메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

Efficacy and safety of a liposome-based vaccine against protein Tau, assessed in Tau.P301L mice that model tauopathy

Author keywords

[No Author keywords available]

Indexed keywords

ACI 35 VACCINE; EPITOPE; TAU PROTEIN; UNCLASSIFIED DRUG; VACCINE; ALZHEIMER DISEASE VACCINE; LIPOSOME; NEUTRALIZING ANTIBODY; PEPTIDE; PHOSPHOPROTEIN;

EID: 84922479255     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0072301     Document Type: Article
Times cited : (217)

References (72)
  • 2
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland DW, Hwo SY, Kirschner MW (1977) Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J Mol Biol 2: 227-247.
    • (1977) J Mol Biol , vol.2 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 3
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • Chen J, Kanai Y, Cowan NJ, Hirokawa N (1992) Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature 6405: 674-677.
    • (1992) Nature , vol.6405 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 4
    • 44949259180 scopus 로고    scopus 로고
    • Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis
    • Rosenberg KJ, Ross JL, Feinstein HE, Feinstein SC, Israelachvili J (2008) Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis. Proc Natl Acad Sci U S A 21: 7445-7450.
    • (2008) Proc Natl Acad Sci U S A , vol.21 , pp. 7445-7450
    • Rosenberg, K.J.1    Ross, J.L.2    Feinstein, H.E.3    Feinstein, S.C.4    Israelachvili, J.5
  • 5
    • 0027361281 scopus 로고
    • Microtubuleassociated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke E, Tung YC, Shaikh S, Alonso AC, Iqbal K, et al. (1993) Microtubuleassociated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem 32: 24374-24384.
    • (1993) J Biol Chem , vol.32 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5
  • 6
    • 0028856460 scopus 로고
    • An English translation of Alzheimer's 1907 paper, '' Uber eine eigenartige Erkankung der Hirnrinde''
    • Alzheimer A, Stelzmann RA, Schnitzlein HN, Murtagh FR (1995) An English translation of Alzheimer's 1907 paper, ''Uber eine eigenartige Erkankung der Hirnrinde''. Clin Anat 6: 429-431.
    • (1995) Clin Anat , vol.6 , pp. 429-431
    • Alzheimer, A.1    Stelzmann, R.A.2    Schnitzlein, H.N.3    Murtagh, F.R.4
  • 7
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 4: 239-259.
    • (1991) Acta Neuropathol , vol.4 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 8
    • 0033639241 scopus 로고    scopus 로고
    • Novel method to quantify neuropil threads in brains from elders with or without cognitive impairment
    • Mitchell TW, Nissanov J, Han LY, Mufson EJ, Schneider JA, et al. (2000) Novel method to quantify neuropil threads in brains from elders with or without cognitive impairment. J Histochem Cytochem 12: 1627-1638.
    • (2000) J Histochem Cytochem , vol.12 , pp. 1627-1638
    • Mitchell, T.W.1    Nissanov, J.2    Han, L.Y.3    Mufson, E.J.4    Schneider, J.A.5
  • 9
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • Duyckaerts C, Delatour B, Potier MC (2009) Classification and basic pathology of Alzheimer disease. Acta Neuropathol 1: 5-36.
    • (2009) Acta Neuropathol , vol.1 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 10
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada PV, Growdon JH, Hedley-Whyte ET, Hyman BT (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 3 Pt 1: 631-639.
    • (1992) Neurology 3 Pt , vol.1 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 11
    • 0032894121 scopus 로고    scopus 로고
    • The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease
    • Delacourte A, David JP, Sergeant N, Buee L, Wattez A, et al. (1999) The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease. Neurology 6: 1158-1165.
    • (1999) Neurology , vol.6 , pp. 1158-1165
    • Delacourte, A.1    David, J.P.2    Sergeant, N.3    Buee, L.4    Wattez, A.5
  • 12
    • 84863641754 scopus 로고    scopus 로고
    • Protein tau: Prime cause of synaptic and neuronal degeneration in Alzheimer's disease
    • Crespo-Biel N, Theunis C, van Leuven F. (2012) Protein tau: prime cause of synaptic and neuronal degeneration in Alzheimer's disease. Int J Alzheimers Dis 251426.
    • (2012) Int J Alzheimers Dis , pp. 251426
    • Crespo-Biel, N.1    Theunis, C.2    Van Leuven, F.3
  • 13
    • 0026567475 scopus 로고
    • Familial presenile dementia with psychosis associated with cortical neurofibrillary tangles and degeneration of the amygdala
    • Sumi SM, Bird TD, Nochlin D, Raskind MA (1992) Familial presenile dementia with psychosis associated with cortical neurofibrillary tangles and degeneration of the amygdala. Neurology 1: 120-127.
    • (1992) Neurology , vol.1 , pp. 120-127
    • Sumi, S.M.1    Bird, T.D.2    Nochlin, D.3    Raskind, M.A.4
  • 14
    • 0003374626 scopus 로고    scopus 로고
    • Tau protein pathology in neurodegenerative diseases
    • Spillantini MG, Goedert M (1998) Tau protein pathology in neurodegenerative diseases. Trends Neurosci 10: 428-433.
    • (1998) Trends Neurosci , vol.10 , pp. 428-433
    • Spillantini, M.G.1    Goedert, M.2
  • 15
    • 0033850080 scopus 로고    scopus 로고
    • Abnormal tau-containing filaments in neurodegenerative diseases
    • Crowther RA, Goedert M (2000) Abnormal tau-containing filaments in neurodegenerative diseases. J Struct Biol 2-3: 271-279.
    • (2000) J Struct Biol 2-3 , pp. 271-279
    • Crowther, R.A.1    Goedert, M.2
  • 17
    • 61849185913 scopus 로고    scopus 로고
    • Recent developments in Alzheimer's disease therapeutics
    • Rafii MS, Aisen PS (2009) Recent developments in Alzheimer's disease therapeutics. BMC Med 7.
    • (2009) BMC Med , vol.7
    • Rafii, M.S.1    Aisen, P.S.2
  • 18
    • 80053971718 scopus 로고    scopus 로고
    • Current and emerging drug treatment options for Alzheimer's disease: A systematic review
    • Herrmann N, Chau SA, Kircanski I, Lanctot KL (2011) Current and emerging drug treatment options for Alzheimer's disease: a systematic review. Drugs 15: 2031-2065.
    • (2011) Drugs , vol.15 , pp. 2031-2065
    • Herrmann, N.1    Chau, S.A.2    Kircanski, I.3    Lanctot, K.L.4
  • 19
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloidbeta peptide: A case report
    • Nicoll JA, Wilkinson D, Holmes C, Steart P, Markham H, et al. (2003) Neuropathology of human Alzheimer disease after immunization with amyloidbeta peptide: a case report. Nat Med 4: 448-452.
    • (2003) Nat Med , vol.4 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5
  • 20
    • 20944448555 scopus 로고    scopus 로고
    • Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial
    • Gilman S, Koller M, Black RS, Jenkins L, Griffith SG, et al. (2005) Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial. Neurology 9: 1553-1562.
    • (2005) Neurology , vol.9 , pp. 1553-1562
    • Gilman, S.1    Koller, M.2    Black, R.S.3    Jenkins, L.4    Griffith, S.G.5
  • 21
    • 0037133324 scopus 로고    scopus 로고
    • A liposome-based therapeutic vaccine against beta -amyloid plaques on the pancreas of transgenic NORBA mice
    • Nicolau C, Greferath R, Balaban TS, Lazarte JE, Hopkins RJ (2002) A liposome-based therapeutic vaccine against beta -amyloid plaques on the pancreas of transgenic NORBA mice. Proc Natl Acad Sci U S A 4: 2332-2337.
    • (2002) Proc Natl Acad Sci U S A , vol.4 , pp. 2332-2337
    • Nicolau, C.1    Greferath, R.2    Balaban, T.S.3    Lazarte, J.E.4    Hopkins, R.J.5
  • 22
    • 34547473731 scopus 로고    scopus 로고
    • Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice
    • Muhs A, Hickman DT, Pihlgren M, Chuard N, Giriens V, et al. (2007) Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice. Proc Natl Acad Sci U S A 23: 9810-9815.
    • (2007) Proc Natl Acad Sci U S A , vol.23 , pp. 9810-9815
    • Muhs, A.1    Hickman, D.T.2    Pihlgren, M.3    Chuard, N.4    Giriens, V.5
  • 23
    • 79954592900 scopus 로고    scopus 로고
    • Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases
    • Hickman DT, Lopez-Deber MP, Ndao DM, Silva AB, Nand D, et al. (2011) Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases. J Biol Chem 16: 13966-13976.
    • (2011) J Biol Chem , vol.16 , pp. 13966-13976
    • Hickman, D.T.1    Lopez-Deber, M.P.2    Ndao, D.M.3    Silva, A.B.4    Nand, D.5
  • 24
    • 84872093437 scopus 로고    scopus 로고
    • TLR4 and TRIF-dependent stimulation of B lymphocytes by peptide liposomes enables T-cell independent isotype switch in mice
    • Pihlgren M, Silva AB, Madani R, Giriens V, Waeckerle-Men Y, et al. (2013) TLR4 and TRIF-dependent stimulation of B lymphocytes by peptide liposomes enables T-cell independent isotype switch in mice. Blood 1: 85-94.
    • (2013) Blood , vol.1 , pp. 85-94
    • Pihlgren, M.1    Silva, A.B.2    Madani, R.3    Giriens, V.4    Waeckerle-Men, Y.5
  • 25
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH (1992) Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci Lett 1: 58-62.
    • (1992) Neurosci Lett , vol.1 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 26
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg SG, Davies P (1990) A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci U S A 15: 5827-5831.
    • (1990) Proc Natl Acad Sci U S A , vol.15 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 27
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L, Jr., Feiner L, Lang E, Szendrei GI, Goedert M, et al. (1994) Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J Neurosci Res 6: 669-673.
    • (1994) J Neurosci Res , vol.6 , pp. 669-673
    • Otvos, L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5
  • 28
    • 0040299037 scopus 로고    scopus 로고
    • AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease
    • Buee-Scherrer V, Condamines O, Mourton-Gilles C, Jakes R, Goedert M, et al. (1996) AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease. Brain Res Mol Brain Res 1-2: 79-88.
    • (1996) Brain Res Mol Brain Res , vol.1-2 , pp. 79-88
    • Buee-Scherrer, V.1    Condamines, O.2    Mourton-Gilles, C.3    Jakes, R.4    Goedert, M.5
  • 29
    • 0034738171 scopus 로고    scopus 로고
    • Binding specificity of monoclonal antibody AD2: Influence of the phosphorylation state of tau
    • Torreilles F, Roquet F, Granier C, Pau B, Mourton-Gilles C (2000) Binding specificity of monoclonal antibody AD2: influence of the phosphorylation state of tau. Brain Res Mol Brain Res 1-2: 181-185.
    • (2000) Brain Res Mol Brain Res , vol.1-2 , pp. 181-185
    • Torreilles, F.1    Roquet, F.2    Granier, C.3    Pau, B.4    Mourton-Gilles, C.5
  • 30
    • 13644268449 scopus 로고    scopus 로고
    • Changed conformation of mutant Tau-P301L underlies the moribund tauopathy, absent in progressive, nonlethal axonopathy of Tau-4R/2N transgenic mice
    • Terwel D, Lasrado R, Snauwaert J, Vandeweert E, Van Haesendonck C, et al. (2005) Changed conformation of mutant Tau-P301L underlies the moribund tauopathy, absent in progressive, nonlethal axonopathy of Tau-4R/2N transgenic mice. J Biol Chem 5: 3963-3973.
    • (2005) J Biol Chem , vol.5 , pp. 3963-3973
    • Terwel, D.1    Lasrado, R.2    Snauwaert, J.3    Vandeweert, E.4    Van Haesendonck, C.5
  • 31
    • 40449098952 scopus 로고    scopus 로고
    • Amyloid activates GSK-3beta to aggravate neuronal tauopathy in bigenic mice
    • Terwel D, Muyllaert D, Dewachter I, Borghgraef P, Croes S, et al. (2008) Amyloid activates GSK-3beta to aggravate neuronal tauopathy in bigenic mice. Am J Pathol 3: 786-798.
    • (2008) Am J Pathol , vol.3 , pp. 786-798
    • Terwel, D.1    Muyllaert, D.2    Dewachter, I.3    Borghgraef, P.4    Croes, S.5
  • 32
    • 33645454579 scopus 로고    scopus 로고
    • Improved long-term potentiation and memory in young tau-P301L transgenic mice before onset of hyperphosphorylation and tauopathy
    • Boekhoorn K, Terwel D, Biemans B, Borghgraef P, Wiegert O, et al. (2006) Improved long-term potentiation and memory in young tau-P301L transgenic mice before onset of hyperphosphorylation and tauopathy. Journal of Neuroscience 13: 3514-3523.
    • (2006) Journal of Neuroscience , vol.13 , pp. 3514-3523
    • Boekhoorn, K.1    Terwel, D.2    Biemans, B.3    Borghgraef, P.4    Wiegert, O.5
  • 34
    • 76149113615 scopus 로고    scopus 로고
    • Upper airway dysfunction of Tau-P301L mice correlates with tauopathy in midbrain and ponto-medullary brainstem nuclei
    • Dutschmann M, Menuet C, Stettner GM, Gestreau C, Borghgraef P, et al. (2010) Upper airway dysfunction of Tau-P301L mice correlates with tauopathy in midbrain and ponto-medullary brainstem nuclei. Journal of Neuroscience 5: 1810-1821.
    • (2010) Journal of Neuroscience , vol.5 , pp. 1810-1821
    • Dutschmann, M.1    Menuet, C.2    Stettner, G.M.3    Gestreau, C.4    Borghgraef, P.5
  • 35
    • 80054053747 scopus 로고    scopus 로고
    • Agerelated impairment of ultrasonic vocalization in Tau.P301L mice: Possible implication for progressive language disorders
    • Menuet C, Cazals Y, Gestreau C, Borghgraef P, Gielis L, et al. (2011) Agerelated impairment of ultrasonic vocalization in Tau.P301L mice: possible implication for progressive language disorders. PLoS One 10: e25770.
    • (2011) PLoS One , vol.10 , pp. e25770
    • Menuet, C.1    Cazals, Y.2    Gestreau, C.3    Borghgraef, P.4    Gielis, L.5
  • 36
    • 80052352120 scopus 로고    scopus 로고
    • Raphe tauopathy alters serotonin metabolism and breathing activity in terminal Tau.P301L mice: Possible implications for tauopathies and Alzheimer's disease
    • Menuet C, Borghgraef P, Matarazzo V, Gielis L, Lajard AM, et al. (2011) Raphe tauopathy alters serotonin metabolism and breathing activity in terminal Tau.P301L mice: possible implications for tauopathies and Alzheimer's disease. Respir Physiol Neurobiol 2: 290-303.
    • (2011) Respir Physiol Neurobiol , vol.2 , pp. 290-303
    • Menuet, C.1    Borghgraef, P.2    Matarazzo, V.3    Gielis, L.4    Lajard, A.M.5
  • 37
    • 83055160858 scopus 로고    scopus 로고
    • Early Improved and Late Defective Cognition is Reflected by Dendritic Spines in Tau.P301L Mice
    • Kremer A, Maurin H, Demedts D, Devijver H, Borghgraef P, et al. (2011) Early Improved and Late Defective Cognition Is Reflected by Dendritic Spines in Tau.P301L Mice. Journal of Neuroscience 49: 18036-18047.
    • (2011) Journal of Neuroscience , vol.49 , pp. 18036-18047
    • Kremer, A.1    Maurin, H.2    Demedts, D.3    Devijver, H.4    Borghgraef, P.5
  • 38
    • 84877940109 scopus 로고    scopus 로고
    • Tauopathy differentially affects Cell Adhesion Molecules in mouse brain: Early down-regulation of Nectin-3 in Stratum Lacunosum Moleculare
    • Maurin H, Seymour CM, Lechat B, Borghgraef P, Devijver H, et al. (2013) Tauopathy differentially affects Cell Adhesion Molecules in mouse brain: early down-regulation of Nectin-3 in Stratum Lacunosum Moleculare. PLoS One May 21, 2013.
    • (2013) PLoS One May , vol.21 , pp. 2013
    • Maurin, H.1    Seymour, C.M.2    Lechat, B.3    Borghgraef, P.4    Devijver, H.5
  • 39
    • 23944469853 scopus 로고    scopus 로고
    • Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast
    • Vandebroek T, Vanhelmont T, Terwel D, Borghgraef P, Lemaire K, et al. (2005) Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast. Biochemistry 34: 11466-11475.
    • (2005) Biochemistry , vol.34 , pp. 11466-11475
    • Vandebroek, T.1    Vanhelmont, T.2    Terwel, D.3    Borghgraef, P.4    Lemaire, K.5
  • 40
    • 33748746596 scopus 로고    scopus 로고
    • Microtubule binding and clustering of human Tau-4R and Tau- P301L proteins isolated from yeast deficient in orthologues of glycogen synthase kinase-3beta or cdk5
    • Vandebroek T, Terwel D, Vanhelmont T, Gysemans M, Van Haesendonck C, et al. (2006) Microtubule binding and clustering of human Tau-4R and Tau- P301L proteins isolated from yeast deficient in orthologues of glycogen synthase kinase-3beta or cdk5. J Biol Chem 35: 25388-25397.
    • (2006) J Biol Chem , vol.35 , pp. 25388-25397
    • Vandebroek, T.1    Terwel, D.2    Vanhelmont, T.3    Gysemans, M.4    Van Haesendonck, C.5
  • 41
    • 33749614555 scopus 로고    scopus 로고
    • Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein
    • Rosenmann H, Grigoriadis N, Karussis D, Boimel M, Touloumi O, et al. (2006) Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein. Arch Neurol 10: 1459-1467.
    • (2006) Arch Neurol , vol.10 , pp. 1459-1467
    • Rosenmann, H.1    Grigoriadis, N.2    Karussis, D.3    Boimel, M.4    Touloumi, O.5
  • 42
    • 0037317234 scopus 로고    scopus 로고
    • Vaccination with amyloid-beta peptide induces autoimmune encephalomyelitis in C57/BL6 mice
    • Furlan R, Brambilla E, Sanvito F, Roccatagliata L, Olivieri S, et al. (2003) Vaccination with amyloid-beta peptide induces autoimmune encephalomyelitis in C57/BL6 mice. Brain Pt 2: 285-291.
    • (2003) Brain Pt , vol.2 , pp. 285-291
    • Furlan, R.1    Brambilla, E.2    Sanvito, F.3    Roccatagliata, L.4    Olivieri, S.5
  • 43
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo JM, Gilman S, Dartigues JF, Laurent B, Puel M, et al. (2003) Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology 1: 46-54.
    • (2003) Neurology , vol.1 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3    Laurent, B.4    Puel, M.5
  • 44
    • 40449086748 scopus 로고    scopus 로고
    • Progress in the active immunotherapeutic approach to Alzheimer's disease: Clinical investigations into AN1792-associated meningoencephalitis
    • Pride M, Seubert P, Grundman M, Hagen M, Eldridge J, et al. (2008) Progress in the active immunotherapeutic approach to Alzheimer's disease: clinical investigations into AN1792-associated meningoencephalitis. Neurodegener Dis 3-4: 194-196.
    • (2008) Neurodegener Dis , vol.3-4 , pp. 194-196
    • Pride, M.1    Seubert, P.2    Grundman, M.3    Hagen, M.4    Eldridge, J.5
  • 45
    • 34250876388 scopus 로고    scopus 로고
    • Immunology. The shape of things to come
    • Fitzgerald KA, Golenbock DT (2007) Immunology. The shape of things to come. Science 5831: 1574-1576.
    • (2007) Science , vol.5831 , pp. 1574-1576
    • Fitzgerald, K.A.1    Golenbock, D.T.2
  • 46
    • 34250854079 scopus 로고    scopus 로고
    • The vaccine adjuvant monophosphoryl lipid A as a TRIF-biased agonist of TLR4
    • Mata-Haro V, Cekic C, Martin M, Chilton PM, Casella CR, et al. (2007) The vaccine adjuvant monophosphoryl lipid A as a TRIF-biased agonist of TLR4. Science 5831: 1628-1632.
    • (2007) Science , vol.5831 , pp. 1628-1632
    • Mata-Haro, V.1    Cekic, C.2    Martin, M.3    Chilton, P.M.4    Casella, C.R.5
  • 47
    • 0016840819 scopus 로고
    • Radioimmunoassays for Ig classes G, A, M, D, and e in spinal fluids: Normal values of different age groups
    • Nerenberg ST and Prasad R (1975) Radioimmunoassays for Ig classes G, A, M, D, and E in spinal fluids: normal values of different age groups. J Lab Clin Med 5: 887-898.
    • (1975) J Lab Clin Med , vol.5 , pp. 887-898
    • Nerenberg, S.T.1    Prasad, R.2
  • 48
    • 0025213058 scopus 로고
    • A saturable mechanism for transport of immunoglobulin G across the blood-brain barrier of the guinea pig
    • Zlokovic BV, Skundric DS, Segal MB, Lipovac MN, Mackic JB, et al. (1990) A saturable mechanism for transport of immunoglobulin G across the blood-brain barrier of the guinea pig. Exp Neurol 3: 263-270.
    • (1990) Exp Neurol , vol.3 , pp. 263-270
    • Zlokovic, B.V.1    Skundric, D.S.2    Segal, M.B.3    Lipovac, M.N.4    Mackic, J.B.5
  • 49
    • 77953404881 scopus 로고    scopus 로고
    • Immunotherapy and neuroimmunology in Alzheimer's disease: A perspective from the blood-brain barrier
    • Banks WA (2010) Immunotherapy and neuroimmunology in Alzheimer's disease: a perspective from the blood-brain barrier. Immunotherapy 1: 1-3.
    • (2010) Immunotherapy , vol.1 , pp. 1-3
    • Banks, W.A.1
  • 50
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F, Cannon C, Barbour R, Burke RL, Games D, et al. (2000) Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med 8: 916-919.
    • (2000) Nat Med , vol.8 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.L.4    Games, D.5
  • 51
    • 0037000396 scopus 로고    scopus 로고
    • Cyclooxygenase-2-positive macrophages infiltrate the Alzheimer's disease brain and damage the blood-brain barrier
    • Fiala M, Liu QN, Sayre J, Pop V, Brahmandam V, et al. (2002) Cyclooxygenase-2-positive macrophages infiltrate the Alzheimer's disease brain and damage the blood-brain barrier. Eur J Clin Invest 5: 360-371.
    • (2002) Eur J Clin Invest , vol.5 , pp. 360-371
    • Fiala, M.1    Liu, Q.N.2    Sayre, J.3    Pop, V.4    Brahmandam, V.5
  • 52
    • 2342614850 scopus 로고    scopus 로고
    • Neurovascular regulation in the normal brain and in Alzheimer's disease
    • Iadecola C (2004) Neurovascular regulation in the normal brain and in Alzheimer's disease. Nat Rev Neurosci 5: 347-360.
    • (2004) Nat Rev Neurosci , vol.5 , pp. 347-360
    • Iadecola, C.1
  • 53
    • 34250623663 scopus 로고    scopus 로고
    • Blood-brain barrier pathology in Alzheimer's and Parkinson's disease: Implications for drug therapy
    • Desai BS, Monahan AJ, Carvey PM, Hendey B (2007) Blood-brain barrier pathology in Alzheimer's and Parkinson's disease: implications for drug therapy. Cell Transplant 3: 285-299.
    • (2007) Cell Transplant , vol.3 , pp. 285-299
    • Desai, B.S.1    Monahan, A.J.2    Carvey, P.M.3    Hendey, B.4
  • 54
    • 79953836673 scopus 로고    scopus 로고
    • Sink hypothesis and therapeutic strategies for attenuating Abeta levels
    • Zhang Y and Lee DH (2011) Sink hypothesis and therapeutic strategies for attenuating Abeta levels. Neuroscientist 2: 163-173.
    • (2011) Neuroscientist , vol.2 , pp. 163-173
    • Zhang, Y.1    Lee, D.H.2
  • 55
    • 84860531636 scopus 로고    scopus 로고
    • Targeting phospho-Ser422 by active tau immunotherapy in the THYTau22 mouse model: A suitable therapeutic approach
    • Troquier L, Caillierez R, Burnouf S, Fernandez-Gomez FJ, Grosjean ME, et al. (2012) Targeting Phospho-Ser422 by Active Tau Immunotherapy in the THYTau22 Mouse Model: A Suitable Therapeutic Approach. Curr Alzheimer Res 4: 397-405.
    • (2012) Curr Alzheimer Res , vol.4 , pp. 397-405
    • Troquier, L.1    Caillierez, R.2    Burnouf, S.3    Fernandez-Gomez, F.J.4    Grosjean, M.E.5
  • 56
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • Asuni AA, Boutajangout A, Quartermain D, Sigurdsson EM (2007) Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. Journal of Neuroscience 34: 9115-9129.
    • (2007) Journal of Neuroscience , vol.34 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 57
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • Boimel M, Grigoriadis N, Lourbopoulos A, Haber E, Abramsky O, et al. (2010) Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp Neurol 2: 472-485.
    • (2010) Exp Neurol , vol.2 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3    Haber, E.4    Abramsky, O.5
  • 58
    • 78650065372 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model
    • Boutajangout A, Quartermain D, Sigurdsson EM (2010) Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model. Journal of Neuroscience 49: 16559-16566.
    • (2010) Journal of Neuroscience , vol.49 , pp. 16559-16566
    • Boutajangout, A.1    Quartermain, D.2    Sigurdsson, E.M.3
  • 59
    • 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
    • Boutajangout A, Ingadottir J, Davies P, and Sigurdsson EM (2011) Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain. J Neurochem 4: 658-667.
    • (2011) J Neurochem , vol.4 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 60
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L Tau transgenic mice
    • Bi M, Ittner A, Ke YD, Gotz J, and Ittner LM (2011) Tau-Targeted Immunization Impedes Progression of Neurofibrillary Histopathology in Aged P301L Tau Transgenic Mice. PLoS One 12: e26860.
    • (2011) PLoS One , vol.12 , pp. e26860
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Gotz, J.4    Ittner, L.M.5
  • 61
    • 80053202160 scopus 로고    scopus 로고
    • 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, et al. (2011) Passive immunization with anti-Tau antibodies in two transgenic models: reduction of Tau pathology and delay of disease progression. J Biol Chem 39: 34457-34467.
    • (2011) J Biol Chem , vol.39 , pp. 34457-34467
    • Chai, X.1    Wu, S.2    Murray, T.K.3    Kinley, R.4    Cella, C.V.5
  • 62
    • 84876908676 scopus 로고    scopus 로고
    • Tau Passive Immunotherapy in Mutant P301L Mice: Antibody Affinity versus Specificity
    • d'Abramo C, Acker CM, Jimenez HT, Davies P (2013) Tau Passive Immunotherapy in Mutant P301L Mice: Antibody Affinity versus Specificity. PLoS One 4: e62402.
    • (2013) PLoS One , vol.4 , pp. e62402
    • D'Abramo, C.1    Acker, C.M.2    Jimenez, H.T.3    Davies, P.4
  • 63
    • 20444413356 scopus 로고    scopus 로고
    • Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease
    • Masliah E, Rockenstein E, Adame A, Alford M, Crews L, et al. (2005) Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease. Neuron 6: 857-868.
    • (2005) Neuron , vol.6 , pp. 857-868
    • Masliah, E.1    Rockenstein, E.2    Adame, A.3    Alford, M.4    Crews, L.5
  • 64
    • 33847787621 scopus 로고    scopus 로고
    • Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis
    • Urushitani M, Ezzi SA, and Julien JP (2007) Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 7: 2495-2500.
    • (2007) Proc Natl Acad Sci U S A , vol.7 , pp. 2495-2500
    • Urushitani, M.1    Ezzi, S.A.2    Julien, J.P.3
  • 66
    • 34147125835 scopus 로고    scopus 로고
    • Accumulation of pathological tau species and memory loss in a conditional model of tauopathy
    • Berger Z, Roder H, Hanna A, Carlson A, Rangachari V, et al. (2007) Accumulation of pathological tau species and memory loss in a conditional model of tauopathy. Journal of Neuroscience 14: 3650-3662.
    • (2007) Journal of Neuroscience , vol.14 , pp. 3650-3662
    • Berger, Z.1    Roder, H.2    Hanna, A.3    Carlson, A.4    Rangachari, V.5
  • 67
    • 79959571777 scopus 로고    scopus 로고
    • Characterization of prefibrillar tau oligomers in vitro and in Alzheimers disease
    • Patterson KR, Remmers C, Fu Y, Brooker S, Kanaan NM, et al. (2011) Characterization of prefibrillar tau oligomers in vitro and in Alzheimers disease. J Biol Chem.
    • (2011) J Biol Chem
    • Patterson, K.R.1    Remmers, C.2    Fu, Y.3    Brooker, S.4    Kanaan, N.M.5
  • 69
    • 80052940324 scopus 로고    scopus 로고
    • In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice
    • Yamada K, Cirrito JR, Stewart FR, Jiang H, Finn MB, et al. (2011) In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice. Journal of Neuroscience 37: 13110-13117.
    • (2011) Journal of Neuroscience , vol.37 , pp. 13110-13117
    • Yamada, K.1    Cirrito, J.R.2    Stewart, F.R.3    Jiang, H.4    Finn, M.B.5
  • 71
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, and Diamond MI (2009) Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 19: 12845-12852.
    • (2009) J Biol Chem , vol.19 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 72
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R (2010) Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 4: 301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.4 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.