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Volumn 192, Issue 4, 2011, Pages 647-661

The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM ION; LIPOCORTIN 2; TAU PROTEIN;

EID: 79951873381     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201007161     Document Type: Article
Times cited : (130)

References (52)
  • 1
    • 34547101740 scopus 로고    scopus 로고
    • Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau
    • DOI 10.1074/jbc.M611876200
    • Aoyagi, H., M. Hasegawa, and A. Tamaoka. 2007. Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau. J. Biol. Chem. 282:20309-20318. doi:10.1074/jbc.M611876200 (Pubitemid 47099993)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20309-20318
    • Aoyagi, H.1    Hasegawa, M.2    Tamaoka, A.3
  • 2
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • DOI 10.1016/0896-6273(93)90279-Z
    • Biernat, J., N. Gustke, G. Drewes, E.M. Mandelkow, and E. Mandelkow. 1993. Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron. 11:153-163. doi:10.1016/0896-6273(93)90279-Z (Pubitemid 23222542)
    • (1993) Neuron , vol.11 , Issue.1 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 3
    • 1842581909 scopus 로고    scopus 로고
    • Comprehensive Proteomic Analysis of Human Par Protein Complexes Reveals an Interconnected Protein Network
    • DOI 10.1074/jbc.M312171200
    • Brajenovic, M., G. Joberty, B. Küster, T. Bouwmeester, and G. Drewes. 2004. Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. J. Biol. Chem. 279:12804-12811. doi:10.1074/jbc.M312171200 (Pubitemid 38445853)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12804-12811
    • Brajenovic, M.1    Joberty, G.2    Kuster, B.3    Bouwmeester, T.4    Drewes, G.5
  • 4
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • doi:10.1083/jcb.131.5.1327
    • Brandt, R., J. Léger, and G. Lee. 1995. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol. 131:1327-1340. doi:10.1083/jcb.131.5.1327
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Léger, J.2    Lee, G.3
  • 5
    • 33744952341 scopus 로고    scopus 로고
    • FTDP-17 mutations compromise the ability of Tau to regulate microtubule dynamics in cells
    • DOI 10.1074/jbc.M509420200
    • Bunker, J.M., K. Kamath, L. Wilson, M.A. Jordan, and S.C. Feinstein. 2006. FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells. J. Biol. Chem. 281:11856-11863. doi:10.1074/jbc.M509420200 (Pubitemid 43855446)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 11856-11863
    • Bunker, J.M.1    Kamath, K.2    Wilson, L.3    Jordan, M.A.4    Feinstein, S.C.5
  • 6
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • doi:10.1016/0896-6273(95)90232-5
    • Busciglio, J., A. Lorenzo, J. Yeh, and B.A. Yankner. 1995. beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron. 14:879-888. doi:10.1016/0896-6273(95)90232-5
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 7
    • 54349085644 scopus 로고    scopus 로고
    • Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps
    • Chang, E., S. Kim, H. Yin, H.N. Nagaraja, and J. Kuret. 2008. Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps. J. Neurochem. 107:1113-1123.
    • (2008) J. Neurochem. , vol.107 , pp. 1113-1123
    • Chang, E.1    Kim, S.2    Yin, H.3    Nagaraja, H.N.4    Kuret, J.5
  • 8
    • 0035937481 scopus 로고    scopus 로고
    • Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3beta identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes
    • DOI 10.1016/S0014-5793(01)02267-0, PII S0014579301022670
    • Connell, J.W., G.M. Gibb, J.C. Betts, W.P. Blackstock, J. Gallo, S. Lovestone, M. Hutton, and B.H. Anderton. 2001. Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3beta identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes. FEBS Lett. 493:40-44. doi:10.1016/S0014-5793(01)02267-0 (Pubitemid 32241173)
    • (2001) FEBS Letters , vol.493 , Issue.1 , pp. 40-44
    • Connell, J.W.1    Gibb, G.M.2    Betts, J.C.3    Blackstock, W.P.4    Gallo, J.-M.5    Lovestone, S.6    Hutton, M.7    Anderton, B.H.8
  • 9
    • 4444262625 scopus 로고    scopus 로고
    • Cdk5 deregulation in the pathogenesis of Alzheimer's disease
    • DOI 10.1016/j.molmed.2004.07.001, PII S1471491404001807
    • Cruz, J.C., and L.H. Tsai. 2004. Cdk5 deregulation in the pathogenesis of Alzheimer's disease. Trends Mol. Med. 10:452-458. doi:10.1016/j.molmed.2004.07. 001 (Pubitemid 39209212)
    • (2004) Trends in Molecular Medicine , vol.10 , Issue.9 , pp. 452-458
    • Cruz, J.C.1    Tsai, L.-H.2
  • 10
    • 0033042978 scopus 로고    scopus 로고
    • Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation
    • DOI 10.1016/S0014-5793(99)00222-7, PII S0014579399002227
    • Dayanandan, R., M. Van Slegtenhorst, T.G. Mack, L. Ko, S.H. Yen, K. Leroy, J.P. Brion, B.H. Anderton, M. Hutton, and S. Lovestone. 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 (Pubitemid 29132731)
    • (1999) FEBS Letters , vol.446 , Issue.2-3 , pp. 228-232
    • Dayanandan, R.1    Van, S.M.2    Mack, T.G.A.3    Ko, L.4    Yen, S.-H.5    Leroy, K.6    Brion, J.-P.7    Anderton, B.H.8    Hutton, M.9    Lovestone, S.10
  • 11
    • 0033982344 scopus 로고    scopus 로고
    • Missense tau mutations identified in FTDP-17 have a small effect on tau-microtubule interactions
    • DOI 10.1016/S0006-8993(99)02124-1, PII S0006899399021241
    • DeTure, M., L.W. Ko, S.H. Yen, P. Nacharaju, C. Easson, J. Lewis, M. van Slegtenhorst, M. Hutton, and S.H. Yen. 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 (Pubitemid 30015993)
    • (2000) Brain Research , vol.853 , Issue.1 , pp. 5-14
    • Deture, M.1    Ko, L.-W.2    Yen, S.3    Nacharaju, P.4    Easson, C.5    Lewis, J.6    Van, S.M.7    Hutton, M.8    Yen, S.-H.9
  • 12
    • 0036841609 scopus 로고    scopus 로고
    • Tau Assembly in inducible transfectants expressing wild-type or FTDP-17 tau
    • DeTure, M., L.W. Ko, C. Easson, and S.H. Yen. 2002. Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau. Am. J. Pathol. 161:1711-1722. doi:10.1016/S0002-9440(10)64448-3 (Pubitemid 35265530)
    • (2002) American Journal of Pathology , vol.161 , Issue.5 , pp. 1711-1722
    • DeTure, M.1    Ko, L.-W.2    Easson, C.3    Yen, S.-H.4
  • 14
    • 0023937193 scopus 로고
    • Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells
    • doi:10.1083/jcb.106.5.1583
    • Drubin, D., S. Kobayashi, D. Kellogg, and M. Kirschner. 1988. Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells. J. Cell Biol. 106:1583-1591. doi:10.1083/jcb.106.5. 1583
    • (1988) J. Cell Biol. , vol.106 , pp. 1583-1591
    • Drubin, D.1    Kobayashi, S.2    Kellogg, D.3    Kirschner, M.4
  • 15
    • 0027981954 scopus 로고
    • Alterations of annexin expression in pathological neuronal and glial reactions: Immunohistochemical localization of annexins I, II (p36 and p11 subunits), IV, and VI in the human hippocampus
    • Eberhard, D.A., M.D. Brown, and S.R. VandenBerg. 1994. Alterations of annexin expression in pathological neuronal and glial reactions. Immunohistochemical localization of annexins I, II (p36 and p11 subunits), IV, and VI in the human hippocampus. Am. J. Pathol. 145:640-649. (Pubitemid 24285971)
    • (1994) American Journal of Pathology , vol.145 , Issue.3 , pp. 640-649
    • Eberhard, D.A.1    Brown, M.D.2    VandenBerg, S.R.3
  • 16
    • 0035425347 scopus 로고    scopus 로고
    • Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein
    • DOI 10.1042/0264-6021:3570759
    • Eidenmüller, J., T. Fath, T. Maas, M. Pool, E. Sontag, and R. Brandt. 2001. Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein. Biochem. J. 357:759-767. doi:10.1042/0264-6021: 3570759 (Pubitemid 32735156)
    • (2001) Biochemical Journal , vol.357 , Issue.3 , pp. 759-767
    • Eidenmuller, J.1    Fath, T.2    Maas, T.3    Pool, M.4    Sontag, E.5    Brandt, R.6
  • 17
    • 0037111833 scopus 로고    scopus 로고
    • Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease
    • Fath, T., J. Eidenmüller, and R. Brandt. 2002. Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease. J. Neurosci. 22:9733-9741. (Pubitemid 35332856)
    • (2002) Journal of Neuroscience , vol.22 , Issue.22 , pp. 9733-9741
    • Fath, T.1    Eidenmuller, J.2    Brandt, R.3
  • 18
    • 0030977392 scopus 로고    scopus 로고
    • Frontotemporal dementia and parkinsonism linked to chromosome 17: A consensus conference
    • DOI 10.1002/ana.410410606
    • Foster, N.L., K. Wilhelmsen, A.A. Sima, M.Z. Jones, C.J. D'Amato, and S. Gilman; Conference Participants. 1997. Frontotemporal dementia and parkinsonism linked to chromosome 17: a consensus conference. Ann. Neurol. 41:706-715. doi:10.1002/ana.410410606 (Pubitemid 27249175)
    • (1997) Annals of Neurology , vol.41 , Issue.6 , pp. 706-715
    • Foster, N.L.1    Wilhelmsen, K.2    Sima, A.A.F.3    Jones, M.Z.4    D'Amato, C.J.5    Gilman, S.6
  • 19
    • 0025744090 scopus 로고
    • Increases in p11 and annexin II proteins correlate with differentiation in the PC12 pheochromocytoma
    • doi:10.1016/0006-291X(91)90666-U
    • Fox, M.T., D.A. Prentice, and J.P. Hughes. 1991. Increases in p11 and annexin II proteins correlate with differentiation in the PC12 pheochromocytoma. Biochem. Biophys. Res. Commun. 177:1188-1193. doi:10.1016/0006-291X(91)90666-U
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 1188-1193
    • Fox, M.T.1    Prentice, D.A.2    Hughes, J.P.3
  • 20
  • 21
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke, V., and S.E. Moss. 2002. Annexins: from structure to function. Physiol. Rev. 82:331-371. (Pubitemid 34654456)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 22
    • 20344369564 scopus 로고    scopus 로고
    • 2+ signalling to membrane dynamics
    • DOI 10.1038/nrm1661
    • Gerke, V., C.E. Creutz, and S.E. Moss. 2005. Annexins: linking Ca2+ signalling to membrane dynamics. Nat. Rev. Mol. Cell Biol. 6:449-461. doi:10.1038/nrm1661 (Pubitemid 40780557)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 23
    • 45749151056 scopus 로고    scopus 로고
    • Animal models of Alzheimer's disease and frontotemporal dementia
    • DOI 10.1038/nrn2420, PII NRN2420
    • Götz, J., and L.M. Ittner. 2008. Animal models of Alzheimer's disease and frontotemporal dementia. Nat. Rev. Neurosci. 9:532-544. doi:10.1038/nrn2420 (Pubitemid 351873467)
    • (2008) Nature Reviews Neuroscience , vol.9 , Issue.7 , pp. 532-544
    • Gotz, J.1    Ittner, L.M.2
  • 24
    • 0002845567 scopus 로고
    • Methodologies for the culture and experimental use of the PC12 rat pheochromocytoma cell line
    • G. Banker and K. Goslin, editors. MIT Press, Cambridge, Massachusetts
    • Greene, L.A., M.M. Sobeih, and K.K. Teng. 1991. Methodologies for the culture and experimental use of the PC12 rat pheochromocytoma cell line. In Culturing Nerve Cells. G. Banker and K. Goslin, editors. MIT Press, Cambridge, Massachusetts. 207-226.
    • (1991) Culturing Nerve Cells , pp. 207-226
    • Greene, L.A.1    Sobeih, M.M.2    Teng, K.K.3
  • 25
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer's disease
    • DOI 10.1111/j.1471-4159.2007.05194.x
    • Hooper, C., R. Killick, and S. Lovestone. 2008. The GSK3 hypothesis of Alzheimer's disease. J. Neurochem. 104:1433-1439. doi:10.1111/j.1471-4159.2007. 05194.x (Pubitemid 351316776)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.6 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 27
    • 0035966011 scopus 로고    scopus 로고
    • Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation
    • doi:10.1074/jbc.M106289200
    • Jacovina, A.T., F. Zhong, E. Khazanova, E. Lev, A.B. Deora, and K.A. Hajjar. 2001. Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation. J. Biol. Chem. 276:49350-49358. doi:10.1074/jbc.M106289200
    • (2001) J. Biol. Chem. , vol.276 , pp. 49350-49358
    • Jacovina, A.T.1    Zhong, F.2    Khazanova, E.3    Lev, E.4    Deora, A.B.5    Hajjar, K.A.6
  • 28
    • 33144463940 scopus 로고    scopus 로고
    • Global hairpin folding of tau in solution
    • DOI 10.1021/bi0521543
    • Jeganathan, S., M. von Bergen, H. Brutlach, H.J. Steinhoff, and E. Mandelkow. 2006. Global hairpin folding of tau in solution. Biochemistry. 45:2283-2293. doi:10.1021/bi0521543 (Pubitemid 43271328)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2283-2293
    • Jeganathan, S.1    Von, B.M.2    Brutlach, H.3    Steinhoff, H.-J.4    Mandelkow, E.5
  • 29
    • 0034697989 scopus 로고    scopus 로고
    • Comparative genetic and physiological studies of the MAP kinase Mpk1p from Kluyveromyces lactis and Saccharomyces cerevisiae
    • doi:10.1006/jmbi.2000.3916
    • Kirchrath, L., A. Lorberg, H.P. Schmitz, U. Gengenbacher, and J.J. Heinisch. 2000. Comparative genetic and physiological studies of the MAP kinase Mpk1p from Kluyveromyces lactis and Saccharomyces cerevisiae. J. Mol. Biol. 300:743-758. doi:10.1006/jmbi.2000.3916
    • (2000) J. Mol. Biol. , vol.300 , pp. 743-758
    • Kirchrath, L.1    Lorberg, A.2    Schmitz, H.P.3    Gengenbacher, U.4    Heinisch, J.J.5
  • 30
    • 1542289803 scopus 로고    scopus 로고
    • Mutant (R406W) Human Tau Is Hyperphosphorylated and Does Not Efficiently Bind Microtubules in a Neuronal Cortical Cell Model
    • DOI 10.1074/jbc.M311203200
    • Krishnamurthy, P.K., and G.V. Johnson. 2004. Mutant (R406W) human tau is hyperphosphorylated and does not efficiently bind microtubules in a neuronal cortical cell model. J. Biol. Chem. 279:7893-7900. doi:10.1074/jbc.M311203200 (Pubitemid 38294676)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7893-7900
    • Krishnamurthy, P.K.1    Johnson, G.V.W.2
  • 31
    • 34248222732 scopus 로고    scopus 로고
    • Inverse and distinct modulation of tau-dependent neurodegeneration by presenilin 1 and amyloid-beta in cultured cortical neurons: Evidence that tau phosphorylation is the limiting factor in amyloid-beta-induced cell death
    • DOI 10.1111/j.1471-4159.2006.04435.x
    • Leschik, J., A. Welzel, C. Weissmann, A. Eckert, and R. Brandt. 2007. Inverse and distinct modulation of tau-dependent neurodegeneration by presenilin 1 and amyloid-beta in cultured cortical neurons: evidence that tau phosphorylation is the limiting factor in amyloid-beta-induced cell death. J. Neurochem. 101:1303-1315. doi:10.1111/j.1471-4159.2006.04435.x (Pubitemid 46718815)
    • (2007) Journal of Neurochemistry , vol.101 , Issue.5 , pp. 1303-1315
    • Leschik, J.1    Welzel, A.2    Weissmann, C.3    Eckert, A.4    Brandt, R.5
  • 32
    • 77953524779 scopus 로고    scopus 로고
    • Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding
    • doi:10.1074/jbc.M110.105387
    • Leugers, C.J., and G. Lee. 2010. Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding. J. Biol. Chem. 285:19125-19134. doi:10.1074/jbc.M110.105387
    • (2010) J. Biol. Chem. , vol.285 , pp. 19125-19134
    • Leugers, C.J.1    Lee, G.2
  • 33
    • 41049106547 scopus 로고    scopus 로고
    • Alzheimer disease-like clinical phenotype in a family with FTDP-17 caused by a MAPT R406W mutation
    • DOI 10.1111/j.1468-1331.2008.02069.x
    • Lindquist, S.G., I.E. Holm, M. Schwartz, I. Law, J. Stokholm, M. Batbayli, G. Waldemar, and J.E. Nielsen. 2008. Alzheimer disease-like clinical phenotype in a family with FTDP-17 caused by a MAPT R406W mutation. Eur. J. Neurol. 15:377-385. doi:10.1111/j.1468-1331.2008.02069.x (Pubitemid 351422379)
    • (2008) European Journal of Neurology , vol.15 , Issue.4 , pp. 377-385
    • Lindquist, S.G.1    Holm, I.E.2    Schwartz, M.3    Law, I.4    Stokholm, J.5    Batbayli, M.6    Waldemar, G.7    Nielsen, J.E.8
  • 34
    • 0040141570 scopus 로고    scopus 로고
    • Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
    • DOI 10.1074/jbc.M000389200
    • Maas, T., J. Eidenmüller, and R. Brandt. 2000. Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J. Biol. Chem. 275:15733-15740. doi:10.1074/jbc.M000389200 (Pubitemid 30366871)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 15733-15740
    • Maas, T.1    Eidenmuller, J.2    Brandt, R.3
  • 35
    • 0033055359 scopus 로고    scopus 로고
    • Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17)
    • Matsumura, N., T. Yamazaki, and Y. Ihara. 1999. Stable expression in Chinese hamster ovary cells of mutated tau genes causing frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Am. J. Pathol. 154:1649-1656. doi:10.1016/S0002-9440(10)65420-X (Pubitemid 29262846)
    • (1999) American Journal of Pathology , vol.154 , Issue.6 , pp. 1649-1656
    • Matsumura, N.1    Yamazaki, T.2    Ihara, Y.3
  • 36
    • 0035131614 scopus 로고    scopus 로고
    • Molecular analysis of mutant and wild-type tau deposited in the brain affected by the FTDP-17 R406W mutation
    • Miyasaka, T., M. Morishima-Kawashima, R. Ravid, P. Heutink, J.C. van Swieten, K. Nagashima, and Y. Ihara. 2001. Molecular analysis of mutant and wild-ype tau deposited in the brain affected by the FTDP-17 R406W mutation. Am. J. Pathol. 158:373-379. doi:10.1016/S0002-9440(10)63979-X (Pubitemid 32158599)
    • (2001) American Journal of Pathology , vol.158 , Issue.2 , pp. 373-379
    • Miyasaka, T.1    Morishima-Kawashima, M.2    Ravid, R.3    Heutink, P.4    Van, S.J.C.5    Nagashima, K.6    Ihara, Y.7
  • 37
    • 0030775075 scopus 로고    scopus 로고
    • Annexin gene structures and molecular evolutionary genetics
    • DOI 10.1007/s000180050064
    • Morgan, R.O., and M.P. Fernández. 1997. Annexin gene structures and molecular evolutionary genetics. Cell. Mol. Life Sci. 53:508-515. doi:10.1007/s000180050064 (Pubitemid 27374491)
    • (1997) Cellular and Molecular Life Sciences , vol.53 , Issue.6 , pp. 508-515
    • Morgan, R.O.1    Fernandez, M.P.2
  • 39
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • doi:10.1126/science.1074952
    • Patterson, G.H., and J. Lippincott-Schwartz. 2002. A photoactivatable GFP for selective photolabeling of proteins and cells. Science. 297:1873-1877. doi:10.1126/science.1074952
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 40
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha-tubulin in mammalian cells in culture
    • doi:10.1083/jcb.104.2.289
    • Piperno, G., M. LeDizet, and X.J. Chang. 1987. Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J. Cell Biol. 104:289-302. doi:10.1083/jcb.104.2.289
    • (1987) J. Cell Biol. , vol.104 , pp. 289-302
    • Piperno, G.1    LeDizet, M.2    Chang, X.J.3
  • 41
    • 3242877433 scopus 로고    scopus 로고
    • Annexins - Unique membrane binding proteins with diverse functions
    • DOI 10.1242/jcs.01245
    • Rescher, U., and V. Gerke. 2004. Annexins-unique membrane binding proteins with diverse functions. J. Cell Sci. 117:2631-2639. doi:10.1242/jcs.01245 (Pubitemid 38997247)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 43
    • 0025296934 scopus 로고
    • Expression of annexins as a function of cellular growth state
    • doi:10.1083/jcb.111.1.229
    • Schlaepfer, D.D., and H.T. Haigler. 1990. Expression of annexins as a function of cellular growth state. J. Cell Biol. 111:229-238. doi:10.1083/jcb.111.1.229
    • (1990) J. Cell Biol. , vol.111 , pp. 229-238
    • Schlaepfer, D.D.1    Haigler, H.T.2
  • 44
    • 0030000867 scopus 로고    scopus 로고
    • Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles
    • DOI 10.1007/s004010050487
    • Spillantini, M.G., R.A. Crowther, and M. Goedert. 1996. Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles. Acta Neuropathol. 92:42-48. doi:10.1007/s004010050487 (Pubitemid 26192081)
    • (1996) Acta Neuropathologica , vol.92 , Issue.1 , pp. 42-48
    • Spillantini, M.G.1    Crowther, R.A.2    Goedert, M.3
  • 45
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • DOI 10.1529/biophysj.103.026765
    • Sprague, B.L., R.L. Pego, D.A. Stavreva, and J.G. McNally. 2004. Analysis of binding reactions by fluorescence recovery after photobleaching. Biophys. J. 86:3473-3495. doi:10.1529/biophysj.103.026765 (Pubitemid 38780231)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 47
    • 70949090395 scopus 로고    scopus 로고
    • Divergent pathways mediate spine alterations and cell death induced by amyloid-beta, wild-type tau, and R406W tau
    • doi:10.1523/JNEUROSCI.3590-09.2009
    • Tackenberg, C., and R. Brandt. 2009. Divergent pathways mediate spine alterations and cell death induced by amyloid-beta, wild-type tau, and R406W tau. J. Neurosci. 29:14439-14450. doi:10.1523/JNEUROSCI.3590-09.2009
    • (2009) J. Neurosci. , vol.29 , pp. 14439-14450
    • Tackenberg, C.1    Brandt, R.2
  • 48
    • 0027094236 scopus 로고
    • 2+- binding sites
    • Thiel, C., M. Osborn, and V. Gerke. 1992. The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites. J. Cell Sci. 103:733-742. (Pubitemid 23023243)
    • (1992) Journal of Cell Science , vol.103 , Issue.3 , pp. 733-742
    • Thiel, C.1    Osborn, M.2    Gerke, V.3
  • 49
  • 50
    • 70350674912 scopus 로고    scopus 로고
    • Microtubule binding and trapping at the tip of neurites regulate tau motion in living neurons
    • doi:10.1111/j.1600-0854.2009.00977.x
    • Weissmann, C., H.J. Reyher, A. Gauthier, H.J. Steinhoff, W. Junge, and R. Brandt. 2009. Microtubule binding and trapping at the tip of neurites regulate tau motion in living neurons. Traffic. 10:1655-1668. doi:10.1111/j.1600-0854. 2009.00977.x
    • (2009) Traffic , vol.10 , pp. 1655-1668
    • Weissmann, C.1    Reyher, H.J.2    Gauthier, A.3    Steinhoff, H.J.4    Junge, W.5    Brandt, R.6
  • 51
    • 0035468538 scopus 로고    scopus 로고
    • Frontotemporal dementia and tauopathy
    • doi:10.1007/s11910-001-0100-0
    • Yoshiyama, Y., V.M. Lee, and J.Q. Trojanowski. 2001. Frontotemporal dementia and tauopathy. Curr. Neurol. Neurosci. Rep. 1:413-421. doi:10.1007/s11910-001-0100-0
    • (2001) Curr. Neurol. Neurosci. Rep. , vol.1 , pp. 413-421
    • Yoshiyama, Y.1    Lee, V.M.2    Trojanowski, J.Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.