메뉴 건너뛰기




Volumn 15, Issue 6, 2004, Pages 2720-2728

Modulation of microtubule dynamics by tau in living cells: Implications for development and neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; TAU PROTEIN;

EID: 2542464892     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-01-0062     Document Type: Article
Times cited : (126)

References (57)
  • 1
    • 0036114344 scopus 로고    scopus 로고
    • Inflammation, apoptosis, and Alzheimer's disease
    • Bamberger, M.E., and Landreth, G.E. (2002). Inflammation, apoptosis, and Alzheimer's disease. Neuroscientist 8, 276-283.
    • (2002) Neuroscientist , vol.8 , pp. 276-283
    • Bamberger, M.E.1    Landreth, G.E.2
  • 2
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn, S., and Mandelkow, E. (2002). Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry 41, 14885-14896.
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 4
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner, K.A., and Kirschner, M.W. (1991). Tau protein binds to microtubules through a flexible array of distributed weak sites. J. Cell Biol. 115, 717-730.
    • (1991) J. Cell Biol. , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 5
    • 0025098891 scopus 로고
    • Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons
    • Caceres, A., and Kosik, K.S. (1990). Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 343, 461-463.
    • (1990) Nature , vol.343 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 6
    • 0032573083 scopus 로고    scopus 로고
    • Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17
    • Clark, L.N. et al. (1998). Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17. Proc. Natl. Acad. Sci. USA 95, 13103-13107.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13103-13107
    • Clark, L.N.1
  • 7
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland, D.W., Hwo, S.Y., and Kirschner, M.W. (1977). Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J. Mol. Biol. 116, 227-247.
    • (1977) J. Mol. Biol. , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 8
    • 0028924141 scopus 로고
    • Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins
    • Dhamodharan, R., and Wadsworth, P. (1995). Modulation of microtubule dynamic instability in vivo by brain microtubule associated proteins. J. Cell Sci. 108(Pt 4), 1679-1689.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 4 , pp. 1679-1689
    • Dhamodharan, R.1    Wadsworth, P.2
  • 9
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D.N., Hyman, A.A., Cobb, M.H., and Kirschner, M.W. (1992). Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 3, 1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 10
    • 0022395021 scopus 로고
    • Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors
    • Drubin, D.G., Feinstein, S.C., Shooter, E.M., and Kirschner, M.W. (1985). Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors. J. Mol. Biol. 101, 1799-1807.
    • (1985) J. Mol. Biol. , vol.101 , pp. 1799-1807
    • Drubin, D.G.1    Feinstein, S.C.2    Shooter, E.M.3    Kirschner, M.W.4
  • 11
    • 0033545946 scopus 로고    scopus 로고
    • Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements
    • D'Souza, I., Poorkaj, P., Hong, M., Nochlin, D., Lee, V.M., Bird, T.D., and Schellenberg, G.D. (1999). Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements. Proc. Natl. Acad. Sci. USA 96, 5598-5603.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5598-5603
    • D'Souza, I.1    Poorkaj, P.2    Hong, M.3    Nochlin, D.4    Lee, V.M.5    Bird, T.D.6    Schellenberg, G.D.7
  • 12
    • 0028316882 scopus 로고
    • Sense and antisense transfection analysis of tau function: Tau influences net microtubule assembly, neurite outgrowth and neuritic stability
    • Esmaeli-Azad, B., McCarty, J.H., and Feinstein, S.C. (1994). Sense and antisense transfection analysis of tau function: tau influences net microtubule assembly, neurite outgrowth and neuritic stability. J. Cell Sci. 107(Pt 4), 869-879.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 4 , pp. 869-879
    • Esmaeli-Azad, B.1    McCarty, J.H.2    Feinstein, S.C.3
  • 13
    • 0017646208 scopus 로고
    • Microtubule assembly in vitro. Purification of assembly-promoting factors
    • Fellous, A., Francon, J., Lennon, A.M., and Nunez, J. (1977). Microtubule assembly in vitro. Purification of assembly-promoting factors. Eur. J. Biochem. 78, 167-174.
    • (1977) Eur. J. Biochem. , vol.78 , pp. 167-174
    • Fellous, A.1    Francon, J.2    Lennon, A.M.3    Nunez, J.4
  • 14
    • 0347594304 scopus 로고    scopus 로고
    • Modeling tau polymerization in vitro: A review and synthesis
    • Gamblin, T.C., Berry, R.W., and Binder, L.I. (2003). Modeling tau polymerization in vitro: a review and synthesis. Biochemistry 42, 15009-15017.
    • (2003) Biochemistry , vol.42 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 15
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • Gamblin, T.C., King, M.E., Dawson, H., Vitek, M.P., Kuret, J., Berry, R.W., and Binder, L.I. (2000). In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry 39, 6136-6144.
    • (2000) Biochemistry , vol.39 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3    Vitek, M.P.4    Kuret, J.5    Berry, R.W.6    Binder, L.I.7
  • 16
    • 0035963277 scopus 로고    scopus 로고
    • Low concentrations of paclitaxel induce cell type-dependent p53, p21 and G1/G2 arrest instead of mitotic arrest: Molecular determinants of paclitaxel-induced cytotoxicity
    • Giannakakou, P., Robey, R., Fojo, T., and Blagosklonny, M.V. (2001). Low concentrations of paclitaxel induce cell type-dependent p53, p21 and G1/G2 arrest instead of mitotic arrest: molecular determinants of paclitaxel-induced cytotoxicity. Oncogene 20, 3806-3813.
    • (2001) Oncogene , vol.20 , pp. 3806-3813
    • Giannakakou, P.1    Robey, R.2    Fojo, T.3    Blagosklonny, M.V.4
  • 17
    • 0032950744 scopus 로고    scopus 로고
    • Tau gene mutation in familial progressive subcortical gliosis
    • Goedert, M. et al. (1999). Tau gene mutation in familial progressive subcortical gliosis. Nat Med 5, 454-457.
    • (1999) Nat. Med. , vol.5 , pp. 454-457
    • Goedert, M.1
  • 18
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert, M., Spillantini, M.G., Jakes, R., Rutherford, D., and Crowther, R.A. (1989a). Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 19
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert, M., Spillantini, M.G., Potier, M.C., Ulrich, J., and Crowther, R.A. (1989b). Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J. 8, 393-399.
    • (1989) EMBO J. , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 21
    • 0034624014 scopus 로고    scopus 로고
    • Structural and functional differences between 3-repeat and 4-repeat tau isoforms. Implications for normal tau function and the onset of neurodegenetative disease
    • Goode, B.L., Chau, M., Denis, P.E., and Feinstein, S.C. (2000). Structural and functional differences between 3-repeat and 4-repeat tau isoforms. Implications for normal tau function and the onset of neurodegenetative disease. J. Biol. Chem. 275, 38182-38189.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38182-38189
    • Goode, B.L.1    Chau, M.2    Denis, P.E.3    Feinstein, S.C.4
  • 22
    • 0031035402 scopus 로고    scopus 로고
    • Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly
    • Goode, B.L., Denis, P.E., Panda, D., Radeke, M.J., Miller, H.P., Wilson, L., and Feinstein, S.C. (1997). Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly. Mol. Biol. Cell 8, 353-365.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 353-365
    • Goode, B.L.1    Denis, P.E.2    Panda, D.3    Radeke, M.J.4    Miller, H.P.5    Wilson, L.6    Feinstein, S.C.7
  • 23
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • Goode, B.L., and Feinstein, S.C. (1994). Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau. J. Cell Biol. 124, 769-782.
    • (1994) J. Cell Biol. , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 24
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena, S., and Goldstein, L.S. (2001). Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron 32, 389-401.
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 27
    • 0018149343 scopus 로고
    • Radioimmunoassay for tubulin: A quantitative comparison of the tubulin content of different established tissue culture cells and tissues
    • Hiller, G., and Weber, K. (1978). Radioimmunoassay for tubulin: a quantitative comparison of the tubulin content of different established tissue culture cells and tissues. Cell 14, 795-804.
    • (1978) Cell , vol.14 , pp. 795-804
    • Hiller, G.1    Weber, K.2
  • 28
    • 0024498630 scopus 로고
    • Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family
    • Himmler, A. (1989). Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family. Mol. Cell. Biol. 9, 1389-1396.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1389-1396
    • Himmler, A.1
  • 29
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler, A., Drechsel, D., Kirschner, M.W., and Martin, D.W., Jr. (1989). Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol. Cell. Biol. 9, 1381-1388.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin Jr., D.W.4
  • 30
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17
    • Hong, M. et al. (1998). Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 282, 1914-1917.
    • (1998) Science , vol.282 , pp. 1914-1917
    • Hong, M.1
  • 31
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton, M. et al. (1998). Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702-705.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1
  • 32
    • 0036083301 scopus 로고    scopus 로고
    • Mechanism of action of antitumor drugs that interact with microtubules and tubulin
    • Jordan, M.A. (2002). Mechanism of action of antitumor drugs that interact with microtubules and tubulin. Curr. Med. Chem. Anti-Cancer Agents 2, 1-17.
    • (2002) Curr. Med. Chem. Anti-Cancer Agents , vol.2 , pp. 1-17
    • Jordan, M.A.1
  • 33
    • 0030020158 scopus 로고    scopus 로고
    • Mitotic block induced in HeLa cells by low concentrations of paclitaxel (Taxol) results in abnormal mitotic exit and apoptotic cell death
    • Jordan, M.A., Wendell, K., Gardiner, S., Derry, W.B., Copp, H., and Wilson, L. (1996). Mitotic block induced in HeLa cells by low concentrations of paclitaxel (Taxol) results in abnormal mitotic exit and apoptotic cell death. Cancer Res. 56, 816-825.
    • (1996) Cancer Res. , vol.56 , pp. 816-825
    • Jordan, M.A.1    Wendell, K.2    Gardiner, S.3    Derry, W.B.4    Copp, H.5    Wilson, L.6
  • 34
    • 0030462207 scopus 로고    scopus 로고
    • Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins
    • Kaech, S., Ludin, B., and Matus, A. (1996). Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins. Neuron 17, 1189-1199.
    • (1996) Neuron , vol.17 , pp. 1189-1199
    • Kaech, S.1    Ludin, B.2    Matus, A.3
  • 36
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik, K.S., Orecchio, L.D., Bakalis, S., and Neve, R.L. (1989). Developmentally regulated expression of specific tau sequences. Neuron 2, 1389-1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 37
    • 0030842531 scopus 로고    scopus 로고
    • Microinjection of antibodies into mammalian cells
    • Lamb, N.J., and Fernandez, A. (1997). Microinjection of antibodies into mammalian cells. Methods Enzymol. 283, 72-83.
    • (1997) Methods Enzymol. , vol.283 , pp. 72-83
    • Lamb, N.J.1    Fernandez, A.2
  • 39
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee, G., Cowan, N., and Kirschner, M. (1988). The primary structure and heterogeneity of tau protein from mouse brain. Science 239, 285-288.
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 40
    • 0028853922 scopus 로고
    • Functional implications for the microtubule-associated protein tau: Localization in oligodendrocytes
    • LoPresti, P., Szuchet, S., Papasozomenos, S.C., Zinkowski, R.P., and Binder, L.I. (1995). Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes. Proc. Natl. Acad. Sci. USA 92, 10369-10373.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10369-10373
    • LoPresti, P.1    Szuchet, S.2    Papasozomenos, S.C.3    Zinkowski, R.P.4    Binder, L.I.5
  • 41
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow, E.M., Stamer, K., Vogel, R., Thies, E., and Mandelkow, E. (2003). Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol. Aging 24, 1079-1085.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 42
    • 0036931159 scopus 로고    scopus 로고
    • Tau neurofibrillary pathology and microtubule stability
    • Michaelis, M.L., Dobrowsky, R.T., and Li, G. (2002). Tau neurofibrillary pathology and microtubule stability. J. Mol. Neurosci. 19, 289-293.
    • (2002) J. Mol. Neurosci. , vol.19 , pp. 289-293
    • Michaelis, M.L.1    Dobrowsky, R.T.2    Li, G.3
  • 43
    • 0141656303 scopus 로고    scopus 로고
    • Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head
    • Nakata, T., and Hirokawa, N. (2003). Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head. J. Cell Biol. 162, 1045-1055.
    • (2003) J. Cell Biol. , vol.162 , pp. 1045-1055
    • Nakata, T.1    Hirokawa, N.2
  • 44
    • 0029098802 scopus 로고
    • Kinetic stabilization of microtubule dynamics at steady state by tau and microtubule-binding domains of tau
    • Panda, D., Goode, B.L., Feinstein, S.C., and Wilson, L. (1995). Kinetic stabilization of microtubule dynamics at steady state by tau and microtubule-binding domains of tau. Biochemistry 34, 11117-11127.
    • (1995) Biochemistry , vol.34 , pp. 11117-11127
    • Panda, D.1    Goode, B.L.2    Feinstein, S.C.3    Wilson, L.4
  • 45
    • 0033607298 scopus 로고    scopus 로고
    • Rapid treadmilling of brain microtubules free of microtubule-associated proteins in vitro and its suppression by tau
    • Panda, D., Miller, H.P., and Wilson, L. (1999). Rapid treadmilling of brain microtubules free of microtubule-associated proteins in vitro and its suppression by tau. Proc. Natl. Acad. Sci. USA 96, 12459-12464.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12459-12464
    • Panda, D.1    Miller, H.P.2    Wilson, L.3
  • 46
    • 0042924434 scopus 로고    scopus 로고
    • Differential regulation of microtubule dynamics by three- and four-repeat tau: Implications for the onset of neurodegenerative disease
    • Panda, D., Samuel, J.C., Massie, M., Feinstein, S.C., and Wilson, L. (2003). Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease. Proc. Natl. Acad. Sci. USA 100, 9548-9553.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9548-9553
    • Panda, D.1    Samuel, J.C.2    Massie, M.3    Feinstein, S.C.4    Wilson, L.5
  • 47
    • 0001468493 scopus 로고
    • A cellophane strip technique for culturing tissue in multipurpose culture chambers
    • Rose, G.G., Pomerat, C.M., Shindler, T., and Trunnell, J. (1958). A cellophane strip technique for culturing tissue in multipurpose culture chambers. J. Biophys. Biochem. Cytol. 4, 761-764.
    • (1958) J. Biophys. Biochem. Cytol. , vol.4 , pp. 761-764
    • Rose, G.G.1    Pomerat, C.M.2    Shindler, T.3    Trunnell, J.4
  • 48
    • 0031738468 scopus 로고    scopus 로고
    • Tau pathology in two Dutch families with mutations in the microtubule-binding region of tau
    • Spillantini, M.G., Crowther, R.A., Kamphorst, W., Heutink, P., and van Swieten, J.C. (1998). Tau pathology in two Dutch families with mutations in the microtubule-binding region of tau. Am. J. Pathol. 153, 1359-1363.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1359-1363
    • Spillantini, M.G.1    Crowther, R.A.2    Kamphorst, W.3    Heutink, P.4    Van Swieten, J.C.5
  • 49
    • 0031813790 scopus 로고    scopus 로고
    • Involvement of microtubules in the regulation of Bcl2 phosphorylation and apoptosis through cyclic AMP-dependent protein kinase
    • Srivastava, R.K., Srivastava, A.R., Korsmeyer, S.J., Nesterova, M., Cho-Chung, Y.S., and Longo, D.L. (1998). Involvement of microtubules in the regulation of Bcl2 phosphorylation and apoptosis through cyclic AMP-dependent protein kinase. Mol. Cell. Biol. 18, 3509-3517.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3509-3517
    • Srivastava, R.K.1    Srivastava, A.R.2    Korsmeyer, S.J.3    Nesterova, M.4    Cho-Chung, Y.S.5    Longo, D.L.6
  • 50
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer, K., Vogel, R., Thies, E., Mandelkow, E., and Mandelkow, E.M. (2002). Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156, 1051-1063.
    • (2002) J. Cell Biol. , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 51
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • Trinczek, B., Biernat, J., Baumann, K., Mandelkow, E.M., and Mandelkow, E. (1995). Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol. Biol. Cell 6, 1887-1902.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1887-1902
    • Trinczek, B.1    Biernat, J.2    Baumann, K.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 52
    • 0032799381 scopus 로고    scopus 로고
    • Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles
    • Trinczek, B., Ebneth, A., Mandelkow, E.M., and Mandelkow, E. (1999). Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles. J. Cell Sci. 112(Pt 14), 2355-2367.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 14 , pp. 2355-2367
    • Trinczek, B.1    Ebneth, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 53
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker, R.A., O'Brien, E.T., Pryer, N.K., Soboeiro, M.F., Voter, W.A., Erickson, H.P., and Salmon, E.D. (1988). Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies. J. Cell Biol. 107, 1437-1448.
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Soboeiro, M.F.4    Voter, W.A.5    Erickson, H.P.6    Salmon, E.D.7
  • 54
    • 0038457895 scopus 로고    scopus 로고
    • Regulation of leading edge microtubule and actin dynamics downstream of Rac1
    • Wittmann, T., Bokoch, G.M., and Waterman-Storer, C.M. (2003). Regulation of leading edge microtubule and actin dynamics downstream of Rac1. J. Cell Biol. 161, 845-851.
    • (2003) J. Cell Biol. , vol.161 , pp. 845-851
    • Wittmann, T.1    Bokoch, G.M.2    Waterman-Storer, C.M.3
  • 55
    • 0344874553 scopus 로고    scopus 로고
    • Reduction of detyrosinated microtubules and golgi fragmentation are linked to tau-induced degeneration in astrocytes
    • Yoshiyama, Y., Zhang, B., Bruce, J., Trojanowski, J.Q., and Lee, V.M. (2003). Reduction of detyrosinated microtubules and golgi fragmentation are linked to tau-induced degeneration in astrocytes. J. Neurosci. 23, 10662-10671.
    • (2003) J. Neurosci. , vol.23 , pp. 10662-10671
    • Yoshiyama, Y.1    Zhang, B.2    Bruce, J.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 56
    • 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.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 947-959
    • Yvon, A.M.1    Wadsworth, P.2    Jordan, M.A.3
  • 57
    • 0028231706 scopus 로고
    • Quantitative determination of the proportion of microtubule polymer present during the mitosis-interphase transition
    • Zhai, Y., and Borisy, G.G. (1994). Quantitative determination of the proportion of microtubule polymer present during the mitosis-interphase transition. J. Cell Sci. 107(Pt 4), 881-890.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 4 , pp. 881-890
    • Zhai, Y.1    Borisy, G.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.