메뉴 건너뛰기




Volumn 131, Issue 6, 2008, Pages 1416-1432

Argyrophilic grain disease

Author keywords

Alzheimer's disease; Argyrophilic grain disease; GSK 3 ; Mutant ubiquitin; Oxidative stress; P62; Stress kinases; Tau; Ubiquitin

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; GLYCOGEN SYNTHASE KINASE 3BETA; MANGANESE SUPEROXIDE DISMUTASE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE P38; MUTANT PROTEIN; NEUROTRANSMITTER; NEUROTRANSMITTER RECEPTOR; PROTEIN P62; PROTEIN TAU 4R; TAU PROTEIN; THROMBIN; UBIQUITIN;

EID: 44949150103     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awm305     Document Type: Review
Times cited : (172)

References (153)
  • 1
    • 0033677809 scopus 로고    scopus 로고
    • C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease
    • Abraha A, Ghoshal N, Gamblin TC, Cryns V, Berry RW, Kuret J, et al. C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease. J Cell Sci 2000; 113: 3737-45.
    • (2000) J Cell Sci , vol.113 , pp. 3737-3745
    • Abraha, A.1    Ghoshal, N.2    Gamblin, T.C.3    Cryns, V.4    Berry, R.W.5    Kuret, J.6
  • 2
    • 33746922758 scopus 로고    scopus 로고
    • Interlaboratory comparison of assessments of Alzheimer disease-related lesions: A study of the BrainNet Europe Consortium
    • Alafuzoff I, Pikkarainen M, Al-Sarraj S, Arzberger T, Bell J, Bodi I, et al. Interlaboratory comparison of assessments of Alzheimer disease-related lesions: a study of the BrainNet Europe Consortium. J Neuropathol Exp Neurol 2006; 65: 740-57.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 740-757
    • Alafuzoff, I.1    Pikkarainen, M.2    Al-Sarraj, S.3    Arzberger, T.4    Bell, J.5    Bodi, I.6
  • 3
    • 14044278145 scopus 로고    scopus 로고
    • Proteolysis of non-phosphorylated and phosphorylated tau by thrombin
    • Arai T, Guo GP, McGeer PL. Proteolysis of non-phosphorylated and phosphorylated tau by thrombin. J Biol Chem 2005; 280: 5145-53.
    • (2005) J Biol Chem , vol.280 , pp. 5145-5153
    • Arai, T.1    Guo, G.P.2    McGeer, P.L.3
  • 4
    • 33644905917 scopus 로고    scopus 로고
    • Thrombin and prothrombin are expressed by neurons and glial cells and accumulate in neurofibrillary tangles in Alzheimer disease brain
    • Arai T, Miklossy J, Klegeris A, Guo JP, McGeer PL. Thrombin and prothrombin are expressed by neurons and glial cells and accumulate in neurofibrillary tangles in Alzheimer disease brain. J Neuropathol Exp Neurol 2006; 65: 19-25.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 19-25
    • Arai, T.1    Miklossy, J.2    Klegeris, A.3    Guo, J.P.4    McGeer, P.L.5
  • 5
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes tau formation of neurofibrillary tangles in Alzheimer's disease
    • Bancher C, Brunner C, Lassman H, Budka H, Jellinger K, Wiche G, et al. Accumulation of abnormally phosphorylated tau precedes tau formation of neurofibrillary tangles in Alzheimer's disease. Brain Res 1989; 477: 90-9.
    • (1989) Brain Res , vol.477 , pp. 90-99
    • Bancher, C.1    Brunner, C.2    Lassman, H.3    Budka, H.4    Jellinger, K.5    Wiche, G.6
  • 8
    • 0032862488 scopus 로고    scopus 로고
    • Astrocytes expressing hyperphosphorylated tau protein without glial fibrillary tangles in argyrophilic grain disease
    • Botez G, Probst A, Ipsen S, Tolnay M. Astrocytes expressing hyperphosphorylated tau protein without glial fibrillary tangles in argyrophilic grain disease. Acta Neuropathol 1999; 98: 251-6.
    • (1999) Acta Neuropathol , vol.98 , pp. 251-256
    • Botez, G.1    Probst, A.2    Ipsen, S.3    Tolnay, M.4
  • 9
    • 33749150163 scopus 로고    scopus 로고
    • Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
    • Braak H, Alafuzoff I, Arzberger T, Kretzschmar H, Del Tredici K. Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry. Acta Neuropathol 2006; 112: 389-404.
    • (2006) Acta Neuropathol , vol.112 , pp. 389-404
    • Braak, H.1    Alafuzoff, I.2    Arzberger, T.3    Kretzschmar, H.4    Del Tredici, K.5
  • 10
    • 0023111344 scopus 로고
    • Argyrophylic grains: Characteristic pathology of cerebral cortex in cases of adult-onset dementia without Alzheimer changes
    • Braak H, Braak E. Argyrophylic grains: characteristic pathology of cerebral cortex in cases of adult-onset dementia without Alzheimer changes. Neurosci Lett 1987; 76: 124-7.
    • (1987) Neurosci Lett , vol.76 , pp. 124-127
    • Braak, H.1    Braak, E.2
  • 11
    • 0024518532 scopus 로고
    • Cortical and subcortical argyrophylic grains characterize a disease associated with adult onset dementia
    • Braak H, Braak E. Cortical and subcortical argyrophylic grains characterize a disease associated with adult onset dementia. Neuropathol Appl Neurobiol 1989; 15: 13-26.
    • (1989) Neuropathol Appl Neurobiol , vol.15 , pp. 13-26
    • Braak, H.1    Braak, E.2
  • 12
    • 0031736575 scopus 로고    scopus 로고
    • Argyrophilic grain disease: Frequency of occurrence in different age categories and neuropathological diagnostic criteria
    • Braak H, Braak E. Argyrophilic grain disease: frequency of occurrence in different age categories and neuropathological diagnostic criteria. J Neural Transm 1998; 105: 801-19.
    • (1998) J Neural Transm , vol.105 , pp. 801-819
    • Braak, H.1    Braak, E.2
  • 13
    • 44949231869 scopus 로고    scopus 로고
    • Braak H, Braak E. Temporal sequence of Alzheimer's disease-related pathology. In: Peters A and Morrison JH, editors. Cerebral Cortex 14: Neurodegenerative and Age-related Changes in Structure and Function of Cerebral Cortex. New York, Boston, Dordrecht, London, Moscow: Kluwer Academic/Plenum Press; 1999. p. 475-512.
    • Braak H, Braak E. Temporal sequence of Alzheimer's disease-related pathology. In: Peters A and Morrison JH, editors. Cerebral Cortex Vol 14: Neurodegenerative and Age-related Changes in Structure and Function of Cerebral Cortex. New York, Boston, Dordrecht, London, Moscow: Kluwer Academic/Plenum Press; 1999. p. 475-512.
  • 14
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak H, Braak E, Mandelkow EM. A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol 1994; 87: 554-67.
    • (1994) Acta Neuropathol , vol.87 , pp. 554-567
    • Braak, H.1    Braak, E.2    Mandelkow, E.M.3
  • 16
    • 0037181485 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells
    • Buée-Scherrer V, Goedert M. Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells. FEBS Lett 2002; 515: 151-4.
    • (2002) FEBS Lett , vol.515 , pp. 151-154
    • Buée-Scherrer, V.1    Goedert, M.2
  • 17
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
    • Butterfield DA, Perluigi M, Sultana R. Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. Eur J Pharmacol 2006a; 545: 39-50.
    • (2006) Eur J Pharmacol , vol.545 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 18
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease
    • Butterfield DA, Poon HF, St Clair D, Keller JN, Pierce WN, Klein JB, et al. Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiol Dis 2006b; 22: 223-32.
    • Neurobiol Dis 2006b , vol.22 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    St Clair, D.3    Keller, J.N.4    Pierce, W.N.5    Klein, J.B.6
  • 19
    • 34447096691 scopus 로고    scopus 로고
    • Neuropathologic diagnostic and nosologic criteria for frontotemporal lobal degeneration: Consensus of the consortium for frontotemporal lobar degeneration
    • Cairns NJ, Bigio EH, MacKenzie IRA, Neumann M, Lee VMY, Hatanpaa KJ, et al. Neuropathologic diagnostic and nosologic criteria for frontotemporal lobal degeneration: consensus of the consortium for frontotemporal lobar degeneration. Acta Neuropathol 2007; 114: 5-22.
    • (2007) Acta Neuropathol , vol.114 , pp. 5-22
    • Cairns, N.J.1    Bigio, E.H.2    MacKenzie, I.R.A.3    Neumann, M.4    Lee, V.M.Y.5    Hatanpaa, K.J.6
  • 20
    • 34249810042 scopus 로고    scopus 로고
    • Oxidative inactivation of the proteasome in Alzheimer's disease
    • Cecarini V, Ding Q, Keller JN. Oxidative inactivation of the proteasome in Alzheimer's disease. Free Radic Res 2007; 41: 673-80.
    • (2007) Free Radic Res , vol.41 , pp. 673-680
    • Cecarini, V.1    Ding, Q.2    Keller, J.N.3
  • 21
    • 33747606218 scopus 로고    scopus 로고
    • Expression of a truncated tau protein induces oxidative stress in a rodent model of tauopathy
    • Cente M, Filipcik P, Pevalova M, Novak M. Expression of a truncated tau protein induces oxidative stress in a rodent model of tauopathy. Eur J Neurosci 2006; 24: 1085-90.
    • (2006) Eur J Neurosci , vol.24 , pp. 1085-1090
    • Cente, M.1    Filipcik, P.2    Pevalova, M.3    Novak, M.4
  • 22
    • 0029879877 scopus 로고    scopus 로고
    • Glial inclusions in the CNS degenerative diseases
    • Chin SM, Goldman EJ. Glial inclusions in the CNS degenerative diseases. J Neuropathol Exp Neurol 1996; 55: 499-508.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 499-508
    • Chin, S.M.1    Goldman, E.J.2
  • 23
    • 0025833715 scopus 로고
    • Dementia with argyrophilic grains
    • Cras P, Perry G. Dementia with argyrophilic grains. Ann Neurol 1991; 30: 853-4.
    • (1991) Ann Neurol , vol.30 , pp. 853-854
    • Cras, P.1    Perry, G.2
  • 26
    • 4444274236 scopus 로고    scopus 로고
    • Accumulation of aberrant ubiquitin induces aggregate formation and cell death in polyglutamine diseases
    • de Pril R, Fischer DF, Maat-Schieman ML, Hobo B, De Vos RA, Brunt ER, et al. Accumulation of aberrant ubiquitin induces aggregate formation and cell death in polyglutamine diseases. Hum Mol Genet 2004; 13: 1803-13.
    • (2004) Hum Mol Genet , vol.13 , pp. 1803-1813
    • de Pril, R.1    Fischer, D.F.2    Maat-Schieman, M.L.3    Hobo, B.4    De Vos, R.A.5    Brunt, E.R.6
  • 29
    • 0033928035 scopus 로고    scopus 로고
    • The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis
    • Fasulo L, Ugolini G, Visintin M, Bradbury A, Brancolini C, Verzillo V, et al. The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis. J Neurochem 2000; 75: 624-33.
    • (2000) J Neurochem , vol.75 , pp. 624-633
    • Fasulo, L.1    Ugolini, G.2    Visintin, M.3    Bradbury, A.4    Brancolini, C.5    Verzillo, V.6
  • 30
    • 44949182456 scopus 로고    scopus 로고
    • El método de Golgi en neuropatología humana
    • Cruz-Sanchez F, editor, Madrid: Edimsa;
    • Ferrer I. El método de Golgi en neuropatología humana. In: Cruz-Sanchez F, editor. Neuropatología. Madrid: Edimsa; 2000. p. 113-6.
    • (2000) Neuropatología , pp. 113-116
    • Ferrer, I.1
  • 31
    • 13944281035 scopus 로고    scopus 로고
    • Stress kinases involved in tau phosphorylation in Alzheimer's disease, tauopathies, and APP transgenic mice
    • Ferrer I. Stress kinases involved in tau phosphorylation in Alzheimer's disease, tauopathies, and APP transgenic mice. Neurotox Res 2004; 6: 469-75.
    • (2004) Neurotox Res , vol.6 , pp. 469-475
    • Ferrer, I.1
  • 32
    • 0020692937 scopus 로고
    • Growth of abnormal neurites in Alzheimer's disease. A study with the Golgi method
    • Ferrer I, Aymami A, Rovira A, Grau Veciana JM. Growth of abnormal neurites in Alzheimer's disease. A study with the Golgi method. Acta Neuropathol 1983; 59: 167-70.
    • (1983) Acta Neuropathol , vol.59 , pp. 167-170
    • Ferrer, I.1    Aymami, A.2    Rovira, A.3    Grau Veciana, J.M.4
  • 33
    • 0036942843 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is associated with neuronal and glial hyperphosphorylated tau deposits in Alzheimer's disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration
    • Ferrer I, Barrachina M, Puig B. Glycogen synthase kinase-3 is associated with neuronal and glial hyperphosphorylated tau deposits in Alzheimer's disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration. Acta Neuropathol 2002a; 104: 583-91.
    • (2002) Acta Neuropathol , vol.104 , pp. 583-591
    • Ferrer, I.1    Barrachina, M.2    Puig, B.3
  • 34
    • 0036944509 scopus 로고    scopus 로고
    • Anti-tau phosphospecific Ser262 antibody recognizes a variety of abnormal hyper-phosphorylated tau deposits in tauopathies including Pick's disease and argyrophilic grains
    • Ferrer I, Barrachina M, Puig B. Anti-tau phosphospecific Ser262 antibody recognizes a variety of abnormal hyper-phosphorylated tau deposits in tauopathies including Pick's disease and argyrophilic grains. Acta Neuropathol 2002b; 104: 658-64.
    • (2002) Acta Neuropathol , vol.104 , pp. 658-664
    • Ferrer, I.1    Barrachina, M.2    Puig, B.3
  • 35
    • 0037246583 scopus 로고    scopus 로고
    • Phosphorylated protein kinases associated with neuronal and glial tau deposits in argyrophilic grain disease
    • Ferrer I, Barrachina M, Tolnay M, Rey MJ, Vidal N, Carmona M, et al. Phosphorylated protein kinases associated with neuronal and glial tau deposits in argyrophilic grain disease. Brain Pathol 2003; 13: 62-78.
    • (2003) Brain Pathol , vol.13 , pp. 62-78
    • Ferrer, I.1    Barrachina, M.2    Tolnay, M.3    Rey, M.J.4    Vidal, N.5    Carmona, M.6
  • 36
    • 25844458239 scopus 로고    scopus 로고
    • Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies
    • Ferrer I, Gomez-Isla T, Puig B, Freixes M, Ribe E, Dalfo E, et al. Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies. Curr Alzheimer Res 2005; 2: 3-18.
    • (2005) Curr Alzheimer Res , vol.2 , pp. 3-18
    • Ferrer, I.1    Gomez-Isla, T.2    Puig, B.3    Freixes, M.4    Ribe, E.5    Dalfo, E.6
  • 37
    • 0025330884 scopus 로고
    • Neuronal alterations in patients with dementia: A Golgi study on biopsy samples
    • Ferrer I, Guionnet N, Cruz-Sanchez F, Tuñon T. Neuronal alterations in patients with dementia: a Golgi study on biopsy samples. Neurosci Lett 1990; 114: 11-6.
    • (1990) Neurosci Lett , vol.114 , pp. 11-16
    • Ferrer, I.1    Guionnet, N.2    Cruz-Sanchez, F.3    Tuñon, T.4
  • 38
    • 0142124410 scopus 로고    scopus 로고
    • Primary progressive aphasia as the initial manifestation of corticobasal degeneration and unusual tauopathies
    • Ferrer I, Hernandez I, Boada M, Llorente A, Rey MJ, Cardozo A, et al. Primary progressive aphasia as the initial manifestation of corticobasal degeneration and unusual tauopathies. Acta Neuropathol 2003; 106: 419-35.
    • (2003) Acta Neuropathol , vol.106 , pp. 419-435
    • Ferrer, I.1    Hernandez, I.2    Boada, M.3    Llorente, A.4    Rey, M.J.5    Cardozo, A.6
  • 39
    • 0242611535 scopus 로고    scopus 로고
    • Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain
    • Fischer DF, De Vos RA, Van DR, De Vrij FM, Proper EA, Sonnemans MA, et al. Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain. FASEB J 2003; 17: 2014-24.
    • (2003) FASEB J , vol.17 , pp. 2014-2024
    • Fischer, D.F.1    De Vos, R.A.2    Van, D.R.3    De Vrij, F.M.4    Proper, E.A.5    Sonnemans, M.A.6
  • 40
    • 9444267091 scopus 로고    scopus 로고
    • Ballooned neurons in the limbic lobe are associated with Alzheimer type pathology and lack diagnostic specificity
    • Fujino Y, Delucia MW, Davies P, Dickson DW. Ballooned neurons in the limbic lobe are associated with Alzheimer type pathology and lack diagnostic specificity. Neuropathol Appl Neurobiol 2004; 30: 676-82.
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 676-682
    • Fujino, Y.1    Delucia, M.W.2    Davies, P.3    Dickson, D.W.4
  • 41
    • 15244350098 scopus 로고    scopus 로고
    • Increased frequency of argyrophilic grain disease in Alzheimer disease with 4R tau-specific immunohistochemistry
    • Fujino Y, Wang DS, Thomas N, Espinoza M, Davies P, Dickson DW. Increased frequency of argyrophilic grain disease in Alzheimer disease with 4R tau-specific immunohistochemistry. J Neuropathol Exp Neurol 2005; 64: 209-14.
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 209-214
    • Fujino, Y.1    Wang, D.S.2    Thomas, N.3    Espinoza, M.4    Davies, P.5    Dickson, D.W.6
  • 42
    • 0037070216 scopus 로고    scopus 로고
    • Structure and functional properties of the ubiquitin binding protein p62
    • Geetha T, Wooten MW. Structure and functional properties of the ubiquitin binding protein p62. FEBS Lett 2002; 512: 19-24.
    • (2002) FEBS Lett , vol.512 , pp. 19-24
    • Geetha, T.1    Wooten, M.W.2
  • 43
    • 0031679880 scopus 로고    scopus 로고
    • Argyrophilic grain disease is associated with apolipoprotein E epsilon 2 allele
    • Ghebremedin E, Schultz C, Botez G, Rub U, Sassin I, Braak E, et al. Argyrophilic grain disease is associated with apolipoprotein E epsilon 2 allele. Acta Neuropathol 1998; 96: 222-4.
    • (1998) Acta Neuropathol , vol.96 , pp. 222-224
    • Ghebremedin, E.1    Schultz, C.2    Botez, G.3    Rub, U.4    Sassin, I.5    Braak, E.6
  • 44
    • 0036372586 scopus 로고    scopus 로고
    • Genetic association of argyrophilic grain disease with polymorphisms in alpha-2 macroglobulin and low-density lipoprotein receptor-related protein genes
    • Ghebremedin E, Schultz C, Thal DR, Del Tredici K, Rueb U, Braak H. Genetic association of argyrophilic grain disease with polymorphisms in alpha-2 macroglobulin and low-density lipoprotein receptor-related protein genes. Neuropathol Appl Neurobiol 2002; 28: 308-13.
    • (2002) Neuropathol Appl Neurobiol , vol.28 , pp. 308-313
    • Ghebremedin, E.1    Schultz, C.2    Thal, D.R.3    Del Tredici, K.4    Rueb, U.5    Braak, H.6
  • 45
    • 40149111037 scopus 로고    scopus 로고
    • Interactive domains in the molecular chaperone human αB-crystallin modulate microtubule assembly and disassembly
    • Ghosh JG, Houck SA, Clark JI. Interactive domains in the molecular chaperone human αB-crystallin modulate microtubule assembly and disassembly. PLoS ONE 2007a; 2: e498.
    • PLoS ONE 2007a , vol.2
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 46
    • 34548241302 scopus 로고    scopus 로고
    • Interactive sequences in the stress protein and molecular chaperone human αB-crystallin recognize and modulate the assembly of filaments
    • Ghosh JG, Houck SA, Clark JI. Interactive sequences in the stress protein and molecular chaperone human αB-crystallin recognize and modulate the assembly of filaments. In J Biochem Cell Biol 2007b; 39: 1804-15.
    • (2007) In J Biochem Cell Biol , vol.39 , pp. 1804-1815
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 47
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002; 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 48
    • 0030963035 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases
    • Goedert M, Hasegawa M, Jakes R, Lawler S, Cuenda A, Cohen P. Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. FEBS Lett 1997; 409: 57-62.
    • (1997) FEBS Lett , vol.409 , pp. 57-62
    • Goedert, M.1    Hasegawa, M.2    Jakes, R.3    Lawler, S.4    Cuenda, A.5    Cohen, P.6
  • 49
    • 0032191105 scopus 로고    scopus 로고
    • Filamentous nerve cell inclusions in neurodegenerative diseases
    • Goedert M, Spillantini MG, Davies SW. Filamentous nerve cell inclusions in neurodegenerative diseases. Curr Opin Neurobiol 1998; 8: 619-32.
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 619-632
    • Goedert, M.1    Spillantini, M.G.2    Davies, S.W.3
  • 50
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert M, Spillanini MG, Potier MC, Ulrich J, Crowther RA. Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J 1989; 8: 393-9.
    • (1989) EMBO J , vol.8 , pp. 393-399
    • Goedert, M.1    Spillanini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 51
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci Lett 1992; 147: 58-62.
    • (1992) Neurosci Lett , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 53
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeat C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler A, Drechsel D, Kirschner MW, Martin DW. Tau consists of a set of proteins with repeat C-terminal microtubule-binding domains and variable N-terminal domains. Mol Cell Biol 1989; 9: 1381-8.
    • (1989) Mol Cell Biol , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin, D.W.4
  • 56
    • 0031957225 scopus 로고    scopus 로고
    • Glial tau pathology in neurodegenerative diseases: Their nature and comparison with neuronal tangles
    • Ikeda K, Akiyama H, Arai T, Nishima T. Glial tau pathology in neurodegenerative diseases: their nature and comparison with neuronal tangles. Neurobiol Dis 1998; 19: 85-91.
    • (1998) Neurobiol Dis , vol.19 , pp. 85-91
    • Ikeda, K.1    Akiyama, H.2    Arai, T.3    Nishima, T.4
  • 57
    • 0028932725 scopus 로고
    • A study of dementia with argyrophilic grains. Possible cytoskeletal abnormality in dendrospinal portion of neurons and oligodendroglia
    • Ikeda K, Akiyama H, Kondo H, Haga C. A study of dementia with argyrophilic grains. Possible cytoskeletal abnormality in dendrospinal portion of neurons and oligodendroglia. Acta Neuropathol 1995; 89: 409-14.
    • (1995) Acta Neuropathol , vol.89 , pp. 409-414
    • Ikeda, K.1    Akiyama, H.2    Kondo, H.3    Haga, C.4
  • 58
    • 17644375139 scopus 로고    scopus 로고
    • Argyrophilic grain disease presenting with frontotemporal dementia: A neuropsychological and pathological study of an autopsied case with presenile onset
    • Ishihara K, Araki S, Ihori N, Shiota J, Kawamura M, Yoshida M, et al. Argyrophilic grain disease presenting with frontotemporal dementia: a neuropsychological and pathological study of an autopsied case with presenile onset. Neuropathology 2005; 25: 165-70.
    • (2005) Neuropathology , vol.25 , pp. 165-170
    • Ishihara, K.1    Araki, S.2    Ihori, N.3    Shiota, J.4    Kawamura, M.5    Yoshida, M.6
  • 59
    • 0036898065 scopus 로고    scopus 로고
    • Selective neurofibrillary degeneration of the hippocampal CA2 sector is associated with four-repeat tauopathies
    • Ishizawa T, Ko LW, Cookson N, Davias P, Espinoza M, Dickson DW. Selective neurofibrillary degeneration of the hippocampal CA2 sector is associated with four-repeat tauopathies. J Neuropathol Exp Neurol 2002; 61: 1040-7.
    • (2002) J Neuropathol Exp Neurol , vol.61 , pp. 1040-1047
    • Ishizawa, T.1    Ko, L.W.2    Cookson, N.3    Davias, P.4    Espinoza, M.5    Dickson, D.W.6
  • 61
    • 0031922290 scopus 로고    scopus 로고
    • Dementia with grains (argyrophilic grain disease)
    • Jellinger KA. Dementia with grains (argyrophilic grain disease). Brain Pathol 1998; 8: 377-86.
    • (1998) Brain Pathol , vol.8 , pp. 377-386
    • Jellinger, K.A.1
  • 62
    • 0031949083 scopus 로고    scopus 로고
    • Senile dementia with tangles (tangle predominant form of senile dementia)
    • Jellinger KA, Bancher C. Senile dementia with tangles (tangle predominant form of senile dementia). Brain Pathol 1998; 8: 367-76.
    • (1998) Brain Pathol , vol.8 , pp. 367-376
    • Jellinger, K.A.1    Bancher, C.2
  • 63
    • 0034650631 scopus 로고    scopus 로고
    • Modulation of tau phosphorylation and intracellular localization by cellular stress
    • Jenkins SM, Zinnerman M, Garner C, Johnson GV. Modulation of tau phosphorylation and intracellular localization by cellular stress. Biochem J 2000; 345: 263-70.
    • (2000) Biochem J , vol.345 , pp. 263-270
    • Jenkins, S.M.1    Zinnerman, M.2    Garner, C.3    Johnson, G.V.4
  • 64
    • 33746689889 scopus 로고    scopus 로고
    • Argyrophilic grain disease in demented subjects presenting initially with amnestic mild cognitive impairment
    • Jicha GA, Petersen RC, Knopman DS, Boeve BF, Smith GE, Geda YE, et al. Argyrophilic grain disease in demented subjects presenting initially with amnestic mild cognitive impairment. J Neuropathol Exp Neurol 2006; 65: 602-9.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 602-609
    • Jicha, G.A.1    Petersen, R.C.2    Knopman, D.S.3    Boeve, B.F.4    Smith, G.E.5    Geda, Y.E.6
  • 65
    • 44949172239 scopus 로고    scopus 로고
    • Josephs KA, Whitwell JL, Parisi JE, Knopman DS, Boeve BF, Geda YE, et al. Argyrophilic grai: a distinct disease or an additive pathology? Neurobiol Aging 2006 Dec 22 [Epub ahead of print].
    • Josephs KA, Whitwell JL, Parisi JE, Knopman DS, Boeve BF, Geda YE, et al. Argyrophilic grai: a distinct disease or an additive pathology? Neurobiol Aging 2006 Dec 22 [Epub ahead of print].
  • 66
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S, Nitsch R, Grune T, Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 2003; 85: 115-22.
    • (2003) J Neurochem , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 67
    • 0032994877 scopus 로고    scopus 로고
    • Argyrophilic grains in late-onset Creutzfeldt-Jakob diseased brains
    • Kiwashima T, Katsumi D, Iwaki T. Argyrophilic grains in late-onset Creutzfeldt-Jakob diseased brains. Pathol Internat 1999; 49: 369-73.
    • (1999) Pathol Internat , vol.49 , pp. 369-373
    • Kiwashima, T.1    Katsumi, D.2    Iwaki, T.3
  • 68
    • 30444461074 scopus 로고    scopus 로고
    • Alpha-synuclein immunohistochemistry in two cases of co-ocurring idiopathic Parkinson's disease and motor neuron disease
    • Klos KJ, Josephs KA, Parisi JE, Dickson DW. Alpha-synuclein immunohistochemistry in two cases of co-ocurring idiopathic Parkinson's disease and motor neuron disease. Mov Disord 2005; 20: 1515-20.
    • (2005) Mov Disord , vol.20 , pp. 1515-1520
    • Klos, K.J.1    Josephs, K.A.2    Parisi, J.E.3    Dickson, D.W.4
  • 70
    • 0032886469 scopus 로고    scopus 로고
    • Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease
    • Komori T. Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease. Brain Pathol 1999; 9: 663-79.
    • (1999) Brain Pathol , vol.9 , pp. 663-679
    • Komori, T.1
  • 71
    • 47749139615 scopus 로고    scopus 로고
    • MAPT S305I mutation: Implications for argyrophilic grain disease
    • Dec 8 [Epub ahead of print
    • Kovacks GK, Pittman A, Revesz T, Luk C, Lees A, et al. MAPT S305I mutation: implications for argyrophilic grain disease. Acta Neuropathol 2007; Dec 8 [Epub ahead of print].
    • (2007) Acta Neuropathol
    • Kovacks, G.K.1    Pittman, A.2    Revesz, T.3    Luk, C.4    Lees, A.5
  • 72
    • 0344305371 scopus 로고    scopus 로고
    • Morphogenesis of Lewy bodies: Dissimilar incorporation of alpha-synuclein, ubiquitin, and p62
    • Kuusisto E, Parkkinen L, Alafuzoff I. Morphogenesis of Lewy bodies: dissimilar incorporation of alpha-synuclein, ubiquitin, and p62. J Neuropathol Exp Neurol 2003; 62: 1241-53.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 1241-1253
    • Kuusisto, E.1    Parkkinen, L.2    Alafuzoff, I.3
  • 73
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto E, Salminen A, Alafuzoff I. Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. Neuroreport 2001; 12: 2085-90.
    • (2001) Neuroreport , vol.12 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 74
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: Possible role in tangle formation
    • Kuusisto E, Salminen A, Alafuzoff I. Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation. Neuropathol Appl Neurobiol 2002; 28: 228-37.
    • (2002) Neuropathol Appl Neurobiol , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 76
    • 0141428795 scopus 로고    scopus 로고
    • Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders
    • Layfield R, Cavey JR, Lowe J. Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders. Ageing Res Rev 2003; 2: 343-56.
    • (2003) Ageing Res Rev , vol.2 , pp. 343-356
    • Layfield, R.1    Cavey, J.R.2    Lowe, J.3
  • 77
    • 33846129434 scopus 로고    scopus 로고
    • Increased level of active GSK-3β in Alzheimer's disease and accumulation in argyrophilic grains in neurones at different stages of neurofibrillary degeneration
    • Leroy K, Yilmaz Z, Brion JP. Increased level of active GSK-3β in Alzheimer's disease and accumulation in argyrophilic grains in neurones at different stages of neurofibrillary degeneration. Neuropathol Appl Neurobiol 2007; 33: 43-55.
    • (2007) Neuropathol Appl Neurobiol , vol.33 , pp. 43-55
    • Leroy, K.1    Yilmaz, Z.2    Brion, J.P.3
  • 79
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten K, De Vrij FM, Verhoef LG, Fischer DF, van Leeuwen FW, Hol EM, et al. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J Cell Biol 2002; 157: 417-27.
    • (2002) J Cell Biol , vol.157 , pp. 417-427
    • Lindsten, K.1    De Vrij, F.M.2    Verhoef, L.G.3    Fischer, D.F.4    van Leeuwen, F.W.5    Hol, E.M.6
  • 80
    • 0030937952 scopus 로고    scopus 로고
    • The phosphorylation of tau: A critical stage in neurodevelopment and neurodegenerative processes
    • Lovestone S, Reynolds CH. The phosphorylation of tau: a critical stage in neurodevelopment and neurodegenerative processes. Neuroscience 1997; 78: 309-24.
    • (1997) Neuroscience , vol.78 , pp. 309-324
    • Lovestone, S.1    Reynolds, C.H.2
  • 81
    • 0026619584 scopus 로고
    • Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau
    • Mandelkow EM, Drewes G, Biernat J, Gustke N, Van Lint J, Vandenheede JR, et al. Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau. FEBS Lett 1992; 314: 315-21.
    • (1992) FEBS Lett , vol.314 , pp. 315-321
    • Mandelkow, E.M.1    Drewes, G.2    Biernat, J.3    Gustke, N.4    Van Lint, J.5    Vandenheede, J.R.6
  • 82
    • 0030817295 scopus 로고    scopus 로고
    • Prevalence and disease association of argyrophilic grains of Braak
    • Martinez-Lage M, Muñoz DG. Prevalence and disease association of argyrophilic grains of Braak. J Neuropathol Exp Neurol 1997; 56: 157-64.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 157-164
    • Martinez-Lage, M.1    Muñoz, D.G.2
  • 83
    • 0025804556 scopus 로고
    • Late onset dementia with argyrophilic grains and subcortical tangles or atypical progressive supranuclear palsy
    • Masliah E, Hansen LA, Quijata S, De Teresa R, Alford M, Kauss J, et al. Late onset dementia with argyrophilic grains and subcortical tangles or atypical progressive supranuclear palsy. Ann Neurol 1991; 29: 389-96.
    • (1991) Ann Neurol , vol.29 , pp. 389-396
    • Masliah, E.1    Hansen, L.A.2    Quijata, S.3    De Teresa, R.4    Alford, M.5    Kauss, J.6
  • 84
    • 0345307188 scopus 로고    scopus 로고
    • Diffuse form of argyrophilic grain disease: A new variant of four-repeat tauopathy different from limbic argyrophilic grain disease
    • Maurage CA, Sergeant N, Schraen-Maschke SS, Lebert F, Ruchoux MM, Sablonnière B, et al. Diffuse form of argyrophilic grain disease: a new variant of four-repeat tauopathy different from limbic argyrophilic grain disease. Acta Neuropathol 2003; 106: 575-83.
    • (2003) Acta Neuropathol , vol.106 , pp. 575-583
    • Maurage, C.A.1    Sergeant, N.2    Schraen-Maschke, S.S.3    Lebert, F.4    Ruchoux, M.M.5    Sablonnière, B.6
  • 85
    • 33144489150 scopus 로고    scopus 로고
    • Diagnostic [Diagnostics? Diagnosis?] and management of dementia with Lewy bodies: Third report of the DLB Consortium
    • McKeith IG, Dickson DW, Lowe J, Emre M, O'Brien JT, Feldman H, et al. Diagnostic [Diagnostics? Diagnosis?] and management of dementia with Lewy bodies: third report of the DLB Consortium. Neurology 2005; 65: 1863-72.
    • (2005) Neurology , vol.65 , pp. 1863-1872
    • McKeith, I.G.1    Dickson, D.W.2    Lowe, J.3    Emre, M.4    O'Brien, J.T.5    Feldman, H.6
  • 86
    • 0142062477 scopus 로고    scopus 로고
    • Argyrophilic grain disease: Molecular genetic difference to other four-repeat tauopathies
    • Miserez AR, Clavaguera F, Monsch AU, Probst A, Tolnay M. Argyrophilic grain disease: molecular genetic difference to other four-repeat tauopathies. Acta Neuropathol 2003; 106: 363-6.
    • (2003) Acta Neuropathol , vol.106 , pp. 363-366
    • Miserez, A.R.1    Clavaguera, F.2    Monsch, A.U.3    Probst, A.4    Tolnay, M.5
  • 88
    • 0035937652 scopus 로고    scopus 로고
    • Deafferentation of the hippocampus results in the induction of AT8 positive 'granules' in the rat
    • Mudher AK, Yee B, Smith AD, Perry VH. Deafferentation of the hippocampus results in the induction of AT8 positive 'granules' in the rat. Neurosci Lett 2001; 301: 5-8.
    • (2001) Neurosci Lett , vol.301 , pp. 5-8
    • Mudher, A.K.1    Yee, B.2    Smith, A.D.3    Perry, V.H.4
  • 89
    • 2442585133 scopus 로고    scopus 로고
    • Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: Possible mechanisms and the role in Lewy body formation in Parkinson's disease
    • Nakaso K, Yoshimoto Y, Nakano T, Takeshima T, Fukuhara Y, Yasui K, et al. Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson's disease. Brain Res 2004; 1012: 42-51.
    • (2004) Brain Res , vol.1012 , pp. 42-51
    • Nakaso, K.1    Yoshimoto, Y.2    Nakano, T.3    Takeshima, T.4    Fukuhara, Y.5    Yasui, K.6
  • 90
    • 0026053022 scopus 로고
    • Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51
    • Novak M, Jakes R, Edwards PC, Milstein C, Wischik CM. Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51. Proc Natl Acad Sci USA 1991; 88: 5837-41.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5837-5841
    • Novak, M.1    Jakes, R.2    Edwards, P.C.3    Milstein, C.4    Wischik, C.M.5
  • 91
    • 0027398169 scopus 로고
    • Molecular characterisation of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak M, Kabat J, Wischik CM. Molecular characterisation 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
  • 93
    • 34548028021 scopus 로고    scopus 로고
    • Analysis of the αB-crystallin domain responsible for inhibiting tubulin aggregation
    • Ohto-Fujita E, Fujita Y, Atomi Y. Analysis of the αB-crystallin domain responsible for inhibiting tubulin aggregation. Cell Stress Chaperones 2007; 12: 163-71.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 163-171
    • Ohto-Fujita, E.1    Fujita, Y.2    Atomi, Y.3
  • 94
    • 20444373701 scopus 로고    scopus 로고
    • Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets
    • Pamplona R, Dalfó E, Ayala V, Bellmunt J, Prat J, Ferrer I, et al. Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets. J Biol Chem 2005; 280: 21522-30.
    • (2005) J Biol Chem , vol.280 , pp. 21522-21530
    • Pamplona, R.1    Dalfó, E.2    Ayala, V.3    Bellmunt, J.4    Prat, J.5    Ferrer, I.6
  • 95
    • 34548132073 scopus 로고    scopus 로고
    • Expression levels of adenosine receptors in hippocampus and frontal cortex in argyrophilic grain disease
    • Perez-Buira S, Barrachina M, Rodriguez A, Albasanz JL, Martin M, Ferrer I. Expression levels of adenosine receptors in hippocampus and frontal cortex in argyrophilic grain disease. Neurosci Lett 2007; 423: 194-9.
    • (2007) Neurosci Lett , vol.423 , pp. 194-199
    • Perez-Buira, S.1    Barrachina, M.2    Rodriguez, A.3    Albasanz, J.L.4    Martin, M.5    Ferrer, I.6
  • 98
    • 10044281817 scopus 로고    scopus 로고
    • Lewy bodies in the amygdala: Increase of α-synuclein aggregates in neurodegenerative diseases with tau-based inclusions
    • Popescu A, Lippa CF, Lee VM, Trojanowski JQ. Lewy bodies in the amygdala: increase of α-synuclein aggregates in neurodegenerative diseases with tau-based inclusions. Arch Neurol 2004; 61: 1915-9.
    • (2004) Arch Neurol , vol.61 , pp. 1915-1919
    • Popescu, A.1    Lippa, C.F.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 99
    • 44949244613 scopus 로고
    • Neuritic plaques in senile dementia of Alzheimer's type: A Golgi analysis in the hippocampal region
    • Probst A, Basler V, Bron B, Ulrich J. Neuritic plaques in senile dementia of Alzheimer's type: a Golgi analysis in the hippocampal region. Brain Res 1983; 59: 167-70.
    • (1983) Brain Res , vol.59 , pp. 167-170
    • Probst, A.1    Basler, V.2    Bron, B.3    Ulrich, J.4
  • 100
    • 34848856633 scopus 로고    scopus 로고
    • Hippocampal sclerosis dementia: A reappraisal
    • Probst A, Taylor KI, Tolnay M. Hippocampal sclerosis dementia: a reappraisal. Acta Neuropathol 2007; 114: 335-45.
    • (2007) Acta Neuropathol , vol.114 , pp. 335-345
    • Probst, A.1    Taylor, K.I.2    Tolnay, M.3
  • 101
    • 21444458486 scopus 로고    scopus 로고
    • BetaII-tubulin and phospho-tau aggregates in Alzheimer's disease and Pick's disease
    • Puig B, Ferrer I, Ludueña RF, Avila J. BetaII-tubulin and phospho-tau aggregates in Alzheimer's disease and Pick's disease. J Alzheimers Dis 2005; 7: 213-20.
    • (2005) J Alzheimers Dis , vol.7 , pp. 213-220
    • Puig, B.1    Ferrer, I.2    Ludueña, R.F.3    Avila, J.4
  • 102
    • 7044284920 scopus 로고    scopus 로고
    • Expression of stress-activated kinase c-Jun N-terminal kinase (SAPK/JNK-P) and p38 (p38-P), and tau hyperphosphorylation in neurites surrounding βA plaques in APP Tg2576 mice
    • Puig B, Gómez-Isla T, Ribé E, Cuadrado M, Torrejón-Escribano B, Dalfó E, et al. Expression of stress-activated kinase c-Jun N-terminal kinase (SAPK/JNK-P) and p38 (p38-P), and tau hyperphosphorylation in neurites surrounding βA plaques in APP Tg2576 mice. Neuropathol. Appl Neurobiol 2004; 30: 491-502.
    • (2004) Neuropathol. Appl Neurobiol , vol.30 , pp. 491-502
    • Puig, B.1    Gómez-Isla, T.2    Ribé, E.3    Cuadrado, M.4    Torrejón-Escribano, B.5    Dalfó, E.6
  • 103
    • 29844456397 scopus 로고    scopus 로고
    • Study of the localization of iron, ferritin, and hemosiderin in Alzheimer's disease hippocampus by analytical microscopy at the subcellular level
    • Quintana C, Bellefgih S, Laval JY, Guerkin-Kern JL, Wu TD, Avila J, et al. Study of the localization of iron, ferritin, and hemosiderin in Alzheimer's disease hippocampus by analytical microscopy at the subcellular level. J Struct Biol 2006; 153: 42-54.
    • (2006) J Struct Biol , vol.153 , pp. 42-54
    • Quintana, C.1    Bellefgih, S.2    Laval, J.Y.3    Guerkin-Kern, J.L.4    Wu, T.D.5    Avila, J.6
  • 104
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: Differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and p38, and glycogen synthase kinase-3b
    • Reynolds CH, Betts JC, Blackstock WP, Nebreda AR, Anderton BH. Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and p38, and glycogen synthase kinase-3b. J Neurochem 2000; 74: 1587-95.
    • (2000) J Neurochem , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3    Nebreda, A.R.4    Anderton, B.H.5
  • 106
    • 0030943263 scopus 로고    scopus 로고
    • Stress-activated protein kinase/c-Jun N-terminal kinase phosphorylates tau protein
    • Reynolds CH, Utton MA, Gibb GM, Yates A, Anderton BH. Stress-activated protein kinase/c-Jun N-terminal kinase phosphorylates tau protein. J Neurochem 1997b; 68: 1736-44.
    • (1997) J Neurochem , vol.68 , pp. 1736-1744
    • Reynolds, C.H.1    Utton, M.A.2    Gibb, G.M.3    Yates, A.4    Anderton, B.H.5
  • 107
    • 21244472711 scopus 로고    scopus 로고
    • Late-onset frontotemporal dementia associated with progressive supranuclear palsy/argyrophilic grain disease/Alzheimer's disease pathology
    • Rippon GA, Boeve BF, Parisi JE, Dickson DW, Ivnik RI, Jack CR, et al. Late-onset frontotemporal dementia associated with progressive supranuclear palsy/argyrophilic grain disease/Alzheimer's disease pathology. Neurocase 2005; 11: 204-11.
    • (2005) Neurocase , vol.11 , pp. 204-211
    • Rippon, G.A.1    Boeve, B.F.2    Parisi, J.E.3    Dickson, D.W.4    Ivnik, R.I.5    Jack, C.R.6
  • 110
    • 33646091514 scopus 로고    scopus 로고
    • Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing
    • Santpere G, Puig B, Ferrer I. Low molecular weight species of tau in Alzheimer's disease are dependent on tau phosphorylation sites but not on delayed post-mortem delay in tissue processing. Neurosci Lett 2006; 399: 106-10.
    • (2006) Neurosci Lett , vol.399 , pp. 106-110
    • Santpere, G.1    Puig, B.2    Ferrer, I.3
  • 111
    • 0018193920 scopus 로고
    • Dendritic sprouting in Alzheimer's senile dementia
    • Scheibel AB, Tomiyasu U. Dendritic sprouting in Alzheimer's senile dementia. Expl Neurol 1978; 60: 1-8.
    • (1978) Expl Neurol , vol.60 , pp. 1-8
    • Scheibel, A.B.1    Tomiyasu, U.2
  • 112
    • 0034695098 scopus 로고    scopus 로고
    • The biology of the receptor for advanced glycation end products and its ligands
    • Schmidt AM, Yan SD, Yan SF, Stern DM. The biology of the receptor for advanced glycation end products and its ligands. Biochim Biophys Acta 2000; 1498: 99-111.
    • (2000) Biochim Biophys Acta , vol.1498 , pp. 99-111
    • Schmidt, A.M.1    Yan, S.D.2    Yan, S.F.3    Stern, D.M.4
  • 113
    • 0031739937 scopus 로고    scopus 로고
    • Cytoskeletal alterations in the human tuberal hypothalamus related to argyrophilic grain disease
    • Schultz C, Koppers D, Sassin I, Braak E, Braak H. Cytoskeletal alterations in the human tuberal hypothalamus related to argyrophilic grain disease. Acta Neuropathol 1998; 96: 596-602.
    • (1998) Acta Neuropathol , vol.96 , pp. 596-602
    • Schultz, C.1    Koppers, D.2    Sassin, I.3    Braak, E.4    Braak, H.5
  • 114
    • 33947248608 scopus 로고    scopus 로고
    • The ubiquitin-binding protein p62 identifies argyrophylic grain pathology with greater sensitivity than conventional silver stains
    • Scott IS, Lowe JS. The ubiquitin-binding protein p62 identifies argyrophylic grain pathology with greater sensitivity than conventional silver stains. Acta Neuropathol 2007; 113: 417-20.
    • (2007) Acta Neuropathol , vol.113 , pp. 417-420
    • Scott, I.S.1    Lowe, J.S.2
  • 115
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener ML, Babu JR, Geetha T, Wong HC, Krishna NR, Wooten MW. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol 2004; 24: 8055-68.
    • (2004) Mol Cell Biol , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 116
    • 0034283167 scopus 로고    scopus 로고
    • Parkinson's disease associated with argyrophilic grains clinically resembling progressive supranuclear palsy: An autopsy case
    • Seno H, Kobayashi S, Inagaki T, Yamamori C, Miyaoka T, Horiguchi J, et al. Parkinson's disease associated with argyrophilic grains clinically resembling progressive supranuclear palsy: an autopsy case. J Neurol Sci 2000; 178: 70-4.
    • (2000) J Neurol Sci , vol.178 , pp. 70-74
    • Seno, H.1    Kobayashi, S.2    Inagaki, T.3    Yamamori, C.4    Miyaoka, T.5    Horiguchi, J.6
  • 117
    • 33846618592 scopus 로고    scopus 로고
    • Association of αB-crystallin, a small heat shock protein, with actin: Role in modulating actin filament dynamics in vivo
    • Singh BN, Rao KS, Ramakrishna T, Rangaraj N, Rao ChM. Association of αB-crystallin, a small heat shock protein, with actin: role in modulating actin filament dynamics in vivo. J Mol Biol 2007; 366: 756-67.
    • (2007) J Mol Biol , vol.366 , pp. 756-767
    • Singh, B.N.1    Rao, K.S.2    Ramakrishna, T.3    Rangaraj, N.4    Rao, C.M.5
  • 118
    • 2942594301 scopus 로고    scopus 로고
    • Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423
    • Skrabana R, Kontsek P, Mederlyova A, Iqbal K, Novak M. Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423. FEBS Lett 2004; 568: 178-82.
    • (2004) FEBS Lett , vol.568 , pp. 178-182
    • Skrabana, R.1    Kontsek, P.2    Mederlyova, A.3    Iqbal, K.4    Novak, M.5
  • 119
    • 0032923260 scopus 로고    scopus 로고
    • Microtubule-associated protein tau, heparin sulphate and synuclein in several neurodegenerative diseases with dementia
    • Spillantini MG, Tolnay M, Love S, Goedert M. Microtubule-associated protein tau, heparin sulphate and synuclein in several neurodegenerative diseases with dementia. Acta Neuropathol 1999; 97: 585-94.
    • (1999) Acta Neuropathol , vol.97 , pp. 585-594
    • Spillantini, M.G.1    Tolnay, M.2    Love, S.3    Goedert, M.4
  • 120
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD
    • Sultana R, Boyd-Kimball D, Poon HF, Cai J, Pierce WM, Klein JB, et al. Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: an approach to understand pathological and biochemical alterations in AD. Neurobiol Aging 2006a; 27: 1564-76.
    • (2006) Neurobiol Aging , vol.27 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4    Pierce, W.M.5    Klein, J.B.6
  • 121
    • 33947644871 scopus 로고    scopus 로고
    • Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: Insights into mechanisms of neurodegeneration from redox proteomics
    • Sultana R, Perluigi M, Butterfield DA. Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer's disease: insights into mechanisms of neurodegeneration from redox proteomics. Antioxid Redox Signal 2006b; 8: 2021-37.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 2021-2037
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 122
    • 33645089917 scopus 로고    scopus 로고
    • Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach
    • Sultana R, Poon HF, Cai J, Pierce WM, Merchant M, Klein JB, et al. Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach. Neurobiol Dis 2006c; 22: 76-87.
    • (2006) Neurobiol Dis , vol.22 , pp. 76-87
    • Sultana, R.1    Poon, H.F.2    Cai, J.3    Pierce, W.M.4    Merchant, M.5    Klein, J.B.6
  • 123
    • 20044395488 scopus 로고    scopus 로고
    • The impact or agyrophilic grain disease on the development of dementia and its relationship to concurrent Alzheimer's disease-related pathology
    • Thal DR, Schultz C, Botez G, Del Tedici K, Mrak RE, Griffin WST, et al. The impact or agyrophilic grain disease on the development of dementia and its relationship to concurrent Alzheimer's disease-related pathology. Neuropathol Appl Neurobiol 2005; 31: 270-9.
    • (2005) Neuropathol Appl Neurobiol , vol.31 , pp. 270-279
    • Thal, D.R.1    Schultz, C.2    Botez, G.3    Del Tedici, K.4    Mrak, R.E.5    Griffin, W.S.T.6
  • 124
    • 0036132868 scopus 로고    scopus 로고
    • Argyrophilic grain disease: Neuropathology, frequency in a dementia brain bank and lack of relationship with apolipoprotein E
    • Togo T, Cookson N, Dickson D. Argyrophilic grain disease: neuropathology, frequency in a dementia brain bank and lack of relationship with apolipoprotein E. Brain Pathol 2002; 12: 45-52.
    • (2002) Brain Pathol , vol.12 , pp. 45-52
    • Togo, T.1    Cookson, N.2    Dickson, D.3
  • 125
    • 0036944428 scopus 로고    scopus 로고
    • Ballooned neurons in progressive supranuclear palsy are usually due to concurrent argyrophilic grain disease
    • Togo T, Dickson DW. Ballooned neurons in progressive supranuclear palsy are usually due to concurrent argyrophilic grain disease. Acta Neuropathol 2002; 104: 53-6.
    • (2002) Acta Neuropathol , vol.104 , pp. 53-56
    • Togo, T.1    Dickson, D.W.2
  • 126
    • 33645749941 scopus 로고    scopus 로고
    • Clinical features of argyrophilic grain disease. A retrospective survey of cases with neuropsychiatric symptoms
    • Togo T, Isojima D, Akatsu H, Suzuki K, Uchikado H, Katsuse O, et al. Clinical features of argyrophilic grain disease. A retrospective survey of cases with neuropsychiatric symptoms. Am J Geriatr Psychiatry 2005; 13: 1083-91.
    • (2005) Am J Geriatr Psychiatry , vol.13 , pp. 1083-1091
    • Togo, T.1    Isojima, D.2    Akatsu, H.3    Suzuki, K.4    Uchikado, H.5    Katsuse, O.6
  • 128
    • 0032587612 scopus 로고    scopus 로고
    • Low amyloid (Aβ) plaque load and relative predominance of diffuse plaques distinguish argyrophilic grain disease from Alzheimer's disease
    • Tolnay M, Calhoum M, Pham HC, Egensperger R, Probst A. Low amyloid (Aβ) plaque load and relative predominance of diffuse plaques distinguish argyrophilic grain disease from Alzheimer's disease. Neuropathol Appl Neurobiol 1999; 25: 295-305.
    • (1999) Neuropathol Appl Neurobiol , vol.25 , pp. 295-305
    • Tolnay, M.1    Calhoum, M.2    Pham, H.C.3    Egensperger, R.4    Probst, A.5
  • 129
    • 10844254688 scopus 로고    scopus 로고
    • Argyrophilic grain disease: A late-onset dementia with distinctive features among tauopathies
    • Tolnay M, Clavaguera F. Argyrophilic grain disease: a late-onset dementia with distinctive features among tauopathies. Neuropathology 2004; 24: 269-83.
    • (2004) Neuropathology , vol.24 , pp. 269-283
    • Tolnay, M.1    Clavaguera, F.2
  • 131
    • 0031881676 scopus 로고    scopus 로고
    • Argyrophilic grains of braak: Occurrence in dendrites of neurons containing phosphorylated tau protein
    • Tolnay M, Mistl C, Ipsen S, Probst A. Argyrophilic grains of braak: occurrence in dendrites of neurons containing phosphorylated tau protein. Neuropathol Appl Neurobiol 1998; 24: 53-9.
    • (1998) Neuropathol Appl Neurobiol , vol.24 , pp. 53-59
    • Tolnay, M.1    Mistl, C.2    Ipsen, S.3    Probst, A.4
  • 132
    • 0034988489 scopus 로고    scopus 로고
    • Argyrophilic grain disease. A frequent dementing disorder in aged patients
    • Tolnay M, Monsch AU, Probst A. Argyrophilic grain disease. A frequent dementing disorder in aged patients. Adv Exp Med Biol 2001; 487: 39-58.
    • (2001) Adv Exp Med Biol , vol.487 , pp. 39-58
    • Tolnay, M.1    Monsch, A.U.2    Probst, A.3
  • 133
    • 0032502593 scopus 로고    scopus 로고
    • Ballooned neurons expressing αB-crystallin as a constant feature of the amygdala in argyrophilic grain disease
    • Tolnay M, Probst A. Ballooned neurons expressing αB-crystallin as a constant feature of the amygdala in argyrophilic grain disease. Neurosci Lett 1998; 246: 165-8.
    • (1998) Neurosci Lett , vol.246 , pp. 165-168
    • Tolnay, M.1    Probst, A.2
  • 134
    • 0033142961 scopus 로고    scopus 로고
    • Review: Tau protein pathology in Alzheimer's disease and related disorders
    • Tolnay M, Probst A. Review: tau protein pathology in Alzheimer's disease and related disorders. Neuropathol Appl Neurobiol 1999; 25: 171-87.
    • (1999) Neuropathol Appl Neurobiol , vol.25 , pp. 171-187
    • Tolnay, M.1    Probst, A.2
  • 136
    • 0036938326 scopus 로고    scopus 로고
    • Argyrophilic grain disease and Alzheimer disease are distinguished by their different distribution of tau protein isoforms
    • Tolnay M, Sergeant N, Ghestem A, Chalbot S, de Vos RA, Jansen Steur EN, et al. Argyrophilic grain disease and Alzheimer disease are distinguished by their different distribution of tau protein isoforms. Acta Neuropathol 2002; 104: 425-34.
    • (2002) Acta Neuropathol , vol.104 , pp. 425-434
    • Tolnay, M.1    Sergeant, N.2    Ghestem, A.3    Chalbot, S.4    de Vos, R.A.5    Jansen Steur, E.N.6
  • 137
    • 0030895340 scopus 로고    scopus 로고
    • Argyrophilic grain disease: Widespread hyperphosphorylation of tau protein in limbic neurons
    • Tolnay M, Spillantini MG, Goedert M, Ulrich J, Langui D, Probst A. Argyrophilic grain disease: widespread hyperphosphorylation of tau protein in limbic neurons. Acta Neuropathol 1997a; 93: 477-84.
    • (1997) Acta Neuropathol , vol.93 , pp. 477-484
    • Tolnay, M.1    Spillantini, M.G.2    Goedert, M.3    Ulrich, J.4    Langui, D.5    Probst, A.6
  • 139
    • 0034883274 scopus 로고    scopus 로고
    • Argyrophilic grain disease mimicking temporal Pick's disease: A clinical, radiological, and pathological study of an autopsy case with a clinical course of 15 years
    • Tsuchiya K, Mitani K, Arai T, Yamada S, Komiya T, Esaki Y, et al. Argyrophilic grain disease mimicking temporal Pick's disease: a clinical, radiological, and pathological study of an autopsy case with a clinical course of 15 years. Acta Neuropathol 2001; 102: 195-9.
    • (2001) Acta Neuropathol , vol.102 , pp. 195-199
    • Tsuchiya, K.1    Mitani, K.2    Arai, T.3    Yamada, S.4    Komiya, T.5    Esaki, Y.6
  • 140
    • 34247610312 scopus 로고    scopus 로고
    • Silver diagnosis in neuropathology: Principles, practice and revised interpretation
    • Uchihara T. Silver diagnosis in neuropathology: principles, practice and revised interpretation. Acta Neuropathol 2007; 113: 483-99.
    • (2007) Acta Neuropathol , vol.113 , pp. 483-499
    • Uchihara, T.1
  • 141
    • 0029809134 scopus 로고    scopus 로고
    • p62, a phosphotyrosine- independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
    • Vadlamudi RK, Joung I, Strominger JL, Shin J. p62, a phosphotyrosine- independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. J Biol Chem 1996; 271: 20235-7.
    • (1996) J Biol Chem , vol.271 , pp. 20235-20237
    • Vadlamudi, R.K.1    Joung, I.2    Strominger, J.L.3    Shin, J.4
  • 143
    • 34249713085 scopus 로고    scopus 로고
    • Dose-dependent inhibition of the proteasome activity by a mutant ubiquitin associated with neurodegenerative disease
    • van Tijn P, de Vrij FM, Schuurman KG, Dantuma NP, Fischer DF, van Leeuwen FW, et al. Dose-dependent inhibition of the proteasome activity by a mutant ubiquitin associated with neurodegenerative disease. J Cell Sci 2007; 120: 1615-23.
    • (2007) J Cell Sci , vol.120 , pp. 1615-1623
    • van Tijn, P.1    de Vrij, F.M.2    Schuurman, K.G.3    Dantuma, N.P.4    Fischer, D.F.5    van Leeuwen, F.W.6
  • 144
    • 0032867676 scopus 로고    scopus 로고
    • The 26 S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W. The 26 S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68: 1015-68.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 145
    • 0025609024 scopus 로고
    • Oligodendroglial microtubular masses: An abnormality observed in some human neurodegenerative diseases
    • Yamada T, McGeer PL. Oligodendroglial microtubular masses: an abnormality observed in some human neurodegenerative diseases. Neurosci Lett 1990; 120: 163-6.
    • (1990) Neurosci Lett , vol.120 , pp. 163-166
    • Yamada, T.1    McGeer, P.L.2
  • 146
    • 0026514826 scopus 로고
    • Some immunohistochemical features of argyrophilic grain dementia with normal cortical choline acetyltransferase but extensive subcortical pathology and markedly reduced dopamine
    • Yamada T, McGeer PL, McGeer EG. Some immunohistochemical features of argyrophilic grain dementia with normal cortical choline acetyltransferase but extensive subcortical pathology and markedly reduced dopamine. J Geriatr Psychiatry Neurol 1992; 5: 3-13.
    • (1992) J Geriatr Psychiatry Neurol , vol.5 , pp. 3-13
    • Yamada, T.1    McGeer, P.L.2    McGeer, E.G.3
  • 149
    • 0142139355 scopus 로고    scopus 로고
    • Oxidative stress and neuronal adaptation in Alzheimer disease: The role of SAPK pathways
    • Zhu X, Raina AK, Lee HG, Chao M, Nunomura A, Tabaton M, et al. Oxidative stress and neuronal adaptation in Alzheimer disease: the role of SAPK pathways. Antioxid Redox Signal 2003; 5: 571-6.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 571-576
    • Zhu, X.1    Raina, A.K.2    Lee, H.G.3    Chao, M.4    Nunomura, A.5    Tabaton, M.6
  • 150
    • 0035142804 scopus 로고    scopus 로고
    • Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease
    • Zhu X, Raina AK, Rottkamp CA, Aliev G, Perry G, Boux H, et al. Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease. J Neurochem 2001; 76: 435-41.
    • (2001) J Neurochem , vol.76 , pp. 435-441
    • Zhu, X.1    Raina, A.K.2    Rottkamp, C.A.3    Aliev, G.4    Perry, G.5    Boux, H.6
  • 151
    • 0033782845 scopus 로고    scopus 로고
    • Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cyclerelated events in Alzheimer disease
    • Zhu X, Rottkamp CA, Boux H, Takeda A, Perry G, Smith MA. Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cyclerelated events in Alzheimer disease. J Neuropathol Exp Neurol 2000; 59: 880-8.
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 880-888
    • Zhu, X.1    Rottkamp, C.A.2    Boux, H.3    Takeda, A.4    Perry, G.5    Smith, M.A.6
  • 152
    • 0036790527 scopus 로고    scopus 로고
    • Biochemical analysis of tau proteins in argyrophilic grain disease, Alzheimer's disease, and Pick's disease. A comparative study
    • Zhukareva V, Shah K, Uryu K, Braak H, Del Tredici K, Sundarraj S, et al. Biochemical analysis of tau proteins in argyrophilic grain disease, Alzheimer's disease, and Pick's disease. A comparative study. Am J Pathol 2002; 161: 1135-41.
    • (2002) Am J Pathol , vol.161 , pp. 1135-1141
    • Zhukareva, V.1    Shah, K.2    Uryu, K.3    Braak, H.4    Del Tredici, K.5    Sundarraj, S.6
  • 153
    • 33745152289 scopus 로고    scopus 로고
    • Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo
    • 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.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.