메뉴 건너뛰기




Volumn 5, Issue 5, 2013, Pages

Propagation of tau pathology in Alzheimer's disease: Identification of novel therapeutic targets

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PROTEIN ANTIBODY; TAU PEPTIDE; TAU PROTEIN; TAU PROTEIN ANTIBODY; UNCLASSIFIED DRUG;

EID: 84887899657     PISSN: None     EISSN: 17589193     Source Type: Journal    
DOI: 10.1186/alzrt214     Document Type: Review
Times cited : (88)

References (64)
  • 1
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • 10.1091/mbc.6.12.1887 8590813
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Trinczek B, Biernat J, Baumann K, Mandelkow EM, Mandelkow E, Mol Biol Cell 1995 6 1887 1902 10.1091/mbc.6.12.1887 8590813
    • (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
  • 2
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • 10.1007/s00401-009-0532-1 19381658
    • Classification and basic pathology of Alzheimer disease. Duyckaerts C, Delatour B, Potier MC, Acta Neuropathol 2009 118 5 36 10.1007/s00401-009-0532-1 19381658
    • (2009) Acta Neuropathol , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 4
    • 0021145680 scopus 로고
    • Alzheimer's disease: Cell-specific pathology isolates the hippocampal formation
    • Alzheimer's disease: cell-specific pathology isolates the hippocampal formation. Hyman BT, Van Hoesen GW, Damasio AR, Barnes CL, Science 1984 225 1168 1170 10.1126/science.6474172 6474172 (Pubitemid 14029099)
    • (1984) Science , vol.225 , Issue.4667 , pp. 1168-1170
    • Hyman, B.T.1    Van Hoesen, G.W.2    Damasio, A.R.3    Barnes, C.L.4
  • 6
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • 10.1007/BF00308809 1759558
    • Neuropathological stageing of Alzheimer-related changes. Braak H, Braak E, Acta Neuropathol 1991 82 239 259 10.1007/BF00308809 1759558
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 7
    • 0025717816 scopus 로고
    • The topographical and neuroanatomical distribution of neurofibrillary tangles and neuritic plaques in the cerebral cortex of patients with Alzheimer's disease
    • 10.1093/cercor/1.1.103 1822725
    • The topographical and neuroanatomical distribution of neurofibrillary tangles and neuritic plaques in the cerebral cortex of patients with Alzheimer's disease. Arnold SE, Hyman BT, Flory J, Damasio AR, Van Hoesen GW, Cereb Cortex 1991 1 103 116 10.1093/cercor/1.1.103 1822725
    • (1991) Cereb Cortex , vol.1 , pp. 103-116
    • Arnold, S.E.1    Hyman, B.T.2    Flory, J.3    Damasio, A.R.4    Van Hoesen, G.W.5
  • 8
    • 0025107676 scopus 로고
    • Memory-related neural systems in Alzheimer's disease: An anatomic study
    • Memory-related neural systems in Alzheimer's disease: an anatomic study. Hyman BT, Van Hoesen GW, Damasio AR, Neurology 1990 40 1721 1730 10.1212/WNL.40.11.1721 2234428 (Pubitemid 20383139)
    • (1990) Neurology , vol.40 , Issue.11 , pp. 1721-1730
    • Hyman, B.T.1    Van Hoesen, G.W.2    Damasio, A.R.3
  • 10
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • 10.1073/pnas.1017275108 21321227
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Munch C, O'Brien J, Bertolotti A, Proc Natl Acad Sci USA 2011 108 3548 3553 10.1073/pnas.1017275108 21321227
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3548-3553
    • Munch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 11
    • 84870061595 scopus 로고    scopus 로고
    • Cellular mechanisms of protein aggregate propagation
    • 10.1097/WCO.0b013e32835a3ee0 23108252
    • Cellular mechanisms of protein aggregate propagation. Holmes BB, Diamond MI, Curr Opin Neurol 2012 25 721 726 10.1097/WCO.0b013e32835a3ee0 23108252
    • (2012) Curr Opin Neurol , vol.25 , pp. 721-726
    • Holmes, B.B.1    Diamond, M.I.2
  • 13
    • 84879980118 scopus 로고    scopus 로고
    • Prion-like propagation of protein aggregation and related therapeutic strategies
    • 10.1007/s13311-013-0196-3 23801258
    • Prion-like propagation of protein aggregation and related therapeutic strategies. Kaufman SK, Diamond MI, Neurotherapeutics 2013 10 371 382 10.1007/s13311-013-0196-3 23801258
    • (2013) Neurotherapeutics , vol.10 , pp. 371-382
    • Kaufman, S.K.1    Diamond, M.I.2
  • 14
    • 33646043777 scopus 로고    scopus 로고
    • CaMKII activation in the entorhinal cortex disrupts previously encoded spatial memory
    • 10.1016/j.neuron.2006.03.035 16630840
    • CaMKII activation in the entorhinal cortex disrupts previously encoded spatial memory. Yasuda M, Mayford MR, Neuron 2006 50 309 318 10.1016/j.neuron.2006.03.035 16630840
    • (2006) Neuron , vol.50 , pp. 309-318
    • Yasuda, M.1    Mayford, M.R.2
  • 16
    • 84866681445 scopus 로고    scopus 로고
    • Human P301L-mutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive deficits
    • 10.1371/journal.pone.0045881 23029293
    • Human P301L-mutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive deficits. Harris JA, Koyama A, Maeda S, Ho K, Devidze N, Dubal DB, Yu GQ, Masliah E, Mucke L, PLoS One 2012 7 45881 10.1371/journal.pone.0045881 23029293
    • (2012) PLoS One , vol.7 , pp. 545881
    • Harris, J.A.1    Koyama, A.2    Maeda, S.3    Ho, K.4    Devidze, N.5    Dubal, D.B.6    Yu, G.Q.7    Masliah, E.8    Mucke, L.9
  • 18
    • 84856454190 scopus 로고    scopus 로고
    • Trans-synaptic spread of tau pathology in vivo
    • 10.1371/journal.pone.0031302 22312444
    • Trans-synaptic spread of tau pathology in vivo. Liu L, Drouet V, Wu JW, Witter MP, Small SA, Clelland C, Duff K, PLoS One 2012 7 31302 10.1371/journal.pone.0031302 22312444
    • (2012) PLoS One , vol.7 , pp. 531302
    • Liu, L.1    Drouet, V.2    Wu, J.W.3    Witter, M.P.4    Small, S.A.5    Clelland, C.6    Duff, K.7
  • 19
    • 77049123465 scopus 로고    scopus 로고
    • Interneuronal transfer of human tau between Lamprey central neurons in situ
    • 20110609
    • Interneuronal transfer of human tau between Lamprey central neurons in situ. Kim W, Lee S, Jung C, Ahmed A, Lee G, Hall GF, J Alzheimers Dis 2010 19 647 664 20110609
    • (2010) J Alzheimers Dis , vol.19 , pp. 647-664
    • Kim, W.1    Lee, S.2    Jung, C.3    Ahmed, A.4    Lee, G.5    Hall, G.F.6
  • 20
    • 84863011855 scopus 로고    scopus 로고
    • Accumulation of vesicle-associated human tau in distal dendrites drives degeneration and tau secretion in an in situ cellular tauopathy model
    • 22315694
    • Accumulation of vesicle-associated human tau in distal dendrites drives degeneration and tau secretion in an in situ cellular tauopathy model. Lee S, Kim W, Li Z, Hall GF, Int J Alzheimers Dis 2012 2012 172837 22315694
    • (2012) Int J Alzheimers Dis , vol.2012 , pp. 172837
    • Lee, S.1    Kim, W.2    Li, Z.3    Hall, G.F.4
  • 21
    • 84871158190 scopus 로고    scopus 로고
    • Hyperphosphorylation and cleavage at D421 enhance tau secretion
    • 10.1371/journal.pone.0036873 22615831
    • Hyperphosphorylation and cleavage at D421 enhance tau secretion. Plouffe V, Mohamed NV, Rivest-McGraw J, Bertrand J, Lauzon M, Leclerc N, PLoS One 2012 7 36873 10.1371/journal.pone.0036873 22615831
    • (2012) PLoS One , vol.7 , pp. 536873
    • Plouffe, V.1    Mohamed, N.V.2    Rivest-Mcgraw, J.3    Bertrand, J.4    Lauzon, M.5    Leclerc, N.6
  • 22
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • 10.1074/jbc.M111.277061 22057275
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. Saman S, Kim W, Raya M, Visnick Y, Miro S, Jackson B, McKee AC, Alvarez VE, Lee NC, Hall GF, J Biol Chem 2012 287 3842 3849 10.1074/jbc.M111.277061 22057275
    • (2012) J Biol Chem , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Jackson, B.6    McKee, A.C.7    Alvarez, V.E.8    Lee, N.C.9    Hall, G.F.10
  • 23
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • 10.1038/embor.2013.15 23412472
    • Physiological release of endogenous tau is stimulated by neuronal activity. Pooler AM, Phillips EC, Lau DH, Noble W, Hanger DP, EMBO Rep 2013 14 389 394 10.1038/embor.2013.15 23412472
    • (2013) EMBO Rep , vol.14 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.3    Noble, W.4    Hanger, D.P.5
  • 25
    • 84980053087 scopus 로고    scopus 로고
    • Multiple mechanisms of extracellular tau spreading in a non-transgenic tauopathy model
    • 23383401
    • Multiple mechanisms of extracellular tau spreading in a non-transgenic tauopathy model. Le MN, Kim W, Lee S, McKee AC, Hall GF, Am J Neurodegener Dis 2012 1 316 333 23383401
    • (2012) Am J Neurodegener Dis , vol.1 , pp. 316-333
    • Le, M.N.1    Kim, W.2    Lee, S.3    McKee, A.C.4    Hall, G.F.5
  • 26
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • 10.1016/j.ajpath.2012.06.033 22867711
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Tai HC, Serrano-Pozo A, Hashimoto T, Frosch MP, Spires-Jones TL, Hyman BT, Am J Pathol 2012 181 1426 1435 10.1016/j.ajpath.2012.06.033 22867711
    • (2012) Am J Pathol , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3    Frosch, M.P.4    Spires-Jones, T.L.5    Hyman, B.T.6
  • 28
    • 84866361333 scopus 로고    scopus 로고
    • Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-D-aspartate receptor-dependent tau phosphorylation
    • 10.1074/jbc.M112.401240 22833681
    • Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-D-aspartate receptor-dependent tau phosphorylation. Mondragon-Rodriguez S, Trillaud-Doppia E, Dudilot A, Bourgeois C, Lauzon M, Leclerc N, Boehm J, J Biol Chem 2012 287 32040 32053 10.1074/jbc.M112.401240 22833681
    • (2012) J Biol Chem , vol.287 , pp. 32040-32053
    • Mondragon-Rodriguez, S.1    Trillaud-Doppia, E.2    Dudilot, A.3    Bourgeois, C.4    Lauzon, M.5    Leclerc, N.6    Boehm, J.7
  • 29
    • 77955941947 scopus 로고    scopus 로고
    • Functional implications of the association of tau with the plasma membrane
    • 10.1042/BST0381012 20658995
    • Functional implications of the association of tau with the plasma membrane. Pooler AM, Hanger DP, Biochem Soc Trans 2010 38 1012 1015 10.1042/BST0381012 20658995
    • (2010) Biochem Soc Trans , vol.38 , pp. 1012-1015
    • Pooler, A.M.1    Hanger, D.P.2
  • 32
    • 84878439275 scopus 로고    scopus 로고
    • Clinical utility and analytical challenges in measurement of cerebrospinal fluid amyloid-beta1-42 and tau proteins as Alzheimer disease biomarkers
    • 10.1373/clinchem.2013.202937 23519967
    • Clinical utility and analytical challenges in measurement of cerebrospinal fluid amyloid-beta1-42 and tau proteins as Alzheimer disease biomarkers. Kang JH, Korecka M, Toledo JB, Trojanowski JQ, Shaw LM, Clin Chem 2013 59 903 916 10.1373/clinchem.2013.202937 23519967
    • (2013) Clin Chem , vol.59 , pp. 903-916
    • Kang, J.H.1    Korecka, M.2    Toledo, J.B.3    Trojanowski, J.Q.4    Shaw, L.M.5
  • 33
    • 84864935106 scopus 로고    scopus 로고
    • Constitutive secretion of tau protein by an unconventional mechanism
    • 10.1016/j.nbd.2012.05.021 22668776
    • Constitutive secretion of tau protein by an unconventional mechanism. Chai X, Dage JL, Citron M, Neurobiol Dis 2012 48 356 366 10.1016/j.nbd.2012.05. 021 22668776
    • (2012) Neurobiol Dis , vol.48 , pp. 356-366
    • Chai, X.1    Dage, J.L.2    Citron, M.3
  • 34
    • 84871141635 scopus 로고    scopus 로고
    • Extracellular Tau levels are influenced by variability in Tau that is associated with tauopathies
    • 10.1074/jbc.M112.380642 23105105
    • Extracellular Tau levels are influenced by variability in Tau that is associated with tauopathies. Karch CM, Jeng AT, Goate AM, J Biol Chem 2012 287 42751 42762 10.1074/jbc.M112.380642 23105105
    • (2012) J Biol Chem , vol.287 , pp. 42751-42762
    • Karch, C.M.1    Jeng, A.T.2    Goate, A.M.3
  • 35
    • 84878879881 scopus 로고    scopus 로고
    • Exosomes: Mediators of communication in eukaryotes
    • 10.4067/S0716-97602013000100001 23760408
    • Exosomes: mediators of communication in eukaryotes. Lopez-Verrilli MA, Court FA, Biol Res 2013 46 5 11 10.4067/S0716-97602013000100001 23760408
    • (2013) Biol Res , vol.46 , pp. 5-11
    • Lopez-Verrilli, M.A.1    Court, F.A.2
  • 36
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • 10.1083/jcb.131.5.1327 8522593
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. Brandt R, Leger J, Lee G, J Cell Biol 1995 131 1327 1340 10.1083/jcb.131.5.1327 8522593
    • (1995) J Cell Biol , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 38
    • 84655176335 scopus 로고    scopus 로고
    • Proteostasis of tau. Tau overexpression results in its secretion via membrane vesicles
    • 10.1016/j.febslet.2011.11.022 22138183
    • Proteostasis of tau. Tau overexpression results in its secretion via membrane vesicles. Simon D, Garcia-Garcia E, Royo F, Falcon-Perez JM, Avila J, FEBS Lett 2012 586 47 54 10.1016/j.febslet.2011.11.022 22138183
    • (2012) FEBS Lett , vol.586 , pp. 47-54
    • Simon, D.1    Garcia-Garcia, E.2    Royo, F.3    Falcon-Perez, J.M.4    Avila, J.5
  • 39
    • 84862003756 scopus 로고    scopus 로고
    • Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes
    • 10.1074/jbc.M111.323279 22496370
    • Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes. Santa-Maria I, Varghese M, Ksiezak-Reding H, Dzhun A, Wang J, Pasinetti GM, J Biol Chem 2012 287 20522 20533 10.1074/jbc.M111.323279 22496370
    • (2012) J Biol Chem , vol.287 , pp. 20522-20533
    • Santa-Maria, I.1    Varghese, M.2    Ksiezak-Reding, H.3    Dzhun, A.4    Wang, J.5    Pasinetti, G.M.6
  • 41
    • 53049107224 scopus 로고    scopus 로고
    • Proteomic analysis of exosomes from human neural stem cells by flow field-flow fractionation and nanoflow liquid chromatography-tandem mass spectrometry
    • 10.1021/pr800225z 18570454
    • Proteomic analysis of exosomes from human neural stem cells by flow field-flow fractionation and nanoflow liquid chromatography-tandem mass spectrometry. Kang D, Oh S, Ahn SM, Lee BH, Moon MH, J Proteome Res 2008 7 3475 3480 10.1021/pr800225z 18570454
    • (2008) J Proteome Res , vol.7 , pp. 3475-3480
    • Kang, D.1    Oh, S.2    Ahn, S.M.3    Lee, B.H.4    Moon, M.H.5
  • 42
    • 0034607960 scopus 로고    scopus 로고
    • Quantification of tau phosphorylated at threonine 181 in human cerebrospinal fluid: A sandwich ELISA with a synthetic phosphopeptide for standardization
    • DOI 10.1016/S0304-3940(00)01036-3, PII S0304394000010363
    • Quantification of tau phosphorylated at threonine 181 in human cerebrospinal fluid: a sandwich ELISA with a synthetic phosphopeptide for standardization. Vanmechelen E, Vanderstichele H, Davidsson P, Van Kerschaver E, Van Der Perre B, Sjogren M, Andreasen N, Blennow K, Neurosci Lett 2000 285 49 52 10.1016/S0304-3940(00)01036-3 10788705 (Pubitemid 30224621)
    • (2000) Neuroscience Letters , vol.285 , Issue.1 , pp. 49-52
    • Vanmechelen, E.1    Vanderstichele, H.2    Davidsson, P.3    Van Kerschaver, E.4    Van Der Perre, B.5    Sjogren, M.6    Andreasen, N.7    Blennow, K.8
  • 43
    • 84869090391 scopus 로고    scopus 로고
    • Calcium phosphatase calcineurin influences tau metabolism
    • 10.1016/j.neurobiolaging.2012.05.003 22676853
    • Calcium phosphatase calcineurin influences tau metabolism. Karch CM, Jeng AT, Goate AM, Neurobiol Aging 2013 34 374 386 10.1016/j.neurobiolaging.2012.05. 003 22676853
    • (2013) Neurobiol Aging , vol.34 , pp. 374-386
    • Karch, C.M.1    Jeng, A.T.2    Goate, A.M.3
  • 45
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • 10.1074/jbc.M808759200 19282288
    • Propagation of tau misfolding from the outside to the inside of a cell. Frost B, Jacks RL, Diamond MI, J Biol Chem 2009 284 12845 12852 10.1074/jbc.M808759200 19282288
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 46
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy
    • 10.1523/JNEUROSCI.2642-12.2013 23325240
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy. Iba M, Guo JL, McBride JD, Zhang B, Trojanowski JQ, Lee VM, J Neurosci 2013 33 1024 1037 10.1523/JNEUROSCI.2642-12.2013 23325240
    • (2013) J Neurosci , vol.33 , pp. 1024-1037
    • Iba, M.1    Guo, J.L.2    McBride, J.D.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 50
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of Tau aggregation by fibrillar species
    • 10.1074/jbc.M112.346072 22461630
    • Trans-cellular propagation of Tau aggregation by fibrillar species. Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond MI, J Biol Chem 2012 287 19440 19451 10.1074/jbc.M112.346072 22461630
    • (2012) J Biol Chem , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 51
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles
    • 10.1074/jbc.M110.209296 21372138
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. Guo JL, Lee VM, J Biol Chem 2011 286 15317 15331 10.1074/jbc.M110.209296 21372138
    • (2011) J Biol Chem , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.2
  • 52
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • 20029438
    • Prion-like mechanisms in neurodegenerative diseases. Frost B, Diamond MI, Nat Rev Neurosci 2010 11 155 159 20029438
    • (2010) Nat Rev Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 53
    • 84874853965 scopus 로고    scopus 로고
    • Mechanisms of protein seeding in neurodegenerative diseases
    • 10.1001/jamaneurol.2013.1453 23599928
    • Mechanisms of protein seeding in neurodegenerative diseases. Walker LC, Diamond MI, Duff KE, Hyman BT, JAMA Neurol 2013 70 304 310 10.1001/jamaneurol. 2013.1453 23599928
    • (2013) JAMA Neurol , vol.70 , pp. 304-310
    • Walker, L.C.1    Diamond, M.I.2    Duff, K.E.3    Hyman, B.T.4
  • 54
    • 84879040199 scopus 로고    scopus 로고
    • Progress and developments in tau aggregation inhibitors for Alzheimer disease
    • 10.1021/jm3017317 23484434
    • Progress and developments in tau aggregation inhibitors for Alzheimer disease. Bulic B, Pickhardt M, Mandelkow E, J Med Chem 2013 56 4135 4155 10.1021/jm3017317 23484434
    • (2013) J Med Chem , vol.56 , pp. 4135-4155
    • Bulic, B.1    Pickhardt, M.2    Mandelkow, E.3
  • 58
    • 41149111293 scopus 로고    scopus 로고
    • Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells
    • 10.1016/j.mcn.2007.12.010 18272392
    • Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells. Gomez-Ramos A, Diaz-Hernandez M, Rubio A, Miras-Portugal MT, Avila J, Mol Cell Neurosci 2008 37 673 681 10.1016/j.mcn.2007.12.010 18272392
    • (2008) Mol Cell Neurosci , vol.37 , pp. 673-681
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Rubio, A.3    Miras-Portugal, M.T.4    Avila, J.5
  • 59
    • 84881546833 scopus 로고    scopus 로고
    • The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease
    • 10.1016/j.arr.2013.03.002 23528367
    • The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease. Crimins JL, Pooler A, Polydoro M, Luebke JI, Spires-Jones TL, Ageing Res Rev 2013 12 757 763 10.1016/j.arr.2013.03.002 23528367
    • (2013) Ageing Res Rev , vol.12 , pp. 757-763
    • Crimins, J.L.1    Pooler, A.2    Polydoro, M.3    Luebke, J.I.4    Spires-Jones, T.L.5
  • 60
    • 80053202160 scopus 로고    scopus 로고
    • Passive immunization with anti-Tau antibodies in two transgenic models: Reduction of Tau pathology and delay of disease progression
    • 10.1074/jbc.M111.229633 21841002
    • Passive immunization with anti-Tau antibodies in two transgenic models: reduction of Tau pathology and delay of disease progression. Chai X, Wu S, Murray TK, Kinley R, Cella CV, Sims H, Buckner N, Hanmer J, Davies P, O'Neill MJ, Hutton ML, Citron M, J Biol Chem 2011 286 34457 34467 10.1074/jbc.M111. 229633 21841002
    • (2011) J Biol Chem , vol.286 , pp. 34457-34467
    • Chai, X.1    Wu, S.2    Murray, T.K.3    Kinley, R.4    Cella, C.V.5    Sims, H.6    Buckner, N.7    Hanmer, J.8    Davies, P.9    O'Neill, M.J.10    Hutton, M.L.11    Citron, M.12
  • 61
    • 79960563632 scopus 로고    scopus 로고
    • Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain
    • 10.1111/j.1471-4159.2011.07337.x 21644996
    • Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain. Boutajangout A, Ingadottir J, Davies P, Sigurdsson EM, J Neurochem 2011 118 658 667 10.1111/j.1471-4159.2011.07337.x 21644996
    • (2011) J Neurochem , vol.118 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 62
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice
    • 10.1371/journal.pone.0026860 22174735
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice. Bi M, Ittner A, Ke YD, Gotz J, Ittner LM, PLoS One 2011 6 26860 10.1371/journal.pone.0026860 22174735
    • (2011) PLoS One , vol.6 , pp. 526860
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Gotz, J.4    Ittner, L.M.5
  • 63
    • 84879968745 scopus 로고    scopus 로고
    • Developing therapeutic antibodies for neurodegenerative disease
    • 10.1007/s13311-013-0187-4 23549647
    • Developing therapeutic antibodies for neurodegenerative disease. Yu YJ, Watts RJ, Neurotherapeutics 2013 10 459 472 10.1007/s13311-013-0187-4 23549647
    • (2013) Neurotherapeutics , vol.10 , pp. 459-472
    • Yu, Y.J.1    Watts, R.J.2
  • 64
    • 0842265475 scopus 로고    scopus 로고
    • The neuropathology of frontotemporal lobar degeneration with respect to the cytological and biochemical characteristics of tau protein
    • DOI 10.1046/j.0305-1846.2003.00481.x
    • The neuropathology of frontotemporal lobar degeneration with respect to the cytological and biochemical characteristics of tau protein. Taniguchi S, McDonagh AM, Pickering-Brown SM, Umeda Y, Iwatsubo T, Hasegawa M, Mann DM, Neuropathol Appl Neurobiol 2004 30 1 18 10.1046/j.0305-1846.2003.00481.x 14720172 (Pubitemid 38177998)
    • (2004) Neuropathology and Applied Neurobiology , vol.30 , Issue.1 , pp. 1-18
    • Taniguchi, S.1    McDonagh, A.M.2    Pickering-Brown, S.M.3    Umeda, Y.4    Iwatsubo, T.5    Hasegawa, M.6    Mann, D.M.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.