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Volumn 11, Issue , 2017, Pages

Dysregulation of microtubule stability impairs morphofunctional connectivity in primary neuronal networks

Author keywords

High content microscopy; Live cell imaging; Microtubule; Neuronal network; P301L; Primary hippocampal neuron; Synapse; Tau aggregation

Indexed keywords

EPOTHILONE D; NOCODAZOLE; PACLITAXEL; TAU PROTEIN;

EID: 85021443211     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2017.00173     Document Type: Article
Times cited : (18)

References (77)
  • 1
    • 84884321808 scopus 로고    scopus 로고
    • Taxane-and epothilone-based chemotherapy: From molecule cargo cytoskeletal logistics to management of castration-resistant prostate carcinoma
    • Alberti, C. (2013). Taxane-and epothilone-based chemotherapy: from molecule cargo cytoskeletal logistics to management of castration-resistant prostate carcinoma. Eur. Rev. Med. Pharmacol. Sci. 17, 1658-1664.
    • (2013) Eur. Rev. Med. Pharmacol. Sci , vol.17 , pp. 1658-1664
    • Alberti, C.1
  • 2
    • 33750607448 scopus 로고    scopus 로고
    • Microtubule stabilizer ameliorates synaptic function and behavior in a mouse model for schizophrenia
    • Andrieux, A., Salin, P., Schweitzer, A., Begou, M., Pachoud, B., Brun, P., et al. (2006). Microtubule stabilizer ameliorates synaptic function and behavior in a mouse model for schizophrenia. Biol. Psychiatry 60, 1224-1230. doi:10.1016/j.biopsych.2006.03.048
    • (2006) Biol. Psychiatry , vol.60 , pp. 1224-1230
    • Andrieux, A.1    Salin, P.2    Schweitzer, A.3    Begou, M.4    Pachoud, B.5    Brun, P.6
  • 3
    • 85007614141 scopus 로고    scopus 로고
    • Increased susceptibility to Abeta toxicity in neuronal cultures derived from familial Alzheimer’s disease (PSEN1-A246E) induced pluripotent stem cells
    • Armijo, E., Gonzalez, C., Shahnawaz, M., Flores, A., Davis, B., and Soto, C. (2017). Increased susceptibility to Abeta toxicity in neuronal cultures derived from familial Alzheimer’s disease (PSEN1-A246E) induced pluripotent stem cells. Neurosci. Lett. 639, 74-81. doi:10.1016/j.neulet.2016.12.060
    • (2017) Neurosci. Lett , vol.639 , pp. 74-81
    • Armijo, E.1    Gonzalez, C.2    Shahnawaz, M.3    Flores, A.4    Davis, B.5    Soto, C.6
  • 4
    • 69249100953 scopus 로고    scopus 로고
    • Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses
    • Aslund, A., Sigurdson, C. J., Klingstedt, T., Grathwohl, S., Bolmont, T., Dickstein, D. L., et al. (2009). Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses. ACS Chem. Biol. 4, 673-684. doi:10.1021/cb900112v
    • (2009) ACS Chem. Biol , vol.4 , pp. 673-684
    • Aslund, A.1    Sigurdson, C.J.2    Klingstedt, T.3    Grathwohl, S.4    Bolmont, T.5    Dickstein, D.L.6
  • 5
    • 0026561904 scopus 로고
    • The plus ends of stable microtubules are the exclusive nucleating structures for microtubules in the axon
    • Baas, P.W., and Ahmad, F. J. (1992). The plus ends of stable microtubules are the exclusive nucleating structures for microtubules in the axon. J. Cell Biol. 116, 1231-1241. doi:10.1083/jcb.116.5.1231
    • (1992) J. Cell Biol , vol.116 , pp. 1231-1241
    • Baas, P.W.1    Ahmad, F.J.2
  • 6
    • 84986564735 scopus 로고    scopus 로고
    • Stability properties of neuronal microtubules
    • Baas, P. W., Rao, A. N., Matamoros, A. J., and Leo, L. (2016). Stability properties of neuronal microtubules. Cytoskeleton (Hoboken). 73, 442-460. doi:10.1002/cm.21286
    • (2016) Cytoskeleton (Hoboken) , vol.73 , pp. 442-460
    • Baas, P.W.1    Rao, A.N.2    Matamoros, A.J.3    Leo, L.4
  • 7
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S., Zheng-Fischhofer, Q., Ackmann, M., Biernat, J., von Bergen, M., Mandelkow, E.M., et al. (2000). Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39, 11714-11721. doi:10.1021/bi000850r
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1    Zheng-Fischhofer, Q.2    Ackmann, M.3    Biernat, J.4    Von Bergen, M.5    Mandelkow, E.M.6
  • 8
    • 84861313192 scopus 로고    scopus 로고
    • Hyperdynamic microtubules, cognitive deficits, and pathology are improved in tau transgenic mice with low doses of the microtubule-stabilizing agent BMS-241027
    • Barten, D. M., Fanara, P., Andorfer, C., Hoque, N., Wong, P. Y., Husted, K. H., et al. (2012). Hyperdynamic microtubules, cognitive deficits, and pathology are improved in tau transgenic mice with low doses of the microtubule-stabilizing agent BMS-241027. J. Neurosci. 32, 7137-7145. doi:10.1523/JNEUROSCI.0188-12.2012
    • (2012) J. Neurosci , vol.32 , pp. 7137-7145
    • Barten, D.M.1    Fanara, P.2    Orfer, C.3    Hoque, N.4    Wong, P.Y.5    Husted, K.H.6
  • 9
    • 84930625091 scopus 로고    scopus 로고
    • The fluorescent pentameric oligothiophene pFTAA identifies filamentous tau in live neurons cultured from adult P301S tau mice
    • Brelstaff, J., Ossola, B., Neher, J. J., Klingstedt, T., Nilsson, K. P., Goedert, M., et al. (2015). The fluorescent pentameric oligothiophene pFTAA identifies filamentous tau in live neurons cultured from adult P301S tau mice. Front. Neurosci. 9:184. doi:10.3389/fnins.2015.00184
    • (2015) Front. Neurosci , vol.9 , pp. 184
    • Brelstaff, J.1    Ossola, B.2    Neher, J.J.3    Klingstedt, T.4    Nilsson, K.P.5    Goedert, M.6
  • 10
    • 79951814364 scopus 로고    scopus 로고
    • The characterization of microtubule-stabilizing drugs as possible therapeutic agents for Alzheimer’s disease and related tauopathies
    • Brunden, K. R., Yao, Y., Potuzak, J. S., Ferrer, N. I., Ballatore, C., James, M. J., et al. (2011). The characterization of microtubule-stabilizing drugs as possible therapeutic agents for Alzheimer’s disease and related tauopathies. Pharmacol. Res. 63, 341-351. doi:10.1016/j.phrs.2010.12.002
    • (2011) Pharmacol. Res , vol.63 , pp. 341-351
    • Brunden, K.R.1    Yao, Y.2    Potuzak, J.S.3    Ferrer, N.I.4    Ballatore, C.5    James, M.J.6
  • 11
    • 77958065504 scopus 로고    scopus 로고
    • Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy
    • Brunden, K. R., Zhang, B., Carroll, J., Yao, Y., Potuzak, J. S., Hogan, A. M., et al. (2010). Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J. Neurosci. 30, 13861-13866. doi:10.1523/JNEUROSCI.3059-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 13861-13866
    • Brunden, K.R.1    Zhang, B.2    Carroll, J.3    Yao, Y.4    Potuzak, J.S.5    Hogan, A.M.6
  • 12
    • 84929951298 scopus 로고    scopus 로고
    • Synaptic contacts enhance cell-to-cell tau pathology propagation
    • Calafate, S., Buist, A., Miskiewicz, K., Vijayan, V., Daneels, G., de Strooper, B., et al. (2015). Synaptic contacts enhance cell-to-cell tau pathology propagation. Cell Rep. 11, 1176-1183. doi:10.1016/j.celrep.2015.04.043
    • (2015) Cell Rep , vol.11 , pp. 1176-1183
    • Calafate, S.1    Buist, A.2    Miskiewicz, K.3    Vijayan, V.4    Daneels, G.5    De Strooper, B.6
  • 13
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland, D. W., Hwo, S. Y., and Kirschner, M. W. (1977). Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J.Mol. Biol. 116, 207-225. doi:10.1016/0022-2836(77)90213-3
    • (1977) J.Mol. Biol , vol.116 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 14
    • 84880767690 scopus 로고    scopus 로고
    • Quantitation of chronic and acute treatment effects on neuronal network activity using image and signal analysis: Toward a highcontent assay
    • Cornelissen, F., Verstraelen, P., Verbeke, T., Pintelon, I., Timmermans, J. P., Nuydens, R., et al. (2013). Quantitation of chronic and acute treatment effects on neuronal network activity using image and signal analysis: toward a highcontent assay. J. Biomol. Screen. 18, 807-819. doi:10.1177/1087057113486518
    • (2013) J. Biomol. Screen , vol.18 , pp. 807-819
    • Cornelissen, F.1    Verstraelen, P.2    Verbeke, T.3    Pintelon, I.4    Timmermans, J.P.5    Nuydens, R.6
  • 15
    • 84883503648 scopus 로고    scopus 로고
    • Are tau aggregates toxic or protective in tauopathies?
    • Cowan, C. M., and Mudher, A. (2013). Are tau aggregates toxic or protective in tauopathies? Front. Neurol. 4:114. doi:10.3389/fneur.2013.00114
    • (2013) Front. Neurol , vol.4 , pp. 114
    • Cowan, C.M.1    Mudher, A.2
  • 16
    • 0033042978 scopus 로고    scopus 로고
    • Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation
    • Dayanandan, R., Van Slegtenhorst, M., Mack, T. G., Ko, L., Yen, S. H., Leroy, K., et al. (1999). Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation. FEBS Lett. 446, 228-232. doi:10.1016/S0014-5793(99)00222-7
    • (1999) FEBS Lett , vol.446 , pp. 228-232
    • Dayanandan, R.1    Van Slegtenhorst, M.2    Mack, T.G.3    Ko, L.4    Yen, S.H.5    Leroy, K.6
  • 17
    • 85008178956 scopus 로고    scopus 로고
    • Of microtubules and memory: Implications for microtubule dynamics in dendrites and spines
    • Dent, E. W. (2017). Of microtubules and memory: implications for microtubule dynamics in dendrites and spines. Mol. Biol. Cell 28, 1-8. doi:10.1091/mbc.E15-11-0769
    • (2017) Mol. Biol. Cell , vol.28 , pp. 1-8
    • Dent, E.W.1
  • 18
    • 84897993752 scopus 로고    scopus 로고
    • Microtubules in neurons as information carriers
    • Dent, E. W., and Baas, P. W. (2014). Microtubules in neurons as information carriers. J. Neurochem. 129, 235-239. doi:10.1111/jnc.12621
    • (2014) J. Neurochem , vol.129 , pp. 235-239
    • Dent, E.W.1    Baas, P.W.2
  • 20
    • 0033982344 scopus 로고    scopus 로고
    • Missense tau mutations identified in FTDP-17 have a small effect on tau-microtubule interactions
    • DeTure, M., Ko, L. W., Yen, S., Nacharaju, P., Easson, C., Lewis, J., et al. (2000). Missense tau mutations identified in FTDP-17 have a small effect on tau-microtubule interactions. Brain Res. 853, 5-14. doi:10.1016/S0006-8993(99)02124-1
    • (2000) Brain Res , vol.853 , pp. 5-14
    • Deture, M.1    Ko, L.W.2    Yen, S.3    Nacharaju, P.4    Easson, C.5    Lewis, J.6
  • 21
    • 74049110106 scopus 로고    scopus 로고
    • High content image cytometry in the context of subnuclear organization
    • De Vos, W. H., Van Neste, L., Dieriks, B., Joss, G. H., and Van Oostveldt, P. (2010). High content image cytometry in the context of subnuclear organization. Cytometry A 77, 64-75. doi:10.1002/cyto.a.20807
    • (2010) Cytometry A , vol.77 , pp. 64-75
    • De Vos, W.H.1    Van Neste, L.2    Dieriks, B.3    Joss, G.H.4    Van Oostveldt, P.5
  • 22
    • 84861604521 scopus 로고
    • Multiple comparisons using rank sums
    • Dunn, O. J. (1964). Multiple comparisons using rank sums. Technometrics 6, 241-252. doi:10.1080/00401706.1964.10490181
    • (1964) Technometrics , vol.6 , pp. 241-252
    • Dunn, O.J.1
  • 23
    • 84903215603 scopus 로고    scopus 로고
    • March separate, strike together-role of phosphorylated TAU in mitochondrial dysfunction in Alzheimer’s disease
    • Eckert, A., Nisbet, R., Grimm, A., and Gotz, J. (2014). March separate, strike together-role of phosphorylated TAU in mitochondrial dysfunction in Alzheimer’s disease. Biochim. Biophys. Acta 1842, 1258-1266. doi:10.1016/j.bbadis.2013.08.013
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 1258-1266
    • Eckert, A.1    Nisbet, R.2    Grimm, A.3    Gotz, J.4
  • 24
    • 84893647317 scopus 로고    scopus 로고
    • Rescue of tau-induced synaptic transmission pathology by paclitaxel
    • Erez, H., Shemesh, O. A., and Spira, M. E. (2014). Rescue of tau-induced synaptic transmission pathology by paclitaxel. Front. Cell. Neurosci. 8:34. doi:10.3389/fncel.2014.00034
    • (2014) Front. Cell. Neurosci , vol.8 , pp. 34
    • Erez, H.1    Shemesh, O.A.2    Spira, M.E.3
  • 25
    • 33947261950 scopus 로고    scopus 로고
    • Structural and microtubule binding properties of tau mutants of frontotemporal dementias
    • Fischer, D., Mukrasch, M. D., von Bergen, M., Klos-Witkowska, A., Biernat, J., Griesinger, C., et al. (2007). Structural and microtubule binding properties of tau mutants of frontotemporal dementias. Biochemistry 46, 2574-2582. doi:10.1021/bi061318s
    • (2007) Biochemistry , vol.46 , pp. 2574-2582
    • Fischer, D.1    Mukrasch, M.D.2    Von Bergen, M.3    Klos-Witkowska, A.4    Biernat, J.5    Griesinger, C.6
  • 26
    • 84899474632 scopus 로고    scopus 로고
    • Activity-dependent tau protein translocation to excitatory synapse is disrupted by exposure to amyloid-beta oligomers
    • Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., et al. (2014). Activity-dependent tau protein translocation to excitatory synapse is disrupted by exposure to amyloid-beta oligomers. J. Neurosci. 34, 6084-6097. doi:10.1523/JNEUROSCI.4261-13.2014
    • (2014) J. Neurosci , vol.34 , pp. 6084-6097
    • Frandemiche, M.L.1    De Seranno, S.2    Rush, T.3    Borel, E.4    Elie, A.5    Arnal, I.6
  • 27
    • 84896719812 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration through global chromatin relaxation
    • Frost, B., Hemberg, M., Lewis, J., and Feany, M. B. (2014). Tau promotes neurodegeneration through global chromatin relaxation. Nat. Neurosci. 17, 357-366. doi:10.1038/nn.3639
    • (2014) Nat. Neurosci , vol.17 , pp. 357-366
    • Frost, B.1    Hemberg, M.2    Lewis, J.3    Feany, M.B.4
  • 28
    • 78650660972 scopus 로고    scopus 로고
    • The microtubule cytoskeleton acts as a key downstream effector of neurotransmitter signaling
    • Gardiner, J., Overall, R., and Marc, J. (2011). The microtubule cytoskeleton acts as a key downstream effector of neurotransmitter signaling. Synapse 65, 249-256. doi:10.1002/syn.20841
    • (2011) Synapse , vol.65 , pp. 249-256
    • Gardiner, J.1    Overall, R.2    Marc, J.3
  • 29
    • 84886583599 scopus 로고    scopus 로고
    • The paradox of paclitaxel neurotoxicity: Mechanisms and unanswered questions
    • Gornstein, E., and Schwarz, T. L. (2014). The paradox of paclitaxel neurotoxicity: mechanisms and unanswered questions. Neuropharmacology 76(Pt A), 175-183. doi:10.1016/j.neuropharm.2013.08.016
    • (2014) Neuropharmacology , vol.76 , pp. 175-183
    • Gornstein, E.1    Schwarz, T.L.2
  • 30
    • 84954047109 scopus 로고    scopus 로고
    • Tau oligomers: The toxic player at synapses in Alzheimer’s disease
    • Guerrero-Munoz, M. J., Gerson, J., and Castillo-Carranza, D. L. (2015). Tau oligomers: the toxic player at synapses in Alzheimer’s disease. Front. Cell. Neurosci. 9:464. doi:10.3389/fncel.2015.00464
    • (2015) Front. Cell. Neurosci , vol.9 , pp. 464
    • Guerrero-Munoz, M.J.1    Gerson, J.2    Castillo-Carranza, D.L.3
  • 31
    • 84875218639 scopus 로고    scopus 로고
    • Neurofibrillary tangle-like tau pathology induced by synthetic tau fibrils in primary neurons over-expressing mutant tau
    • Guo, J. L., and Lee, V.M. (2013). Neurofibrillary tangle-like tau pathology induced by synthetic tau fibrils in primary neurons over-expressing mutant tau. FEBS Lett. 587, 717-723. doi:10.1016/j.febslet.2013.01.051
    • (2013) FEBS Lett , vol.587 , pp. 717-723
    • Guo, J.L.1    Lee, V.M.2
  • 32
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo, J. L., and Lee, V. M. (2014). Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat. Med. 20, 130-138. doi:10.1038/nm.3457
    • (2014) Nat. Med , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.2
  • 33
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17
    • Hong, M., Zhukareva, V., Vogelsberg-Ragaglia, V., Wszolek, Z., Reed, L., Miller, B. I., et al. (1998). Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 282, 1914-1917. doi:10.1126/science.282.5395.1914
    • (1998) Science , vol.282 , pp. 1914-1917
    • Hong, M.1    Zhukareva, V.2    Vogelsberg-Ragaglia, V.3    Wszolek, Z.4    Reed, L.5    Miller, B.I.6
  • 34
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., et al. (2010). Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron 68, 1067-1081. doi:10.1016/j.neuron.2010.11.030
    • (2010) Neuron , vol.68 , pp. 1067-1081
    • Hoover, B.R.1    Reed, M.N.2    Su, J.3    Penrod, R.D.4    Kotilinek, L.A.5    Grant, M.K.6
  • 35
    • 84155167955 scopus 로고    scopus 로고
    • Mechanisms in cancer-chemotherapeutic drugs-induced peripheral neuropathy
    • Jaggi, A. S., and Singh, N. (2012). Mechanisms in cancer-chemotherapeutic drugs-induced peripheral neuropathy. Toxicology 291, 1-9. doi:10.1016/j.tox.2011.10.019
    • (2012) Toxicology , vol.291 , pp. 1-9
    • Jaggi, A.S.1    Singh, N.2
  • 36
    • 58149214025 scopus 로고    scopus 로고
    • Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity
    • Jaworski, J., Kapitein, L. C., Gouveia, S. M., Dortland, B. R., Wulf, P. S., Grigoriev, I., et al. (2009). Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity. Neuron 61, 85-100. doi:10.1016/j.neuron.2008.11.013
    • (2009) Neuron , vol.61 , pp. 85-100
    • Jaworski, J.1    Kapitein, L.C.2    Gouveia, S.M.3    Dortland, B.R.4    Wulf, P.S.5    Grigoriev, I.6
  • 37
    • 84935895529 scopus 로고    scopus 로고
    • Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
    • Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., et al. (2015). Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proc. Natl. Acad. Sci. U.S.A. 112, 7501-7506. doi:10.1073/pnas.1504081112
    • (2015) Proc. Natl. Acad. Sci. U.S.A. , vol.112 , pp. 7501-7506
    • Kadavath, H.1    Hofele, R.V.2    Biernat, J.3    Kumar, S.4    Tepper, K.5    Urlaub, H.6
  • 38
    • 84938594437 scopus 로고    scopus 로고
    • Building the neuronal microtubule cytoskeleton
    • Kapitein, L. C., and Hoogenraad, C. C. (2015). Building the neuronal microtubule cytoskeleton. Neuron 87, 492-506. doi:10.1016/j.neuron.2015.05.046
    • (2015) Neuron , vol.87 , pp. 492-506
    • Kapitein, L.C.1    Hoogenraad, C.C.2
  • 39
    • 84940172441 scopus 로고    scopus 로고
    • Microtechnologies for studying the role of mechanics in axon growth and guidance
    • Kilinc, D., Blasiak, A., and Lee, G. U. (2015). Microtechnologies for studying the role of mechanics in axon growth and guidance. Front. Cell. Neurosci. 9:282. doi:10.3389/fncel.2015.00282
    • (2015) Front. Cell. Neurosci , vol.9 , pp. 282
    • Kilinc, D.1    Blasiak, A.2    Lee, G.U.3
  • 40
    • 84942769755 scopus 로고    scopus 로고
    • Tau neurotoxicity and rescue in animal models of human Tauopathies
    • Kruger, L., and Mandelkow, E. M. (2016). Tau neurotoxicity and rescue in animal models of human Tauopathies. Curr. Opin. Neurobiol. 36, 52-58. doi:10.1016/j.conb.2015.09.004
    • (2016) Curr. Opin. Neurobiol , vol.36 , pp. 52-58
    • Kruger, L.1    Mandelkow, E.M.2
  • 41
    • 84994528824 scopus 로고    scopus 로고
    • Sustained synchronized neuronal network activity in a human astrocyte co-culture system
    • Kuijlaars, J., Oyelami, T., Diels, A., Rohrbacher, J., Versweyveld, S., Meneghello, G., et al. (2016). Sustained synchronized neuronal network activity in a human astrocyte co-culture system. Sci. Rep. 6:36529. doi:10.1038/srep36529
    • (2016) Sci. Rep , vol.6 , pp. 36529
    • Kuijlaars, J.1    Oyelami, T.2    Diels, A.3    Rohrbacher, J.4    Versweyveld, S.5    Meneghello, G.6
  • 42
    • 84869102343 scopus 로고    scopus 로고
    • Translocation of CaMKII to dendritic microtubules supports the plasticity of local synapses
    • Lemieux, M., Labrecque, S., Tardif, C., Labrie-Dion, E., Lebel, E., and De Koninck, P. (2012). Translocation of CaMKII to dendritic microtubules supports the plasticity of local synapses. J. Cell Biol. 198, 1055-1073. doi:10.1083/jcb.201202058
    • (2012) J. Cell Biol , vol.198 , pp. 1055-1073
    • Lemieux, M.1    Labrecque, S.2    Tardif, C.3    Labrie-Dion, E.4    Lebel, E.5    De Koninck, P.6
  • 43
    • 0035181835 scopus 로고    scopus 로고
    • Competition for microtubulebinding withdual expression of tau missense and splice isoforms
    • Lu, M., Orecchio, L. D., and Kosik, K. S. (2000). Competition for microtubulebinding withdual expression of tau missense and splice isoforms. Mol. Biol. Cell 11, 363a-363a. doi:10.1091/mbc.12.1.171
    • (2000) Mol. Biol. Cell , vol.11 , pp. 363a-363a
    • Lu, M.1    Orecchio, L.D.2    Kosik, K.S.3
  • 44
    • 0027418205 scopus 로고
    • Measurement of colocalization of objects in dual-colour confocal images
    • Manders, E. M. M., Verbeek, F. J., and Aten, J. A. (1993). Measurement of colocalization of objects in dual-colour confocal images. J. Microsc. 169, 375-382. doi:10.1111/j.1365-2818.1993.tb03313.x
    • (1993) J. Microsc , vol.169 , pp. 375-382
    • Manders, E.M.M.1    Verbeek, F.J.2    Aten, J.A.3
  • 45
    • 84970965915 scopus 로고    scopus 로고
    • Microtubule and microtubule associated protein anomalies in psychiatric disease
    • Marchisella, F., Coffey, E. T., and Hollos, P. (2016). Microtubule and microtubule associated protein anomalies in psychiatric disease. Cytoskeleton 73, 596-611. doi:10.1002/cm.21300
    • (2016) Cytoskeleton , vol.73 , pp. 596-611
    • Marchisella, F.1    Coffey, E.T.2    Hollos, P.3
  • 46
    • 84925351605 scopus 로고    scopus 로고
    • A nanoscale resolution view on synaptic vesicle dynamics
    • Maschi, D., and Klyachko, V. A. (2015). A nanoscale resolution view on synaptic vesicle dynamics. Synapse 69, 256-267. doi:10.1002/syn.21795
    • (2015) Synapse , vol.69 , pp. 256-267
    • Maschi, D.1    Klyachko, V.A.2
  • 47
    • 84994008627 scopus 로고    scopus 로고
    • Microtubules in health and degenerative disease of the nervous system
    • Matamoros, A. J., and Baas, P. W. (2016). Microtubules in health and degenerative disease of the nervous system. Brain Res. Bull. 126(Pt 3), 217-225. doi:10.1016/j.brainresbull.2016.06.016
    • (2016) Brain Res. Bull , vol.126 , pp. 217-225
    • Matamoros, A.J.1    Baas, P.W.2
  • 48
    • 84925012440 scopus 로고    scopus 로고
    • Signaling to the microtubule cytoskeleton: An unconventional role for CaMKII
    • McVicker, D. P., Millette, M. M., and Dent, E. W. (2015). Signaling to the microtubule cytoskeleton: an unconventional role for CaMKII. Dev. Neurobiol. 75, 423-434. doi:10.1002/dneu.22227
    • (2015) Dev. Neurobiol , vol.75 , pp. 423-434
    • McVicker, D.P.1    Millette, M.M.2    Dent, E.W.3
  • 49
    • 85012065303 scopus 로고    scopus 로고
    • New features about tau function and dysfunction
    • Medina, M., Hernandez, F., and Avila, J. (2016). New features about tau function and dysfunction. Biomolecules 6:E21 doi:10.3390/biom6020021
    • (2016) Biomolecules , vol.6
    • Medina, M.1    Hernandez, F.2    Avila, J.3
  • 50
    • 84955056016 scopus 로고    scopus 로고
    • Pathological tau promotes neuronal damage by impairing ribosomal function and decreasing protein synthesis
    • Meier, S., Bell, M., Lyons, D. N., Rodriguez-Rivera, J., Ingram, A., Fontaine, S. N., et al. (2016). Pathological tau promotes neuronal damage by impairing ribosomal function and decreasing protein synthesis. J. Neurosci. 36, 1001-1007. doi:10.1523/JNEUROSCI.3029-15.2016
    • (2016) J. Neurosci , vol.36 , pp. 1001-1007
    • Meier, S.1    Bell, M.2    Lyons, D.N.3    Rodriguez-Rivera, J.4    Ingram, A.5    Fontaine, S.N.6
  • 51
    • 84885454518 scopus 로고    scopus 로고
    • Synaptic regulation of microtubule dynamics in dendritic spines by calcium, F-actin, and drebrin
    • Merriam, E. B., Millette, M., Lumbard, D. C., Saengsawang, W., Fothergill, T., Hu, X., et al. (2013). Synaptic regulation of microtubule dynamics in dendritic spines by calcium, F-actin, and drebrin. J. Neurosci. 33, 16471-16482. doi:10.1523/JNEUROSCI.0661-13.2013
    • (2013) J. Neurosci , vol.33 , pp. 16471-16482
    • Merriam, E.B.1    Millette, M.2    Lumbard, D.C.3    Saengsawang, W.4    Fothergill, T.5    Hu, X.6
  • 53
    • 21644446496 scopus 로고    scopus 로고
    • Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions
    • Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., and Zweckstetter, M. (2005). Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions. J. Biol. Chem. 280, 24978-24986. doi:10.1074/jbc.M501565200
    • (2005) J. Biol. Chem , vol.280 , pp. 24978-24986
    • Mukrasch, M.D.1    Biernat, J.2    Von Bergen, M.3    Griesinger, C.4    Mandelkow, E.5    Zweckstetter, M.6
  • 55
    • 84971299957 scopus 로고    scopus 로고
    • Efficient introduction of specific homozygous and heterozygous mutations using CRISPR/Cas9
    • Paquet, D., Kwart, D., Chen, A., Sproul, A., Jacob, S., Teo, S., et al. (2016). Efficient introduction of specific homozygous and heterozygous mutations using CRISPR/Cas9. Nature 533, 125-129. doi:10.1038/nature17664
    • (2016) Nature , vol.533 , pp. 125-129
    • Paquet, D.1    Kwart, D.2    Chen, A.3    Sproul, A.4    Jacob, S.5    Teo, S.6
  • 56
    • 54049120586 scopus 로고    scopus 로고
    • Discrimination of cell types in mixed cortical culture using calcium imaging: A comparison to immunocytochemical labeling
    • Pickering, M., Pickering, B. W., Murphy, K. J., and O’Connor, J. J. (2008). Discrimination of cell types in mixed cortical culture using calcium imaging: a comparison to immunocytochemical labeling. J. Neurosci. Methods 173, 27-33. doi:10.1016/j.jneumeth.2008.05.014
    • (2008) J. Neurosci. Methods , vol.173 , pp. 27-33
    • Pickering, M.1    Pickering, B.W.2    Murphy, K.J.3    O’Connor, J.J.4
  • 58
    • 84925858509 scopus 로고    scopus 로고
    • Tau Phosphorylation at serine 396 residue is required for hippocampal LTD
    • Regan, P., Piers, T., Yi, J. H., Kim, D. H., Huh, S., Park, S. J., et al. (2015). Tau Phosphorylation at serine 396 residue is required for hippocampal LTD. J. Neurosci. 35, 4804-4812. doi:10.1523/JNEUROSCI.2842-14.2015
    • (2015) J. Neurosci , vol.35 , pp. 4804-4812
    • Regan, P.1    Piers, T.2    Yi, J.H.3    Kim, D.H.4    Huh, S.5    Park, S.J.6
  • 59
    • 84928035433 scopus 로고    scopus 로고
    • Tau regulates the localization and function of End-binding proteins 1 and 3 in developing neuronal cells
    • Sayas, C. L., Tortosa, E., Bollati, F., Ramirez-Rios, S., Arnal, I., and Avila, J. (2015). Tau regulates the localization and function of End-binding proteins 1 and 3 in developing neuronal cells. J. Neurochem. 133, 653-667. doi:10.1111/jnc.13091
    • (2015) J. Neurochem , vol.133 , pp. 653-667
    • Sayas, C.L.1    Tortosa, E.2    Bollati, F.3    Ramirez-Rios, S.4    Arnal, I.5    Avila, J.6
  • 61
    • 79955952344 scopus 로고    scopus 로고
    • Rescue of neurons from undergoing hallmark tau-induced Alzheimer’s disease cell pathologies by the antimitotic drug paclitaxel
    • Shemesh, O. A., and Spira, M. E. (2011). Rescue of neurons from undergoing hallmark tau-induced Alzheimer’s disease cell pathologies by the antimitotic drug paclitaxel. Neurobiol. Dis. 43, 163-175. doi:10.1016/j.nbd.2011.03.008
    • (2011) Neurobiol. Dis , vol.43 , pp. 163-175
    • Shemesh, O.A.1    Spira, M.E.2
  • 62
    • 78549275132 scopus 로고    scopus 로고
    • Three-and four-repeat Tau coassemble into heterogeneous filaments: An implication for Alzheimer disease
    • Siddiqua, A., and Margittai, M. (2010). Three-and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease. J. Biol. Chem. 285, 37920-37926. doi:10.1074/jbc.M110.185728
    • (2010) J. Biol. Chem , vol.285 , pp. 37920-37926
    • Siddiqua, A.1    Margittai, M.2
  • 63
    • 0000441073 scopus 로고
    • A multiple comparison rank sum test: Treatments versus control
    • Steel, R. G. D. (1959). A multiple comparison rank sum test: treatments versus control. Biometrics 15, 560-572. doi:10.2307/2527654
    • (1959) Biometrics , vol.15 , pp. 560-572
    • Steel, R.G.D.1
  • 64
    • 0345701251 scopus 로고    scopus 로고
    • Visualization of microtubule growth in cultured neurons via the use of EB3-GFP (End-binding protein 3-green fluorescent protein)
    • Stepanova, T., Slemmer, J., Hoogenraad, C. C., Lansbergen, G., Dortland, B., De Zeeuw, C. I., et al. (2003). Visualization of microtubule growth in cultured neurons via the use of EB3-GFP (end-binding protein 3-green fluorescent protein). J. Neurosci. 23, 2655-2664. doi:10.3410/f.1015054.195569
    • (2003) J. Neurosci , vol.23 , pp. 2655-2664
    • Stepanova, T.1    Slemmer, J.2    Hoogenraad, C.C.3    Lansbergen, G.4    Dortland, B.5    De Zeeuw, C.I.6
  • 65
    • 84883279162 scopus 로고    scopus 로고
    • Beta-synuclein aggregates and induces neurodegeneration in dopaminergic neurons
    • Taschenberger, G., Toloe, J., Tereshchenko, J., Akerboom, J., Wales, P., Benz, R., et al. (2013). beta-synuclein aggregates and induces neurodegeneration in dopaminergic neurons. Ann. Neurol. 74, 109-118. doi:10.1002/ana.23905
    • (2013) Ann. Neurol , vol.74 , pp. 109-118
    • Taschenberger, G.1    Toloe, J.2    Tereshchenko, J.3    Akerboom, J.4    Wales, P.5    Benz, R.6
  • 66
    • 13644268449 scopus 로고    scopus 로고
    • Changed conformation of mutant Tau-P301L underlies the moribund tauopathy, absent in progressive, nonlethal axonopathy of Tau-4R/2N transgenic mice
    • Terwel, D., Lasrado, R., Snauwaert, J., Vandeweert, E., Van Haesendonck, C., Borghgraef, P., et al. (2005). Changed conformation of mutant Tau-P301L underlies the moribund tauopathy, absent in progressive, nonlethal axonopathy of Tau-4R/2N transgenic mice. J. Biol. Chem. 280, 3963-3973. doi:10.1074/jbc.M409876200
    • (2005) J. Biol. Chem , vol.280 , pp. 3963-3973
    • Terwel, D.1    Lasrado, R.2    Snauwaert, J.3    Vandeweert, E.4    Van Haesendonck, C.5    Borghgraef, P.6
  • 67
    • 84947266958 scopus 로고    scopus 로고
    • Risperidone and NAP protect cognition and normalize gene expression in a schizophrenia mouse model
    • Vaisburd, S., Shemer, Z., Yeheskel, A., Giladi, E., and Gozes, I. (2015). Risperidone and NAP protect cognition and normalize gene expression in a schizophrenia mouse model. Sci. Rep. 5:16300. doi:10.1038/srep16300
    • (2015) Sci. Rep , vol.5 , pp. 16300
    • Vaisburd, S.1    Shemer, Z.2    Yeheskel, A.3    Giladi, E.4    Gozes, I.5
  • 68
    • 84858123747 scopus 로고    scopus 로고
    • Molecular motors in cargo trafficking and synapse assembly
    • van den Berg, R., and Hoogenraad, C. C. (2012). Molecular motors in cargo trafficking and synapse assembly. Adv. Exp. Med. Biol. 970, 173-196. doi:10.1007/978-3-7091-0932-8_8
    • (2012) Adv. Exp. Med. Biol , vol.970 , pp. 173-196
    • Van Den Berg, R.1    Hoogenraad, C.C.2
  • 69
    • 84904096390 scopus 로고    scopus 로고
    • Pharmacological characterization of cultivated neuronal networks: Relevance to synaptogenesis and synaptic connectivity
    • Verstraelen, P., Pintelon, I., Nuydens, R., Cornelissen, F., Meert, T., and Timmermans, J. P. (2014). Pharmacological characterization of cultivated neuronal networks: relevance to synaptogenesis and synaptic connectivity. Cell. Mol. Neurobiol. 34, 757-776. doi:10.1007/s10571-014-0057-6
    • (2014) Cell. Mol. Neurobiol , vol.34 , pp. 757-776
    • Verstraelen, P.1    Pintelon, I.2    Nuydens, R.3    Cornelissen, F.4    Meert, T.5    Timmermans, J.P.6
  • 70
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure
    • von Bergen, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E. M., et al. (2001). Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J. Biol. Chem. 276, 48165-48174. doi:10.1074/jbc.M105196200
    • (2001) J. Biol. Chem , vol.276 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6
  • 71
    • 77954898295 scopus 로고    scopus 로고
    • Acute and late onset cognitive dysfunction associated with chemotherapy in women with breast cancer
    • Wefel, J. S., Saleeba, A. K., Buzdar, A. U., and Meyers, C. A. (2010). Acute and late onset cognitive dysfunction associated with chemotherapy in women with breast cancer. Cancer 116, 3348-3356. doi:10.1002/cncr.25098
    • (2010) Cancer , vol.116 , pp. 3348-3356
    • Wefel, J.S.1    Saleeba, A.K.2    Buzdar, A.U.3    Meyers, C.A.4
  • 73
    • 78651100112 scopus 로고    scopus 로고
    • Post-translational modifications of microtubules (Vol 123, pg 3447, 2010)
    • Wloga, D., and Gaertig, J. (2011). Post-translational modifications of microtubules (vol 123, pg 3447, 2010). J. Cell Sci. 124, 154-154. doi:10.1242/jcs.083576
    • (2011) J. Cell Sci , vol.124 , pp. 154
    • Wloga, D.1    Gaertig, J.2
  • 74
    • 0032933622 scopus 로고    scopus 로고
    • Taxol suppresses dynamics of individual microtubules in living human tumor cells
    • Yvon, A.M., Wadsworth, P., and Jordan, M. A. (1999). Taxol suppresses dynamics of individual microtubules in living human tumor cells. Mol. Biol. Cell 10, 947-959. doi:10.1091/mbc.10.4.947
    • (1999) Mol. Biol. Cell , vol.10 , pp. 947-959
    • Yvon, A.M.1    Wadsworth, P.2    Jordan, M.A.3
  • 75
    • 84954078732 scopus 로고    scopus 로고
    • Tau missorting and spastininduced microtubule disruption in neurodegeneration: Alzheimer Disease and Hereditary Spastic Paraplegia
    • Zempel, H., and Mandelkow, E.-M. (2015). Tau missorting and spastininduced microtubule disruption in neurodegeneration: Alzheimer Disease and Hereditary Spastic Paraplegia. Mol. Neurodegener. 10:68. doi:10.1186/s13024-015-0064-1
    • (2015) Mol. Neurodegener , vol.10 , pp. 68
    • Zempel, H.1    Mandelkow, E.-M.2
  • 76
    • 84863230105 scopus 로고    scopus 로고
    • The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice
    • Zhang, B., Carroll, J., Trojanowski, J. Q., Yao, Y., Iba, M., Potuzak, J. S., et al. (2012). The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J. Neurosci. 32, 3601-3611. doi:10.1523/JNEUROSCI.4922-11.2012
    • (2012) J. Neurosci , vol.32 , pp. 3601-3611
    • Zhang, B.1    Carroll, J.2    Trojanowski, J.Q.3    Yao, Y.4    Iba, M.5    Potuzak, J.S.6
  • 77
    • 80053371503 scopus 로고    scopus 로고
    • An expanded palette of genetically encoded Ca(2)(+) indicators
    • Zhao, Y., Araki, S., Wu, J., Teramoto, T., Chang, Y. F., Nakano, M., et al. (2011). An expanded palette of genetically encoded Ca(2)(+) indicators. Science 333, 1888-1891. doi:10.1126/science.1208592
    • (2011) Science , vol.333 , pp. 1888-1891
    • Zhao, Y.1    Araki, S.2    Wu, J.3    Teramoto, T.4    Chang, Y.F.5    Nakano, M.6


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