메뉴 건너뛰기




Volumn 57, Issue 5, 2010, Pages 497-503

Filamentous microtubules in the neuronal spinous process and the role of microtubule regulatory drugs in neuropathic pain

Author keywords

Chemotherapy; CNS; Microtubule; Pain; Synapse; Taxol; Vinca drugs

Indexed keywords

ACTIN; BINDING PROTEIN; KINESIN; MYOSIN; MYOSIN IIA; MYOSIN V; MYOSIN VIIA; MYOSIN X; NOCODAZOLE; PACLITAXEL; TUBULIN; TUBULIN BINDING PROTEIN; UNCLASSIFIED DRUG; VINCA ALKALOID;

EID: 77956226927     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2010.06.022     Document Type: Short Survey
Times cited : (6)

References (106)
  • 3
    • 0022630780 scopus 로고
    • Synapsin I is a microtubule-bundling protein
    • Baines A.J., Bennett V. Synapsin I is a microtubule-bundling protein. Nature 1986, 319:145-147.
    • (1986) Nature , vol.319 , pp. 145-147
    • Baines, A.J.1    Bennett, V.2
  • 6
    • 0025802986 scopus 로고
    • Site specificity in the interactions of synapsin 1 with tubulin
    • Bennett A.F., Hayes N.V., Baines A.J. Site specificity in the interactions of synapsin 1 with tubulin. Biochem. J. 1991, 276:793-799.
    • (1991) Biochem. J. , vol.276 , pp. 793-799
    • Bennett, A.F.1    Hayes, N.V.2    Baines, A.J.3
  • 7
    • 1642430703 scopus 로고    scopus 로고
    • Microtubule-targeted anticancer agents and apoptosis
    • Bhalla K.N. Microtubule-targeted anticancer agents and apoptosis. Oncogene 2003, 22:9075-9086.
    • (2003) Oncogene , vol.22 , pp. 9075-9086
    • Bhalla, K.N.1
  • 8
    • 0016786424 scopus 로고
    • Membrane-bound tubulin in brain and thyroid tissue
    • Bhattacharyya B., Wolff J. Membrane-bound tubulin in brain and thyroid tissue. J. Biol. Chem. 1975, 250:7639-7646.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7639-7646
    • Bhattacharyya, B.1    Wolff, J.2
  • 9
    • 0017166466 scopus 로고
    • Polymerisation of membrane tubulin
    • Bhattacharyya B., Wolff J. Polymerisation of membrane tubulin. Nature 1976, 264:576-577.
    • (1976) Nature , vol.264 , pp. 576-577
    • Bhattacharyya, B.1    Wolff, J.2
  • 10
    • 0032883001 scopus 로고    scopus 로고
    • Molecular effects of paclitaxel: myths and reality (a critical review)
    • Blagosklonny M.V., Fojo T. Molecular effects of paclitaxel: myths and reality (a critical review). Int. J. Cancer 1999, 83:151-156.
    • (1999) Int. J. Cancer , vol.83 , pp. 151-156
    • Blagosklonny, M.V.1    Fojo, T.2
  • 11
    • 0016268885 scopus 로고
    • Muscle-like contractile proteins and tubulin in synaptosomes
    • Blitz A.L., Fine R.E. Muscle-like contractile proteins and tubulin in synaptosomes. Proc. Natl. Acad. Sci. U.S.A. 1974, 71:4472-4476.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 4472-4476
    • Blitz, A.L.1    Fine, R.E.2
  • 12
    • 21244475513 scopus 로고    scopus 로고
    • Plasma membrane localization and function of TRPC1 is dependent on its interaction with beta-tubulin in retinal epithelium cells
    • Bollimuntha S., Cornatzer E., Singh B.B. Plasma membrane localization and function of TRPC1 is dependent on its interaction with beta-tubulin in retinal epithelium cells. Vis. Neurosci. 2005, 22:163-170.
    • (2005) Vis. Neurosci. , vol.22 , pp. 163-170
    • Bollimuntha, S.1    Cornatzer, E.2    Singh, B.B.3
  • 13
    • 60349116495 scopus 로고    scopus 로고
    • Cryoelectron microscopy of vitreous sections: a step further towards the native state
    • Bouchet-Marquis C., Fakan S. Cryoelectron microscopy of vitreous sections: a step further towards the native state. Methods Mol. Biol. 2009, 464:425-439.
    • (2009) Methods Mol. Biol. , vol.464 , pp. 425-439
    • Bouchet-Marquis, C.1    Fakan, S.2
  • 15
    • 46149090341 scopus 로고    scopus 로고
    • Tubulin as a binding partner of the Heag2 voltage-gated potassium channel
    • Bracey K., Ju M., Tian C., Stevens L., Wray D. Tubulin as a binding partner of the Heag2 voltage-gated potassium channel. J. Membr. Biol. 2008, 222:115-125.
    • (2008) J. Membr. Biol. , vol.222 , pp. 115-125
    • Bracey, K.1    Ju, M.2    Tian, C.3    Stevens, L.4    Wray, D.5
  • 16
    • 0842290746 scopus 로고    scopus 로고
    • Short-range axonal/dendritic transport by myosin-V: a model for vesicle delivery to the synapse
    • Brown J.R., Stafford P., Langford G.M. Short-range axonal/dendritic transport by myosin-V: a model for vesicle delivery to the synapse. J. Neurobiol. 2004, 58:175-188.
    • (2004) J. Neurobiol. , vol.58 , pp. 175-188
    • Brown, J.R.1    Stafford, P.2    Langford, G.M.3
  • 17
    • 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. 1984, 141:609-615.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 609-615
    • Burns, R.G.1    Islam, K.2    Chapman, R.3
  • 18
    • 0005907946 scopus 로고
    • Immunocytochemical localization of actin and microtubule-associated protein MAP2 in dendritic spines
    • Caceres 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. 1983, 80:1738-1742.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 1738-1742
    • Caceres, A.1    Payne, M.R.2    Binder, L.I.3    Steward, O.4
  • 19
    • 65649086010 scopus 로고    scopus 로고
    • Tubulin: a target for antineoplastic drugs into the cancer cells but also in the peripheral nervous system
    • Canta A., Chiorazzi A., Cavaletti G. Tubulin: a target for antineoplastic drugs into the cancer cells but also in the peripheral nervous system. Curr. Med. Chem. 2009, 16:1315-1324.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 1315-1324
    • Canta, A.1    Chiorazzi, A.2    Cavaletti, G.3
  • 20
    • 0346729934 scopus 로고    scopus 로고
    • Myosin-Va binds to and mechanochemically couples microtubules to actin filaments
    • Cao T.T., Chang W., Masters S.E., Mooseker M.S. Myosin-Va binds to and mechanochemically couples microtubules to actin filaments. Mol. Biol. Cell. 2004, 15:151-161.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 151-161
    • Cao, T.T.1    Chang, W.2    Masters, S.E.3    Mooseker, M.S.4
  • 21
    • 0020059402 scopus 로고
    • Postmortem accumulation of tubulin in postsynaptic density preparations
    • Carlin R.K., Grab D.J., Siekevitz P. Postmortem accumulation of tubulin in postsynaptic density preparations. J. Neurochem. 1982, 38:94-100.
    • (1982) J. Neurochem. , vol.38 , pp. 94-100
    • Carlin, R.K.1    Grab, D.J.2    Siekevitz, P.3
  • 22
    • 0037072776 scopus 로고    scopus 로고
    • Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel
    • Carre M., Andre N., Carles G., Borghi H., Brichese L., Briand C., Braguer D. Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel. J. Biol. Chem. 2002, 277:33664-33669.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33664-33669
    • Carre, M.1    Andre, N.2    Carles, G.3    Borghi, H.4    Brichese, L.5    Briand, C.6    Braguer, D.7
  • 24
    • 0026778684 scopus 로고
    • Three-dimensional analysis of the structure and composition of CA3 branched dendritic spines and their synaptic relationships with mossy fiber boutons in the rat hippocampus
    • Chicurel, Harris Three-dimensional analysis of the structure and composition of CA3 branched dendritic spines and their synaptic relationships with mossy fiber boutons in the rat hippocampus. J. Comp. Neurol. 1992, 325:169-182.
    • (1992) J. Comp. Neurol. , vol.325 , pp. 169-182
    • Chicurel1    Harris2
  • 25
    • 0035154143 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor type 1α and tubulin assemble into dynamic interacting complexes
    • Ciruela F., McIlhinney R.A. Metabotropic glutamate receptor type 1α and tubulin assemble into dynamic interacting complexes. J. Neurochem. 2001, 76:750-757.
    • (2001) J. Neurochem. , vol.76 , pp. 750-757
    • Ciruela, F.1    McIlhinney, R.A.2
  • 26
    • 0032947013 scopus 로고    scopus 로고
    • Interactions of the C-terminus of metabotropic glutamate receptor type 1alpha with rat brain proteins:evidence for a direct interaction with tubulin
    • Ciruela F., Robbins M.J., Willis A.C., McIlhinney R.A. Interactions of the C-terminus of metabotropic glutamate receptor type 1alpha with rat brain proteins:evidence for a direct interaction with tubulin. J. Neurochem. 1999, 72:346-354.
    • (1999) J. Neurochem. , vol.72 , pp. 346-354
    • Ciruela, F.1    Robbins, M.J.2    Willis, A.C.3    McIlhinney, R.A.4
  • 28
    • 77952889767 scopus 로고    scopus 로고
    • Changes in microtubule turnover accompany synaptic plasticity and memory formation in response to contextual fear conditioning in mice
    • Fanara P., Husted K.H., Selle K., Wong P.Y., Banerjee J., Brandt R., Hellerstein M.K. Changes in microtubule turnover accompany synaptic plasticity and memory formation in response to contextual fear conditioning in mice. Neuroscience 2010, 168:167-178.
    • (2010) Neuroscience , vol.168 , pp. 167-178
    • Fanara, P.1    Husted, K.H.2    Selle, K.3    Wong, P.Y.4    Banerjee, J.5    Brandt, R.6    Hellerstein, M.K.7
  • 29
    • 0014843005 scopus 로고
    • Colchicine-binding activity in particulate fractions of mouse brain
    • Feit H., Barondes S.H. Colchicine-binding activity in particulate fractions of mouse brain. J. Neurochem. 1970, 17:1355-1364.
    • (1970) J. Neurochem. , vol.17 , pp. 1355-1364
    • Feit, H.1    Barondes, S.H.2
  • 31
    • 56749104130 scopus 로고    scopus 로고
    • Fluorescent probes for super-resolution imaging in living cells
    • Fernández-Suárez M., Ting A.Y. Fluorescent probes for super-resolution imaging in living cells. Nat. Rev. Mol. Cell Biol. 2008, 9:929-943.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 929-943
    • Fernández-Suárez, M.1    Ting, A.Y.2
  • 34
    • 38449097524 scopus 로고    scopus 로고
    • Mechanisms of multidrug resistance: the potential role of microtubule-stabilizing agents
    • Fojo T., Menefee M. Mechanisms of multidrug resistance: the potential role of microtubule-stabilizing agents. Ann. Oncol. 2007, 18(Suppl. (5)):v3-v8.
    • (2007) Ann. Oncol. , vol.18 , Issue.SUPPL. 5
    • Fojo, T.1    Menefee, M.2
  • 40
    • 26444514141 scopus 로고    scopus 로고
    • Proteomic analysis of TRPC5- and TRPC6-binding partners reveals interaction with the plasmalemmal Na(+)/K(+)-ATPase
    • Goel M., Sinkins W., Keightley A., Kinter M., Schilling W.P. Proteomic analysis of TRPC5- and TRPC6-binding partners reveals interaction with the plasmalemmal Na(+)/K(+)-ATPase. Pflugers Arch. 2005, 451:87-98.
    • (2005) Pflugers Arch. , vol.451 , pp. 87-98
    • Goel, M.1    Sinkins, W.2    Keightley, A.3    Kinter, M.4    Schilling, W.P.5
  • 42
    • 33947244356 scopus 로고    scopus 로고
    • Identification and characterisation of novel tubulin-binding motifs located within the C-terminus of TRPV1
    • Goswami C., Hucho T.B., Hucho F. Identification and characterisation of novel tubulin-binding motifs located within the C-terminus of TRPV1. J. Neurochem. 2007, 101:250-262.
    • (2007) J. Neurochem. , vol.101 , pp. 250-262
    • Goswami, C.1    Hucho, T.B.2    Hucho, F.3
  • 43
    • 35448937926 scopus 로고    scopus 로고
    • TRPV1 expression-dependent initiation and regulation of filopodia
    • Goswami C., Hucho T. TRPV1 expression-dependent initiation and regulation of filopodia. J. Neurochem. 2007, 103:1319-1333.
    • (2007) J. Neurochem. , vol.103 , pp. 1319-1333
    • Goswami, C.1    Hucho, T.2
  • 44
    • 77955379568 scopus 로고    scopus 로고
    • Importance of non-selective cation channel TRPV4 interaction with cytoskeleton and their reciprocal regulations in cultured cells
    • Goswami C*., Kuhn J., Heppenstall P.A., Hucho T. Importance of non-selective cation channel TRPV4 interaction with cytoskeleton and their reciprocal regulations in cultured cells. PLOS One 2010, 5(7):e11654.
    • (2010) PLOS One , vol.5 , Issue.7
    • Goswami, C.1    Kuhn, J.2    Heppenstall, P.A.3    Hucho, T.4
  • 46
    • 0020287381 scopus 로고
    • The interaction of actin filaments with microtubules and microtubule-associated proteins
    • Griffith L.M., Pollard T.D. The interaction of actin filaments with microtubules and microtubule-associated proteins. J. Biol. Chem. 1982, 257:9143-9151.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9143-9151
    • Griffith, L.M.1    Pollard, T.D.2
  • 47
    • 36849092908 scopus 로고    scopus 로고
    • Isoform specificity of P2X(2) purinergic receptor C-terminus binding to tubulin
    • Guimaraes M.Z. Isoform specificity of P2X(2) purinergic receptor C-terminus binding to tubulin. Neurochem. Int. 2008, 52:314-320.
    • (2008) Neurochem. Int. , vol.52 , pp. 314-320
    • Guimaraes, M.Z.1
  • 49
    • 58149225472 scopus 로고    scopus 로고
    • Microtubules in dendritic spine development
    • Gu J., Firestein B.L., Zheng J.Q. Microtubules in dendritic spine development. J. Neurosci. 2008, 28:12120-12124.
    • (2008) J. Neurosci. , vol.28 , pp. 12120-12124
    • Gu, J.1    Firestein, B.L.2    Zheng, J.Q.3
  • 51
    • 0037035809 scopus 로고    scopus 로고
    • 2+-dependent interaction between tubulin and synaptotagmin I: a possible mechanism for attaching synaptic vesicles to microtubules
    • 2+-dependent interaction between tubulin and synaptotagmin I: a possible mechanism for attaching synaptic vesicles to microtubules. J. Biol. Chem. 2002, 277:20234-20242.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20234-20242
    • Honda, A.1    Yamada, M.2    Saisu, H.3    Takahashi, H.4    Mori, K.J.5    Abe, T.6
  • 52
    • 58149272090 scopus 로고    scopus 로고
    • Activity-dependent dynamic microtubule invasion of dendritic spines
    • Hu X., Viesselmann C., Nam S., Merriam E., Dent E.W. Activity-dependent dynamic microtubule invasion of dendritic spines. J. Neurosci. 2008, 28:13094-13105.
    • (2008) J. Neurosci. , vol.28 , pp. 13094-13105
    • Hu, X.1    Viesselmann, C.2    Nam, S.3    Merriam, E.4    Dent, E.W.5
  • 53
    • 0028169498 scopus 로고
    • Binding of gamma-aminobutyric acid A receptors to tubulin
    • Item C., Sieghart W. Binding of gamma-aminobutyric acid A receptors to tubulin. J. Neurochem. 1994, 63:1119-1125.
    • (1994) J. Neurochem. , vol.63 , pp. 1119-1125
    • Item, C.1    Sieghart, W.2
  • 55
    • 67649202108 scopus 로고    scopus 로고
    • Drosophila Tubulin-specific chaperone E functions at neuromuscular synapses and is required for microtubule network formation
    • Jin S., Pan L., Liu Z., Wang Q., Xu Z., Zhang Y.Q. Drosophila Tubulin-specific chaperone E functions at neuromuscular synapses and is required for microtubule network formation. Development 2009, 136:1571-1581.
    • (2009) Development , vol.136 , pp. 1571-1581
    • Jin, S.1    Pan, L.2    Liu, Z.3    Wang, Q.4    Xu, Z.5    Zhang, Y.Q.6
  • 56
    • 0035912770 scopus 로고    scopus 로고
    • Cytoskeletal microdifferentiation: a mechanism for organizing morphological plasticity in dendrites
    • Kaech S., Parmar H., Roelandse M., Bornmann C., Matus A. Cytoskeletal microdifferentiation: a mechanism for organizing morphological plasticity in dendrites. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:7086-7092.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7086-7092
    • Kaech, S.1    Parmar, H.2    Roelandse, M.3    Bornmann, C.4    Matus, A.5
  • 58
    • 0019349993 scopus 로고
    • Developmental changes in morphology and molecular composition of isolated synaptic junctional structures
    • Kelly P.T., Cotman C.W. Developmental changes in morphology and molecular composition of isolated synaptic junctional structures. Brain Res. 1981, 206:251-257.
    • (1981) Brain Res. , vol.206 , pp. 251-257
    • Kelly, P.T.1    Cotman, C.W.2
  • 60
    • 60649084165 scopus 로고    scopus 로고
    • Proteomics analysis of immuno-precipitated synaptic protein complexes
    • Klemmer P., Smit A.B., Li K.W. Proteomics analysis of immuno-precipitated synaptic protein complexes. J. Proteomics 2009, 72:82-90.
    • (2009) J. Proteomics , vol.72 , pp. 82-90
    • Klemmer, P.1    Smit, A.B.2    Li, K.W.3
  • 61
    • 0016706720 scopus 로고
    • Isolation and partial characterization of a tubulin-like protein from human and swine synaptosomal membranes
    • Kornguth S.E., Sunderland E. Isolation and partial characterization of a tubulin-like protein from human and swine synaptosomal membranes. Biochim. Biophys. Acta 1975, 393:100-114.
    • (1975) Biochim. Biophys. Acta , vol.393 , pp. 100-114
    • Kornguth, S.E.1    Sunderland, E.2
  • 62
    • 0020318730 scopus 로고
    • The interaction between calmodulin and microtubule proteins. IV. Quantitative analysis of the binding between calmodulin and tubulin dimer
    • Kumagai H., Nishida E., Sakai H. The interaction between calmodulin and microtubule proteins. IV. Quantitative analysis of the binding between calmodulin and tubulin dimer. J. Biochem. 1982, 91:1329-1336.
    • (1982) J. Biochem. , vol.91 , pp. 1329-1336
    • Kumagai, H.1    Nishida, E.2    Sakai, H.3
  • 63
    • 0031688873 scopus 로고    scopus 로고
    • Characterization of granular particles isolated from postsynaptic densities
    • Lai S.L., Ling S.C., Kuo L.H., Shu Y.C., Chow W.Y., Chang Y.C. Characterization of granular particles isolated from postsynaptic densities. J. Neurochem. 1998, 71:1694-1701.
    • (1998) J. Neurochem. , vol.71 , pp. 1694-1701
    • Lai, S.L.1    Ling, S.C.2    Kuo, L.H.3    Shu, Y.C.4    Chow, W.Y.5    Chang, Y.C.6
  • 64
    • 0020550407 scopus 로고
    • Cytoplasmic organization in cerebellar dendritic spines
    • Landis D.M., Reese T.S. Cytoplasmic organization in cerebellar dendritic spines. J. Cell Biol. 1983, 97:1169-1178.
    • (1983) J. Cell Biol. , vol.97 , pp. 1169-1178
    • Landis, D.M.1    Reese, T.S.2
  • 65
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V, a versatile motor for short-range vesicle transport
    • Langford G.M. Myosin-V, a versatile motor for short-range vesicle transport. Traffic 2002, 3:859-865.
    • (2002) Traffic , vol.3 , pp. 859-865
    • Langford, G.M.1
  • 66
    • 0026584947 scopus 로고
    • The 93kDa protein gephyrin and tubulin associated with the inhibitory glycine receptor are phosphorylated by an endogenous protein kinase
    • Langosch D., Hoch W., Betz H. The 93kDa protein gephyrin and tubulin associated with the inhibitory glycine receptor are phosphorylated by an endogenous protein kinase. FEBS Lett. 1992, 298:113-117.
    • (1992) FEBS Lett. , vol.298 , pp. 113-117
    • Langosch, D.1    Hoch, W.2    Betz, H.3
  • 67
    • 33645736326 scopus 로고    scopus 로고
    • Peripheral neuropathy induced by microtubule-stabilizing agents
    • Lee J.J., Swain S.M. Peripheral neuropathy induced by microtubule-stabilizing agents. J. Clin. Oncol. 2006, 24:1633-1642.
    • (2006) J. Clin. Oncol. , vol.24 , pp. 1633-1642
    • Lee, J.J.1    Swain, S.M.2
  • 69
    • 0034721711 scopus 로고    scopus 로고
    • Actin-based plasticity in dendritic spines
    • Matus A. Actin-based plasticity in dendritic spines. Science 2000, 290:754-758.
    • (2000) Science , vol.290 , pp. 754-758
    • Matus, A.1
  • 70
    • 0018233287 scopus 로고
    • Morphology and molecular composition of isolated postsynaptic junctional structures
    • Matus A.I., Taff-Jones D.H. Morphology and molecular composition of isolated postsynaptic junctional structures. Proc. R. Soc. Lond. B Biol. Sci. 1978, 203:135-151.
    • (1978) Proc. R. Soc. Lond. B Biol. Sci. , vol.203 , pp. 135-151
    • Matus, A.I.1    Taff-Jones, D.H.2
  • 71
    • 29144478503 scopus 로고    scopus 로고
    • Peripheral neuropathy: a persisting challenge in paclitaxel-based regimes
    • Mielke S., Sparreboom A., Mross K. Peripheral neuropathy: a persisting challenge in paclitaxel-based regimes. Eur. J. Cancer 2006, 42:24-30.
    • (2006) Eur. J. Cancer , vol.42 , pp. 24-30
    • Mielke, S.1    Sparreboom, A.2    Mross, K.3
  • 75
    • 0035500991 scopus 로고    scopus 로고
    • Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells
    • Payton J.E., Perrin R.J., Clayton D.F., George J.M. Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells. Brain Res. Mol. Brain Res. 2001, 95:138-145.
    • (2001) Brain Res. Mol. Brain Res. , vol.95 , pp. 138-145
    • Payton, J.E.1    Perrin, R.J.2    Clayton, D.F.3    George, J.M.4
  • 76
    • 58149231221 scopus 로고    scopus 로고
    • Not just actin? A role for dynamic microtubules in dendritic spines
    • Penzes P., Srivastava D.P., Woolfrey K.M. Not just actin? A role for dynamic microtubules in dendritic spines. Neuron 2009, 61:3-5.
    • (2009) Neuron , vol.61 , pp. 3-5
    • Penzes, P.1    Srivastava, D.P.2    Woolfrey, K.M.3
  • 77
    • 0030614363 scopus 로고    scopus 로고
    • Tubulin, Gq, and phosphatidylinositol 4,5-bisphosphate interact to regulate phospholipase Cbeta1 signaling
    • Popova J.S., Garrison J.C., Rhee S.G., Rasenick M.M. Tubulin, Gq, and phosphatidylinositol 4,5-bisphosphate interact to regulate phospholipase Cbeta1 signaling. J. Biol. Chem. 1997, 272:6760-6765.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6760-6765
    • Popova, J.S.1    Garrison, J.C.2    Rhee, S.G.3    Rasenick, M.M.4
  • 79
    • 0033710887 scopus 로고    scopus 로고
    • Drosophila Futsch regulates synaptic microtubule organization and is necessary for synaptic growth
    • Roos J., Hummel T., Ng N., Klämbt C., Davis G.W. Drosophila Futsch regulates synaptic microtubule organization and is necessary for synaptic growth. Neuron 2000, 26:371-382.
    • (2000) Neuron , vol.26 , pp. 371-382
    • Roos, J.1    Hummel, T.2    Ng, N.3    Klämbt, C.4    Davis, G.W.5
  • 80
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation: role of cytosolic proteins and mitochondrial lipids
    • Rostovtseva T.K., Bezrukov S.M. VDAC regulation: role of cytosolic proteins and mitochondrial lipids. J. Bioenerg. Biomembr. 2008, 40:163-170.
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 82
    • 0031282982 scopus 로고    scopus 로고
    • G protein beta 1 gamma 2 subunits promote microtubule assembly
    • Roychowdhury S., Rasenick M.M. G protein beta 1 gamma 2 subunits promote microtubule assembly. J. Biol. Chem. 1997, 272:31576-31581.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31576-31581
    • Roychowdhury, S.1    Rasenick, M.M.2
  • 83
    • 0033532053 scopus 로고    scopus 로고
    • G protein alpha subunits activate tubulin GTPase and modulate microtubule polymerisation dynamics
    • Roychowdhury S., Panda D., Wilson L., Rasenick M.M. G protein alpha subunits activate tubulin GTPase and modulate microtubule polymerisation dynamics. J. Biol. Chem. 1999, 274:13485-13490.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13485-13490
    • Roychowdhury, S.1    Panda, D.2    Wilson, L.3    Rasenick, M.M.4
  • 84
    • 0022021178 scopus 로고
    • Taxol-induced neuropathy: further ultrastructural studies of nerve fibre changes in situ
    • Röytta M., Raine C.S. Taxol-induced neuropathy: further ultrastructural studies of nerve fibre changes in situ. J. Neurocytol. 1985, 14:157-175.
    • (1985) J. Neurocytol. , vol.14 , pp. 157-175
    • Röytta, M.1    Raine, C.S.2
  • 85
    • 0038414642 scopus 로고    scopus 로고
    • Heterotrimeric G-proteins associate with microtubules during differentiation in PC12 pheochromocytoma cells
    • Sarma T., Voyno-Yasenetskaya T., Hope T.J., Rasenick M.M. Heterotrimeric G-proteins associate with microtubules during differentiation in PC12 pheochromocytoma cells. FASEB J. 2003, 17:848-859.
    • (2003) FASEB J. , vol.17 , pp. 848-859
    • Sarma, T.1    Voyno-Yasenetskaya, T.2    Hope, T.J.3    Rasenick, M.M.4
  • 86
    • 0036321077 scopus 로고    scopus 로고
    • Interaction between metabotropic glutamate receptor 7 and alpha tubulin
    • Saugstad J.A., Yang S., Pohl J., Hall R.A., Conn P.J. Interaction between metabotropic glutamate receptor 7 and alpha tubulin. J. Neurochem. 2002, 80:980-988.
    • (2002) J. Neurochem. , vol.80 , pp. 980-988
    • Saugstad, J.A.1    Yang, S.2    Pohl, J.3    Hall, R.A.4    Conn, P.J.5
  • 88
    • 33646581965 scopus 로고    scopus 로고
    • Peripheral neuropathy induced by Paclitaxel: recent insights and future perspectives
    • Scripture C.D., Figg W.D., Sparreboom A. Peripheral neuropathy induced by Paclitaxel: recent insights and future perspectives. Curr. Neuropharmacol. 2006, 4:165-172.
    • (2006) Curr. Neuropharmacol. , vol.4 , pp. 165-172
    • Scripture, C.D.1    Figg, W.D.2    Sparreboom, A.3
  • 89
    • 33847151787 scopus 로고    scopus 로고
    • Effects of body temperature on neural activity in the hippocampus: regulation of resting membrane potentials by transient receptor potential vanilloid 4
    • Shibasaki K., Suzuki M., Mizuno A., Tominaga M. Effects of body temperature on neural activity in the hippocampus: regulation of resting membrane potentials by transient receptor potential vanilloid 4. J. Neurosci. 2007, 27:1566-1575.
    • (2007) J. Neurosci. , vol.27 , pp. 1566-1575
    • Shibasaki, K.1    Suzuki, M.2    Mizuno, A.3    Tominaga, M.4
  • 90
    • 77950908179 scopus 로고    scopus 로고
    • Imaging cytoskeleton components by electron microscopy
    • Svitkina T. Imaging cytoskeleton components by electron microscopy. Methods Mol. Biol. 2009, 586:187-206.
    • (2009) Methods Mol. Biol. , vol.586 , pp. 187-206
    • Svitkina, T.1
  • 91
    • 4944252855 scopus 로고    scopus 로고
    • Cell biology: myosins meet microtubules
    • Titus M.A. Cell biology: myosins meet microtubules. Nature 2004, 431:252-253.
    • (2004) Nature , vol.431 , pp. 252-253
    • Titus, M.A.1
  • 92
    • 0017194630 scopus 로고
    • Isolation of synaptic junctional complexes of high structural integrity from rat brain
    • Therien H.M., Mushynski W.E. Isolation of synaptic junctional complexes of high structural integrity from rat brain. J. Cell. Biol. 1976, 71:807-822.
    • (1976) J. Cell. Biol. , vol.71 , pp. 807-822
    • Therien, H.M.1    Mushynski, W.E.2
  • 94
    • 0035282080 scopus 로고    scopus 로고
    • Myosin VIIA is specifically associated with calmodulin and microtubule-associated protein-2B (MAP-2B)
    • Todorov P.T., Hardisty R.E., Brown S.D. Myosin VIIA is specifically associated with calmodulin and microtubule-associated protein-2B (MAP-2B). Biochem. J. 2001, 354:267-274.
    • (2001) Biochem. J. , vol.354 , pp. 267-274
    • Todorov, P.T.1    Hardisty, R.E.2    Brown, S.D.3
  • 95
    • 0033011462 scopus 로고    scopus 로고
    • Dynamic interaction between soluble tubulin and C-terminal domains of N-methyl-D-aspartate receptor subunits
    • van Rossum D., Kuhse J., Betz H. Dynamic interaction between soluble tubulin and C-terminal domains of N-methyl-D-aspartate receptor subunits. J. Neurochem. 1999, 72:962-973.
    • (1999) J. Neurochem. , vol.72 , pp. 962-973
    • van Rossum, D.1    Kuhse, J.2    Betz, H.3
  • 96
    • 0033168992 scopus 로고    scopus 로고
    • Cytoskeletal dynamics in dendritic spines: direct modulation by glutamate receptors?
    • van Rossum D., Hanisch U.K. Cytoskeletal dynamics in dendritic spines: direct modulation by glutamate receptors?. Trends Neurosci. 1999, 22:290-295.
    • (1999) Trends Neurosci. , vol.22 , pp. 290-295
    • van Rossum, D.1    Hanisch, U.K.2
  • 97
    • 0016594329 scopus 로고
    • Tubulin in postynaptic junctional lattice
    • Walters B.B., Matus A.I. Tubulin in postynaptic junctional lattice. Nature 1975, 257:496-498.
    • (1975) Nature , vol.257 , pp. 496-498
    • Walters, B.B.1    Matus, A.I.2
  • 98
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S., Weber K. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 2003, 4:938-947.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 101
    • 0018139321 scopus 로고
    • Induction of paracrystalline arrays by vincristine in the synaptic formations of the teleost retina
    • Wolburg H., Kurz-Isler G. Induction of paracrystalline arrays by vincristine in the synaptic formations of the teleost retina. Cell Tissue Res. 1978, 191:75-82.
    • (1978) Cell Tissue Res. , vol.191 , pp. 75-82
    • Wolburg, H.1    Kurz-Isler, G.2
  • 102
    • 33644525528 scopus 로고    scopus 로고
    • Motor proteins at the microtubule plus-end
    • Wu X., Xiang X., Hammer J.A. Motor proteins at the microtubule plus-end. Trends Cell Biol. 2006, 16:135-143.
    • (2006) Trends Cell Biol. , vol.16 , pp. 135-143
    • Wu, X.1    Xiang, X.2    Hammer, J.A.3
  • 103
    • 27544458296 scopus 로고    scopus 로고
    • Melanophilin and myosin Va track the microtubule plus end on EB1
    • Wu X.S., Tsan G.L., Hammer J.A. Melanophilin and myosin Va track the microtubule plus end on EB1. J. Cell Biol. 2005, 171:201-207.
    • (2005) J. Cell Biol. , vol.171 , pp. 201-207
    • Wu, X.S.1    Tsan, G.L.2    Hammer, J.A.3
  • 104
    • 34047163872 scopus 로고    scopus 로고
    • In vivo assay of presynaptic microtubule cytoskeleton dynamics in Drosophila
    • Yan Y., Broadie K. In vivo assay of presynaptic microtubule cytoskeleton dynamics in Drosophila. J. Neurosci. Methods 2007, 162:198-205.
    • (2007) J. Neurosci. Methods , vol.162 , pp. 198-205
    • Yan, Y.1    Broadie, K.2
  • 105
    • 0017055827 scopus 로고
    • Microtubular proteins in pigeon erythrocyte membranes
    • Zenner H.P., Pfeuffer T. Microtubular proteins in pigeon erythrocyte membranes. Eur. J. Biochem. 1976, 71:177-184.
    • (1976) Eur. J. Biochem. , vol.71 , pp. 177-184
    • Zenner, H.P.1    Pfeuffer, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.