메뉴 건너뛰기




Volumn 132, Issue 7, 2009, Pages 1820-1832

Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease

Author keywords

glucose metabolism; neurofibrillary degeneration; O GlcNAcylation; protein phosphatase 2A; tau phosphorylation

Indexed keywords

CYTOPLASM PROTEIN; HEXOSAMINE; N ACETYLGLUCOSAMINE; PHOSPHOPROTEIN PHOSPHATASE 2A; SHORT HAIRPIN RNA; TAU PROTEIN;

EID: 67650072530     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awp099     Document Type: Article
Times cited : (339)

References (66)
  • 1
    • 4844219627 scopus 로고    scopus 로고
    • Promotion of hyperphosphorylation by frontotemporal dementia tau mutations
    • 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.
    • (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
  • 2
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer's disease
    • Alonso AD, Zaidi T, Grundke-Iqbal I, Iqbal K. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer's disease. Proc Natl Acad Sci USA 1994; 91: 5562-6.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5562-5566
    • Alonso, A.D.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 3
    • 0035851157 scopus 로고    scopus 로고
    • Interaction of tau isoforms with Alzheimer's disease abnormally hyper-phosphorylated 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 hyper-phosphorylated tau and in vitro phosphorylation into the disease-like protein. J Biol Chem 2001a; 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
  • 4
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso AD, 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 USA 2001b; 98: 6923-8.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6923-6928
    • Alonso, A.D.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 5
    • 10544236116 scopus 로고    scopus 로고
    • The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine
    • 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.
    • (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
  • 6
    • 33846047004 scopus 로고    scopus 로고
    • Pathways by which Abeta facilitates tau pathology
    • Blurton-Jones M, Laferla FM. Pathways by which Abeta facilitates tau pathology. Curr Alzheimer Res 2006; 3: 437-48.
    • (2006) Curr Alzheimer Res , vol.3 , pp. 437-448
    • Blurton-Jones, M.1    Laferla, F.M.2
  • 7
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • discussion 278-84
    • Braak H, Braak E. Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol Aging 1995; 16: 271-8; discussion 278-84.
    • (1995) Neurobiol Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 8
    • 0035845499 scopus 로고    scopus 로고
    • Prediction of cognitive decline in normal elderly subjects with 2-[(18)F]fluoro-2-deoxy-D-glucose/poitron-emission tomography (FDG/PET)
    • de Leon MJ, Convit A, Wolf OT, Tarshish CY, DeSanti S, Rusinek H, et al. Prediction of cognitive decline in normal elderly subjects with 2-[(18)F]fluoro-2-deoxy-D-glucose/poitron-emission tomography (FDG/PET). Proc Natl Acad Sci USA 2001; 98: 10966-71.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10966-10971
    • de Leon, M.J.1    Convit, A.2    Wolf, O.T.3    Tarshish, C.Y.4    DeSanti, S.5    Rusinek, H.6
  • 9
    • 38049121347 scopus 로고    scopus 로고
    • Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer's disease
    • Deng Y, Li B, Liu F, Iqbal K, Grundke-Iqbal I, Brandt R, et al. Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer's disease. FASEB J 2008; 22:138-45.
    • (2008) FASEB J , vol.22 , pp. 138-145
    • Deng, Y.1    Li, B.2    Liu, F.3    Iqbal, K.4    Grundke-Iqbal, I.5    Brandt, R.6
  • 11
    • 0042736668 scopus 로고    scopus 로고
    • Cerebral metabolic changes accompanying conversion of mild cognitive impairment into Alzheimer's disease: A PET follow-up study
    • Drzezga A, Lautenschlager N, Siebner H, Riemenschneider M, Willoch F, Minoshima S, et al. Cerebral metabolic changes accompanying conversion of mild cognitive impairment into Alzheimer's disease: a PET follow-up study. Eur J Nucl Med Mol Imaging 2003; 30: 1104-13.
    • (2003) Eur J Nucl Med Mol Imaging , vol.30 , pp. 1104-1113
    • Drzezga, A.1    Lautenschlager, N.2    Siebner, H.3    Riemenschneider, M.4    Willoch, F.5    Minoshima, S.6
  • 12
    • 0037111833 scopus 로고    scopus 로고
    • Tau-mediated cytotoxicity in a pseudo- hyperphosphorylation model of Alzheimer's disease
    • Fath T, Eidenmuller J, Brandt R. Tau-mediated cytotoxicity in a pseudo- hyperphosphorylation model of Alzheimer's disease. J Neurosci 2002; 22: 9733-41.
    • (2002) J Neurosci , vol.22 , pp. 9733-9741
    • Fath, T.1    Eidenmuller, J.2    Brandt, R.3
  • 13
    • 33746278194 scopus 로고    scopus 로고
    • The selfish brain: Competition for energy resources
    • Fehm HL, Kern W, Peters A. The selfish brain: competition for energy resources. Prog Brain Res 2006; 153: 129-40.
    • (2006) Prog Brain Res , vol.153 , pp. 129-140
    • Fehm, H.L.1    Kern, W.2    Peters, A.3
  • 14
    • 0028885494 scopus 로고
    • Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP- dependent protein kinase
    • Goedert M, Jakes R, Qi Z, Wang JH, Cohen P. Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP- dependent protein kinase. J Neurochem 1995; 65: 2804-7.
    • (1995) J Neurochem , vol.65 , pp. 2804-2807
    • Goedert, M.1    Jakes, R.2    Qi, Z.3    Wang, J.H.4    Cohen, P.5
  • 15
    • 55249086251 scopus 로고    scopus 로고
    • Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer's disease
    • Gong CX, Iqbal K. Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer's disease. Curr Med Chem 2008; 15: 2321-8.
    • (2008) Curr Med Chem , vol.15 , pp. 2321-2328
    • Gong, C.X.1    Iqbal, K.2
  • 16
    • 0034088846 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease
    • Gong CX, Lidsky T, Wegiel J, Zuck L, Grundke-Iqbal I, Iqbal K. Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease. J Biol Chem 2000; 275: 5535-44.
    • (2000) J Biol Chem , vol.275 , pp. 5535-5544
    • Gong, C.X.1    Lidsky, T.2    Wegiel, J.3    Zuck, L.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 17
    • 18544390506 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein in Alzheimer's disease
    • Gong CX, Liu F, Grundke-Iqbal I, Iqbal K. Post-translational modifications of tau protein in Alzheimer's disease. J Neural Transm 2005; 112: 813-38.
    • (2005) J Neural Transm , vol.112 , pp. 813-838
    • Gong, C.X.1    Liu, F.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 18
    • 0029113874 scopus 로고
    • Phosphatase activity toward abnormally phosphorylated tau: Decrease in Alzheimer's disease brain
    • Gong CX, Shaikh S, Wang JZ, Zaidi T, Grundke-Iqbal I, Iqbal K. Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer's disease brain. J Neurochem 1995; 65: 732-8.
    • (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
  • 19
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer's disease brain
    • Gong CX, Singh TJ, Grundke-Iqbal I, Iqbal K. Phosphoprotein phosphatase activities in Alzheimer's disease brain. J Neurochem 1993; 61: 921-7.
    • (1993) J Neurochem , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 21
    • 34548191034 scopus 로고    scopus 로고
    • Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis
    • Hanger DP, Byers HL, Wray S, Leung KY, Saxton MJ, Seereeram A, et al. Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J Biol Chem 2007; 282: 23645-54.
    • (2007) J Biol Chem , vol.282 , pp. 23645-23654
    • Hanger, D.P.1    Byers, H.L.2    Wray, S.3    Leung, K.Y.4    Saxton, M.J.5    Seereeram, A.6
  • 22
    • 0026406816 scopus 로고
    • Abnormalities of energy metabolism in Alzheimer's disease studied with PET
    • Heiss WD, Szelies B, Kessler J, Herholz K. Abnormalities of energy metabolism in Alzheimer's disease studied with PET. Ann N Y Acad Sci 1991; 640: 65-71.
    • (1991) Ann N Y Acad Sci , vol.640 , pp. 65-71
    • Heiss, W.D.1    Szelies, B.2    Kessler, J.3    Herholz, K.4
  • 23
    • 14244253319 scopus 로고    scopus 로고
    • Metabolic/signal transduction hypothesis of Alzheimer's disease and other tauopathies
    • Iqbal K, Grundke-Iqbal I. Metabolic/signal transduction hypothesis of Alzheimer's disease and other tauopathies. Acta Neuropathol 2005; 109: 25-31.
    • (2005) Acta Neuropathol , vol.109 , pp. 25-31
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 25
    • 0342647324 scopus 로고    scopus 로고
    • Regional cerebral glucose metabolism in healthy volunteers determined by fluordeoxyglucose positron emission tomography: Appearance and variance in the transaxial, coronal, and sagittal planes
    • Ivancevic V, Alavi A, Souder E, Mozley PD, Gur RE, Benard F, et al. Regional cerebral glucose metabolism in healthy volunteers determined by fluordeoxyglucose positron emission tomography: appearance and variance in the transaxial, coronal, and sagittal planes. Clin Nucl Med 2000; 25: 596-602.
    • (2000) Clin Nucl Med , vol.25 , pp. 596-602
    • Ivancevic, V.1    Alavi, A.2    Souder, E.3    Mozley, P.D.4    Gur, R.E.5    Benard, F.6
  • 26
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson GR, Wiedau-Pazos M, Sang TK, Wagle N, Brown CA, Massachi S, et al. Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 2002; 34: 509-19.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3    Wagle, N.4    Brown, C.A.5    Massachi, S.6
  • 27
    • 0026694783 scopus 로고
    • Brain levels of microtubule- associated protein tau are elevated in Alzheimer's disease: A radioim- muno-slot-blot assay for nanograms of the protein
    • Khatoon S, Grundke-Iqbal I, Iqbal K. Brain levels of microtubule- associated protein tau are elevated in Alzheimer's disease: a radioim- muno-slot-blot assay for nanograms of the protein. J Neurochem 1992; 59: 750-3.
    • (1992) J Neurochem , vol.59 , pp. 750-753
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 28
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer's disease
    • Kopke E, Tung YC, Shaikh S, Alonso AC, Iqbal K, Grundke-Iqbal I. Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer's disease. J Biol Chem 1993; 268: 24374-84.
    • (1993) J Biol Chem , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 29
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • Kreppel LK, Hart GW. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 1999; 274: 32015-22.
    • (1999) J Biol Chem , vol.274 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 30
    • 0020317216 scopus 로고
    • Effects of human aging on patterns of local cerebral glucose utilization determined by the [18F]fluorodeoxyglucose method
    • Kuhl DE, Metter EJ, Riege WH, Phelps ME. Effects of human aging on patterns of local cerebral glucose utilization determined by the [18F]fluorodeoxyglucose method. J Cereb Blood Flow Metab 1982; 2: 163-71.
    • (1982) J Cereb Blood Flow Metab , vol.2 , pp. 163-171
    • Kuhl, D.E.1    Metter, E.J.2    Riege, W.H.3    Phelps, M.E.4
  • 32
    • 33646008860 scopus 로고    scopus 로고
    • Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting
    • 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.
    • (2006) Eur J Neurosci , vol.23 , pp. 2078-2086
    • Li, X.1    Lu, F.2    Wang, J.Z.3    Gong, C.X.4
  • 33
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • 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.
    • (2005) Eur J Neurosci , vol.22 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 34
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • 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 USA 2004; 101: 10804-9.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 35
    • 38049050725 scopus 로고    scopus 로고
    • Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in Alzheimer's disease
    • Liu Y, Liu F, Iqbal K, Grundke-Iqbal I, Gong CX. Decreased glucose transporters correlate to abnormal hyperphosphorylation of tau in Alzheimer's disease. FEBS Lett 2008b; 582: 359-64.
    • (2008) FEBS Lett , vol.582 , pp. 359-364
    • Liu, Y.1    Liu, F.2    Iqbal, K.3    Grundke-Iqbal, I.4    Gong, C.X.5
  • 36
    • 0037049240 scopus 로고    scopus 로고
    • Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and depho- sphorylation of tau by protein phosphatase 2A and 5
    • Liu F, Zaidi T, Iqbal K, Grundke-Iqbal I, Gong CX. Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and depho- sphorylation of tau by protein phosphatase 2A and 5. Neuroscience 2002; 115: 829-37.
    • (2002) Neuroscience , vol.115 , pp. 829-837
    • Liu, F.1    Zaidi, T.2    Iqbal, K.3    Grundke-Iqbal, I.4    Gong, C.X.5
  • 37
    • 41149086325 scopus 로고    scopus 로고
    • Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibrillary pathology
    • Liu R, Zhou XW, Tanila H, Bjorkdahl C, Wang JZ, Guan ZZ, et al. Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibrillary pathology. J Cell Mol Med 2008a; 12: 241-57.
    • (2008) J Cell Mol Med , vol.12 , pp. 241-257
    • Liu, R.1    Zhou, X.W.2    Tanila, H.3    Bjorkdahl, C.4    Wang, J.Z.5    Guan, Z.Z.6
  • 38
    • 0029067185 scopus 로고
    • Regional cerebral function determined by FDG-PET in healthy volunteers: Normal patterns and changes with age
    • Loessner A, Alavi A, Lewandrowski KU, Mozley D, Souder E, Gur RE. Regional cerebral function determined by FDG-PET in healthy volunteers: normal patterns and changes with age. J Nucl Med 1995; 36: 1141-9.
    • (1995) J Nucl Med , vol.36 , pp. 1141-1149
    • Loessner, A.1    Alavi, A.2    Lewandrowski, K.U.3    Mozley, D.4    Souder, E.5    Gur, R.E.6
  • 40
    • 33644874204 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: Deciphering the ''O-GlcNAc code''
    • Love DC, Hanover JA. The hexosamine signaling pathway: deciphering the ''O-GlcNAc code''. Sci STKE 2005; 2005: re13.
    • (2005) Sci STKE 2005
    • Love, D.C.1    Hanover, J.A.2
  • 41
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas JJ, Hernandez F, Gomez-Ramos P, Moran MA, Hen R, Avila J. Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J 2001; 20: 27-39.
    • (2001) EMBO J , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 42
    • 0024467472 scopus 로고
    • Cortical glutaminase, beta-glucuronidase and glucose utilization in Alzheimer's disease
    • McGeer EG, McGeer PL, Akiyama H, Harrop R. Cortical glutaminase, beta-glucuronidase and glucose utilization in Alzheimer's disease. Can J Neurol Sci 1989; 16: 511-5.
    • (1989) Can J Neurol Sci , vol.16 , pp. 511-515
    • McGeer, E.G.1    McGeer, P.L.2    Akiyama, H.3    Harrop, R.4
  • 43
    • 0025193563 scopus 로고
    • 18Fluorodeoxyglucose positron emission tomography studies in presumed Alzheimer cases, including 13 serial scans
    • McGeer EG, Peppard RP, McGeer PL, Tuokko H, Crockett D, Parks R, et al. 18Fluorodeoxyglucose positron emission tomography studies in presumed Alzheimer cases, including 13 serial scans. Can J Neurol Sci 1990; 17: 1-11.
    • (1990) Can J Neurol Sci , vol.17 , pp. 1-11
    • McGeer, E.G.1    Peppard, R.P.2    McGeer, P.L.3    Tuokko, H.4    Crockett, D.5    Parks, R.6
  • 45
    • 0028008696 scopus 로고
    • Clinical deterioration in probable Alzheimer's disease correlates with progressive metabolic impairment of association areas
    • Mielke R, Herholz K, Grond M, Kessler J, Heiss WD. Clinical deterioration in probable Alzheimer's disease correlates with progressive metabolic impairment of association areas. Dementia 1994; 5: 36-41.
    • (1994) Dementia , vol.5 , pp. 36-41
    • Mielke, R.1    Herholz, K.2    Grond, M.3    Kessler, J.4    Heiss, W.D.5
  • 46
    • 0029040216 scopus 로고
    • A diagnostic approach in Alzheimer's disease using three-dimensional stereotactic surface projections of fluorine-18-FDG PET
    • Minoshima S, Frey KA, Koeppe RA, Foster NL, Kuhl DE. A diagnostic approach in Alzheimer's disease using three-dimensional stereotactic surface projections of fluorine-18-FDG PET. J Nucl Med 1995; 36:1238-48.
    • (1995) J Nucl Med , vol.36 , pp. 1238-1248
    • Minoshima, S.1    Frey, K.A.2    Koeppe, R.A.3    Foster, N.L.4    Kuhl, D.E.5
  • 47
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, et al. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 1991; 41: 479-86.
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6
  • 49
    • 19944406770 scopus 로고    scopus 로고
    • MCI conversion to dementia and the APOE genotype: A prediction study with FDG-PET
    • Mosconi L, Perani D, Sorbi S, Herholz K, Nacmias B, Holthoff V, et al. MCI conversion to dementia and the APOE genotype: a prediction study with FDG-PET. Neurology 2004; 63: 2332-40.
    • (2004) Neurology , vol.63 , pp. 2332-2340
    • Mosconi, L.1    Perani, D.2    Sorbi, S.3    Herholz, K.4    Nacmias, B.5    Holthoff, V.6
  • 50
    • 34548170737 scopus 로고    scopus 로고
    • Quantitation, regional vulnerability, and kinetic modeling of brain glucose metabolism in mild Alzheimer's disease
    • Mosconi L, Tsui WH, Rusinek H, De Santi S, Li Y, Wang GJ, et al. Quantitation, regional vulnerability, and kinetic modeling of brain glucose metabolism in mild Alzheimer's disease. Eur J Nucl Med Mol Imaging 2007; 34: 1467-79.
    • (2007) Eur J Nucl Med Mol Imaging , vol.34 , pp. 1467-1479
    • Mosconi, L.1    Tsui, W.H.2    Rusinek, H.3    De Santi, S.4    Li, Y.5    Wang, G.J.6
  • 51
    • 56249083216 scopus 로고    scopus 로고
    • Neurofibrillary degeneration in Alzheimer's disease: From molecular mechanisms to identification of drug targets
    • Pei JJ, Sjogren M, Winblad B. Neurofibrillary degeneration in Alzheimer's disease: from molecular mechanisms to identification of drug targets. Curr Opin Psychiatry 2008; 21: 555-61.
    • (2008) Curr Opin Psychiatry , vol.21 , pp. 555-561
    • Pei, J.J.1    Sjogren, M.2    Winblad, B.3
  • 55
    • 0027167891 scopus 로고
    • Pattern of cerebral metabolic interactions in a subject with isolated amnesia at risk for Alzheimer's disease: A longitudinal evaluation
    • Pietrini P, Azari NP, Grady CL, Salerno JA, Gonzales-Aviles A, Heston LL, et al. Pattern of cerebral metabolic interactions in a subject with isolated amnesia at risk for Alzheimer's disease: a longitudinal evaluation. Dementia 1993; 4: 94-101.
    • (1993) Dementia , vol.4 , pp. 94-101
    • Pietrini, P.1    Azari, N.P.2    Grady, C.L.3    Salerno, J.A.4    Gonzales-Aviles, A.5    Heston, L.L.6
  • 56
    • 12144289492 scopus 로고    scopus 로고
    • Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: Implications for Alzheimer's disease
    • Planel E, Miyasaka T, Launey T, Chui DH, Tanemura K, Sato S, et al. Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: implications for Alzheimer's disease. J Neurosci 2004; 24: 2401-11.
    • (2004) J Neurosci , vol.24 , pp. 2401-2411
    • Planel, E.1    Miyasaka, T.2    Launey, T.3    Chui, D.H.4    Tanemura, K.5    Sato, S.6
  • 57
    • 0035823496 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse
    • Planel E, Yasutake K, Fujita SC, Ishiguro K. Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse. J Biol Chem 2001; 276: 34298-306.
    • (2001) J Biol Chem , vol.276 , pp. 34298-34306
    • Planel, E.1    Yasutake, K.2    Fujita, S.C.3    Ishiguro, K.4
  • 58
    • 0026303718 scopus 로고
    • Decrease of frontal metabolism demonstrated by positron emission tomography in a population of healthy elderly volunteers
    • Salmon E, Maquet P, Sadzot B, Degueldre C, Lemaire C, Franck G. Decrease of frontal metabolism demonstrated by positron emission tomography in a population of healthy elderly volunteers. Acta Neurol Belg 1991; 91: 288-95.
    • (1991) Acta Neurol Belg , vol.91 , pp. 288-295
    • Salmon, E.1    Maquet, P.2    Sadzot, B.3    Degueldre, C.4    Lemaire, C.5    Franck, G.6
  • 59
    • 0028241915 scopus 로고
    • Decreased concentrations of GLUT1 and GLUT3 glucose transporters in the brains of patients with Alzheimer's disease
    • Simpson IA, Chundu KR, Davies-Hill T, Honer WG, Davies P. Decreased concentrations of GLUT1 and GLUT3 glucose transporters in the brains of patients with Alzheimer's disease. Ann Neurol 1994; 35: 546-51.
    • (1994) Ann Neurol , vol.35 , pp. 546-551
    • Simpson, I.A.1    Chundu, K.R.2    Davies-Hill, T.3    Honer, W.G.4    Davies, P.5
  • 60
    • 0026446225 scopus 로고
    • Topography of cross-sectional and longitudinal glucose metabolic deficits in Alzheimer's disease. Pathophysiologic implications
    • Smith GS, de Leon MJ, George AE, Kluger A, Volkow ND, McRae T, et al. Topography of cross-sectional and longitudinal glucose metabolic deficits in Alzheimer's disease. Pathophysiologic implications. Arch Neurol 1992; 49: 1142-50.
    • (1992) Arch Neurol , vol.49 , pp. 1142-1150
    • Smith, G.S.1    de Leon, M.J.2    George, A.E.3    Kluger, A.4    Volkow, N.D.5    McRae, T.6
  • 61
    • 1842510667 scopus 로고    scopus 로고
    • Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer's disease pathology
    • Sontag E, Luangpirom A, Hladik C, Mudrak I, Ogris E, Speciale S, et al. Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer's disease pathology. J Neuropathol Exp Neurol 2004; 63: 287-301.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 287-301
    • Sontag, E.1    Luangpirom, A.2    Hladik, C.3    Mudrak, I.4    Ogris, E.5    Speciale, S.6
  • 62
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule- binding activity of Tau by protein phosphatase 2A
    • Sontag E, Nunbhakdi-Craig V, Lee G, Bloom GS, Mumby MC. Regulation of the phosphorylation state and microtubule- binding activity of Tau by protein phosphatase 2A. Neuron 1996;17: 1201-7.
    • (1996) Neuron , vol.17 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 63
    • 41649095537 scopus 로고    scopus 로고
    • Risk and protective factors for sporadic Alzheimer's disease
    • Stozicka Z, Zilka N, Novak M. Risk and protective factors for sporadic Alzheimer's disease. Acta Virol 2007; 51: 205-22.
    • (2007) Acta Virol , vol.51 , pp. 205-222
    • Stozicka, Z.1    Zilka, N.2    Novak, M.3
  • 64
    • 44649165063 scopus 로고    scopus 로고
    • Physiological regulation of tau phosphorylation during hibernation
    • 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.
    • (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
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia V, Schuck T, Trojanowski JQ, Lee VM. PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp Neurol 2001; 168: 402-12.
    • (2001) Exp Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 66
    • 49349110718 scopus 로고    scopus 로고
    • Tau hyperphosphorylation correlates with reduced methylation of protein phosphatase 2A
    • Zhou XW, Gustafsson JA, Tanila H, Bjorkdahl C, Liu R, Winblad B, et al. Tau hyperphosphorylation correlates with reduced methylation of protein phosphatase 2A. Neurobiol Dis 2008; 31: 386-94.
    • (2008) Neurobiol Dis , vol.31 , pp. 386-394
    • Zhou, X.W.1    Gustafsson, J.A.2    Tanila, H.3    Bjorkdahl, C.4    Liu, R.5    Winblad, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.