메뉴 건너뛰기




Volumn 22, Issue 2, 2012, Pages 240-250

Ubiquitin is associated with early truncation of tau protein at aspartic acid 421 during the maturation of neurofibrillary tangles in Alzheimer's disease

Author keywords

Alzheimer's disease; neurofibrillary tangles; phosphorylated tau; proteasome; truncation; ubiquitin

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; PROTEASOME; TAU PROTEIN; UBIQUITIN;

EID: 84857641625     PISSN: 10156305     EISSN: 17503639     Source Type: Journal    
DOI: 10.1111/j.1750-3639.2011.00525.x     Document Type: Article
Times cited : (30)

References (84)
  • 1
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso AC, Grundke-Iqbal I, Iqbal K, (1996) Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 2: 783-787.
    • (1996) Nat Med , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 2
    • 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
    • Alonso AD, Grundke-Iqbal I, Barra HS, Iqbal K, (1997) 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 94: 298-303.
    • (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
  • 4
    • 67449127077 scopus 로고    scopus 로고
    • Proteasome-caspase-cathepsin sequence leading to tau pathology induced by prostaglandin J2 in neuronal cells
    • Arnaud LT, Myeku N, Figueiredo-Pereira ME, (2009) Proteasome-caspase- cathepsin sequence leading to tau pathology induced by prostaglandin J2 in neuronal cells. J Neurochem 110: 328-342.
    • (2009) J Neurochem , vol.110 , pp. 328-342
    • Arnaud, L.T.1    Myeku, N.2    Figueiredo-Pereira, M.E.3
  • 5
    • 0017358355 scopus 로고
    • Neuronal loss, neurofibrillary tangles and granulovacuolar degeneration in the hippocampus with ageing and dementia. A quantitative study
    • Ball MJ, (1977) Neuronal loss, neurofibrillary tangles and granulovacuolar degeneration in the hippocampus with ageing and dementia. A quantitative study. Acta Neuropathol 37: 111-118.
    • (1977) Acta Neuropathol , vol.37 , pp. 111-118
    • Ball, M.J.1
  • 6
    • 0024795714 scopus 로고
    • Tau and ubiquitin immunoreactivity at different stages of formation of Alzheimer neurofibrillary tangles
    • Bancher C, Brunner C, Lassmann H, Budka H, Jellinger K, Seitelberger F, et al, (1989) Tau and ubiquitin immunoreactivity at different stages of formation of Alzheimer neurofibrillary tangles. Prog Clin Biol Res 317: 837-848.
    • (1989) Prog Clin Biol Res , vol.317 , pp. 837-848
    • Bancher, C.1    Brunner, C.2    Lassmann, H.3    Budka, H.4    Jellinger, K.5    Seitelberger, F.6
  • 7
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease
    • Bancher C, Brunner C, Lassmann H, Budka H, Jellinger K, Wiche G, et al, (1989) Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res 477: 90-99.
    • (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
  • 8
    • 1042288284 scopus 로고    scopus 로고
    • Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain
    • Barghorn S, Davies P, Mandelkow E, (2004) Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. Biochemistry 43: 1694-1703.
    • (2004) Biochemistry , vol.43 , pp. 1694-1703
    • Barghorn, S.1    Davies, P.2    Mandelkow, E.3
  • 9
    • 43249129441 scopus 로고    scopus 로고
    • Accumulation of aspartic acid421- and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease
    • Basurto-Islas G, Luna-Munoz J, Guillozet-Bongaarts AL, Binder LI, Mena R, Garcia-Sierra F, (2008) Accumulation of aspartic acid421- and glutamic acid391-cleaved tau in neurofibrillary tangles correlates with progression in Alzheimer disease. J Neuropathol Exp Neurol 67: 470-483.
    • (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
  • 10
    • 2542567240 scopus 로고    scopus 로고
    • Alzheimer's disease: Intraneuronal alterations precede insoluble amyloid-beta formation
    • Braak H, Del Tredici K, (2004) Alzheimer's disease: intraneuronal alterations precede insoluble amyloid-beta formation. Neurobiol Aging 25: 713-718.
    • (2004) Neurobiol Aging , vol.25 , pp. 713-718
    • Braak, H.1    Del Tredici, K.2
  • 11
    • 0025949088 scopus 로고
    • A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities
    • Brion JP, Hanger DP, Couck AM, Anderton BH, (1991) A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities. Biochem J 279 (Pt 3): 831-836.
    • (1991) Biochem J , vol.279 , Issue.PART 3 , pp. 831-836
    • Brion, J.P.1    Hanger, D.P.2    Couck, A.M.3    Anderton, B.H.4
  • 12
    • 15244345543 scopus 로고    scopus 로고
    • Proteasome or calpain inhibition does not alter cellular tau levels in neuroblastoma cells or primary neurons
    • Brown MR, Bondada V, Keller JN, Thorpe J, Geddes JW, (2005) Proteasome or calpain inhibition does not alter cellular tau levels in neuroblastoma cells or primary neurons. J Alzheimers Dis 7: 15-24.
    • (2005) J Alzheimers Dis , vol.7 , pp. 15-24
    • Brown, M.R.1    Bondada, V.2    Keller, J.N.3    Thorpe, J.4    Geddes, J.W.5
  • 14
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel G, Mager EM, Binder LI, Kuret J, (1996) The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J Biol Chem 271: 32789-32795.
    • (1996) J Biol Chem , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 15
    • 0034004683 scopus 로고    scopus 로고
    • Ubiquitin immunochemistry as a diagnostic aid for community pathologists evaluating patients who have dementia
    • Chu CT, Caruso JL, Cummings TJ, Ervin J, Rosenberg C, Hulette CM, (2000) Ubiquitin immunochemistry as a diagnostic aid for community pathologists evaluating patients who have dementia. Mod Pathol 13: 420-426.
    • (2000) Mod Pathol , vol.13 , pp. 420-426
    • Chu, C.T.1    Caruso, J.L.2    Cummings, T.J.3    Ervin, J.4    Rosenberg, C.5    Hulette, C.M.6
  • 17
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland DW, Hwo SY, Kirschner MW, (1977) Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J Mol Biol 116: 227-247.
    • (1977) J Mol Biol , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 19
    • 33744950091 scopus 로고    scopus 로고
    • Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation
    • Cripps D, Thomas SN, Jeng Y, Yang F, Davies P, Yang AJ, (2006) Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation. J Biol Chem 281: 10825-10838.
    • (2006) J Biol Chem , vol.281 , pp. 10825-10838
    • Cripps, D.1    Thomas, S.N.2    Jeng, Y.3    Yang, F.4    Davies, P.5    Yang, A.J.6
  • 20
    • 79953197650 scopus 로고    scopus 로고
    • Polyubiquitin linkage profiles in three models of proteolytic stress suggest the etiology of Alzheimer disease
    • Dammer EB, Na CH, Xu P, Seyfried NT, Duong DM, Cheng D, et al, (2011) Polyubiquitin linkage profiles in three models of proteolytic stress suggest the etiology of Alzheimer disease. J Biol Chem 286: 10457-10465.
    • (2011) J Biol Chem , vol.286 , pp. 10457-10465
    • Dammer, E.B.1    Na, C.H.2    Xu, P.3    Seyfried, N.T.4    Duong, D.M.5    Cheng, D.6
  • 21
    • 9744222883 scopus 로고    scopus 로고
    • Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
    • de Vrij FM, Fischer DF, van Leeuwen FW, Hol EM, (2004) Protein quality control in Alzheimer's disease by the ubiquitin proteasome system. Prog Neurobiol 74: 249-270.
    • (2004) Prog Neurobiol , vol.74 , pp. 249-270
    • De Vrij, F.M.1    Fischer, D.F.2    Van Leeuwen, F.W.3    Hol, E.M.4
  • 23
    • 33745959291 scopus 로고    scopus 로고
    • Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
    • Dickey CA, Yue M, Lin WL, Dickson DW, Dunmore JH, Lee WC, et al, (2006) Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species. J Neurosci 26: 6985-6996.
    • (2006) J Neurosci , vol.26 , pp. 6985-6996
    • Dickey, C.A.1    Yue, M.2    Lin, W.L.3    Dickson, D.W.4    Dunmore, J.H.5    Lee, W.C.6
  • 24
    • 33745827715 scopus 로고    scopus 로고
    • Site-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation
    • Ding H, Matthews TA, Johnson GV, (2006) Site-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation. J Biol Chem 281: 19107-19114.
    • (2006) J Biol Chem , vol.281 , pp. 19107-19114
    • Ding, H.1    Matthews, T.A.2    Johnson, G.V.3
  • 25
    • 34748824095 scopus 로고    scopus 로고
    • Phosphorylation modulates the local conformation and self-aggregation ability of a peptide from the fourth tau microtubule-binding repeat
    • Du JT, Yu CH, Zhou LX, Wu WH, Lei P, Li Y, et al, (2007) Phosphorylation modulates the local conformation and self-aggregation ability of a peptide from the fourth tau microtubule-binding repeat. FEBS J 274: 5012-5020.
    • (2007) FEBS J , vol.274 , pp. 5012-5020
    • Du, J.T.1    Yu, C.H.2    Zhou, L.X.3    Wu, W.H.4    Lei, P.5    Li, Y.6
  • 26
    • 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, (2000) The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis. J Neurochem 75: 624-633.
    • (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
  • 29
    • 0034929144 scopus 로고    scopus 로고
    • Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer's disease
    • Garcia-Sierra F, Wischik CM, Harrington CR, Luna-Munoz J, Mena R, (2001) Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer's disease. J Chem Neuroanat 22: 65-77.
    • (2001) J Chem Neuroanat , vol.22 , pp. 65-77
    • Garcia-Sierra, F.1    Wischik, C.M.2    Harrington, C.R.3    Luna-Munoz, J.4    Mena, R.5
  • 30
    • 0038291981 scopus 로고    scopus 로고
    • Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease
    • Garcia-Sierra F, Ghoshal N, Quinn B, Berry RW, Binder LI, (2003) Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease. J Alzheimers Dis 5: 65-77.
    • (2003) J Alzheimers Dis , vol.5 , pp. 65-77
    • Garcia-Sierra, F.1    Ghoshal, N.2    Quinn, B.3    Berry, R.W.4    Binder, L.I.5
  • 31
    • 49149098756 scopus 로고    scopus 로고
    • Truncation of tau protein and its pathological significance in Alzheimer's disease
    • Garcia-Sierra F, Mondragon-Rodriguez S, Basurto-Islas G, (2008) Truncation of tau protein and its pathological significance in Alzheimer's disease. J Alzheimers Dis 14: 401-409.
    • (2008) J Alzheimers Dis , vol.14 , pp. 401-409
    • Garcia-Sierra, F.1    Mondragon-Rodriguez, S.2    Basurto-Islas, G.3
  • 34
    • 0026683725 scopus 로고
    • The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs
    • Gustke N, Steiner B, Mandelkow EM, Biernat J, Meyer HE, Goedert M, Mandelkow E, (1992) The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs. FEBS Lett 307: 199-205.
    • (1992) FEBS Lett , vol.307 , pp. 199-205
    • Gustke, N.1    Steiner, B.2    Mandelkow, E.M.3    Biernat, J.4    Meyer, H.E.5    Goedert, M.6    Mandelkow, E.7
  • 35
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation
    • Haas AL, Warms JV, Hershko A, Rose IA, (1982) Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J Biol Chem 257: 2543-2548.
    • (1982) J Biol Chem , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3    Rose, I.A.4
  • 36
    • 0025074187 scopus 로고
    • Lipofuscin and ceroid formation: The cellular recycling system
    • Harman D, (1989) Lipofuscin and ceroid formation: the cellular recycling system. Adv Exp Med Biol 266: 3-15.
    • (1989) Adv Exp Med Biol , vol.266 , pp. 3-15
    • Harman, D.1
  • 37
    • 11144283513 scopus 로고    scopus 로고
    • Transcriptional and conformational changes of the tau molecule in Alzheimer's disease
    • Hyman BT, Augustinack JC, Ingelsson M, (2005) Transcriptional and conformational changes of the tau molecule in Alzheimer's disease. Biochim Biophys Acta 1739: 150-157.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 150-157
    • Hyman, B.T.1    Augustinack, J.C.2    Ingelsson, M.3
  • 38
    • 41149156856 scopus 로고    scopus 로고
    • Alzheimer neurofibrillary degeneration: Significance, etiopathogenesis, therapeutics and prevention
    • Iqbal K, Grundke-Iqbal I, (2008) Alzheimer neurofibrillary degeneration: significance, etiopathogenesis, therapeutics and prevention. J Cell Mol Med 12: 38-55.
    • (2008) J Cell Mol Med , vol.12 , pp. 38-55
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 39
    • 0026569062 scopus 로고
    • Lack of ubiquitin immunoreactivities at both ends of neuropil threads. Possible bidirectional growth of neuropil threads
    • Iwatsubo T, Hasegawa M, Esaki Y, Ihara Y, (1992) Lack of ubiquitin immunoreactivities at both ends of neuropil threads. Possible bidirectional growth of neuropil threads. Am J Pathol 140: 277-282.
    • (1992) Am J Pathol , vol.140 , pp. 277-282
    • Iwatsubo, T.1    Hasegawa, M.2    Esaki, Y.3    Ihara, Y.4
  • 40
    • 33747410184 scopus 로고    scopus 로고
    • The history of the paired helical filaments
    • Kidd M, (2006) The history of the paired helical filaments. J Alzheimers Dis 9: 71-75.
    • (2006) J Alzheimers Dis , vol.9 , pp. 71-75
    • Kidd, M.1
  • 41
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ, (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci U S A 83: 4044-4048.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 43
    • 0025254157 scopus 로고
    • Alzheimer disease proteins (A68) share epitopes with tau but show distinct biochemical properties
    • Ksiezak-Reding H, Binder LI, Yen SH, (1990) Alzheimer disease proteins (A68) share epitopes with tau but show distinct biochemical properties. J Neurosci Res 25: 420-430.
    • (1990) J Neurosci Res , vol.25 , pp. 420-430
    • Ksiezak-Reding, H.1    Binder, L.I.2    Yen, S.H.3
  • 44
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee G, Cowan N, Kirschner M, (1988) The primary structure and heterogeneity of tau protein from mouse brain. Science 239: 285-288.
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 45
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal Tau
    • Lee VM, Balin BJ, Otvos L, Jr, Trojanowski JQ, (1991) A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251: 675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos Jr., L.3    Trojanowski, J.Q.4
  • 46
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman NL, (2009) The ubiquitin proteasome system in neuropathology. Acta Neuropathol 118: 329-347.
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 48
    • 24644433910 scopus 로고    scopus 로고
    • Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease
    • Luna-Munoz J, Garcia-Sierra F, Falcon V, Menendez I, Chavez-Macias L, Mena R, (2005) Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease. J Alzheimers Dis 8: 29-41.
    • (2005) J Alzheimers Dis , vol.8 , pp. 29-41
    • Luna-Munoz, J.1    Garcia-Sierra, F.2    Falcon, V.3    Menendez, I.4    Chavez-Macias, L.5    Mena, R.6
  • 49
    • 38049030324 scopus 로고    scopus 로고
    • Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease
    • Luna-Munoz J, Chavez-Macias L, Garcia-Sierra F, Mena R, (2007) Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease. J Alzheimers Dis 12: 365-375.
    • (2007) J Alzheimers Dis , vol.12 , pp. 365-375
    • Luna-Munoz, J.1    Chavez-Macias, L.2    Garcia-Sierra, F.3    Mena, R.4
  • 53
    • 0023793690 scopus 로고
    • Ubiquitin is associated with abnormal cytoplasmic filaments characteristic of neurodegenerative diseases
    • Manetto V, Perry G, Tabaton M, Mulvihill P, Fried VA, Smith HT, et al, (1988) Ubiquitin is associated with abnormal cytoplasmic filaments characteristic of neurodegenerative diseases. Proc Natl Acad Sci U S A 85: 4501-4505.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4501-4505
    • Manetto, V.1    Perry, G.2    Tabaton, M.3    Mulvihill, P.4    Fried, V.A.5    Smith, H.T.6
  • 55
    • 0028798197 scopus 로고
    • Monitoring pathological assembly of tau and beta-amyloid proteins in Alzheimer's disease
    • Mena R, Edwards P, Perez-Olvera O, Wischik CM, (1995) Monitoring pathological assembly of tau and beta-amyloid proteins in Alzheimer's disease. Acta Neuropathol 89: 50-56.
    • (1995) Acta Neuropathol , vol.89 , pp. 50-56
    • Mena, R.1    Edwards, P.2    Perez-Olvera, O.3    Wischik, C.M.4
  • 56
    • 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, (1991) The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 41: 479-486.
    • (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
  • 59
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori H, Kondo J, Ihara Y, (1987) Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science 235: 1641-1644.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 60
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Titani K, Ihara Y, (1993) Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 10: 1151-1160.
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 61
    • 0024814559 scopus 로고
    • Characterisation of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF
    • Novak M, Wischik CM, Edwards P, Pannell R, Milstein C, (1989) Characterisation of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF. Prog Clin Biol Res 317: 755-761.
    • (1989) Prog Clin Biol Res , vol.317 , pp. 755-761
    • Novak, M.1    Wischik, C.M.2    Edwards, P.3    Pannell, R.4    Milstein, C.5
  • 62
    • 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, (1991) 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 88: 5837-5841.
    • (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
  • 63
    • 42349089604 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Alzheimer's disease
    • Oddo S, (2008) The ubiquitin-proteasome system in Alzheimer's disease. J Cell Mol Med 12: 363-373.
    • (2008) J Cell Mol Med , vol.12 , pp. 363-373
    • Oddo, S.1
  • 64
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L, Jr., Feiner L, Lang E, Szendrei GI, Goedert M, Lee VM, (1994) Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J Neurosci Res 39: 669-673.
    • (1994) J Neurosci Res , vol.39 , pp. 669-673
    • Otvos Jr., L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.6
  • 65
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains
    • Perry G, Friedman R, Shaw G, Chau V, (1987) Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains. Proc Natl Acad Sci U S A 84: 3033-3036.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 66
    • 0024560685 scopus 로고
    • Immunochemical properties of ubiquitin conjugates in the paired helical filaments of Alzheimer disease
    • Perry G, Mulvihill P, Fried VA, Smith HT, Grundke-Iqbal I, Iqbal K, (1989) Immunochemical properties of ubiquitin conjugates in the paired helical filaments of Alzheimer disease. J Neurochem 52: 1523-1528.
    • (1989) J Neurochem , vol.52 , pp. 1523-1528
    • Perry, G.1    Mulvihill, P.2    Fried, V.A.3    Smith, H.T.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 67
    • 0026009171 scopus 로고
    • Neuropil threads of Alzheimer's disease show a marked alteration of the normal cytoskeleton
    • Perry G, Kawai M, Tabaton M, Onorato M, Mulvihill P, Richey P, et al, (1991) Neuropil threads of Alzheimer's disease show a marked alteration of the normal cytoskeleton. J Neurosci 11: 1748-1755.
    • (1991) J Neurosci , vol.11 , pp. 1748-1755
    • Perry, G.1    Kawai, M.2    Tabaton, M.3    Onorato, M.4    Mulvihill, P.5    Richey, P.6
  • 69
    • 67650556426 scopus 로고    scopus 로고
    • Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: Implications for the pathogenesis of Alzheimer disease
    • Quintanilla RA, Matthews-Roberson TA, Dolan PJ, Johnson GV, (2009) Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: implications for the pathogenesis of Alzheimer disease. J Biol Chem 284: 18754-18766.
    • (2009) J Biol Chem , vol.284 , pp. 18754-18766
    • Quintanilla, R.A.1    Matthews-Roberson, T.A.2    Dolan, P.J.3    Johnson, G.V.4
  • 71
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: Implications for human pathobiology
    • Schwartz AL, Ciechanover A, (2009) Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu Rev Pharmacol Toxicol 49: 73-96.
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 72
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H, Schwartz D, Gygi SP, Kosik KS, (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J Biol Chem 279: 4869-4876.
    • (2004) J Biol Chem , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 73
    • 67649622427 scopus 로고    scopus 로고
    • Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization
    • Sun Q, Gamblin TC, (2009) Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization. Biochemistry 48: 6002-6011.
    • (2009) Biochemistry , vol.48 , pp. 6002-6011
    • Sun, Q.1    Gamblin, T.C.2
  • 75
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai HC, Schuman EM, (2008) Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat Rev Neurosci 9: 826-838.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 76
    • 0029010034 scopus 로고
    • Relationship between plaques, tangles, and dystrophic processes in Alzheimer's disease
    • discussion 341-335.
    • Trojanowski JQ, Shin RW, Schmidt ML, Lee VM, (1995) Relationship between plaques, tangles, and dystrophic processes in Alzheimer's disease. Neurobiol Aging 16: 335-340. discussion 341-335.
    • (1995) Neurobiol Aging , vol.16 , pp. 335-340
    • Trojanowski, J.Q.1    Shin, R.W.2    Schmidt, M.L.3    Lee, V.M.4
  • 77
    • 38449094180 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in Alzheimer's disease
    • Upadhya SC, Hegde AN, (2007) Role of the ubiquitin proteasome system in Alzheimer's disease. BMC Biochem 8 (Suppl. 1): S12.
    • (2007) BMC Biochem , vol.8 , Issue.1 SUPPL. 1
    • Upadhya, S.C.1    Hegde, A.N.2
  • 78
    • 0025306543 scopus 로고
    • ATP-induced loss of Alz-50 immunoreactivity with the A68 proteins from Alzheimer brain is mediated by ubiquitin
    • Vincent IJ, Davies P, (1990) ATP-induced loss of Alz-50 immunoreactivity with the A68 proteins from Alzheimer brain is mediated by ubiquitin. Proc Natl Acad Sci U S A 87: 4840-4844.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4840-4844
    • Vincent, I.J.1    Davies, P.2
  • 82
    • 0028998417 scopus 로고
    • Quantitative analysis of tau protein in paired helical filament preparations: Implications for the role of tau protein phosphorylation in PHF assembly in Alzheimer's disease
    • Wischik CM, Edwards PC, Lai RY, Gertz HN, Xuereb JH, Paykel ES, et al, (1995) Quantitative analysis of tau protein in paired helical filament preparations: implications for the role of tau protein phosphorylation in PHF assembly in Alzheimer's disease. Neurobiol Aging 16: 409-417.
    • (1995) Neurobiol Aging , vol.16 , pp. 409-417
    • Wischik, C.M.1    Edwards, P.C.2    Lai, R.Y.3    Gertz, H.N.4    Xuereb, J.H.5    Paykel, E.S.6
  • 83
    • 29344434456 scopus 로고    scopus 로고
    • C-terminal truncation modulates both nucleation and extension phases of tau fibrillization
    • Yin H, Kuret J, (2006) C-terminal truncation modulates both nucleation and extension phases of tau fibrillization. FEBS Lett 580: 211-215.
    • (2006) FEBS Lett , vol.580 , pp. 211-215
    • Yin, H.1    Kuret, J.2
  • 84
    • 69349096418 scopus 로고    scopus 로고
    • Hyperphosphorylation of microtubule-associated tau protein plays dual role in neurodegeneration and neuroprotection
    • Zhang Y, Tian Q, Zhang Q, Zhou X, Liu S, Wang JZ, (2009) Hyperphosphorylation of microtubule-associated tau protein plays dual role in neurodegeneration and neuroprotection. Pathophysiology 16: 311-316.
    • (2009) Pathophysiology , vol.16 , pp. 311-316
    • Zhang, Y.1    Tian, Q.2    Zhang, Q.3    Zhou, X.4    Liu, S.5    Wang, J.Z.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.