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Volumn 24, Issue 6, 1999, Pages 767-774

The expression of several mitochondrial and nuclear genes encoding the subunits of electron transport chain enzyme complexes, cytochrome c oxidase, and NADH dehydrogenase, in different brain regions in Alzheimer's disease

Author keywords

Alzheimer's disease; Cytochrome c oxidase; Gene expression; MRNA; NADH dehydrogenase; RT PCR

Indexed keywords

CYTOCHROME C OXIDASE; MESSENGER RNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 0032971621     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020783614031     Document Type: Article
Times cited : (97)

References (56)
  • 1
    • 0029548561 scopus 로고
    • Free radical theory of aging: Alzheimer's disease pathogenesis
    • Harman, D. 1995. Free radical theory of aging: Alzheimer's disease pathogenesis. Age 18:97-119.
    • (1995) Age , vol.18 , pp. 97-119
    • Harman, D.1
  • 2
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling, A. C., and Beal, M. F. 1995. Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sciences. 56: 1151-1171.
    • (1995) Life Sciences , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 3
    • 0030928406 scopus 로고    scopus 로고
    • β-Amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • Butterfield, D. A. 1997. β-Amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem. Res. Toxicol. 10:495-506.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 495-506
    • Butterfield, D.A.1
  • 4
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W. R. 1997. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 23:134-147.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 6
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya, E. M., Bowling, A. C., and Beal, M. F. 1994. Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 63:2179-2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 7
    • 0030273295 scopus 로고    scopus 로고
    • Mitochondria, free radicals, and neurodegeneration
    • Beal, M. F. 1996. Mitochondria, free radicals, and neurodegeneration. Curr. Opin. Neurobiol. 6:661-666.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 661-666
    • Beal, M.F.1
  • 8
    • 0030830677 scopus 로고    scopus 로고
    • Cytochrome oxidase in Alzheimer's disease: Biochemical, histochemical, and immunohistochemical analyses of the visual and other systems
    • Wong-Riley, M., Antuono, P., Ho, K. C., Egan, R., Hevner, R., Liebl, W., Huang, Z., Rachel, R., and Jones, J. 1997. Cytochrome oxidase in Alzheimer's disease: biochemical, histochemical, and immunohistochemical analyses of the visual and other systems. Vision Res. 37:3593-3608.
    • (1997) Vision Res. , vol.37 , pp. 3593-3608
    • Wong-Riley, M.1    Antuono, P.2    Ho, K.C.3    Egan, R.4    Hevner, R.5    Liebl, W.6    Huang, Z.7    Rachel, R.8    Jones, J.9
  • 9
    • 0030923869 scopus 로고    scopus 로고
    • Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease
    • Sheenan, J. P., Swerdlow, R. H., Miller, S. W., Davis, R. E., Parks, J. K., Parker, W. D., and Tuttle, J. B. 1997. Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease. J. Neurosci. 17:4612-4622.
    • (1997) J. Neurosci. , vol.17 , pp. 4612-4622
    • Sheenan, J.P.1    Swerdlow, R.H.2    Miller, S.W.3    Davis, R.E.4    Parks, J.K.5    Parker, W.D.6    Tuttle, J.B.7
  • 10
    • 0025024024 scopus 로고
    • Cytochrome oxidase deficiency in Alzheimer's disease
    • Parker, W. D. Jr., Filley, C. M., and Parks, J. K. 1990. Cytochrome oxidase deficiency in Alzheimer's disease. Neurology. 40: 1302-1303.
    • (1990) Neurology , vol.40 , pp. 1302-1303
    • Parker W.D., Jr.1    Filley, C.M.2    Parks, J.K.3
  • 11
    • 0030296713 scopus 로고    scopus 로고
    • Evidence for physiological down-regulation of brain oxidative phosphorylation in Alzheimer's disease
    • Chandrasekaran, K., Hatanpaa, K., Brady, D. R., and Rapoport, S.I. 1996. Evidence for physiological down-regulation of brain oxidative phosphorylation in Alzheimer's disease. Exp. Neurol. 142:80-88.
    • (1996) Exp. Neurol. , vol.142 , pp. 80-88
    • Chandrasekaran, K.1    Hatanpaa, K.2    Brady, D.R.3    Rapoport, S.I.4
  • 12
    • 0030498070 scopus 로고    scopus 로고
    • Brain energy metabolism, cognitive function and down-regulated oxidative phosphorylation in Alzheimer disease
    • Rapoport, S. I., Hatanpaa, K., Brady, D. R., and Chandrasekaran, K. 1996. Brain energy metabolism, cognitive function and down-regulated oxidative phosphorylation in Alzheimer disease. Neurodegeneration. 5:473-476.
    • (1996) Neurodegeneration , vol.5 , pp. 473-476
    • Rapoport, S.I.1    Hatanpaa, K.2    Brady, D.R.3    Chandrasekaran, K.4
  • 13
    • 0030723048 scopus 로고    scopus 로고
    • Brain energy metabolizing enzymes in Alzheimer's disease: Alpha-ketoglutarate dehydrogenase complex and cytochrome oxidase
    • Kish, S. J. 1997. Brain energy metabolizing enzymes in Alzheimer's disease: alpha-ketoglutarate dehydrogenase complex and cytochrome oxidase. Ann. NY Acad. Sci. 826: 218-228.
    • (1997) Ann. NY Acad. Sci. , vol.826 , pp. 218-228
    • Kish, S.J.1
  • 14
    • 0030708717 scopus 로고    scopus 로고
    • Pathogenesis of decreased glucose turnover and oxidative phosphorylation in ischemic and trauma-induced dementia of the Alzheimer type
    • Meier-Ruge, W. A., and Bertoni-Freddari, C. 1997. Pathogenesis of decreased glucose turnover and oxidative phosphorylation in ischemic and trauma-induced dementia of the Alzheimer type. Ann. NY Acad. Sci. 826:229-241
    • (1997) Ann. NY Acad. Sci. , vol.826 , pp. 229-241
    • Meier-Ruge, W.A.1    Bertoni-Freddari, C.2
  • 15
    • 0029939002 scopus 로고    scopus 로고
    • Gene expression of ND4, a subunit of complex I of oxidative phosphorylation in mitochondria, is decreased in temporal cortex of brains of Alzheimer's disease patients
    • Fukuyama, R., Hatanpaa, K., Rapoport, S. I., and Chandrasekaran, K. 1996. Gene expression of ND4, a subunit of complex I of oxidative phosphorylation in mitochondria, is decreased in temporal cortex of brains of Alzheimer's disease patients. Brain Res. 713:290-293.
    • (1996) Brain Res. , vol.713 , pp. 290-293
    • Fukuyama, R.1    Hatanpaa, K.2    Rapoport, S.I.3    Chandrasekaran, K.4
  • 16
    • 0031036773 scopus 로고    scopus 로고
    • Decreased, expression of nuclear and mitochondrial DNA-encoded genes of oxidative phosphorylation in association neocortex in Alzheimer disease
    • Chandrasekaran, K. Hatanpaa, K., Rapoport, S.I., and Brady, D. R. 1997. Decreased, expression of nuclear and mitochondrial DNA-encoded genes of oxidative phosphorylation in association neocortex in Alzheimer disease. Mol. Brain Res. 44: 99-104.
    • (1997) Mol. Brain Res. , vol.44 , pp. 99-104
    • Chandrasekaran, K.1    Hatanpaa, K.2    Rapoport, S.I.3    Brady, D.R.4
  • 17
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration
    • Davey, G.P., Peuchen, S., and Clark, J. B. 1998. Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration. J. Biol. Chem. 273:12753-12757.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 19
    • 0027420891 scopus 로고
    • Functional alterations in Alzheimer's disease: Diminution of cytochrome oxidase in the hippocampal formation
    • Simonian, N. A., and Hyman, B. T. 1993. Functional alterations in Alzheimer's disease: diminution of cytochrome oxidase in the hippocampal formation. J. Neuropathol. Exp. Neurol. 52: 580-585.
    • (1993) J. Neuropathol. Exp. Neurol. , vol.52 , pp. 580-585
    • Simonian, N.A.1    Hyman, B.T.2
  • 20
    • 0028948660 scopus 로고
    • Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases
    • Changnon, P., Betard, C., Robitaille., Y., Cholette, A., and Gauvreau, D. 1995. Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases. Neuroreport. 6: 711-715.
    • (1995) Neuroreport , vol.6 , pp. 711-715
    • Changnon, P.1    Betard, C.2    Robitaille, Y.3    Cholette, A.4    Gauvreau, D.5
  • 21
    • 0030941592 scopus 로고    scopus 로고
    • Quantitative cytochemistry of cytochrome oxidase and cellular morphometry of the inferior colliculus in control and Alzheimer's patients
    • Gonzalez-Lima, F., Valla, J., and Matos-Collazo, S. 1997. Quantitative cytochemistry of cytochrome oxidase and cellular morphometry of the inferior colliculus in control and Alzheimer's patients. Brain Res. 758:117-126.
    • (1997) Brain Res. , vol.758 , pp. 117-126
    • Gonzalez-Lima, F.1    Valla, J.2    Matos-Collazo, S.3
  • 22
    • 0028869597 scopus 로고    scopus 로고
    • Human diseases with defects in oxidative phosphorylation. 2. F1F0 ATP-synthase defects in Alzheimer disease revealed by blue native polyacrylamide electrophoresis
    • Schagger, H., and Ohm, T. G. 1996. Human diseases with defects in oxidative phosphorylation. 2. F1F0 ATP-synthase defects in Alzheimer disease revealed by blue native polyacrylamide electrophoresis Eur. J. Biochem. 227:916-921.
    • (1996) Eur. J. Biochem. , vol.227 , pp. 916-921
    • Schagger, H.1    Ohm, T.G.2
  • 23
    • 0028023533 scopus 로고
    • Functional alterations in Alzheimer's disease: Selective loss of mitochondrial-encoded cytochrome oxidase mRNA in the hippocampal formation
    • Simonian, N. A., and Hyman, B. T. 1994. Functional alterations in Alzheimer's disease: Selective loss of mitochondrial-encoded cytochrome oxidase mRNA in the hippocampal formation. J. Neuropathol. Exp. Neurol. 53:508-512.
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 508-512
    • Simonian, N.A.1    Hyman, B.T.2
  • 24
    • 0029055772 scopus 로고
    • Cytochrome c oxidase in Alzheimer's disease brain: Purification and characterization
    • Parker, W. D. Jr., and Parks, J. K. 1995. Cytochrome c oxidase in Alzheimer's disease brain: purification and characterization. Neurology. 45:482-486.
    • (1995) Neurology , vol.45 , pp. 482-486
    • Parker W.D., Jr.1    Parks, J.K.2
  • 26
    • 0029814873 scopus 로고    scopus 로고
    • Differential susceptibility of human skeletal muscle proteins to free radical induced oxidative damage: A histochemical, immunocytochemical and electron microscopical study in vitro
    • Berl.
    • Haycock, J. W., Jones, P., Harris, J. B., and Mantle, D. 1996. Differential susceptibility of human skeletal muscle proteins to free radical induced oxidative damage: a histochemical, immunocytochemical and electron microscopical study in vitro. Acta Neuropathol. (Berl.) 92:331-340.
    • (1996) Acta Neuropathol. , vol.92 , pp. 331-340
    • Haycock, J.W.1    Jones, P.2    Harris, J.B.3    Mantle, D.4
  • 27
    • 0025335849 scopus 로고
    • Structure and assembly of cytochrome c oxidase
    • Calpaldi, R. A. Structure and assembly of cytochrome c oxidase. 1990. Arch. Biochem. Biophys. 280:252-262.
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 252-262
    • Calpaldi, R.A.1
  • 28
    • 0026217899 scopus 로고
    • Cytochrome c oxidase: Structure, function, and membrane topology of the polypeptide subunits
    • Cooper, C. E., Nicholls, P., and Freedman, J. A. 1991. Cytochrome c oxidase: structure, function, and membrane topology of the polypeptide subunits. Biochem. Cell Biol. 69: 586-607.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 586-607
    • Cooper, C.E.1    Nicholls, P.2    Freedman, J.A.3
  • 29
    • 0026487290 scopus 로고
    • Sequences of 20 subunits of NADH: Ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction
    • Walker, J. E., Arizmendi, J. M., Dupuis, A., Fearnley, I. M., Finel, M., Medd, S. M., Pilkington, S. J., Runswick, M. J., and Skehel, J. M. 1992. Sequences of 20 subunits of NADH: ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction. J. Mol. Biol. 226:1051-1072.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1051-1072
    • Walker, J.E.1    Arizmendi, J.M.2    Dupuis, A.3    Fearnley, I.M.4    Finel, M.5    Medd, S.M.6    Pilkington, S.J.7    Runswick, M.J.8    Skehel, J.M.9
  • 30
    • 0027328630 scopus 로고
    • Regulation of the expression of mitochondrial proteins: Relationship between mtDNA copy number and cytochrome-c oxidase activity in human cells and tissues
    • Van den Bogert, C., De Vries, H., Holtrop, M., Muus, P., Dekker, H. L., Van Galen, M. J., Bolhuis, P. A., and Taanman, J. W. 1993. Regulation of the expression of mitochondrial proteins: relationship between mtDNA copy number and cytochrome-c oxidase activity in human cells and tissues. Biochim. Biophys. Acta. 1144:177-183.
    • (1993) Biochim. Biophys. Acta. , vol.1144 , pp. 177-183
    • Van Den Bogert, C.1    De Vries, H.2    Holtrop, M.3    Muus, P.4    Dekker, H.L.5    Van Galen, M.J.6    Bolhuis, P.A.7    Taanman, J.W.8
  • 31
    • 0029780531 scopus 로고    scopus 로고
    • Mitochondrial- And nuclear-encoded subunits of cytochrome oxidase in neurons: Differences in compartmental distribution, correlation with enzyme activity, and regulation by neuronal activity
    • Nie, F., and Wong-Riley, M. T. 1996. Mitochondrial- and nuclear-encoded subunits of cytochrome oxidase in neurons: differences in compartmental distribution, correlation with enzyme activity, and regulation by neuronal activity. J. Comp. Neurol. 373:139-155.
    • (1996) J. Comp. Neurol. , vol.373 , pp. 139-155
    • Nie, F.1    Wong-Riley, M.T.2
  • 32
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D. J. 1991. The molecular pathology of Alzheimer's disease. Neuron. 61:487-498.
    • (1991) Neuron. , vol.61 , pp. 487-498
    • Selkoe, D.J.1
  • 33
    • 0019841867 scopus 로고
    • Changes in chromatin structure associated with Alzheimer's disease
    • Lewis, P. N., Lukiw, W. J., De Boni, U., and Crapper McLachlan, D. R. 1981. Changes in chromatin structure associated with Alzheimer's disease. J.Neurochem. 37:1193-1202.
    • (1981) J.Neurochem. , vol.37 , pp. 1193-1202
    • Lewis, P.N.1    Lukiw, W.J.2    De Boni, U.3    Crapper McLachlan, D.R.4
  • 34
    • 0022483705 scopus 로고
    • The presence of nucleosomes on a DNa template prevents initiation by RNa II polymerase in vitro
    • Knezetic, J. A., and Luse, D. S. 1986. The presence of nucleosomes on a DNA template prevents initiation by RNA II polymerase in vitro. Cell. 45:95-104.
    • (1986) Cell , vol.45 , pp. 95-104
    • Knezetic, J.A.1    Luse, D.S.2
  • 36
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease
    • Mecocci, P., MacGarvey, U., and Beal, M. F. 1994. Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease. Ann. Neurol. 36:747-751.
    • (1994) Ann. Neurol. , vol.36 , pp. 747-751
    • Mecocci, P.1    MacGarvey, U.2    Beal, A.3    F, M.4
  • 37
    • 0031754202 scopus 로고    scopus 로고
    • Increased nuclear DNA oxidation in the brain in Alzheimer's disease
    • Gabbita, S. P., Lovell, M. A., and Markesbery, W. R. 1998. Increased nuclear DNA oxidation in the brain in Alzheimer's disease. J. Neurochem. 71:2034-2090.
    • (1998) J. Neurochem. , vol.71 , pp. 2034-2090
    • Gabbita, S.P.1    Lovell, M.A.2    Markesbery, W.R.3
  • 38
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS ADRDA work group under the auspices of Department of Health and Human Services Task Force on Alzheimer's disease
    • McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D. and Stadlan, E. M. 1984. Clinical diagnosis of Alzheimer's disease: report of the NINCDS ADRDA work group under the auspices of Department of Health and Human Services Task Force on Alzheimer's disease. Neurology. 34:939-944.
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 39
    • 0022414054 scopus 로고
    • Diagnosis of Alzheimer's disease
    • Khachaturian, Z. S. 1985. Diagnosis of Alzheimer's disease. Arch. Neurol. 42:1097-1105.
    • (1985) Arch. Neurol. , vol.42 , pp. 1097-1105
    • Khachaturian, Z.S.1
  • 40
    • 0025908356 scopus 로고
    • The Consorcium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standartization of the neuropathologic assessment of Alzheimer's disease
    • Mirra, S. S., Heyman, A., and McKeel, D. 1991. The Consorcium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standartization 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
  • 41
    • 24444462098 scopus 로고    scopus 로고
    • Consensus Recommendations
    • National Institute on Aging and Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer's disease. 1997. Consensus Recommendations. Neurobiol. Aging. S1-S2.
    • (1997) Neurobiol. Aging
  • 42
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinum thiocyanate-phenol-chloroform extraction
    • Chromzynski, P., and Sacchi, N. 1987. Single-step method of RNA isolation by acid guanidinum thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chromzynski, P.1    Sacchi, N.2
  • 44
    • 0002038519 scopus 로고    scopus 로고
    • Optimization and validation of RT-PCR as a tool to analyze apoptotic gene expression
    • Poirier J., (ed.), Humana, Totowa, NJ
    • Estus, S. 1997. Optimization and validation of RT-PCR as a tool to analyze apoptotic gene expression, Pages 67-84, in Poirier J., (ed.), NeuroMethods 29: Apoptosis techniques and protocols. Humana, Totowa, NJ.
    • (1997) NeuroMethods 29: Apoptosis Techniques and Protocols , vol.29 , pp. 67-84
    • Estus, S.1
  • 48
    • 0029999853 scopus 로고    scopus 로고
    • Probing a role of subunit of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses
    • Saiki, K., Nakamura, H., Mogi, T., and Anraku, Y. 1996. Probing a role of subunit of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses. J. Biol. Chem. 271:15336-15340.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15336-15340
    • Saiki, K.1    Nakamura, H.2    Mogi, T.3    Anraku, Y.4
  • 49
    • 0031449003 scopus 로고    scopus 로고
    • Apparent mtDNA heteroplasmy in Alzheimer's disease patients and normals due to PCR amplification of nucleus-embedded mtDNA pseudogenes
    • Hirano, M., Shtilbans, A., Mayeux, R., Davidson, M. M., DiMauro, S., Knowles, J. A., and Schon, E. A. 1997. Apparent mtDNA heteroplasmy in Alzheimer's disease patients and normals due to PCR amplification of nucleus-embedded mtDNA pseudogenes. Proc. Natl. Acad. Sci. USA. 94:14894-14899.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14894-14899
    • Hirano, M.1    Shtilbans, A.2    Mayeux, R.3    Davidson, M.M.4    Dimauro, S.5    Knowles, J.A.6    Schon, E.A.7
  • 50
    • 0027270863 scopus 로고
    • Lack of assembly of mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase and loss of enzyme activity in human cell mutant lacking the mitochondrial ND4 gene product
    • Hofhaus, G., Attardi, G. 1993. Lack of assembly of mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase and loss of enzyme activity in human cell mutant lacking the mitochondrial ND4 gene product. EMBO J. 12:3043-3048.
    • (1993) EMBO J. , vol.12 , pp. 3043-3048
    • Hofhaus, G.1    Attardi, G.2
  • 52
    • 0021238760 scopus 로고
    • Alzheimer's disease brain: Alterations in RNa levels and in a ribonuclease-inhibitor complex
    • Sajdel-Sulkowska, E. M., Marotta, C. A. 1984. Alzheimer's disease brain: alterations in RNA levels and in a ribonuclease-inhibitor complex. Science. 225:947-949.
    • (1984) Science , vol.225 , pp. 947-949
    • Sajdel-Sulkowska, E.M.1    Marotta, C.A.2
  • 53
    • 0022553154 scopus 로고
    • Recovery and measurement of specific RNa species from postmortem brain tissue: A general reduction in Alzheimer's disease detected by molecular hybridization
    • Taylor, G. R., Carte, G. I., Grow, T. J., Johnson, J. A., Fairbairn, A. F., Perry, E. K., Perry, R. H. 1986. Recovery and measurement of specific RNA species from postmortem brain tissue: A general reduction in Alzheimer's disease detected by molecular hybridization. Exp. Mol. Pathol. 44:111-116
    • (1986) Exp. Mol. Pathol. , vol.44 , pp. 111-116
    • Taylor, G.R.1    Carte, G.I.2    Grow, T.J.3    Johnson, J.A.4    Fairbairn, A.F.5    Perry, E.K.6    Perry, R.H.7
  • 54
    • 0022516004 scopus 로고
    • Characterization of messenger RNA from the cerebral cortex of control and Alzheimer-afflicted brain
    • Guillemette, J. G., Wong, L., Crapper McLachlan, D. R., Lewis, P. N. 1987. Characterization of messenger RNA from the cerebral cortex of control and Alzheimer-afflicted brain. J. Neurochem. 47:987-997.
    • (1987) J. Neurochem. , vol.47 , pp. 987-997
    • Guillemette, J.G.1    Wong, L.2    Crapper McLachlan, D.R.3    Lewis, P.N.4


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