메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; APBB1 PROTEIN, MOUSE; APBB2 PROTEIN, MOUSE; CARRIER PROTEIN; NERVE PROTEIN; NUCLEAR PROTEIN;

EID: 85009072607     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep25652     Document Type: Article
Times cited : (18)

References (49)
  • 1
    • 40549088942 scopus 로고    scopus 로고
    • The FE65 proteins and Alzheimer's disease
    • McLoughlin, D. M. & Miller, C. C. The FE65 proteins and Alzheimer's disease. J Neurosci Res 86, 744-754, doi: 10.1002/jnr.21532 (2008).
    • (2008) J Neurosci Res , vol.86 , pp. 744-754
    • McLoughlin, D.M.1    Miller, C.C.2
  • 2
    • 33747692276 scopus 로고    scopus 로고
    • FE65 interaction with the ApoE receptor ApoEr2
    • Hoe, H. S. et al. FE65 interaction with the ApoE receptor ApoEr2. J Biol Chem 281, 24521-24530, doi: 10.1074/jbc.M600728200 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 24521-24530
    • Hoe, H.S.1
  • 3
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein e receptors and the amyloid precursor protein
    • Trommsdorff, M., Borg, J. P., Margolis, B. & Herz, J. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J Biol Chem 273, 33556-33560 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 33556-33560
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 4
    • 84858300270 scopus 로고    scopus 로고
    • FE65 as a link between VLDLR and APP to regulate their trafficking and processing
    • Dumanis, S. B. et al. FE65 as a link between VLDLR and APP to regulate their trafficking and processing. Molecular neurodegeneration 7, 9, doi: 10.1186/1750-1326-7-9 (2012).
    • (2012) Molecular Neurodegeneration , vol.7 , pp. 9
    • Dumanis, S.B.1
  • 5
    • 0031451149 scopus 로고    scopus 로고
    • The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled
    • Ermekova, K. S. et al. The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. J Biol Chem 272, 32869-32877 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 32869-32877
    • Ermekova, K.S.1
  • 6
    • 34247349579 scopus 로고    scopus 로고
    • A macromolecular complex involving the amyloid precursor protein (APP) and the cytosolic adapter FE65 is a negative regulator of axon branching
    • Ikin, A. F., Sabo, S. L., Lanier, L. M. & Buxbaum, J. D. A macromolecular complex involving the amyloid precursor protein (APP) and the cytosolic adapter FE65 is a negative regulator of axon branching. Molecular and cellular neurosciences 35, 57-63, doi: 10.1016/j.mcn.2007.02.003 (2007).
    • (2007) Molecular and Cellular Neurosciences , vol.35 , pp. 57-63
    • Ikin, A.F.1    Sabo, S.L.2    Lanier, L.M.3    Buxbaum, J.D.4
  • 8
    • 84893318361 scopus 로고    scopus 로고
    • Amyloid beta a4 precursor protein-binding family B member 1 (FE65) interactomics revealed synaptic vesicle glycoprotein 2A (SV2A) and sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) as new binding proteins in the human brain
    • Nensa, F. M. et al. Amyloid beta a4 precursor protein-binding family B member 1 (FE65) interactomics revealed synaptic vesicle glycoprotein 2A (SV2A) and sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) as new binding proteins in the human brain. Molecular & cellular proteomics: MCP 13, 475-488, doi: 10.1074/mcp.M113.029280 (2014).
    • (2014) Molecular & Cellular Proteomics: MCP , vol.13 , pp. 475-488
    • Nensa, F.M.1
  • 9
    • 29644441522 scopus 로고    scopus 로고
    • Role of 14-3-3gamma in FE65-dependent gene transactivation mediated by the amyloid beta-protein precursor cytoplasmic fragment
    • Sumioka, A. et al. Role of 14-3-3gamma in FE65-dependent gene transactivation mediated by the amyloid beta-protein precursor cytoplasmic fragment. J Biol Chem 280, 42364-42374 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 42364-42374
    • Sumioka, A.1
  • 10
    • 58049200124 scopus 로고    scopus 로고
    • Dexras1 interacts with FE65 to regulate FE65-amyloid precursor protein-dependent transcription
    • Lau, K. F. et al. Dexras1 interacts with FE65 to regulate FE65-amyloid precursor protein-dependent transcription. J Biol Chem 283, 34728-34737, doi: 10.1074/jbc.M801874200 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 34728-34737
    • Lau, K.F.1
  • 11
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X. & Sudhof, T. C. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115-120 (2001).
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 12
    • 84870156483 scopus 로고    scopus 로고
    • Fe65 matters: New light on an old molecule
    • Minopoli, G., Gargiulo, A., Parisi, S. & Russo, T. Fe65 matters: new light on an old molecule. IUBMB life 64, 936-942, doi: 10.1002/ iub.1094 (2012).
    • (2012) IUBMB Life , vol.64 , pp. 936-942
    • Minopoli, G.1    Gargiulo, A.2    Parisi, S.3    Russo, T.4
  • 13
    • 9144262348 scopus 로고    scopus 로고
    • Isoform-specific knockout of FE65 leads to impaired learning and memory
    • Wang, B. et al. Isoform-specific knockout of FE65 leads to impaired learning and memory. J Neurosci Res 75, 12-24, doi: 10.1002/ jnr.10834 (2004).
    • (2004) J Neurosci Res , vol.75 , pp. 12-24
    • Wang, B.1
  • 14
    • 31444442064 scopus 로고    scopus 로고
    • Essential roles for the FE65 amyloid precursor protein-interacting proteins in brain development
    • Guenette, S. et al. Essential roles for the FE65 amyloid precursor protein-interacting proteins in brain development. The EMBO journal 25, 420-431, doi: 10.1038/sj.emboj.7600926 (2006).
    • (2006) The EMBO Journal , vol.25 , pp. 420-431
    • Guenette, S.1
  • 15
    • 69749090759 scopus 로고    scopus 로고
    • The APP-interacting protein FE65 is required for hippocampus-dependent learning and long-term potentiation
    • Wang, Y. et al. The APP-interacting protein FE65 is required for hippocampus-dependent learning and long-term potentiation. Learning & memory 16, 537-544, doi: 10.1101/lm.1499309 (2009).
    • (2009) Learning & Memory , vol.16 , pp. 537-544
    • Wang, Y.1
  • 17
    • 79955721148 scopus 로고    scopus 로고
    • Brain regions and genes affecting limb-clasping responses
    • Lalonde, R. & Strazielle, C. Brain regions and genes affecting limb-clasping responses. Brain Res Rev 67, 252-259, doi: 10.1016/j. brainresrev.2011.02.005 (2011).
    • (2011) Brain Res Rev , vol.67 , pp. 252-259
    • Lalonde, R.1    Strazielle, C.2
  • 18
    • 78650939557 scopus 로고    scopus 로고
    • Specific functions for ERK/MAPK signaling during PNS development
    • Newbern, J. M. et al. Specific functions for ERK/MAPK signaling during PNS development. Neuron 69, 91-105, doi: 10.1016/j. neuron.2010.12.003 (2011).
    • (2011) Neuron , vol.69 , pp. 91-105
    • Newbern, J.M.1
  • 19
    • 41849099298 scopus 로고    scopus 로고
    • Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness
    • Hayward, L. J. et al. Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness. J Clin Invest 118, 1437-1449, doi: 10.1172/JCI32638 (2008).
    • (2008) J Clin Invest , vol.118 , pp. 1437-1449
    • Hayward, L.J.1
  • 20
    • 0035888618 scopus 로고    scopus 로고
    • The HD mutation causes progressive lethal neurological disease in mice expressing reduced levels of huntingtin
    • Auerbach, W. et al. The HD mutation causes progressive lethal neurological disease in mice expressing reduced levels of huntingtin. Human molecular genetics 10, 2515-2523 (2001).
    • (2001) Human Molecular Genetics , vol.10 , pp. 2515-2523
    • Auerbach, W.1
  • 21
    • 84937643751 scopus 로고    scopus 로고
    • Attention-Deficit/Hyperactivity Disorder-like Phenotype in a Mouse Model with Impaired Actin Dynamics
    • Zimmermann, A. M. et al. Attention-Deficit/Hyperactivity Disorder-like Phenotype in a Mouse Model with Impaired Actin Dynamics. Biol Psychiatry, doi: 10.1016/j.biopsych.2014.03.011 (2014).
    • (2014) Biol Psychiatry
    • Zimmermann, A.M.1
  • 22
    • 58149337412 scopus 로고    scopus 로고
    • Ex vivo imaging of motor axon dynamics in murine triangularis sterni explants
    • Kerschensteiner, M., Reuter, M. S., Lichtman, J. W. & Misgeld, T. Ex vivo imaging of motor axon dynamics in murine triangularis sterni explants. Nat Protoc 3, 1645-1653, doi: 10.1038/nprot.2008.160 (2008).
    • (2008) Nat Protoc , vol.3 , pp. 1645-1653
    • Kerschensteiner, M.1    Reuter, M.S.2    Lichtman, J.W.3    Misgeld, T.4
  • 23
    • 13944274830 scopus 로고    scopus 로고
    • Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2
    • Wang, P. et al. Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2. J Neurosci 25, 1219-1225 (2005).
    • (2005) J Neurosci , vol.25 , pp. 1219-1225
    • Wang, P.1
  • 24
    • 84904536244 scopus 로고    scopus 로고
    • Differential role of APP and APLPs for neuromuscular synaptic morphology and function
    • Klevanski, M. et al. Differential role of APP and APLPs for neuromuscular synaptic morphology and function. Molecular and cellular neurosciences 61, 201-210, doi: 10.1016/j.mcn.2014.06.004 (2014).
    • (2014) Molecular and Cellular Neurosciences , vol.61 , pp. 201-210
    • Klevanski, M.1
  • 25
    • 34447640166 scopus 로고    scopus 로고
    • The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice
    • Ring, S. et al. The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice. J Neurosci 27, 7817-7826 (2007).
    • (2007) J Neurosci , vol.27 , pp. 7817-7826
    • Ring, S.1
  • 26
    • 79952903577 scopus 로고    scopus 로고
    • A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function
    • Barbagallo, A. P., Wang, Z., Zheng, H. & D'Adamio, L. A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function. J Biol Chem 286, 8717-8721, doi: 10.1074/jbc.C111.219873 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 8717-8721
    • Barbagallo, A.P.1    Wang, Z.2    Zheng, H.3    D'Adamio, L.4
  • 27
    • 69749115919 scopus 로고    scopus 로고
    • Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis
    • doi: 29/35/10788
    • Wang, Z. et al. Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis. J Neurosci 29, 10788-10801, doi: 29/35/10788 (2009).
    • (2009) J Neurosci , vol.29 , pp. 10788-10801
    • Wang, Z.1
  • 28
    • 79957909084 scopus 로고    scopus 로고
    • APP and APLP2 are essential at PNS and CNS synapses for transmission, spatial learning and LTP
    • Weyer, S. W. et al. APP and APLP2 are essential at PNS and CNS synapses for transmission, spatial learning and LTP. The EMBO journal 30, 2266-2280, doi: 10.1038/emboj.2011.119 (2011).
    • (2011) The EMBO Journal , vol.30 , pp. 2266-2280
    • Weyer, S.W.1
  • 29
    • 78049267204 scopus 로고    scopus 로고
    • Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP
    • doi: 1012568107
    • Li, H. et al. Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP. Proc Natl Acad Sci USA 107, 17362-17367, doi: 1012568107 (2010).
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17362-17367
    • Li, H.1
  • 30
    • 84949599741 scopus 로고    scopus 로고
    • The APP intracellular domain is required for normal synaptic morphology, synaptic plasticity, and hippocampus-dependent behavior
    • Klevanski, M. et al. The APP Intracellular Domain Is Required for Normal Synaptic Morphology, Synaptic Plasticity, and Hippocampus-Dependent Behavior. J Neurosci 35, 16018-16033, doi: 10.1523/JNEUROSCI.2009-15.2015 (2015).
    • (2015) J Neurosci , vol.35 , pp. 16018-16033
    • Klevanski, M.1
  • 31
    • 84973431930 scopus 로고    scopus 로고
    • FE65: Roles beyond amyloid precursor protein processing
    • Chow, W. N., Cheung, H. N., Li, W. & Lau, K. F. FE65: Roles beyond amyloid precursor protein processing. Cell Mol Biol Lett 20, 66-87, doi: 10.1515/cmble-2015-0002 (2015).
    • (2015) Cell Mol Biol Lett , vol.20 , pp. 66-87
    • Chow, W.N.1    Cheung, H.N.2    Li, W.3    Lau, K.F.4
  • 32
    • 0346728801 scopus 로고    scopus 로고
    • Long-term potentiation and memory
    • Lynch, M. A. Long-term potentiation and memory. Physiol Rev 84, 87-136, doi: 10.1152/physrev.00014.2003 (2004).
    • (2004) Physiol Rev , vol.84 , pp. 87-136
    • Lynch, M.A.1
  • 33
    • 84857720147 scopus 로고    scopus 로고
    • AICD nuclear signaling and its possible contribution to Alzheimer's disease
    • Konietzko, U. AICD nuclear signaling and its possible contribution to Alzheimer's disease. Curr Alzheimer Res 9, 200-216 (2012).
    • (2012) Curr Alzheimer Res , vol.9 , pp. 200-216
    • Konietzko, U.1
  • 34
    • 72849144007 scopus 로고    scopus 로고
    • Structural and functional characterization of a novel FE65 protein product upregulated in cognitively impaired FE65 knockout mice
    • Cool, B. H., Zitnik, G., Martin, G. M. & Hu, Q. Structural and functional characterization of a novel FE65 protein product upregulated in cognitively impaired FE65 knockout mice. J Neurochem 112, 410-419, doi: 10.1111/j.1471-4159.2009.06456.x (2010).
    • (2010) J Neurochem , vol.112 , pp. 410-419
    • Cool, B.H.1    Zitnik, G.2    Martin, G.M.3    Hu, Q.4
  • 35
    • 33845646925 scopus 로고    scopus 로고
    • Genetic analysis of Mint/X11 proteins: Essential presynaptic functions of a neuronal adaptor protein family
    • Ho, A. et al. Genetic analysis of Mint/X11 proteins: essential presynaptic functions of a neuronal adaptor protein family. J Neurosci 26, 13089-13101, doi: 10.1523/JNEUROSCI.2855-06.2006 (2006).
    • (2006) J Neurosci , vol.26 , pp. 13089-13101
    • Ho, A.1
  • 36
    • 80053566644 scopus 로고    scopus 로고
    • FE65 proteins regulate NMDA receptor activation-induced amyloid precursor protein processing
    • Suh, J., Lyckman, A., Wang, L., Eckman, E. A. & Guenette, S. Y. FE65 proteins regulate NMDA receptor activation-induced amyloid precursor protein processing. J Neurochem 119, 377-388, doi: 10.1111/j.1471-4159.2011.07419.x (2011).
    • (2011) J Neurochem , vol.119 , pp. 377-388
    • Suh, J.1    Lyckman, A.2    Wang, L.3    Eckman, E.A.4    Guenette, S.Y.5
  • 37
    • 84949114764 scopus 로고    scopus 로고
    • Rotarod training in mice is associated with changes in brain structure observable with multimodal MRI
    • Scholz, J., Niibori, Y., Frankland, P. W. & Lerch, J. P. Rotarod training in mice is associated with changes in brain structure observable with multimodal MRI. Neuroimage 107, 182-189, doi: 10.1016/j.neuroimage.2014.12.003 (2015).
    • (2015) Neuroimage , vol.107 , pp. 182-189
    • Scholz, J.1    Niibori, Y.2    Frankland, P.W.3    Lerch, J.P.4
  • 38
    • 77957254613 scopus 로고    scopus 로고
    • Genetic dissection of the amyloid precursor protein in developmental function and amyloid pathogenesis
    • M1
    • Li, H. et al. Genetic dissection of the amyloid precursor protein in developmental function and amyloid pathogenesis. J Biol Chem 285, 30598-30605, doi: M110.137729/jbc.M110.137729 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 30598-30605
    • Li, H.1
  • 39
    • 84949599741 scopus 로고    scopus 로고
    • The APP Intracellular domain is required for normal synaptic morphology, synaptic plasticity, and hippocampus-dependent behavior
    • Klevanski, M. et al. The APP Intracellular Domain Is Required for Normal Synaptic Morphology, Synaptic Plasticity, and Hippocampus-Dependent Behavior. J Neurosci 35, 16018-16033, doi: 10.1523/JNEUROSCI.2009-15.2015 (2015).
    • (2015) J Neurosci , vol.35 , pp. 16018-16033
    • Klevanski, M.1
  • 40
    • 85024947233 scopus 로고    scopus 로고
    • APP interacts with LRP4 and agrin to coordinate the development of the neuromuscular junction in mice
    • Choi, H. Y. et al. APP interacts with LRP4 and agrin to coordinate the development of the neuromuscular junction in mice. eLife 2, e00220, doi: 10.7554/eLife.00220 (2013).
    • (2013) ELife , vol.2
    • Choi, H.Y.1
  • 41
    • 53649090611 scopus 로고    scopus 로고
    • O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors
    • Kim, M. L. et al. O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors. Molecular and cellular neurosciences 39, 452-464, doi: 10.1016/j.mcn.2008.07.026 (2008).
    • (2008) Molecular and Cellular Neurosciences , vol.39 , pp. 452-464
    • Kim, M.L.1
  • 42
    • 80855153205 scopus 로고    scopus 로고
    • Agrin binds to the N-terminal region of Lrp4 protein and stimulates association between Lrp4 and the first immunoglobulin-like domain in muscle-specific kinase (MuSK)
    • Zhang, W., Coldefy, A. S., Hubbard, S. R. & Burden, S. J. Agrin binds to the N-terminal region of Lrp4 protein and stimulates association between Lrp4 and the first immunoglobulin-like domain in muscle-specific kinase (MuSK). J Biol Chem 286, 40624-40630, doi: 10.1074/jbc.M111.279307 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 40624-40630
    • Zhang, W.1    Coldefy, A.S.2    Hubbard, S.R.3    Burden, S.J.4
  • 43
    • 84865963074 scopus 로고    scopus 로고
    • Distinct roles of muscle and motoneuron LRP4 in neuromuscular junction formation
    • Wu, H. et al. Distinct roles of muscle and motoneuron LRP4 in neuromuscular junction formation. Neuron 75, 94-107, doi: 10.1016/j.neuron.2012.04.033 (2012).
    • (2012) Neuron , vol.75 , pp. 94-107
    • Wu, H.1
  • 44
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly, W. T., Zheng, J. B., Guenette, S. Y. & Selkoe, D. J. The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J Biol Chem 276, 40288-40292 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 45
    • 0034680938 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains
    • Lambrechts, A. et al. cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains. J Biol Chem 275, 36143-36151, doi: 10.1074/jbc.M006274200 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 36143-36151
    • Lambrechts, A.1
  • 46
    • 0038722283 scopus 로고    scopus 로고
    • The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo
    • Sabo, S. L., Ikin, A. F., Buxbaum, J. D. & Greengard, P. The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo. J Neurosci 23, 5407-5415 (2003).
    • (2003) J Neurosci , vol.23 , pp. 5407-5415
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 47
    • 0021173996 scopus 로고
    • Developments of a water-maze procedure for studying spatial learning in the rat
    • Morris, R. Developments of a water-maze procedure for studying spatial learning in the rat. J Neurosci Methods 11, 47-60 (1984).
    • (1984) J Neurosci Methods , vol.11 , pp. 47-60
    • Morris, R.1
  • 48
    • 84862596869 scopus 로고    scopus 로고
    • Clinical testing and spinal cord removal in a mouse model for amyotrophic lateral sclerosis (ALS)
    • Gunther, R. et al. Clinical testing and spinal cord removal in a mouse model for amyotrophic lateral sclerosis (ALS). J Vis Exp, doi: 10.3791/3936 (2012).
    • (2012) J Vis Exp
    • Gunther, R.1
  • 49
    • 84871668254 scopus 로고    scopus 로고
    • Vertebral landmarks for the identification of spinal cord segments in the mouse
    • Harrison, M. et al. Vertebral landmarks for the identification of spinal cord segments in the mouse. Neuroimage 68, 22-29, doi: 10.1016/j.neuroimage.2012.11.048 (2013).
    • (2013) Neuroimage , vol.68 , pp. 22-29
    • Harrison, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.