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Volumn 61, Issue 2, 2000, Pages 133-168

Phosphorylation of microtubule-associated protein 2 (MAP2) and its relevance for the regulation of the neuronal cytoskeleton function

Author keywords

Cytoskeleton; Dephosphorylation; Microtubule; Microtubule associated protein 2 (MAP2); Neuronal development; Phosphorylation; Protein kinases; Protein phosphatases; Synaptic plasticity; Synaptic transmission

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; CYTOSKELETON PROTEIN; ISOPROTEIN; MICROTUBULE ASSOCIATED PROTEIN 2; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN) II;

EID: 0342546002     PISSN: 03010082     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-0082(99)00046-5     Document Type: Review
Times cited : (443)

References (473)
  • 1
    • 0028004383 scopus 로고
    • Stimulation of tubulin polymerization by MAP-2. Control by protein kinase C-mediated phosphorylation at specific sites in the microtubule-binding region
    • Ainsztein A.M., Purich D.L. Stimulation of tubulin polymerization by MAP-2. Control by protein kinase C-mediated phosphorylation at specific sites in the microtubule-binding region. J. Biol. Chem. 269:1994;28465-28471.
    • (1994) J. Biol. Chem , vol.269 , pp. 28465-28471
    • Ainsztein, A.M.1    Purich, D.L.2
  • 4
    • 0028997083 scopus 로고
    • Human microtubule-associated protein-2c localizes to dendrites and axons in fetal spinal motor neurons
    • Albala J.S., Kress Y., Liu W.K., Weidenheim K., Yen S.H., Shafit Z.B. Human microtubule-associated protein-2c localizes to dendrites and axons in fetal spinal motor neurons. J. Neurochem. 64:1995;2480-2490.
    • (1995) J. Neurochem , vol.64 , pp. 2480-2490
    • Albala, J.S.1    Kress, Y.2    Liu, W.K.3    Weidenheim, K.4    Yen, S.H.5    Shafit, Z.B.6
  • 5
    • 0029991680 scopus 로고    scopus 로고
    • Mutual protection of microtubule-associated protein 2 (MAP2) and cyclic AMP-dependent protein kinase II against mu-calpain
    • Alexa A., Tompa P., Baki A., Vereb G., Friedrich P. Mutual protection of microtubule-associated protein 2 (MAP2) and cyclic AMP-dependent protein kinase II against mu-calpain. J. Neurosci. Res. 44:1996;438-445.
    • (1996) J. Neurosci. Res , vol.44 , pp. 438-445
    • Alexa, A.1    Tompa, P.2    Baki, A.3    Vereb, G.4    Friedrich, P.5
  • 6
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison D.W., Gelfand V.I., Spector I., Craig A.M. Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J. Neurosci. 18:1998;2423-2436.
    • (1998) J. Neurosci , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 7
    • 0031012497 scopus 로고    scopus 로고
    • Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: Sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau
    • Alonso A.D., Grundke-Iqbal I., Barra H.S., Iqbal K. Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. Proc. Natl. Acad. Sci. U.S.A. 94:1997;298-303.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 298-303
    • Alonso, A.D.1    Grundke-Iqbal, I.2    Barra, H.S.3    Iqbal, K.4
  • 8
    • 0032079141 scopus 로고    scopus 로고
    • Long-term potentiation and spatial training are both associated with the generation of new excitatory synapses
    • Andersen P., Soleng A.F. Long-term potentiation and spatial training are both associated with the generation of new excitatory synapses. Brain Res. Rev. 26:1998;353-359.
    • (1998) Brain Res. Rev , vol.26 , pp. 353-359
    • Andersen, P.1    Soleng, A.F.2
  • 9
    • 0029895904 scopus 로고    scopus 로고
    • Increased density of microtubule associated protein 2-immunoreactive neurons in the prefrontal white matter of schizophrenic subjects
    • Anderson S.A., Volk D.W., Lewis D.A. Increased density of microtubule associated protein 2-immunoreactive neurons in the prefrontal white matter of schizophrenic subjects. Schizophrenia Res. 19:1996;111-119.
    • (1996) Schizophrenia Res , vol.19 , pp. 111-119
    • Anderson, S.A.1    Volk, D.W.2    Lewis, D.A.3
  • 11
    • 0029963611 scopus 로고    scopus 로고
    • Pieces of the Schizophrenia puzzle fall into place
    • Andreasen N. Pieces of the Schizophrenia puzzle fall into place. Neuron. 16:1996;697-700.
    • (1996) Neuron , vol.16 , pp. 697-700
    • Andreasen, N.1
  • 12
    • 0021891112 scopus 로고
    • Ontogenetic changes in the cyclic adenosine 3′,5′-monophosphate-stimulatable phosphorylation of cat visual cortex proteins, particularly of microtubule-associated protein 2 (MAP 2): Effects of normal and dark rearing and of the exposure to light
    • Aoki C., Siekevitz P. Ontogenetic changes in the cyclic adenosine 3′,5′-monophosphate-stimulatable phosphorylation of cat visual cortex proteins, particularly of microtubule-associated protein 2 (MAP 2): effects of normal and dark rearing and of the exposure to light. J. Neurosci. 5:1985;2465-2483.
    • (1985) J. Neurosci , vol.5 , pp. 2465-2483
    • Aoki, C.1    Siekevitz, P.2
  • 13
    • 0024228848 scopus 로고
    • Plasticity in brain development
    • Aoki C., Siekevitz P. Plasticity in brain development. Sci. Am. 259:1988;56-64.
    • (1988) Sci. Am , vol.259 , pp. 56-64
    • Aoki, C.1    Siekevitz, P.2
  • 14
    • 0030874793 scopus 로고    scopus 로고
    • Neuronal damage and MAP2 changes induced by the glutamate transport inhibitor dihydrokainate and by kainate in rat hippocampus in vivo
    • Arias C., Arrieta I., Massieu L., Tapia R. Neuronal damage and MAP2 changes induced by the glutamate transport inhibitor dihydrokainate and by kainate in rat hippocampus in vivo. Exp. Brain Res. 116:(1997):1997;467-476.
    • (1997) Exp. Brain Res , vol.116 , Issue.1997 , pp. 467-476
    • Arias, C.1    Arrieta, I.2    Massieu, L.3    Tapia, R.4
  • 15
    • 0032191966 scopus 로고    scopus 로고
    • The protein phosphatase inhibitor okadaic acid induces heat shock protein expression and neurodegeneration in rat hippocampus in vivo
    • Arias C., BecerraGarcia F., Arrieta I., Tapia R. The protein phosphatase inhibitor okadaic acid induces heat shock protein expression and neurodegeneration in rat hippocampus in vivo. Exp. Neurol. 153:1998;242-254.
    • (1998) Exp. Neurol , vol.153 , pp. 242-254
    • Arias, C.1    Becerragarcia, F.2    Arrieta, I.3    Tapia, R.4
  • 16
    • 0027162369 scopus 로고
    • Okadaic acid induces early changes in microtubule-associated protein 2 and tau phosphorylation prior to neurodegeneration in cultured cortical neurons
    • Arias C., Sharma N., Davies P., Shafit-Zagardo B. Okadaic acid induces early changes in microtubule-associated protein 2 and tau phosphorylation prior to neurodegeneration in cultured cortical neurons. J. Neurochem. 61:1993;673-682.
    • (1993) J. Neurochem , vol.61 , pp. 673-682
    • Arias, C.1    Sharma, N.2    Davies, P.3    Shafit-Zagardo, B.4
  • 17
    • 0025885699 scopus 로고
    • Abnormal expression of two microtubule-associated proteins (MAP2 and MAP5) in specific subfields of the hippocampal formation in schizophrenia
    • Arnold S.E., Lee V.M., Gur R.E., Trojanowski J.Q. 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. 88:1991;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
  • 18
    • 0030854130 scopus 로고    scopus 로고
    • Modulation of neurite branching by protein phosphorylation in cultured rat hippocampal neurons
    • Audesirk G., Cabell L., Kern M. Modulation of neurite branching by protein phosphorylation in cultured rat hippocampal neurons. Dev. Brain Res. 102:1997;247-260.
    • (1997) Dev. Brain Res , vol.102 , pp. 247-260
    • Audesirk, G.1    Cabell, L.2    Kern, M.3
  • 21
    • 0028216212 scopus 로고
    • Regulation of microtubule dynamics by microtubule-associated protein expression and phosphorylation during neuronal development
    • Avila J., Dominguez J., Díaz-Nido J. Regulation of microtubule dynamics by microtubule-associated protein expression and phosphorylation during neuronal development. Int. J. Dev. Biol. 38:1994;13-25.
    • (1994) Int. J. Dev. Biol , vol.38 , pp. 13-25
    • Avila, J.1    Dominguez, J.2    Díaz-Nido, J.3
  • 22
    • 0031919552 scopus 로고    scopus 로고
    • Insulin signal transduction through protein kinase cascades
    • Avruch J. Insulin signal transduction through protein kinase cascades. Mol. Cell Biochem. 182:1998;31-48.
    • (1998) Mol. Cell Biochem , vol.182 , pp. 31-48
    • Avruch, J.1
  • 23
    • 0031048886 scopus 로고    scopus 로고
    • Microtubules and axonal growth
    • Baas P.W. Microtubules and axonal growth. Curr. Op. Cell Biol. 9:1997;29-36.
    • (1997) Curr. Op. Cell Biol , vol.9 , pp. 29-36
    • Baas, P.W.1
  • 24
    • 0032930953 scopus 로고    scopus 로고
    • Microtubules and neuronal polarity: Lessons from mitosis
    • Baas P.W. Microtubules and neuronal polarity: lessons from mitosis. Neuron. 22:1999;23-31.
    • (1999) Neuron , vol.22 , pp. 23-31
    • Baas, P.W.1
  • 27
    • 0029990059 scopus 로고    scopus 로고
    • Long-term depression in hippocampus
    • Bear M., Abraham W. Long-term depression in hippocampus. Ann. Rev. Neurosci. 19:1996;437-462.
    • (1996) Ann. Rev. Neurosci , vol.19 , pp. 437-462
    • Bear, M.1    Abraham, W.2
  • 28
    • 0028282932 scopus 로고
    • Phosphorylation of microtubule-associated proteins MAP2a,b and MAP2c at Ser136 by proline-directed kinases in vivo and in vitro
    • Berling B., Wille H., Roll B., Mandelkow E.M., Garner C., Mandelkow E. Phosphorylation of microtubule-associated proteins MAP2a,b and MAP2c at Ser136 by proline-directed kinases in vivo and in vitro. Eur. J. Cell Biol. 64:1994;120-130.
    • (1994) Eur. J. Cell Biol , vol.64 , pp. 120-130
    • Berling, B.1    Wille, H.2    Roll, B.3    Mandelkow, E.M.4    Garner, C.5    Mandelkow, E.6
  • 29
    • 0020035707 scopus 로고
    • Initial phase of dendrite growth: Evidence for the involvement of high molecular weight microtubule-associated proteins (HMWP) before the appearance of tubulin
    • Bernhardt R., Matus A. Initial phase of dendrite growth: evidence for the involvement of high molecular weight microtubule-associated proteins (HMWP) before the appearance of tubulin. J. Cell Biol. 92:1982;589-593.
    • (1982) J. Cell Biol , vol.92 , pp. 589-593
    • Bernhardt, R.1    Matus, A.2
  • 31
    • 0032935412 scopus 로고    scopus 로고
    • The development of cell processes induced by tau protein requires phosphoryaltion of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains
    • Biernat J., Mandelkow E.M. The development of cell processes induced by tau protein requires phosphoryaltion of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains. Mol. Biol. Cell. 10:1999;727-740.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 727-740
    • Biernat, J.1    Mandelkow, E.M.2
  • 32
    • 0025264785 scopus 로고
    • Effect of excitatory amino acids on microtubule-associated proteins in cultured cortical and spinal neurones
    • Bigot D., Hunt S.P. Effect of excitatory amino acids on microtubule-associated proteins in cultured cortical and spinal neurones. Neurosci. Lett. 111:1990;275-280.
    • (1990) Neurosci. Lett , vol.111 , pp. 275-280
    • Bigot, D.1    Hunt, S.P.2
  • 33
    • 0026048124 scopus 로고
    • The effects of quisqualate and nocodazole on the organization of MAP2 and neurofilaments in spinal cord neurons in vitro
    • Bigot D., Hunt S.P. The effects of quisqualate and nocodazole on the organization of MAP2 and neurofilaments in spinal cord neurons in vitro. Neurosci. Lett. 131:1991;21-26.
    • (1991) Neurosci. Lett , vol.131 , pp. 21-26
    • Bigot, D.1    Hunt, S.P.2
  • 34
    • 0025801234 scopus 로고
    • Reorganization of the cytoskeleton in rat neurons following stimulation with excitatory amino acids in vitro
    • Bigot D., Matus A., Hunt S. Reorganization of the cytoskeleton in rat neurons following stimulation with excitatory amino acids in vitro. Eur. J. Neurosci. 3:1991;551-558.
    • (1991) Eur. J. Neurosci , vol.3 , pp. 551-558
    • Bigot, D.1    Matus, A.2    Hunt, S.3
  • 35
    • 0023931244 scopus 로고
    • Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules
    • Billger M., Wallin M., Karlsson J.O. Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules. Cell Calcium. 9:1988;33-44.
    • (1988) Cell Calcium , vol.9 , pp. 33-44
    • Billger, M.1    Wallin, M.2    Karlsson, J.O.3
  • 36
    • 0031007546 scopus 로고    scopus 로고
    • Regulated phosphorylation and dephosphorylation of tau protein: Effects on microtubule interaction, intracellular trafficking and neurodegeneration
    • Billingsley M.L., Kincaid R.L. Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem. J. 323:1997;577-591.
    • (1997) Biochem. J , vol.323 , pp. 577-591
    • Billingsley, M.L.1    Kincaid, R.L.2
  • 38
    • 0031968294 scopus 로고    scopus 로고
    • The role of calcium in activity-dependent neuronal gene regulation
    • Bito H. The role of calcium in activity-dependent neuronal gene regulation. Cell Calcium. 23:1998;143-150.
    • (1998) Cell Calcium , vol.23 , pp. 143-150
    • Bito, H.1
  • 39
    • 0029553116 scopus 로고
    • Acetylcholine: A neurotransmitter for learning and memory?
    • Blokland A. Acetylcholine: a neurotransmitter for learning and memory? Brain Res. Rev. 21:1995;285-300.
    • (1995) Brain Res. Rev , vol.21 , pp. 285-300
    • Blokland, A.1
  • 40
    • 0020608562 scopus 로고
    • Association of microtubule-associated protein 2 (MAP 2) with microtubules and intermediate filaments in cultured brain cells
    • Bloom G.S., Vallee R.B. Association of microtubule-associated protein 2 (MAP 2) with microtubules and intermediate filaments in cultured brain cells. J. Cell Biol. 96:1983;1523-1531.
    • (1983) J. Cell Biol , vol.96 , pp. 1523-1531
    • Bloom, G.S.1    Vallee, R.B.2
  • 41
    • 0344061515 scopus 로고    scopus 로고
    • Tau-mediated process outgrowth is differentially altered by the expression of MAP2b and MAP2c in Sf9 cells
    • Boucher M., Bélanger D., Beaulieu C., Leclerc N. Tau-mediated process outgrowth is differentially altered by the expression of MAP2b and MAP2c in Sf9 cells. Cell Motil. Cytos. 42:1999;257-273.
    • (1999) Cell Motil. Cytos , vol.42 , pp. 257-273
    • Boucher, M.1    Bélanger, D.2    Beaulieu, C.3    Leclerc, N.4
  • 42
    • 0025976722 scopus 로고
    • Purification and properties of extracellular signal-regulated kinase 1, an insulin-stimulated microtubule-associated protein 2 kinase
    • Boulton T.G., Gregory J.S., Cobb M.H. Purification and properties of extracellular signal-regulated kinase 1, an insulin-stimulated microtubule-associated protein 2 kinase. Biochemistry. 30:1991;278-286.
    • (1991) Biochemistry , vol.30 , pp. 278-286
    • Boulton, T.G.1    Gregory, J.S.2    Cobb, M.H.3
  • 46
    • 0031961216 scopus 로고    scopus 로고
    • Cytoskeletal mechanisms of axon outgrowth and pathfinding
    • Brandt R. Cytoskeletal mechanisms of axon outgrowth and pathfinding. Cell Tissue Res. 292:1998;181-189.
    • (1998) Cell Tissue Res , vol.292 , pp. 181-189
    • Brandt, R.1
  • 47
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixin-moesin protein family
    • Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr. Opin. Cell Biol. 11:1999;109-116.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 48
    • 0028143773 scopus 로고
    • Distribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons
    • Brion J.P., Octave J.N., Couck A.M. Distribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons. Neuroscience. 63:1994;895-909.
    • (1994) Neuroscience , vol.63 , pp. 895-909
    • Brion, J.P.1    Octave, J.N.2    Couck, A.M.3
  • 49
    • 0025689362 scopus 로고
    • Distinct spatial localization of specific mRNAs in cultured sympathetic neurons
    • Bruckenstein D.A., Lein P.J., Higgins D., Fremeau R.J. Distinct spatial localization of specific mRNAs in cultured sympathetic neurons. Neuron. 5:1990;809-819.
    • (1990) Neuron , vol.5 , pp. 809-819
    • Bruckenstein, D.A.1    Lein, P.J.2    Higgins, D.3    Fremeau, R.J.4
  • 50
    • 0025913094 scopus 로고
    • Phosphorylation determines the binding of microtubule-associated protein 2 (MAP2) to microtubules in living cells
    • Brugg B., Matus A. Phosphorylation determines the binding of microtubule-associated protein 2 (MAP2) to microtubules in living cells. J. Cell Biol. 114:1991;735-743.
    • (1991) J. Cell Biol , vol.114 , pp. 735-743
    • Brugg, B.1    Matus, A.2
  • 51
    • 0029798061 scopus 로고    scopus 로고
    • Induction of long-term potentiation is associated with major ultrastructural changes of activated synapses
    • Buchs P.A., Muller D. Induction of long-term potentiation is associated with major ultrastructural changes of activated synapses. Proc. Natl. Acad. Sci. U.S.A. 93:1996;8040-8045.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 8040-8045
    • Buchs, P.A.1    Muller, D.2
  • 52
    • 0028272365 scopus 로고
    • Bundling of microtubules in transfected cells does not involve an autonomous dimerization site on the MAP2 molecule
    • Burgin K.E., Ludin B., Ferralli J., Matus A. Bundling of microtubules in transfected cells does not involve an autonomous dimerization site on the MAP2 molecule. Mol. Biol. Cell. 5:1994;511-517.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 511-517
    • Burgin, K.E.1    Ludin, B.2    Ferralli, J.3    Matus, A.4
  • 53
    • 0021314373 scopus 로고
    • Ontogeny of microtubule-associated protein 2 in rat cerebellum: Differential expression of the doublet polypeptides
    • Burgoyne R.D., Cumming R. Ontogeny of microtubule-associated protein 2 in rat cerebellum: differential expression of the doublet polypeptides. Neuroscience. 11:1984;156-167.
    • (1984) Neuroscience , vol.11 , pp. 156-167
    • Burgoyne, R.D.1    Cumming, R.2
  • 54
    • 0021256085 scopus 로고
    • The multiple phosphorylation of the microtubule-associated protein MAP2 controls the MAP2:tubulin interaction
    • Burns R.G., Islam K., Chapman R. The multiple phosphorylation of the microtubule-associated protein MAP2 controls the MAP2:tubulin interaction. Eur. J. Biochem. 141:1984;609-615.
    • (1984) Eur. J. Biochem , vol.141 , pp. 609-615
    • Burns, R.G.1    Islam, K.2    Chapman, R.3
  • 55
    • 0028912414 scopus 로고
    • The phosphatidylinositol-binding site of microtubule-associated protein MAP2
    • Burns R.G., Surridge C.D. The phosphatidylinositol-binding site of microtubule-associated protein MAP2. Biochem. Soc. Trans. 23:1995;41-46.
    • (1995) Biochem. Soc. Trans , vol.23 , pp. 41-46
    • Burns, R.G.1    Surridge, C.D.2
  • 56
    • 0021418148 scopus 로고
    • MAP2 is localized to the dendrites of hippocampal neurons which develop in culture
    • Cácares A., Banker G., Steward O., Binder L., Payne M. MAP2 is localized to the dendrites of hippocampal neurons which develop in culture. Brain Res. 315:1984;314-318.
    • (1984) Brain Res , vol.315 , pp. 314-318
    • Cácares, A.1    Banker, G.2    Steward, O.3    Binder, L.4    Payne, M.5
  • 57
    • 0022641260 scopus 로고
    • Immunocytochemical localization of tubulin and microtubule- associated protein 2 during the development of hippocampal neurons in culture
    • Cácares A., Banker G.A., Binder L. Immunocytochemical localization of tubulin and microtubule- associated protein 2 during the development of hippocampal neurons in culture. J. Neurosci. 6:1986;714-722.
    • (1986) J. Neurosci , vol.6 , pp. 714-722
    • Cácares, A.1    Banker, G.A.2    Binder, L.3
  • 58
    • 0021260405 scopus 로고
    • Differential subcellular localization of tubulin and the microtubule-associated protein MAP2 in brain tissue as revealed by immunocytochemistry with monoclonal hybridoma antibodies
    • Cácares A., Binder L.I., Payne M.R., Bender P., Rebhun L., Steward O. Differential subcellular localization of tubulin and the microtubule-associated protein MAP2 in brain tissue as revealed by immunocytochemistry with monoclonal hybridoma antibodies. J. Neurosci. 4:1984;394-410.
    • (1984) J. Neurosci , vol.4 , pp. 394-410
    • Cácares, A.1    Binder, L.I.2    Payne, M.R.3    Bender, P.4    Rebhun, L.5    Steward, O.6
  • 59
    • 0026713275 scopus 로고
    • Suppression of MAP2 in cultured cerebellar macroneurons inhibits minor neurite formation
    • Cácares A., Mautino J., Kosik K.S. Suppression of MAP2 in cultured cerebellar macroneurons inhibits minor neurite formation. Neuron. 9:1992;607-618.
    • (1992) Neuron , vol.9 , pp. 607-618
    • Cácares, A.1    Mautino, J.2    Kosik, K.S.3
  • 60
    • 0005907946 scopus 로고
    • Immunocytochemical localization of actin and microtubule-associated protein MAP2 in dendritic spines
    • Cácares A., Payne M.R., Binder L.I., Steward O. Immunocytochemical localization of actin and microtubule-associated protein MAP2 in dendritic spines. Proc. Natl. Acad. Sci. U.S.A. 80:1983;1738-1742.
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 1738-1742
    • Cácares, A.1    Payne, M.R.2    Binder, L.I.3    Steward, O.4
  • 61
    • 0031456158 scopus 로고    scopus 로고
    • Wnt signaling: A common theme in animal development
    • Cadigan K.M., Nusse R. Wnt signaling: a common theme in animal development. Genes & Development. 11:1997;3286-3305.
    • (1997) Genes & Development , vol.11 , pp. 3286-3305
    • Cadigan, K.M.1    Nusse, R.2
  • 62
    • 0032588515 scopus 로고    scopus 로고
    • +2-calmodulin and protein kinase Cs: A hypothetical synthesis of their conflicting convergences on shared substrate domains
    • +2-calmodulin and protein kinase Cs: a hypothetical synthesis of their conflicting convergences on shared substrate domains. TINS. 22:1999;12-16.
    • (1999) TINS , vol.22 , pp. 12-16
    • Chakravarthy, B.1    Morley, P.2    Whitfield, J.3
  • 63
    • 0029882050 scopus 로고    scopus 로고
    • Role of the cytoskeleton in growth cone motility and axonal elongation
    • Challacombe J., Snow D., Letourneau P. Role of the cytoskeleton in growth cone motility and axonal elongation. Seminars in Neurosci. 8:1996;67-80.
    • (1996) Seminars in Neurosci , vol.8 , pp. 67-80
    • Challacombe, J.1    Snow, D.2    Letourneau, P.3
  • 64
    • 0027085694 scopus 로고
    • Microtubule stabilization by assembly-promoting microtubule-associated proteins: A repeat performance
    • Chapin S.J., Bulinski J.C. Microtubule stabilization by assembly-promoting microtubule-associated proteins: a repeat performance. Cell. Motil. Cytoskeleton. 23:1992;236-243.
    • (1992) Cell. Motil. Cytoskeleton , vol.23 , pp. 236-243
    • Chapin, S.J.1    Bulinski, J.C.2
  • 65
    • 0026011365 scopus 로고
    • Expression of various microtubule-associated protein 2 forms in the developing mouse brain and in cultured neurons and astrocytes
    • Charriere B.C., Garner C., Tardy M., Nunez J. Expression of various microtubule-associated protein 2 forms in the developing mouse brain and in cultured neurons and astrocytes. J. Neurochem. 56:1991;385-391.
    • (1991) J. Neurochem , vol.56 , pp. 385-391
    • Charriere, B.C.1    Garner, C.2    Tardy, M.3    Nunez, J.4
  • 66
    • 0032559031 scopus 로고    scopus 로고
    • The microtubule-associated protein tau cross-links to two distinct sites on each alpha and beta tubulin monomer via separate domains
    • Chau M.F., Radeke M.J., deInes C., Barasoain I., Kohlstaedt L.A., Feinstein S.C. The microtubule-associated protein tau cross-links to two distinct sites on each alpha and beta tubulin monomer via separate domains. Biochemistry Usa. 37:1998;17692-17703.
    • (1998) Biochemistry Usa , vol.37 , pp. 17692-17703
    • Chau, M.F.1    Radeke, M.J.2    Deines, C.3    Barasoain, I.4    Kohlstaedt, L.A.5    Feinstein, S.C.6
  • 67
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • Chen J., Kanai Y., Cowan N.J., Hirokawa N. Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature. 360:1992;674-677.
    • (1992) Nature , vol.360 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 69
    • 0006227378 scopus 로고    scopus 로고
    • MAP2a, an alternatively spliced variant of microtubule-associated protein 2
    • Chung W.J., Kindler S., Seidenbecher C., Garner C.C. MAP2a, an alternatively spliced variant of microtubule-associated protein 2. J. Neurochem. 66:1996;1273-1281.
    • (1996) J. Neurochem , vol.66 , pp. 1273-1281
    • Chung, W.J.1    Kindler, S.2    Seidenbecher, C.3    Garner, C.C.4
  • 70
    • 0025219162 scopus 로고
    • Microtubule MAPping
    • Cleveland D. Microtubule MAPping. Cell. 60:1990;701-702.
    • (1990) Cell , vol.60 , pp. 701-702
    • Cleveland, D.1
  • 72
    • 0028943777 scopus 로고
    • Association of protein kinase A and protein phosphatase 2B with a common anchoring protein
    • Coghlan V., Perrino B., Howard M., Langeberg L., Hicks J., Gallatin W., Scott J. Association of protein kinase A and protein phosphatase 2B with a common anchoring protein. Science. 267:1995;108-111.
    • (1995) Science , vol.267 , pp. 108-111
    • Coghlan, V.1    Perrino, B.2    Howard, M.3    Langeberg, L.4    Hicks, J.5    Gallatin, W.6    Scott, J.7
  • 73
    • 0026625670 scopus 로고
    • Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain
    • Correas I., Díaz-Nido J., Avila J. Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain. J. Biol. Chem. 267:1992;15721-15728.
    • (1992) J. Biol. Chem , vol.267 , pp. 15721-15728
    • Correas, I.1    Díaz-Nido, J.2    Avila, J.3
  • 74
    • 0025335664 scopus 로고
    • The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding
    • Correas I., Padilla R., Avila J. The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding. Biochem. J. 269:1990;61-64.
    • (1990) Biochem. J , vol.269 , pp. 61-64
    • Correas, I.1    Padilla, R.2    Avila, J.3
  • 75
    • 0030982394 scopus 로고    scopus 로고
    • Alterations in hippocampal non-phosphorylated MAP2 protein expression in schizophrenia
    • Cotter D., Kerwin R., Doshi B., Sánchez C., Everall E. Alterations in hippocampal non-phosphorylated MAP2 protein expression in schizophrenia. Brain Res. 765:1997;238-246.
    • (1997) Brain Res , vol.765 , pp. 238-246
    • Cotter, D.1    Kerwin, R.2    Doshi, B.3    Sánchez, C.4    Everall, E.5
  • 76
    • 0029977256 scopus 로고    scopus 로고
    • New forms of HMW MAP2 are preferentially expressed in the spinal cord
    • Couchie D., Chabas S., Mavilia C., Nunez J. New forms of HMW MAP2 are preferentially expressed in the spinal cord. FEBS Lett. 388:1996;76-79.
    • (1996) FEBS Lett , vol.388 , pp. 76-79
    • Couchie, D.1    Chabas, S.2    Mavilia, C.3    Nunez, J.4
  • 77
    • 0022185841 scopus 로고
    • Immunological characterization of microtubule-associated proteins specific for the immature brain
    • Couchie D., Nunez J. Immunological characterization of microtubule-associated proteins specific for the immature brain. FEBS Lett. 188:1985;331-335.
    • (1985) FEBS Lett , vol.188 , pp. 331-335
    • Couchie, D.1    Nunez, J.2
  • 79
    • 0030473999 scopus 로고    scopus 로고
    • Molecular characterization of the dendritic growth cone: Regulated mRNA transport and local protein synthesis
    • Crino P.B., Eberwine J. Molecular characterization of the dendritic growth cone: regulated mRNA transport and local protein synthesis. Neuron. 17:1996;1173-1187.
    • (1996) Neuron , vol.17 , pp. 1173-1187
    • Crino, P.B.1    Eberwine, J.2
  • 80
    • 0025793801 scopus 로고
    • MAP-1 and MAP-2 binding sites at the C-terminus of beta-tubulin. Studies with synthetic tubulin peptides
    • Cross D., Dominguez J., Maccioni R.B., Avila J. MAP-1 and MAP-2 binding sites at the C-terminus of beta-tubulin. Studies with synthetic tubulin peptides. Biochemistry. 30:1991;4362-4366.
    • (1991) Biochemistry , vol.30 , pp. 4362-4366
    • Cross, D.1    Dominguez, J.2    Maccioni, R.B.3    Avila, J.4
  • 81
    • 0031025417 scopus 로고    scopus 로고
    • Microtubule-associated protein 2c reorganizes both microtubules and microfilaments into distinct cytological structures in an actin-binding protein-280-deficient melanoma cell line
    • Cunningham C.C., Leclerc N., Flanagan L.A., Lu M., Janmey P.A., Kosik K.S. Microtubule-associated protein 2c reorganizes both microtubules and microfilaments into distinct cytological structures in an actin-binding protein-280-deficient melanoma cell line. J. Cell Biol. 136:1997;845-857.
    • (1997) J. Cell Biol , vol.136 , pp. 845-857
    • Cunningham, C.C.1    Leclerc, N.2    Flanagan, L.A.3    Lu, M.4    Janmey, P.A.5    Kosik, K.S.6
  • 82
    • 0029998871 scopus 로고    scopus 로고
    • The dynamics of dendritic structure in developing hippocampal slices
    • Dailey M., Smith S. The dynamics of dendritic structure in developing hippocampal slices. J. Neurosci. 16:1996;2983-2994.
    • (1996) J. Neurosci , vol.16 , pp. 2983-2994
    • Dailey, M.1    Smith, S.2
  • 84
    • 0028082161 scopus 로고
    • Protein kinase C: A question of specifity
    • Dekker L., Parker P. Protein kinase C: a question of specifity. TIBS. 19:1994;73-77.
    • (1994) TIBS , vol.19 , pp. 73-77
    • Dekker, L.1    Parker, P.2
  • 85
    • 0030914913 scopus 로고    scopus 로고
    • Protein kinase A anchoring
    • Dell'Acqua M., Scott J. Protein kinase A anchoring. J. Biol. Chem. 272:1997;12881-12884.
    • (1997) J. Biol. Chem , vol.272 , pp. 12881-12884
    • Dell'Acqua, M.1    Scott, J.2
  • 87
    • 0028924141 scopus 로고
    • Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins
    • Dhamodharan, R., Wadsworth, P., 1995. Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins. J. Cell Sci. 108, 1679-1689.
    • (1995) J. Cell Sci. , vol.108 , pp. 1679-1689
    • Dhamodharan, R.1    Wadsworth, P.2
  • 88
    • 84993904452 scopus 로고
    • Microtubule proteins in neuronal cells
    • J. Avila. Boca Ratón, FL, USA: CRC Press
    • Díaz-Nido J., Hernández M., Avila J. Microtubule proteins in neuronal cells. Avila J. Microtubule Proteins. 1990;193-259 CRC Press, Boca Ratón, FL, USA.
    • (1990) Microtubule Proteins , pp. 193-259
    • Díaz-Nido, J.1    Hernández, M.2    Avila, J.3
  • 89
    • 0027265929 scopus 로고
    • High external potassium induces an increase in the phosphorylation of the cytoskeletal protein MAP2 in rat hippocampal slices
    • Díaz-Nido J., Montoro R.J., Lopez B.J., Avila J. High external potassium induces an increase in the phosphorylation of the cytoskeletal protein MAP2 in rat hippocampal slices. Eur. J. Neurosci. 5:1993;818-824.
    • (1993) Eur. J. Neurosci , vol.5 , pp. 818-824
    • Díaz-Nido, J.1    Montoro, R.J.2    Lopez, B.J.3    Avila, J.4
  • 90
    • 0025019690 scopus 로고
    • Phosphorylation of microtubule proteins in rat brain at different developmental stages: Comparison with that found in neuronal cultures
    • Díaz-Nido J., Serrano L., Hernandez M.A., Avila J. Phosphorylation of microtubule proteins in rat brain at different developmental stages: comparison with that found in neuronal cultures. J. Neurochem. 54:1990;211-222.
    • (1990) J. Neurochem , vol.54 , pp. 211-222
    • Díaz-Nido, J.1    Serrano, L.2    Hernandez, M.A.3    Avila, J.4
  • 91
    • 0027408594 scopus 로고
    • MAP2 phosphorylation parallels dendrite arborization in hippocampal neurones in culture
    • Díez-Guerra F., Avila J. MAP2 phosphorylation parallels dendrite arborization in hippocampal neurones in culture. Neuroreport. 4:1993;419-422.
    • (1993) Neuroreport , vol.4 , pp. 419-422
    • Díez-Guerra, F.1    Avila, J.2
  • 92
    • 0027296751 scopus 로고
    • Rapid dephosphorylation of microtubule-associated protein 2 in the rat brain hippocampus after pentylenetetrazole-induced seizures
    • Díez-Guerra F., Avila J. Rapid dephosphorylation of microtubule-associated protein 2 in the rat brain hippocampus after pentylenetetrazole-induced seizures. Eur. J. Biochem. 215:1993;181-187.
    • (1993) Eur. J. Biochem , vol.215 , pp. 181-187
    • Díez-Guerra, F.1    Avila, J.2
  • 93
    • 0028855827 scopus 로고
    • An increase in phosphorylation of microtubule-associated protein 2 accompanies dendrite extension during the differentiation of cultured hippocampal neurons
    • Díez-Guerra J., Avila J. An increase in phosphorylation of microtubule-associated protein 2 accompanies dendrite extension during the differentiation of cultured hippocampal neurons. Eur. J. Biochem. 227:1995;68-77.
    • (1995) Eur. J. Biochem , vol.227 , pp. 68-77
    • Díez-Guerra, J.1    Avila, J.2
  • 94
    • 0029952572 scopus 로고    scopus 로고
    • High molecular weight microtubule-associated proteins contain O-linked N-acetylglucosamine
    • Ding M., Vandre D.D. High molecular weight microtubule-associated proteins contain O-linked N-acetylglucosamine. J. Biol. Chem. 271:1996;12555-12561.
    • (1996) J. Biol. Chem , vol.271 , pp. 12555-12561
    • Ding, M.1    Vandre, D.D.2
  • 95
    • 0025968644 scopus 로고
    • Inhibition of MAP2 expression affects both morphological and cell division phenotypes of neuronal differentiation
    • Dinsmore J.H., Solomon F. Inhibition of MAP2 expression affects both morphological and cell division phenotypes of neuronal differentiation. Cell. 64:1991;817-826.
    • (1991) Cell , vol.64 , pp. 817-826
    • Dinsmore, J.H.1    Solomon, F.2
  • 96
    • 0027665581 scopus 로고
    • Probing modifications of the neuronal cytoskeleton
    • Doering L.C. Probing modifications of the neuronal cytoskeleton. Mol. Neurobiol. 7:1993;265-291.
    • (1993) Mol. Neurobiol , vol.7 , pp. 265-291
    • Doering, L.C.1
  • 97
    • 0027519666 scopus 로고
    • An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif
    • Doll T., Meichsner M., Riederer B.M., Honegger P., Matus A. An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif. J. Cell Sci. 106:1993;633-639.
    • (1993) J. Cell Sci , vol.106 , pp. 633-639
    • Doll, T.1    Meichsner, M.2    Riederer, B.M.3    Honegger, P.4    Matus, A.5
  • 98
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel D., Hyman A., Cobb M., Kirschnen M. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell. 3:1992;1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.1    Hyman, A.2    Cobb, M.3    Kirschnen, M.4
  • 100
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G., Ebneth A., Preuss U., Mandelkow E.M., Mandelkow E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell. 89:1997;297-308.
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 101
    • 0028886016 scopus 로고
    • Postnatal changes in serine/threonine protein phosphatases and their association with microtubules
    • Dudek S., Johnson G. Postnatal changes in serine/threonine protein phosphatases and their association with microtubules. Dev. Brain Res. 90:1995;54-61.
    • (1995) Dev. Brain Res , vol.90 , pp. 54-61
    • Dudek, S.1    Johnson, G.2
  • 102
  • 103
    • 0027521086 scopus 로고
    • Actin depolymerisation induces process formation on MAP2-transfected non-neuronal cells
    • Edson K., Weisshaar B., Matus A. Actin depolymerisation induces process formation on MAP2-transfected non-neuronal cells. Development. 117:1993;689-700.
    • (1993) Development , vol.117 , pp. 689-700
    • Edson, K.1    Weisshaar, B.2    Matus, A.3
  • 105
    • 0026556757 scopus 로고
    • Cdc2 kinase-induced destabilization of MAP2-coated microtubules in Xenopus egg extracts
    • Faruki S., Doree M., Karsenti E. cdc2 kinase-induced destabilization of MAP2-coated microtubules in Xenopus egg extracts. J. Cell Sci. 101:1992;69-78.
    • (1992) J. Cell Sci , vol.101 , pp. 69-78
    • Faruki, S.1    Doree, M.2    Karsenti, E.3
  • 106
    • 0029980440 scopus 로고    scopus 로고
    • Molecular glue: Kinase anchoring and scaffold proteins
    • Faux M., Scott J. Molecular glue: kinase anchoring and scaffold proteins. Cell. 85:1996;9-12.
    • (1996) Cell , vol.85 , pp. 9-12
    • Faux, M.1    Scott, J.2
  • 108
    • 0027232160 scopus 로고
    • Ammonium injection induces an N-methyl-D-aspartate receptor-mediated proteolysis of the microtubule-associated protein MAP-2
    • Felipo V., Grau E., Minana M.D., Grisolia S. Ammonium injection induces an N-methyl-D-aspartate receptor-mediated proteolysis of the microtubule-associated protein MAP-2. J. Neurochem. 60:1993;1626-1630.
    • (1993) J. Neurochem , vol.60 , pp. 1626-1630
    • Felipo, V.1    Grau, E.2    Minana, M.D.3    Grisolia, S.4
  • 109
    • 0027276211 scopus 로고
    • Hyperammonemia decreases protein-kinase-C-dependent phosphorylation of microtubule-associated protein 2 and increases its binding to tubulin
    • Felipo V., Grau E., Minana M.D., Grisolia S. Hyperammonemia decreases protein-kinase-C-dependent phosphorylation of microtubule-associated protein 2 and increases its binding to tubulin. Eur. J. Biochem. 214:1993;243-249.
    • (1993) Eur. J. Biochem , vol.214 , pp. 243-249
    • Felipo, V.1    Grau, E.2    Minana, M.D.3    Grisolia, S.4
  • 110
    • 0028670597 scopus 로고
    • Association of p34cdc2 kinase and MAP kinase with microtubules during the meiotic maturation of Xenopus oocytes
    • Fellous A., Kubelka M., Thibier C., Taieb F., Haccard O., Jessus C. Association of p34cdc2 kinase and MAP kinase with microtubules during the meiotic maturation of Xenopus oocytes. Int. J. Dev. Biol. 38:1994;651-659.
    • (1994) Int. J. Dev. Biol , vol.38 , pp. 651-659
    • Fellous, A.1    Kubelka, M.2    Thibier, C.3    Taieb, F.4    Haccard, O.5    Jessus, C.6
  • 111
    • 0027936387 scopus 로고
    • Structure, regional and developmental expression of rat MAP2d, a MAP2 splice variant encoding four microtubule-binding domains
    • Ferhat L., Bernard A., Ribas d.P.L., Ben A.Y., Khrestchatisky M. Structure, regional and developmental expression of rat MAP2d, a MAP2 splice variant encoding four microtubule-binding domains. Neurochem. Int. 25:1994;327-338.
    • (1994) Neurochem. Int , vol.25 , pp. 327-338
    • Ferhat, L.1    Bernard, A.2    Ribas, D.P.L.3    Ben, A.Y.4    Khrestchatisky, M.5
  • 112
    • 0031870960 scopus 로고    scopus 로고
    • Expression of the mitotic motor protein CHO1/MKLPI in postmitotic neurons
    • Ferhat L., Kuriyama R., Lyons G.E., Micales B., Baas P.W. Expression of the mitotic motor protein CHO1/MKLPI in postmitotic neurons. Eur. J. Neurosci. 10:1998;1383-1393.
    • (1998) Eur. J. Neurosci , vol.10 , pp. 1383-1393
    • Ferhat, L.1    Kuriyama, R.2    Lyons, G.E.3    Micales, B.4    Baas, P.W.5
  • 113
    • 0029948585 scopus 로고    scopus 로고
    • MAP2d promotes bundling and stabilization of both microtubules and microfilaments
    • Ferhat L., Represa A., Bernard A., Benari Y., Khrestchatisky M. MAP2d promotes bundling and stabilization of both microtubules and microfilaments. J. Cell Sci. 109:1996;1095-1103.
    • (1996) J. Cell Sci , vol.109 , pp. 1095-1103
    • Ferhat, L.1    Represa, A.2    Bernard, A.3    Benari, Y.4    Khrestchatisky, M.5
  • 114
    • 0031814040 scopus 로고    scopus 로고
    • MAP2d mRNA is expressed in identified neuronal populations in the developing and adult rat brain and its subcellular distribution differs from that of MAP2b in hippocampal neurones
    • Ferhat L., Represa A., Ferhat W., Ben-Ari Y., Khrestchatisky M. MAP2d mRNA is expressed in identified neuronal populations in the developing and adult rat brain and its subcellular distribution differs from that of MAP2b in hippocampal neurones. Eur. J. Neurosci. 10:1998;161-171.
    • (1998) Eur. J. Neurosci , vol.10 , pp. 161-171
    • Ferhat, L.1    Represa, A.2    Ferhat, W.3    Ben-Ari, Y.4    Khrestchatisky, M.5
  • 115
    • 0028134711 scopus 로고
    • Sequence analysis of MAP2 function in living cells
    • Ferralli J., Doll T., Matus A. Sequence analysis of MAP2 function in living cells. J. Cell Sci. 107:1994;3115-3125.
    • (1994) J. Cell Sci , vol.107 , pp. 3115-3125
    • Ferralli, J.1    Doll, T.2    Matus, A.3
  • 116
    • 0024433060 scopus 로고
    • Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: Evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau
    • Ferreira A., Busciglio J., Cácares A. Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau. Brain Res. Dev. Brain Res. 49:1989;215-228.
    • (1989) Brain Res. Dev. Brain Res , vol.49 , pp. 215-228
    • Ferreira, A.1    Busciglio, J.2    Cácares, A.3
  • 117
    • 0027751889 scopus 로고
    • Calcineurin is associated with the cytoskeleton of cultured neurons and has a role in the acquisition of polarity
    • Ferreira A., Kincaid R., Kosik K.S. Calcineurin is associated with the cytoskeleton of cultured neurons and has a role in the acquisition of polarity. Mol. Biol. Cell. 4:1993;1225-1238.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1225-1238
    • Ferreira, A.1    Kincaid, R.2    Kosik, K.S.3
  • 118
    • 0032211079 scopus 로고    scopus 로고
    • Synaptogenesis via dendritic filopodia in developing hippocampal area CA1
    • Fiala J.C., Feinberg M., Popov V., Harris K.M. Synaptogenesis via dendritic filopodia in developing hippocampal area CA1. J. Neurosci. 18:1998;8900-8911.
    • (1998) J. Neurosci , vol.18 , pp. 8900-8911
    • Fiala, J.C.1    Feinberg, M.2    Popov, V.3    Harris, K.M.4
  • 119
    • 0027052542 scopus 로고
    • Actin matrix of dendritic spines, synaptic plasticity, and long-term potentiation
    • Fifkova E., Morales M. Actin matrix of dendritic spines, synaptic plasticity, and long-term potentiation. Int. Rev. Cytol. 139:1992;267-307.
    • (1992) Int. Rev. Cytol , vol.139 , pp. 267-307
    • Fifkova, E.1    Morales, M.2
  • 120
    • 0027184141 scopus 로고
    • P42 mitogen-activated protein kinase in brain: Prominent localization in neuronal cell bodies and dendrites
    • Fiore R.S., Bayer V.E., Pelech S.L., Posada J., Cooper J.A., Baraban J.M. p42 mitogen-activated protein kinase in brain: prominent localization in neuronal cell bodies and dendrites. Neuroscience. 55:1993;463-472.
    • (1993) Neuroscience , vol.55 , pp. 463-472
    • Fiore, R.S.1    Bayer, V.E.2    Pelech, S.L.3    Posada, J.4    Cooper, J.A.5    Baraban, J.M.6
  • 121
    • 0025941559 scopus 로고
    • Calpain-mediated proteolysis of microtubule associated proteins MAP1B and MAP2 in developing brain
    • Fischer I., Romano C.G., Grynspan F. Calpain-mediated proteolysis of microtubule associated proteins MAP1B and MAP2 in developing brain. Neurochem. Res. 16:1991;891-898.
    • (1991) Neurochem. Res , vol.16 , pp. 891-898
    • Fischer, I.1    Romano, C.G.2    Grynspan, F.3
  • 122
    • 0027984312 scopus 로고
    • Synaptogenesis in hippocampal cultures: Evidence indicating that axons and dendrites become competent to form synapses at different stages of neuronal development
    • Fletcher T.L., De Camilli P., Banker G. Synaptogenesis in hippocampal cultures: evidence indicating that axons and dendrites become competent to form synapses at different stages of neuronal development. J. Neurosci. 14:1994;6695-6706.
    • (1994) J. Neurosci , vol.14 , pp. 6695-6706
    • Fletcher, T.L.1    De Camilli, P.2    Banker, G.3
  • 123
    • 0031978355 scopus 로고    scopus 로고
    • Disruption of MAP-2 immunostaining in rat hippocampus after traumatic brain injury
    • Folkerts M.M., Berman R.F., Muizelaar J.P., Rafols J.A. Disruption of MAP-2 immunostaining in rat hippocampus after traumatic brain injury. J. Neurotrauma. 15:1998;349-363.
    • (1998) J. Neurotrauma , vol.15 , pp. 349-363
    • Folkerts, M.M.1    Berman, R.F.2    Muizelaar, J.P.3    Rafols, J.A.4
  • 124
    • 0032079680 scopus 로고    scopus 로고
    • Synaptic tagging: Implications for late maintenance of hippocampal long-term potentiation
    • Frey U., Morris R.G.M. Synaptic tagging: implications for late maintenance of hippocampal long-term potentiation. Trends Neurosci. 21:1998;181-188.
    • (1998) Trends Neurosci , vol.21 , pp. 181-188
    • Frey, U.1    Morris, R.G.M.2
  • 125
    • 0026354927 scopus 로고
    • MAP2: A sensitive cross-linker and adjustable spacer in dendritic architecture
    • Friedrich P., Aszodi A. MAP2: a sensitive cross-linker and adjustable spacer in dendritic architecture. FEBS Lett. 295:1991;5-9.
    • (1991) FEBS Lett , vol.295 , pp. 5-9
    • Friedrich, P.1    Aszodi, A.2
  • 126
    • 0031855511 scopus 로고    scopus 로고
    • Role of MAP kinase in neurons
    • Fukunaga K., Miyamoto E. Role of MAP kinase in neurons. Mol. Neurobiol. 16:1998;79-95.
    • (1998) Mol. Neurobiol , vol.16 , pp. 79-95
    • Fukunaga, K.1    Miyamoto, E.2
  • 127
    • 0028988308 scopus 로고
    • 2+/calmodulin-dependent protein kinase II and its endogenous substrates in the induction of long-term potentiation
    • 2+/calmodulin-dependent protein kinase II and its endogenous substrates in the induction of long-term potentiation. J. Biol. Chem. 270:1995;6119-6124.
    • (1995) J. Biol. Chem , vol.270 , pp. 6119-6124
    • Fukunaga, K.1    Muller, D.2    Miyamoto, E.3
  • 128
  • 129
    • 0026613087 scopus 로고
    • +2/calmodulin-dependent protein kinase II and protein kinase C by glutamate in cultured hippocampal neurons
    • +2/calmodulin-dependent protein kinase II and protein kinase C by glutamate in cultured hippocampal neurons. J. Biol. Chem. 267:1992;22527-22533.
    • (1992) J. Biol. Chem , vol.267 , pp. 22527-22533
    • Fukunaga, K.1    Soderling, T.2    Miyamoto, E.3
  • 130
    • 0023859086 scopus 로고
    • Different forms of microtubule-associated protein 2 are encoded by separate mRNA transcripts
    • Garner C.C., Matus A. Different forms of microtubule-associated protein 2 are encoded by separate mRNA transcripts. J. Cell Biol. 106:1988;779-783.
    • (1988) J. Cell Biol , vol.106 , pp. 779-783
    • Garner, C.C.1    Matus, A.2
  • 132
    • 0025870729 scopus 로고
    • Neuronal polarity: Targeting of microtubule components into axons and dendrites
    • Ginzburg I. Neuronal polarity: targeting of microtubule components into axons and dendrites. Trends Biochem. Sci. 16:1991;257-261.
    • (1991) Trends Biochem. Sci , vol.16 , pp. 257-261
    • Ginzburg, I.1
  • 133
    • 0025772021 scopus 로고
    • Molecular characterization of microtubule-associated proteins tau and MAP2
    • Goedert M., Crowther R.A., Garner C.C. Molecular characterization of microtubule-associated proteins tau and MAP2. Trends Neurosci. 14:1991;193-199.
    • (1991) Trends Neurosci , vol.14 , pp. 193-199
    • Goedert, M.1    Crowther, R.A.2    Garner, C.C.3
  • 134
    • 0032946279 scopus 로고    scopus 로고
    • Protein phosphatase 2A: Who shall regulate the regulator?
    • Goldberg Y. Protein phosphatase 2A: who shall regulate the regulator? Biochem. Pharmacol. 57:1999;321-328.
    • (1999) Biochem. Pharmacol , vol.57 , pp. 321-328
    • Goldberg, Y.1
  • 135
    • 0022557180 scopus 로고
    • Phosphorylation of MAP-2 at distinct sites by calmodulin- And cyclic AMP-dependent kinases
    • Goldenring J.R., DeLorenzo R.J. Phosphorylation of MAP-2 at distinct sites by calmodulin- and cyclic AMP-dependent kinases. Ann. N.Y. Acad. Sci. 466:1986;457-459.
    • (1986) Ann. N.Y. Acad. Sci , vol.466 , pp. 457-459
    • Goldenring, J.R.1    Delorenzo, R.J.2
  • 136
    • 0021796819 scopus 로고
    • Phosphorylation of microtubule-associated protein 2 at distinct sites by calmodulin-dependent and cyclic-AMP-dependent kinases
    • Goldenring J.R., Vallano M.L., DeLorenzo R.J. Phosphorylation of microtubule-associated protein 2 at distinct sites by calmodulin-dependent and cyclic-AMP-dependent kinases. J. Neurochem. 45:1985;900-905.
    • (1985) J. Neurochem , vol.45 , pp. 900-905
    • Goldenring, J.R.1    Vallano, M.L.2    Delorenzo, R.J.3
  • 137
    • 0031035402 scopus 로고    scopus 로고
    • Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly
    • Goode B., Denis P., Panda D., Radeke M., Miller H., Wilson L., Feinstein S. Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly. Mol. Biol. of the Cell. 8:1997;353-365.
    • (1997) Mol. Biol. of the Cell , vol.8 , pp. 353-365
    • Goode, B.1    Denis, P.2    Panda, D.3    Radeke, M.4    Miller, H.5    Wilson, L.6    Feinstein, S.7
  • 138
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat domain of tau
    • Goode B., Feinstein S. Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat domain of tau. J. Cell Biol. 124:1994;769-782.
    • (1994) J. Cell Biol , vol.124 , pp. 769-782
    • Goode, B.1    Feinstein, S.2
  • 139
    • 0021842984 scopus 로고
    • Dephosphorylation of microtubule-associated protein 2, tau factor, and tubulin by calcineurin
    • Goto S., Yamamoto H., Fukunaga K., Iwasa T., Matsukado Y., Miyamoto E. Dephosphorylation of microtubule-associated protein 2, tau factor, and tubulin by calcineurin. J. Neurochem. 45:1985;276-283.
    • (1985) J. Neurochem , vol.45 , pp. 276-283
    • Goto, S.1    Yamamoto, H.2    Fukunaga, K.3    Iwasa, T.4    Matsukado, Y.5    Miyamoto, E.6
  • 140
    • 0025119512 scopus 로고
    • Okadaic acid activates microtubule-associated protein kinase in quiescent fibroblastic cells
    • Gotoh Y., Nishida E., Sakai H. Okadaic acid activates microtubule-associated protein kinase in quiescent fibroblastic cells. Eur. J. Biochem. 193:1990;671-674.
    • (1990) Eur. J. Biochem , vol.193 , pp. 671-674
    • Gotoh, Y.1    Nishida, E.2    Sakai, H.3
  • 141
    • 0025028911 scopus 로고
    • Microtubule-associated-protein (MAP) kinase activated by nerve growth factor and epidermal growth factor in PC12 cells. Identity with the mitogen-activated MAP kinase of fibroblastic cells
    • Gotoh Y., Nishida E., Yamashita T., Hoshi M., Kawakami M., Sakai H. Microtubule-associated-protein (MAP) kinase activated by nerve growth factor and epidermal growth factor in PC12 cells. Identity with the mitogen-activated MAP kinase of fibroblastic cells. Eur. J. Biochem. 193:1990;661-669.
    • (1990) Eur. J. Biochem , vol.193 , pp. 661-669
    • Gotoh, Y.1    Nishida, E.2    Yamashita, T.3    Hoshi, M.4    Kawakami, M.5    Sakai, H.6
  • 142
    • 0026740766 scopus 로고
    • The susceptibility of MAP-2 to proteolytic degradation increases when bound to tubulin
    • Grau E., Felipo V., Minana M.D., Grisolia S. The susceptibility of MAP-2 to proteolytic degradation increases when bound to tubulin. Neurochem. Res. 17:1992;967-971.
    • (1992) Neurochem. Res , vol.17 , pp. 967-971
    • Grau, E.1    Felipo, V.2    Minana, M.D.3    Grisolia, S.4
  • 144
    • 0031577154 scopus 로고    scopus 로고
    • Calcineurin: Not just a simple protein phosphatase
    • Guerini D. Calcineurin: not just a simple protein phosphatase. Biochem. Biophys. Res. Commu. 235:1997;271-275.
    • (1997) Biochem. Biophys. Res. Commu , vol.235 , pp. 271-275
    • Guerini, D.1
  • 147
    • 0027957063 scopus 로고
    • Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules
    • Hagiwara H., Yorifuji H., Sato Y.R., Hirokawa N. Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules. J. Biol. Chem. 269:1994;3581-3589.
    • (1994) J. Biol. Chem , vol.269 , pp. 3581-3589
    • Hagiwara, H.1    Yorifuji, H.2    Sato, Y.R.3    Hirokawa, N.4
  • 148
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science. 279:1998;509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 149
    • 0025039456 scopus 로고
    • Activation of NMDA receptors induces rapid dephosphorylation of the cytoskeletal protein MAP2
    • Halpain S., Greengard P. Activation of NMDA receptors induces rapid dephosphorylation of the cytoskeletal protein MAP2. Neuron. 5:1990;237-246.
    • (1990) Neuron , vol.5 , pp. 237-246
    • Halpain, S.1    Greengard, P.2
  • 150
    • 0032403433 scopus 로고    scopus 로고
    • Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin
    • Halpain S., Hipolito A., Saffer L. Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin. J. Neurosci. 18:1998;9835-9844.
    • (1998) J. Neurosci , vol.18 , pp. 9835-9844
    • Halpain, S.1    Hipolito, A.2    Saffer, L.3
  • 151
    • 0343961567 scopus 로고    scopus 로고
    • Production of a mice deficient in microtubule-associated protein 2 (MAP2)
    • Harada A., Oguchi K., Teng J., Hirokawa N. Production of a mice deficient in microtubule-associated protein 2 (MAP2). Mol. Biol. Cell. 9:(156a):1998;902.
    • (1998) Mol. Biol. Cell , vol.9 , Issue.156 A , pp. 902
    • Harada, A.1    Oguchi, K.2    Teng, J.3    Hirokawa, N.4
  • 152
    • 0023767727 scopus 로고
    • The characterization of phospholipids associated with microtubules, purified tubulin and microtubule associated proteins in vitro
    • Hargreaves A.J., McLean W.G. The characterization of phospholipids associated with microtubules, purified tubulin and microtubule associated proteins in vitro. Int. J. Biochem. 20:1988;1133-1138.
    • (1988) Int. J. Biochem , vol.20 , pp. 1133-1138
    • Hargreaves, A.J.1    McLean, W.G.2
  • 153
    • 0030894591 scopus 로고    scopus 로고
    • Cytoskeletal maturation in cultured hippocampal slices
    • Hartel R., Matus A. Cytoskeletal maturation in cultured hippocampal slices. Neuroscience. 78:1997;1-5.
    • (1997) Neuroscience , vol.78 , pp. 1-5
    • Hartel, R.1    Matus, A.2
  • 154
    • 0028921410 scopus 로고
    • Immunohistochemical localization of protein phosphatase isoforms in the rat cerebellum
    • Hashikawa T., Nakazawa K., Mikawa S., Shima H., Nagao M. Immunohistochemical localization of protein phosphatase isoforms in the rat cerebellum. Neurosci. Res. 22:1995;133-136.
    • (1995) Neurosci. Res , vol.22 , pp. 133-136
    • Hashikawa, T.1    Nakazawa, K.2    Mikawa, S.3    Shima, H.4    Nagao, M.5
  • 155
    • 0029825623 scopus 로고    scopus 로고
    • Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex
    • Hayashi K., Ishikawa R., Ye L.H., He X.L., Takata K., Kohama K., Shirao T. Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex. J. Neurosci. 16:1996;7161-7170.
    • (1996) J. Neurosci , vol.16 , pp. 7161-7170
    • Hayashi, K.1    Ishikawa, R.2    Ye, L.H.3    He, X.L.4    Takata, K.5    Kohama, K.6    Shirao, T.7
  • 156
  • 157
    • 0029870656 scopus 로고    scopus 로고
    • Cytoplasmic mechanisms of axonal and dendritic growth in neurons
    • Heidemann S. Cytoplasmic mechanisms of axonal and dendritic growth in neurons. Int. Rev. Cytol. 165:1996;235-296.
    • (1996) Int. Rev. Cytol , vol.165 , pp. 235-296
    • Heidemann, S.1
  • 158
    • 0022406440 scopus 로고
    • Microtubule-associated proteins bind specifically to the 70-kDa neurofilament protein
    • Heimann R., Shelanski M.L., Liem R.K. Microtubule-associated proteins bind specifically to the 70-kDa neurofilament protein. J. Biol. Chem. 260:1985;12160-12166.
    • (1985) J. Biol. Chem , vol.260 , pp. 12160-12166
    • Heimann, R.1    Shelanski, M.L.2    Liem, R.K.3
  • 160
    • 0026452774 scopus 로고
    • Neuronal cdc2-like kinase: A cdc2-related protein kinase with predominantly neuronal expression
    • Hellmich M., Pant H., Wada E., Battey J. Neuronal cdc2-like kinase: A cdc2-related protein kinase with predominantly neuronal expression. Proc. Natl. Acad. Sci. U.S.A. 89:1992;10867-10871.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 10867-10871
    • Hellmich, M.1    Pant, H.2    Wada, E.3    Battey, J.4
  • 161
    • 0022447345 scopus 로고
    • Physicochemical characterization of the heat-stable microtubule-associated protein MAP2
    • Hernandez M.A., Avila J., Andreu J.M. Physicochemical characterization of the heat-stable microtubule-associated protein MAP2. Eur. J. Biochem. 154:1986;41-48.
    • (1986) Eur. J. Biochem , vol.154 , pp. 41-48
    • Hernandez, M.A.1    Avila, J.2    Andreu, J.M.3
  • 162
    • 0023127873 scopus 로고
    • Localization of the phosphorylation sites for different kinases in the microtubule-associated protein MAP2
    • Hernandez M.A., Wandosell F., Avila J. Localization of the phosphorylation sites for different kinases in the microtubule-associated protein MAP2. J. Neurochem. 48:1987;84-93.
    • (1987) J. Neurochem , vol.48 , pp. 84-93
    • Hernandez, M.A.1    Wandosell, F.2    Avila, J.3
  • 163
    • 0028902692 scopus 로고
    • Temporal response and effects of excitatory amino acid antagonism on microtubule-associated protein 2 immunoreactivity following experimental brain injury in rats
    • Hicks R.R., Smith D.H., McIntosh T.K. Temporal response and effects of excitatory amino acid antagonism on microtubule-associated protein 2 immunoreactivity following experimental brain injury in rats. Brain Res. 678:1995;151-160.
    • (1995) Brain Res , vol.678 , pp. 151-160
    • Hicks, R.R.1    Smith, D.H.2    McIntosh, T.K.3
  • 165
    • 0028118917 scopus 로고
    • Microtubule organization and dynamics dependent on microtubule-associated proteins
    • Hirokawa N. Microtubule organization and dynamics dependent on microtubule-associated proteins. Curr. Opin. Cell Biol. 6:1994;74-81.
    • (1994) Curr. Opin. Cell Biol , vol.6 , pp. 74-81
    • Hirokawa, N.1
  • 166
    • 0030028366 scopus 로고    scopus 로고
    • Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons
    • Hirokawa N., Funakoshi T., Sato-Harada R., Kanai Y. Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons. J. Cell Biol. 132:1996;667-679.
    • (1996) J. Cell Biol , vol.132 , pp. 667-679
    • Hirokawa, N.1    Funakoshi, T.2    Sato-Harada, R.3    Kanai, Y.4
  • 167
    • 0023766743 scopus 로고
    • MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: Quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies
    • Hirokawa N., Hisanaga S., Shiomura Y. MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies. J. Neurosci. 8:1988;2769-2779.
    • (1988) J. Neurosci , vol.8 , pp. 2769-2779
    • Hirokawa, N.1    Hisanaga, S.2    Shiomura, Y.3
  • 168
    • 0031018774 scopus 로고    scopus 로고
    • Okadaic acid induces hyperphosphorylation of tau independently of mitogen-activated protein kinase activation
    • Ho D., Shayan H., Murphy T. Okadaic acid induces hyperphosphorylation of tau independently of mitogen-activated protein kinase activation. J. Neurochem. 68:1997;106-111.
    • (1997) J. Neurochem , vol.68 , pp. 106-111
    • Ho, D.1    Shayan, H.2    Murphy, T.3
  • 169
    • 0030738354 scopus 로고    scopus 로고
    • Distribution of the messenger RNA for the extracellularly regulated kinases 1, 2 and 3 in rat brain: Effects of excitotoxic hippocampal lesions
    • Hollister R.D., Page K.J., Hyman B.T. Distribution of the messenger RNA for the extracellularly regulated kinases 1, 2 and 3 in rat brain: effects of excitotoxic hippocampal lesions. Neuroscience. 79:1997;1111-1119.
    • (1997) Neuroscience , vol.79 , pp. 1111-1119
    • Hollister, R.D.1    Page, K.J.2    Hyman, B.T.3
  • 170
    • 0027138757 scopus 로고
    • Inhibitors of protein phosphatase-1 and -2A; Two of the major serine/threonine protein phosphatases involved in cellular regulation
    • Holmes C., Boland M. Inhibitors of protein phosphatase-1 and -2A; two of the major serine/threonine protein phosphatases involved in cellular regulation. Curr. Op. Struc. Biol. 3:1993;934-943.
    • (1993) Curr. Op. Struc. Biol , vol.3 , pp. 934-943
    • Holmes, C.1    Boland, M.2
  • 171
    • 0030868557 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3
    • Hong M., Chen D., Klein P., Lee V. Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. J. Biol. Chem. 272:1997;25326-25332.
    • (1997) J. Biol. Chem , vol.272 , pp. 25326-25332
    • Hong, M.1    Chen, D.2    Klein, P.3    Lee, V.4
  • 172
    • 0023929120 scopus 로고
    • Protein-kinase-C-catalyzed phosphorylation of the microtubule-binding domain of microtubule-associated protein 2 inhibits its ability to induce tubulin polymerization
    • Hoshi M., Akiyama T., Shinohara Y., Miyata Y., Ogawara H., Nishida E., Sakai H. Protein-kinase-C-catalyzed phosphorylation of the microtubule-binding domain of microtubule-associated protein 2 inhibits its ability to induce tubulin polymerization. Eur. J. Biochem. 174:1988;225-230.
    • (1988) Eur. J. Biochem , vol.174 , pp. 225-230
    • Hoshi, M.1    Akiyama, T.2    Shinohara, Y.3    Miyata, Y.4    Ogawara, H.5    Nishida, E.6    Sakai, H.7
  • 173
    • 0026517618 scopus 로고
    • Mitogen-activated-protein-kinase-catalyzed phosphorylation of microtubule-associated proteins, microtubule-associated protein 2 and microtubule-associated protein 4, induces an alteration in their function
    • Hoshi M., Ohta K., Gotoh Y., Mori A., Murofushi H., Sakai H., Nishida E. Mitogen-activated-protein-kinase-catalyzed phosphorylation of microtubule-associated proteins, microtubule-associated protein 2 and microtubule-associated protein 4, induces an alteration in their function. Eur. J. Biochem. 203:1992;43-52.
    • (1992) Eur. J. Biochem , vol.203 , pp. 43-52
    • Hoshi, M.1    Ohta, K.2    Gotoh, Y.3    Mori, A.4    Murofushi, H.5    Sakai, H.6    Nishida, E.7
  • 174
    • 0030883128 scopus 로고    scopus 로고
    • Kinase and phosphatase inhibitors cause rapid alterations in microtubule dynamic instability in living cells
    • Howell B., Odde D., Cassimeris L. Kinase and phosphatase inhibitors cause rapid alterations in microtubule dynamic instability in living cells. Cell Motil. Cytos. 38:1997;201-214.
    • (1997) Cell Motil. Cytos , vol.38 , pp. 201-214
    • Howell, B.1    Odde, D.2    Cassimeris, L.3
  • 175
    • 0032493041 scopus 로고    scopus 로고
    • Synaptic plasticity: Going through phases with LTP
    • Huang E.P. Synaptic plasticity: going through phases with LTP. Curr. Biol. 8:1998;R350-R352.
    • (1998) Curr. Biol , vol.8
    • Huang, E.P.1
  • 176
    • 0021358628 scopus 로고
    • Differences in the cellular distributions of two microtubule-associated proteins, MAP1 and MAP2, in rat brain
    • Huber G., Matus A. Differences in the cellular distributions of two microtubule-associated proteins, MAP1 and MAP2, in rat brain. J. Neurosci. 4:1984;151-160.
    • (1984) J. Neurosci , vol.4 , pp. 151-160
    • Huber, G.1    Matus, A.2
  • 177
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug H., Sarre T. Protein kinase C isoenzymes: divergence in signal transduction? Biochem. J. 291:1993;329-343.
    • (1993) Biochem. J , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.2
  • 178
    • 0029965781 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110(mark): Phosphorylation sites and regulation of microtubule dynamics
    • Illenberger S., Drewes G., Trinczek B., Biernat J., Meyer H.E., Olmsted J.B., Mandelkow E.M., Mandelkow E. Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110(mark): Phosphorylation sites and regulation of microtubule dynamics. J. Biol. Chem. 271:1996;10834-10843.
    • (1996) J. Biol. Chem , vol.271 , pp. 10834-10843
    • Illenberger, S.1    Drewes, G.2    Trinczek, B.3    Biernat, J.4    Meyer, H.E.5    Olmsted, J.B.6    Mandelkow, E.M.7    Mandelkow, E.8
  • 179
    • 0031045216 scopus 로고    scopus 로고
    • Physiology and pathology of tau protein kinases in relation to Alzheimer's disease
    • Imahori K., Uchida T. Physiology and pathology of tau protein kinases in relation to Alzheimer's disease. Journal of Biochemistry. 121:1997;179-188.
    • (1997) Journal of Biochemistry , vol.121 , pp. 179-188
    • Imahori, K.1    Uchida, T.2
  • 182
    • 0027255817 scopus 로고
    • Glycogen synthase kinase 3ß is identical to tau protein kinase I generating several epitopes of paired helical filaments
    • Ishiguro K., Shiratsuchi A., Sato S., Omori A., Arioka M., Kobayashi S., Uchida T., Imahori K. Glycogen synthase kinase 3ß is identical to tau protein kinase I generating several epitopes of paired helical filaments. FEBS Lett. 325:1993;167-172.
    • (1993) FEBS Lett , vol.325 , pp. 167-172
    • Ishiguro, K.1    Shiratsuchi, A.2    Sato, S.3    Omori, A.4    Arioka, M.5    Kobayashi, S.6    Uchida, T.7    Imahori, K.8
  • 183
    • 0030847540 scopus 로고    scopus 로고
    • Phosphorylation states of microtubule-associated protein 2 (MAP2) determine the regulatory role of MAP2 in microtubule dynamics
    • Itoh T., Hisanaga S., Hosoi T., Kishimoto T., Hotani H. Phosphorylation states of microtubule-associated protein 2 (MAP2) determine the regulatory role of MAP2 in microtubule dynamics. Biochemistry. 36:1997;12574-12582.
    • (1997) Biochemistry , vol.36 , pp. 12574-12582
    • Itoh, T.1    Hisanaga, S.2    Hosoi, T.3    Kishimoto, T.4    Hotani, H.5
  • 184
    • 0028132184 scopus 로고
    • Microtubule-stabilizing activity of microtubule-associated proteins (MAPs) is due to increase in frequency of rescue in dynamic instability: Shortening length decreases with binding of MAPs onto microtubules
    • Itoh T., Hotani H. Microtubule-stabilizing activity of microtubule-associated proteins (MAPs) is due to increase in frequency of rescue in dynamic instability: shortening length decreases with binding of MAPs onto microtubules. Cell Struct. Funct. 19:1994;279-290.
    • (1994) Cell Struct. Funct , vol.19 , pp. 279-290
    • Itoh, T.1    Hotani, H.2
  • 186
    • 0009623452 scopus 로고
    • Modification of microtubule steady-state dynamics by phosphorylation of the microtubule-associated proteins
    • Jameson L., Caplow M. Modification of microtubule steady-state dynamics by phosphorylation of the microtubule-associated proteins. Proc. Natl. Acad. Sci. U.S.A. 78:1981;3413-3417.
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 3413-3417
    • Jameson, L.1    Caplow, M.2
  • 187
    • 0018958961 scopus 로고
    • Inhibition of microtubule assembly by phosphorylation of microtubule-associated proteins
    • Jameson L., Frey T., Zeeberg B., Dalldorf F., Caplow M. Inhibition of microtubule assembly by phosphorylation of microtubule-associated proteins. Biochemistry. 19:1980;2472-2479.
    • (1980) Biochemistry , vol.19 , pp. 2472-2479
    • Jameson, L.1    Frey, T.2    Zeeberg, B.3    Dalldorf, F.4    Caplow, M.5
  • 188
    • 0025966261 scopus 로고
    • Phosphorylation of microtubule-associated protein-2 in GH3 cells. Regulation by cAMP and by calcium
    • Jefferson A.B., Schulman H. Phosphorylation of microtubule-associated protein-2 in GH3 cells. Regulation by cAMP and by calcium. J. Biol. Chem. 266:1991;346-354.
    • (1991) J. Biol. Chem , vol.266 , pp. 346-354
    • Jefferson, A.B.1    Schulman, H.2
  • 189
    • 0030628307 scopus 로고    scopus 로고
    • Protein phosphatases: Structures and implications
    • Jia Z.C. Protein phosphatases: structures and implications. Biochemistry and Cell Biology. 75:1997;17-26.
    • (1997) Biochemistry and Cell Biology , vol.75 , pp. 17-26
    • Jia, Z.C.1
  • 190
  • 191
    • 0026472560 scopus 로고
    • The role of microtubule-associated protein 2 (MAP-2) in neuronal growth, plasticity, and degeneration
    • Johnson G.V., Jope R.S. The role of microtubule-associated protein 2 (MAP-2) in neuronal growth, plasticity, and degeneration. J. Neurosci. Res. 33:1992;505-512.
    • (1992) J. Neurosci. Res , vol.33 , pp. 505-512
    • Johnson, G.V.1    Jope, R.S.2
  • 192
    • 0025731595 scopus 로고
    • Degradation of microtubule-associated protein 2 and brain spectrin by calpain: A comparative study
    • Johnson G.V., Litersky J.M., Jope R.S. Degradation of microtubule-associated protein 2 and brain spectrin by calpain: a comparative study. J. Neurochem. 56:1991;1630-1638.
    • (1991) J. Neurochem , vol.56 , pp. 1630-1638
    • Johnson, G.V.1    Litersky, J.M.2    Jope, R.S.3
  • 193
    • 0028232890 scopus 로고
    • NMDA and nitric oxide increase microtubule-associated protein 2 gene expression in hippocampal granule cells
    • Johnston H.M., Morris B.J. NMDA and nitric oxide increase microtubule-associated protein 2 gene expression in hippocampal granule cells. J. Neurochem. 63:1994;379-382.
    • (1994) J. Neurochem , vol.63 , pp. 379-382
    • Johnston, H.M.1    Morris, B.J.2
  • 194
    • 0032947795 scopus 로고    scopus 로고
    • Anti-bipolar therapy: Mechanism of action of lithium
    • Jope R.S. Anti-bipolar therapy: mechanism of action of lithium. Mol. Psychiatr. 4:1999;117-128.
    • (1999) Mol. Psychiatr , vol.4 , pp. 117-128
    • Jope, R.S.1
  • 195
    • 0033013011 scopus 로고    scopus 로고
    • A bimodal model of the mechanism of action of lithium
    • Jope R.S. A bimodal model of the mechanism of action of lithium. Mol. Psychiatr. 4:1999;21-25.
    • (1999) Mol. Psychiatr , vol.4 , pp. 21-25
    • Jope, R.S.1
  • 196
    • 0030462207 scopus 로고    scopus 로고
    • Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins
    • Kaech S., Ludin B., Matus A. Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins. Neuron. 17:1996;1189-1199.
    • (1996) Neuron , vol.17 , pp. 1189-1199
    • Kaech, S.1    Ludin, B.2    Matus, A.3
  • 197
    • 0028793125 scopus 로고
    • Genomic structure of human microtubule-associated protein 2 (MAP-2) and characterization of additional MAP-2 isoforms
    • Kalcheva N., Albala J., O'Guin K., Rubino H., Garner C., Shafit-Zagardo B. Genomic structure of human microtubule-associated protein 2 (MAP-2) and characterization of additional MAP-2 isoforms. Proc. Natl. Acad. Sci. U.S.A. 92:1995;10894-10898.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 10894-10898
    • Kalcheva, N.1    Albala, J.2    O'Guin, K.3    Rubino, H.4    Garner, C.5    Shafit-Zagardo, B.6
  • 198
    • 0028153172 scopus 로고
    • Localization of specific epitopes on human microtubule-associated protein 2
    • Kalcheva N., Albala J.S., Binder L.I., Shafit-Zagardo B. Localization of specific epitopes on human microtubule-associated protein 2. J. Neurochem. 63:1994;2336-2341.
    • (1994) J. Neurochem , vol.63 , pp. 2336-2341
    • Kalcheva, N.1    Albala, J.S.2    Binder, L.I.3    Shafit-Zagardo, B.4
  • 199
    • 0031747115 scopus 로고    scopus 로고
    • Molecular and functional characteristics of MAP-2a: Ability of MAP-2a versus MAP-2b to induce stable microtubules in COS cells
    • Kalcheva N., Rockwood J.M., Kress Y., Steiner A., ShafitZagardo B. Molecular and functional characteristics of MAP-2a: ability of MAP-2a versus MAP-2b to induce stable microtubules in COS cells. Cell Motil. Cytoskeleton. 40:1998;272-285.
    • (1998) Cell Motil. Cytoskeleton , vol.40 , pp. 272-285
    • Kalcheva, N.1    Rockwood, J.M.2    Kress, Y.3    Steiner, A.4    Shafitzagardo, B.5
  • 200
    • 0031037198 scopus 로고    scopus 로고
    • Expression of microtubule-associated protein-2a and other novel microtubule-associated protein-2 transcripts in human fetal spinal cord
    • Kalcheva N., Weidenheim K.M., Kress Y., Shafit-Zagardo B. Expression of microtubule-associated protein-2a and other novel microtubule-associated protein-2 transcripts in human fetal spinal cord. J. Neurochem. 68:1997;383-391.
    • (1997) J. Neurochem , vol.68 , pp. 383-391
    • Kalcheva, N.1    Weidenheim, K.M.2    Kress, Y.3    Shafit-Zagardo, B.4
  • 201
    • 0030951668 scopus 로고    scopus 로고
    • Mechanisms of calpain proteolysis following traumatic brain injury: Implications for pathology and therapy: A review and update
    • Kampfl A., Posmantur R.M., Zhao X., Schmutzhard E., Clifton G.L., Hayes R.L. Mechanisms of calpain proteolysis following traumatic brain injury: implications for pathology and therapy: a review and update. Journal of Neurotrauma. 14:1997;121-134.
    • (1997) Journal of Neurotrauma , vol.14 , pp. 121-134
    • Kampfl, A.1    Posmantur, R.M.2    Zhao, X.3    Schmutzhard, E.4    Clifton, G.L.5    Hayes, R.L.6
  • 202
    • 0028838142 scopus 로고
    • Sorting mechanisms of tau and MAP2 in neurons: Suppressed axonal transit of MAP2 and locally regulated microtubule binding
    • Kanai Y., Hirokawa N. Sorting mechanisms of tau and MAP2 in neurons: suppressed axonal transit of MAP2 and locally regulated microtubule binding. Neuron. 14:1995;421-432.
    • (1995) Neuron , vol.14 , pp. 421-432
    • Kanai, Y.1    Hirokawa, N.2
  • 203
    • 0030813634 scopus 로고    scopus 로고
    • A turning point in Schizophrenia genetics
    • Karayiorgou M., Gogos J. A turning point in Schizophrenia genetics. Neuron. 19:1997;967-979.
    • (1997) Neuron , vol.19 , pp. 967-979
    • Karayiorgou, M.1    Gogos, J.2
  • 204
    • 0029812945 scopus 로고    scopus 로고
    • Tau binds to the distal axon early in development of polarity in a microtubule- And microfilament-dependent manner
    • Kempf M., Clement A., Faissner A., Lee G., Brandt R. Tau binds to the distal axon early in development of polarity in a microtubule- and microfilament-dependent manner. Journal of Neuroscience. 16:1996;5583-5592.
    • (1996) Journal of Neuroscience , vol.16 , pp. 5583-5592
    • Kempf, M.1    Clement, A.2    Faissner, A.3    Lee, G.4    Brandt, R.5
  • 205
    • 0032077680 scopus 로고    scopus 로고
    • Signal transduction molecules at the glutamatergic postsynaptic membrane
    • Kennedy M.B. Signal transduction molecules at the glutamatergic postsynaptic membrane. Brain Res. Rev. 26:1998;243-257.
    • (1998) Brain Res. Rev , vol.26 , pp. 243-257
    • Kennedy, M.B.1
  • 206
    • 0028027393 scopus 로고
    • Four repeat MAP2 isoforms in human and rat brain
    • Kindler S., Garner C.C. Four repeat MAP2 isoforms in human and rat brain. Brain Res. Mol. Brain Res. 26:1994;218-224.
    • (1994) Brain Res. Mol. Brain Res , vol.26 , pp. 218-224
    • Kindler, S.1    Garner, C.C.2
  • 207
    • 0343090204 scopus 로고    scopus 로고
    • Molecular characterization of dendritically localized transcripts encoding MAP2
    • Kindler S., Muller R., Chung W.J., Garner C.C. Molecular characterization of dendritically localized transcripts encoding MAP2. Brain Res. Mol. Brain Res. 36:1996;63-69.
    • (1996) Brain Res. Mol. Brain Res , vol.36 , pp. 63-69
    • Kindler, S.1    Muller, R.2    Chung, W.J.3    Garner, C.C.4
  • 208
    • 0025200975 scopus 로고
    • Molecular structure of microtubule-associated protein 2b and 2c from rat brain
    • Kindler S., Schulz B., Goedert M., Garner C.C. Molecular structure of microtubule-associated protein 2b and 2c from rat brain. J. Biol. Chem. 265:1990;19679-19684.
    • (1990) J. Biol. Chem , vol.265 , pp. 19679-19684
    • Kindler, S.1    Schulz, B.2    Goedert, M.3    Garner, C.C.4
  • 210
    • 0025603077 scopus 로고
    • Differential subcellular localization of particular mRNAs in hippocampal neurons in culture
    • Kleiman R., Banker G., Steward O. Differential subcellular localization of particular mRNAs in hippocampal neurons in culture. Neuron. 5:1990;821-830.
    • (1990) Neuron , vol.5 , pp. 821-830
    • Kleiman, R.1    Banker, G.2    Steward, O.3
  • 211
    • 0028265297 scopus 로고
    • Development of subcellular mRNA compartmentation in hippocampal neurons in culture
    • Kleiman, R., Banker, G., Steward, O., 1994. Development of subcellular mRNA compartmentation in hippocampal neurons in culture. J. Neurosci. 14, 1130-1140.
    • (1994) J. Neurosci. , vol.14 , pp. 1130-1140
    • Kleiman, R.1    Banker, G.2    Steward, O.3
  • 212
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein P., Melton D. A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. U.S.A. 93:1996;8455-8459.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 8455-8459
    • Klein, P.1    Melton, D.2
  • 213
    • 0032576544 scopus 로고    scopus 로고
    • Nonuniform microtubular polarity established by CHO1/MKLP1 motor protein is necessary for process formation of podocytes
    • Kobayashi N., Reiser J., Kriz W., Kuriyama R., Mundel P. Nonuniform microtubular polarity established by CHO1/MKLP1 motor protein is necessary for process formation of podocytes. J. Cell Biol. 143:1998;1961-1970.
    • (1998) J. Cell Biol , vol.143 , pp. 1961-1970
    • Kobayashi, N.1    Reiser, J.2    Kriz, W.3    Kuriyama, R.4    Mundel, P.5
  • 214
  • 215
    • 0030920771 scopus 로고    scopus 로고
    • A kinase to remember: Dual roles for MAP kinase in long-term memory
    • Kornhauser J.M., Greenberg M.E. A kinase to remember: dual roles for MAP kinase in long-term memory. Neuron. 18:1997;839-842.
    • (1997) Neuron , vol.18 , pp. 839-842
    • Kornhauser, J.M.1    Greenberg, M.E.2
  • 216
    • 0028229455 scopus 로고
    • Microtubule-associated protein function: Lessons from expression in Spodoptera frugiperda cells
    • Kosik K.S., McConlogue L. Microtubule-associated protein function: lessons from expression in Spodoptera frugiperda cells. Cell Motil. Cytoskeleton. 28:1994;195-198.
    • (1994) Cell Motil. Cytoskeleton , vol.28 , pp. 195-198
    • Kosik, K.S.1    McConlogue, L.2
  • 217
    • 0027285334 scopus 로고
    • Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly
    • Kowalski R.J., Williams R.J. Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly. J. Biol. Chem. 268:1993;9847-9855.
    • (1993) J. Biol. Chem , vol.268 , pp. 9847-9855
    • Kowalski, R.J.1    Williams, R.J.2
  • 218
    • 0032953178 scopus 로고    scopus 로고
    • Upregulation of nuclear GM1 accompanies axon- like, but not dendrite-like, outgrowth in NG108-15 cells
    • Kozireski-Chuback D., Wu G.S., Ledeen R.W. Upregulation of nuclear GM1 accompanies axon- like, but not dendrite-like, outgrowth in NG108-15 cells. J. Neurosci. Res. 55:1999;107-118.
    • (1999) J. Neurosci. Res , vol.55 , pp. 107-118
    • Kozireski-Chuback, D.1    Wu, G.S.2    Ledeen, R.W.3
  • 220
    • 0028822031 scopus 로고
    • Microtubule-associated proteins and the flexibility of microtubules
    • Kurz J.C., Williams R.J. Microtubule-associated proteins and the flexibility of microtubules. Biochemistry. 34:1995;13374-13380.
    • (1995) Biochemistry , vol.34 , pp. 13374-13380
    • Kurz, J.C.1    Williams, R.J.2
  • 221
    • 0032550114 scopus 로고    scopus 로고
    • Differential interactions of MAP2, tau and MAP5 during axogenesis in culture
    • Kwei S.L., Clement A., Faissner A., Brandt R. Differential interactions of MAP2, tau and MAP5 during axogenesis in culture. Neuroreport. 9:1998;1035-1040.
    • (1998) Neuroreport , vol.9 , pp. 1035-1040
    • Kwei, S.L.1    Clement, A.2    Faissner, A.3    Brandt, R.4
  • 222
    • 0028890306 scopus 로고
    • Tau and microtubule-associated protein 2c transfection and neurite outgrowth in ND 7/23 cells
    • Langkopf A., Guilleminot J., Nunez J. Tau and microtubule-associated protein 2c transfection and neurite outgrowth in ND 7/23 cells. J. Neurochem. 64:1995;1045-1053.
    • (1995) J. Neurochem , vol.64 , pp. 1045-1053
    • Langkopf, A.1    Guilleminot, J.2    Nunez, J.3
  • 224
    • 0029921189 scopus 로고    scopus 로고
    • Juvenile and mature MAP2 isoforms induce distinct patterns of process outgrowth
    • Leclerc N., Baas P., Garner C., Kosik K. Juvenile and mature MAP2 isoforms induce distinct patterns of process outgrowth. Mol. Biol. Cell. 7:1996;443-455.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 443-455
    • Leclerc, N.1    Baas, P.2    Garner, C.3    Kosik, K.4
  • 225
    • 0027318768 scopus 로고
    • Process formation in Sf9 cells induced by the expression of a microtubule-associated protein 2C-like construct
    • Leclerc N., Kosik K.S., Cowan N., Pienkowski T.P., Baas P.W. Process formation in Sf9 cells induced by the expression of a microtubule-associated protein 2C-like construct. Proc. Natl. Acad. Sci. U.S.A. 90:1993;6223-6227.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 6223-6227
    • Leclerc, N.1    Kosik, K.S.2    Cowan, N.3    Pienkowski, T.P.4    Baas, P.W.5
  • 226
    • 0026694067 scopus 로고
    • Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease
    • Ledesma M.D., Correas I., Avila J., Díaz-Nido J. Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease. FEBS Lett. 308:1992;218-224.
    • (1992) FEBS Lett , vol.308 , pp. 218-224
    • Ledesma, M.D.1    Correas, I.2    Avila, J.3    Díaz-Nido, J.4
  • 227
    • 0027551389 scopus 로고
    • Non-motor microtubule-associated proteins
    • Lee G. Non-motor microtubule-associated proteins. Curr. Opin. Cell Biol. 5:1993;88-94.
    • (1993) Curr. Opin. Cell Biol , vol.5 , pp. 88-94
    • Lee, G.1
  • 228
    • 0026670808 scopus 로고
    • Microtubule-bundling studies revisited: Is there a role for MAPs?
    • Lee G., Brandt R. Microtubule-bundling studies revisited: is there a role for MAPs? TICB. 2:1993;286-289.
    • (1993) TICB , vol.2 , pp. 286-289
    • Lee, G.1    Brandt, R.2
  • 229
    • 0033026832 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II is associated with the N-methyl-D-aspartate receptor
    • Leonard A.S., Lim I.A., Hemsworth D.E., Horne M.C., Hell J.W. Calcium/calmodulin-dependent protein kinase II is associated with the N-methyl-D-aspartate receptor. Proc. Natl. Acad. Sci. U.S.A. 96:1999;3239-3244.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 3239-3244
    • Leonard, A.S.1    Lim, I.A.2    Hemsworth, D.E.3    Horne, M.C.4    Hell, J.W.5
  • 230
    • 0032955426 scopus 로고    scopus 로고
    • Insulin transiently increases tau phosphorylation: Involvement of glycogen synthase kinase-3 beta and Fyn tyrosine kinase
    • Lesort M., Jope R.S., Johnson G.V.W. Insulin transiently increases tau phosphorylation: Involvement of glycogen synthase kinase-3 beta and Fyn tyrosine kinase. J. Neurochem. 72:1999;576-584.
    • (1999) J. Neurochem , vol.72 , pp. 576-584
    • Lesort, M.1    Jope, R.S.2    Johnson, G.V.W.3
  • 231
    • 0030318068 scopus 로고    scopus 로고
    • The cytoskeleton in nerve growth cone motility and axonal pathfinding
    • Letourneau P.C. The cytoskeleton in nerve growth cone motility and axonal pathfinding. Perspectives Dev. Neurobiol. 4:1996;111-123.
    • (1996) Perspectives Dev. Neurobiol , vol.4 , pp. 111-123
    • Letourneau, P.C.1
  • 232
    • 0031055418 scopus 로고    scopus 로고
    • Organization of pyramidal cell apical dendrites and composition of dendritic clusters in the mouse: Emphasis on primary motor cortex
    • Lev D.L., White E.L. Organization of pyramidal cell apical dendrites and composition of dendritic clusters in the mouse: emphasis on primary motor cortex. Eur. J. Neurosci. 9:1997;280-290.
    • (1997) Eur. J. Neurosci , vol.9 , pp. 280-290
    • Lev, D.L.1    White, E.L.2
  • 233
  • 234
    • 0025289620 scopus 로고
    • Microtubule bundling
    • Lewis S., Cowan N. Microtubule bundling. Nature. 345:1990;674.
    • (1990) Nature , vol.345 , pp. 674
    • Lewis, S.1    Cowan, N.2
  • 236
    • 0024268202 scopus 로고
    • Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein
    • Lewis S.A., Wang D.H., Cowan N.J. Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein. Science. 242:1988;936-939.
    • (1988) Science , vol.242 , pp. 936-939
    • Lewis, S.A.1    Wang, D.H.2    Cowan, N.J.3
  • 237
    • 0032555642 scopus 로고    scopus 로고
    • Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau
    • Liao H., Li Y.R., Brautigan D.L., Gundersen G.G. Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau. J. Biol. Chem. 273:1998;21901-21908.
    • (1998) J. Biol. Chem , vol.273 , pp. 21901-21908
    • Liao, H.1    Li, Y.R.2    Brautigan, D.L.3    Gundersen, G.G.4
  • 238
    • 0030843838 scopus 로고    scopus 로고
    • Glutamatergic effects and depolarization block
    • Lidsky T.I., Banerjee S.P. Glutamatergic effects and depolarization block. Trends in Neurosciences. 20:1997;393-393.
    • (1997) Trends in Neurosciences , vol.20 , pp. 393-393
    • Lidsky, T.I.1    Banerjee, S.P.2
  • 239
    • 4243762257 scopus 로고    scopus 로고
    • Intereaction of the neuronal microtubule-associated protein MAP2 with SH3 domains
    • (ne903)
    • Lim, R., Halpain, S., 1998. Intereaction of the neuronal microtubule-associated protein MAP2 with SH3 domains. Mol. Biol. Cell. 9. 156a (ne903).
    • (1998) Mol. Biol. Cell. , vol.9
    • Lim, R.1    Halpain, S.2
  • 240
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • Lis H., Sharon N. Protein glycosylation. Structural and functional aspects. Eur. J. Biochem. 218:1993;1-27.
    • (1993) Eur. J. Biochem , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 241
    • 0030345101 scopus 로고    scopus 로고
    • Factors regulating organelles transport along microtubules
    • Lopez L.A. Factors regulating organelles transport along microtubules. Biocell. 20:1996;313-316.
    • (1996) Biocell , vol.20 , pp. 313-316
    • Lopez, L.A.1
  • 242
    • 0027533201 scopus 로고
    • Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2
    • Lopez L.A., Sheetz M.P. Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2. Cell Motil. Cytoskeleton. 24:1993;1-16.
    • (1993) Cell Motil. Cytoskeleton , vol.24 , pp. 1-16
    • Lopez, L.A.1    Sheetz, M.P.2
  • 243
    • 0028999047 scopus 로고
    • A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain
    • Lopez L.A., Sheetz M.P. A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain. J. Biol. Chem. 270:1995;12511-12517.
    • (1995) J. Biol. Chem , vol.270 , pp. 12511-12517
    • Lopez, L.A.1    Sheetz, M.P.2
  • 244
    • 0141722008 scopus 로고    scopus 로고
    • Pharmacology of glutamate receptor antagonists in the kindling model of epilepsy
    • Loscher W. Pharmacology of glutamate receptor antagonists in the kindling model of epilepsy. Prog. Neurobiol. 54:1998;721-741.
    • (1998) Prog. Neurobiol , vol.54 , pp. 721-741
    • Loscher, W.1
  • 246
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by GSK-3β in intact mammalian cells: The effects on the organization and stability of microtubules
    • Lovestone S., Hartley C., Pearce J., Anderton B. Phosphorylation of tau by GSK-3β in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience. 73:1996;1145-1157.
    • (1996) Neuroscience , vol.73 , pp. 1145-1157
    • Lovestone, S.1    Hartley, C.2    Pearce, J.3    Anderton, B.4
  • 247
    • 0030937952 scopus 로고    scopus 로고
    • The phosphorylation of tau: A critical stage in neurodevelopment and neurodegenerative processes
    • Lovestone S., Reynolds C.H. The phosphorylation of tau: a critical stage in neurodevelopment and neurodegenerative processes. Neuroscience. 78:1997;309-324.
    • (1997) Neuroscience , vol.78 , pp. 309-324
    • Lovestone, S.1    Reynolds, C.H.2
  • 248
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu K., Hanes S., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature. 380:1996;544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.1    Hanes, S.2    Hunter, T.3
  • 249
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin 1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu P., Wulf G., Zhou X., Davies P., Lu K. The prolyl isomerase Pin 1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature. 399:1999;784-788.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.1    Wulf, G.2    Zhou, X.3    Davies, P.4    Lu, K.5
  • 250
    • 0031800971 scopus 로고    scopus 로고
    • Inhibition of GSK-3 beta leading to the loss of phosphorylated MAP-1B is an early event in axonal remodelling induced by WNT-7a or lithium
    • Lucas F.R., Goold R.G., GordonWeeks P.R., Salinas P.C. Inhibition of GSK-3 beta leading to the loss of phosphorylated MAP-1B is an early event in axonal remodelling induced by WNT-7a or lithium. J. Cell Sci. 111:1998;1351-1361.
    • (1998) J. Cell Sci , vol.111 , pp. 1351-1361
    • Lucas, F.R.1    Goold, R.G.2    Gordonweeks, P.R.3    Salinas, P.C.4
  • 251
  • 252
    • 0027371221 scopus 로고
    • The neuronal cytoskeleton and its role in axonal and dendritic plasticity
    • Ludin B., Matus A. The neuronal cytoskeleton and its role in axonal and dendritic plasticity. Hippocampus. 3:1993;61-71.
    • (1993) Hippocampus , vol.3 , pp. 61-71
    • Ludin, B.1    Matus, A.2
  • 254
    • 0028845388 scopus 로고
    • Role of microtubule-associated proteins in the control of microtubule assembly
    • Maccioni R.B., Cambiazo V. Role of microtubule-associated proteins in the control of microtubule assembly. Physiol. Rev. 75:1995;835-864.
    • (1995) Physiol. Rev , vol.75 , pp. 835-864
    • Maccioni, R.B.1    Cambiazo, V.2
  • 255
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications: Enzymes and their mechanisms of action
    • MacRae T.H. Tubulin post-translational modifications: enzymes and their mechanisms of action. European Journal of Biochemistry. 244:1997;265-278.
    • (1997) European Journal of Biochemistry , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 256
    • 0026600692 scopus 로고
    • A novel 24-kDa microtubule-associated protein purified from sea urchin eggs
    • Maekawa S., Toriyama M., Sakai H. A novel 24-kDa microtubule-associated protein purified from sea urchin eggs. Eur. J. Biochem. 205:1992;1195-1200.
    • (1992) Eur. J. Biochem , vol.205 , pp. 1195-1200
    • Maekawa, S.1    Toriyama, M.2    Sakai, H.3
  • 257
    • 0027941257 scopus 로고
    • Synaptic plasticity in the hippocampus: LTP and LTD
    • Malenka R. Synaptic plasticity in the hippocampus: LTP and LTD. Cell. 78:1994;535-538.
    • (1994) Cell , vol.78 , pp. 535-538
    • Malenka, R.1
  • 258
    • 0032966626 scopus 로고    scopus 로고
    • Structures of kinesin and kinesin-microtubule interactions
    • Mandelkow E., Hoenger A. Structures of kinesin and kinesin-microtubule interactions. Curr. Opin. Cell Biol. 11:1999;34-44.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 34-44
    • Mandelkow, E.1    Hoenger, A.2
  • 259
    • 0028945057 scopus 로고
    • Microtubules and microtubule-associated proteins
    • Mandelkow E., Mandelkow E.M. Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol. 7:1995;72-81.
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 72-81
    • Mandelkow, E.1    Mandelkow, E.M.2
  • 260
    • 0029037004 scopus 로고
    • The microtubule lattice-dynamic instability of concepts
    • Mandelkow E., Song Y., Mandelkow E. The microtubule lattice-dynamic instability of concepts. TICB. 5:1995;262-266.
    • (1995) TICB , vol.5 , pp. 262-266
    • Mandelkow, E.1    Song, Y.2    Mandelkow, E.3
  • 262
    • 0030319523 scopus 로고    scopus 로고
    • Microtubule-associated proteins, phosphorylation gradients, and the establishment of neuronal polarity
    • Mandell J.W., Banker G.A. Microtubule-associated proteins, phosphorylation gradients, and the establishment of neuronal polarity. Perspectives Dev. Neurobiol. 4:1996;125-135.
    • (1996) Perspectives Dev. Neurobiol , vol.4 , pp. 125-135
    • Mandell, J.W.1    Banker, G.A.2
  • 263
    • 0029835019 scopus 로고    scopus 로고
    • A spatial gradient of tau protein phosphorylation in nascent axons
    • Mandell J.W., Banker G.A. A spatial gradient of tau protein phosphorylation in nascent axons. J. Neurosci. 16:1996;5727-5740.
    • (1996) J. Neurosci , vol.16 , pp. 5727-5740
    • Mandell, J.W.1    Banker, G.A.2
  • 264
    • 0031593391 scopus 로고    scopus 로고
    • The role of GSK3 beta in regulating neuronal differentiation in Xenopus laevis
    • Marcus E.A., Kintner C., Harris W. The role of GSK3 beta in regulating neuronal differentiation in Xenopus laevis. Mol. Cell Neurosci. 12:1998;269-280.
    • (1998) Mol. Cell Neurosci , vol.12 , pp. 269-280
    • Marcus, E.A.1    Kintner, C.2    Harris, W.3
  • 265
    • 0029927743 scopus 로고    scopus 로고
    • Transgenic expression of embryonic MAP2 in adult mouse brain: Implications for neuronal polarization
    • Marsden K.M., Doll T., Ferralli J., Botteri F., Matus A. Transgenic expression of embryonic MAP2 in adult mouse brain: implications for neuronal polarization. J. Neurosci. 16:1996;3265-3273.
    • (1996) J. Neurosci , vol.16 , pp. 3265-3273
    • Marsden, K.M.1    Doll, T.2    Ferralli, J.3    Botteri, F.4    Matus, A.5
  • 267
    • 0029958251 scopus 로고    scopus 로고
    • Ultrastructural localization of dendritic messenger RNA in adult rat hippocampus
    • Martone M.E., Pollock J.A., Jones Y.Z., Ellisman M.H. Ultrastructural localization of dendritic messenger RNA in adult rat hippocampus. J. Neurosci. 16:1996;7437-7446.
    • (1996) J. Neurosci , vol.16 , pp. 7437-7446
    • Martone, M.E.1    Pollock, J.A.2    Jones, Y.Z.3    Ellisman, M.H.4
  • 268
    • 0032890340 scopus 로고    scopus 로고
    • Microtubule-associated protein-2 in the hypothalamo-neurohypophysial system: Low-molecular-weight microtubule-associated protein-2 in pituitary astrocytes
    • Matsunaga W., Miyata S., Hashimoto Y., Lin S.H., Nakashima T., Kiyohara T., Matsumoto T. Microtubule-associated protein-2 in the hypothalamo-neurohypophysial system: low-molecular-weight microtubule-associated protein-2 in pituitary astrocytes. Neuroscience. 88:1999;1289-1297.
    • (1999) Neuroscience , vol.88 , pp. 1289-1297
    • Matsunaga, W.1    Miyata, S.2    Hashimoto, Y.3    Lin, S.H.4    Nakashima, T.5    Kiyohara, T.6    Matsumoto, T.7
  • 269
    • 0023674299 scopus 로고
    • Microtubule-associated proteins: Their potential role in determining neuronal morphology
    • Matus A. Microtubule-associated proteins: their potential role in determining neuronal morphology. Annu. Rev. Neurosci. 11:1988;29-44.
    • (1988) Annu. Rev. Neurosci , vol.11 , pp. 29-44
    • Matus, A.1
  • 270
    • 0025082438 scopus 로고
    • Microtubule-associated proteins
    • Matus A. Microtubule-associated proteins. Curr. Opin. Cell Biol. 2:1990;10-14.
    • (1990) Curr. Opin. Cell Biol , vol.2 , pp. 10-14
    • Matus, A.1
  • 271
    • 0026309309 scopus 로고
    • Microtubule-associated proteins and neuronal morphogenesis
    • Matus A. Microtubule-associated proteins and neuronal morphogenesis. J. Cell. Sci. Suppl. 15:1991;61-67.
    • (1991) J. Cell. Sci. Suppl , vol.15 , pp. 61-67
    • Matus, A.1
  • 272
    • 0028082066 scopus 로고
    • Stiff microtubules and neuronal morphology
    • Matus A. Stiff microtubules and neuronal morphology. TINS. 17:1994;19-22.
    • (1994) TINS , vol.17 , pp. 19-22
    • Matus, A.1
  • 273
    • 0027299438 scopus 로고
    • The low molecular weight form of microtubule-associated protein 2 is transported into both axons and dendrites
    • Meichsner M., Doll T., Reddy D., Weisshaar B., Matus A. The low molecular weight form of microtubule-associated protein 2 is transported into both axons and dendrites. Neuroscience. 54:1993;873-880.
    • (1993) Neuroscience , vol.54 , pp. 873-880
    • Meichsner, M.1    Doll, T.2    Reddy, D.3    Weisshaar, B.4    Matus, A.5
  • 274
    • 0032030754 scopus 로고    scopus 로고
    • Effect of glutamate on dendritic growth in embryonic rat motoneurons
    • Metzger F., Wiese S., Sendtner M. Effect of glutamate on dendritic growth in embryonic rat motoneurons. J. Neurosci. 18:1998;1735-1742.
    • (1998) J. Neurosci , vol.18 , pp. 1735-1742
    • Metzger, F.1    Wiese, S.2    Sendtner, M.3
  • 275
    • 0032473367 scopus 로고    scopus 로고
    • Molecular biology of glutamate receptors in the central nervous system and their role in excitotoxicity, oxidative stress and aging
    • Michaelis E.K. Molecular biology of glutamate receptors in the central nervous system and their role in excitotoxicity, oxidative stress and aging. Prog. Neurobiol. 54:1998;369-415.
    • (1998) Prog. Neurobiol , vol.54 , pp. 369-415
    • Michaelis, E.K.1
  • 276
    • 0032502829 scopus 로고    scopus 로고
    • Characterization of tau phosphorylation in glycogen synthase kinase-3 beta and cyclin dependent kinase-5 activator (p23) transfected cells
    • Michel G., Mercken M., Murayama M., Noguchi K., Ishiguro K., Imahori K., Takashima A. Characterization of tau phosphorylation in glycogen synthase kinase-3 beta and cyclin dependent kinase-5 activator (p23) transfected cells. Bba. Gen. Subjects. 1380:1998;177-182.
    • (1998) Bba. Gen. Subjects , vol.1380 , pp. 177-182
    • Michel, G.1    Mercken, M.2    Murayama, M.3    Noguchi, K.4    Ishiguro, K.5    Imahori, K.6    Takashima, A.7
  • 277
    • 0029964851 scopus 로고    scopus 로고
    • Signal transduction through b-catenin and specification of cell fate during embryogenesis
    • Miller J., Moon R. Signal transduction through b-catenin and specification of cell fate during embryogenesis. Genes and Development. 10:1996;2527-2539.
    • (1996) Genes and Development , vol.10 , pp. 2527-2539
    • Miller, J.1    Moon, R.2
  • 278
    • 0032032006 scopus 로고    scopus 로고
    • Cognitive neuroscience and the study of memory
    • Milner B., Squire L.R., Kandel E.R. Cognitive neuroscience and the study of memory. Neuron. 20:1998;445-468.
    • (1998) Neuron , vol.20 , pp. 445-468
    • Milner, B.1    Squire, L.R.2    Kandel, E.R.3
  • 279
    • 0344765458 scopus 로고    scopus 로고
    • Nicotine prevents glutamate-induced proteolysis of the microtubule-associated protein MAP-2 and glutamate neurotoxicity in primary cultures of cerebellar neurons
    • Miñana M.D., Montoliu C., Llansola M., Grisolia S., Felipo V. Nicotine prevents glutamate-induced proteolysis of the microtubule-associated protein MAP-2 and glutamate neurotoxicity in primary cultures of cerebellar neurons. Neuropharmacology. 37:1998;847-857.
    • (1998) Neuropharmacology , vol.37 , pp. 847-857
    • Miñana, M.D.1    Montoliu, C.2    Llansola, M.3    Grisolia, S.4    Felipo, V.5
  • 281
    • 0025228723 scopus 로고
    • Nerve growth factor stimulates a protein kinase in PC-12 cells that phosphorylates microtubule-associated protein-2
    • Miyasaka T., Chao M.V., Sherline P., Saltiel A.R. Nerve growth factor stimulates a protein kinase in PC-12 cells that phosphorylates microtubule-associated protein-2. J. Biol. Chem. 265:1990;4730-4735.
    • (1990) J. Biol. Chem , vol.265 , pp. 4730-4735
    • Miyasaka, T.1    Chao, M.V.2    Sherline, P.3    Saltiel, A.R.4
  • 282
    • 0025326750 scopus 로고
    • Okadaic acid stimulates the activity of microtubule associated protein kinase in PC-12 pheochromocytoma cells
    • Miyasaka T., Miyasaka J., Saltiel A.R. Okadaic acid stimulates the activity of microtubule associated protein kinase in PC-12 pheochromocytoma cells. Biochem. Biophys. Res. Commun. 168:1990;1237-1243.
    • (1990) Biochem. Biophys. Res. Commun , vol.168 , pp. 1237-1243
    • Miyasaka, T.1    Miyasaka, J.2    Saltiel, A.R.3
  • 283
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D. Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science. 268:1995;247-251.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 284
    • 0027162747 scopus 로고
    • N-methyl-D-aspartate stimulates the dephosphorylation of the microtubule-associated protein 2 and potentiates excitatory synaptic pathways in the rat hippocampus
    • Montoro R.J., Díaz-Nido J., Avila J., Lopez B.J. N-methyl-D-aspartate stimulates the dephosphorylation of the microtubule-associated protein 2 and potentiates excitatory synaptic pathways in the rat hippocampus. Neuroscience. 54:1993;859-871.
    • (1993) Neuroscience , vol.54 , pp. 859-871
    • Montoro, R.J.1    Díaz-Nido, J.2    Avila, J.3    Lopez, B.J.4
  • 285
    • 0029161619 scopus 로고
    • Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine-262 in the presence of heparin (or tubulin)
    • Moreno F.J., Medina M., Pérez M., Montejo E., Avila J. Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine-262 in the presence of heparin (or tubulin). FEBS Lett. 372:1995;65-68.
    • (1995) FEBS Lett , vol.372 , pp. 65-68
    • Moreno, F.J.1    Medina, M.2    Pérez, M.3    Montejo, E.4    Avila, J.5
  • 286
    • 0025193506 scopus 로고
    • cdc2: In vivo veritas?
    • cdc2: in vivo veritas? Cell. 61:1990;549-551.
    • (1990) Cell , vol.61 , pp. 549-551
    • Moreno, S.1    Nurse, P.2
  • 287
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan D. Principles of CDK regulation. Nature. 9:1995;131-134.
    • (1995) Nature , vol.9 , pp. 131-134
    • Morgan, D.1
  • 288
    • 0030963509 scopus 로고    scopus 로고
    • Calcineurin in the adult rat hippocampus: Different distribution in CA1 and CA3 subfields
    • Morioka M., Nagahiro S., Fukunaga K., Miyamoto E., Ushio Y. Calcineurin in the adult rat hippocampus: Different distribution in CA1 and CA3 subfields. Neuroscience. 78:1997;673-684.
    • (1997) Neuroscience , vol.78 , pp. 673-684
    • Morioka, M.1    Nagahiro, S.2    Fukunaga, K.3    Miyamoto, E.4    Ushio, Y.5
  • 289
    • 0029943566 scopus 로고    scopus 로고
    • The pool of MAP kinase associated with microtubules is small but constitutively active
    • Morishima-Kawashima M., Kosik K.S. The pool of MAP kinase associated with microtubules is small but constitutively active. Mol. Biol. of the Cell. 7:1996;893-905.
    • (1996) Mol. Biol. of the Cell , vol.7 , pp. 893-905
    • Morishima-Kawashima, M.1    Kosik, K.S.2
  • 290
    • 0027533093 scopus 로고
    • Reversible loss of dendritic spines and altered excitability after chronic epilepsy in hippocampal slice cultures
    • Müller M., Gähwiler B., Rietschin L., Thompson S. Reversible loss of dendritic spines and altered excitability after chronic epilepsy in hippocampal slice cultures. Proc. Natl. Acad. Sci. U.S.A. 90:1993;257-261.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 257-261
    • Müller, M.1    Gähwiler, B.2    Rietschin, L.3    Thompson, S.4
  • 291
    • 0031567583 scopus 로고    scopus 로고
    • Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons
    • Muñoz-Montaño J.R., Moreno F.J., Avila J., Díaz-Nido J. Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons. FEBS Lett. 14:1997;183-188.
    • (1997) FEBS Lett , vol.14 , pp. 183-188
    • Muñoz-Montaño, J.R.1    Moreno, F.J.2    Avila, J.3    Díaz-Nido, J.4
  • 292
    • 0039169482 scopus 로고    scopus 로고
    • Downregulation of glycogen synthase kinase-3 beta (GSK-3 beta) protein expression during neuroblastoma IMR-32 cell differentiation
    • Muñoz-Montaño J.R., Moreno F.J., Avila J., Díaz-Nido J. Downregulation of glycogen synthase kinase-3 beta (GSK-3 beta) protein expression during neuroblastoma IMR-32 cell differentiation. J. Neurosci. Res. 55:1999;278-285.
    • (1999) J. Neurosci. Res , vol.55 , pp. 278-285
    • Muñoz-Montaño, J.R.1    Moreno, F.J.2    Avila, J.3    Díaz-Nido, J.4
  • 293
    • 0031036208 scopus 로고    scopus 로고
    • Morphological plasticity of dendritic spines in central neurons is mediated by activation of cAMP response element binding protein
    • Murphy D.D., Segal M. Morphological plasticity of dendritic spines in central neurons is mediated by activation of cAMP response element binding protein. Proc. Natl. Acad. Sci. U.S.A. 94:1997;1482-1487.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 1482-1487
    • Murphy, D.D.1    Segal, M.2
  • 294
    • 0020980162 scopus 로고
    • Microtubule assembly using the microtubule-associated protein MAP-2 prepared in defined states of phosphorylation with protein kinase and phosphatase
    • Murthy A.S., Flavin M. Microtubule assembly using the microtubule-associated protein MAP-2 prepared in defined states of phosphorylation with protein kinase and phosphatase. Eur. J. Biochem. 137:1983;37-46.
    • (1983) Eur. J. Biochem , vol.137 , pp. 37-46
    • Murthy, A.S.1    Flavin, M.2
  • 295
    • 0026875581 scopus 로고
    • The role of protein phosphatases in synaptic transmission, plasticity and neuronal development
    • Nairn A., Shenolikar S. The role of protein phosphatases in synaptic transmission, plasticity and neuronal development. Curr. Op. Neurobiology. 2:1992;296-301.
    • (1992) Curr. Op. Neurobiology , vol.2 , pp. 296-301
    • Nairn, A.1    Shenolikar, S.2
  • 296
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
    • Neve R.L., Harris P., Kosik K.S., Kurnit D.M., Donlon T.A. Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain Res. 387:1986;271-280.
    • (1986) Brain Res , vol.387 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 297
    • 0027186606 scopus 로고
    • Cellular substrates of p34cdc2 and its companion cyclin-dependent kinases
    • Nigg E. Cellular substrates of p34cdc2 and its companion cyclin-dependent kinases. TICB. 3:1993;296-301.
    • (1993) TICB , vol.3 , pp. 296-301
    • Nigg, E.1
  • 298
    • 0029966469 scopus 로고    scopus 로고
    • The cdk5/p35 kinase is essential for neurite outgrowth during neuronal differentiation
    • Nikolic M., Dudek H., Kwon Y., Ramos Y., Tsai L.-H. The cdk5/p35 kinase is essential for neurite outgrowth during neuronal differentiation. Genes and Development. 10:1996;816-825.
    • (1996) Genes and Development , vol.10 , pp. 816-825
    • Nikolic, M.1    Dudek, H.2    Kwon, Y.3    Ramos, Y.4    Tsai, L.-H.5
  • 299
    • 0027098178 scopus 로고
    • Mitogen-activated protein kinase and cytoskeleton in mitogenic signal transduction
    • Nishida E., Gotoh Y. Mitogen-activated protein kinase and cytoskeleton in mitogenic signal transduction. Int. Rev. Cytol. 138:1992;211-238.
    • (1992) Int. Rev. Cytol , vol.138 , pp. 211-238
    • Nishida, E.1    Gotoh, Y.2
  • 300
    • 0032478088 scopus 로고    scopus 로고
    • Chronic lithium treatment robustly protects neurons in the central nervous system against excitotoxicity by inhibiting N-methyl-D-aspartate receptor-mediated calcium influx
    • Nonaka S., Hough C.J., Chuang D.M. Chronic lithium treatment robustly protects neurons in the central nervous system against excitotoxicity by inhibiting N-methyl-D-aspartate receptor-mediated calcium influx. Proc. Natl. Acad. Sci. U.S.A. 95:1998;2642-2647.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 2642-2647
    • Nonaka, S.1    Hough, C.J.2    Chuang, D.M.3
  • 301
    • 0032487572 scopus 로고    scopus 로고
    • Ethanol induces MAP2 changes in organotypic hippocampal slice cultures
    • Noraberg J., Zimmer J. Ethanol induces MAP2 changes in organotypic hippocampal slice cultures. Neuroreport. 9:1998;3177-3182.
    • (1998) Neuroreport , vol.9 , pp. 3177-3182
    • Noraberg, J.1    Zimmer, J.2
  • 302
    • 0023680842 scopus 로고
    • Immature and mature variants of MAP2 and tau proteins and neuronal plasticity [news]
    • Nunez J. Immature and mature variants of MAP2 and tau proteins and neuronal plasticity [news]. Trends Neurosci. 11:1988;477-479.
    • (1988) Trends Neurosci , vol.11 , pp. 477-479
    • Nunez, J.1
  • 303
    • 0024761741 scopus 로고
    • The RII subunit of cAMP-dependent protein kinase binds to a common amino-terminal domain in microtubule-associated proteins 2A, 2B, and 2C
    • Obar R.A., Dingus J., Bayley H., Vallee R.B. The RII subunit of cAMP-dependent protein kinase binds to a common amino-terminal domain in microtubule-associated proteins 2A, 2B, and 2C. Neuron. 3:1989;639-645.
    • (1989) Neuron , vol.3 , pp. 639-645
    • Obar, R.A.1    Dingus, J.2    Bayley, H.3    Vallee, R.B.4
  • 304
    • 0031049236 scopus 로고    scopus 로고
    • Altered glutamatergic transmission in neurological disorders: From high extracellular glutamate to excessive synaptic efficacy
    • Obrenovitch T.P., Urenjak J. Altered glutamatergic transmission in neurological disorders: from high extracellular glutamate to excessive synaptic efficacy. Progress in Neurobiology. 51:1997;39-87.
    • (1997) Progress in Neurobiology , vol.51 , pp. 39-87
    • Obrenovitch, T.P.1    Urenjak, J.2
  • 305
    • 0024354716 scopus 로고
    • Rapid turnover of microtubule-associated protein MAP2 in the axon revealed by microinjection of biotinylated MAP2 into cultured neurons
    • Okabe S., Hirokawa N. Rapid turnover of microtubule-associated protein MAP2 in the axon revealed by microinjection of biotinylated MAP2 into cultured neurons. Proc. Natl. Acad. Sci. U.S.A. 86:1989;4127-4131.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 4127-4131
    • Okabe, S.1    Hirokawa, N.2
  • 306
    • 0028566654 scopus 로고
    • Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro
    • Olesen O.F. Expression of low molecular weight isoforms of microtubule-associated protein 2. Phosphorylation and induction of microtubule assembly in vitro. J. Biol. Chem. 269:1994;32904-32908.
    • (1994) J. Biol. Chem , vol.269 , pp. 32904-32908
    • Olesen, O.F.1
  • 307
    • 0022850973 scopus 로고
    • Microtubule-associated proteins
    • Olmsted J.B. Microtubule-associated proteins. Annu. Rev. Cell Biol. 2:1986;421-457.
    • (1986) Annu. Rev. Cell Biol , vol.2 , pp. 421-457
    • Olmsted, J.B.1
  • 308
    • 0028927505 scopus 로고
    • Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics
    • Ookata K., Hisanaga S., Bulinski J.C., Murofushi H., Aizawa H., Itoh T.J., Hotani H., Okumura E., Tachibana K., Kishimoto T. Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics. J. Cell Biol. 128:1995;849-862.
    • (1995) J. Cell Biol , vol.128 , pp. 849-862
    • Ookata, K.1    Hisanaga, S.2    Bulinski, J.C.3    Murofushi, H.4    Aizawa, H.5    Itoh, T.J.6    Hotani, H.7    Okumura, E.8    Tachibana, K.9    Kishimoto, T.10
  • 309
    • 0027239819 scopus 로고
    • Association of p34cdc2/cyclin B complex with microtubules in starfish oocytes
    • Ookata, K., Hisanaga S., Okumura E., Kishimoto, T, 1993. Association of p34cdc2/cyclin B complex with microtubules in starfish oocytes. J. Cell Sci. 105, 873-881.
    • (1993) J. Cell Sci. , vol.105 , pp. 873-881
    • Ookata, K.1    Hisanaga, S.2    Okumura, E.3    Kishimoto, T.4
  • 310
  • 311
    • 0242722234 scopus 로고    scopus 로고
    • Is the Ras-MAPK signalling pathway necessary for long-term memory formation?
    • Orban P., Chapman P., Brambilla R. Is the Ras-MAPK signalling pathway necessary for long-term memory formation? TINS. 22:1999;38-43.
    • (1999) TINS , vol.22 , pp. 38-43
    • Orban, P.1    Chapman, P.2    Brambilla, R.3
  • 312
    • 0028985603 scopus 로고
    • The a and g 1 isoforms of protein phosphatase 1 are highly and specifically concentrated in dendritic spines
    • Ouimet C., Da Cruz e Silva E., Greengard P. The a and g 1 isoforms of protein phosphatase 1 are highly and specifically concentrated in dendritic spines. Proc. Natl. Acad. Sci. U.S.A. 92:1995;3396-3400.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 3396-3400
    • Ouimet, C.1    Da Cruz, E.2    Silva, E.3    Greengard, P.4
  • 313
    • 0029948582 scopus 로고    scopus 로고
    • Organelle motility and metabolism in axons vs. dendrites of cultured hippocampal neurons
    • Overly C.C., Rieff H.I., Hollenbeck P.J. Organelle motility and metabolism in axons vs. dendrites of cultured hippocampal neurons. J. Cell Sci. 109:1996;971-980.
    • (1996) J. Cell Sci , vol.109 , pp. 971-980
    • Overly, C.C.1    Rieff, H.I.2    Hollenbeck, P.J.3
  • 314
    • 0032403434 scopus 로고    scopus 로고
    • Evidence for the participation of the neuron-specific CDK5 activator p35 during laminin-enhanced axonal growth
    • Paglini G., Pigino G., Kunda P., Morfini G., Maccioni R., Quiroga S., Ferreira A., Cácares A. Evidence for the participation of the neuron-specific CDK5 activator p35 during laminin-enhanced axonal growth. J. Neurosci. 18:1998;9858-9869.
    • (1998) J. Neurosci , vol.18 , pp. 9858-9869
    • Paglini, G.1    Pigino, G.2    Kunda, P.3    Morfini, G.4    Maccioni, R.5    Quiroga, S.6    Ferreira, A.7    Cácares, A.8
  • 315
    • 0028860053 scopus 로고
    • Morphological analysis of dendritic spine development in primary cultures of hippocampal neurons
    • Papa M., Bundman M., Greenberger V., Segal M. Morphological analysis of dendritic spine development in primary cultures of hippocampal neurons. J. Neurosci. 15:1995;1-11.
    • (1995) J. Neurosci , vol.15 , pp. 1-11
    • Papa, M.1    Bundman, M.2    Greenberger, V.3    Segal, M.4
  • 316
    • 0021958575 scopus 로고
    • Microtubule-associated protein 2 within axons of spinal motor neurons: Associations with microtubules and neurofilaments in normal and beta,beta′-iminodipropionitrile-treated axons
    • Papasozomenos S.C., Binder L.I., Bender P.K., Payne M.R. Microtubule-associated protein 2 within axons of spinal motor neurons: associations with microtubules and neurofilaments in normal and beta,beta′-iminodipropionitrile-treated axons. J. Cell Biol. 100:1985;74-85.
    • (1985) J. Cell Biol , vol.100 , pp. 74-85
    • Papasozomenos, S.C.1    Binder, L.I.2    Bender, P.K.3    Payne, M.R.4
  • 317
    • 0031853418 scopus 로고    scopus 로고
    • Age-related alteration of PKC, a key enzyme in memory processes - physiological and pathological examples
    • Pascale A., Govoni S., Battaini F. Age-related alteration of PKC, a key enzyme in memory processes - physiological and pathological examples. Mol. Neurobiol. 16:1998;49-62.
    • (1998) Mol. Neurobiol , vol.16 , pp. 49-62
    • Pascale, A.1    Govoni, S.2    Battaini, F.3
  • 318
    • 0033535545 scopus 로고    scopus 로고
    • The MAP location of GABA receptors
    • Passafaro M., Sheng M. The MAP location of GABA receptors. Curr. Biol. 9:1999;R261-R263.
    • (1999) Curr. Biol , vol.9
    • Passafaro, M.1    Sheng, M.2
  • 319
    • 0022979015 scopus 로고
    • A brain phosphatase with specificity for microtubule-associated protein-2
    • Patterson C.J., Flavin M. A brain phosphatase with specificity for microtubule-associated protein-2. J. Biol. Chem. 261:1986;7791-7796.
    • (1986) J. Biol. Chem , vol.261 , pp. 7791-7796
    • Patterson, C.J.1    Flavin, M.2
  • 320
    • 0028110888 scopus 로고
    • Interactions of microtubule-associated protein MAP2 with unpolymerized and polymerized tubulin and actin using a 96-well microtiter plate solid-phase immunoassay
    • Pedrotti B., Colombo R., Islam K. Interactions of microtubule-associated protein MAP2 with unpolymerized and polymerized tubulin and actin using a 96-well microtiter plate solid-phase immunoassay. Biochemistry. 33:1994;8798-8806.
    • (1994) Biochemistry , vol.33 , pp. 8798-8806
    • Pedrotti, B.1    Colombo, R.2    Islam, K.3
  • 321
    • 0031051127 scopus 로고    scopus 로고
    • Estramustine phosphate but not estramustine inhibits the interaction of microtubule associated protein 2 (MAP2) with actin filaments
    • Pedrotti B., Islam K. Estramustine phosphate but not estramustine inhibits the interaction of microtubule associated protein 2 (MAP2) with actin filaments. FEBS Lett. 403:1997;123-126.
    • (1997) FEBS Lett , vol.403 , pp. 123-126
    • Pedrotti, B.1    Islam, K.2
  • 322
    • 0032536435 scopus 로고    scopus 로고
    • Changes in mRNA abundance of microtubule-associated proteins in the rat brain following electroconvulsive shock
    • Pei Q., Burnet P.J.W., Zetterstrom T.S.C. Changes in mRNA abundance of microtubule-associated proteins in the rat brain following electroconvulsive shock. Neuroreport. 9:1998;391-394.
    • (1998) Neuroreport , vol.9 , pp. 391-394
    • Pei, Q.1    Burnet, P.J.W.2    Zetterstrom, T.S.C.3
  • 323
    • 0024418709 scopus 로고
    • CAMP-dependent phosphorylation of soluble and crude microtubule fractions of rat cerebral cortex after prolonged desmethylimipramine treatment
    • Perez J., Tinelli D., Brunello N., Racagni G. cAMP-dependent phosphorylation of soluble and crude microtubule fractions of rat cerebral cortex after prolonged desmethylimipramine treatment. Eur. J. Pharmacol. 172:1989;305-316.
    • (1989) Eur. J. Pharmacol , vol.172 , pp. 305-316
    • Perez, J.1    Tinelli, D.2    Brunello, N.3    Racagni, G.4
  • 324
    • 0031439984 scopus 로고    scopus 로고
    • Experience-dependent modifications in MAP2 phosphorylation in rat olfactory bulb
    • Philpot B.D., Lim J.H., Halpain S., Brunjes P.C. Experience-dependent modifications in MAP2 phosphorylation in rat olfactory bulb. J. Neurosci. 17:1997;9596-9604.
    • (1997) J. Neurosci , vol.17 , pp. 9596-9604
    • Philpot, B.D.1    Lim, J.H.2    Halpain, S.3    Brunjes, P.C.4
  • 325
    • 0031039081 scopus 로고    scopus 로고
    • Analysis of the expression, distribution and function of cyclin dependent kinase 5 (cdk5) in developing cerebellar macroneurons
    • Pigino G., Paglini G., Ulloa L., Avila J., Cáceres A. Analysis of the expression, distribution and function of cyclin dependent kinase 5 (cdk5) in developing cerebellar macroneurons. J. Cell Sci. 110:1997;257-270.
    • (1997) J. Cell Sci , vol.110 , pp. 257-270
    • Pigino, G.1    Paglini, G.2    Ulloa, L.3    Avila, J.4    Cáceres, A.5
  • 327
    • 0028120469 scopus 로고
    • Correlation between reactive sprouting and microtubule protein expression in epileptic hippocampus [published erratum appears in Neuroscience 1994 Nov;63(2):627]
    • Pollard H., Khrestchatisky M., Moreau J., Ben A.Y., Represa A. Correlation between reactive sprouting and microtubule protein expression in epileptic hippocampus [published erratum appears in Neuroscience 1994 Nov;63(2):627]. Neuroscience. 61:1994;773-787.
    • (1994) Neuroscience , vol.61 , pp. 773-787
    • Pollard, H.1    Khrestchatisky, M.2    Moreau, J.3    Ben, A.Y.4    Represa, A.5
  • 328
    • 0030913980 scopus 로고    scopus 로고
    • The 'jaws' model of tau-microtubule interaction examined in CHO cells
    • Preuss U., Biernat J., Mandelkow E.M., Mandelkow E. The 'jaws' model of tau-microtubule interaction examined in CHO cells. J. Cell. Sci. 110:1997;789-800.
    • (1997) J. Cell. Sci , vol.110 , pp. 789-800
    • Preuss, U.1    Biernat, J.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 329
    • 0033153258 scopus 로고    scopus 로고
    • Brain protein serine/threonine phosphatases
    • Price N., Mumby M. Brain protein serine/threonine phosphatases. Curr. Op. Neurobiol. 9:1999;336-342.
    • (1999) Curr. Op. Neurobiol , vol.9 , pp. 336-342
    • Price, N.1    Mumby, M.2
  • 330
    • 0028847151 scopus 로고
    • Neuronal polarity: Giving neurons heads and tails
    • Prochiantz A. Neuronal polarity: giving neurons heads and tails. Neuron. 15:1995;743-746.
    • (1995) Neuron , vol.15 , pp. 743-746
    • Prochiantz, A.1
  • 331
    • 0027048607 scopus 로고
    • Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro. Real-time observations using video microscopy
    • Pryer, N.K., Walker, R.A., Skeen, V.P., Bourns, B.D., Soboeiro, M.F., Salmon, E.D., 1992. Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro. Real-time observations using video microscopy. J. Cell Sci. 103, 965-976.
    • (1992) J. Cell Sci. , vol.103 , pp. 965-976
    • Pryer, N.K.1    Walker, R.A.2    Skeen, V.P.3    Bourns, B.D.4    Soboeiro, M.F.5    Salmon, E.D.6
  • 332
    • 0028829054 scopus 로고
    • Developmental regulation of MAP2 variants during neuronal differentiation in vitro
    • Przyborski S.A., Cambray-Deakin M.A. Developmental regulation of MAP2 variants during neuronal differentiation in vitro. Dev. Brain Res. 89:1995;187-201.
    • (1995) Dev. Brain Res , vol.89 , pp. 187-201
    • Przyborski, S.A.1    Cambray-Deakin, M.A.2
  • 333
    • 0032569937 scopus 로고    scopus 로고
    • Long-term alcohol self-administration and alcohol withdrawal differentially modulate microtubule-associated protein 2 (MAP2) gene expression in the rat brain
    • Putzke J., DeBeun R., Schreiber R., DeVry J., Tolle T.R., Zieglgansberger W., Spanagel R. Long-term alcohol self-administration and alcohol withdrawal differentially modulate microtubule-associated protein 2 (MAP2) gene expression in the rat brain. Mol. Brain Res. 62:1998;196-205.
    • (1998) Mol. Brain Res , vol.62 , pp. 196-205
    • Putzke, J.1    Debeun, R.2    Schreiber, R.3    Devry, J.4    Tolle, T.R.5    Zieglgansberger, W.6    Spanagel, R.7
  • 334
    • 0029909492 scopus 로고    scopus 로고
    • Emergence of activity-dependent, bidirectional control of microtubule-associated protein MAP2 phosphorylation during postnatal development
    • Quinlan E., Halpain S. Emergence of activity-dependent, bidirectional control of microtubule-associated protein MAP2 phosphorylation during postnatal development. J. Neurosci. 16:1996;7627-7637.
    • (1996) J. Neurosci , vol.16 , pp. 7627-7637
    • Quinlan, E.1    Halpain, S.2
  • 335
    • 0030069916 scopus 로고    scopus 로고
    • Postsynaptic mechanisms for bidirectional control of MAP2 phosphorylation by glutamate receptors
    • Quinlan E., Halpain S. Postsynaptic mechanisms for bidirectional control of MAP2 phosphorylation by glutamate receptors. Neuron. 16:1996;357-368.
    • (1996) Neuron , vol.16 , pp. 357-368
    • Quinlan, E.1    Halpain, S.2
  • 336
    • 0031943325 scopus 로고    scopus 로고
    • Schizophrenia as a developmental disorder of the cerebral cortex
    • Raedler T.J., Knable M.B., Weinberger D.R. Schizophrenia as a developmental disorder of the cerebral cortex. Curr. Opin. Neurobiol. 8:1998;157-161.
    • (1998) Curr. Opin. Neurobiol , vol.8 , pp. 157-161
    • Raedler, T.J.1    Knable, M.B.2    Weinberger, D.R.3
  • 337
    • 0026500112 scopus 로고
    • Microtubule-associated protein autophosphorylation alters in vitro microtubule dynamic instability
    • Raffaelli N., Yamauchi P.S., Purich D.L. Microtubule-associated protein autophosphorylation alters in vitro microtubule dynamic instability. FEBS Lett. 296:1992;21-24.
    • (1992) FEBS Lett , vol.296 , pp. 21-24
    • Raffaelli, N.1    Yamauchi, P.S.2    Purich, D.L.3
  • 338
    • 0029097251 scopus 로고
    • Time course of protein changes following in vitro ischemia in the rat hippocampal slice
    • Raley-Susman K., Murata K. Time course of protein changes following in vitro ischemia in the rat hippocampal slice. Rrain Res. 694:1995;94-102.
    • (1995) Rrain Res , vol.694 , pp. 94-102
    • Raley-Susman, K.1    Murata, K.2
  • 339
    • 0031055682 scopus 로고    scopus 로고
    • Differential expression of microtubule-associated protein 1B phosphorylated isoforms in the adult rat nervous system
    • Ramón-Cueto A., Avila J. Differential expression of microtubule-associated protein 1B phosphorylated isoforms in the adult rat nervous system. Neurosci. 77:1997;485-501.
    • (1997) Neurosci , vol.77 , pp. 485-501
    • Ramón-Cueto, A.1    Avila, J.2
  • 340
    • 0005261734 scopus 로고
    • Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro
    • Ray L.B., Sturgill T.W. Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro. Proc. Natl. Acad. Sci. U.S.A. 84:1987;1502-1506.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 1502-1506
    • Ray, L.B.1    Sturgill, T.W.2
  • 341
    • 0024245612 scopus 로고
    • Characterization of insulin-stimulated microtubule-associated protein kinase. Rapid isolation and stabilization of a novel serine/threonine kinase from 3T3-L1 cells
    • Ray L.B., Sturgill T.W. Characterization of insulin-stimulated microtubule-associated protein kinase. Rapid isolation and stabilization of a novel serine/threonine kinase from 3T3-L1 cells. J. Biol. Chem. 263:1988;12721-12727.
    • (1988) J. Biol. Chem , vol.263 , pp. 12721-12727
    • Ray, L.B.1    Sturgill, T.W.2
  • 342
    • 0029117155 scopus 로고
    • Dark-rearing changes dendritic microtubule-associated protein 2 (MAP2) but not subplate neurons in cat visual cortex
    • Reid S.N., Daw N.W. Dark-rearing changes dendritic microtubule-associated protein 2 (MAP2) but not subplate neurons in cat visual cortex. J. Comp. Neurol. 359:1995;38-47.
    • (1995) J. Comp. Neurol , vol.359 , pp. 38-47
    • Reid, S.N.1    Daw, N.W.2
  • 343
    • 0030855766 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase/extracellular signal-regulated kinase 2 regulates cytoskeletal organization and chemotaxis via catalytic and microtubule-specific interactions
    • Reszka A.A., Bulinski J.C., Krebs E.G., Fischer E.H. Mitogen-activated protein kinase/extracellular signal-regulated kinase 2 regulates cytoskeletal organization and chemotaxis via catalytic and microtubule-specific interactions. Mol. Biol. Cell. 8:1997;1219-1232.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1219-1232
    • Reszka, A.A.1    Bulinski, J.C.2    Krebs, E.G.3    Fischer, E.H.4
  • 345
    • 0032567777 scopus 로고    scopus 로고
    • NMDA receptor activation during status epilepticus is required for the development of epilepsy
    • Rice A.C., DeLorenzo R.J. NMDA receptor activation during status epilepticus is required for the development of epilepsy. Brain Res. 782:1998;240-247.
    • (1998) Brain Res , vol.782 , pp. 240-247
    • Rice, A.C.1    Delorenzo, R.J.2
  • 346
    • 0030005401 scopus 로고    scopus 로고
    • Function of metabotropic glutamate receptors in learning and memory
    • Riedel G. Function of metabotropic glutamate receptors in learning and memory. TINS. 6:1996;219-224.
    • (1996) TINS , vol.6 , pp. 219-224
    • Riedel, G.1
  • 347
    • 0000146080 scopus 로고
    • Differential expression of distinct microtubule-associated proteins during brain development
    • Riederer B., Matus A. Differential expression of distinct microtubule-associated proteins during brain development. Proc. Natl. Acad. Sci. U.S.A. 82:1985;6006-6009.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 6006-6009
    • Riederer, B.1    Matus, A.2
  • 348
    • 0026447621 scopus 로고
    • Differential phosphorylation of some proteins of the neuronal cytoskeleton during brain development
    • Riederer B.M. Differential phosphorylation of some proteins of the neuronal cytoskeleton during brain development. Histochem. J. 24:1992;783-790.
    • (1992) Histochem. J , vol.24 , pp. 783-790
    • Riederer, B.M.1
  • 350
    • 0031930469 scopus 로고    scopus 로고
    • Disruption by lithium of phosphoinositide signalling in cerebellar granule cells in primary culture
    • Rio del E., Shinomura T., van der Kaay J., Nicholls D.G., Downes C.P. Disruption by lithium of phosphoinositide signalling in cerebellar granule cells in primary culture. J. Neurochem. 70:1998;1662-1669.
    • (1998) J. Neurochem , vol.70 , pp. 1662-1669
    • Rio Del, E.1    Shinomura, T.2    Van Der Kaay, J.3    Nicholls, D.G.4    Downes, C.P.5
  • 351
    • 0031579432 scopus 로고    scopus 로고
    • Co-expression of MAP-2 and GFAP in cells developing from rat ECF responsive precursor cells
    • Rosser A.E., Tyers P., terBorg M., Dunnett S.B., Svendsen C.N. Co-expression of MAP-2 and GFAP in cells developing from rat ECF responsive precursor cells. Dev. Brain Res. 98:1997;291-295.
    • (1997) Dev. Brain Res , vol.98 , pp. 291-295
    • Rosser, A.E.1    Tyers, P.2    Terborg, M.3    Dunnett, S.B.4    Svendsen, C.N.5
  • 352
    • 0033168992 scopus 로고    scopus 로고
    • Cytoskeletal dynamics in dendritic spines: Direct modulation by glutamate receptors?
    • Rossum v.D., Hanisch U.-K. Cytoskeletal dynamics in dendritic spines: direct modulation by glutamate receptors? Trends Neursoci. 22:1999;290-295.
    • (1999) Trends Neursoci , vol.22 , pp. 290-295
    • Rossum, V.D.1    Hanisch, U.-K.2
  • 353
    • 0033011462 scopus 로고    scopus 로고
    • Dynamic interaction between soluble tubulin and C-terminal domains of N-methyl-D-aspartate receptor subunits
    • Rossum v.D., Kuhse J., Betz H. Dynamic interaction between soluble tubulin and C-terminal domains of N-methyl-D-aspartate receptor subunits. J. Neurochem. 72:1999;962-973.
    • (1999) J. Neurochem , vol.72 , pp. 962-973
    • Rossum, V.D.1    Kuhse, J.2    Betz, H.3
  • 354
    • 0024763898 scopus 로고
    • Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2
    • Rubino H.M., Dammerman M., Shafit Z.B., Erlichman J. Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2. Neuron. 3:1989;631-638.
    • (1989) Neuron , vol.3 , pp. 631-638
    • Rubino, H.M.1    Dammerman, M.2    Shafit, Z.B.3    Erlichman, J.4
  • 355
    • 0030969931 scopus 로고    scopus 로고
    • Glutamate receptors are selectively targeted to postsynaptic sites in neurons
    • Rubio M.E., Wenthold R.J. Glutamate receptors are selectively targeted to postsynaptic sites in neurons. Neuron. 18:1997;939-950.
    • (1997) Neuron , vol.18 , pp. 939-950
    • Rubio, M.E.1    Wenthold, R.J.2
  • 356
    • 0024824485 scopus 로고
    • Regulation of microtubule-associated protein 2 (MAP2) mRNA expression during rat brain development
    • Safaei R., Fischer I. Regulation of microtubule-associated protein 2 (MAP2) mRNA expression during rat brain development. J. Mol. Neurosci. 1:1989;189-198.
    • (1989) J. Mol. Neurosci , vol.1 , pp. 189-198
    • Safaei, R.1    Fischer, I.2
  • 357
    • 0028836147 scopus 로고
    • Reexpression of developmentally regulated MAP2c mRNA after ischemia: Colocalization with hsp72 mRNA in vulnerable neurons
    • Saito N., Kawai K., Nowak T.J. Reexpression of developmentally regulated MAP2c mRNA after ischemia: colocalization with hsp72 mRNA in vulnerable neurons. J. Cereb. Blood Flow Metab. 15:1995;205-215.
    • (1995) J. Cereb. Blood Flow Metab , vol.15 , pp. 205-215
    • Saito, N.1    Kawai, K.2    Nowak, T.J.3
  • 359
    • 0028912050 scopus 로고
    • Variations in in vivo phosphorylation at the proline-rich domain of the microtubule-associated protein 2 (MAP2) during rat brain development
    • Sánchez C., Díaz-Nido J., Avila J. Variations in in vivo phosphorylation at the proline-rich domain of the microtubule-associated protein 2 (MAP2) during rat brain development. Biochem. J. 306:1995;481-487.
    • (1995) Biochem. J , vol.306 , pp. 481-487
    • Sánchez, C.1    Díaz-Nido, J.2    Avila, J.3
  • 360
    • 0032544119 scopus 로고    scopus 로고
    • Regulation of a site-specific phosphorylation of the microtubule-associated protein 2 (MAP2) during the development of cultured neurons
    • Sánchez C., Díaz-Nido J., Avila J. Regulation of a site-specific phosphorylation of the microtubule-associated protein 2 (MAP2) during the development of cultured neurons. Neuroscience. 87:1998;861-870.
    • (1998) Neuroscience , vol.87 , pp. 861-870
    • Sánchez, C.1    Díaz-Nido, J.2    Avila, J.3
  • 361
    • 0029987421 scopus 로고    scopus 로고
    • Phosphorylation and dephosphorylation in the proline-rich C-terminal domain of microtubule-associated protein 2
    • Sánchez C., Tompa P., Szucs K., Friedrich P., Avila J. Phosphorylation and dephosphorylation in the proline-rich C-terminal domain of microtubule-associated protein 2. Eur. J. Biochem. 241:1996;765-771.
    • (1996) Eur. J. Biochem , vol.241 , pp. 765-771
    • Sánchez, C.1    Tompa, P.2    Szucs, K.3    Friedrich, P.4    Avila, J.5
  • 362
    • 0342710347 scopus 로고    scopus 로고
    • NMDA-glutamate receptors regulate phosphorylation of dendritic cytoskeletal proteins in the hippocampus
    • Sánchez C., Ulloa L., Montoro R., López-Barneo J., Avila J. NMDA-glutamate receptors regulate phosphorylation of dendritic cytoskeletal proteins in the hippocampus. Brain Res. 765:1997;141-148.
    • (1997) Brain Res , vol.765 , pp. 141-148
    • Sánchez, C.1    Ulloa, L.2    Montoro, R.3    López-Barneo, J.4    Avila, J.5
  • 363
    • 0026706777 scopus 로고
    • Chromatographic resolution and characterization of a nerve growth factor-dependent kinase that phosphorylates microtubule-associated proteins 1 and 2 in PC12 cells
    • Sano M. Chromatographic resolution and characterization of a nerve growth factor-dependent kinase that phosphorylates microtubule-associated proteins 1 and 2 in PC12 cells. J. Neurochem. 59:1992;1263-1272.
    • (1992) J. Neurochem , vol.59 , pp. 1263-1272
    • Sano, M.1
  • 364
    • 0028887946 scopus 로고
    • Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins
    • Saoudi Y., Paintrand I., Multigner L., Job D. Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins. J. Cell Sci. 108:1995;357-367.
    • (1995) J. Cell Sci , vol.108 , pp. 357-367
    • Saoudi, Y.1    Paintrand, I.2    Multigner, L.3    Job, D.4
  • 365
    • 0026567861 scopus 로고
    • Microtubule protein ADP-ribosylation in vitro leads to assembly inhibition and rapid depolymerization
    • Scaife R.M., Wilson L., Purich D.L. Microtubule protein ADP-ribosylation in vitro leads to assembly inhibition and rapid depolymerization. Biochem. 31:1992;310-316.
    • (1992) Biochem , vol.31 , pp. 310-316
    • Scaife, R.M.1    Wilson, L.2    Purich, D.L.3
  • 366
    • 0028355245 scopus 로고
    • Cytochemical polarity in lateral geniculate interneurons
    • Scheetz A.J., Dubin M.W. Cytochemical polarity in lateral geniculate interneurons. Brain Res. 639:1994;181-192.
    • (1994) Brain Res , vol.639 , pp. 181-192
    • Scheetz, A.J.1    Dubin, M.W.2
  • 367
    • 0019889058 scopus 로고
    • Taxol assembles tubulin in the absence of exogenous guanosine 5′- triphosphate or microtubule-associated proteins
    • Schiff P.B., Horwitz S.B. Taxol assembles tubulin in the absence of exogenous guanosine 5′- triphosphate or microtubule-associated proteins. Biochemistry. 20:1981;3247-3252.
    • (1981) Biochemistry , vol.20 , pp. 3247-3252
    • Schiff, P.B.1    Horwitz, S.B.2
  • 368
    • 0032506657 scopus 로고    scopus 로고
    • Pixel-based image analysis of HSP70, GADD45 and MAP2 mRNA expression after focal cerebral ischemia: Hemodynamic and histological correlates
    • Schmidt-Kastner R., Zhao W., Truettner J., Belayev L., Busto R., Ginsberg M.D. Pixel-based image analysis of HSP70, GADD45 and MAP2 mRNA expression after focal cerebral ischemia: hemodynamic and histological correlates. Mol. Brain Res. 63:1998;79-97.
    • (1998) Mol. Brain Res , vol.63 , pp. 79-97
    • Schmidt-Kastner, R.1    Zhao, W.2    Truettner, J.3    Belayev, L.4    Busto, R.5    Ginsberg, M.D.6
  • 370
    • 0027936669 scopus 로고
    • Diverse distribution and function of fibrous microtubule-associated proteins in the nervous system
    • Schoenfeld T.A., Obar R.A. Diverse distribution and function of fibrous microtubule-associated proteins in the nervous system. Int. Rev. Cytol. 151:1994;67-137.
    • (1994) Int. Rev. Cytol , vol.151 , pp. 67-137
    • Schoenfeld, T.A.1    Obar, R.A.2
  • 371
    • 0021277059 scopus 로고
    • 2+/calmodulin-dependent protein kinase
    • 2+/calmodulin-dependent protein kinase. J. Cell Biol. 99:1984;11-19.
    • (1984) J. Cell Biol , vol.99 , pp. 11-19
    • Schulman, H.1
  • 372
    • 0026168058 scopus 로고
    • Serine/threonine kinases in the nervous system
    • Schulman H. Serine/threonine kinases in the nervous system. Curr. Op. Neurobiol. 1:1991;43-52.
    • (1991) Curr. Op. Neurobiol , vol.1 , pp. 43-52
    • Schulman, H.1
  • 373
    • 0027340098 scopus 로고
    • 2+/calmodulin-dependent protein kinase
    • 2+/calmodulin-dependent protein kinase. Neurochem. Res. 18:1993;65-77.
    • (1993) Neurochem. Res , vol.18 , pp. 65-77
    • Schulman, H.1    Hanson, P.2
  • 374
    • 0022272881 scopus 로고
    • 2+/calmodulin-dependent microtubule-associated protein 2 kinase: Broad substrate specificity and multifunctional potential in diverse tissues
    • 2+/calmodulin-dependent microtubule-associated protein 2 kinase: broad substrate specificity and multifunctional potential in diverse tissues. Biochemistry. 24:1985;5320-5327.
    • (1985) Biochemistry , vol.24 , pp. 5320-5327
    • Schulman, H.1    Kuret, J.2    Jefferson, A.B.3    Nose, P.S.4    Spitzer, K.H.5
  • 375
    • 0032554636 scopus 로고    scopus 로고
    • Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin 1 substrate recognition
    • Schutkowski M., Bernhardt A., Zhou X.Z., Shen M., Reimer U., Rahfeld J.U., Lu K.P., Fischer G. Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin 1 substrate recognition. Biochemistry. 37:1998;5566-5575.
    • (1998) Biochemistry , vol.37 , pp. 5566-5575
    • Schutkowski, M.1    Bernhardt, A.2    Zhou, X.Z.3    Shen, M.4    Reimer, U.5    Rahfeld, J.U.6    Lu, K.P.7    Fischer, G.8
  • 376
    • 0028999215 scopus 로고
    • Morphological alterations in dendritic spines of rat hippocampal neurons exposed to N-methyl-D-aspartate
    • Segal M. Morphological alterations in dendritic spines of rat hippocampal neurons exposed to N-methyl-D-aspartate. Neurosci. Lett. 193:1995;73-76.
    • (1995) Neurosci. Lett , vol.193 , pp. 73-76
    • Segal, M.1
  • 377
    • 0020607502 scopus 로고
    • Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments
    • Selden S.C., Pollard T.D. Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments. J. Biol. Chem. 258:1983;7064-7071.
    • (1983) J. Biol. Chem , vol.258 , pp. 7064-7071
    • Selden, S.C.1    Pollard, T.D.2
  • 378
    • 0021135071 scopus 로고
    • Controlled proteolysis of tubulin by subtilisin: Localization of the site for MAP2 interaction
    • Serrano L., Avila J., Maccioni R.B. Controlled proteolysis of tubulin by subtilisin: localization of the site for MAP2 interaction. Biochemistry. 23:1984;4675-4681.
    • (1984) Biochemistry , vol.23 , pp. 4675-4681
    • Serrano, L.1    Avila, J.2    Maccioni, R.B.3
  • 380
    • 0031853417 scopus 로고    scopus 로고
    • Making sense of the multiple MAP-2 transcripts and their role in the neuron
    • Shafit-Zagardo B., Kalcheva N. Making sense of the multiple MAP-2 transcripts and their role in the neuron. Mol. Neurobiol. 16:1998;149-162.
    • (1998) Mol. Neurobiol , vol.16 , pp. 149-162
    • Shafit-Zagardo, B.1    Kalcheva, N.2
  • 381
    • 0031030967 scopus 로고    scopus 로고
    • Distribution and subcellular localization of high-molecular-weight microtubule-associated protein-2 expressing exon 8 in brain and spinal cord
    • Shafit-Zagardo B., Kalcheva N., Dickson D., Davies P., Kress Y. Distribution and subcellular localization of high-molecular-weight microtubule-associated protein-2 expressing exon 8 in brain and spinal cord. J. Neurochem. 68:1997;862-873.
    • (1997) J. Neurochem , vol.68 , pp. 862-873
    • Shafit-Zagardo, B.1    Kalcheva, N.2    Dickson, D.3    Davies, P.4    Kress, Y.5
  • 382
    • 0028215972 scopus 로고
    • Antisense MAP-2 oligonucleotides induce changes in microtubule assembly and neuritic elongation in pre-existing neurites of rat cortical neurons
    • Sharma N., Kress Y., Shafit Z.B. Antisense MAP-2 oligonucleotides induce changes in microtubule assembly and neuritic elongation in pre-existing neurites of rat cortical neurons. Cell Motil. Cytoskeleton. 27:1994;234-247.
    • (1994) Cell Motil. Cytoskeleton , vol.27 , pp. 234-247
    • Sharma, N.1    Kress, Y.2    Shafit, Z.B.3
  • 383
    • 0007675625 scopus 로고    scopus 로고
    • Expression of a minus-end-directed motor protein induces Sf9 cells to form axon-like processes with uniform microtubule polarity orientation
    • Sharp D.J., Kuriyama R., Essner R., Baas P.W. Expression of a minus-end-directed motor protein induces Sf9 cells to form axon-like processes with uniform microtubule polarity orientation. Journal of Cell Science. 110:1997;2373-2380.
    • (1997) Journal of Cell Science , vol.110 , pp. 2373-2380
    • Sharp, D.J.1    Kuriyama, R.2    Essner, R.3    Baas, P.W.4
  • 384
    • 0030857398 scopus 로고    scopus 로고
    • Identification of a microtubule-associated motor protein essential for dendritic differentiation
    • Sharp D.J., Yu W.Q., Ferhat L., Kuriyama R., Rueger D.C., Baas P.W. Identification of a microtubule-associated motor protein essential for dendritic differentiation. Journal of Cell Biology. 138:1997;833-843.
    • (1997) Journal of Cell Biology , vol.138 , pp. 833-843
    • Sharp, D.J.1    Yu, W.Q.2    Ferhat, L.3    Kuriyama, R.4    Rueger, D.C.5    Baas, P.W.6
  • 386
    • 0032144774 scopus 로고    scopus 로고
    • Mechanisms of trafficking in axons and dendrites: Implications for development and neurodegeneration
    • Sheetz M.P., Pfister K.K., Bulinski J.C., Cotman C.W. Mechanisms of trafficking in axons and dendrites: Implications for development and neurodegeneration. Prog. Neurobiol. 55:1998;577-594.
    • (1998) Prog. Neurobiol , vol.55 , pp. 577-594
    • Sheetz, M.P.1    Pfister, K.K.2    Bulinski, J.C.3    Cotman, C.W.4
  • 387
    • 0029737896 scopus 로고    scopus 로고
    • Stimulation of microtubule dynamic turnover in living cells treated with okadaic acid
    • Shelden E., Wadsworth P. Stimulation of microtubule dynamic turnover in living cells treated with okadaic acid. Cell Motility and the Cytoskeleton. 35:1996;24-34.
    • (1996) Cell Motility and the Cytoskeleton , vol.35 , pp. 24-34
    • Shelden, E.1    Wadsworth, P.2
  • 388
    • 0032031634 scopus 로고    scopus 로고
    • The essential mitotic peptidyl-prolyl isomerase Pin 1 binds and regulates mitosis-specific phosphoproteins
    • Shen M., Stukenbag P., Kirschner M., Lu K. The essential mitotic peptidyl-prolyl isomerase Pin 1 binds and regulates mitosis-specific phosphoproteins. Genes and Dev. 12:1998;706-720.
    • (1998) Genes and Dev , vol.12 , pp. 706-720
    • Shen, M.1    Stukenbag, P.2    Kirschner, M.3    Lu, K.4
  • 389
    • 0024324790 scopus 로고
    • Phosphorylation of microtubule-associated protein 2 by MAP kinase primarily involves the projection domain
    • Silliman C.C., Sturgill T.W. Phosphorylation of microtubule-associated protein 2 by MAP kinase primarily involves the projection domain. Biochem. Biophys. Res. Commun. 160:1989;993-998.
    • (1989) Biochem. Biophys. Res. Commun , vol.160 , pp. 993-998
    • Silliman, C.C.1    Sturgill, T.W.2
  • 390
    • 0026276683 scopus 로고
    • The regulation and function of protein phosphatases in the brain
    • Sim A. The regulation and function of protein phosphatases in the brain. Mol. Neurobiol. 5:1992;229-246.
    • (1992) Mol. Neurobiol , vol.5 , pp. 229-246
    • Sim, A.1
  • 391
    • 0342752607 scopus 로고
    • Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein
    • Sloboda R., Rudolph S., Rosenbaum J., Greengard P. Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein. Proc. Natl. Acad. Sci. U.S.A. 72:1975;177-181.
    • (1975) Proc. Natl. Acad. Sci. U.S.A , vol.72 , pp. 177-181
    • Sloboda, R.1    Rudolph, S.2    Rosenbaum, J.3    Greengard, P.4
  • 393
    • 0026942005 scopus 로고
    • Neuronal cytoskeleton and growth
    • Solomon F. Neuronal cytoskeleton and growth. Curr. Op. Neurobiol. 2:1992;613-617.
    • (1992) Curr. Op. Neurobiol , vol.2 , pp. 613-617
    • Solomon, F.1
  • 394
    • 0028924295 scopus 로고
    • A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
    • Sontag E., Nunbhakdi C.V., Bloom G.S., Mumby M.C. A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J. Cell Biol. 128:1995;1131-1144.
    • (1995) J. Cell Biol , vol.128 , pp. 1131-1144
    • Sontag, E.1    Nunbhakdi, C.V.2    Bloom, G.S.3    Mumby, M.C.4
  • 395
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H., Ishiura S., Suzuki K. Structure and physiological function of calpains. Biochem. J. 328:1997;721-732.
    • (1997) Biochem. J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 396
    • 0030930824 scopus 로고    scopus 로고
    • Rapid calpain I activation and cytoskeletal protein degradation following traumatic spinal cord injury: Attenuation with riluzole pretreatment
    • Springer J., Azbill R., Kennedy S., George J., Geddes J. Rapid calpain I activation and cytoskeletal protein degradation following traumatic spinal cord injury: attenuation with riluzole pretreatment. J. Neurochem. 69:1997;1592-1600.
    • (1997) J. Neurochem , vol.69 , pp. 1592-1600
    • Springer, J.1    Azbill, R.2    Kennedy, S.3    George, J.4    Geddes, J.5
  • 397
    • 0030449964 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 activity and mimics Wingless signalling in intact cells
    • Stambolic V., Ruel L., Woodgett J. Lithium inhibits glycogen synthase kinase-3 activity and mimics Wingless signalling in intact cells. Curr. Biol. 6:1996;1664-1668.
    • (1996) Curr. Biol , vol.6 , pp. 1664-1668
    • Stambolic, V.1    Ruel, L.2    Woodgett, J.3
  • 398
    • 0028949725 scopus 로고
    • Targeting of mRNAs to subsynaptic microdomains in dendrites
    • Steward O. Targeting of mRNAs to subsynaptic microdomains in dendrites. Curr. Opin. Neurobiol. 5:1995;55-61.
    • (1995) Curr. Opin. Neurobiol , vol.5 , pp. 55-61
    • Steward, O.1
  • 399
    • 0028893377 scopus 로고
    • MRNA distribution within dendrites: Relationship to afferent innervation
    • Steward O., Wallace C.S. mRNA distribution within dendrites: relationship to afferent innervation. J. Neurobiol. 26:1995;447-449.
    • (1995) J. Neurobiol , vol.26 , pp. 447-449
    • Steward, O.1    Wallace, C.S.2
  • 400
    • 0026715791 scopus 로고
    • Phosphatidylinositol inhibits microtubule assembly by binding to microtubule-associated protein 2 at a single, specific, high-affinity site
    • Surridge C.D., Burns R.G. Phosphatidylinositol inhibits microtubule assembly by binding to microtubule-associated protein 2 at a single, specific, high-affinity site. Biochemistry. 31:1992;6140-6144.
    • (1992) Biochemistry , vol.31 , pp. 6140-6144
    • Surridge, C.D.1    Burns, R.G.2
  • 401
    • 0028233811 scopus 로고
    • The difference in the binding of phosphatidylinositol distinguishes MAP2 from MAP2C and Tau
    • Surridge C.D., Burns R.G. The difference in the binding of phosphatidylinositol distinguishes MAP2 from MAP2C and Tau. Biochemistry. 33:1994;8051-8057.
    • (1994) Biochemistry , vol.33 , pp. 8051-8057
    • Surridge, C.D.1    Burns, R.G.2
  • 402
    • 0031967521 scopus 로고    scopus 로고
    • An emerging link between cytoskeletal dynamics and cell adhesion molecules in growth cone guidance
    • Suter D.M., Forscher P. An emerging link between cytoskeletal dynamics and cell adhesion molecules in growth cone guidance. Curr. Opin. Neurobiol. 8:1998;106-116.
    • (1998) Curr. Opin. Neurobiol , vol.8 , pp. 106-116
    • Suter, D.M.1    Forscher, P.2
  • 403
    • 0028177233 scopus 로고
    • Protein kinases involved in the expression of long-term potentiation
    • Suzuki T. Protein kinases involved in the expression of long-term potentiation. Int. J. Biochem. 26:1993;735-744.
    • (1993) Int. J. Biochem , vol.26 , pp. 735-744
    • Suzuki, T.1
  • 404
    • 0026489693 scopus 로고
    • Microtubule-associated protein 2 levels decrease in hippocampus following traumatic brain injury
    • Taft W.C., Yang K., Dixon C.E., Hayes R.L. Microtubule-associated protein 2 levels decrease in hippocampus following traumatic brain injury. J. Neurotrauma. 9:1992;281-290.
    • (1992) J. Neurotrauma , vol.9 , pp. 281-290
    • Taft, W.C.1    Yang, K.2    Dixon, C.E.3    Hayes, R.L.4
  • 405
    • 0028357787 scopus 로고
    • Localization and developmental changes of t protein kinase I/Glycogen synthase kinase-3b in rat brain
    • Takahashi M., Tomizawa K., Kato R., Sato K., Uchida T., Fujita S., Imahori K. Localization and developmental changes of t protein kinase I/Glycogen synthase kinase-3b in rat brain. J. Neurochem. 63:1994;245-255.
    • (1994) J. Neurochem , vol.63 , pp. 245-255
    • Takahashi, M.1    Tomizawa, K.2    Kato, R.3    Sato, K.4    Uchida, T.5    Fujita, S.6    Imahori, K.7
  • 407
    • 0029157258 scopus 로고
    • Polarity orientation and assembly process of microtubule bundles in nocodazole-treated, MAP2c-transfected COS cells
    • Takemura R., Okabe S., Umeyama T., Hirokawa N. Polarity orientation and assembly process of microtubule bundles in nocodazole-treated, MAP2c-transfected COS cells. Mol. Biol. Cell. 6:1995;981-996.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 981-996
    • Takemura, R.1    Okabe, S.2    Umeyama, T.3    Hirokawa, N.4
  • 408
    • 0028863477 scopus 로고
    • Making the connection: Cytoskeletal rearrangements during growth cone guidance
    • Tanaka E., Sabry J. Making the connection: cytoskeletal rearrangements during growth cone guidance. Cell. 83:1995;171-176.
    • (1995) Cell , vol.83 , pp. 171-176
    • Tanaka, E.1    Sabry, J.2
  • 409
    • 0032540459 scopus 로고    scopus 로고
    • The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: The role of protein phosphatases
    • Tanaka T., Zhong J., Iqbal K., Trenkner E., GrundkeIqbal I. The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases. FEBS Lett. 426:1998;248-254.
    • (1998) FEBS Lett , vol.426 , pp. 248-254
    • Tanaka, T.1    Zhong, J.2    Iqbal, K.3    Trenkner, E.4    Grundkeiqbal, I.5
  • 410
    • 0020490408 scopus 로고
    • Molecular characterization of the cAMP-dependent protein kinase bound to microtubule-associated protein 2
    • Theurkauf W.E., Vallee R.B. Molecular characterization of the cAMP-dependent protein kinase bound to microtubule-associated protein 2. J. Biol. Chem. 257:1982;3284-3290.
    • (1982) J. Biol. Chem , vol.257 , pp. 3284-3290
    • Theurkauf, W.E.1    Vallee, R.B.2
  • 411
    • 0020516072 scopus 로고
    • Extensive cAMP-dependent and cAMP-independent phosphorylation of microtubule-associated protein 2
    • Theurkauf W.E., Vallee R.B. Extensive cAMP-dependent and cAMP-independent phosphorylation of microtubule-associated protein 2. J. Biol. Chem. 258:1983;7883-7886.
    • (1983) J. Biol. Chem , vol.258 , pp. 7883-7886
    • Theurkauf, W.E.1    Vallee, R.B.2
  • 412
    • 0027440776 scopus 로고
    • The regional distribution of extracellularly regulated kinase-1 and -2 messenger RNA in the adult rat central nervous system
    • Thomas K.L., Hunt S.P. The regional distribution of extracellularly regulated kinase-1 and -2 messenger RNA in the adult rat central nervous system. Neuroscience. 56:1993;741-757.
    • (1993) Neuroscience , vol.56 , pp. 741-757
    • Thomas, K.L.1    Hunt, S.P.2
  • 413
    • 0032420215 scopus 로고    scopus 로고
    • Regulation of neuronal plasticity in the central nervous system by phosphorylation and dephosphorylation
    • Tokuda M., Hatase O. Regulation of neuronal plasticity in the central nervous system by phosphorylation and dephosphorylation. Mol. Neurobiol. 17:1998;137-156.
    • (1998) Mol. Neurobiol , vol.17 , pp. 137-156
    • Tokuda, M.1    Hatase, O.2
  • 414
    • 0033555273 scopus 로고    scopus 로고
    • A new model for microtubule-associated protein (MAP)-induced microtubule assembly: The Pro-rich region of MAP4 promotes nucleation of microtubule assembly in vitro
    • Tokuraku K., Katsuki M., Nakagawa H., Kotani S. A new model for microtubule-associated protein (MAP)-induced microtubule assembly: the Pro-rich region of MAP4 promotes nucleation of microtubule assembly in vitro. Eur. J. Biochem. 259:1999;158-166.
    • (1999) Eur. J. Biochem , vol.259 , pp. 158-166
    • Tokuraku, K.1    Katsuki, M.2    Nakagawa, H.3    Kotani, S.4
  • 415
    • 0026532298 scopus 로고
    • Demonstration of local protein synthesis within dendrites using a new cell culture system that permits the isolation of living axons and dendrites from their cell bodies
    • Torre E.R., Steward O. Demonstration of local protein synthesis within dendrites using a new cell culture system that permits the isolation of living axons and dendrites from their cell bodies. J. Neurosci. 12:1992;762-772.
    • (1992) J. Neurosci , vol.12 , pp. 762-772
    • Torre, E.R.1    Steward, O.2
  • 416
    • 0027425599 scopus 로고
    • Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system
    • Tsai L., Takahashi T., Caviness V., Harlow E. Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system. Development. 119:1993;1029-1040.
    • (1993) Development , vol.119 , pp. 1029-1040
    • Tsai, L.1    Takahashi, T.2    Caviness, V.3    Harlow, E.4
  • 417
    • 0031712741 scopus 로고    scopus 로고
    • Specificity in signaling pathways: Assembly into multimolecular signaling complexes
    • Tsunoda S., Sierralta J., Zuker C.S. Specificity in signaling pathways: assembly into multimolecular signaling complexes. Curr. Opin. Genet Develop. 8:1998;419-422.
    • (1998) Curr. Opin. Genet Develop , vol.8 , pp. 419-422
    • Tsunoda, S.1    Sierralta, J.2    Zuker, C.S.3
  • 418
    • 0022980293 scopus 로고
    • Calcium/phospholipid-dependent kinase recognizes sites in microtubule-associated protein 2 which are phosphorylated in living brain and are not accessible to other kinases
    • Tsuyama S., Bramblett G.T., Huang K.P., Flavin M. Calcium/phospholipid-dependent kinase recognizes sites in microtubule-associated protein 2 which are phosphorylated in living brain and are not accessible to other kinases. J. Biol. Chem. 261:1986;4110-4116.
    • (1986) J. Biol. Chem , vol.261 , pp. 4110-4116
    • Tsuyama, S.1    Bramblett, G.T.2    Huang, K.P.3    Flavin, M.4
  • 419
    • 0023645332 scopus 로고
    • Numerous phosphates of microtubule-associated protein 2 in living rat brain
    • Tsuyama S., Terayama Y., Matsuyama S. Numerous phosphates of microtubule-associated protein 2 in living rat brain. J. Biol. Chem. 262:1987;10886-10892.
    • (1987) J. Biol. Chem , vol.262 , pp. 10886-10892
    • Tsuyama, S.1    Terayama, Y.2    Matsuyama, S.3
  • 420
    • 0025201210 scopus 로고
    • The roles of microtubule-associated proteins in brain morphogenesis: A review
    • Tucker R.P. The roles of microtubule-associated proteins in brain morphogenesis: a review. Brain Res. Brain Res. Rev. 15:1990;101-120.
    • (1990) Brain Res. Brain Res. Rev , vol.15 , pp. 101-120
    • Tucker, R.P.1
  • 421
    • 0023832948 scopus 로고
    • Differential localization of the high- And low-molecular weight variants of MAP2 in the developing retina
    • Tucker R.P., Binder L.I., Matus A.I. Differential localization of the high- and low-molecular weight variants of MAP2 in the developing retina. Brain Res. 466:1988;313-318.
    • (1988) Brain Res , vol.466 , pp. 313-318
    • Tucker, R.P.1    Binder, L.I.2    Matus, A.I.3
  • 422
    • 0024623621 scopus 로고
    • In situ localization of microtubule-associated protein mRNA in the developing and adult rat brain
    • Tucker R.P., Garner C.C., Matus A. In situ localization of microtubule-associated protein mRNA in the developing and adult rat brain. Neuron. 2:1989;1245-1256.
    • (1989) Neuron , vol.2 , pp. 1245-1256
    • Tucker, R.P.1    Garner, C.C.2    Matus, A.3
  • 423
    • 0024202731 scopus 로고
    • Microtubule-associated proteins characteristic of embryonic brain are found in the adult mammalian retina
    • Tucker R.P., Matus A.I. Microtubule-associated proteins characteristic of embryonic brain are found in the adult mammalian retina. Dev. Biol. 130:1988;423-434.
    • (1988) Dev. Biol , vol.130 , pp. 423-434
    • Tucker, R.P.1    Matus, A.I.2
  • 425
    • 0027275670 scopus 로고
    • Heterogeneity in the phosphorylation of microtubule-associated protein MAP1B during rat brain development
    • Ulloa L., Avila J., Díaz-Nido J. Heterogeneity in the phosphorylation of microtubule-associated protein MAP1B during rat brain development. J. Neurochem. 61:1993;961-972.
    • (1993) J. Neurochem , vol.61 , pp. 961-972
    • Ulloa, L.1    Avila, J.2    Díaz-Nido, J.3
  • 426
    • 0028365718 scopus 로고
    • Localization of differentially phosphorylated isoforms of microtubule-associated protein 1B in cultured rat hippocampal neurons
    • Ulloa L., Díez-Guerra F., Avila J., Díaz-Nido J. Localization of differentially phosphorylated isoforms of microtubule-associated protein 1B in cultured rat hippocampal neurons. Neuroscience. 61:1994;211-223.
    • (1994) Neuroscience , vol.61 , pp. 211-223
    • Ulloa, L.1    Díez-Guerra, F.2    Avila, J.3    Díaz-Nido, J.4
  • 427
    • 0027446346 scopus 로고
    • Dynamics of microtubules bundled by microtubule associated protein 2C (MAP2C)
    • Umeyama T., Okabe S., Kanai Y., Hirokawa N. Dynamics of microtubules bundled by microtubule associated protein 2C (MAP2C). J. Cell Biol. 120:1993;451-465.
    • (1993) J. Cell Biol , vol.120 , pp. 451-465
    • Umeyama, T.1    Okabe, S.2    Kanai, Y.3    Hirokawa, N.4
  • 428
    • 0020415711 scopus 로고
    • Quantitation and characterization of the microtubule associated MAP2 in porcine tissues and its isolation from porcine (PK15) and human (HeLa) cell lines
    • Valdivia M.M., Avila J., Coll J., Colaco C., Sandoval I.V. Quantitation and characterization of the microtubule associated MAP2 in porcine tissues and its isolation from porcine (PK15) and human (HeLa) cell lines. Biochem. Biophys. Res. Commun. 105:1982;1241-1249.
    • (1982) Biochem. Biophys. Res. Commun , vol.105 , pp. 1241-1249
    • Valdivia, M.M.1    Avila, J.2    Coll, J.3    Colaco, C.4    Sandoval, I.V.5
  • 429
    • 0019028065 scopus 로고
    • Structure and phosphorylation of microtubule-associated protein 2 (MAP 2)
    • Vallee R. Structure and phosphorylation of microtubule-associated protein 2 (MAP 2). Proc. Natl. Acad. Sci. U.S.A. 77:1980;3206-3210.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 3206-3210
    • Vallee, R.1
  • 430
    • 0030332245 scopus 로고    scopus 로고
    • Differences in the regulation of microtubule dynamics by microtubule-associated proteins MAP1B and MAP2
    • Vandecandelaere A., Pedrotti B., Utton M., Calvert R., Bayley P. Differences in the regulation of microtubule dynamics by microtubule-associated proteins MAP1B and MAP2. Cell Motil. Cytoskeleton. 35:1996;134-146.
    • (1996) Cell Motil. Cytoskeleton , vol.35 , pp. 134-146
    • Vandecandelaere, A.1    Pedrotti, B.2    Utton, M.3    Calvert, R.4    Bayley, P.5
  • 431
    • 0030815426 scopus 로고    scopus 로고
    • Microtubule function in morphological differentiation: Growth zones and growth cones
    • Vega L.R., Solomon F. Microtubule function in morphological differentiation: Growth zones and growth cones. Cell. 89:1997;825-828.
    • (1997) Cell , vol.89 , pp. 825-828
    • Vega, L.R.1    Solomon, F.2
  • 432
    • 0025037989 scopus 로고
    • Regulation of microtubule dynamics by cdc2 protein kinase in cell-free extracts of Xenopus eggs
    • Verde F., Labbé J., Dorée M., Karsenti E. Regulation of microtubule dynamics by cdc2 protein kinase in cell-free extracts of Xenopus eggs. Nature. 343:1990;233-238.
    • (1990) Nature , vol.343 , pp. 233-238
    • Verde, F.1    Labbé, J.2    Dorée, M.3    Karsenti, E.4
  • 433
    • 0024420788 scopus 로고
    • The adult rat olfactory system expresses microtubule-associated proteins found in the developing brain
    • Viereck C., Tucker R.P., Matus A. The adult rat olfactory system expresses microtubule-associated proteins found in the developing brain. J. Neurosci. 9:1989;3547-3557.
    • (1989) J. Neurosci , vol.9 , pp. 3547-3557
    • Viereck, C.1    Tucker, R.P.2    Matus, A.3
  • 434
    • 0029619129 scopus 로고
    • Microtubule-associated proteins in developing oligodendrocytes: Transient expression of a MAP2c isoform in oligodendrocyte precursors
    • Vouyiouklis D.A., Brophy P.J. Microtubule-associated proteins in developing oligodendrocytes: transient expression of a MAP2c isoform in oligodendrocyte precursors. J. Neurosci. Res. 42:1995;803-817.
    • (1995) J. Neurosci. Res , vol.42 , pp. 803-817
    • Vouyiouklis, D.A.1    Brophy, P.J.2
  • 435
    • 0029998294 scopus 로고    scopus 로고
    • Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubules and microtubule organisation
    • Wagner U., Utton M., Gallo J.M., Miller C.C.J. Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubules and microtubule organisation. J. Cell. Sci. 109:1996;1537-1543.
    • (1996) J. Cell. Sci , vol.109 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.M.3    Miller, C.C.J.4
  • 436
    • 52449145661 scopus 로고
    • Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
    • Walaas S.I., Nairn A.C. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. J. Mol. Neurosci. 1:1989;117-127.
    • (1989) J. Mol. Neurosci , vol.1 , pp. 117-127
    • Walaas, S.I.1    Nairn, A.C.2
  • 437
    • 0027218491 scopus 로고
    • The mechanism of equilibrium binding of microtubule-associated protein 2 to microtubules. Binding is a multi-phasic process and exhibits positive cooperativity
    • Wallis K.T., Azhar S., Rho M.B., Lewis S.A., Cowan N.J., Murphy D.B. The mechanism of equilibrium binding of microtubule-associated protein 2 to microtubules. Binding is a multi-phasic process and exhibits positive cooperativity. J. Biol. Chem. 268:1993;15158-15167.
    • (1993) J. Biol. Chem , vol.268 , pp. 15158-15167
    • Wallis, K.T.1    Azhar, S.2    Rho, M.B.3    Lewis, S.A.4    Cowan, N.J.5    Murphy, D.B.6
  • 438
    • 0032502046 scopus 로고    scopus 로고
    • Ganglioside GM1 alters neuronal morphology by modulating the association of MAP2 with microtubules and actin filaments
    • Wang L.J., Colella R., Roisen F.J. Ganglioside GM1 alters neuronal morphology by modulating the association of MAP2 with microtubules and actin filaments. Dev. Brain Res. 105:1998;227-239.
    • (1998) Dev. Brain Res , vol.105 , pp. 227-239
    • Wang, L.J.1    Colella, R.2    Roisen, F.J.3
  • 439
    • 0029942129 scopus 로고    scopus 로고
    • The ganglioside GM1 enhances microtubule networks and changes the morphology of Neuro-2a cells in vitro by altering the distribution of MAP2
    • Wang L.J., Colella R., Yorke G., Roisen F.J. The ganglioside GM1 enhances microtubule networks and changes the morphology of Neuro-2a cells in vitro by altering the distribution of MAP2. Experimental Neurology. 139:1996;1-11.
    • (1996) Experimental Neurology , vol.139 , pp. 1-11
    • Wang, L.J.1    Colella, R.2    Yorke, G.3    Roisen, F.J.4
  • 440
    • 0032966238 scopus 로고    scopus 로고
    • Positive feedback interactions between microtubule and actin dynamics during cell motility
    • WatermanStorer C.M., Salmon E.D. Positive feedback interactions between microtubule and actin dynamics during cell motility. Curr. Opin. Cell Biol. 11:1999;61-67.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 61-67
    • Watermanstorer, C.M.1    Salmon, E.D.2
  • 441
    • 0027090118 scopus 로고
    • Reorganisation of the microtubular cytoskeleton by embryonic microtubule-associated protein 2 (MAP2c)
    • Weisshaar B., Doll T., Matus A. Reorganisation of the microtubular cytoskeleton by embryonic microtubule-associated protein 2 (MAP2c). Development. 116:1992;1151-1161.
    • (1992) Development , vol.116 , pp. 1151-1161
    • Weisshaar, B.1    Doll, T.2    Matus, A.3
  • 442
    • 0029995794 scopus 로고    scopus 로고
    • GSK3: A SHAGGY frog story
    • Welsh G.I., Wilson C., Proud C.G. GSK3: a SHAGGY frog story. TICB. 6:1996;274-279.
    • (1996) TICB , vol.6 , pp. 274-279
    • Welsh, G.I.1    Wilson, C.2    Proud, C.G.3
  • 443
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera S., Hemmings B. Serine/threonine protein phosphatases. Biochem. J. 311:1995;17-29.
    • (1995) Biochem. J , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.2
  • 444
    • 0024477637 scopus 로고
    • High-Mr microtubule-associated proteins: Properties and functions
    • Wiche G. High-Mr microtubule-associated proteins: properties and functions. Biochem. J. 259:1989;1-12.
    • (1989) Biochem. J , vol.259 , pp. 1-12
    • Wiche, G.1
  • 445
    • 0021432483 scopus 로고
    • Widespread occurrence of polypeptides related to neurotubule-associated proteins (MAP-1 and MAP-2) in non-neuronal cells and tissues
    • Wiche G., Briones E., Koszka C., Artlieb U., Krepler R. Widespread occurrence of polypeptides related to neurotubule-associated proteins (MAP-1 and MAP-2) in non-neuronal cells and tissues. EMBO J. 3:1984;991-998.
    • (1984) EMBO J , vol.3 , pp. 991-998
    • Wiche, G.1    Briones, E.2    Koszka, C.3    Artlieb, U.4    Krepler, R.5
  • 446
    • 0026323985 scopus 로고
    • Molecular structure and function of microtubule-associated proteins
    • Wiche G., Oberkanins C., Himmler A. Molecular structure and function of microtubule-associated proteins. Int. Rev. Cytol. 124:1991;217-273.
    • (1991) Int. Rev. Cytol , vol.124 , pp. 217-273
    • Wiche, G.1    Oberkanins, C.2    Himmler, A.3
  • 447
    • 0027361733 scopus 로고
    • RNA on the move: The mRNA localization pathway
    • Wilhelm J.E., Vale R.D. RNA on the move: the mRNA localization pathway. J. Cell. Biol. 123:1993;269-274.
    • (1993) J. Cell. Biol , vol.123 , pp. 269-274
    • Wilhelm, J.E.1    Vale, R.D.2
  • 449
    • 0026675230 scopus 로고
    • The juvenile microtubule-associated protein MAP2c is a rod-like molecule that forms antiparallel dimers
    • Wille H., Mandelkow E.M., Mandelkow E. The juvenile microtubule-associated protein MAP2c is a rod-like molecule that forms antiparallel dimers. J. Biol. Chem. 267:1992;10737-10742.
    • (1992) J. Biol. Chem , vol.267 , pp. 10737-10742
    • Wille, H.1    Mandelkow, E.M.2    Mandelkow, E.3
  • 450
    • 0031888098 scopus 로고    scopus 로고
    • Beta-catenin: A key mediator of Wnt signaling
    • Willert K., Nusse R. beta-catenin: a key mediator of Wnt signaling. Curr. Opin. Genet Develop. 8:1998;95-102.
    • (1998) Curr. Opin. Genet Develop , vol.8 , pp. 95-102
    • Willert, K.1    Nusse, R.2
  • 451
    • 0032100540 scopus 로고    scopus 로고
    • Glutamate modulation of dendritic outgrowth: Alterations in the distribution of dendritic microtubules
    • Wilson M., Keith C. Glutamate modulation of dendritic outgrowth: alterations in the distribution of dendritic microtubules. J. Neurosci. Res. 52:1998;599-611.
    • (1998) J. Neurosci. Res , vol.52 , pp. 599-611
    • Wilson, M.1    Keith, C.2
  • 452
    • 0032406715 scopus 로고    scopus 로고
    • Mechanisms of Wnt signaling in development
    • Wodarz A., Nusse R. Mechanisms of Wnt signaling in development. Annu. Rev. Cell Dev. Biol. 14:1998;59-88.
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 59-88
    • Wodarz, A.1    Nusse, R.2
  • 453
    • 0025286104 scopus 로고
    • Molecular clonning and expression of glycogen synthase kinase-3/Factor A
    • Woodgett J. Molecular clonning and expression of glycogen synthase kinase-3/Factor A. EMBO J. 9:1990;2431-2438.
    • (1990) EMBO J , vol.9 , pp. 2431-2438
    • Woodgett, J.1
  • 454
    • 0031778575 scopus 로고    scopus 로고
    • A structural basis for memory storage in mammals
    • Woolf N.J. A structural basis for memory storage in mammals. Prog. Neurobiol. 55:1998;59-77.
    • (1998) Prog. Neurobiol , vol.55 , pp. 59-77
    • Woolf, N.J.1
  • 455
    • 0028355681 scopus 로고
    • Pavlovian conditioning alters cortical microtubule-associated protein-2
    • Woolf N.J., Young S.L., Johnson G.V., Fanselow M.S. Pavlovian conditioning alters cortical microtubule-associated protein-2. Neuroreport. 5:1994;1045-1048.
    • (1994) Neuroreport , vol.5 , pp. 1045-1048
    • Woolf, N.J.1    Young, S.L.2    Johnson, G.V.3    Fanselow, M.S.4
  • 456
    • 0033528427 scopus 로고    scopus 로고
    • Hippocampal microtubule-associated protein-2 alterations with contextual memory
    • Woolf N.J., Zinnerman M.D., Johnson G.V.W. Hippocampal microtubule-associated protein-2 alterations with contextual memory. Brain Res. 821:1999;241-249.
    • (1999) Brain Res , vol.821 , pp. 241-249
    • Woolf, N.J.1    Zinnerman, M.D.2    Johnson, G.V.W.3
  • 457
    • 0026548243 scopus 로고
    • On the identity of the major postsynaptic density protein
    • Wu K., Huang J., Adler J., Black I. On the identity of the major postsynaptic density protein. Proc. Natl. Acad. Sci. U.S.A. 89:1992;3015-3019.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 3015-3019
    • Wu, K.1    Huang, J.2    Adler, J.3    Black, I.4
  • 458
    • 0032490652 scopus 로고    scopus 로고
    • The interrelationship between selective tau phosphorylation and microtubule association
    • Xie H.Q., Litersky J.M., Hartigan J.A., Jope R.S., Johnson G.V.W. The interrelationship between selective tau phosphorylation and microtubule association. Brain Res. 798:1998;173-183.
    • (1998) Brain Res , vol.798 , pp. 173-183
    • Xie, H.Q.1    Litersky, J.M.2    Hartigan, J.A.3    Jope, R.S.4    Johnson, G.V.W.5
  • 460
    • 0030887172 scopus 로고    scopus 로고
    • Calcineurin regulation of synaptic function: From ion channels to transmitter release and gene transcription
    • Yakel J.L. Calcineurin regulation of synaptic function: from ion channels to transmitter release and gene transcription. TIPS. 18:1997;124-134.
    • (1997) TIPS , vol.18 , pp. 124-134
    • Yakel, J.L.1
  • 461
    • 0021894684 scopus 로고
    • 2+, calmodulin-dependent regulation of microtubule formation via phosphorylation of microtubule-associated protein 2, tau factor, and tubulin, and comparison with the cyclic AMP-dependent phosphorylation
    • 2+, calmodulin-dependent regulation of microtubule formation via phosphorylation of microtubule-associated protein 2, tau factor, and tubulin, and comparison with the cyclic AMP-dependent phosphorylation. J. Neurochem. 44:1985;759-768.
    • (1985) J. Neurochem , vol.44 , pp. 759-768
    • Yamamoto, H.1    Fukunaga, K.2    Goto, S.3    Tanaka, E.4    Miyamoto, E.5
  • 462
    • 0020642587 scopus 로고
    • 2+- And calmodulin-dependent phosphorylation of microtubule-associated protein 2 and tau factor, and inhibition of microtubule assembly
    • 2+- and calmodulin-dependent phosphorylation of microtubule-associated protein 2 and tau factor, and inhibition of microtubule assembly. J. Neurochem. 41:1983;1119-1125.
    • (1983) J. Neurochem , vol.41 , pp. 1119-1125
    • Yamamoto, H.1    Fukunaga, K.2    Tanaka, E.3    Miyamoto, E.4
  • 463
    • 0023933407 scopus 로고
    • Dephosphorylation of microtubule proteins by brain protein phosphatases 1 and 2A, and its effect on microtubule assembly
    • Yamamoto H., Saitoh Y., Fukunaga K., Nishimura H., Miyamoto E. Dephosphorylation of microtubule proteins by brain protein phosphatases 1 and 2A, and its effect on microtubule assembly. J. Neurochem. 50:1988;1614-1623.
    • (1988) J. Neurochem , vol.50 , pp. 1614-1623
    • Yamamoto, H.1    Saitoh, Y.2    Fukunaga, K.3    Nishimura, H.4    Miyamoto, E.5
  • 464
    • 0032063674 scopus 로고    scopus 로고
    • Early forms of microtubule-associated protein are strongly expressed in cortical dysplasia
    • Yamanouchi H., Jay V., Otsubo H., Kaga M., Becker L.E., Takashima S. Early forms of microtubule-associated protein are strongly expressed in cortical dysplasia. Acta Neuropathol. 95:1998;466-470.
    • (1998) Acta Neuropathol , vol.95 , pp. 466-470
    • Yamanouchi, H.1    Jay, V.2    Otsubo, H.3    Kaga, M.4    Becker, L.E.5    Takashima, S.6
  • 465
    • 0030930199 scopus 로고    scopus 로고
    • Specific binding of acidic phospholipids to microtubule-associated protein MAP1B regulates its interaction with tubulin
    • Yamauchi E., Titani K., Taniguchi H. Specific binding of acidic phospholipids to microtubule-associated protein MAP1B regulates its interaction with tubulin. Journal of Biological Chemistry. 272:1997;22948-22953.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 22948-22953
    • Yamauchi, E.1    Titani, K.2    Taniguchi, H.3
  • 466
    • 0027474128 scopus 로고
    • Reduction in microtubule dynamics in vitro by brain microtubule-associated proteins and by a microtubule-associated protein-2 second repeated sequence analogue
    • Yamauchi P.S., Flynn G.C., Marsh R.L., Purich D.L. Reduction in microtubule dynamics in vitro by brain microtubule-associated proteins and by a microtubule-associated protein-2 second repeated sequence analogue. J. Neurochem. 60:1993;817-826.
    • (1993) J. Neurochem , vol.60 , pp. 817-826
    • Yamauchi, P.S.1    Flynn, G.C.2    Marsh, R.L.3    Purich, D.L.4
  • 467
    • 0023644674 scopus 로고
    • Modulation of microtubule assembly and stability by phosphatidylinositol action on microtubule-associated protein-2
    • Yamauchi P.S., Purich D.L. Modulation of microtubule assembly and stability by phosphatidylinositol action on microtubule-associated protein-2. J. Biol. Chem. 262:1987;3369-3375.
    • (1987) J. Biol. Chem , vol.262 , pp. 3369-3375
    • Yamauchi, P.S.1    Purich, D.L.2
  • 468
    • 0020456472 scopus 로고
    • Phosphorylation of microtubule-associated protein 2 by calmodulin-dependent protein kinase (Kinase II) which occurs only in the brain tissues
    • Yamauchi T., Fujisawa H. Phosphorylation of microtubule-associated protein 2 by calmodulin-dependent protein kinase (Kinase II) which occurs only in the brain tissues. Biochem. Biophys. Res. Commun. 109:1982;975-981.
    • (1982) Biochem. Biophys. Res. Commun , vol.109 , pp. 975-981
    • Yamauchi, T.1    Fujisawa, H.2
  • 469
    • 0023931532 scopus 로고
    • Regulation of the interaction of actin filaments with microtubule-associated protein 2 by calmodulin-dependent protein kinase II
    • Yamauchi T., Fujisawa H. Regulation of the interaction of actin filaments with microtubule-associated protein 2 by calmodulin-dependent protein kinase II. Biochim. Biophys. Acta. 968:1988;77-85.
    • (1988) Biochim. Biophys. Acta , vol.968 , pp. 77-85
    • Yamauchi, T.1    Fujisawa, H.2
  • 470
    • 0021716563 scopus 로고
    • Calpain and calpastatin in porcine retina. Identification and action on microtubule-associated proteins
    • Yoshimura N., Tsukahara I., Murachi T. Calpain and calpastatin in porcine retina. Identification and action on microtubule-associated proteins. Biochem. J. 223:1984;47-51.
    • (1984) Biochem. J , vol.223 , pp. 47-51
    • Yoshimura, N.1    Tsukahara, I.2    Murachi, T.3
  • 471
    • 0031955853 scopus 로고    scopus 로고
    • Region-specific expression of cyclin-dependent kinase 5 (cdk5) and its activators, p35 and p39, in the developing and adult rat central nervous system
    • Zheng M., Leung C.L., Liem R.K.H. Region-specific expression of cyclin-dependent kinase 5 (cdk5) and its activators, p35 and p39, in the developing and adult rat central nervous system. J. Neurobiol. 35:1998;141-159.
    • (1998) J. Neurobiol , vol.35 , pp. 141-159
    • Zheng, M.1    Leung, C.L.2    Liem, R.K.H.3
  • 472
    • 0031442806 scopus 로고    scopus 로고
    • Enlightening the postsynaptic density
    • Ziff E.B. Enlightening the postsynaptic density. Neuron. 19:1997;1163-1174.
    • (1997) Neuron , vol.19 , pp. 1163-1174
    • Ziff, E.B.1
  • 473
    • 0030200393 scopus 로고    scopus 로고
    • Evidence for a role of dendritic filopodia in synaptogenesis and spine formation
    • Ziv N.E., Smith S.J. Evidence for a role of dendritic filopodia in synaptogenesis and spine formation. Neuron. 17:1996;91-102.
    • (1996) Neuron , vol.17 , pp. 91-102
    • Ziv, N.E.1    Smith, S.J.2


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