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Volumn 4 AUG, Issue , 2013, Pages

Hyperphosphorylation-induced tau oligomers

Author keywords

Abnormal hyperphosphorylation of tau; Alternate splicing of tau; Alzheimer disease; Alzheimer neurofibrillary degeneration; Microtubule associated protein tau; O GlcNAcylation of tau; Protein phosphatase 2A; Tauopathies

Indexed keywords

AMYLOID BETA PROTEIN; N ACETYLGLUCOSAMINE; PHOSPHOPROTEIN PHOSPHATASE 2A; TAU PROTEIN; TUBULIN;

EID: 84883502350     PISSN: None     EISSN: 16642295     Source Type: Journal    
DOI: 10.3389/fneur.2013.00112     Document Type: Article
Times cited : (80)

References (110)
  • 1
    • 84862833600 scopus 로고    scopus 로고
    • Tau in Alzheimer disease and related tauopathies
    • doi:10.2174/156720510793611592
    • Iqbal K, Liu F, Gong CX, Grundke-Iqbal I. Tau in Alzheimer disease and related tauopathies. Curr Alzheimer Res (2010) 7:656-64. doi:10.2174/156720510793611592
    • (2010) Curr Alzheimer Res , vol.7 , pp. 656-664
    • Iqbal, K.1    Liu, F.2    Gong, C.X.3    Grundke-Iqbal, I.4
  • 2
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • doi:10.1016/0896-6273(89)90210-9
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron (1989) 3:519-26. doi:10.1016/0896-6273(89)90210-9
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 3
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • doi:10.1083/jcb.115.3.717
    • Butner KA, Kirschner MW. Tau protein binds to microtubules through a flexible array of distributed weak sites. J Cell Biol (1991) 115:717-30. doi:10.1083/jcb.115.3.717
    • (1991) J Cell Biol , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 4
    • 0026694783 scopus 로고
    • Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: a radioimmuno-slot-blot assay for nanograms of the protein
    • doi:10.1111/j.1471-4159.1992.tb09432.x
    • Khatoon S, Grundke-Iqbal I, Iqbal K. Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: a radioimmuno-slot-blot assay for nanograms of the protein. J Neurochem (1992) 59:750-3. doi:10.1111/j.1471-4159.1992.tb09432.x
    • (1992) J Neurochem , vol.59 , pp. 750-753
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 5
    • 0034730759 scopus 로고    scopus 로고
    • Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation
    • doi:10.1074/jbc.M002590200
    • Ackmann M, Wiech H, Mandelkow E. Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation. J Biol Chem (2000) 275:30335-43. doi:10.1074/jbc.M002590200
    • (2000) J Biol Chem , vol.275 , pp. 30335-30343
    • Ackmann, M.1    Wiech, H.2    Mandelkow, E.3
  • 6
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • doi:10.1073/pnas.83.13.4913
    • Grundke-Iqbal I, Iqbal K, Tung YC, Quinlan M, Wisniewski HM, Binder LI. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci U S A (1986) 83:4913-7. doi:10.1073/pnas.83.13.4913
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3    Quinlan, M.4    Wisniewski, H.M.5    Binder, L.I.6
  • 7
    • 0022550260 scopus 로고
    • Defective brain microtubule assembly in Alzheimer's disease
    • doi:10.1016/S0140-6736(86)92134-3
    • Iqbal K, Grundke-Iqbal I, Zaidi T, Merz PA, Wen GY, Shaikh SS, et al. Defective brain microtubule assembly in Alzheimer's disease. Lancet (1986) 2:421-6. doi:10.1016/S0140-6736(86)92134-3
    • (1986) Lancet , vol.2 , pp. 421-426
    • Iqbal, K.1    Grundke-Iqbal, I.2    Zaidi, T.3    Merz, P.A.4    Wen, G.Y.5    Shaikh, S.S.6
  • 9
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • doi:10.1073/pnas.91.12.5562
    • Alonso AD, Zaidi T, Grundke-Iqbal I, Iqbal K. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci U S A (1994) 91:5562-6. doi:10.1073/pnas.91.12.5562
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5562-5566
    • Alonso, A.D.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 10
    • 33947691643 scopus 로고    scopus 로고
    • Granular tau oligomers as intermediates of tau filaments
    • doi:10.1021/bi061359o
    • Maeda S, Sahara N, Saito Y, Murayama M, Yoshiike Y, Kim H, et al. Granular tau oligomers as intermediates of tau filaments. Biochemistry (2007) 46:3856-61. doi:10.1021/bi061359o
    • (2007) Biochemistry , vol.46 , pp. 3856-3861
    • Maeda, S.1    Sahara, N.2    Saito, Y.3    Murayama, M.4    Yoshiike, Y.5    Kim, H.6
  • 11
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease
    • doi:10.1016/0006-8993(89)91396-6
    • Bancher C, Brunner C, Lassmann H, Budka H, Jellinger K, Wiche G, et al. Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res (1989) 477:90-9. doi:10.1016/0006-8993(89)91396-6
    • (1989) Brain Res , vol.477 , pp. 90-99
    • Bancher, C.1    Brunner, C.2    Lassmann, H.3    Budka, H.4    Jellinger, K.5    Wiche, G.6
  • 12
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • doi:10.1038/nm0796-783
    • Alonso AD, Grundke-Iqbal I, Iqbal K. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med (1996) 2:783-7. doi:10.1038/nm0796-783
    • (1996) Nat Med , vol.2 , pp. 783-787
    • Alonso, A.D.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 13
    • 0031012497 scopus 로고    scopus 로고
    • Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau
    • doi:10.1073/pnas.94.1.298
    • Alonso AD, Grundke-Iqbal I, Barra HS, Iqbal K. Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. Proc Natl Acad Sci U S A (1997) 94:298-303. doi:10.1073/pnas.94.1.298
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 298-303
    • Alonso, A.D.1    Grundke-Iqbal, I.2    Barra, H.S.3    Iqbal, K.4
  • 14
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • doi:10.1073/pnas.121119298
    • Alonso A, Zaidi T, Novak M, Grundke-Iqbal I, Iqbal K. Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc Natl Acad Sci U S A (2001) 98:6923-8. doi:10.1073/pnas.121119298
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 15
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • doi:10.1073/pnas.0603214103
    • Alonso AD, Li B, Grundke-Iqbal I, Iqbal K. Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc Natl Acad Sci U S A (2006) 23:8864-9. doi:10.1073/pnas.0603214103
    • (2006) Proc Natl Acad Sci U S A , vol.23 , pp. 8864-8869
    • Alonso, A.D.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 16
    • 34247574162 scopus 로고    scopus 로고
    • Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau
    • doi:10.1007/s00401-007-0207-8
    • Li B, Chohan MO, Grundke-Iqbal I, Iqbal K. Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau. Acta Neuropathol (2007) 113:501-11. doi:10.1007/s00401-007-0207-8
    • (2007) Acta Neuropathol , vol.113 , pp. 501-511
    • Li, B.1    Chohan, M.O.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 17
    • 0028852644 scopus 로고
    • Guanosine triphosphate binding to beta-subunit of tubulin in Alzheimer's disease brain: role of microtubule-associated protein tau
    • doi:10.1046/j.1471-4159.1995.64020777.x
    • Khatoon S, Grundke-Iqbal I, Iqbal K. Guanosine triphosphate binding to beta-subunit of tubulin in Alzheimer's disease brain: role of microtubule-associated protein tau. J Neurochem (1995) 64:777-87. doi:10.1046/j.1471-4159.1995.64020777.x
    • (1995) J Neurochem , vol.64 , pp. 777-787
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 18
    • 0029995590 scopus 로고    scopus 로고
    • Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1
    • doi:10.1016/0169-328X(95)00316-K
    • Wang JZ, Grundke-Iqbal I, Iqbal K. Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1. Brain Res Mol Brain Res (1996) 38:200-8. doi:10.1016/0169-328X(95)00316-K
    • (1996) Brain Res Mol Brain Res , vol.38 , pp. 200-208
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 19
    • 0028902487 scopus 로고
    • Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
    • doi:10.1074/jbc.270.9.4854
    • Wang JZ, Gong CX, Zaidi T, Grundke-Iqbal I, Iqbal K. Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B. J Biol Chem (1995) 270:4854-60. doi:10.1074/jbc.270.9.4854
    • (1995) J Biol Chem , vol.270 , pp. 4854-4860
    • Wang, J.Z.1    Gong, C.X.2    Zaidi, T.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 20
    • 33846212717 scopus 로고    scopus 로고
    • Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
    • doi:10.1111/j.1460-9568.2006.05226.x
    • Wang JZ, Grundke-Iqbal I, Iqbal K. Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration. Eur J Neurosci (2007) 25:59-68. doi:10.1111/j.1460-9568.2006.05226.x
    • (2007) Eur J Neurosci , vol.25 , pp. 59-68
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 21
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • doi:10.1073/pnas.95.11.6448
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A (1998) 95:6448-53. doi:10.1073/pnas.95.11.6448
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 22
    • 0031789527 scopus 로고    scopus 로고
    • Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation
    • doi:10.1515/bchm.1998.379.11.1307
    • Post K, Pitschke M, Schafer O, Wille H, Appel TR, Kirsch D, et al. Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation. Biol Chem (1998) 379:1307-17. doi:10.1515/bchm.1998.379.11.1307
    • (1998) Biol Chem , vol.379 , pp. 1307-1317
    • Post, K.1    Pitschke, M.2    Schafer, O.3    Wille, H.4    Appel, T.R.5    Kirsch, D.6
  • 23
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • doi:10.1021/bi991967m
    • Swietnicki W, Morillas M, Chen SG, Gambetti P, Surewicz WK. Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry (2000) 39:424-31. doi:10.1021/bi991967m
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 24
    • 0030026759 scopus 로고    scopus 로고
    • Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity
    • Riesner D, Kellings K, Post K, Wille H, Serban H, Groth D, et al. Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity. J Virol (1996) 70:1714-22.
    • (1996) J Virol , vol.70 , pp. 1714-1722
    • Riesner, D.1    Kellings, K.2    Post, K.3    Wille, H.4    Serban, H.5    Groth, D.6
  • 25
    • 84877144645 scopus 로고    scopus 로고
    • The cellular prion protein traps Alzheimer's Abeta in an oligomeric form and disassembles amyloid fibers
    • doi:10.1096/fj.12-222588
    • Younan ND, Sarell CJ, Davies P, Brown DR, Viles JH. The cellular prion protein traps Alzheimer's Abeta in an oligomeric form and disassembles amyloid fibers. FASEB J (2013) 27:1847-58. doi:10.1096/fj.12-222588
    • (2013) FASEB J , vol.27 , pp. 1847-1858
    • Younan, N.D.1    Sarell, C.J.2    Davies, P.3    Brown, D.R.4    Viles, J.H.5
  • 26
    • 77949769388 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • doi:10.1016/j.bbagen.2009.07.018
    • Butkinaree C, Park K, Hart GW. O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim Biophys Acta (2010) 1800:96-106. doi:10.1016/j.bbagen.2009.07.018
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 27
    • 67650072530 scopus 로고    scopus 로고
    • Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease
    • doi:10.1093/brain/awp099
    • Liu F, Shi J, Tanimukai H, Gu J, Gu J, Grundke-Iqbal I, et al. Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease. Brain (2009) 132:1820-32. doi:10.1093/brain/awp099
    • (2009) Brain , vol.132 , pp. 1820-1832
    • Liu, F.1    Shi, J.2    Tanimukai, H.3    Gu, J.4    Gu, J.5    Grundke-Iqbal, I.6
  • 28
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways
    • doi:10.1242/jcs.053678
    • Zeidan Q, Hart GW. The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J Cell Sci (2010) 123:13-22. doi:10.1242/jcs.053678
    • (2010) J Cell Sci , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 29
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • doi:10.1016/j.bbagen.2004.03.016
    • Zachara NE, Hart GW. O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim Biophys Acta (2004) 1673:13-28. doi:10.1016/j.bbagen.2004.03.016
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 30
    • 10544236116 scopus 로고    scopus 로고
    • The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine
    • doi:10.1074/jbc.271.46.28741
    • Arnold CS, Johnson GV, Cole RN, Dong DL, Lee M, Hart GW. The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine. J Biol Chem (1996) 271:28741-4. doi:10.1074/jbc.271.46.28741
    • (1996) J Biol Chem , vol.271 , pp. 28741-28744
    • Arnold, C.S.1    Johnson, G.V.2    Cole, R.N.3    Dong, D.L.4    Lee, M.5    Hart, G.W.6
  • 31
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease
    • doi:10.1073/pnas.0400348101
    • Liu F, Iqbal K, Grundke-Iqbal I, Hart GW, Gong CX. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc Natl Acad Sci U S A (2004) 101:10804-9. doi:10.1073/pnas.0400348101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 32
    • 76649126396 scopus 로고    scopus 로고
    • Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry
    • doi:10.1074/mcp.M900268-MCP200
    • Wang Z, Udeshi ND, O'Malley M, Shabanowitz J, Hunt DF, Hart GW. Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry. Mol Cell Proteomics (2010) 9:153-60. doi:10.1074/mcp.M900268-MCP200
    • (2010) Mol Cell Proteomics , vol.9 , pp. 153-160
    • Wang, Z.1    Udeshi, N.D.2    O'Malley, M.3    Shabanowitz, J.4    Hunt, D.F.5    Hart, G.W.6
  • 33
    • 79954538679 scopus 로고    scopus 로고
    • Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation
    • doi:10.1039/c0mb00337a
    • Smet-Nocca C, Broncel M, Wieruszeski JM, Tokarski C, Hanoulle X, Leroy A, et al. Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation. Mol Biosyst (2011) 7:1420-9. doi:10.1039/c0mb00337a
    • (2011) Mol Biosyst , vol.7 , pp. 1420-1429
    • Smet-Nocca, C.1    Broncel, M.2    Wieruszeski, J.M.3    Tokarski, C.4    Hanoulle, X.5    Leroy, A.6
  • 34
    • 79954437580 scopus 로고    scopus 로고
    • Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody
    • doi:10.1007/s00726-010-0705-1
    • Yuzwa SA, Yadav AK, Skorobogatko Y, Clark T, Vosseller K, Vocadlo DJ. Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody. Amino Acids (2011) 40:857-68. doi:10.1007/s00726-010-0705-1
    • (2011) Amino Acids , vol.40 , pp. 857-868
    • Yuzwa, S.A.1    Yadav, A.K.2    Skorobogatko, Y.3    Clark, T.4    Vosseller, K.5    Vocadlo, D.J.6
  • 35
    • 33646008860 scopus 로고    scopus 로고
    • Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting
    • doi:10.1111/j.1460-9568.2006.04735.x
    • Li X, Lu F, Wang JZ, Gong CX. Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting. Eur J Neurosci (2006) 23:2078-86. doi:10.1111/j.1460-9568.2006.04735.x
    • (2006) Eur J Neurosci , vol.23 , pp. 2078-2086
    • Li, X.1    Lu, F.2    Wang, J.Z.3    Gong, C.X.4
  • 36
    • 50949099668 scopus 로고    scopus 로고
    • O-GlcNAcylation modulates the self-aggregation ability of the fourth microtubule-binding repeat of tau
    • doi:10.1016/j.bbrc.2008.07.101
    • Yu CH, Si T, Wu WH, Hu J, Du JT, Zhao YF, et al. O-GlcNAcylation modulates the self-aggregation ability of the fourth microtubule-binding repeat of tau. Biochem Biophys Res Commun (2008) 375:59-62. doi:10.1016/j.bbrc.2008.07.101
    • (2008) Biochem Biophys Res Commun , vol.375 , pp. 59-62
    • Yu, C.H.1    Si, T.2    Wu, W.H.3    Hu, J.4    Du, J.T.5    Zhao, Y.F.6
  • 37
    • 84858664547 scopus 로고    scopus 로고
    • Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation
    • doi:10.1038/nchembio.797
    • Yuzwa SA, Shan X, Macauley MS, Clark T, Skorobogatko Y, Vosseller K, et al. Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation. Nat Chem Biol (2012) 8:393-9. doi:10.1038/nchembio.797
    • (2012) Nat Chem Biol , vol.8 , pp. 393-399
    • Yuzwa, S.A.1    Shan, X.2    Macauley, M.S.3    Clark, T.4    Skorobogatko, Y.5    Vosseller, K.6
  • 38
    • 84867903851 scopus 로고    scopus 로고
    • O-GlcNAc cycling modulates neurodegeneration
    • doi:10.1073/pnas.1215395109
    • Gong CX, Liu F, Iqbal K. O-GlcNAc cycling modulates neurodegeneration. Proc Natl Acad Sci U S A (2012) 109:17319-20. doi:10.1073/pnas.1215395109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 17319-17320
    • Gong, C.X.1    Liu, F.2    Iqbal, K.3
  • 39
    • 84867908726 scopus 로고    scopus 로고
    • O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases
    • doi:10.1073/pnas.1205748109
    • Wang P, Lazarus BD, Forsythe ME, Love DC, Krause MW, Hanover JA. O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases. Proc Natl Acad Sci U S A (2012) 109:17669-74. doi:10.1073/pnas.1205748109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 17669-17674
    • Wang, P.1    Lazarus, B.D.2    Forsythe, M.E.3    Love, D.C.4    Krause, M.W.5    Hanover, J.A.6
  • 40
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • doi:10.1111/j.1460-9568.2005.04391.x
    • Liu F, Grundke-Iqbal I, Iqbal K, Gong CX. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur J Neurosci (2005) 22:1942-50. doi:10.1111/j.1460-9568.2005.04391.x
    • (2005) Eur J Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 41
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • doi:10.1111/j.1471-4159.1993.tb03603.x
    • Gong CX, Singh TJ, Grundke-Iqbal I, Iqbal K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J Neurochem (1993) 61:921-7. doi:10.1111/j.1471-4159.1993.tb03603.x
    • (1993) J Neurochem , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 42
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain
    • doi:10.1046/j.1471-4159.1995.65020732.x
    • Gong CX, Shaikh S, Wang JZ, Zaidi T, Grundke-Iqbal I, Iqbal K. Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J Neurochem (1995) 65:732-8. doi:10.1046/j.1471-4159.1995.65020732.x
    • (1995) J Neurochem , vol.65 , pp. 732-738
    • Gong, C.X.1    Shaikh, S.2    Wang, J.Z.3    Zaidi, T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 43
    • 47849120642 scopus 로고    scopus 로고
    • Decrease of protein phosphatase 2A and its association with accumulation and hyperphosphorylation of tau in Down syndrome
    • Liang Z, Liu F, Iqbal K, Grundke-Iqbal I, Wegiel J, Gong CX. Decrease of protein phosphatase 2A and its association with accumulation and hyperphosphorylation of tau in Down syndrome. J Alzheimers Dis (2008) 13:295-302.
    • (2008) J Alzheimers Dis , vol.13 , pp. 295-302
    • Liang, Z.1    Liu, F.2    Iqbal, K.3    Grundke-Iqbal, I.4    Wegiel, J.5    Gong, C.X.6
  • 44
    • 0028931302 scopus 로고
    • Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
    • doi:10.1021/bi00006a020
    • Li M, Guo H, Damuni Z. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry (1995) 34:1988-96. doi:10.1021/bi00006a020
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 45
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • doi:10.1074/jbc.271.19.11059
    • Li M, Makkinje A, Damuni Z. The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J Biol Chem (1996) 271:11059-62. doi:10.1074/jbc.271.19.11059
    • (1996) J Biol Chem , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 46
    • 11844273281 scopus 로고    scopus 로고
    • Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau
    • doi:10.1016/j.febslet.2004.11.097
    • Tsujio I, Zaidi T, Xu J, Kotula L, Grundke-Iqbal I, Iqbal K. Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau. FEBS Lett (2005) 579:363-72. doi:10.1016/j.febslet.2004.11.097
    • (2005) FEBS Lett , vol.579 , pp. 363-372
    • Tsujio, I.1    Zaidi, T.2    Xu, J.3    Kotula, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 47
    • 3042711967 scopus 로고    scopus 로고
    • Inhibitors of protein phosphatase-2A: topography and subcellular localization
    • doi:10.1016/j.molbrainres.2004.04.003
    • Tanimukai H, Grundke-Iqbal I, Iqbal K. Inhibitors of protein phosphatase-2A: topography and subcellular localization. Brain Res Mol Brain Res (2004) 126:146-56. doi:10.1016/j.molbrainres.2004.04.003
    • (2004) Brain Res Mol Brain Res , vol.126 , pp. 146-156
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 48
    • 0028369492 scopus 로고
    • Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII
    • doi:10.1515/bchm3.1994.375.2.113
    • Vaesen M, Barnikol-Watanabe S, Gotz H, Awni LA, Cole T, Zimmermann B, et al. Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII. Biol Chem Hoppe Seyler (1994) 375:113-26. doi:10.1515/bchm3.1994.375.2.113
    • (1994) Biol Chem Hoppe Seyler , vol.375 , pp. 113-126
    • Vaesen, M.1    Barnikol-Watanabe, S.2    Gotz, H.3    Awni, L.A.4    Cole, T.5    Zimmermann, B.6
  • 49
    • 0026693436 scopus 로고
    • Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene
    • von Lindern M, Van Baal S, Wiegant J, Raap A, Hagemeijer A, Grosveld G. Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene. Mol Cell Biol (1992) 12:3346-55.
    • (1992) Mol Cell Biol , vol.12 , pp. 3346-3355
    • von Lindern, M.1    Van Baal, S.2    Wiegant, J.3    Raap, A.4    Hagemeijer, A.5    Grosveld, G.6
  • 50
    • 0027938950 scopus 로고
    • A nuclear factor containing the leucine-rich repeats expressed in murine cerebellar neurons
    • doi:10.1073/pnas.91.21.9670
    • Matsuoka K, Taoka M, Satozawa N, Nakayama H, Ichimura T, Takahashi N, et al. A nuclear factor containing the leucine-rich repeats expressed in murine cerebellar neurons. Proc Natl Acad Sci U S A (1994) 91:9670-4. doi:10.1073/pnas.91.21.9670
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9670-9674
    • Matsuoka, K.1    Taoka, M.2    Satozawa, N.3    Nakayama, H.4    Ichimura, T.5    Takahashi, N.6
  • 51
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • doi:10.1016/S0002-9440(10)62486-8
    • Tanimukai H, Grundke-Iqbal I, Iqbal K. Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am J Pathol (2005) 166:1761-71. doi:10.1016/S0002-9440(10)62486-8
    • (2005) Am J Pathol , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 52
    • 80052259754 scopus 로고    scopus 로고
    • Mechanism of inhibition of PP2A activity and abnormal hyperphosphorylation of tau by I(2)(PP2A)/SET
    • doi:10.1016/j.febslet.2011.07.020
    • Arnaud L, Chen S, Liu F, Li B, Khatoon S, Grundke-Iqbal I, et al. Mechanism of inhibition of PP2A activity and abnormal hyperphosphorylation of tau by I(2)(PP2A)/SET. FEBS Lett (2011) 585:2653-9. doi:10.1016/j.febslet.2011.07.020
    • (2011) FEBS Lett , vol.585 , pp. 2653-2659
    • Arnaud, L.1    Chen, S.2    Liu, F.3    Li, B.4    Khatoon, S.5    Grundke-Iqbal, I.6
  • 53
    • 78649859760 scopus 로고    scopus 로고
    • The carboxy-terminal fragment of inhibitor-2 of protein phosphatase-2A induces Alzheimer disease pathology and cognitive impairment
    • doi:10.1096/fj.10-158477
    • Wang X, Blanchard J, Kohlbrenner E, Clement N, Linden RM, Radu A, et al. The carboxy-terminal fragment of inhibitor-2 of protein phosphatase-2A induces Alzheimer disease pathology and cognitive impairment. FASEB J (2010) 24:4420-32. doi:10.1096/fj.10-158477
    • (2010) FASEB J , vol.24 , pp. 4420-4432
    • Wang, X.1    Blanchard, J.2    Kohlbrenner, E.3    Clement, N.4    Linden, R.M.5    Radu, A.6
  • 54
    • 84857032101 scopus 로고    scopus 로고
    • An experimental rat model of sporadic Alzheimer's disease and rescue of cognitive impairment with a neurotrophic peptide
    • doi:10.1007/s00401-011-0908-x
    • Bolognin S, Blanchard J, Wang X, Basurto-Islas G, Tung YC, Kohlbrenner E, et al. An experimental rat model of sporadic Alzheimer's disease and rescue of cognitive impairment with a neurotrophic peptide. Acta Neuropathol (2012) 123:133-51. doi:10.1007/s00401-011-0908-x
    • (2012) Acta Neuropathol , vol.123 , pp. 133-151
    • Bolognin, S.1    Blanchard, J.2    Wang, X.3    Basurto-Islas, G.4    Tung, Y.C.5    Kohlbrenner, E.6
  • 55
    • 23944469853 scopus 로고    scopus 로고
    • Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast
    • doi:10.1021/bi0506775
    • Vandebroek T, Vanhelmont T, Terwel D, Borghgraef P, Lemaire K, Snauwaert J, et al. Identification and isolation of a hyperphosphorylated, conformationally changed intermediate of human protein tau expressed in yeast. Biochemistry (2005) 44:11466-75. doi:10.1021/bi0506775
    • (2005) Biochemistry , vol.44 , pp. 11466-11475
    • Vandebroek, T.1    Vanhelmont, T.2    Terwel, D.3    Borghgraef, P.4    Lemaire, K.5    Snauwaert, J.6
  • 56
    • 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
    • doi:10.1074/jbc.M602792200
    • Vandebroek T, Terwel D, Vanhelmont T, Gysemans M, Van Haesendonck C, Engelborghs Y, et al. 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 (2006) 281:25388-97. doi:10.1074/jbc.M602792200
    • (2006) J Biol Chem , vol.281 , pp. 25388-25397
    • Vandebroek, T.1    Terwel, D.2    Vanhelmont, T.3    Gysemans, M.4    Van Haesendonck, C.5    Engelborghs, Y.6
  • 57
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles
    • doi:10.1126/science.1062382
    • Wittmann CW, Wszolek MF, Shulman JM, Salvaterra PM, Lewis J, Hutton M, et al. Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science (2001) 293:711-4. doi:10.1126/science.1062382
    • (2001) Science , vol.293 , pp. 711-714
    • Wittmann, C.W.1    Wszolek, M.F.2    Shulman, J.M.3    Salvaterra, P.M.4    Lewis, J.5    Hutton, M.6
  • 58
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • doi:10.1126/science.1113694
    • Santacruz K, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M, et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science (2005) 309:476-81. doi:10.1126/science.1113694
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3    Paulson, J.4    Kotilinek, L.5    Ingelsson, M.6
  • 59
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • doi:10.1074/jbc.M608485200
    • Oddo S, Vasilevko V, Caccamo A, Kitazawa M, Cribbs DH, Laferla FM. Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J Biol Chem (2006) 281:39413-23. doi:10.1074/jbc.M608485200
    • (2006) J Biol Chem , vol.281 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    Laferla, F.M.6
  • 60
    • 0017345388 scopus 로고
    • Decrease in levels and rates of synthesis of tubulin and actin in developing rat brain
    • doi:10.1016/0006-8993(77)90155-X
    • Schmitt H, Gozes I, Littauer UZ. Decrease in levels and rates of synthesis of tubulin and actin in developing rat brain. Brain Res (1977) 121:327-42. doi:10.1016/0006-8993(77)90155-X
    • (1977) Brain Res , vol.121 , pp. 327-342
    • Schmitt, H.1    Gozes, I.2    Littauer, U.Z.3
  • 61
    • 0042125603 scopus 로고    scopus 로고
    • Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals
    • Arendt T, Stieler J, Strijkstra AM, Hut RA, Rudiger J, Van Der Zee EA, et al. Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals. J Neurosci (2003) 23:6972-81.
    • (2003) J Neurosci , vol.23 , pp. 6972-6981
    • Arendt, T.1    Stieler, J.2    Strijkstra, A.M.3    Hut, R.A.4    Rudiger, J.5    Van Der Zee, E.A.6
  • 62
    • 33947536100 scopus 로고    scopus 로고
    • Anesthesia leads to tau hyperphosphorylation through inhibition of phosphatase activity by hypothermia
    • doi:10.1523/JNEUROSCI.4854-06.2007
    • Planel E, Richter KE, Nolan CE, Finley JE, Liu L, Wen Y, et al. Anesthesia leads to tau hyperphosphorylation through inhibition of phosphatase activity by hypothermia. J Neurosci (2007) 27:3090-7. doi:10.1523/JNEUROSCI.4854-06.2007
    • (2007) J Neurosci , vol.27 , pp. 3090-3097
    • Planel, E.1    Richter, K.E.2    Nolan, C.E.3    Finley, J.E.4    Liu, L.5    Wen, Y.6
  • 63
    • 44649165063 scopus 로고    scopus 로고
    • Physiological regulation of tau phosphorylation during hibernation
    • doi:10.1111/j.1471-4159.2008.05294.x
    • Su B, Wang X, Drew KL, Perry G, Smith MA, Zhu X. Physiological regulation of tau phosphorylation during hibernation. J Neurochem (2008) 105:2098-108. doi:10.1111/j.1471-4159.2008.05294.x
    • (2008) J Neurochem , vol.105 , pp. 2098-2108
    • Su, B.1    Wang, X.2    Drew, K.L.3    Perry, G.4    Smith, M.A.5    Zhu, X.6
  • 65
    • 0028095224 scopus 로고
    • Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains
    • doi:10.1016/0014-5793(94)00829-9
    • Khatoon S, Grundke-Iqbal I, Iqbal K. Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains. FEBS Lett (1994) 351:80-4. doi:10.1016/0014-5793(94)00829-9
    • (1994) FEBS Lett , vol.351 , pp. 80-84
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 66
    • 17844387375 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus induced by the overexpression of wild-type and mutant human tau forms in neurons
    • doi:10.1016/S0002-9440(10)62366-8
    • Liazoghli D, Perreault S, Micheva KD, Desjardins M, Leclerc N. Fragmentation of the Golgi apparatus induced by the overexpression of wild-type and mutant human tau forms in neurons. Am J Pathol (2005) 166:1499-514. doi:10.1016/S0002-9440(10)62366-8
    • (2005) Am J Pathol , vol.166 , pp. 1499-1514
    • Liazoghli, D.1    Perreault, S.2    Micheva, K.D.3    Desjardins, M.4    Leclerc, N.5
  • 67
    • 33750553861 scopus 로고    scopus 로고
    • Tau interacts with Golgi membranes and mediates their association with microtubules
    • doi:10.1002/cm.20157
    • Farah CA, Perreault S, Liazoghli D, Desjardins M, Anton A, Lauzon M, et al. Tau interacts with Golgi membranes and mediates their association with microtubules. Cell Motil Cytoskeleton (2006) 63:710-24. doi:10.1002/cm.20157
    • (2006) Cell Motil Cytoskeleton , vol.63 , pp. 710-724
    • Farah, C.A.1    Perreault, S.2    Liazoghli, D.3    Desjardins, M.4    Anton, A.5    Lauzon, M.6
  • 68
    • 0023187131 scopus 로고
    • Alzheimer's disease: paired helical filaments and cytomembranes
    • doi:10.1111/j.1365-2990.1987.tb00174.x
    • Gray EG, Paula-Barbosa M, Roher A. Alzheimer's disease: paired helical filaments and cytomembranes. Neuropathol Appl Neurobiol (1987) 13:91-110. doi:10.1111/j.1365-2990.1987.tb00174.x
    • (1987) Neuropathol Appl Neurobiol , vol.13 , pp. 91-110
    • Gray, E.G.1    Paula-Barbosa, M.2    Roher, A.3
  • 69
    • 0029815467 scopus 로고    scopus 로고
    • Glycosylation of microtubule-associated protein tau: an abnormal posttranslational modification in Alzheimer's disease
    • doi:10.1038/nm0896-871
    • Wang JZ, Grundke-Iqbal I, Iqbal K. Glycosylation of microtubule-associated protein tau: an abnormal posttranslational modification in Alzheimer's disease. Nat Med (1996) 2:871-5. doi:10.1038/nm0896-871
    • (1996) Nat Med , vol.2 , pp. 871-875
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 70
    • 3442884830 scopus 로고    scopus 로고
    • Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau
    • doi:10.1023/B:NEUR.0000021904.61387.95
    • Lin WL, Lewis J, Yen SH, Hutton M, Dickson DW. Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau. J Neurocytol (2003) 32:1091-105. doi:10.1023/B:NEUR.0000021904.61387.95
    • (2003) J Neurocytol , vol.32 , pp. 1091-1105
    • Lin, W.L.1    Lewis, J.2    Yen, S.H.3    Hutton, M.4    Dickson, D.W.5
  • 71
    • 70149098692 scopus 로고    scopus 로고
    • Increased association between rough endoplasmic reticulum membranes and mitochondria in transgenic mice that express P301L tau
    • doi:10.1097/NEN.0b013e3181a1fc49
    • Perreault S, Bousquet O, Lauzon M, Paiement J, Leclerc N. Increased association between rough endoplasmic reticulum membranes and mitochondria in transgenic mice that express P301L tau. J Neuropathol Exp Neurol (2009) 68:503-14. doi:10.1097/NEN.0b013e3181a1fc49
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 503-514
    • Perreault, S.1    Bousquet, O.2    Lauzon, M.3    Paiement, J.4    Leclerc, N.5
  • 72
    • 0029974421 scopus 로고    scopus 로고
    • Immunohistochemical examination of phosphorylated tau in granulovacuolar degeneration granules
    • doi:10.1111/j.1440-1819.1996.tb01678.x
    • Ikegami K, Kimura T, Katsuragi S, Ono T, Yamamoto H, Miyamoto E, et al. Immunohistochemical examination of phosphorylated tau in granulovacuolar degeneration granules. Psychiatry Clin Neurosci (1996) 50:137-40. doi:10.1111/j.1440-1819.1996.tb01678.x
    • (1996) Psychiatry Clin Neurosci , vol.50 , pp. 137-140
    • Ikegami, K.1    Kimura, T.2    Katsuragi, S.3    Ono, T.4    Yamamoto, H.5    Miyamoto, E.6
  • 73
    • 0032870947 scopus 로고    scopus 로고
    • A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease
    • doi:10.1016/S0002-9440(10)65219-4
    • Ghoshal N, Smiley JF, Demaggio AJ, Hoekstra MF, Cochran EJ, Binder LI, et al. A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease. Am J Pathol (1999) 155:1163-72. doi:10.1016/S0002-9440(10)65219-4
    • (1999) Am J Pathol , vol.155 , pp. 1163-1172
    • Ghoshal, N.1    Smiley, J.F.2    Demaggio, A.J.3    Hoekstra, M.F.4    Cochran, E.J.5    Binder, L.I.6
  • 74
    • 33751256001 scopus 로고    scopus 로고
    • Relation of hippocampal phospho-SAPK/JNK granules in Alzheimer's disease and tauopathies to granulovacuolar degeneration bodies
    • doi:10.1007/s00401-006-0159-4
    • Lagalwar S, Berry RW, Binder LI. Relation of hippocampal phospho-SAPK/JNK granules in Alzheimer's disease and tauopathies to granulovacuolar degeneration bodies. Acta Neuropathol (2007) 113:63-73. doi:10.1007/s00401-006-0159-4
    • (2007) Acta Neuropathol , vol.113 , pp. 63-73
    • Lagalwar, S.1    Berry, R.W.2    Binder, L.I.3
  • 75
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • doi:10.1016/j.neuron.2007.01.010
    • Yoshiyama Y, Higuchi M, Zhang B, Huang SM, Iwata N, Saido TC, et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron (2007) 53:337-51. doi:10.1016/j.neuron.2007.01.010
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1    Higuchi, M.2    Zhang, B.3    Huang, S.M.4    Iwata, N.5    Saido, T.C.6
  • 76
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities
    • doi:10.1038/nrd2755
    • Kim I, Xu W, Reed JC. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat Rev Drug Discov (2008) 7:1013-30. doi:10.1038/nrd2755
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 77
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak M, Kabat J, Wischik CM. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J (1993) 12:365-70.
    • (1993) EMBO J , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 78
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • doi:10.1073/pnas.1630428100
    • Gamblin TC, Chen F, Zambrano A, Abraha A, Lagalwar S, Guillozet AL, et al. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc Natl Acad Sci U S A (2003) 100:10032-7. doi:10.1073/pnas.1630428100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1    Chen, F.2    Zambrano, A.3    Abraha, A.4    Lagalwar, S.5    Guillozet, A.L.6
  • 79
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • doi:10.1016/S0002-9440(10)63317-2
    • Guo H, Albrecht S, Bourdeau M, Petzke T, Bergeron C, Leblanc AC. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am J Pathol (2004) 165:523-31. doi:10.1016/S0002-9440(10)63317-2
    • (2004) Am J Pathol , vol.165 , pp. 523-531
    • Guo, H.1    Albrecht, S.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    Leblanc, A.C.6
  • 81
    • 3242749074 scopus 로고    scopus 로고
    • Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
    • doi:10.1172/JCI20640
    • Rissman RA, Poon WW, Blurton-Jones M, Oddo S, Torp R, Vitek MP, et al. Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J Clin Invest (2004) 114:121-30. doi:10.1172/JCI20640
    • (2004) J Clin Invest , vol.114 , pp. 121-130
    • Rissman, R.A.1    Poon, W.W.2    Blurton-Jones, M.3    Oddo, S.4    Torp, R.5    Vitek, M.P.6
  • 82
    • 43249129441 scopus 로고    scopus 로고
    • Accumulation of aspartic acid421- and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease
    • doi:10.1097/NEN.0b013e31817275c7
    • Basurto-Islas G, Luna-Munoz J, Guillozet-Bongaarts AL, Binder LI, Mena R, Garcia-Sierra F. Accumulation of aspartic acid421- and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease. J Neuropathol Exp Neurol (2008) 67:470-83. doi:10.1097/NEN.0b013e31817275c7
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 470-483
    • Basurto-Islas, G.1    Luna-Munoz, J.2    Guillozet-Bongaarts, A.L.3    Binder, L.I.4    Mena, R.5    Garcia-Sierra, F.6
  • 83
    • 20044381844 scopus 로고    scopus 로고
    • Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease
    • doi:10.1016/j.neurobiolaging.2004.09.019
    • Guillozet-Bongaarts AL, Garcia-Sierra F, Reynolds MR, Horowitz PM, Fu Y, Wang T, et al. Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease. Neurobiol Aging (2005) 26:1015-22. doi:10.1016/j.neurobiolaging.2004.09.019
    • (2005) Neurobiol Aging , vol.26 , pp. 1015-1022
    • Guillozet-Bongaarts, A.L.1    Garcia-Sierra, F.2    Reynolds, M.R.3    Horowitz, P.M.4    Fu, Y.5    Wang, T.6
  • 85
    • 11144228296 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 beta induces caspase-cleaved tau aggregation in situ
    • doi:10.1074/jbc.M403364200
    • Cho JH, Johnson GV. Glycogen synthase kinase 3 beta induces caspase-cleaved tau aggregation in situ. J Biol Chem (2004) 279:54716-23. doi:10.1074/jbc.M403364200
    • (2004) J Biol Chem , vol.279 , pp. 54716-54723
    • Cho, J.H.1    Johnson, G.V.2
  • 86
    • 33745152289 scopus 로고    scopus 로고
    • Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo
    • doi:10.1016/j.febslet.2006.05.029
    • Zilka N, Filipcik P, Koson P, Fialova L, Skrabana R, Zilkova M, et al. Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett (2006) 580:3582-8. doi:10.1016/j.febslet.2006.05.029
    • (2006) FEBS Lett , vol.580 , pp. 3582-3588
    • Zilka, N.1    Filipcik, P.2    Koson, P.3    Fialova, L.4    Skrabana, R.5    Zilkova, M.6
  • 87
    • 38549129613 scopus 로고    scopus 로고
    • The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy
    • doi:10.1523/JNEUROSCI.2824-07.2008
    • Mocanu MM, Nissen A, Eckermann K, Khlistunova I, Biernat J, Drexler D, et al. The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. J Neurosci (2008) 28:737-48. doi:10.1523/JNEUROSCI.2824-07.2008
    • (2008) J Neurosci , vol.28 , pp. 737-748
    • Mocanu, M.M.1    Nissen, A.2    Eckermann, K.3    Khlistunova, I.4    Biernat, J.5    Drexler, D.6
  • 88
    • 67349087945 scopus 로고    scopus 로고
    • Misfolded tau protein and disease modifying pathways in transgenic rodent models of human tauopathies
    • doi:10.1007/s00401-009-0499-y
    • Zilka N, Korenova M, Novak M. Misfolded tau protein and disease modifying pathways in transgenic rodent models of human tauopathies. Acta Neuropathol (2009) 118:71-86. doi:10.1007/s00401-009-0499-y
    • (2009) Acta Neuropathol , vol.118 , pp. 71-86
    • Zilka, N.1    Korenova, M.2    Novak, M.3
  • 89
    • 38749144389 scopus 로고    scopus 로고
    • Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy
    • doi:10.2353/ajpath.2008.070627
    • Delobel P, Lavenir I, Fraser G, Ingram E, Holzer M, Ghetti B, et al. Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy. Am J Pathol (2008) 172:123-31. doi:10.2353/ajpath.2008.070627
    • (2008) Am J Pathol , vol.172 , pp. 123-131
    • Delobel, P.1    Lavenir, I.2    Fraser, G.3    Ingram, E.4    Holzer, M.5    Ghetti, B.6
  • 91
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17
    • doi:10.1038/31508
    • Hutton M, Lendon CL, Rizzu P, Baker M, Froelich S, Houlden H, et al. Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17. Nature (1998) 393:702-5. doi:10.1038/31508
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3    Baker, M.4    Froelich, S.5    Houlden, H.6
  • 92
    • 14444284106 scopus 로고    scopus 로고
    • Tau is a candidate gene for chromosome 17 frontotemporal dementia
    • doi:10.1002/ana.410430617
    • Poorkaj P, Bird TD, Wijsman E, Nemens E, Garruto RM, Anderson L, et al. Tau is a candidate gene for chromosome 17 frontotemporal dementia. Ann Neurol (1998) 43:815-25. doi:10.1002/ana.410430617
    • (1998) Ann Neurol , vol.43 , pp. 815-825
    • Poorkaj, P.1    Bird, T.D.2    Wijsman, E.3    Nemens, E.4    Garruto, R.M.5    Anderson, L.6
  • 93
    • 0032560487 scopus 로고    scopus 로고
    • Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
    • doi:10.1073/pnas.95.13.7737
    • Spillantini MG, Murrell JR, Goedert M, Farlow MR, Klug A, Ghetti B. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc Natl Acad Sci U S A (1998) 95:7737-41. doi:10.1073/pnas.95.13.7737
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7737-7741
    • Spillantini, M.G.1    Murrell, J.R.2    Goedert, M.3    Farlow, M.R.4    Klug, A.5    Ghetti, B.6
  • 94
    • 4844219627 scopus 로고    scopus 로고
    • Promotion of hyperphosphorylation by frontotemporal dementia tau mutations
    • doi:10.1074/jbc.M405131200
    • Alonso AD, Mederlyova A, Novak M, Grundke-Iqbal I, Iqbal K. Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J Biol Chem (2004) 279:34873-81. doi:10.1074/jbc.M405131200
    • (2004) J Biol Chem , vol.279 , pp. 34873-34881
    • Alonso, A.D.1    Mederlyova, A.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 96
    • 27644460461 scopus 로고    scopus 로고
    • Hereditary Pick's disease with the G272V tau mutation shows predominant three-repeat tau pathology
    • doi:10.1093/brain/awh591
    • Bronner IF, Ter Meulen BC, Azmani A, Severijnen LA, Willemsen R, Kamphorst W, et al. Hereditary Pick's disease with the G272V tau mutation shows predominant three-repeat tau pathology. Brain (2005) 128:2645-53. doi:10.1093/brain/awh591
    • (2005) Brain , vol.128 , pp. 2645-2653
    • Bronner, I.F.1    Ter Meulen, B.C.2    Azmani, A.3    Severijnen, L.A.4    Willemsen, R.5    Kamphorst, W.6
  • 98
    • 0242317909 scopus 로고    scopus 로고
    • Mutations in the tau gene that cause an increase in three repeat tau and frontotemporal dementia
    • doi:10.1093/brain/awg090
    • Stanford PM, Shepherd CE, Halliday GM, Brooks WS, Schofield PW, Brodaty H, et al. Mutations in the tau gene that cause an increase in three repeat tau and frontotemporal dementia. Brain (2003) 126:814-26. doi:10.1093/brain/awg090
    • (2003) Brain , vol.126 , pp. 814-826
    • Stanford, P.M.1    Shepherd, C.E.2    Halliday, G.M.3    Brooks, W.S.4    Schofield, P.W.5    Brodaty, H.6
  • 99
    • 33748996792 scopus 로고    scopus 로고
    • Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies
    • doi:10.1111/j.1440-1789.2006.00743.x
    • Yoshida M. Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies. Neuropathology (2006) 26:457-70. doi:10.1111/j.1440-1789.2006.00743.x
    • (2006) Neuropathology , vol.26 , pp. 457-470
    • Yoshida, M.1
  • 100
    • 48249148310 scopus 로고    scopus 로고
    • Tau exon 10 alternative splicing and tauopathies
    • doi:10.1186/1750-1326-3-8
    • Liu F, Gong CX. Tau exon 10 alternative splicing and tauopathies. Mol Neurodegener (2008) 3:8. doi:10.1186/1750-1326-3-8
    • (2008) Mol Neurodegener , vol.3 , pp. 8
    • Liu, F.1    Gong, C.X.2
  • 101
    • 33845425431 scopus 로고    scopus 로고
    • Regulation of phosphorylation of tau by protein kinases in rat brain
    • doi:10.1007/s11064-006-9205-9
    • Sengupta A, Grundke-Iqbal I, Iqbal K. Regulation of phosphorylation of tau by protein kinases in rat brain. Neurochem Res (2006) 31:1473-80. doi:10.1007/s11064-006-9205-9
    • (2006) Neurochem Res , vol.31 , pp. 1473-1480
    • Sengupta, A.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 102
    • 51349109221 scopus 로고    scopus 로고
    • Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome
    • doi:10.1096/fj.07-104539
    • Liu F, Liang Z, Wegiel J, Hwang YW, Iqbal K, Grundke-Iqbal I, et al. Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome. FASEB J (2008) 22:3224-33. doi:10.1096/fj.07-104539
    • (2008) FASEB J , vol.22 , pp. 3224-3233
    • Liu, F.1    Liang, Z.2    Wegiel, J.3    Hwang, Y.W.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 103
    • 57649134248 scopus 로고    scopus 로고
    • Increased dosage of Dyrk1A alters alternative splicing factor (ASF)-regulated alternative splicing of tau in Down syndrome
    • doi:10.1074/jbc.M802645200
    • Shi J, Zhang T, Zhou C, Chohan MO, Gu X, Wegiel J, et al. Increased dosage of Dyrk1A alters alternative splicing factor (ASF)-regulated alternative splicing of tau in Down syndrome. J Biol Chem (2008) 283:28660-9. doi:10.1074/jbc.M802645200
    • (2008) J Biol Chem , vol.283 , pp. 28660-28669
    • Shi, J.1    Zhang, T.2    Zhou, C.3    Chohan, M.O.4    Gu, X.5    Wegiel, J.6
  • 104
    • 0028897322 scopus 로고
    • Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases
    • doi:10.1016/0014-5793(94)01383-C
    • Singh TJ, Zaidi T, Grundke-Iqbal I, Iqbal K. Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. FEBS Lett (1995) 358:4-8. doi:10.1016/0014-5793(94)01383-C
    • (1995) FEBS Lett , vol.358 , pp. 4-8
    • Singh, T.J.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 105
    • 0030067749 scopus 로고    scopus 로고
    • Non-proline-dependent protein kinases phosphorylate several sites found in tau from Alzheimer disease brain
    • doi:10.1007/BF00226782
    • Singh TJ, Zaidi T, Grundke-Iqbal I, Iqbal K. Non-proline-dependent protein kinases phosphorylate several sites found in tau from Alzheimer disease brain. Mol Cell Biochem (1996) 154:143-51. doi:10.1007/BF00226782
    • (1996) Mol Cell Biochem , vol.154 , pp. 143-151
    • Singh, T.J.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 106
    • 0032530145 scopus 로고    scopus 로고
    • Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules
    • doi:10.1006/abbi.1998.0813
    • Sengupta A, Kabat J, Novak M, Wu Q, Grundke-Iqbal I, Iqbal K. Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. Arch Biochem Biophys (1998) 357:299-309. doi:10.1006/abbi.1998.0813
    • (1998) Arch Biochem Biophys , vol.357 , pp. 299-309
    • Sengupta, A.1    Kabat, J.2    Novak, M.3    Wu, Q.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 107
    • 66249137771 scopus 로고    scopus 로고
    • GSK-3beta phosphorylation of functionally distinct tau isoforms has differential, but mild effects
    • doi:10.1186/1750-1326-4-18
    • Voss K, Gamblin TC. GSK-3beta phosphorylation of functionally distinct tau isoforms has differential, but mild effects. Mol Neurodegener (2009) 4:18. doi:10.1186/1750-1326-4-18
    • (2009) Mol Neurodegener , vol.4 , pp. 18
    • Voss, K.1    Gamblin, T.C.2
  • 108
    • 80155166000 scopus 로고    scopus 로고
    • Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms
    • doi:10.1021/bi2010569
    • Combs B, Voss K, Gamblin TC. Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms. Biochemistry (2011) 50:9446-56. doi:10.1021/bi2010569
    • (2011) Biochemistry , vol.50 , pp. 9446-9456
    • Combs, B.1    Voss, K.2    Gamblin, T.C.3
  • 109
    • 84862027756 scopus 로고    scopus 로고
    • Tau isoform composition influences rate and extent of filament formation
    • doi:10.1074/jbc.M112.364067
    • Zhong Q, Congdon EE, Nagaraja HN, Kuret J. Tau isoform composition influences rate and extent of filament formation. J Biol Chem (2012) 287:20711-9. doi:10.1074/jbc.M112.364067
    • (2012) J Biol Chem , vol.287 , pp. 20711-20719
    • Zhong, Q.1    Congdon, E.E.2    Nagaraja, H.N.3    Kuret, J.4
  • 110
    • 0035851157 scopus 로고    scopus 로고
    • Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein
    • Alonso AD, Zaidi T, Novak M, Barra HS, Grundke-Iqbal I, Iqbal K. Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein. J Biol Chem (2001) 276:37967-73.
    • (2001) J Biol Chem , vol.276 , pp. 37967-37973
    • Alonso, A.D.1    Zaidi, T.2    Novak, M.3    Barra, H.S.4    Grundke-Iqbal, I.5    Iqbal, K.6


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