메뉴 건너뛰기




Volumn 10, Issue 8, 2010, Pages 992-1005

Serine-409 phosphorylation and oxidative damage define aggregation of human protein tau in yeast

Author keywords

Aggregation; FTDP 17; Oxidative stress; Phosphorylation; Tau; Yeast

Indexed keywords

CYCLIN DEPENDENT KINASE 5; GLYCOGEN SYNTHASE KINASE 3BETA; SERINE; SERINE 409; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 78349245542     PISSN: 15671356     EISSN: 15671364     Source Type: Journal    
DOI: 10.1111/j.1567-1364.2010.00662.x     Document Type: Article
Times cited : (38)

References (76)
  • 1
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • Alonso Adel C, Li B, Grundke-Iqbal I & Iqbal K (2006) Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. P Natl Acad Sci USA 103: 8864-8869.
    • (2006) P Natl Acad Sci USA , vol.103 , pp. 8864-8869
    • Alonso Adel, C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 2
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack JC, Schneider A, Mandelkow EM & Hyman BT (2002) Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol 103: 26-35.
    • (2002) Acta Neuropathol , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 3
    • 0028216212 scopus 로고
    • Regulation of microtubule dynamics by microtubule-associated protein expression and phosphorylation during neuronal development
    • Avila J, Dominguez J & Diaz-Nido J (1994) Regulation of microtubule dynamics by microtubule-associated protein expression and phosphorylation during neuronal development. Int J Dev Biol 38: 13-25.
    • (1994) Int J Dev Biol , vol.38 , pp. 13-25
    • Avila, J.1    Dominguez, J.2    Diaz-Nido, J.3
  • 4
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn S & Mandelkow E (2002) Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry 41: 14885-14896.
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 5
    • 33744952341 scopus 로고    scopus 로고
    • FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells
    • Bunker JM, Kamath K, Wilson L, Jordan MA & Feinstein SC (2006) FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells. J Biol Chem 281: 11856-11863.
    • (2006) J Biol Chem , vol.281 , pp. 11856-11863
    • Bunker, J.M.1    Kamath, K.2    Wilson, L.3    Jordan, M.A.4    Feinstein, S.C.5
  • 7
    • 54349085644 scopus 로고    scopus 로고
    • Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps
    • Chang E, Kim S, Yin H, Nagaraja HN & Kuret J (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
    • Connell JW, Gibb GM, Betts JC et al. (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.
    • (2001) FEBS Lett , vol.493 , pp. 40-44
    • Connell, J.W.1    Gibb, G.M.2    Betts, J.C.3
  • 9
    • 0037088687 scopus 로고    scopus 로고
    • Functional characterization of FTDP-17 tau gene mutations through their effects on Xenopus oocyte maturation
    • Delobel P, Flament S, Hamdane M et al. (2002) Functional characterization of FTDP-17 tau gene mutations through their effects on Xenopus oocyte maturation. J Biol Chem 277: 9199-9205.
    • (2002) J Biol Chem , vol.277 , pp. 9199-9205
    • Delobel, P.1    Flament, S.2    Hamdane, M.3
  • 10
    • 0036841609 scopus 로고    scopus 로고
    • Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau
    • DeTure M, Ko LW, Easson C & Yen SH (2002) Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau. Am J Pathol 161: 1711-1722.
    • (2002) Am J Pathol , vol.161 , pp. 1711-1722
    • DeTure, M.1    Ko, L.W.2    Easson, C.3    Yen, S.H.4
  • 11
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey CA, Kamal A, Lundgren K et al. (2007) The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest 117: 648-658.
    • (2007) J Clin Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1    Kamal, A.2    Lundgren, K.3
  • 12
    • 4644360412 scopus 로고    scopus 로고
    • MARKing tau for tangles and toxicity
    • Drewes G (2004) MARKing tau for tangles and toxicity. Trends Biochem Sci 29: 548-555.
    • (2004) Trends Biochem Sci , vol.29 , pp. 548-555
    • Drewes, G.1
  • 13
    • 0035659377 scopus 로고    scopus 로고
    • Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies
    • Ferrer I, Blanco R, Carmona M & Puig B (2001) Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies. J Neural Transm 108: 1397-1415.
    • (2001) J Neural Transm , vol.108 , pp. 1397-1415
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4
  • 14
    • 33745819942 scopus 로고    scopus 로고
    • The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease
    • Galas MC, Dourlen P, Begard S, Ando K, Blum D, Hamdane M & Buee L (2006) The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease. J Biol Chem 281: 19296-19304.
    • (2006) J Biol Chem , vol.281 , pp. 19296-19304
    • Galas, M.C.1    Dourlen, P.2    Begard, S.3    Ando, K.4    Blum, D.5    Hamdane, M.6    Buee, L.7
  • 16
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St Jean A, Woods RA & Schiestl RH (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20: 1425.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 19
    • 0344011447 scopus 로고    scopus 로고
    • Decreased cyclin-dependent kinase 5 (cdk5) activity is accompanied by redistribution of cdk5 and cytoskeletal proteins and increased cytoskeletal protein phosphorylation in p35 null mice
    • Hallows JL, Chen K, DePinho RA & Vincent I (2003) Decreased cyclin-dependent kinase 5 (cdk5) activity is accompanied by redistribution of cdk5 and cytoskeletal proteins and increased cytoskeletal protein phosphorylation in p35 null mice. J Neurosci 23: 10633-10644.
    • (2003) J Neurosci , vol.23 , pp. 10633-10644
    • Hallows, J.L.1    Chen, K.2    DePinho, R.A.3    Vincent, I.4
  • 20
    • 67649388412 scopus 로고    scopus 로고
    • Familial FTDP-17 missense mutations inhibit microtubule assembly-promoting activity of tau by increasing phosphorylation at Ser202 in vitro
    • Han D, Qureshi HY, Lu Y & Paudel HK (2009) Familial FTDP-17 missense mutations inhibit microtubule assembly-promoting activity of tau by increasing phosphorylation at Ser202 in vitro. J Biol Chem 284: 13422-13433.
    • (2009) J Biol Chem , vol.284 , pp. 13422-13433
    • Han, D.1    Qureshi, H.Y.2    Lu, Y.3    Paudel, H.K.4
  • 24
    • 57649129018 scopus 로고    scopus 로고
    • Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation
    • Jeganathan S, Hascher A, Chinnathambi S, Biernat J, Mandelkow EM & Mandelkow E (2008) Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation. J Biol Chem 283: 32066-32076.
    • (2008) J Biol Chem , vol.283 , pp. 32066-32076
    • Jeganathan, S.1    Hascher, A.2    Chinnathambi, S.3    Biernat, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 25
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha GA, Bowser R, Kazam IG & Davies P (1997) Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J Neurosci Res 48: 128-132.
    • (1997) J Neurosci Res , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 28
    • 0037413708 scopus 로고    scopus 로고
    • Repeat motifs of tau bind to the insides of microtubules in the absence of taxol
    • Kar S, Fan J, Smith MJ, Goedert M & Amos LA (2003) Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J 22: 70-77.
    • (2003) EMBO J , vol.22 , pp. 70-77
    • Kar, S.1    Fan, J.2    Smith, M.J.3    Goedert, M.4    Amos, L.A.5
  • 29
    • 0029817689 scopus 로고    scopus 로고
    • Sequential changes of tau-site-specific phosphorylation during development of paired helical filaments
    • Kimura T, Ono T, Takamatsu J et al. (1996) Sequential changes of tau-site-specific phosphorylation during development of paired helical filaments. Dementia 7: 177-181.
    • (1996) Dementia , vol.7 , pp. 177-181
    • Kimura, T.1    Ono, T.2    Takamatsu, J.3
  • 31
    • 0035100306 scopus 로고    scopus 로고
    • Aged mother cells of Saccharomyces cerevisiae show markers of oxidative stress and apoptosis
    • Laun P, Pichova A, Madeo F et al. (2001) Aged mother cells of Saccharomyces cerevisiae show markers of oxidative stress and apoptosis. Mol Microbiol 39: 1166-1173.
    • (2001) Mol Microbiol , vol.39 , pp. 1166-1173
    • Laun, P.1    Pichova, A.2    Madeo, F.3
  • 32
    • 33644870413 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism
    • Li T & Paudel HK (2006) Glycogen synthase kinase 3beta phosphorylates Alzheimer's disease-specific Ser396 of microtubule-associated protein tau by a sequential mechanism. Biochemistry 45: 3125-3133.
    • (2006) Biochemistry , vol.45 , pp. 3125-3133
    • Li, T.1    Paudel, H.K.2
  • 33
    • 0035964883 scopus 로고    scopus 로고
    • Hydrogen peroxide induces transient dephosphorylation of tau protein in cultured rat oligodendrocytes
    • LoPresti P & Konat GW (2001) Hydrogen peroxide induces transient dephosphorylation of tau protein in cultured rat oligodendrocytes. Neurosci Lett 311: 142-144.
    • (2001) Neurosci Lett , vol.311 , pp. 142-144
    • LoPresti, P.1    Konat, G.W.2
  • 34
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu KP, Hanes SD & Hunter T (1996) A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380: 544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 35
    • 0041355331 scopus 로고    scopus 로고
    • Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies
    • Makrides V, Shen TE, Bhatia R, Smith BL, Thimm J, Lal R & Feinstein SC (2003) Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies. J Biol Chem 278: 33298-33304.
    • (2003) J Biol Chem , vol.278 , pp. 33298-33304
    • Makrides, V.1    Shen, T.E.2    Bhatia, R.3    Smith, B.L.4    Thimm, J.5    Lal, R.6    Feinstein, S.C.7
  • 36
    • 34648843067 scopus 로고    scopus 로고
    • Mitochondrial cascade hypothesis of Alzheimer's disease
    • &, Antioxid Redox Sign
    • Mancuso M, Coppede F, Murri L & Siciliano G (2007) Mitochondrial cascade hypothesis of Alzheimer's disease: myth or reality? Antioxid Redox Sign 9: 1631-1646.
    • (2007) myth or reality? , vol.9 , pp. 1631-1646
    • Mancuso, M.1    Coppede, F.2    Murri, L.3    Siciliano, G.4
  • 38
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow EM, Stamer K, Vogel R, Thies E & 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
  • 39
    • 75949083202 scopus 로고    scopus 로고
    • Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates
    • Martinez A, Portero-Otin M, Pamplona R & Ferrer I (2009) Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates. Brain Pathol 20: 281-297.
    • (2009) Brain Pathol , vol.20 , pp. 281-297
    • Martinez, A.1    Portero-Otin, M.2    Pamplona, R.3    Ferrer, I.4
  • 40
    • 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, Yamazaki T & Ihara Y (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.
    • (1999) Am J Pathol , vol.154 , pp. 1649-1656
    • Matsumura, N.1    Yamazaki, T.2    Ihara, Y.3
  • 41
    • 38849150935 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress causes hyperphosphorylation of tau
    • Melov S, Adlard PA, Morten K et al. (2007) Mitochondrial oxidative stress causes hyperphosphorylation of tau. PLoS One 2: e536.
    • (2007) PLoS One , vol.2
    • Melov, S.1    Adlard, P.A.2    Morten, K.3
  • 42
    • 42049116923 scopus 로고    scopus 로고
    • Alzheimer disease and the role of free radicals in the pathogenesis of the disease
    • Moreira PI, Santos MS, Oliveira CR et al. (2008) Alzheimer disease and the role of free radicals in the pathogenesis of the disease. CNS Neurol Disord Drug Targets 7: 3-10.
    • (2008) CNS Neurol Disord Drug Targets , vol.7 , pp. 3-10
    • Moreira, P.I.1    Santos, M.S.2    Oliveira, C.R.3
  • 43
    • 0342368837 scopus 로고    scopus 로고
    • The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules
    • Perez M, Lim F, Arrasate M & Avila J (2000) The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules. J Neurochem 74: 2583-2589.
    • (2000) J Neurochem , vol.74 , pp. 2583-2589
    • Perez, M.1    Lim, F.2    Arrasate, M.3    Avila, J.4
  • 44
    • 18744374615 scopus 로고    scopus 로고
    • Is oxidative damage the fundamental pathogenic mechanism of Alzheimer's and other neurodegenerative diseases?
    • Perry G, Nunomura A, Hirai K et al. (2002) Is oxidative damage the fundamental pathogenic mechanism of Alzheimer's and other neurodegenerative diseases? Free Radical Bio Med 33: 1475-1479.
    • (2002) Free Radical Bio Med , vol.33 , pp. 1475-1479
    • Perry, G.1    Nunomura, A.2    Hirai, K.3
  • 45
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner F, Angelo M & Giese KP (2006) The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J Biol Chem 281: 25457-25465.
    • (2006) J Biol Chem , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 46
    • 33845757628 scopus 로고    scopus 로고
    • Phosphorylation inhibits turnover of the tau protein by the proteasome
    • Biochem J
    • Poppek D, Keck S, Ermak G et al. (2006) Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem J 400: 511-520.
    • (2006) influence of RCAN1 and oxidative stress , vol.400 , pp. 511-520
    • Poppek, D.1    Keck, S.2    Ermak, G.3
  • 47
    • 5044235577 scopus 로고    scopus 로고
    • The role of tau (MAPT) in frontotemporal dementia and related tauopathies
    • Rademakers R, Cruts M & Van Broeckhoven C (2004) The role of tau (MAPT) in frontotemporal dementia and related tauopathies. Hum Mutat 24: 277-295.
    • (2004) Hum Mutat , vol.24 , pp. 277-295
    • Rademakers, R.1    Cruts, M.2    Van Broeckhoven, C.3
  • 51
    • 24744462506 scopus 로고    scopus 로고
    • Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39
    • Sakaue F, Saito T, Sato Y, Asada A, Ishiguro K, Hasegawa M & Hisanaga S (2005) Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39. J Biol Chem 280: 31522-31529.
    • (2005) J Biol Chem , vol.280 , pp. 31522-31529
    • Sakaue, F.1    Saito, T.2    Sato, Y.3    Asada, A.4    Ishiguro, K.5    Hasegawa, M.6    Hisanaga, S.7
  • 52
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K, Lewis J, Spires T et al. (2005) Tau suppression in a neurodegenerative mouse model improves memory function. Science 309: 476-481.
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3
  • 53
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • Schweers O, Mandelkow EM, Biernat J & Mandelkow E (1995) Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. P Natl Acad Sci USA 92: 8463-8467.
    • (1995) P Natl Acad Sci USA , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 54
    • 43449128899 scopus 로고    scopus 로고
    • Biochemistry of Tau in Alzheimer's disease and related neurological disorders
    • Sergeant N, Bretteville A, Hamdane M et al. (2008) Biochemistry of Tau in Alzheimer's disease and related neurological disorders. Expert Rev Proteomic 5: 207-224.
    • (2008) Expert Rev Proteomic , vol.5 , pp. 207-224
    • Sergeant, N.1    Bretteville, A.2    Hamdane, M.3
  • 55
    • 0031738468 scopus 로고    scopus 로고
    • Tau pathology in two Dutch families with mutations in the microtubule-binding region of tau
    • Spillantini MG, Crowther RA, Kamphorst W, Heutink P & Van Swieten JC (1998) Tau pathology in two Dutch families with mutations in the microtubule-binding region of tau. Am J Pathol 153: 1359-1363.
    • (1998) Am J Pathol , vol.153 , pp. 1359-1363
    • Spillantini, M.G.1    Crowther, R.A.2    Kamphorst, W.3    Heutink, P.4    Van Swieten, J.C.5
  • 56
    • 0034081234 scopus 로고    scopus 로고
    • Tau gene mutations in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17)
    • Spillantini MG, Van Swieten JC & Goedert M (2000) Tau gene mutations in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Neurogenetics 2: 193-205.
    • (2000) Neurogenetics , vol.2 , pp. 193-205
    • Spillantini, M.G.1    Van Swieten, J.C.2    Goedert, M.3
  • 58
    • 72249109630 scopus 로고    scopus 로고
    • Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells
    • Su B, Wang X, Lee HG, Tabaton M, Perry G, Smith MA & Zhu X (2010) Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells. Neurosci Lett 468: 267-271.
    • (2010) Neurosci Lett , vol.468 , pp. 267-271
    • Su, B.1    Wang, X.2    Lee, H.G.3    Tabaton, M.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 59
    • 0033836580 scopus 로고    scopus 로고
    • In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of tau induced by 4-hydroxy-2-nonenal modification
    • Takeda A, Smith MA, Avila J et al. (2000) In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of tau induced by 4-hydroxy-2-nonenal modification. J Neurochem 75: 1234-1241.
    • (2000) J Neurochem , vol.75 , pp. 1234-1241
    • Takeda, A.1    Smith, M.A.2    Avila, J.3
  • 60
    • 0037414754 scopus 로고    scopus 로고
    • Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in vivo
    • Tan YS, Morcos PA & Cannon JF (2003) Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in vivo. J Biol Chem 278: 147-153.
    • (2003) J Biol Chem , vol.278 , pp. 147-153
    • Tan, Y.S.1    Morcos, P.A.2    Cannon, J.F.3
  • 61
    • 0025232840 scopus 로고
    • S. cerevisiae genes IRA1 and IRA2 encode proteins that may be functionally equivalent to mammalian ras GTPase activating protein
    • Tanaka K, Nakafuku M, Satoh T et al. (1990) S. cerevisiae genes IRA1 and IRA2 encode proteins that may be functionally equivalent to mammalian ras GTPase activating protein. Cell 60: 803-807.
    • (1990) Cell , vol.60 , pp. 803-807
    • Tanaka, K.1    Nakafuku, M.2    Satoh, T.3
  • 62
    • 33646236562 scopus 로고    scopus 로고
    • c-jun N-terminal kinase hyperphosphorylates R406W tau at the PHF-1 site during mitosis
    • Tatebayashi Y, Planel E, Chui DH et al. (2006) c-jun N-terminal kinase hyperphosphorylates R406W tau at the PHF-1 site during mitosis. FASEB J 20: 762-764.
    • (2006) FASEB J , vol.20 , pp. 762-764
    • Tatebayashi, Y.1    Planel, E.2    Chui, D.H.3
  • 64
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets
    • &, P Natl Acad Sci USA
    • Towbin H, Staehelin T & Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. P Natl Acad Sci USA 76: 4350-4354.
    • (1979) procedure and some applications , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 65
    • 77049126656 scopus 로고    scopus 로고
    • Tau phosphorylated at tyrosine 394 is found in Alzheimer's disease tangles and can be a product of the Abl-related kinase, Arg
    • Tremblay MA, Acker CM & Davies P (2009) Tau phosphorylated at tyrosine 394 is found in Alzheimer's disease tangles and can be a product of the Abl-related kinase, Arg. J Alzheimers Dis 19: 721-733.
    • (2009) J Alzheimers Dis , vol.19 , pp. 721-733
    • Tremblay, M.A.1    Acker, C.M.2    Davies, P.3
  • 66
    • 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 et al. (2005) Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast. Biochemistry 44: 11466-11475.
    • (2005) Biochemistry , vol.44 , pp. 11466-11475
    • Vandebroek, T.1    Vanhelmont, T.2    Terwel, D.3
  • 67
    • 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 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 281: 25388-25397.
    • (2006) J Biol Chem , vol.281 , pp. 25388-25397
    • Vandebroek, T.1    Terwel, D.2    Vanhelmont, T.3
  • 68
    • 0026784158 scopus 로고
    • A single-stranded DNA binding protein required for mitochondrial DNA replication in S. cerevisiae is homologous to E. coli SSB
    • Van Dyck E, Foury F, Stillman B & Brill SJ (1992) A single-stranded DNA binding protein required for mitochondrial DNA replication in S. cerevisiae is homologous to E. coli SSB. EMBO J 11: 3421-3430.
    • (1992) EMBO J , vol.11 , pp. 3421-3430
    • Van Dyck, E.1    Foury, F.2    Stillman, B.3    Brill, S.J.4
  • 69
    • 0039604509 scopus 로고
    • A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen
    • Van Loon AP, Pesold-Hurt B & Schatz G (1986) A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen. P Natl Acad Sci USA 83: 3820-3824.
    • (1986) P Natl Acad Sci USA , vol.83 , pp. 3820-3824
    • Van Loon, A.P.1    Pesold-Hurt, B.2    Schatz, G.3
  • 70
    • 0032880430 scopus 로고    scopus 로고
    • Phenotypic variation in hereditary frontotemporal dementia with tau mutations
    • Van Swieten JC, Stevens M, Rosso SM et al. (1999) Phenotypic variation in hereditary frontotemporal dementia with tau mutations. Ann Neurol 46: 617-626.
    • (1999) Ann Neurol , vol.46 , pp. 617-626
    • Van Swieten, J.C.1    Stevens, M.2    Rosso, S.M.3
  • 72
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach A, Brachat A, Pohlmann R & Philippsen P (1994) New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10: 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 74
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler EA, Shoemaker DD, Astromoff A et al. (1999) Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285: 901-906.
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1    Shoemaker, D.D.2    Astromoff, A.3
  • 76
    • 2442642836 scopus 로고    scopus 로고
    • Retarded axonal transport of R406W mutant tau in transgenic mice with a neurodegenerative tauopathy
    • Zhang B, Higuchi M, Yoshiyama Y et al. (2004) Retarded axonal transport of R406W mutant tau in transgenic mice with a neurodegenerative tauopathy. J Neurosci 24: 4657-4667.
    • (2004) J Neurosci , vol.24 , pp. 4657-4667
    • Zhang, B.1    Higuchi, M.2    Yoshiyama, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.