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Volumn 152, Issue 6, 1998, Pages 1531-1539

Ferritin is associated with the aberrant tau filaments present in progressive supranuclear palsy

Author keywords

[No Author keywords available]

Indexed keywords

FERRITIN; IRON; TAU PROTEIN;

EID: 0343336439     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (96)

References (66)
  • 2
    • 0015978141 scopus 로고
    • Neurofibrillary tangles in progressive supranuclear palsy: Electron microscopic observations
    • Powell HC, London GW, Lampert PW: Neurofibrillary tangles in progressive supranuclear palsy: electron microscopic observations. J Neuropathol Exp Neurol 1974, 33:98-106
    • (1974) J Neuropathol Exp Neurol , vol.33 , pp. 98-106
    • Powell, H.C.1    London, G.W.2    Lampert, P.W.3
  • 3
    • 0020687196 scopus 로고
    • Unusual paired helical filaments in progressive supranuclear palsy
    • Takauchi S, Mizuhara T, Miyoshi K: Unusual paired helical filaments in progressive supranuclear palsy. Acta Neuropathol 1983, 59:225-228
    • (1983) Acta Neuropathol , vol.59 , pp. 225-228
    • Takauchi, S.1    Mizuhara, T.2    Miyoshi, K.3
  • 4
    • 0015738782 scopus 로고
    • Ultrastructure of neurofibrillary tangles in Steele-Richardson-Olszewski syndrome
    • Tellez-Nagel I, Wisniewski HM: Ultrastructure of neurofibrillary tangles in Steele-Richardson-Olszewski syndrome. Arch Neurol 1973, 29: 324-327
    • (1973) Arch Neurol , vol.29 , pp. 324-327
    • Tellez-Nagel, I.1    Wisniewski, H.M.2
  • 5
    • 0018968363 scopus 로고
    • Neurofibrillary pathology in progressive supranuclear palsy
    • Ghatak NR, Nochlin D, Hadfield MG: Neurofibrillary pathology in progressive supranuclear palsy. Acta Neuropathol 1980, 52:73-76
    • (1980) Acta Neuropathol , vol.52 , pp. 73-76
    • Ghatak, N.R.1    Nochlin, D.2    Hadfield, M.G.3
  • 6
    • 0016351662 scopus 로고
    • Electron-microscopic study of neurofibrillary tangles in Steele-Richardson-Olszewski syndrome
    • Berl
    • Roy S, Datta CK, Hirano A, Ghatak NR, Zimmermann HM: Electron-microscopic study of neurofibrillary tangles in Steele-Richardson-Olszewski syndrome. Acta Neuropathol (Berl) 1974, 29:175-179
    • (1974) Acta Neuropathol , vol.29 , pp. 175-179
    • Roy, S.1    Datta, C.K.2    Hirano, A.3    Ghatak, N.R.4    Zimmermann, H.M.5
  • 7
    • 0017581518 scopus 로고
    • Ultrastructure of neurofibrillary tangles in progressive supranuclear palsy
    • Berl
    • Tomonaga M: Ultrastructure of neurofibrillary tangles in progressive supranuclear palsy. Acta Neuropathol (Berl) 1977, 37:177-181
    • (1977) Acta Neuropathol , vol.37 , pp. 177-181
    • Tomonaga, M.1
  • 8
    • 0018709737 scopus 로고
    • Ultrastructure of neurofibrillary tangles in progressive supranuclear palsy
    • Berl
    • Yagishita S, Itoh Y, Amano N, Nakano T, Saitoh A: Ultrastructure of neurofibrillary tangles in progressive supranuclear palsy. Acta Neuropathol (Berl) 1979, 48:27-30
    • (1979) Acta Neuropathol , vol.48 , pp. 27-30
    • Yagishita, S.1    Itoh, Y.2    Amano, N.3    Nakano, T.4    Saitoh, A.5
  • 9
    • 0018712289 scopus 로고
    • The fine structure of subcortical neurofibrillary tangles in progressive supranuclear palsy
    • Bugiani O, Mancardi GL, Brusa A, Ederli A: The fine structure of subcortical neurofibrillary tangles in progressive supranuclear palsy. Acta Neuropathol 1979, 45:147-152
    • (1979) Acta Neuropathol , vol.45 , pp. 147-152
    • Bugiani, O.1    Mancardi, G.L.2    Brusa, A.3    Ederli, A.4
  • 10
    • 0017136257 scopus 로고
    • Frequency of Alzheimer's neurofibrillary tangles in the cerebral cortex in progressive supranuclear palsy (subcortical argyrophilic dystrophy)
    • Ishino H, Otsuki S: Frequency of Alzheimer's neurofibrillary tangles in the cerebral cortex in progressive supranuclear palsy (subcortical argyrophilic dystrophy). J Neurol Sci 1976, 28:309-316
    • (1976) J Neurol Sci , vol.28 , pp. 309-316
    • Ishino, H.1    Otsuki, S.2
  • 11
    • 0019244756 scopus 로고
    • Progressive supranuclear palsy: Clinicopathological and biochemical studies
    • Jellinger K, Riederer R, Tomonaga M: Progressive supranuclear palsy: clinicopathological and biochemical studies. J Neural Transm (Suppl) 1980, 16:111-128
    • (1980) J Neural Transm (Suppl) , vol.16 , pp. 111-128
    • Jellinger, K.1    Riederer, R.2    Tomonaga, M.3
  • 12
    • 0020656619 scopus 로고
    • Immunocytochemical comparison of neurofibrillary tangles in senile dementia of Alzheimer type, progressive supranuclear palsy, and postencephalitic Parkinsonism
    • Yen S-H, Horoupian DS, Terry RD: Immunocytochemical comparison of neurofibrillary tangles in senile dementia of Alzheimer type, progressive supranuclear palsy, and postencephalitic Parkinsonism. Ann Neurol 1983, 13:172-175
    • (1983) Ann Neurol , vol.13 , pp. 172-175
    • Yen, S.-H.1    Horoupian, D.S.2    Terry, R.D.3
  • 13
    • 0028884306 scopus 로고
    • Immunohistochemical investigation of tau-positive structures in the cerebral cortex of patients with progressive supranuclear palsy
    • Nishimura T, Ikeda K, Akiyama H, Kondo H, Kato M, Li F, Iseki E, Kosaka K: Immunohistochemical investigation of tau-positive structures in the cerebral cortex of patients with progressive supranuclear palsy. Neurosci Lett 1995, 201:123-126
    • (1995) Neurosci Lett , vol.201 , pp. 123-126
    • Nishimura, T.1    Ikeda, K.2    Akiyama, H.3    Kondo, H.4    Kato, M.5    Li, F.6    Iseki, E.7    Kosaka, K.8
  • 14
    • 0027978991 scopus 로고
    • Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics
    • Iwatsubo T, Hasegawa M, Ihara Y: Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics. Acta Neuropathol 1994, 88:129-136
    • (1994) Acta Neuropathol , vol.88 , pp. 129-136
    • Iwatsubo, T.1    Hasegawa, M.2    Ihara, Y.3
  • 15
    • 0023192282 scopus 로고
    • Neurofibrillary tangles in Alzheimer's disease and progressive supranuclear palsy: Antigenic similarities and differences. Microtubule-associated protein tau antigenicity is prominent in all types of tangles
    • Berl
    • Bancher C, Lassmann H, Budka H, Grundke-Iqbal I, Iqbal K: Neurofibrillary tangles in Alzheimer's disease and progressive supranuclear palsy: antigenic similarities and differences. Microtubule-associated protein tau antigenicity is prominent in all types of tangles. Acta Neuropathol (Berl) 1987, 74:39-46
    • (1987) Acta Neuropathol , vol.74 , pp. 39-46
    • Bancher, C.1    Lassmann, H.2    Budka, H.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 18
    • 0025857173 scopus 로고
    • Abnormal tau proteins in progressive supranuclear palsy: Similarities and differences with the neurofibrillary degeneration of the Alzheimer type
    • Flament S, Delacourte A, Verny M, Hauw J-J, Javoy-Agid F: Abnormal tau proteins in progressive supranuclear palsy: similarities and differences with the neurofibrillary degeneration of the Alzheimer type. Acta Neuropathol 1991, 81:591-596
    • (1991) Acta Neuropathol , vol.81 , pp. 591-596
    • Flament, S.1    Delacourte, A.2    Verny, M.3    Hauw, J.-J.4    Javoy-Agid, F.5
  • 20
    • 0022257253 scopus 로고
    • Mise en evidence immunologique de la proteine tau an niveau des lesions de degenerescence neurofibrillaire de la maladie d'Alzheimer
    • Brion J-P, Passareiro H, Nunez J, Flament-Durand J: Mise en evidence immunologique de la proteine tau an niveau des lesions de degenerescence neurofibrillaire de la maladie d'Alzheimer. Arch Biol 1985, 95:229-235
    • (1985) Arch Biol , vol.95 , pp. 229-235
    • Brion, J.-P.1    Passareiro, H.2    Nunez, J.3    Flament-Durand, J.4
  • 21
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ: Microtubule-associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 1986, 83:4044-4048
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 22
    • 0029114196 scopus 로고
    • Oxidation of cysteine 322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • Scheweers O, Mandelkow EM, Biernat J, Mandelkow E: Oxidation of cysteine 322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc Natl Acad Sci USA 1995, 92:8463-8467
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8463-8467
    • Scheweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 23
    • 0023687214 scopus 로고
    • A modified form of microtubule-associated tau protein is the main component of paired helical filaments
    • Nieto A, Correas I, Montejo de Garcini E, Avila J: A modified form of microtubule-associated tau protein is the main component of paired helical filaments. Biochem Biophys Res Commun 1988, 154:660-667
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 660-667
    • Nieto, A.1    Correas, I.2    Montejo De Garcini, E.3    Avila, J.4
  • 25
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau
    • Wood JG, Mirra SS, Pollock NJ, Binder LI: Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau. Proc Natl Acad Sci USA 1986, 83:4040-4043
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4040-4043
    • Wood, J.G.1    Mirra, S.S.2    Pollock, N.J.3    Binder, L.I.4
  • 28
    • 0030000867 scopus 로고    scopus 로고
    • Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles
    • Spillantini MG, Crowther RA, Goedert M: Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles. Acta Neuropathol 1996, 92:42-48
    • (1996) Acta Neuropathol , vol.92 , pp. 42-48
    • Spillantini, M.G.1    Crowther, R.A.2    Goedert, M.3
  • 29
    • 0023690545 scopus 로고
    • Tau factor polymers are similar to paired helical filaments of Alzheimer's disease
    • Montejo de Garcini E, Carrascosa JL, Correas I, Nieto A, Avila J: Tau factor polymers are similar to paired helical filaments of Alzheimer's disease. FEBS Lett 1988, 236:150-154
    • (1988) FEBS Lett , vol.236 , pp. 150-154
    • Montejo De Garcini, E.1    Carrascosa, J.L.2    Correas, I.3    Nieto, A.4    Avila, J.5
  • 31
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille H, Drewes G, Biernat J, Mandelkow E-M, Mandelkow E: Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 1992, 188:573-584
    • (1992) J Cell Biol , vol.188 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 33
    • 0025852163 scopus 로고
    • Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self association
    • Ksiezak-Reding H, Yen SH: Structural stability of paired helical filaments requires microtubule-binding domains of tau: a model for self association. Neuron 1991, 6:717-728
    • (1991) Neuron , vol.6 , pp. 717-728
    • Ksiezak-Reding, H.1    Yen, S.H.2
  • 34
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: The minimal sequence required for tau-tau interaction
    • Pérez M, Valpuesta M, Medina M, Montejo de Garcini E, Avila J: Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction. J Neurochem 1996, 67:1183-1190
    • (1996) J Neurochem , vol.67 , pp. 1183-1190
    • Pérez, M.1    Valpuesta, M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 35
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA: Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 1996, 383:550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 36
    • 1842415999 scopus 로고    scopus 로고
    • Role of glycosaminoglycans in determining the helicity of paired helical filaments
    • Arrasate M, Pérez M, Valpuesta JM, Avila J: Role of glycosaminoglycans in determining the helicity of paired helical filaments. Am J Pathol 1997, 151:1115-1122
    • (1997) Am J Pathol , vol.151 , pp. 1115-1122
    • Arrasate, M.1    Pérez, M.2    Valpuesta, J.M.3    Avila, J.4
  • 37
    • 0000173965 scopus 로고
    • Ultrastructure of ferritin and apoferritin: A review
    • Massover WH: Ultrastructure of ferritin and apoferritin: a review. Micron 1993, 24:389-437
    • (1993) Micron , vol.24 , pp. 389-437
    • Massover, W.H.1
  • 38
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg SC, Davies P: A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci USA 1990, 87:5827-5831
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5827-5831
    • Greenberg, S.C.1    Davies, P.2
  • 39
    • 0023864279 scopus 로고
    • The glucose oxidase-DAB-nickel method in peroxidase histochemistry of the nervous system
    • Shu S, Ju G, Fand L: The glucose oxidase-DAB-nickel method in peroxidase histochemistry of the nervous system. Neurosci Lett 1988, 85:169-171
    • (1988) Neurosci Lett , vol.85 , pp. 169-171
    • Shu, S.1    Ju, G.2    Fand, L.3
  • 40
    • 0028065142 scopus 로고
    • Analysis of microtubule associated protein tau glycation in paired helical filaments
    • Ledesma MD, Bonay P, Colaço C, Avila J: Analysis of microtubule associated protein tau glycation in paired helical filaments. J Biol Chem 1994, 269:21614-21619
    • (1994) J Biol Chem , vol.269 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaço, C.3    Avila, J.4
  • 41
    • 0001017366 scopus 로고    scopus 로고
    • Evaluation of the analytical and imaging performances of a non-dedicated TEM equipped with a parallel electron energy loss spectrometer (PEELS) and image filter (IF)
    • Quintana C, Marco S, Carrascosa JL: Evaluation of the analytical and imaging performances of a non-dedicated TEM equipped with a parallel electron energy loss spectrometer (PEELS) and image filter (IF). J Trace Microprobe Technol 1997, 15(2):175-188
    • (1997) J Trace Microprobe Technol , vol.15 , Issue.2 , pp. 175-188
    • Quintana, C.1    Marco, S.2    Carrascosa, J.L.3
  • 42
    • 0029018840 scopus 로고
    • The role of tau phosphorylation in transfected COS-1 cells
    • Medina M, Montejo de Garcini E, Avila J: The role of tau phosphorylation in transfected COS-1 cells. Mol Cell Biochem 1995, 148:79-88
    • (1995) Mol Cell Biochem , vol.148 , pp. 79-88
    • Medina, M.1    Montejo De Garcini, E.2    Avila, J.3
  • 43
    • 0029161619 scopus 로고
    • Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine 262 in the presence of the heparin (or tubulin)
    • Moreno FJ, Medina M, Pérez M, Montejo de Garcini E, Avila J: Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine 262 in the presence of the heparin (or tubulin). FEBS Lett 1995, 372:65-68
    • (1995) FEBS Lett , vol.372 , pp. 65-68
    • Moreno, F.J.1    Medina, M.2    Pérez, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 44
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule associated protein tau: Sequence and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA: Multiple isoforms of human microtubule associated protein tau: sequence and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989, 3:519-526
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 45
    • 0027414336 scopus 로고
    • Differences in microtubule binding and self association abilities of bovine brain tau isoforms
    • Garcia de Ancos J, Correas I, Avila J: Differences in microtubule binding and self association abilities of bovine brain tau isoforms. J Biol Chem 1993, 268:7976-7982
    • (1993) J Biol Chem , vol.268 , pp. 7976-7982
    • Garcia De Ancos, J.1    Correas, I.2    Avila, J.3
  • 46
    • 0026712151 scopus 로고
    • Alzheimer neurofibrillary tangles contain 2.1 nm filaments structurally identical to the microtubule associated protein tau: A high-resolution transmission electron microscope study of tangles and senile plaque core amyloid
    • Ruben GC, Iqbal K, Wisniewski H, Johnson J, Grundke-Iqbal: Alzheimer neurofibrillary tangles contain 2.1 nm filaments structurally identical to the microtubule associated protein tau: a high-resolution transmission electron microscope study of tangles and senile plaque core amyloid. Brain Res 1992, 590:164-179
    • (1992) Brain Res , vol.590 , pp. 164-179
    • Ruben, G.C.1    Iqbal, K.2    Wisniewski, H.3    Johnson, J.4    Grundke-Iqbal5
  • 49
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence of β structure
    • Schweers O, Schornbrunn-Hanebeck E, Marx A, Mandelkow E: Structural studies of tau protein and Alzheimer paired helical filaments show no evidence of β structure. J Biol Chem 1994, 269:24290-24297
    • (1994) J Biol Chem , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schornbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 50
    • 0024094998 scopus 로고
    • Tau proteins: The molecular structure and mode of binding on microtubules
    • Hirokawa N, Shinomura Y, Okaba S: Tau proteins: the molecular structure and mode of binding on microtubules. J Cell Biol 1988, 107:1449-1459
    • (1988) J Cell Biol , vol.107 , pp. 1449-1459
    • Hirokawa, N.1    Shinomura, Y.2    Okaba, S.3
  • 52
    • 0021344498 scopus 로고
    • Alzheimer paired helical filaments: Bulk isolation, solubility and protein composition
    • Iqbal K, Zaidi CH, Thompson PA, Merz PA, Wisniewski HM: Alzheimer paired helical filaments: bulk isolation, solubility and protein composition. Acta Neuropathol 1984, 62:167-177
    • (1984) Acta Neuropathol , vol.62 , pp. 167-177
    • Iqbal, K.1    Zaidi, C.H.2    Thompson, P.A.3    Merz, P.A.4    Wisniewski, H.M.5
  • 54
    • 0025821265 scopus 로고
    • Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease an other neurodegenerative diseases affecting the basal ganglia
    • Dexter DT, Carayon A, Javoy-Agid F, Agid Y, Wells FR, Daniel SE, Lees AJ, Jenner P, Marsden CD: Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease an other neurodegenerative diseases affecting the basal ganglia. Brain 1991, 114: 1953-1975
    • (1991) Brain , vol.114 , pp. 1953-1975
    • Dexter, D.T.1    Carayon, A.2    Javoy-Agid, F.3    Agid, Y.4    Wells, F.R.5    Daniel, S.E.6    Lees, A.J.7    Jenner, P.8    Marsden, C.D.9
  • 55
    • 0030957951 scopus 로고    scopus 로고
    • Regional distribution of iron, transferrin, ferritin, and oxidatively-modified proteins in young and aged Fisher 344 rat brains
    • Focht JS, Snyder BS, Beard JC, Van Gelder WV, Williams LR, Connor JR: Regional distribution of iron, transferrin, ferritin, and oxidatively-modified proteins in young and aged Fisher 344 rat brains. Neuroscience 1997, 79:255-261
    • (1997) Neuroscience , vol.79 , pp. 255-261
    • Focht, J.S.1    Snyder, B.S.2    Beard, J.C.3    Van Gelder, W.V.4    Williams, L.R.5    Connor, J.R.6
  • 57
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation and cellular function in animals, plants and microorganisms
    • Theil EC: Ferritin: structure, gene regulation and cellular function in animals, plants and microorganisms. Annu Rev Biochem 1987, 56: 289-315
    • (1987) Annu Rev Biochem , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 59
    • 0025878817 scopus 로고
    • Structural and functional studies of human ferritin H and L chains
    • Edited by Albertini A, Lenfant CL, Mannucci PM, Sixma JJ. Basel, Karger
    • Arosio P, Levi S, Santambrogio P, Cozzi A, Cesareni G, Albertini A: Structural and functional studies of human ferritin H and L chains. Biotechnology of Plasma Proteins. Edited by Albertini A, Lenfant CL, Mannucci PM, Sixma JJ. Basel, Karger 1991, pp 127-131
    • (1991) Biotechnology of Plasma Proteins , pp. 127-131
    • Arosio, P.1    Levi, S.2    Santambrogio, P.3    Cozzi, A.4    Cesareni, G.5    Albertini, A.6
  • 61
    • 0029433282 scopus 로고
    • Free radical damage, iron and Alzheimer's disease
    • Smith MA, Perry G: Free radical damage, iron and Alzheimer's disease. J Neurol Sci 1995, 134:92-94
    • (1995) J Neurol Sci , vol.134 , pp. 92-94
    • Smith, M.A.1    Perry, G.2
  • 64
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER: Protein oxidation and aging. Science 1992, 257:1220-1224
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 66
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith MA, Harris PL, Sayre LM, Perry G: Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc Natl Acad Sci USA 1997, 94:9866-9868
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4


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