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Volumn 717, Issue 1-2, 1996, Pages 99-108

Quantitative solubilization and analysis of insoluble paired helical filaments from Alzheimer disease

Author keywords

Alzheimer disease; crosslink; glycation; neurofibrillary pathology; paired helical filament; solubility

Indexed keywords

ADULT; AGED; ALZHEIMER DISEASE; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; ELECTRON MICROSCOPY; HUMAN; HUMAN TISSUE; PAIRED HELICAL FILAMENT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PHOSPHORYLATION; SOLUBILITY;

EID: 0029878826     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-8993(95)01473-X     Document Type: Article
Times cited : (56)

References (67)
  • 1
    • 0020085940 scopus 로고
    • An organic phosphorous assay which avoids the use of hazardous perchloric acid
    • Anderson, R.L. and Davis, S., An organic phosphorous assay which avoids the use of hazardous perchloric acid, Clin. Chim. Acta, 121 (1982) 111-116.
    • (1982) Clin. Chim. Acta , vol.121 , pp. 111-116
    • Anderson, R.L.1    Davis, S.2
  • 2
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder, L.I., Frankfurter, A. and Rebhun, L.I., The distribution of tau in the mammalian central nervous system, J. Cell Biol., 101 (1985) 1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 3
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett, G.T., Goedert, M., Jakes, R., Merrick, S.E., Trojanowski, J.Q. and Lee, V.M., Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding, Neuron, 10 (1993) 1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 5
    • 0028918383 scopus 로고
    • Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein crosslinking in Alzheimer disease
    • Cras, P., Smith, M.A., Richey, P.L., Siedlak, S.L., Mulvihill, P. and Perry, G., Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein crosslinking in Alzheimer disease, Acta Neuropathol., 89 (1995) 291-295.
    • (1995) Acta Neuropathol. , vol.89 , pp. 291-295
    • Cras, P.1    Smith, M.A.2    Richey, P.L.3    Siedlak, S.L.4    Mulvihill, P.5    Perry, G.6
  • 6
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • DuBois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A. and Smith, F., Colorimetric method for determination of sugars and related substances, Anal. Chem., 28 (1956) 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • DuBois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 7
    • 0026730350 scopus 로고
    • Amyloidogenicity of βA4 and βa4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation
    • Dyrks, T., Dyrks, E., Hartmann, T., Masters, C. and Beyreuther, K., Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation, J. Biol. Chem., 267 (1992) 18210-18217.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18210-18217
    • Dyrks, T.1    Dyrks, E.2    Hartmann, T.3    Masters, C.4    Beyreuther, K.5
  • 9
    • 0028830958 scopus 로고
    • Localization of superoxide dismutases in Alzheimer's disease and Down's syndrome neocortex and hippocampus
    • Furuta, A., Price, D.L., Pardo, C.A., Troncoso, J.C., Xu, Z.S, Taniguchi, N. and Martin, L.J., Localization of superoxide dismutases in Alzheimer's disease and Down's syndrome neocortex and hippocampus, Am. J. Pathol., 146 (1995), 357-367.
    • (1995) Am. J. Pathol. , vol.146 , pp. 357-367
    • Furuta, A.1    Price, D.L.2    Pardo, C.A.3    Troncoso, J.C.4    Xu, Z.S.5    Taniguchi, N.6    Martin, L.J.7
  • 12
    • 0027420369 scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease
    • Goedert, M., Tau protein and the neurofibrillary pathology of Alzheimer's disease, Trends Neurosci., 16 (1993) 460-465.
    • (1993) Trends Neurosci. , vol.16 , pp. 460-465
    • Goedert, M.1
  • 14
    • 0026231697 scopus 로고
    • Neurofibrillary tangles and beta-amyloid deposits in Alzheimer's disease
    • Goedert, M., Sisodia, S.S. and Price, D.L., Neurofibrillary tangles and beta-amyloid deposits in Alzheimer's disease, Curr. Opin. Neurobiol, 1 (1991) 441-447.
    • (1991) Curr. Opin. Neurobiol , vol.1 , pp. 441-447
    • Goedert, M.1    Sisodia, S.S.2    Price, D.L.3
  • 15
    • 0026796007 scopus 로고
    • Solubilization and fractionation of paired helical filaments
    • González, P.J., Correas, I. and Avila, J., Solubilization and fractionation of paired helical filaments, Neuroscience, 50 (1992) 491-499.
    • (1992) Neuroscience , vol.50 , pp. 491-499
    • González, P.J.1    Correas, I.2    Avila, J.3
  • 16
    • 0026573467 scopus 로고
    • Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study
    • Good, P.F., Perl, D.P., Bierer, L.M. and Schmeidler, J., Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: a laser microprobe (LAMMA) study, Ann. Neurol., 31 (1992) 286-292.
    • (1992) Ann. Neurol. , vol.31 , pp. 286-292
    • Good, P.F.1    Perl, D.P.2    Bierer, L.M.3    Schmeidler, J.4
  • 17
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct t proteins by polyacrylamide gel electrophoresis
    • Greenberg, S.G. and Davies, P., A preparation of Alzheimer paired helical filaments that displays distinct T proteins by polyacrylamide gel electrophoresis, Proc. Natl. Acad. Sci. USA, 87 (1990) 5827-5831.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 18
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated T PHF proteins display the same biochemical properties as normal tau
    • Greenberg, S.G., Davies, P., Schein, J.D. and Binder, L.I., Hydrofluoric acid-treated T PHF proteins display the same biochemical properties as normal tau, J. Biol. Chem., 267 (1992) 564-569.
    • (1992) J. Biol. Chem. , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 20
    • 0026683725 scopus 로고
    • The Alzheimer-like phosphoryla-tion of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs
    • Gustke, N., Steiner, B., Mandelkovv, E.M., Biernat, J., Meyer. H.E., Goedert, M. and Mandelkow, E., The Alzheimer-like phosphoryla-tion of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs, FEBS Lett. 307 (1992) 199-205.
    • (1992) FEBS Lett. , vol.307 , pp. 199-205
    • Gustke, N.1    Steiner, B.2    Mandelkovv, E.M.3    Biernat, J.4    Meyer, H.E.5    Goedert, M.6    Mandelkow, E.7
  • 22
    • 0023877998 scopus 로고
    • Monosaccharide analysis of glycoconjugates by anion exchange chromatography with pulsed amperometric detection
    • Hardy, M.R., Townsend, R.R. and Lee Y.C., Monosaccharide analysis of glycoconjugates by anion exchange chromatography with pulsed amperometric detection. Anal. Biochem., 170 (1988) 54-62.
    • (1988) Anal. Biochem. , vol.170 , pp. 54-62
    • Hardy, M.R.1    Townsend, R.R.2    Lee, Y.C.3
  • 23
    • 0027155834 scopus 로고
    • Characterization of two distinct monoclonal antibodies to paired helical filaments: Further evidence for fetal-type phosphorylation of the tau in paired helical filaments
    • Hasegawa, M., Watanabe, A., Takio, K., Suzuki, M., Arai, T., Titani, K. and Ihara, Y., Characterization of two distinct monoclonal antibodies to paired helical filaments: further evidence for fetal-type phosphorylation of the tau in paired helical filaments, J. Neurochem., 60 (1993) 2068-2077.
    • (1993) J. Neurochem. , vol.60 , pp. 2068-2077
    • Hasegawa, M.1    Watanabe, A.2    Takio, K.3    Suzuki, M.4    Arai, T.5    Titani, K.6    Ihara, Y.7
  • 24
    • 0018248691 scopus 로고
    • Fractionation of brain microtubule associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro
    • Herzog, W. and Weber, K., Fractionation of brain microtubule associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro, Eur. J. Biochem., 92 (1978) 1-8.
    • (1978) Eur. J. Biochem. , vol.92 , pp. 1-8
    • Herzog, W.1    Weber, K.2
  • 25
    • 0025930287 scopus 로고
    • Oxidative glycation and free radical production: A causal mechanism of diabetic complications
    • Hunt, J.V. and Wolff, S.P., Oxidative glycation and free radical production: a causal mechanism of diabetic complications. Free Rad. Res. Comms., 12-13 (1991) 115-123.
    • (1991) Free Rad. Res. Comms. , vol.12-13 , pp. 115-123
    • Hunt, J.V.1    Wolff, S.P.2
  • 26
    • 0023839092 scopus 로고
    • Solubility of neurofibrillary tangles and ultrastructure of paired helical filaments in sodium dodecylsulphate
    • Hussey, S., Gibson, P.H., Elton, R.A., Yates, C.M., Christie, J.E., Eagles, P.A. and Gordon, A., Solubility of neurofibrillary tangles and ultrastructure of paired helical filaments in sodium dodecylsulphate, Acta Neuropathol., 75 (1988) 495-501.
    • (1988) Acta Neuropathol. , vol.75 , pp. 495-501
    • Hussey, S.1    Gibson, P.H.2    Elton, R.A.3    Yates, C.M.4    Christie, J.E.5    Eagles, P.A.6    Gordon, A.7
  • 27
    • 0025905126 scopus 로고
    • Widespread serum amyloid P immunoreactivity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders
    • Kalaria, R.N., Galloway, P.G. and Perry, G., Widespread serum amyloid P immunoreactivity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders, Neuropathol. Appl. Neurobiol., 17 (1991) 189-201.
    • (1991) Neuropathol. Appl. Neurobiol. , vol.17 , pp. 189-201
    • Kalaria, R.N.1    Galloway, P.G.2    Perry, G.3
  • 28
    • 0026711059 scopus 로고
    • Fetal-type phosphorylation of the tau in paired helical filaments
    • Kanemaru, K., Takio, K., Miura, R., Titani, K. and Ihara, Y., Fetal-type phosphorylation of the tau in paired helical filaments, J. Neurochem., 58 (1992) 1667-1675.
    • (1992) J. Neurochem. , vol.58 , pp. 1667-1675
    • Kanemaru, K.1    Takio, K.2    Miura, R.3    Titani, K.4    Ihara, Y.5
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of the bacteriophage T4, Nature, 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0028065142 scopus 로고
    • Analysis of microtubule-associated protein tau glycation in paired helical filaments
    • Ledesma, M.D., Bonay, P., Colaco, C. and Avila, J., Analysis of microtubule-associated protein tau glycation in paired helical filaments, J. Biol. Chem., 269 (1994) 21614-21619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaco, C.3    Avila, J.4
  • 31
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee, V.M., Balin, B.J., Otvos, L. Jr. and Trojanowski, J.Q., A68: a major subunit of paired helical filaments and derivatized forms of normal tau, Science, 251 (1991) 675-678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos L., Jr.3    Trojanowski, J.Q.4
  • 32
    • 0021171445 scopus 로고
    • The purification of tau protein and the occurrence of two phosphorylation states of tau in brain
    • Lindwell, G. and Cole, R.D., The purification of tau protein and the occurrence of two phosphorylation states of tau in brain. J. Biol. Chem., 259 (1984) 12241-12245.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12241-12245
    • Lindwell, G.1    Cole, R.D.2
  • 33
    • 0026541969 scopus 로고
    • aB Crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease
    • Lowe, J., McDermott, H., Pike, I., Spendlove, I., Landon, M. and Mayer, R.J. aB Crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease, J. Pathol, 166 (1992) 61-68.
    • (1992) J. Pathol , vol.166 , pp. 61-68
    • Lowe, J.1    McDermott, H.2    Pike, I.3    Spendlove, I.4    Landon, M.5    Mayer, R.J.6
  • 35
    • 0022156464 scopus 로고
    • Neuronal origin of a cerebral amyloid: Neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • Masters, C.L., Multhaup, G., Simms, G., Pottgiesser, J., Martins, R.N. and Beyreuther, K., Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels, EMBO J., 4 (1985) 2757-2763.
    • (1985) EMBO J. , vol.4 , pp. 2757-2763
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 36
    • 0019878619 scopus 로고
    • Characterization of pepsin-resistant collagen-like tail subunit fragments of 18S and 14S acetylcholinert-erase from Electrophorus electricus
    • Mays, C. and Rosenberry, T.L., Characterization of pepsin-resistant collagen-like tail subunit fragments of 18S and 14S acetylcholinert-erase from Electrophorus electricus, Biochemistry, 20 (1981) 2810-2817.
    • (1981) Biochemistry , vol.20 , pp. 2810-2817
    • Mays, C.1    Rosenberry, T.L.2
  • 37
    • 0019475899 scopus 로고
    • Nonenzymatic browning in xivo: Possible process for aging of long-lived proteins
    • Monnier, V.M. and Cerami, A., Nonenzymatic browning in xivo: possible process for aging of long-lived proteins, Science, 211 (1981) 491-493.
    • (1981) Science , vol.211 , pp. 491-493
    • Monnier, V.M.1    Cerami, A.2
  • 38
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori, H., Kondo, J. and Ihara, Y., Ubiquitin is a component of paired helical filaments in Alzheimer's disease, Science, 235 (1987) 1641-1644.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 39
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey, J.H., Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity, Anal. Biochem., 117 (1981) 307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 40
    • 0024997448 scopus 로고
    • Characterization of tau protein present in microtubules and paired helical filaments of Alzheimer's disease patient's brain
    • Nieto, A., Montejo de Garcini, E., Correas, I. and Avila, J., Characterization of tau protein present in microtubules and paired helical filaments of Alzheimer's disease patient's brain, Neuroscience, 37 (1990) 163-170.
    • (1990) Neuroscience , vol.37 , pp. 163-170
    • Nieto, A.1    Montejo De Garcini, E.2    Correas, I.3    Avila, J.4
  • 41
    • 0026823074 scopus 로고
    • Immunohistochemical evidence of antioxidative stress in Alzheimer's disease
    • Pappolla, M.A., Omar, R.A., Kim, K.S. and Robakis, N.K., Immunohistochemical evidence of antioxidative stress in Alzheimer's disease, Am. J. Pathol. 140 (1992) 621-628.
    • (1992) Am. J. Pathol. , vol.140 , pp. 621-628
    • Pappolla, M.A.1    Omar, R.A.2    Kim, K.S.3    Robakis, N.K.4
  • 43
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaques of Alzheimer disease brains
    • Perry, G., Friedman, R., Shaw, G. and Chau, V., Ubiquitin is detected in neurofibrillary tangles and senile plaques of Alzheimer disease brains, Proc. Natl. Acad. Sci. USA, 84 (1987) 3033-3036.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 46
    • 0027376485 scopus 로고
    • Increased expression of heat-shock protein 27 kDa in Alzheimer disease: A preliminary study
    • Renkawek, K., Busman, G.J. and Gaestel, M., Increased expression of heat-shock protein 27 kDa in Alzheimer disease: a preliminary study. Neuroreport, 5 (1993) 14-16.
    • (1993) Neuroreport , vol.5 , pp. 14-16
    • Renkawek, K.1    Busman, G.J.2    Gaestel, M.3
  • 47
    • 0024231238 scopus 로고
    • Isolation and chemical characterization of Alzheimer's disease paired helical filament cytoskeletons: Differentiation from amyloid plaque core protein
    • Roher, A.E., Palmer, K.C., Chan, V. and Ball, M.J., Isolation and chemical characterization of Alzheimer's disease paired helical filament cytoskeletons: differentiation from amyloid plaque core protein. J. Cell. Biol., 107 (1988) 2703-2716.
    • (1988) J. Cell. Biol. , vol.107 , pp. 2703-2716
    • Roher, A.E.1    Palmer, K.C.2    Chan, V.3    Ball, M.J.4
  • 48
    • 0014779155 scopus 로고
    • Two dimensional thin layer Chromatographie separation of polar lipids and determination of phospholipids by phosphorous analysis of spots
    • Rouser, G., Fleischer, S. and Yamamoto, A., Two dimensional thin layer Chromatographie separation of polar lipids and determination of phospholipids by phosphorous analysis of spots, Lipids, 5 (1970) 494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleischer, S.2    Yamamoto, A.3
  • 49
    • 0019935512 scopus 로고
    • Effects of age and diabetes mellitus on the solubility of collagen from human skin, trachéal cartilage and dura mater
    • Schnider, S.L. and Kohn, R.R., Effects of age and diabetes mellitus on the solubility of collagen from human skin, trachéal cartilage and dura mater, Exp. Gerontol., 17 (1982) 185-194.
    • (1982) Exp. Gerontol. , vol.17 , pp. 185-194
    • Schnider, S.L.1    Kohn, R.R.2
  • 50
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-as-sociated protein r controls the in vitro assembly of paired helical filaments
    • Schweers, O., Mandelkow, E.M., Biernat, J. and Mandelkow, E., Oxidation of cysteine-322 in the repeat domain of microtubule-as-sociated protein r controls the in vitro assembly of paired helical filaments, Proc. Natl. Acad. Sci. USA, 92 (1995) 8463-8467.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 51
    • 0020034866 scopus 로고
    • Alzheimer's disease: Insolubility of partially purified paired helical filaments in sodium dodecyl sulfate and urea
    • Selkoe, D.J., Ihara, Y. and Salazar, F.J., Alzheimer's disease: insolubility of partially purified paired helical filaments in sodium dodecyl sulfate and urea, Science, 215 (1982) 1243-1245.
    • (1982) Science , vol.215 , pp. 1243-1245
    • Selkoe, D.J.1    Ihara, Y.2    Salazar, F.J.3
  • 52
    • 0021167283 scopus 로고
    • The immunological relatedness of neurofilament proteins of higher vertebrates
    • Shaw, G., Debus, E. and Weber, K., The immunological relatedness of neurofilament proteins of higher vertebrates, Eur. J. Cell. Biol., 34(1984) 130-136.
    • (1984) Eur. J. Cell. Biol. , vol.34 , pp. 130-136
    • Shaw, G.1    Debus, E.2    Weber, K.3
  • 53
    • 0019199455 scopus 로고
    • Preparation of neurofilament protein from guinea pig peripheral nerve and spinal cord
    • Shecket, G. and Lasek, R.J., Preparation of neurofilament protein from guinea pig peripheral nerve and spinal cord, J. Neurochem., 35 (1980) 1335-1344.
    • (1980) J. Neurochem. , vol.35 , pp. 1335-1344
    • Shecket, G.1    Lasek, R.J.2
  • 55
    • 0028609520 scopus 로고
    • Advanced Maillard reaction end products, free radicals, and protein oxidation in Abheimer's disease
    • Smith, M.A., Richey, P.L., Taneda, S., Kutty, R.K., Sayre. L.M., Monnier, V.M. and Perry, G., Advanced Maillard reaction end products, free radicals, and protein oxidation in Abheimer's disease, Ann. NY Acad. Sci., 738 (1994) 447-454.
    • (1994) Ann. NY Acad. Sci. , vol.738 , pp. 447-454
    • Smith, M.A.1    Richey, P.L.2    Taneda, S.3    Kutty, R.K.4    Sayre, L.M.5    Monnier, V.M.6    Perry, G.7
  • 56
    • 0342417533 scopus 로고
    • Diabetes mellitus and Alzheimer's disease: Glycation as a biochemical link
    • in press
    • Smith, M.A., Sayre, L.M. and Perry, G., Diabetes mellitus and Alzheimer's disease: glycation as a biochemical link, Diabetologia, 38 (1995) in press.
    • (1995) Diabetologia , vol.38
    • Smith, M.A.1    Sayre, L.M.2    Perry, G.3
  • 57
    • 0029007478 scopus 로고
    • Carbonyl-re-lated posttranslational modification of neurofilament protein in the neurofibrillary pathology of Alzheimer's disease
    • Smith, M.A., Rudnicka-Nawrot, M., Richey, P.L., Praprotnik, D., Mulvihill, P., Miller, C.A., Sayre, L.M. and Perry, G., Carbonyl-re-lated posttranslational modification of neurofilament protein in the neurofibrillary pathology of Alzheimer's disease, J. Neurochem., 64 (1995) 2660-2666.
    • (1995) J. Neurochem. , vol.64 , pp. 2660-2666
    • Smith, M.A.1    Rudnicka-Nawrot, M.2    Richey, P.L.3    Praprotnik, D.4    Mulvihill, P.5    Miller, C.A.6    Sayre, L.M.7    Perry, G.8
  • 61
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl. Acad. Sci. USA, 76 (1979) 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 62
    • 0345515340 scopus 로고
    • Detection of sugars on paper chromatograms
    • Trevelyan, W.E., Procter, D.P. and Harrison, J.S., Detection of sugars on paper chromatograms, Nature, 166 (1950) 444-445.
    • (1950) Nature , vol.166 , pp. 444-445
    • Trevelyan, W.E.1    Procter, D.P.2    Harrison, J.S.3
  • 64
    • 0021796959 scopus 로고
    • Subunit structure of paired helical filaments in Alzheimer's disease
    • Wischik, C.M., Crowther, R.A., Stewart, M. and Roth, M., Subunit structure of paired helical filaments in Alzheimer's disease, J. Cell. Biol., 100 (1985) 1905-1912.
    • (1985) J. Cell. Biol. , vol.100 , pp. 1905-1912
    • Wischik, C.M.1    Crowther, R.A.2    Stewart, M.3    Roth, M.4
  • 66
    • 0022457104 scopus 로고
    • A neuronal antigen in the brains of Alzheimer patients
    • Wolozin, B.L., Pruchnicki, A., Dickson, D.W. and Davies, P., A neuronal antigen in the brains of Alzheimer patients, Science, 232 (1986) 648-650.
    • (1986) Science , vol.232 , pp. 648-650
    • Wolozin, B.L.1    Pruchnicki, A.2    Dickson, D.W.3    Davies, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.