (2013) Immune Netw , vol.13 , pp. 55-62
    • Kim, Y.D.1    Kwon, M.S.2    Na, B.R.3
  • 18
    • 70350176491 scopus 로고    scopus 로고
    • Swiprosin-1 is expressed in mast cells and up-regulated through the protein kinase C beta I/eta pathway
    • Thylur RP, Kim YD, Kwon MS, et al. Swiprosin-1 is expressed in mast cells and up-regulated through the protein kinase C beta I/eta pathway. J Cell Biochem 2009;108:705-15
    • (2009) J Cell Biochem , vol.108 , pp. 705-715
    • Thylur, R.P.1    Kim, Y.D.2    Kwon, M.S.3
  • 19
    • 84859482155 scopus 로고    scopus 로고
    • The B-cell receptor-induced calcium flux involves a calcium mediated positive feedback loop
    • Hagen S, Brachs S, Kroczek C, et al. The B-cell receptor-induced calcium flux involves a calcium mediated positive feedback loop. Cell Calcium 2012;51:411-17
    • (2012) Cell Calcium , vol.51 , pp. 411-417
    • Hagen, S.1    Brachs, S.2    Kroczek, C.3
  • 20
    • 77951648119 scopus 로고    scopus 로고
    • Swiprosin-1/EFhd2 controls B cell receptor signaling through the assembly of the B cell receptor, Syk, and phospholipase C gamma2 in membrane rafts
    • Kroczek C, Lang C, Brachs S, et al. Swiprosin-1/EFhd2 controls B cell receptor signaling through the assembly of the B cell receptor, Syk, and phospholipase C gamma2 in membrane rafts. J Immunol 2010;184:3665-76
    • (2010) J Immunol , vol.184 , pp. 3665-3676
    • Kroczek, C.1    Lang, C.2    Brachs, S.3
  • 21
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev B, Ong S-E, Kratchmarova I, et al. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat Biotech 2004;22:1139-45
    • (2004) Nat Biotech , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.-E.2    Kratchmarova, I.3
  • 22
    • 84889884729 scopus 로고    scopus 로고
    • Swiprosin-1 modulates actin dynamics by regulating the F-actin accessibility to cofilin
    • Huh YH, Kim SH, Chung KH, et al. Swiprosin-1 modulates actin dynamics by regulating the F-actin accessibility to cofilin. Cell Mol Life Sci 2013;70:4841-54
    • (2013) Cell Mol Life Sci , vol.70 , pp. 4841-4854
    • Huh, Y.H.1    Kim, S.H.2    Chung, K.H.3
  • 23
    • 84881606948 scopus 로고    scopus 로고
    • Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration
    • Kwon MS, Park KR, Kim YD, et al. Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration. PLoS One 2013; 8:e71626
    • (2013) PLoS One , vol.8 , pp. e71626
    • Kwon, M.S.1    Park, K.R.2    Kim, Y.D.3
  • 24
    • 84915821571 scopus 로고    scopus 로고
    • The Ca2+ sensor protein Swiprosin-1/EFhd2 is present in neurites and involved in kinesin-mediated transport in neurons
    • Purohit P, Perez-Branguli F, Prots I, et al. The Ca2+ sensor protein Swiprosin-1/EFhd2 is present in neurites and involved in kinesin-mediated transport in neurons. PLoS One 2014;9:e103976
    • (2014) PLoS One , vol.9 , pp. e103976
    • Purohit, P.1    Perez-Branguli, F.2    Prots, I.3
  • 25
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • Tai HC, Serrano-Pozo A, Hashimoto T, et al. The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am J Pathol 2012; 181:1426-35
    • (2012) Am J Pathol , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3
  • 26
    • 35548953798 scopus 로고    scopus 로고
    • The novel adaptor protein Swiprosin-1 enhances BCR signals and contributes to BCR-induced apoptosis
    • Avramidou A, Kroczek C, Lang C, et al. The novel adaptor protein Swiprosin-1 enhances BCR signals and contributes to BCR-induced apoptosis. Cell Death Differ 2007;14:1936-47
    • (2007) Cell Death Differ , vol.14 , pp. 1936-1947
    • Avramidou, A.1    Kroczek, C.2    Lang, C.3
  • 27
    • 3543144332 scopus 로고    scopus 로고
    • Identification of swiprosin 1 in human lymphocytes
    • Vuadens F, Rufer N, Kress A, et al. Identification of swiprosin 1 in human lymphocytes. Proteomics 2004;4:2216-20
    • (2004) Proteomics , vol.4 , pp. 2216-2220
    • Vuadens, F.1    Rufer, N.2    Kress, A.3
  • 28
    • 80053090362 scopus 로고    scopus 로고
    • Drosophila Swiprosin-1/EFHD2 accumulates at the prefusion complex stage during Drosophila myoblast fusion
    • Hornbruch-Freitag C, Griemert B, Buttgereit D, et al. Drosophila Swiprosin-1/EFHD2 accumulates at the prefusion complex stage during Drosophila myoblast fusion. J Cell Sci 2011;124:3266-78
    • (2011) J Cell Sci , vol.124 , pp. 3266-3278
    • Hornbruch-Freitag, C.1    Griemert, B.2    Buttgereit, D.3
  • 29
    • 79956142378 scopus 로고    scopus 로고
    • The diagnosis of dementia due to Alzheimer's disease: Recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease
    • McKhann GM, Knopman DS, Chertkow H, et al. The diagnosis of dementia due to Alzheimer's disease: Recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease. Alzheimers Dement 2011;7:263-69
    • (2011) Alzheimers Dement , vol.7 , pp. 263-269
    • McKhann, G.M.1    Knopman, D.S.2    Chertkow, H.3
  • 30
    • 84893451805 scopus 로고    scopus 로고
    • Cell number changes in Alzheimer's disease relate to dementia, not to plaques and tangles
    • Andrade-Moraes CH, Oliveira-Pinto AV, Castro-Fonseca E, et al. Cell number changes in Alzheimer's disease relate to dementia, not to plaques and tangles. Brain 2013;136:3738-52
    • (2013) Brain , vol.136 , pp. 3738-3752
    • Andrade-Moraes, C.H.1    Oliveira-Pinto, A.V.2    Castro-Fonseca, E.3
  • 31
    • 84915754902 scopus 로고    scopus 로고
    • TDP-43 in the population: Prevalence and associations with dementia and age
    • Keage HA, Hunter S, Matthews FE, et al. TDP-43 in the population: Prevalence and associations with dementia and age. J Alzheimers Dis 2014;42:641-50
    • (2014) J Alzheimers Dis , vol.42 , pp. 641-650
    • Keage, H.A.1    Hunter, S.2    Matthews, F.E.3
  • 32
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • Duyckaerts C, Delatour B, Potier MC. Classification and basic pathology of Alzheimer disease. Acta Neuropathol 2009;118:5-36
    • (2009) Acta Neuropathol , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 33
    • 4644283049 scopus 로고    scopus 로고
    • PET imaging of amyloid in Alzheimer's disease
    • Nordberg A. PET imaging of amyloid in Alzheimer's disease. Lancet Neurol 2004;3:519-27
    • (2004) Lancet Neurol , vol.3 , pp. 519-527
    • Nordberg, A.1
  • 34
    • 29144495943 scopus 로고    scopus 로고
    • Compositional characterization of the cytoskeleton of NK-like cells
    • Meng X, Wilkins JA. Compositional characterization of the cytoskeleton of NK-like cells. J Proteome Res 2005;4:2081-87
    • (2005) J Proteome Res , vol.4 , pp. 2081-2087
    • Meng, X.1    Wilkins, J.A.2
  • 35
    • 84862777951 scopus 로고    scopus 로고
    • Tau protein is involved in morphological plasticity in hippocampal neurons in response to BDNF
    • Chen Q, Zhou Z, Zhang L, et al. Tau protein is involved in morphological plasticity in hippocampal neurons in response to BDNF. Neurochem Int 2012;60:233-42
    • (2012) Neurochem Int , vol.60 , pp. 233-242
    • Chen, Q.1    Zhou, Z.2    Zhang, L.3
  • 36
    • 79951990962 scopus 로고    scopus 로고
    • Phosphoinositide-3-kinase activation controls synaptogenesis and spinogenesis in hippocampal neurons
    • Cuesto G, Enriquez-Barreto L, Carames C, et al. Phosphoinositide-3-kinase activation controls synaptogenesis and spinogenesis in hippocampal neurons. J Neurosci 2011;31:2721-33
    • (2011) J Neurosci , vol.31 , pp. 2721-2733
    • Cuesto, G.1    Enriquez-Barreto, L.2    Carames, C.3
  • 37
    • 80054078702 scopus 로고    scopus 로고
    • Swiprosin-1 regulates cytokine expression of human mast cell line HMC-1 through actin remodeling
    • Ramesh TP, Kim YD, Kwon MS, et al. Swiprosin-1 regulates cytokine expression of human mast cell line HMC-1 through actin remodeling. Immune Netw 2009;9:274-84
    • (2009) Immune Netw , vol.9 , pp. 274-284
    • Ramesh, T.P.1    Kim, Y.D.2    Kwon, M.S.3
  • 38
    • 73549097504 scopus 로고    scopus 로고
    • Functional and dysfunctional synaptic plasticity in prefrontal cortex: Roles in psychiatric disorders
    • Goto Y, Yang CR, Otani S. Functional and dysfunctional synaptic plasticity in prefrontal cortex: Roles in psychiatric disorders. Biol Psych 2010;67:199-207
    • (2010) Biol Psych , vol.67 , pp. 199-207
    • Goto, Y.1    Yang, C.R.2    Otani, S.3
  • 39
    • 40349092941 scopus 로고    scopus 로고
    • Covalent capture of kinasespecific phosphopeptides reveals Cdk1-cyclin B substrates
    • Blethrow JD, Glavy JS, Morgan DO, et al. Covalent capture of kinasespecific phosphopeptides reveals Cdk1-cyclin B substrates. Proc Natl Acad Sci USA 2008;105:1442-47
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1442-1447
    • Blethrow, J.D.1    Glavy, J.S.2    Morgan, D.O.3
  • 40
    • 0029034870 scopus 로고
    • Tau domains, phosphorylation, and interactions with microtubules
    • Mandelkow EM, Biernat J, Drewes G, et al. Tau domains, phosphorylation, and interactions with microtubules. Neurobiol Aging 1995;16:355-62
    • (1995) Neurobiol Aging , vol.16 , pp. 355-362
    • Mandelkow, E.M.1    Biernat, J.2    Drewes, G.3
  • 41
    • 35248821113 scopus 로고    scopus 로고
    • Collapsin response mediator protein-2 hyperphosphorylation is an early event in Alzheimer's disease progression
    • Cole AR, Noble W, van Aalten L, et al. Collapsin response mediator protein-2 hyperphosphorylation is an early event in Alzheimer's disease progression. J Neurochem 2007;103:1132-44
    • (2007) J Neurochem , vol.103 , pp. 1132-1144
    • Cole, A.R.1    Noble, W.2    Van Aalten, L.3
  • 42
    • 33749826587 scopus 로고    scopus 로고
    • P25/Cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid beta in vivo
    • Cruz JC, Kim D, Moy LY, et al. p25/Cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid beta in vivo. J Neurosci 2006;26:10536-41
    • (2006) J Neurosci , vol.26 , pp. 10536-10541
    • Cruz, J.C.1    Kim, D.2    Moy, L.Y.3
  • 43
    • 0032578024 scopus 로고    scopus 로고
    • Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration
    • Pei J-J, Grundke-Iqbal I, Iqbal K, et al. Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration. Brain Res 1998;797:267-77
    • (1998) Brain Res , vol.797 , pp. 267-277
    • Pei, J.-J.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 44
    • 34250897267 scopus 로고    scopus 로고
    • Role of Cdk5-mediated phosphorylation of Prx2 in MPTP toxicity and Parkinson's disease
    • Qu D, Rashidian J, Mount MP, et al. Role of Cdk5-mediated phosphorylation of Prx2 in MPTP toxicity and Parkinson's disease. Neuron 2007; 55:37-52
    • (2007) Neuron , vol.55 , pp. 37-52
    • Qu, D.1    Rashidian, J.2    Mount, M.P.3
  • 45
    • 0344823864 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 is a mediator of dopaminergic neuron loss in a mouse model of Parkinson's disease
    • Smith PD, Crocker SJ, Jackson-Lewis V, et al. Cyclin-dependent kinase 5 is a mediator of dopaminergic neuron loss in a mouse model of Parkinson's disease. Proc Natl Acad Sci USA 2003;100:13650-55
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13650-13655
    • Smith, P.D.1    Crocker, S.J.2    Jackson-Lewis, V.3
  • 46
    • 79959985280 scopus 로고    scopus 로고
    • A dual mechanism linking NGF/proNGF imbalance and early inflammation to Alzheimer's disease neurodegeneration in the AD11 anti-NGF mouse model
    • Capsoni S, Brandi R, Arisi I, et al. A dual mechanism linking NGF/proNGF imbalance and early inflammation to Alzheimer's disease neurodegeneration in the AD11 anti-NGF mouse model. CNS Neurol Dis Drug Targ 2011; 10:635-47
    • (2011) CNS Neurol Dis Drug Targ , vol.10 , pp. 635-647
    • Capsoni, S.1    Brandi, R.2    Arisi, I.3
  • 47
    • 79960881826 scopus 로고    scopus 로고
    • Diabetes as a risk factor for Alzheimer's disease: Insulin signalling impairment in the brain as an alternative model of Alzheimer's disease
    • Holscher C. Diabetes as a risk factor for Alzheimer's disease: Insulin signalling impairment in the brain as an alternative model of Alzheimer's disease. Biochem Soc Trans 2011;39:891-97
    • (2011) Biochem Soc Trans , vol.39 , pp. 891-897
    • Holscher, C.1
  • 48
    • 37849050242 scopus 로고    scopus 로고
    • Neurotrophic factors in Alzheimer's disease: Role of axonal transport
    • Schindowski K, Belarbi K, Buee L. Neurotrophic factors in Alzheimer's disease: Role of axonal transport. Genes Brain Behav 2008;7(Suppl 1):43-56
    • (2008) Genes Brain Behav , vol.7 , pp. 43-56
    • Schindowski, K.1    Belarbi, K.2    Buee, L.3


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