메뉴 건너뛰기




Volumn 1, Issue 4-5, 1999, Pages 307-328

Tau protein in normal and Alzheimer's disease brain

Author keywords

Kinases; Oxidative stress; Pathology; Phosphatases; Phosphorylation

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; PROTEIN KINASE; TAU PROTEIN;

EID: 0033302335     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-1999-14-511     Document Type: Review
Times cited : (42)

References (188)
  • 10
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • (1988) Biochem , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 16
    • 0026578425 scopus 로고
    • Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent tau and accumulation of abnormal tau-isoforms (A68 proteins)
    • (1992) Lab Invest , vol.66 , pp. 212-222
    • Bramblett, G.T.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 21
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down'S syndrome neurons in vitro
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 23
    • 0025098891 scopus 로고
    • Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons
    • (1990) Nature , vol.343 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 25
    • 0026659777 scopus 로고
    • Glucose deprivation elicits neurofibrillary tangle-like antigenic changes in hippocampal neurons: Prevention by NGF and bFGF
    • (1992) Exp Neurol , vol.117 , pp. 114-123
    • Cheng, B.1    Mattson, M.P.2
  • 40
    • 0027184294 scopus 로고
    • Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble, Alz-50-reactive polymers of tau
    • (1993) J Neurochem , vol.61 , pp. 1159-1162
    • Dudek, S.M.1    Johnson, G.V.2
  • 47
    • 0022203159 scopus 로고
    • Transglutaminase activity in rat brain: Characterization; Distribution, and changes with age
    • (1985) J Neurochem , vol.45 , pp. 1522-1526
    • Gilad, G.M.1    Varon, L.E.2
  • 50
    • 0026784416 scopus 로고
    • p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease
    • [published erratum appears in FEBS Lett Nov 23 3132 (1992) 203]
    • (1992) FEBS Lett , vol.312 , pp. 95-99
    • Goedert, M.1    Cohen, E.S.2    Jakes, R.3    Cohen, P.4
  • 51
    • 0027420369 scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease
    • (1993) Trends Neurosci , vol.16 , pp. 460-465
    • Goedert, M.1
  • 55
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • (1994) J Cell Biol , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 74
    • 0024498630 scopus 로고
    • Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family
    • (1989) Mol Cell Biol , vol.9 , pp. 1389-1396
    • Himmler, A.1
  • 83
    • 0026563915 scopus 로고
    • Differential phosphorylation of tau by cyclic AMP-dependent protein kinase and Ca2+/calmodulin-dependent protein kinase II: Metabolic and functional consequences
    • (1992) J Neurochem , vol.59 , pp. 2056-2062
    • Johnson, G.V.1
  • 85
    • 0029032511 scopus 로고
    • Understanding the hyperphosphorylation of tau in Alzheimer's disease: Importance of examining site-specific phosphorylation in non-disease systems
    • (1995) Neurobiol Aging , vol.16 , pp. 371-374
    • Johnson, G.V.W.1    Greenwood, J.A.2
  • 88
    • 0028838142 scopus 로고
    • Sorting mechanisms of tau and MAP2 in neurons: Suppressed axonal transit of MAP2 and locally regulated microtubule binding
    • (1995) Neuron , vol.14 , pp. 421-432
    • Kanai, Y.1    Hirokawa, N.2
  • 91
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's Disease
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 98
    • 0023626638 scopus 로고
    • Axonal disruption and aberrant localization of tau protein characterize the neuropil pathology of Alzheimer's disease
    • (1987) Ann Neurol , vol.22 , pp. 639-643
    • Kowall, N.W.1    Kosik, K.S.2
  • 109
    • 0026704256 scopus 로고
    • Expression of tau protein in non-neuronal cells: Microtubule binding and stabilization
    • (1992) J Cell Sci , vol.102 , pp. 227-237
    • Lee, G.1    Rook, S.L.2
  • 115
    • 0021171445 scopus 로고
    • The purification of tau protein and the occurrence of two phosphorylation states of tau protein and the occurrence of two phosphorylation states of tau in brain
    • (1984) J Biol Chem , vol.259 , pp. 12241-12245
    • Lindwall, G.1    Cole, R.D.2
  • 140
    • 0027421625 scopus 로고
    • Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tan associated with Alzheimer's paired helical filaments
    • (1993) J Biol Chem , vol.268 , pp. 23512-23518
    • Paudel, H.K.1    Lew, J.2    Ali, Z.3    Wang, J.H.4
  • 141
    • 0027978340 scopus 로고
    • Expression of protein phosphatases (PP-1, PP-2A, PP-2B and PTP-1B) and protein kinases (MAP kinase and P34cdc2) in the hippocampus of patients with Alzheimer disease and normal aged individuals
    • (1994) Brain Res , vol.655 , pp. 70-76
    • Pei, J.J.1    Sersen, E.2    Iqbal, K.3    Grundke-Iqbal, I.4
  • 147
    • 0021997433 scopus 로고
    • Proteolysis of mitochondria in reticulocytes during maturation is ubiqutin-dependent and is accompanied by a high rate of ATP hydrolysis
    • (1985) FEBS Lett , vol.180 , pp. 249
    • Rapoport, S.1    Dubiel, W.2    Muller, M.3
  • 150
    • 0025875671 scopus 로고
    • Natural substrates of the ubiquitin proteolytic pathway
    • (1991) Cell , vol.66 , pp. 615-618
    • Rechsteiner, M.1
  • 165
    • 0029569152 scopus 로고
    • Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: Focusing on phosphatases
    • (1995) FASEB J , vol.9 , pp. 1570-1576
    • Trojanowski, J.Q.1    Lee, V.M.-Y.2
  • 188
    • 0027237861 scopus 로고
    • Tau in paired helical filaments is functionally distinct from fetal tau: Assembly incompetence of paired helical filament-tau
    • (1993) J Neurochem , vol.61 , pp. 1183-1186
    • Yoshida, H.1    Ihara, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.