메뉴 건너뛰기




Volumn 137, Issue 1, 2016, Pages 12-25

Cellular and molecular modifier pathways in tauopathies: The big picture from screening invertebrate models

Author keywords

C. elegans; Drosophila; genome wide association studies; modifier screen; neurodegeneration; Tau

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; TAU PROTEIN; HYBRID PROTEIN; MAPT PROTEIN, HUMAN;

EID: 84958260342     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13532     Document Type: Review
Times cited : (29)

References (108)
  • 1
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso A. C., Grundke-Iqbal I., and, Iqbal K., (1996) Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat. Med. 2, 783-787.
    • (1996) Nat. Med. , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 2
    • 81855172495 scopus 로고    scopus 로고
    • Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation
    • Ambegaokar S. S., and, Jackson G. R., (2011) Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation. Hum. Mol. Genet. 20, 4947-4977.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4947-4977
    • Ambegaokar, S.S.1    Jackson, G.R.2
  • 3
    • 84866085693 scopus 로고    scopus 로고
    • The downward spiral of tau and autolysosomes: A new hypothesis in neurodegeneration
    • Ambegaokar S. S., and, Jackson G. R., (2012) The downward spiral of tau and autolysosomes: a new hypothesis in neurodegeneration. Autophagy 8, 1144-1145.
    • (2012) Autophagy , vol.8 , pp. 1144-1145
    • Ambegaokar, S.S.1    Jackson, G.R.2
  • 4
    • 36148960495 scopus 로고    scopus 로고
    • Generation of a transgenic zebrafish model of Tauopathy using a novel promoter element derived from the zebrafish eno2 gene
    • Bai Q., Garver J. A., Hukriede N. A., and, Burton E. A., (2007) Generation of a transgenic zebrafish model of Tauopathy using a novel promoter element derived from the zebrafish eno2 gene. Nucleic Acids Res. 35, 6501-6516.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6501-6516
    • Bai, Q.1    Garver, J.A.2    Hukriede, N.A.3    Burton, E.A.4
  • 5
    • 0033041179 scopus 로고    scopus 로고
    • Association of an extended haplotype in the tau gene with progressive supranuclear palsy
    • Baker M., Litvan I., Houlden H., et al,. (1999) Association of an extended haplotype in the tau gene with progressive supranuclear palsy. Hum. Mol. Genet. 8, 711-715.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 711-715
    • Baker, M.1    Litvan, I.2    Houlden, H.3
  • 6
    • 33846224191 scopus 로고    scopus 로고
    • Altered axonal mitochondrial transport in the pathogenesis of Charcot-Marie-Tooth disease from mitofusin 2 mutations
    • Baloh R. H., Schmidt R. E., Pestronk A., and, Milbrandt J., (2007) Altered axonal mitochondrial transport in the pathogenesis of Charcot-Marie-Tooth disease from mitofusin 2 mutations. J. Neurosci. 27, 422-430.
    • (2007) J. Neurosci. , vol.27 , pp. 422-430
    • Baloh, R.H.1    Schmidt, R.E.2    Pestronk, A.3    Milbrandt, J.4
  • 9
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt R., Leger J., and, Lee G., (1995) Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol. 131, 1327-1340.
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 10
    • 84900441341 scopus 로고    scopus 로고
    • Poldip2 knockout results in perinatal lethality, reduced cellular growth and increased autophagy of mouse embryonic fibroblasts
    • Brown D. I., Lassegue B., Lee M., Zafari R., Long J. S., Saavedra H. I., and, Griendling K. K., (2014) Poldip2 knockout results in perinatal lethality, reduced cellular growth and increased autophagy of mouse embryonic fibroblasts. PLoS ONE 9, e96657.
    • (2014) PLoS ONE , vol.9 , pp. e96657
    • Brown, D.I.1    Lassegue, B.2    Lee, M.3    Zafari, R.4    Long, J.S.5    Saavedra, H.I.6    Griendling, K.K.7
  • 12
    • 84936748562 scopus 로고    scopus 로고
    • Impaired retrograde transport by the Dynein/Dynactin complex contributes to Tau-induced toxicity
    • Butzlaff M., Hannan S. B., Karsten P., et al,. (2015) Impaired retrograde transport by the Dynein/Dynactin complex contributes to Tau-induced toxicity. Hum. Mol. Genet. 24, 3623-3637.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 3623-3637
    • Butzlaff, M.1    Hannan, S.B.2    Karsten, P.3
  • 13
    • 77950818375 scopus 로고    scopus 로고
    • Paxillin and hydrogen peroxide-inducible clone 5 expression and distribution in control and Alzheimer disease hippocampi
    • Caltagarone J., Hamilton R. L., Murdoch G., Jing Z., DeFranco D. B., and, Bowser R., (2010) Paxillin and hydrogen peroxide-inducible clone 5 expression and distribution in control and Alzheimer disease hippocampi. J. Neuropathol. Exp. Neurol. 69, 356-371.
    • (2010) J. Neuropathol. Exp. Neurol. , vol.69 , pp. 356-371
    • Caltagarone, J.1    Hamilton, R.L.2    Murdoch, G.3    Jing, Z.4    DeFranco, D.B.5    Bowser, R.6
  • 14
    • 45149093564 scopus 로고    scopus 로고
    • Identification of novel genes that modify phenotypes induced by Alzheimer's beta-amyloid overexpression in Drosophila
    • Cao W., Song H. J., Gangi T., Kelkar A., Antani I., Garza D., and, Konsolaki M., (2008) Identification of novel genes that modify phenotypes induced by Alzheimer's beta-amyloid overexpression in Drosophila. Genetics 178, 1457-1471.
    • (2008) Genetics , vol.178 , pp. 1457-1471
    • Cao, W.1    Song, H.J.2    Gangi, T.3    Kelkar, A.4    Antani, I.5    Garza, D.6    Konsolaki, M.7
  • 15
    • 57649203362 scopus 로고    scopus 로고
    • Dissociation of tau toxicity and phosphorylation: Role of GSK-3beta, MARK and Cdk5 in a Drosophila model
    • Chatterjee S., Sang T. K., Lawless G. M., and, Jackson G. R., (2009) Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model. Hum. Mol. Genet. 18, 164-177.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 164-177
    • Chatterjee, S.1    Sang, T.K.2    Lawless, G.M.3    Jackson, G.R.4
  • 16
    • 33744994326 scopus 로고    scopus 로고
    • Biochemical investigation of Tau protein phosphorylation status and its solubility properties in Drosophila
    • Chau K. W., Chan W. Y., Shaw P. C., and, Chan H. Y., (2006) Biochemical investigation of Tau protein phosphorylation status and its solubility properties in Drosophila. Biochem. Biophys. Res. Commun. 346, 150-159.
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 150-159
    • Chau, K.W.1    Chan, W.Y.2    Shaw, P.C.3    Chan, H.Y.4
  • 17
    • 27744600579 scopus 로고    scopus 로고
    • Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions
    • Chee F. C., Mudher A., Cuttle M. F., Newman T. A., MacKay D., Lovestone S., and, Shepherd D., (2005) Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions. Neurobiol. Dis. 20, 918-928.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 918-928
    • Chee, F.C.1    Mudher, A.2    Cuttle, M.F.3    Newman, T.A.4    MacKay, D.5    Lovestone, S.6    Shepherd, D.7
  • 18
    • 32544447773 scopus 로고    scopus 로고
    • Overexpression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions
    • Chee F., Mudher A., Newman T. A., Cuttle M., Lovestone S., and, Shepherd D., (2006) Overexpression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions. Biochem. Soc. Trans. 34, 88-90.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 88-90
    • Chee, F.1    Mudher, A.2    Newman, T.A.3    Cuttle, M.4    Lovestone, S.5    Shepherd, D.6
  • 19
    • 34247615021 scopus 로고    scopus 로고
    • Study of tauopathies by comparing Drosophila and human tau in Drosophila
    • Chen X., Li Y., Huang J., Cao D., Yang G., Liu W., Lu H., and, Guo A., (2007) Study of tauopathies by comparing Drosophila and human tau in Drosophila. Cell Tissue Res. 329, 169-178.
    • (2007) Cell Tissue Res. , vol.329 , pp. 169-178
    • Chen, X.1    Li, Y.2    Huang, J.3    Cao, D.4    Yang, G.5    Liu, W.6    Lu, H.7    Guo, A.8
  • 20
    • 70350507090 scopus 로고    scopus 로고
    • Complex splicing and neural expression of duplicated tau genes in zebrafish embryos
    • Chen M., Martins R. N., and, Lardelli M., (2009) Complex splicing and neural expression of duplicated tau genes in zebrafish embryos. J. Alzheimers Dis. 18, 305-317.
    • (2009) J. Alzheimers Dis. , vol.18 , pp. 305-317
    • Chen, M.1    Martins, R.N.2    Lardelli, M.3
  • 21
    • 84878662767 scopus 로고    scopus 로고
    • PTL-1 regulates neuronal integrity and lifespan in C. Elegans
    • Chew Y. L., Fan X., Gotz J., and, Nicholas H. R., (2013) PTL-1 regulates neuronal integrity and lifespan in C. elegans. J. Cell Sci. 126, 2079-2091.
    • (2013) J. Cell Sci. , vol.126 , pp. 2079-2091
    • Chew, Y.L.1    Fan, X.2    Gotz, J.3    Nicholas, H.R.4
  • 22
    • 0034683666 scopus 로고    scopus 로고
    • Myosin VI: Roles for a minus end-directed actin motor in cells
    • Cramer L. P., (2000) Myosin VI: roles for a minus end-directed actin motor in cells. J. Cell Biol. 150, F121-F126.
    • (2000) J. Cell Biol. , vol.150 , pp. F121-F126
    • Cramer, L.P.1
  • 24
    • 0035067021 scopus 로고    scopus 로고
    • Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
    • Dawson H. N., Ferreira A., Eyster M. V., Ghoshal N., Binder L. I., and, Vitek M. P., (2001) Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114, 1179-1187.
    • (2001) J. Cell Sci. , vol.114 , pp. 1179-1187
    • Dawson, H.N.1    Ferreira, A.2    Eyster, M.V.3    Ghoshal, N.4    Binder, L.I.5    Vitek, M.P.6
  • 26
    • 78650918920 scopus 로고    scopus 로고
    • FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging
    • Demontis F., and, Perrimon N., (2010) FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging. Cell 143, 813-825.
    • (2010) Cell , vol.143 , pp. 813-825
    • Demontis, F.1    Perrimon, N.2
  • 27
    • 22244450095 scopus 로고    scopus 로고
    • Aberrant lysosomal carbohydrate storage accompanies endocytic defects and neurodegeneration in Drosophila benchwarmer
    • Dermaut B., Norga K. K., Kania A., Verstreken P., Pan H., Zhou Y., Callaerts P., and, Bellen H. J., (2005) Aberrant lysosomal carbohydrate storage accompanies endocytic defects and neurodegeneration in Drosophila benchwarmer. J. Cell Biol. 170, 127-139.
    • (2005) J. Cell Biol. , vol.170 , pp. 127-139
    • Dermaut, B.1    Norga, K.K.2    Kania, A.3    Verstreken, P.4    Pan, H.5    Zhou, Y.6    Callaerts, P.7    Bellen, H.J.8
  • 28
    • 33745959291 scopus 로고    scopus 로고
    • Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
    • Dickey C. A., Yue M., Lin W. L., et al,. (2006) Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species. J. Neurosci. 26, 6985-6996.
    • (2006) J. Neurosci. , vol.26 , pp. 6985-6996
    • Dickey, C.A.1    Yue, M.2    Lin, W.L.3
  • 29
    • 84865352799 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration via DRP1 mislocalization in vivo
    • DuBoff B., Gotz J., and, Feany M. B., (2012) Tau promotes neurodegeneration via DRP1 mislocalization in vivo. Neuron 75, 618-632.
    • (2012) Neuron , vol.75 , pp. 618-632
    • DuBoff, B.1    Gotz, J.2    Feany, M.B.3
  • 30
    • 84928920470 scopus 로고    scopus 로고
    • Tau co-organizes dynamic microtubule and actin networks
    • Elie A., Prezel E., Guerin C., et al,. (2015) Tau co-organizes dynamic microtubule and actin networks. Sci. Rep. 5, 9964.
    • (2015) Sci. Rep. , vol.5 , pp. 9964
    • Elie, A.1    Prezel, E.2    Guerin, C.3
  • 31
    • 3142763039 scopus 로고    scopus 로고
    • Actin and microtubules in cell motility: Which one is in control?
    • (Copenhagen, Denmark)
    • Etienne-Manneville S., (2004) Actin and microtubules in cell motility: which one is in control? Traffic (Copenhagen, Denmark), 5, 470-477.
    • (2004) Traffic , vol.5 , pp. 470-477
    • Etienne-Manneville, S.1
  • 33
    • 77958459087 scopus 로고    scopus 로고
    • Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies
    • Falzone T. L., Gunawardena S., McCleary D., Reis G. F., and, Goldstein L. S., (2010) Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies. Hum. Mol. Genet. 19, 4399-4408.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4399-4408
    • Falzone, T.L.1    Gunawardena, S.2    McCleary, D.3    Reis, G.F.4    Goldstein, L.S.5
  • 35
    • 77955516967 scopus 로고    scopus 로고
    • Filamin-A and Myosin VI colocalize with fibrillary Tau protein in Alzheimer's disease and FTDP-17 brains
    • Feuillette S., Deramecourt V., Laquerriere A., et al,. (2010) Filamin-A and Myosin VI colocalize with fibrillary Tau protein in Alzheimer's disease and FTDP-17 brains. Brain Res. 1345, 182-189.
    • (2010) Brain Res. , vol.1345 , pp. 182-189
    • Feuillette, S.1    Deramecourt, V.2    Laquerriere, A.3
  • 37
    • 84893488880 scopus 로고    scopus 로고
    • Tangles, toxicity, and tau secretion in AD - New approaches to a vexing problem
    • Gendreau K. L., and, Hall G. F., (2013) Tangles, toxicity, and tau secretion in AD-new approaches to a vexing problem. Front. Neurol. 4, 160.
    • (2013) Front. Neurol. , vol.4 , pp. 160
    • Gendreau, K.L.1    Hall, G.F.2
  • 38
    • 5744248243 scopus 로고    scopus 로고
    • Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases
    • Ghosh S., and, Feany M. B., (2004) Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases. Hum. Mol. Genet. 13, 2011-2018.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2011-2018
    • Ghosh, S.1    Feany, M.B.2
  • 39
    • 0021572660 scopus 로고
    • The amyloid deposits in Alzheimer's disease: Their nature and pathogenesis
    • Glenner G. G., Wong C. W., Quaranta V., and, Eanes E. D., (1984) The amyloid deposits in Alzheimer's disease: their nature and pathogenesis. Appl. Pathol. 2, 357-369.
    • (1984) Appl. Pathol. , vol.2 , pp. 357-369
    • Glenner, G.G.1    Wong, C.W.2    Quaranta, V.3    Eanes, E.D.4
  • 40
    • 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., (1989) 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
  • 41
    • 0032214501 scopus 로고    scopus 로고
    • Tau mutations cause frontotemporal dementias
    • Goedert M., Crowther R. A., and, Spillantini M. G., (1998) Tau mutations cause frontotemporal dementias. Neuron 21, 955-958.
    • (1998) Neuron , vol.21 , pp. 955-958
    • Goedert, M.1    Crowther, R.A.2    Spillantini, M.G.3
  • 42
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • Goode B. L., Drubin D. G., and, Barnes G., (2000) Functional cooperation between the microtubule and actin cytoskeletons. Curr. Opin. Cell Biol. 12, 63-71.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 43
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Gotz J., Probst A., Spillantini M. G., Schafer T., Jakes R., Burki K., and, Goedert M., (1995) Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J. 14, 1304-1313.
    • (1995) EMBO J. , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3    Schafer, T.4    Jakes, R.5    Burki, K.6    Goedert, M.7
  • 44
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J., Chen F., van Dorpe J., and, Nitsch R. M., (2001) Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils. Science 293, 1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 45
    • 77955976865 scopus 로고    scopus 로고
    • Modelling cell and isoform type specificity of tauopathies in Drosophila
    • Grammenoudi S., Anezaki M., Kosmidis S., and, Skoulakis E. M., (2008) Modelling cell and isoform type specificity of tauopathies in Drosophila. SEB Exp. Biol. Ser. 60, 39-56.
    • (2008) SEB Exp. Biol. Ser. , vol.60 , pp. 39-56
    • Grammenoudi, S.1    Anezaki, M.2    Kosmidis, S.3    Skoulakis, E.M.4
  • 46
    • 0028301455 scopus 로고
    • Altered microtubule organization in small-calibre axons of mice lacking tau protein
    • Harada A., Oguchi K., Okabe S., et al,. (1994) Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369, 488-491.
    • (1994) Nature , vol.369 , pp. 488-491
    • Harada, A.1    Oguchi, K.2    Okabe, S.3
  • 47
    • 0034814018 scopus 로고    scopus 로고
    • Identification and characterization of the Drosophila tau homolog
    • Heidary G., and, Fortini M. E., (2001) Identification and characterization of the Drosophila tau homolog. Mech. Dev. 108, 171-178.
    • (2001) Mech. Dev. , vol.108 , pp. 171-178
    • Heidary, G.1    Fortini, M.E.2
  • 48
    • 70449753435 scopus 로고    scopus 로고
    • Control of neuronal polarity and plasticity-A renaissance for microtubules?
    • Hoogenraad C. C., and, Bradke F., (2009) Control of neuronal polarity and plasticity-a renaissance for microtubules? Trends Cell Biol. 19, 669-676.
    • (2009) Trends Cell Biol. , vol.19 , pp. 669-676
    • Hoogenraad, C.C.1    Bradke, F.2
  • 49
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M., Lendon C. L., Rizzu P., 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    Lendon, C.L.2    Rizzu, P.3
  • 50
    • 77957254409 scopus 로고    scopus 로고
    • Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease
    • Iijima K., Gatt A., and, Iijima-Ando K., (2010) Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease. Hum. Mol. Genet. 19, 2947-2957.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2947-2957
    • Iijima, K.1    Gatt, A.2    Iijima-Ando, K.3
  • 51
    • 84866150232 scopus 로고    scopus 로고
    • Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer's disease-related tau phosphorylation via PAR-1
    • Iijima-Ando K., Sekiya M., Maruko-Otake A., Ohtake Y., Suzuki E., Lu B., and, Iijima K. M., (2012) Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer's disease-related tau phosphorylation via PAR-1. PLoS Genet. 8, e1002918.
    • (2012) PLoS Genet. , vol.8 , pp. e1002918
    • Iijima-Ando, K.1    Sekiya, M.2    Maruko-Otake, A.3    Ohtake, Y.4    Suzuki, E.5    Lu, B.6    Iijima, K.M.7
  • 52
    • 0033969771 scopus 로고    scopus 로고
    • Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
    • Ikegami S., Harada A., and, Hirokawa N., (2000) Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice. Neurosci. Lett. 279, 129-132.
    • (2000) Neurosci. Lett. , vol.279 , pp. 129-132
    • Ikegami, S.1    Harada, A.2    Hirokawa, N.3
  • 53
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform
    • Ishihara T., Hong M., Zhang B., Nakagawa Y., Lee M. K., Trojanowski J. Q., and, Lee V. M., (1999) Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron 24, 751-762.
    • (1999) Neuron , vol.24 , pp. 751-762
    • Ishihara, T.1    Hong, M.2    Zhang, B.3    Nakagawa, Y.4    Lee, M.K.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 54
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson G. R., Wiedau-Pazos M., Sang T. K., Wagle N., Brown C. A., Massachi S., and, Geschwind D. H., (2002) Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 34, 509-519.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3    Wagle, N.4    Brown, C.A.5    Massachi, S.6    Geschwind, D.H.7
  • 55
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates Hsp70/Hsp90 interactions in protein folding
    • Johnson B. D., Schumacher R. J., Ross E. D., and, Toft D. O., (1998) Hop modulates Hsp70/Hsp90 interactions in protein folding. J. Biol. Chem. 273, 3679-3686.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3679-3686
    • Johnson, B.D.1    Schumacher, R.J.2    Ross, E.D.3    Toft, D.O.4
  • 56
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers T., Friedhoff P., Biernat J., Mandelkow E. M., and, Mandelkow E., (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399, 344-349.
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 58
    • 84929838913 scopus 로고    scopus 로고
    • Essential role of POLDIP2 in Tau aggregation and neurotoxicity via autophagy/proteasome inhibition
    • Kim Y., Park H., Nah J., Moon S., Lee W., Hong S. H., Kam T. I., and, Jung Y. K., (2015) Essential role of POLDIP2 in Tau aggregation and neurotoxicity via autophagy/proteasome inhibition. Biochem. Biophys. Res. Commun. 462, 112-118.
    • (2015) Biochem. Biophys. Res. Commun. , vol.462 , pp. 112-118
    • Kim, Y.1    Park, H.2    Nah, J.3    Moon, S.4    Lee, W.5    Hong, S.H.6    Kam, T.I.7    Jung, Y.K.8
  • 59
    • 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
  • 61
    • 33646133424 scopus 로고    scopus 로고
    • Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans
    • Kraemer B. C., Burgess J. K., Chen J. H., Thomas J. H., and, Schellenberg G. D., (2006) Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans. Hum. Mol. Genet. 15, 1483-1496.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1483-1496
    • Kraemer, B.C.1    Burgess, J.K.2    Chen, J.H.3    Thomas, J.H.4    Schellenberg, G.D.5
  • 62
    • 84942769755 scopus 로고    scopus 로고
    • Tau neurotoxicity and rescue in animal models of human Tauopathies
    • Kruger L., and, Mandelkow E. M., (2015) Tau neurotoxicity and rescue in animal models of human Tauopathies. Curr. Opin. Neurobiol. 36, 52-58.
    • (2015) Curr. Opin. Neurobiol. , vol.36 , pp. 52-58
    • Kruger, L.1    Mandelkow, E.M.2
  • 63
    • 84893643261 scopus 로고    scopus 로고
    • Drosophila modifier screens to identify novel neuropsychiatric drugs including aminergic agents for the possible treatment of Parkinson's disease and depression
    • Lawal H. O., Terrell A., Lam H. A., et al,. (2014) Drosophila modifier screens to identify novel neuropsychiatric drugs including aminergic agents for the possible treatment of Parkinson's disease and depression. Mol. Psychiatry 19, 235-242.
    • (2014) Mol. Psychiatry , vol.19 , pp. 235-242
    • Lawal, H.O.1    Terrell, A.2    Lam, H.A.3
  • 64
    • 1542267796 scopus 로고    scopus 로고
    • Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease
    • Lee W. C., Yoshihara M., and, Littleton J. T., (2004) Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc. Natl Acad. Sci. USA 101, 3224-3229.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3224-3229
    • Lee, W.C.1    Yoshihara, M.2    Littleton, J.T.3
  • 65
    • 84871759268 scopus 로고    scopus 로고
    • Phospho-dependent ubiquitination and degradation of PAR-1 regulates synaptic morphology and tau-mediated Abeta toxicity in Drosophila
    • Lee S., Wang J. W., Yu W., and, Lu B., (2012) Phospho-dependent ubiquitination and degradation of PAR-1 regulates synaptic morphology and tau-mediated Abeta toxicity in Drosophila. Nat. Commun. 3, 1312.
    • (2012) Nat. Commun. , vol.3 , pp. 1312
    • Lee, S.1    Wang, J.W.2    Yu, W.3    Lu, B.4
  • 66
    • 84887065883 scopus 로고    scopus 로고
    • Drosophila as a screening tool to study human neurodegenerative diseases
    • Lenz S., Karsten P., Schulz J. B., and, Voigt A., (2013) Drosophila as a screening tool to study human neurodegenerative diseases. J. Neurochem. 127, 453-460.
    • (2013) J. Neurochem. , vol.127 , pp. 453-460
    • Lenz, S.1    Karsten, P.2    Schulz, J.B.3    Voigt, A.4
  • 67
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J., McGowan E., Rockwood J., et al,. (2000) Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25, 402-405.
    • (2000) Nat. Genet. , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3
  • 68
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J., Dickson D. W., Lin W. L., et al,. (2001) Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293, 1487-1491.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 69
    • 67349086281 scopus 로고    scopus 로고
    • The trip of the tip: Understanding the growth cone machinery
    • Lowery L. A., and, Van Vactor D., (2009) The trip of the tip: understanding the growth cone machinery. Nat. Rev. Mol. Cell Biol. 10, 332-343.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 332-343
    • Lowery, L.A.1    Van Vactor, D.2
  • 70
    • 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
  • 71
    • 84929193242 scopus 로고    scopus 로고
    • Autophagosome-lysosome fusion is independent of V-ATPase-mediated acidification
    • Mauvezin C., Nagy P., Juhasz G., and, Neufeld T. P., (2015) Autophagosome-lysosome fusion is independent of V-ATPase-mediated acidification. Nat. Commun. 6, 7007.
    • (2015) Nat. Commun. , vol.6 , pp. 7007
    • Mauvezin, C.1    Nagy, P.2    Juhasz, G.3    Neufeld, T.P.4
  • 72
  • 73
    • 84875443717 scopus 로고    scopus 로고
    • Axonal transport deficits and neurodegenerative diseases
    • Millecamps S., and, Julien J. P., (2013) Axonal transport deficits and neurodegenerative diseases. Nat. Rev. Neurosci. 14, 161-176.
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 161-176
    • Millecamps, S.1    Julien, J.P.2
  • 74
    • 84940932191 scopus 로고    scopus 로고
    • Yeast Model of Amyloid-beta and Tau Aggregation in Alzheimer's Disease
    • Moosavi B., Mousavi B., and, Macreadie I. G., (2015) Yeast Model of Amyloid-beta and Tau Aggregation in Alzheimer's Disease. J. Alzheimers Dis. 47, 9-16.
    • (2015) J. Alzheimers Dis. , vol.47 , pp. 9-16
    • Moosavi, B.1    Mousavi, B.2    Macreadie, I.G.3
  • 75
    • 70350455072 scopus 로고    scopus 로고
    • Axonal transport defects in neurodegenerative diseases
    • Morfini G. A., Burns M., Binder L. I., et al,. (2009) Axonal transport defects in neurodegenerative diseases. J. Neurosci. 29, 12776-12786.
    • (2009) J. Neurosci. , vol.29 , pp. 12776-12786
    • Morfini, G.A.1    Burns, M.2    Binder, L.I.3
  • 76
    • 3142592230 scopus 로고    scopus 로고
    • GSK-3beta inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila
    • Mudher A., Shepherd D., Newman T. A., et al,. (2004) GSK-3beta inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila. Mol. Psychiatry 9, 522-530.
    • (2004) Mol. Psychiatry , vol.9 , pp. 522-530
    • Mudher, A.1    Shepherd, D.2    Newman, T.A.3
  • 77
    • 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., and, Donlon T. A., (1986) 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, 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
  • 78
    • 79960284291 scopus 로고    scopus 로고
    • The power and richness of modelling tauopathies in Drosophila
    • Papanikolopoulou K., and, Skoulakis E. M., (2011) The power and richness of modelling tauopathies in Drosophila. Mol. Neurobiol. 44, 122-133.
    • (2011) Mol. Neurobiol. , vol.44 , pp. 122-133
    • Papanikolopoulou, K.1    Skoulakis, E.M.2
  • 79
    • 66449115032 scopus 로고    scopus 로고
    • A zebrafish model of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation
    • Paquet D., Bhat R., Sydow A., et al,. (2009) A zebrafish model of tauopathy allows in vivo imaging of neuronal cell death and drug evaluation. J. Clin. Investig. 119, 1382-1395.
    • (2009) J. Clin. Investig. , vol.119 , pp. 1382-1395
    • Paquet, D.1    Bhat, R.2    Sydow, A.3
  • 80
    • 11144356089 scopus 로고    scopus 로고
    • CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
    • Petrucelli L., Dickson D., Kehoe K., et al,. (2004) CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13, 703-714.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 703-714
    • Petrucelli, L.1    Dickson, D.2    Kehoe, K.3
  • 81
    • 45749114895 scopus 로고    scopus 로고
    • The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice
    • Pickford F., Masliah E., Britschgi M., et al,. (2008) The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice. J. Clin. Investig. 118, 2190-2199.
    • (2008) J. Clin. Investig. , vol.118 , pp. 2190-2199
    • Pickford, F.1    Masliah, E.2    Britschgi, M.3
  • 83
    • 1842432582 scopus 로고    scopus 로고
    • MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain
    • Roger B., Al-Bassam J., Dehmelt L., Milligan R. A., and, Halpain S., (2004) MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Curr. Biol. 14, 363-371.
    • (2004) Curr. Biol. , vol.14 , pp. 363-371
    • Roger, B.1    Al-Bassam, J.2    Dehmelt, L.3    Milligan, R.A.4    Halpain, S.5
  • 85
    • 11144353869 scopus 로고    scopus 로고
    • Parkinson's disease alpha-synuclein mutations exhibit defective axonal transport in cultured neurons
    • Saha A. R., Hill J., Utton M. A., et al,. (2004) Parkinson's disease alpha-synuclein mutations exhibit defective axonal transport in cultured neurons. J. Cell Sci. 117, 1017-1024.
    • (2004) J. Cell Sci. , vol.117 , pp. 1017-1024
    • Saha, A.R.1    Hill, J.2    Utton, M.A.3
  • 87
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H., Schwartz D., Gygi S. P., and, Kosik K. S., (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279, 4869-4876.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 88
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman J. M., and, Feany M. B., (2003) Genetic modifiers of tauopathy in Drosophila. Genetics 165, 1233-1242.
    • (2003) Genetics , vol.165 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 89
    • 84892971323 scopus 로고    scopus 로고
    • Functional screening in Drosophila identifies Alzheimer's disease susceptibility genes and implicates Tau-mediated mechanisms
    • Shulman J. M., Imboywa S., Giagtzoglou N., et al,. (2014) Functional screening in Drosophila identifies Alzheimer's disease susceptibility genes and implicates Tau-mediated mechanisms. Hum. Mol. Genet. 23, 870-877.
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 870-877
    • Shulman, J.M.1    Imboywa, S.2    Giagtzoglou, N.3
  • 91
    • 78049427560 scopus 로고    scopus 로고
    • Inhibition of GSK-3 ameliorates Abeta pathology in an adult-onset Drosophila model of Alzheimer's disease
    • Sofola O., Kerr F., Rogers I., et al,. (2010) Inhibition of GSK-3 ameliorates Abeta pathology in an adult-onset Drosophila model of Alzheimer's disease. PLoS Genet. 6, e1001087.
    • (2010) PLoS Genet. , vol.6 , pp. e1001087
    • Sofola, O.1    Kerr, F.2    Rogers, I.3
  • 93
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin G. B., Lillo C., Falzone T. L., et al,. (2005) Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307, 1282-1288.
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3
  • 95
    • 34548317186 scopus 로고    scopus 로고
    • A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies
    • Ubhi K. K., Shaibah H., Newman T. A., Shepherd D., and, Mudher A., (2007) A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies. Invert. Neurosci. 7, 165-171.
    • (2007) Invert. Neurosci. , vol.7 , pp. 165-171
    • Ubhi, K.K.1    Shaibah, H.2    Newman, T.A.3    Shepherd, D.4    Mudher, A.5
  • 97
    • 84939654955 scopus 로고    scopus 로고
    • Rare coding mutations identified by sequencing of Alzheimer disease genome-wide association studies loci
    • Vardarajan B. N., Ghani M., Kahn A., et al,. (2015) Rare coding mutations identified by sequencing of Alzheimer disease genome-wide association studies loci. Ann. Neurol. 78, 487-498.
    • (2015) Ann. Neurol. , vol.78 , pp. 487-498
    • Vardarajan, B.N.1    Ghani, M.2    Kahn, A.3
  • 98
  • 99
    • 33846448743 scopus 로고    scopus 로고
    • Activation of PAR-1 kinase and stimulation of tau phosphorylation by diverse signals require the tumor suppressor protein LKB1
    • Wang J. W., Imai Y., and, Lu B., (2007) Activation of PAR-1 kinase and stimulation of tau phosphorylation by diverse signals require the tumor suppressor protein LKB1. J. Neurosci. 27, 574-581.
    • (2007) J. Neurosci. , vol.27 , pp. 574-581
    • Wang, J.W.1    Imai, Y.2    Lu, B.3
  • 100
    • 84877980134 scopus 로고    scopus 로고
    • Abnormal hyperphosphorylation of tau: Sites, regulation, and molecular mechanism of neurofibrillary degeneration
    • Wang J. Z., Xia Y. Y., Grundke-Iqbal I., and, Iqbal K., (2013) Abnormal hyperphosphorylation of tau: sites, regulation, and molecular mechanism of neurofibrillary degeneration. J. Alzheimers Dis. 33 (Suppl 1), S123-S139.
    • (2013) J. Alzheimers Dis. , vol.33 , pp. S123-S139
    • Wang, J.Z.1    Xia, Y.Y.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 101
    • 0034716223 scopus 로고    scopus 로고
    • Tau and tau reporters disrupt central projections of sensory neurons in Drosophila
    • Williams D. W., Tyrer M., and, Shepherd D., (2000) Tau and tau reporters disrupt central projections of sensory neurons in Drosophila. J. Comp. Neurol. 428, 630-640.
    • (2000) J. Comp. Neurol. , vol.428 , pp. 630-640
    • Williams, D.W.1    Tyrer, M.2    Shepherd, D.3
  • 102
    • 0033366384 scopus 로고    scopus 로고
    • Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons
    • Williamson T. L., and, Cleveland D. W., (1999) Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Nat. Neurosci. 2, 50-56.
    • (1999) Nat. Neurosci. , vol.2 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 104
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • Wischik C. M., Novak M., Thogersen H. C., et al,. (1988) Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc. Natl Acad. Sci. USA 85, 4506-4510.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4506-4510
    • Wischik, C.M.1    Novak, M.2    Thogersen, H.C.3
  • 106
    • 84857676337 scopus 로고    scopus 로고
    • A critical role for the PAR-1/MARK-tau axis in mediating the toxic effects of Abeta on synapses and dendritic spines
    • Yu W., Polepalli J., Wagh D., Rajadas J., Malenka R., and, Lu B., (2012) A critical role for the PAR-1/MARK-tau axis in mediating the toxic effects of Abeta on synapses and dendritic spines. Hum. Mol. Genet. 21, 1384-1390.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1384-1390
    • Yu, W.1    Polepalli, J.2    Wagh, D.3    Rajadas, J.4    Malenka, R.5    Lu, B.6
  • 108
    • 0035369084 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1Bbeta
    • Zhao C., Takita J., Tanaka Y., et al,. (2001) Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1Bbeta. Cell 105, 587-597.
    • (2001) Cell , vol.105 , pp. 587-597
    • Zhao, C.1    Takita, J.2    Tanaka, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.