메뉴 건너뛰기




Volumn 164, Issue 3, 2009, Pages 1020-1030

Functional difference of receptor-type protein tyrosine phosphatase ζ/β isoforms in neurogenesis of hippocampal neurons

Author keywords

brain; culture; extracellular matrix; glycosaminoglycan; phosphorylation; protein kinase

Indexed keywords

ISOPROTEIN; PHOSPHATASE; PROTEOCHONDROITIN SULFATE; RECEPTOR TYPE PROTEIN TYROSINE PHOSPHATASE ZETA; UNCLASSIFIED DRUG;

EID: 70350549874     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2009.09.012     Document Type: Article
Times cited : (12)

References (46)
  • 1
    • 0037385217 scopus 로고    scopus 로고
    • Junctional protein MAGI-3 interacts with receptor tyrosine phosphataseβ (RPTPβ) and tyrosine-phosphorylated proteins
    • Adamsky K., Arnold K., Sabanay H., and Peles E. Junctional protein MAGI-3 interacts with receptor tyrosine phosphataseβ (RPTPβ) and tyrosine-phosphorylated proteins. J Cell Sci 116 (2002) 1279-1289
    • (2002) J Cell Sci , vol.116 , pp. 1279-1289
    • Adamsky, K.1    Arnold, K.2    Sabanay, H.3    Peles, E.4
  • 2
    • 0031718204 scopus 로고    scopus 로고
    • Differential molecular interactions of β-catenin and plakoglobin in adhesion, signaling and cancer
    • Ben-Ze'ev A., and Geiger B. Differential molecular interactions of β-catenin and plakoglobin in adhesion, signaling and cancer. Curr Opin Cell Biol 10 (1998) 629-639
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 629-639
    • Ben-Ze'ev, A.1    Geiger, B.2
  • 3
    • 57649155878 scopus 로고    scopus 로고
    • Metalloprotease and gamma-secretase-mediated cleavage of protein-tyrosine phosphatase receptor type Z
    • Chow J.P., Fujikawa A., Shintani H., Suzuki R., and Noda M. Metalloprotease and gamma-secretase-mediated cleavage of protein-tyrosine phosphatase receptor type Z. J Biol Chem 283 (2008) 30879-30889
    • (2008) J Biol Chem , vol.283 , pp. 30879-30889
    • Chow, J.P.1    Fujikawa, A.2    Shintani, H.3    Suzuki, R.4    Noda, M.5
  • 4
    • 10644283190 scopus 로고    scopus 로고
    • Yeast substrate-trapping system for isolating substrates of protein tyrosine phosphatases: isolation of substrates for protein tyrosine phosphatase receptor type z
    • Fukada M., Kawachi H., Fujikawa A., and Noda M. Yeast substrate-trapping system for isolating substrates of protein tyrosine phosphatases: isolation of substrates for protein tyrosine phosphatase receptor type z. Methods 35 (2005) 54-63
    • (2005) Methods , vol.35 , pp. 54-63
    • Fukada, M.1    Kawachi, H.2    Fujikawa, A.3    Noda, M.4
  • 5
    • 33745843619 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase receptor type Z is inactivated by ligand-induced oligomerization
    • Fukada M., Fujikawa A., Chow J.P.H., Ikematsu S., Sakuma S., and Noda M. Protein tyrosine phosphatase receptor type Z is inactivated by ligand-induced oligomerization. FEBS Lett 580 (2006) 4051-4056
    • (2006) FEBS Lett , vol.580 , pp. 4051-4056
    • Fukada, M.1    Fujikawa, A.2    Chow, J.P.H.3    Ikematsu, S.4    Sakuma, S.5    Noda, M.6
  • 6
    • 47049130701 scopus 로고    scopus 로고
    • Receptor type protein tyrosine phosphatase zeta-pleiotrophin signaling controls endocytic trafficking of DNER that regulates neuritogenesis
    • Fukazawa N., Yokoyama S., Eiraku M., Kengaku M., and Maeda N. Receptor type protein tyrosine phosphatase zeta-pleiotrophin signaling controls endocytic trafficking of DNER that regulates neuritogenesis. Mol Cell Biol 28 (2008) 4494-4506
    • (2008) Mol Cell Biol , vol.28 , pp. 4494-4506
    • Fukazawa, N.1    Yokoyama, S.2    Eiraku, M.3    Kengaku, M.4    Maeda, N.5
  • 7
    • 0023245565 scopus 로고
    • Modulation of spectrin-actin assembly by erythrocyte adducin
    • Gardner K., and Bennet V. Modulation of spectrin-actin assembly by erythrocyte adducin. Nature 328 (1987) 359-362
    • (1987) Nature , vol.328 , pp. 359-362
    • Gardner, K.1    Bennet, V.2
  • 8
    • 13544259665 scopus 로고    scopus 로고
    • Neuronal expression of the chondroitin sulfate proteoglycans receptor-type protein-tyrosine phosphataseβ and phosphacan
    • Hayashi N., Miyata S., Yamada M., Kamei K., and Oohira A. Neuronal expression of the chondroitin sulfate proteoglycans receptor-type protein-tyrosine phosphataseβ and phosphacan. Neuroscience 131 (2005) 331-348
    • (2005) Neuroscience , vol.131 , pp. 331-348
    • Hayashi, N.1    Miyata, S.2    Yamada, M.3    Kamei, K.4    Oohira, A.5
  • 9
    • 21544482016 scopus 로고    scopus 로고
    • Synaptic localization of receptor-type protein tyrosine phosphataseζ/β in the cerebral and hippocampal neurons of adult rats
    • Hayashi N., Oohira A., and Miyata S. Synaptic localization of receptor-type protein tyrosine phosphataseζ/β in the cerebral and hippocampal neurons of adult rats. Brain Res 1050 (2005) 163-169
    • (2005) Brain Res , vol.1050 , pp. 163-169
    • Hayashi, N.1    Oohira, A.2    Miyata, S.3
  • 10
    • 0037996880 scopus 로고    scopus 로고
    • Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability
    • Hering H., Lin C.C., and Sheng M. Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability. J Neurosci 23 (2003) 3262-3271
    • (2003) J Neurosci , vol.23 , pp. 3262-3271
    • Hering, H.1    Lin, C.C.2    Sheng, M.3
  • 11
    • 33747199616 scopus 로고    scopus 로고
    • N-syndecan deficiency impairs neural migration in brain
    • Hienola A., Tumova S., Kulesskiy E., and Rauvala H. N-syndecan deficiency impairs neural migration in brain. J Cell Biol 174 (2006) 569-580
    • (2006) J Cell Biol , vol.174 , pp. 569-580
    • Hienola, A.1    Tumova, S.2    Kulesskiy, E.3    Rauvala, H.4
  • 13
    • 0035810942 scopus 로고    scopus 로고
    • Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase ζ/β by the yeast substrate-trapping system
    • Kawachi H., Fujikawa A., Maeda N., and Noda M. Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase ζ/β by the yeast substrate-trapping system. Proc Natl Acad Sci U S A 98 (2001) 6593-6598
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6593-6598
    • Kawachi, H.1    Fujikawa, A.2    Maeda, N.3    Noda, M.4
  • 14
    • 0030005249 scopus 로고    scopus 로고
    • A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments
    • Kuhlman P.A., Hughes C.A., Bennet V., and Fowler V.M. A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments. J Biol Chem 271 (1996) 7986-7991
    • (1996) J Biol Chem , vol.271 , pp. 7986-7991
    • Kuhlman, P.A.1    Hughes, C.A.2    Bennet, V.3    Fowler, V.M.4
  • 16
    • 58149300222 scopus 로고    scopus 로고
    • Actin filament assembly by myristoylated, alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branching
    • Li H., Chen G., Zhou B., and Duan S. Actin filament assembly by myristoylated, alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branching. Mol Biol Cell 19 (2008) 4804-4813
    • (2008) Mol Biol Cell , vol.19 , pp. 4804-4813
    • Li, H.1    Chen, G.2    Zhou, B.3    Duan, S.4
  • 17
    • 0034574572 scopus 로고    scopus 로고
    • Rho GTPases in neuronal morphogenesis
    • Luo L. Rho GTPases in neuronal morphogenesis. Nat Rev Neurosci 1 (2000) 173-180
    • (2000) Nat Rev Neurosci , vol.1 , pp. 173-180
    • Luo, L.1
  • 18
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • Luo L. Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annu Rev Cell Dev Biol 18 (2002) 601-635
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 601-635
    • Luo, L.1
  • 19
    • 0028109453 scopus 로고
    • Multiple receptor-like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycans
    • Maeda N., Hamanaka H., Shintani T., Nishiwaki T., and Noda M. Multiple receptor-like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycans. FEBS Lett 354 (1994) 67-70
    • (1994) FEBS Lett , vol.354 , pp. 67-70
    • Maeda, N.1    Hamanaka, H.2    Shintani, T.3    Nishiwaki, T.4    Noda, M.5
  • 20
    • 0028988519 scopus 로고
    • Purification, characterization and developmental expression of a brain-specific chondroitin sulfate proteoglycans, 6B4 proteoglycan/phosphacan
    • Maeda N., Hamanaka H., Oohira A., and Noda M. Purification, characterization and developmental expression of a brain-specific chondroitin sulfate proteoglycans, 6B4 proteoglycan/phosphacan. Neuroscience 67 (1995) 23-35
    • (1995) Neuroscience , vol.67 , pp. 23-35
    • Maeda, N.1    Hamanaka, H.2    Oohira, A.3    Noda, M.4
  • 21
    • 0029834975 scopus 로고    scopus 로고
    • 6B4 proteoglycan/phosphacan, an extracellular variant of receptor-like protein-tyrosine phosphataseζ/β, binds pleiotrophin/heparin-binding growth-associated molecule (HB-GAM)
    • Maeda N., Nishiwaki T., Shintani T., Hamanaka H., and Noda M. 6B4 proteoglycan/phosphacan, an extracellular variant of receptor-like protein-tyrosine phosphataseζ/β, binds pleiotrophin/heparin-binding growth-associated molecule (HB-GAM). J Biol Chem 271 (1996) 21446-21452
    • (1996) J Biol Chem , vol.271 , pp. 21446-21452
    • Maeda, N.1    Nishiwaki, T.2    Shintani, T.3    Hamanaka, H.4    Noda, M.5
  • 22
    • 0032514145 scopus 로고    scopus 로고
    • Involvement of receptor-like protein tyrosine phosphatase ζ/RPTPβ and its ligand pleiotrophin/heparin-binding growth-associated molecule (HB-GAM) in neuronal migration
    • Maeda N., and Noda M. Involvement of receptor-like protein tyrosine phosphatase ζ/RPTPβ and its ligand pleiotrophin/heparin-binding growth-associated molecule (HB-GAM) in neuronal migration. J Cell Biol 142 (1998) 203-216
    • (1998) J Cell Biol , vol.142 , pp. 203-216
    • Maeda, N.1    Noda, M.2
  • 23
    • 0033617313 scopus 로고    scopus 로고
    • A receptor-like protein-tyrosine phosphatase PTPζ/RPTPβ binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPζ
    • Maeda N., Ichihara-Tanaka K., Kimura T., Kadomatsu K., Muramatsu T., and Noda M. A receptor-like protein-tyrosine phosphatase PTPζ/RPTPβ binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPζ. J Biol Chem 274 (1999) 12474-12479
    • (1999) J Biol Chem , vol.274 , pp. 12474-12479
    • Maeda, N.1    Ichihara-Tanaka, K.2    Kimura, T.3    Kadomatsu, K.4    Muramatsu, T.5    Noda, M.6
  • 24
    • 0036537895 scopus 로고    scopus 로고
    • GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration
    • Manabe R., Kovalenko M., Webb D., and Horwitz A. GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration. J Cell Sci 115 (2002) 1497-1510
    • (2002) J Cell Sci , vol.115 , pp. 1497-1510
    • Manabe, R.1    Kovalenko, M.2    Webb, D.3    Horwitz, A.4
  • 25
    • 0030730256 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans as mediators of axon growth and pathfinding
    • Margolis R.U., and Margolis R.K. Chondroitin sulfate proteoglycans as mediators of axon growth and pathfinding. Cell Tissue Res 290 (1997) 343-348
    • (1997) Cell Tissue Res , vol.290 , pp. 343-348
    • Margolis, R.U.1    Margolis, R.K.2
  • 26
    • 0028298023 scopus 로고
    • Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase
    • Maurel P., Rauch U., Flad M., Margolis R.K., and Margolis R.U. Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase. Proc Natl Acad Sci U S A 91 (1994) 2512-2516
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 2512-2516
    • Maurel, P.1    Rauch, U.2    Flad, M.3    Margolis, R.K.4    Margolis, R.U.5
  • 27
    • 0034646459 scopus 로고    scopus 로고
    • Pleiotrophin signals increased tyrosine phosphorylation of β-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphataseζ/β
    • Meng K., Rodriguez-Pena A., Dimitrov T., Chen W., Yamin M., Noda M., and Deuel T.F. Pleiotrophin signals increased tyrosine phosphorylation of β-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphataseζ/β. Proc Natl Acad Sci U S A 97 (2000) 2603-2608
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2603-2608
    • Meng, K.1    Rodriguez-Pena, A.2    Dimitrov, T.3    Chen, W.4    Yamin, M.5    Noda, M.6    Deuel, T.F.7
  • 28
    • 0035844699 scopus 로고    scopus 로고
    • Plasticity of neurohypophysial terminals with increased hormonal release during dehydration: ultrastructural and biochemical analyses
    • Miyata S., Takamatsu H., Maekawa S., Matsumoto N., Watanabe K., Kiyohara T., and Hatton G.I. Plasticity of neurohypophysial terminals with increased hormonal release during dehydration: ultrastructural and biochemical analyses. J Comp Neurol 434 (2001) 413-427
    • (2001) J Comp Neurol , vol.434 , pp. 413-427
    • Miyata, S.1    Takamatsu, H.2    Maekawa, S.3    Matsumoto, N.4    Watanabe, K.5    Kiyohara, T.6    Hatton, G.I.7
  • 29
    • 26944433440 scopus 로고    scopus 로고
    • Constitution of perineuronal net-like structure of cortical neurons in culture
    • Miyata S., Nishimura Y., Hayashi N., and Oohira A. Constitution of perineuronal net-like structure of cortical neurons in culture. Neuroscience 136 (2005) 95-104
    • (2005) Neuroscience , vol.136 , pp. 95-104
    • Miyata, S.1    Nishimura, Y.2    Hayashi, N.3    Oohira, A.4
  • 31
    • 21544454356 scopus 로고    scopus 로고
    • Age-dependent enhancement of hippocampal long-term potentiation and impairment of spatial learning through the Rho-associated pathway in protein tyrosine phosphatase receptor type ζ-deficient mice
    • Niisato K., Fujikawa A., Komai S., Shintani T., Watanabe E., Sakaguchi G., Katsuura G., Manabe T., and Noda M. Age-dependent enhancement of hippocampal long-term potentiation and impairment of spatial learning through the Rho-associated pathway in protein tyrosine phosphatase receptor type ζ-deficient mice. J Neurosci 25 (2005) 1081-1088
    • (2005) J Neurosci , vol.25 , pp. 1081-1088
    • Niisato, K.1    Fujikawa, A.2    Komai, S.3    Shintani, T.4    Watanabe, E.5    Sakaguchi, G.6    Katsuura, G.7    Manabe, T.8    Noda, M.9
  • 32
    • 0031890646 scopus 로고    scopus 로고
    • Characterization and developmental regulation of proteoglycan-type protein tyrosine phosphataseζ/RPTPβ isoforms
    • Nishiwaki T., Maeada N., and Noda M. Characterization and developmental regulation of proteoglycan-type protein tyrosine phosphataseζ/RPTPβ isoforms. J Biochem 123 (1998) 458-467
    • (1998) J Biochem , vol.123 , pp. 458-467
    • Nishiwaki, T.1    Maeada, N.2    Noda, M.3
  • 33
    • 0034141187 scopus 로고    scopus 로고
    • Molecular interactions of neural chondroitin sulfate proteoglycans in the brain development
    • Oohira A., Matsui F., Tokita Y., Yamauchi S., and Aono S. Molecular interactions of neural chondroitin sulfate proteoglycans in the brain development. Arch Biochem Biophys 374 (2000) 24-34
    • (2000) Arch Biochem Biophys , vol.374 , pp. 24-34
    • Oohira, A.1    Matsui, F.2    Tokita, Y.3    Yamauchi, S.4    Aono, S.5
  • 34
    • 27644505092 scopus 로고    scopus 로고
    • Negative regulation of retinal-neurite extension by β-catenin signaling pathway
    • Ouchi Y., Tabata Y., Arai T., and Watanabe S. Negative regulation of retinal-neurite extension by β-catenin signaling pathway. J Cell Sci 118 (2005) 4473-4483
    • (2005) J Cell Sci , vol.118 , pp. 4473-4483
    • Ouchi, Y.1    Tabata, Y.2    Arai, T.3    Watanabe, S.4
  • 35
    • 24644478602 scopus 로고    scopus 로고
    • Pleiotrophin regulates serine phosphorylation and the cellular distribution of β-adducin through the activation of protein kinase C
    • Pariser H., Herradon G., Ezquerra L., Perez-Pinera P., and Deuel T.F. Pleiotrophin regulates serine phosphorylation and the cellular distribution of β-adducin through the activation of protein kinase C. Proc Natl Acad Sci U S A 102 (2005) 12407-12412
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12407-12412
    • Pariser, H.1    Herradon, G.2    Ezquerra, L.3    Perez-Pinera, P.4    Deuel, T.F.5
  • 36
    • 19744369654 scopus 로고    scopus 로고
    • Pleiotrophin stimulates tyrosine phosphorylation of β-adducin through inactivation of the transmembrane receptor protein tyrosine phosphatase beta/zeta
    • Pariser H., Perez-Pinera P., Ezquerra L., Herradon G., and Deuel T.F. Pleiotrophin stimulates tyrosine phosphorylation of β-adducin through inactivation of the transmembrane receptor protein tyrosine phosphatase beta/zeta. Biochem Biophys Res Commun 332 (2005) 664-669
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 664-669
    • Pariser, H.1    Perez-Pinera, P.2    Ezquerra, L.3    Herradon, G.4    Deuel, T.F.5
  • 38
    • 0032891355 scopus 로고    scopus 로고
    • NMDA receptor activity stabilizes presynaptic retinotectal axons and postsynaptic optic tectal cell dendrites in vivo
    • Rajan I., Witte S., and Cline H.T. NMDA receptor activity stabilizes presynaptic retinotectal axons and postsynaptic optic tectal cell dendrites in vivo. J Neurobiol 38 (1999) 357-368
    • (1999) J Neurobiol , vol.38 , pp. 357-368
    • Rajan, I.1    Witte, S.2    Cline, H.T.3
  • 39
    • 16644381829 scopus 로고    scopus 로고
    • Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development
    • Rosso S.B., Sussman D., Wynshaw-Boris A., and Salinas P.C. Wnt signaling through Dishevelled, Rac and JNK regulates dendritic development. Nat Neurosci 8 (2005) 34-42
    • (2005) Nat Neurosci , vol.8 , pp. 34-42
    • Rosso, S.B.1    Sussman, D.2    Wynshaw-Boris, A.3    Salinas, P.C.4
  • 40
    • 35348860243 scopus 로고    scopus 로고
    • Inhibition of Rho via Arg and p190RhoGAP in the postnatal mouse hippocampus regulates dendritic spine maturation, synapse and dendrite stability, and behavior
    • Sfakianos M.K., Eisman A., Gourley S.L., Bradley W.D., Scheetz A.J., Settleman J., Taylor J.R., Greer C.A., Williams A., and Koleske A.J. Inhibition of Rho via Arg and p190RhoGAP in the postnatal mouse hippocampus regulates dendritic spine maturation, synapse and dendrite stability, and behavior. J Neurosci 27 (2007) 10982-10992
    • (2007) J Neurosci , vol.27 , pp. 10982-10992
    • Sfakianos, M.K.1    Eisman, A.2    Gourley, S.L.3    Bradley, W.D.4    Scheetz, A.J.5    Settleman, J.6    Taylor, J.R.7    Greer, C.A.8    Williams, A.9    Koleske, A.J.10
  • 41
    • 0032524632 scopus 로고    scopus 로고
    • Neurons as well as astrocytes express proteoglycan-type protein tyrosine phosphatase ζ/PTPβ: analysis of mice in which the PTPζ/RPTPβ gene was replaced with the lacZ gene
    • Shintani T., Watanabe E., Maeda N., and Noda M. Neurons as well as astrocytes express proteoglycan-type protein tyrosine phosphatase ζ/PTPβ: analysis of mice in which the PTPζ/RPTPβ gene was replaced with the lacZ gene. Neurosci Lett 247 (1998) 135-138
    • (1998) Neurosci Lett , vol.247 , pp. 135-138
    • Shintani, T.1    Watanabe, E.2    Maeda, N.3    Noda, M.4
  • 42
    • 33646118239 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase receptor type Z is involved in hippocampus-dependent memory formation through dephosphorylation at Y1105on p190 RhoGAP
    • Tamura H., Fukada M., Fujikawa A., and Noda M. Protein tyrosine phosphatase receptor type Z is involved in hippocampus-dependent memory formation through dephosphorylation at Y1105on p190 RhoGAP. Neurosci Lett 399 (2006) 33-38
    • (2006) Neurosci Lett , vol.399 , pp. 33-38
    • Tamura, H.1    Fukada, M.2    Fujikawa, A.3    Noda, M.4
  • 43
    • 0345354676 scopus 로고    scopus 로고
    • A chondroitin sulfate proteoglycan PTPζ/RPTPβ regulates the morphogenesis of Purkinje cell dendrites in the developing cerebellum
    • Tanaka M., Maeda N., Noda M., and Mrunouchi T. A chondroitin sulfate proteoglycan PTPζ/RPTPβ regulates the morphogenesis of Purkinje cell dendrites in the developing cerebellum. J Neurosci 23 (2003) 2804-2814
    • (2003) J Neurosci , vol.23 , pp. 2804-2814
    • Tanaka, M.1    Maeda, N.2    Noda, M.3    Mrunouchi, T.4
  • 44
    • 0034520396 scopus 로고    scopus 로고
    • bFGF stimulates GAP-43 phosphorylation at ser41 and modifies its intracellular localization in cultured hippocampal neurons
    • Tejero-Diez P., Rodriguez-Sanchez P., Martin-Cofreces N.B., and Diez-Guerra F.J. bFGF stimulates GAP-43 phosphorylation at ser41 and modifies its intracellular localization in cultured hippocampal neurons. Mol Cell Neurosci 16 (2000) 766-780
    • (2000) Mol Cell Neurosci , vol.16 , pp. 766-780
    • Tejero-Diez, P.1    Rodriguez-Sanchez, P.2    Martin-Cofreces, N.B.3    Diez-Guerra, F.J.4
  • 45
    • 0242384747 scopus 로고    scopus 로고
    • β-catenin is critical for dendritic morphogenesis
    • Yu X., and Malenka R.C. β-catenin is critical for dendritic morphogenesis. Nat Neurosci 203 (2003) 1169-1177
    • (2003) Nat Neurosci , vol.203 , pp. 1169-1177
    • Yu, X.1    Malenka, R.C.2
  • 46
    • 0037437147 scopus 로고    scopus 로고
    • Synapse formation is regulated by the signaling adaptor GIT1
    • Zhang H., Webb D.J., Asmussen H., and Horwitz A.F. Synapse formation is regulated by the signaling adaptor GIT1. J Cell Biol 161 (2003) 131-142
    • (2003) J Cell Biol , vol.161 , pp. 131-142
    • Zhang, H.1    Webb, D.J.2    Asmussen, H.3    Horwitz, A.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.