메뉴 건너뛰기




Volumn 16, Issue 22, 1996, Pages 7161-7170

Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex

Author keywords

actomyosin; cytoskeleton; drebrin; plasticity; spine; synapse

Indexed keywords

DREBRIN;

EID: 0029825623     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.16-22-07161.1996     Document Type: Article
Times cited : (197)

References (57)
  • 1
    • 0025939609 scopus 로고
    • Effect of transient cerebral ischemia in mongolian gerbils on synaptic vesicle protein (SVP-38) and developmentally regulated brain protein (drebrin)
    • Arai H, Sato K, Uto A, Yasumoto Y (1991) Effect of transient cerebral ischemia in mongolian gerbils on synaptic vesicle protein (SVP-38) and developmentally regulated brain protein (drebrin). Neurosci Res Commun 9:143-150.
    • (1991) Neurosci Res Commun , vol.9 , pp. 143-150
    • Arai, H.1    Sato, K.2    Uto, A.3    Yasumoto, Y.4
  • 2
    • 0028306902 scopus 로고
    • Rat myr 4 defines a novel subclass of myosin I: Identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity
    • Bähler M, Kroschewski R, Stöffler H-E, Behrmann T (1994) Rat myr 4 defines a novel subclass of myosin I: identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity. J Cell Biol 126:375-389.
    • (1994) J Cell Biol , vol.126 , pp. 375-389
    • Bähler, M.1    Kroschewski, R.2    Stöffler, H.-E.3    Behrmann, T.4
  • 3
    • 0027520283 scopus 로고
    • The metabotropic glutamate receptor (mGluR1α) is concentrated at perisynaptic membrane of neuronal subpopulations as detected by immunogold reaction
    • Baude A, Nusser Z, Roberts JDB, Mulvihill E, McIlhinney RAJ, Somogyi P (1993) The metabotropic glutamate receptor (mGluR1α) is concentrated at perisynaptic membrane of neuronal subpopulations as detected by immunogold reaction. Neuron 11:771-787.
    • (1993) Neuron , vol.11 , pp. 771-787
    • Baude, A.1    Nusser, Z.2    Roberts, J.D.B.3    Mulvihill, E.4    McIlhinney, R.A.J.5    Somogyi, P.6
  • 4
    • 0028262271 scopus 로고
    • Synaptic and nonsynaptic localization of the GluR1 subunit of the AMPA-type excitatory amino acid receptor in the rat cerebellum
    • Baude A, Molnar E, Latawiec D, McIlhinney RAJ, Somogyi P (1994) Synaptic and nonsynaptic localization of the GluR1 subunit of the AMPA-type excitatory amino acid receptor in the rat cerebellum. J Neurosci 14:2830-2843.
    • (1994) J Neurosci , vol.14 , pp. 2830-2843
    • Baude, A.1    Molnar, E.2    Latawiec, D.3    McIlhinney, R.A.J.4    Somogyi, P.5
  • 5
    • 0018759277 scopus 로고
    • Neuronal plasticity in the chick brain: Morphological effects of visual experience on neurones in hyperstriatum accessorium
    • Bradley P, Horn G (1979) Neuronal plasticity in the chick brain: morphological effects of visual experience on neurones in hyperstriatum accessorium. Brain Res 162:148-153.
    • (1979) Brain Res , vol.162 , pp. 148-153
    • Bradley, P.1    Horn, G.2
  • 6
    • 0020451774 scopus 로고
    • Rapid dendritic spine stem shortening during one-trial learning: The honeybee's first orientation flight
    • Brandon JG, Coss RG (1982) Rapid dendritic spine stem shortening during one-trial learning: the honeybee's first orientation flight. Brain Res 252:51-61.
    • (1982) Brain Res , vol.252 , pp. 51-61
    • Brandon, J.G.1    Coss, R.G.2
  • 7
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss TVP, Collingridge GL (1993) A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361:31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.P.1    Collingridge, G.L.2
  • 8
    • 0020586415 scopus 로고
    • Identification of fodrin as a major calmodulin-binding protein in postsynaptic density preparations
    • Carlin RK, Bartelt DC, Siekevitz P (1983) Identification of fodrin as a major calmodulin-binding protein in postsynaptic density preparations. J Cell Biol 96:443-448.
    • (1983) J Cell Biol , vol.96 , pp. 443-448
    • Carlin, R.K.1    Bartelt, D.C.2    Siekevitz, P.3
  • 9
    • 0021133515 scopus 로고
    • Transient and enduring morphological correlates of synaptic activity and efficacy change in the rat hippocampal slice
    • Chang F-LF, Greenough WT (1984) Transient and enduring morphological correlates of synaptic activity and efficacy change in the rat hippocampal slice. Brain Res 309:34-46.
    • (1984) Brain Res , vol.309 , pp. 34-46
    • Chang, F.-L.F.1    Greenough, W.T.2
  • 10
    • 0017396421 scopus 로고
    • The structure of postsynaptic densities isolated from dog cerebral cortex. I. Overall morphology and protein composition
    • Cohen RS, Blomberg F, Berzins K, Siekevitz P (1977) The structure of postsynaptic densities isolated from dog cerebral cortex. I. Overall morphology and protein composition. J Cell Biol 74:181-203.
    • (1977) J Cell Biol , vol.74 , pp. 181-203
    • Cohen, R.S.1    Blomberg, F.2    Berzins, K.3    Siekevitz, P.4
  • 11
    • 0018191999 scopus 로고
    • Spine stems on tectal interneurons in jewel fish are shortened by social stimulation
    • Coss RG, Globus A (1978) Spine stems on tectal interneurons in jewel fish are shortened by social stimulation. Science 200:787-789.
    • (1978) Science , vol.200 , pp. 787-789
    • Coss, R.G.1    Globus, A.2
  • 12
    • 0020960074 scopus 로고
    • Synapsin I (protein I), a nerve terminal-specific phosphoprotein. II. Its specific association with synaptic vesicles demonstrated by immunocytochemistry in agarose-embedded synaptosomes
    • DeCamilli P, Harris Jr SM, Huttner WB, Greengard P (1983) Synapsin I (protein I), a nerve terminal-specific phosphoprotein. II. Its specific association with synaptic vesicles demonstrated by immunocytochemistry in agarose-embedded synaptosomes. J Cell Biol 96:1355-1373.
    • (1983) J Cell Biol , vol.96 , pp. 1355-1373
    • DeCamilli, P.1    Harris Jr., S.M.2    Huttner, W.B.3    Greengard, P.4
  • 13
    • 0023038983 scopus 로고
    • Changes in the numerical density of synaptic contacts with long-term potentiation in the hippocampal dentate gyrus
    • Desmond NL, Levy WB (1986) Changes in the numerical density of synaptic contacts with long-term potentiation in the hippocampal dentate gyrus. J Comp Neurol 253:466-475.
    • (1986) J Comp Neurol , vol.253 , pp. 466-475
    • Desmond, N.L.1    Levy, W.B.2
  • 14
    • 0020817020 scopus 로고
    • Evidence for the concentration of F-actin and myosin in synapses and in the plasmalemmal zone of axons
    • Drenckhahn D, Kaiser H-W (1983) Evidence for the concentration of F-actin and myosin in synapses and in the plasmalemmal zone of axons. Eur J Cell Biol 31:235-240.
    • (1983) Eur J Cell Biol , vol.31 , pp. 235-240
    • Drenckhahn, D.1    Kaiser, H.-W.2
  • 15
    • 0026642525 scopus 로고
    • Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: A novel calmodulin-binding myosin
    • Espindola FS, Espreafico EM, Coelho MV, Martins AR, Costa FRC, Mooseker MS, Larson RE (1992) Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. J Cell Biol 118:359-368.
    • (1992) J Cell Biol , vol.118 , pp. 359-368
    • Espindola, F.S.1    Espreafico, E.M.2    Coelho, M.V.3    Martins, A.R.4    Costa, F.R.C.5    Mooseker, M.S.6    Larson, R.E.7
  • 16
  • 17
    • 0017345319 scopus 로고
    • Long-lasting morphological changes in dendritic spines of dentate granular cells following stimulation of the entorhinal area
    • Fifkova E, Van Harreveld A (1977) Long-lasting morphological changes in dendritic spines of dentate granular cells following stimulation of the entorhinal area. J Neurocytol 6:211-230.
    • (1977) J Neurocytol , vol.6 , pp. 211-230
    • Fifkova, E.1    Van Harreveld, A.2
  • 18
    • 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
  • 19
    • 0028334953 scopus 로고
    • 2+ concentration exploring possible bases for a sliding synaptic modification threshold
    • 2+ concentration exploring possible bases for a sliding synaptic modification threshold. Proc Natl Acad Sci USA 91:3941-3945.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3941-3945
    • Gold, J.I.1    Bear, M.F.2
  • 20
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease
    • Harigaya Y, Shoji M, Shirao T, Hirai S (1996) Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. J Neurosci Res 43:87-92.
    • (1996) J Neurosci Res , vol.43 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 22
    • 0024473444 scopus 로고
    • Dendritic spines of CA1 pyramidal cells in the rat hippocampus: Serial electron microscopy with reference to their biophysical characteristics
    • Harris KM, Stevens JK (1989) Dendritic spines of CA1 pyramidal cells in the rat hippocampus: serial electron microscopy with reference to their biophysical characteristics. J Neurosci 9:2982-2997.
    • (1989) J Neurosci , vol.9 , pp. 2982-2997
    • Harris, K.M.1    Stevens, J.K.2
  • 23
    • 0026734317 scopus 로고
    • Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: Implications for the maturation of synaptic physiology and long-term potentiation
    • Harris DM, Jensen FE, Tsao BH (1992) Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: implications for the maturation of synaptic physiology and long-term potentiation. J Neurosci 12:2685-2705.
    • (1992) J Neurosci , vol.12 , pp. 2685-2705
    • Harris, D.M.1    Jensen, F.E.2    Tsao, B.H.3
  • 24
    • 0029080517 scopus 로고
    • Repeated confocal imaging of individual dendritic spines in the living hippocampal slice: Evidence for changes in length and orientation associated with chemically induced LTP
    • Hosokawa T, Rusakov DA, Bliss TVP, Fine A (1995) Repeated confocal imaging of individual dendritic spines in the living hippocampal slice: evidence for changes in length and orientation associated with chemically induced LTP. J Neurosci 15:5560-5573.
    • (1995) J Neurosci , vol.15 , pp. 5560-5573
    • Hosokawa, T.1    Rusakov, D.A.2    Bliss, T.V.P.3    Fine, A.4
  • 25
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin
    • Ishikawa R, Yamashiro S, Matsumura F (1989) Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. J Biol Chem 264:7490-7497.
    • (1989) J Biol Chem , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 26
    • 0028139040 scopus 로고
    • Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
    • Ishikawa R, Hayashi K, Shirao T, Xue Y, Takagi T, Sasaki Y, Kohama K (1994) Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J Biol Chem 269:29928-29933.
    • (1994) J Biol Chem , vol.269 , pp. 29928-29933
    • Ishikawa, R.1    Hayashi, K.2    Shirao, T.3    Xue, Y.4    Takagi, T.5    Sasaki, Y.6    Kohama, K.7
  • 27
    • 0038823489 scopus 로고
    • Biochemical and immunochemical evidence that the "major postsynaptic density protein" is a subunit of a calmodulin-dependent protein kinase
    • Kennedy MB, Bennett MK, Erondu NE (1983) Biochemical and immunochemical evidence that the "major postsynaptic density protein" is a subunit of a calmodulin-dependent protein kinase. Proc Natl Acad Sci USA 80:7357-7361.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 7357-7361
    • Kennedy, M.B.1    Bennett, M.K.2    Erondu, N.E.3
  • 29
    • 0027447125 scopus 로고
    • The function of dendritic spines: Devices subserving biochemical rather than electrical compartmentalization
    • Koch C, Zador A (1993) The function of dendritic spines: devices subserving biochemical rather than electrical compartmentalization. J Neurosci 13:413-422.
    • (1993) J Neurosci , vol.13 , pp. 413-422
    • Koch, C.1    Zador, A.2
  • 30
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate
    • Kodama T, Fukui K, Kometani K (1986) The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. J Biochem 99:1465-1472.
    • (1986) J Biochem , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 31
    • 0027289194 scopus 로고
    • Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene
    • Kojima N, Shirao T, Obata K (1993) Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene. Mol Brain Res 19:101-114.
    • (1993) Mol Brain Res , vol.19 , pp. 101-114
    • Kojima, N.1    Shirao, T.2    Obata, K.3
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0020550407 scopus 로고
    • Cytoplasmic organization in cerebellar dendritic spines
    • Landis DMD, 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.D.1    Reese, T.S.2
  • 34
    • 0018936198 scopus 로고
    • Brief bursts of high-frequency stimulation produce two types of structural change in rat hippocampus
    • Lee KS, Schottler F, Oliver M, Lynch G (1980) Brief bursts of high-frequency stimulation produce two types of structural change in rat hippocampus. J Neurophysiol 44:247-258.
    • (1980) J Neurophysiol , vol.44 , pp. 247-258
    • Lee, K.S.1    Schottler, F.2    Oliver, M.3    Lynch, G.4
  • 36
    • 0024557848 scopus 로고
    • In situ localization of myosin and actin in dendritic spines with the immunogold technique
    • Morales M, Fifkova E (1989) In situ localization of myosin and actin in dendritic spines with the immunogold technique. J Comp Neurol 279:666-674.
    • (1989) J Comp Neurol , vol.279 , pp. 666-674
    • Morales, M.1    Fifkova, E.2
  • 37
    • 0022642415 scopus 로고
    • Identification of a synaptic vesicle-specific 38,000-dalton protein by monoclonal antibodies
    • Obata K, Nishiye H, Fujita S, Shirao T, Inoue H, Uchizono K (1986) Identification of a synaptic vesicle-specific 38,000-dalton protein by monoclonal antibodies. Brain Res 375:37-48.
    • (1986) Brain Res , vol.375 , pp. 37-48
    • Obata, K.1    Nishiye, H.2    Fujita, S.3    Shirao, T.4    Inoue, H.5    Uchizono, K.6
  • 38
    • 0025832505 scopus 로고
    • In vitro movement of actin filaments on gizzard smooth muscle myosin: Requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon
    • Tokyo
    • Okagaki T, Higashi-Fujime S, Ishikawa R, Kohama K (1991) In vitro movement of actin filaments on gizzard smooth muscle myosin: requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon. J Biochem (Tokyo) 109:858-866.
    • (1991) J Biochem , vol.109 , pp. 858-866
    • Okagaki, T.1    Higashi-Fujime, S.2    Ishikawa, R.3    Kohama, K.4
  • 39
    • 0028860053 scopus 로고
    • Morphological analysis of dendritic spine development in primary cultures of hippocampal neurons
    • Papa M, Bundman MC, Greenberger V, Segal M (1995) Morphological analysis of dendritic spine development in primary cultures of hippocampal neurons. J Neurosci 15:1-11.
    • (1995) J Neurosci , vol.15 , pp. 1-11
    • Papa, M.1    Bundman, M.C.2    Greenberger, V.3    Segal, M.4
  • 40
    • 0028087773 scopus 로고
    • The NMDA receptor subunits NR2A and NR2B show histological and ultrastructural localization patterns similar to those of NR1
    • Petralia RS, Wang Y-X, Wenthold RJ (1994a) The NMDA receptor subunits NR2A and NR2B show histological and ultrastructural localization patterns similar to those of NR1. J Neurosci 14:6102-6120.
    • (1994) J Neurosci , vol.14 , pp. 6102-6120
    • Petralia, R.S.1    Wang, Y.-X.2    Wenthold, R.J.3
  • 41
    • 0028157362 scopus 로고
    • Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective anti-peptide antibody
    • Petralia RS, Yokotani N, Wenthold RJ (1994b) Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective anti-peptide antibody. J Neurosci 14:667-696.
    • (1994) J Neurosci , vol.14 , pp. 667-696
    • Petralia, R.S.1    Yokotani, N.2    Wenthold, R.J.3
  • 42
    • 0016251748 scopus 로고
    • Dendritic spine "dysgenesis" and mental retardation
    • Purpura DP (1974) Dendritic spine "dysgenesis" and mental retardation. Science 186:1126-1128.
    • (1974) Science , vol.186 , pp. 1126-1128
    • Purpura, D.P.1
  • 43
    • 0027258451 scopus 로고
    • Calcium-induced actin depolymerization reduces NMDA channel activity
    • Rosenmund C, Westbrook GL (1993) Calcium-induced actin depolymerization reduces NMDA channel activity. Neuron 10:805-814.
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 44
    • 0030040876 scopus 로고    scopus 로고
    • Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones
    • Sasaki Y, Hayashi K, Shirao T, Ishikawa R. Kohama K (1996) Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J Neurochem 66:980-988.
    • (1996) J Neurochem , vol.66 , pp. 980-988
    • Sasaki, Y.1    Hayashi, K.2    Shirao, T.3    Ishikawa, R.4    Kohama, K.5
  • 45
    • 85047673845 scopus 로고
    • The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: A review
    • Shirao T (1995) The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: a review. J Biochem 117:231-236.
    • (1995) J Biochem , vol.117 , pp. 231-236
    • Shirao, T.1
  • 46
    • 0021964771 scopus 로고
    • Two acidic proteins associated with brain development in chick embryo
    • Shirao T, Obata K (1985) Two acidic proteins associated with brain development in chick embryo. J Neurochem 44:1210-1216.
    • (1985) J Neurochem , vol.44 , pp. 1210-1216
    • Shirao, T.1    Obata, K.2
  • 47
    • 0022797037 scopus 로고
    • Immunochemical homology of 3 developmentally regulated brain proteins and their developmental change in neuronal distribution
    • Shirao T, Obata K (1986) Immunochemical homology of 3 developmentally regulated brain proteins and their developmental change in neuronal distribution. Dev Brain Res 29:233-244.
    • (1986) Dev Brain Res , vol.29 , pp. 233-244
    • Shirao, T.1    Obata, K.2
  • 48
    • 0023243989 scopus 로고
    • Localization of a developmentally regulated neuron-specific protein S54 in dendrites as revealed by immunoelectron microscopy
    • Shirao T, Inoue HK, Kano Y, Obata K (1987) Localization of a developmentally regulated neuron-specific protein S54 in dendrites as revealed by immunoelectron microscopy. Brain Res 413:374-378.
    • (1987) Brain Res , vol.413 , pp. 374-378
    • Shirao, T.1    Inoue, H.K.2    Kano, Y.3    Obata, K.4
  • 50
    • 0026512294 scopus 로고
    • Cloning of drebrin a and induction of neurite-like processes in drebrin-transfected cells
    • Shirao T, Kojima N, Obata K (1992) Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. NeuroReport 3:109-112.
    • (1992) NeuroReport , vol.3 , pp. 109-112
    • Shirao, T.1    Kojima, N.2    Obata, K.3
  • 52
    • 0025900837 scopus 로고
    • Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems
    • Sobue K, Sellers JR (1991) Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems. J Biol Chem 266:12115-12118.
    • (1991) J Biol Chem , vol.266 , pp. 12115-12118
    • Sobue, K.1    Sellers, J.R.2
  • 53
    • 0028219293 scopus 로고
    • Localization and characterization of gelsolin in nervous tissues: Gelsolin is specifically enriched in myelin-forming cells
    • Tanaka J, Sobue K (1994) Localization and characterization of gelsolin in nervous tissues: gelsolin is specifically enriched in myelin-forming cells. J Neurosci 14:1038-1052.
    • (1994) J Neurosci , vol.14 , pp. 1038-1052
    • Tanaka, J.1    Sobue, K.2
  • 54
    • 0027756675 scopus 로고
    • Gelsolin is localized in neuronal growth cones
    • Tanaka J, Kira M, Sobue K (1993) Gelsolin is localized in neuronal growth cones. Dev Brain Res 76:268-271.
    • (1993) Dev Brain Res , vol.76 , pp. 268-271
    • Tanaka, J.1    Kira, M.2    Sobue, K.3
  • 55
    • 0017236464 scopus 로고
    • Swelling of dendritic spines in the fascia dentata after stimulation of the perforant fibers as a mechanism of post-tetanic potentiation
    • Van Harreveld A, Fifkova E (1975) Swelling of dendritic spines in the fascia dentata after stimulation of the perforant fibers as a mechanism of post-tetanic potentiation. Exp Neurol 49:736-749.
    • (1975) Exp Neurol , vol.49 , pp. 736-749
    • Van Harreveld, A.1    Fifkova, E.2
  • 57
    • 0026779476 scopus 로고
    • Tissue distribution and subcellular localization of mammalian myosin I
    • Wagner MC, Barylko B, Albanesi JP (1992) Tissue distribution and subcellular localization of mammalian myosin I. J Cell Biol 119:163-170.
    • (1992) J Cell Biol , vol.119 , pp. 163-170
    • Wagner, M.C.1    Barylko, B.2    Albanesi, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.