메뉴 건너뛰기




Volumn 16, Issue 1, 2014, Pages 175-190

Monitoring of neuronal loss in the hippocampus of Aβ-injected rat: Autophagy, mitophagy, and mitochondrial biogenesis stand against apoptosis

Author keywords

Alzheimer's disease; Amyloid beta; Apoptosis; Autophagy; Mitochondrial biogenesis

Indexed keywords

ACONITATE HYDRATASE; AMYLOID BETA-PEPTIDES; ANIMALS; APOPTOSIS; AUTOPHAGY; CA1 REGION, HIPPOCAMPAL; CATALASE; CITRATE (SI)-SYNTHASE; CITRIC ACID CYCLE; CYTOCHROMES; ELECTRON TRANSPORT; ENZYME INDUCTION; FUMARATE HYDRATASE; GLUTATHIONE; MALATE DEHYDROGENASE; MALE; MICROINJECTIONS; MITOCHONDRIA; MITOCHONDRIAL DEGRADATION; NERVE TISSUE PROTEINS; NEURONS; PEPTIDE FRAGMENTS; PROTEIN KINASES; RATS; RATS, WISTAR; REACTIVE OXYGEN SPECIES; SUPEROXIDE DISMUTASE; TIME FACTORS;

EID: 84894261400     PISSN: 15351084     EISSN: 15591174     Source Type: Journal    
DOI: 10.1007/s12017-013-8272-8     Document Type: Article
Times cited : (53)

References (79)
  • 1
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • 1:CAS:528:DC%2BD28Xht1eku7fF 10.1016/j.tips.2006.10.005 17056127
    • Adam-Vizi, V., & Chinopoulos, C. (2006). Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends in Pharmacological Sciences, 27(12), 639-645.
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.12 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 2
    • 0021318441 scopus 로고
    • Catalase in vitro
    • 1:CAS:528:DyaL2cXltVKis7s%3D 10.1016/S0076-6879(84)05016-3 6727660
    • Aebi, H. (1984). Catalase in vitro. Methods in Enzymology, 105, 121-126.
    • (1984) Methods in Enzymology , vol.105 , pp. 121-126
    • Aebi, H.1
  • 3
    • 84871005673 scopus 로고    scopus 로고
    • The pathways of mitophagy for quality control and clearance of mitochondria
    • 1:CAS:528:DC%2BC38XhvVWqtLnI 10.1038/cdd.2012.81 22743996
    • Ashrafi, G., & Schwarz, T. L. (2013). The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differentiation, 20(1), 31-42.
    • (2013) Cell Death Differentiation , vol.20 , Issue.1 , pp. 31-42
    • Ashrafi, G.1    Schwarz, T.L.2
  • 4
    • 0024584371 scopus 로고
    • Fatal lactic acidosis in infancy with a defect of complex III of the respiratory chain
    • 1:STN:280:DyaL1M3jvFOrug%3D%3D 10.1203/00006450-198905000-00025 2541396
    • Birch-Machin, M. A., Shepherd, I. M., Watmough, N. J., Sherrat, H. S., Bartlett, K., Darley-Usmar, V. M., et al. (1989). Fatal lactic acidosis in infancy with a defect of complex III of the respiratory chain. Pediatric Research, 25, 553-559.
    • (1989) Pediatric Research , vol.25 , pp. 553-559
    • Birch-Machin, M.A.1    Shepherd, I.M.2    Watmough, N.J.3    Sherrat, H.S.4    Bartlett, K.5    Darley-Usmar, V.M.6
  • 5
    • 79957932138 scopus 로고    scopus 로고
    • Nuclear-encoded mitochondrial proteins and their role in cardioprotection
    • 1:CAS:528:DC%2BC3MXntV2lsLw%3D 10.1016/j.bbamcr.2011.01.009 21255616
    • Boengler, K., Heusch, G., & Schulz, R. (2011). Nuclear-encoded mitochondrial proteins and their role in cardioprotection. Biochimica et Biophysica Acta, 1813(7), 1286-1294.
    • (2011) Biochimica et Biophysica Acta , vol.1813 , Issue.7 , pp. 1286-1294
    • Boengler, K.1    Heusch, G.2    Schulz, R.3
  • 6
    • 0026134421 scopus 로고
    • Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections
    • 1:STN:280:DyaK2c7it12msQ%3D%3D 10.1111/j.1750-3639.1991.tb00661.x 1669710
    • Braak, H., & Braak, E. (1991). Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections. Brain Pathology, 1(3), 213-216.
    • (1991) Brain Pathology , vol.1 , Issue.3 , pp. 213-216
    • Braak, H.1    Braak, E.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 1:CAS:528:DyaE28XksVehtrY%3D 10.1016/0003-2697(76)90527-3 942051
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 18244390483 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
    • 1:CAS:528:DC%2BD2MXkvFykt70%3D 10.1002/ana.20474 15852400
    • Bubber, P., Haroutunian, V., Fisch, G., Parvesh, B., & Vahram, H. (2005). Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications. Annals of Neurology, 57, 695-703.
    • (2005) Annals of Neurology , vol.57 , pp. 695-703
    • Bubber, P.1    Haroutunian, V.2    Fisch, G.3    Parvesh, B.4    Vahram, H.5
  • 9
    • 77951096150 scopus 로고    scopus 로고
    • Mitochondrial dynamics - Fusion, fission, movement, and mitophagy - In neurodegenerative diseases
    • Chen, H., Chan, D. C. (2009). Mitochondrial dynamics - Fusion, fission, movement, and mitophagy - In neurodegenerative diseases. Human Molecular Genetics, 18 (R2), R169-R176.
    • (2009) Human Molecular Genetics , vol.18 , Issue.R2
    • Chen, H.1    Chan, D.C.2
  • 10
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • 1:STN:280:DC%2BD3c7kt1Oguw%3D%3D 10681270
    • Christen, Y. (2000). Oxidative stress and Alzheimer disease. The American Journal of Clinical Nutrition, 71(2), 621S-629S.
    • (2000) The American Journal of Clinical Nutrition , vol.71 , Issue.2
    • Christen, Y.1
  • 12
    • 0014962720 scopus 로고
    • The metabolism of rat brain mitochondria preparation and characterization
    • Clarke, J. B., & Nicklas, W. J. (1970). The metabolism of rat brain mitochondria preparation and characterization. Journal of Biological Chemistry, 245(18), 4724-4731.
    • (1970) Journal of Biological Chemistry , vol.245 , Issue.18 , pp. 4724-4731
    • Clarke, J.B.1    Nicklas, W.J.2
  • 13
    • 0037137221 scopus 로고    scopus 로고
    • Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-beta peptide
    • 1:CAS:528:DC%2BD38XotFGgtb8%3D 10.1021/bi0260334 12427014
    • Cottingham, M. G., Hollinshead, M. S., & Vaux, D. J. (2002). Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-beta peptide. Biochemistry, 41(46), 13539-13547.
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13539-13547
    • Cottingham, M.G.1    Hollinshead, M.S.2    Vaux, D.J.3
  • 14
    • 36749081539 scopus 로고    scopus 로고
    • MTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex
    • 1:CAS:528:DC%2BD2sXhtlKmtb3K 10.1038/nature06322 18046414
    • Cunningham, J. T., Rodgers, J. T., Arlow, D. H., Vazquez, F., Mootha, V. K., & Puigserver, P. (2007). mTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex. Nature, 450(7170), 736-740.
    • (2007) Nature , vol.450 , Issue.7170 , pp. 736-740
    • Cunningham, J.T.1    Rodgers, J.T.2    Arlow, D.H.3    Vazquez, F.4    Mootha, V.K.5    Puigserver, P.6
  • 15
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • 1:CAS:528:DC%2BD3sXisFSlu7c%3D 10.1093/hmg/ddg044 12588799
    • Darios, F., Corti, O., Lucking, C. B., Hampe, C., Muriel, M. P., Abbas, N., et al. (2003). Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Human Molecular Genetics, 12, 517-526.
    • (2003) Human Molecular Genetics , vol.12 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3    Hampe, C.4    Muriel, M.P.5    Abbas, N.6
  • 16
    • 0013865801 scopus 로고
    • Functions of lysosomes
    • 10.1146/annurev.ph.28.030166.002251 5322983
    • De Duve, C., & Wattiaux, R. (1966). Functions of lysosomes. Annual Review of Physiology, 28, 435-492.
    • (1966) Annual Review of Physiology , vol.28 , pp. 435-492
    • De Duve, C.1    Wattiaux, R.2
  • 17
    • 67549142261 scopus 로고    scopus 로고
    • Life and death partners: Apoptosis, autophagy and the cross-talk between them
    • 1:CAS:528:DC%2BD1MXnsV2qs7o%3D 10.1038/cdd.2009.33 19325568
    • Eisenberg-Lerner, A., Bialik, S., Simon, H.-U., & Kimchi, A. (2009). Life and death partners: Apoptosis, autophagy and the cross-talk between them. Cell Death and Differentiation, 16, 966-975.
    • (2009) Cell Death and Differentiation , vol.16 , pp. 966-975
    • Eisenberg-Lerner, A.1    Bialik, S.2    Simon, H.-U.3    Kimchi, A.4
  • 18
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • 1:CAS:528:DyaG1MXotl2ksA%3D%3D 10.1016/0003-9861(59)90090-6 13650640
    • Ellman, G. L. (1959). Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics, 82, 70-77.
    • (1959) Archives of Biochemistry and Biophysics , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 19
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • 1:CAS:528:DyaK3sXlslGms7c%3D 8226748
    • Flint, D. H., Tuminello, J. F., & Emptage, M. H. (1993). The inactivation of Fe-S cluster containing hydro-lyases by superoxide. Journal of Biological Chemistry, 268, 22369-22376.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 20
    • 58149398233 scopus 로고    scopus 로고
    • Atg4BC74A hampers autophagosome closure: A useful protein for inhibiting autophagy
    • 1:CAS:528:DC%2BD1MXnvFCksL0%3D 10.4161/auto.5.1.7183 19104152
    • Fujita, N., Noda, T., & Yoshimori, T. (2009). Atg4BC74A hampers autophagosome closure: A useful protein for inhibiting autophagy. Autophagy, 5(1), 88-89.
    • (2009) Autophagy , vol.5 , Issue.1 , pp. 88-89
    • Fujita, N.1    Noda, T.2    Yoshimori, T.3
  • 21
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • 1:CAS:528:DyaK2MXmtV2hsrY%3D 10.1074/jbc.270.16.9137 7768942
    • Gardner, P. R., Raineri, I., Epstein, L. B., & White, C. W. (1995). Superoxide radical and iron modulate aconitase activity in mammalian cells. Journal of Biological Chemistry, 270, 13399-13405.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 22
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • 1:CAS:528:DyaL2cXitVOntLw%3D 10.1016/S0006-291X(84)80190-4 6375662
    • Glenner, G. G., & Wong, C. W. (1984). Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochemical and Biophysical Research Communications, 120, 885-890.
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 23
    • 13444306450 scopus 로고    scopus 로고
    • Control of mitochondrial transcription specificity factors (TFB1 M and TFB2 M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family coactivators
    • 1:CAS:528:DC%2BD2MXhs1Kgsbc%3D 10.1128/MCB.25.4.1354-1366.2005
    • Gleyzer, N., Vercauteren, K., & Scarpulla, R. C. (2005). Control of mitochondrial transcription specificity factors (TFB1 M and TFB2 M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family coactivators. Molecular Cell Biology, 25(4), 1354-1366.
    • (2005) Molecular Cell Biology , vol.25 , Issue.4 , pp. 1354-1366
    • Gleyzer, N.1    Vercauteren, K.2    Scarpulla, R.C.3
  • 24
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • 1:CAS:528:DC%2BD3sXpvVGmtbc%3D 10.1038/nature02263 14685250
    • Goldberg, A. L. (2003). Protein degradation and protection against misfolded or damaged proteins. Nature, 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 25
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid b-peptide
    • 1:CAS:528:DC%2BD2sXotFKmtw%3D%3D 10.1038/nrm2101 17245412
    • Haass, C., & Selkoe, D. J. (2007). Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid b-peptide. Nature Reviews Molecular Cell Biology, 8, 101-112.
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 26
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • 1:CAS:528:DC%2BD28XlvVGlsbc%3D 10.1038/nature04724 16625204
    • Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., et al. (2006). Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature, 441, 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 27
    • 48849086912 scopus 로고    scopus 로고
    • Deciphering downstream gene targets of PI3 K/mTOR/p70S6 K pathway in breast cancer
    • 10.1186/1471-2164-9-348
    • Heinonen, H., Nieminen, A., Saarela, M., Kallioniemi, A., Klefström, J., Hautaniemi, S., et al. (2008). Deciphering downstream gene targets of PI3 K/mTOR/p70S6 K pathway in breast cancer. BMC Genomics, 2008(9), 348-360.
    • (2008) BMC Genomics , vol.2008 , Issue.9 , pp. 348-360
    • Heinonen, H.1    Nieminen, A.2    Saarela, M.3    Kallioniemi, A.4    Klefström, J.5    Hautaniemi, S.6
  • 28
    • 0037171147 scopus 로고    scopus 로고
    • High pressure, a tool for exploring heme protein active sites
    • 1:CAS:528:DC%2BD38Xjt1Srsro%3D 10.1016/S0167-4838(01)00352-1 11983404
    • Hui Bon Hoa, G., McLean, M. A., & Sligar, S. G. (2002). High pressure, a tool for exploring heme protein active sites. Biochimica et Biophysica Acta, 1595(1-2), 297-308.
    • (2002) Biochimica et Biophysica Acta , vol.1595 , Issue.1-2 , pp. 297-308
    • Hui Bon Hoa, G.1    McLean, M.A.2    Sligar, S.G.3
  • 29
    • 0036372619 scopus 로고    scopus 로고
    • Redox potential of GSH/GSSG couple: Assay and biological significance
    • 1:CAS:528:DC%2BD38XlsVartbo%3D 10.1016/S0076-6879(02)48630-2 11885298
    • Jones, D. P. (2002). Redox potential of GSH/GSSG couple: Assay and biological significance. Methods in Enzymology, 348, 93-112.
    • (2002) Methods in Enzymology , vol.348 , pp. 93-112
    • Jones, D.P.1
  • 30
    • 0001689585 scopus 로고
    • The analysis of cytochromes
    • 1:CAS:528:DyaL2MXltVWmtro%3D 10.1016/S0580-9517(08)70479-3
    • Jones, C. W., & Poole, R. K. (1985). The analysis of cytochromes. Methods of microbiology, 18, 285-328.
    • (1985) Methods of Microbiology , vol.18 , pp. 285-328
    • Jones, C.W.1    Poole, R.K.2
  • 32
    • 0038400956 scopus 로고    scopus 로고
    • Immunocytochemical evidence that amyloid beta (1-42) impairs endogenous antioxidant systems in vivo
    • 1:CAS:528:DC%2BD3sXktFGjsL0%3D 10.1016/S0306-4522(02)00993-4 12770555
    • Kim, H. C., Yamada, K., Nitta, A., Olariu, A., Tran, M. H., Mizuno, M., et al. (2003). Immunocytochemical evidence that amyloid beta (1-42) impairs endogenous antioxidant systems in vivo. Neuroscience, 119, 399-419.
    • (2003) Neuroscience , vol.119 , pp. 399-419
    • Kim, H.C.1    Yamada, K.2    Nitta, A.3    Olariu, A.4    Tran, M.H.5    Mizuno, M.6
  • 33
    • 10744225487 scopus 로고    scopus 로고
    • A unified nomenclature for yeast autophagy-related genes
    • 1:CAS:528:DC%2BD3sXotlSqu7o%3D 10.1016/S1534-5807(03)00296-X 14536056
    • Klionsky, D. J., Cregg, J. M., Dunn, W. A., Jr, Emr, S. D., Sakai, Y., Sandoval, I. V., et al. (2003). A unified nomenclature for yeast autophagy-related genes. Developmental Cell, 5, 539-545.
    • (2003) Developmental Cell , vol.5 , pp. 539-545
    • Klionsky, D.J.1    Cregg, J.M.2    Dunn, Jr.W.A.3    Emr, S.D.4    Sakai, Y.5    Sandoval, I.V.6
  • 34
    • 67649861056 scopus 로고    scopus 로고
    • Transgenic mitochondrial superoxide dismutase and mitochondrially targeted catalase prevent antiretroviral-induced oxidative stress and cardiomyopathy
    • 1:CAS:528:DC%2BD1MXnslKgsrc%3D 10.1038/labinvest.2009.39 19398959
    • Kohler, J. J., Cucoranu, I., Fields, E., Green, E., He, S., Hoying, A., et al. (2009). Transgenic mitochondrial superoxide dismutase and mitochondrially targeted catalase prevent antiretroviral-induced oxidative stress and cardiomyopathy. Laboratory Investigation, 89(7), 782-790.
    • (2009) Laboratory Investigation , vol.89 , Issue.7 , pp. 782-790
    • Kohler, J.J.1    Cucoranu, I.2    Fields, E.3    Green, E.4    He, S.5    Hoying, A.6
  • 35
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • 1:CAS:528:DC%2BD28XlvVGlsbY%3D 10.1038/nature04723 16625205
    • Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J., Tanida, I., et al. (2006). Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature, 441, 880-884.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 36
    • 67650517556 scopus 로고    scopus 로고
    • NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets
    • 1:CAS:528:DC%2BC3cXovFykuw%3D%3D 10.4161/cc.8.13.8892 19502794
    • Lamark, T., Kirkin, V., Dikic, I., & Johansen, T. (2009). NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets. Cell Cycle, 8(13), 1986-1990.
    • (2009) Cell Cycle , vol.8 , Issue.13 , pp. 1986-1990
    • Lamark, T.1    Kirkin, V.2    Dikic, I.3    Johansen, T.4
  • 37
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • 1:CAS:528:DC%2BD1cXhtFehtb8%3D 10.1016/j.cell.2007.12.018 2696814 18191218
    • Levine, B., & Kroemer, G. (2008). Autophagy in the pathogenesis of disease. Cell, 132, 27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 38
    • 79951580982 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: Machinery, regulation and biological consequences
    • 1:CAS:528:DC%2BC3MXhvVWhur0%3D 10.1007/s00018-010-0565-6 20976518
    • Li, W., Yang, Q., & Mao, Z. (2011). Chaperone-mediated autophagy: machinery, regulation and biological consequences. Cellular and Molecular Life Sciences, 68, 749-763.
    • (2011) Cellular and Molecular Life Sciences , vol.68 , pp. 749-763
    • Li, W.1    Yang, Q.2    Mao, Z.3
  • 39
    • 2342628596 scopus 로고    scopus 로고
    • Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: Implications for early mitochondrial dysfunction and oxidative damage
    • 1:CAS:528:DC%2BD2cXjvFChsr0%3D 10.1385/NMM:5:2:147 15075441
    • Manczak, M., Park, B. S., Jung, Y., & Reddy, P. H. (2004). Differential expression of oxidative phosphorylation genes in patients with Alzheimer's disease: Implications for early mitochondrial dysfunction and oxidative damage. NeuroMolecular Medicine, 5, 147-162.
    • (2004) NeuroMolecular Medicine , vol.5 , pp. 147-162
    • Manczak, M.1    Park, B.S.2    Jung, Y.3    Reddy, P.H.4
  • 40
    • 0030874251 scopus 로고    scopus 로고
    • Metabolic reduction in the posterior cingulate cortex in very early Alzheimer's disease
    • 1:STN:280:DyaK2szmvFajsw%3D%3D 10.1002/ana.410420114 9225689
    • Minoshima, S., Giordani, B., Berent, S., Frey, K. A., Foster, N. L., & Kuhl, D. E. (1997). Metabolic reduction in the posterior cingulate cortex in very early Alzheimer's disease. Annals of Neurology, 42, 85-94.
    • (1997) Annals of Neurology , vol.42 , pp. 85-94
    • Minoshima, S.1    Giordani, B.2    Berent, S.3    Frey, K.A.4    Foster, N.L.5    Kuhl, D.E.6
  • 42
    • 0035478618 scopus 로고    scopus 로고
    • β-Amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-Terminal kinase pathway and the induction of Fas ligand
    • 1:STN:280:DC%2BD3MritFGlsg%3D%3D 11567045
    • Morishima, Y., Gotoh, Y., Zieg, J., Barrett, T., Takano, H., Flavell, R., et al. (2001). β-Amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-Terminal kinase pathway and the induction of Fas ligand. Journal of Neuroscience, 21(19), 7551-7560.
    • (2001) Journal of Neuroscience , vol.21 , Issue.19 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6    Davis, R.J.7    Shirasaki, Y.8    Greenberg, M.E.9
  • 43
    • 0037010285 scopus 로고    scopus 로고
    • Alzheimer's disease: Beta-Amyloid protein and tau
    • 1:CAS:528:DC%2BD38XosVaqu7g%3D 10.1002/jnr.10355 12391602
    • Morishima-Kawashima, M., & Ihara, Y. (2002). Alzheimer's disease: Beta-Amyloid protein and tau. Journal of Neuroscience Research, 70(3), 392-401.
    • (2002) Journal of Neuroscience Research , vol.70 , Issue.3 , pp. 392-401
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 44
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • 1:CAS:528:DC%2BD2cXpslKjt7k%3D 10.1074/jbc.M407715200 15317809
    • Muller, F. L., Liu, Y., & Van Remmen, H. (2004). Complex III releases superoxide to both sides of the inner mitochondrial membrane. Journal of Biological Chemistry, 279, 49064-49073.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 45
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • 1:CAS:528:DC%2BD1cXhsV2lt77F 10.1042/BJ20081386 2605959 19061483
    • Murphy, M. P. (2009). How mitochondria produce reactive oxygen species. Biochemical Journal, 417(Pt 1), 1-13.
    • (2009) Biochemical Journal , vol.417 , Issue.PART 1 , pp. 1-13
    • Murphy, M.P.1
  • 46
    • 79954577302 scopus 로고    scopus 로고
    • Targeting mitochondrial dysfunction: Role for PINK1 and Parkin in mitochondrial quality control
    • 1:CAS:528:DC%2BC3MXkvVSqsro%3D 10.1089/ars.2010.3799
    • Narendra, D. P., & Youle, R. J. (2011). Targeting mitochondrial dysfunction: Role for PINK1 and Parkin in mitochondrial quality control. Antioxidants & Redox Signaling, 14(10), 1929-1938.
    • (2011) Antioxidants & Redox Signaling , vol.14 , Issue.10 , pp. 1929-1938
    • Narendra, D.P.1    Youle, R.J.2
  • 47
    • 0030052530 scopus 로고    scopus 로고
    • Requirement for superoxide in excitotoxic cell death
    • 1:CAS:528:DyaK28XhtlGhsLc%3D 10.1016/S0896-6273(00)80052-5 8789949
    • Patel, M., Day, B. J., Crapo, J. D., Fridovich, I., & McNamara, J. O. (1996). Requirement for superoxide in excitotoxic cell death. Neuron, 16, 345-355.
    • (1996) Neuron , vol.16 , pp. 345-355
    • Patel, M.1    Day, B.J.2    Crapo, J.D.3    Fridovich, I.4    McNamara, J.O.5
  • 49
    • 0037974679 scopus 로고    scopus 로고
    • Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: Modulation of enzyme activities by MnSOD
    • 1:CAS:528:DC%2BD3sXls1Wmtrc%3D 12665464
    • Powell, C. S., & Jackson, R. M. (2003). Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: Modulation of enzyme activities by MnSOD. American Journal of Physiology, 285(1), L189-L198.
    • (2003) American Journal of Physiology , vol.285 , Issue.1
    • Powell, C.S.1    Jackson, R.M.2
  • 50
    • 84871832322 scopus 로고    scopus 로고
    • Transcriptional regulation by nuclear corepressors and PGC-1α: Implications for mitochondrial quality control and insulin sensitivity
    • 10.1155/2012/348245
    • Qi, Z., & Ding, S. (2012). Transcriptional regulation by nuclear corepressors and PGC-1α: Implications for mitochondrial quality control and insulin sensitivity. PPAR Research, 2012, 1-12.
    • (2012) PPAR Research , vol.2012 , pp. 1-12
    • Qi, Z.1    Ding, S.2
  • 51
    • 0000342177 scopus 로고
    • Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids
    • 1:CAS:528:DyaG3cXitVehsA%3D%3D 10.1016/0006-3002(50)90026-6 15403927
    • Racker, E. (1950). Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids. Biochimica et Biophysica Acta, 4(1-3), 211-214.
    • (1950) Biochimica et Biophysica Acta , vol.4 , Issue.1-3 , pp. 211-214
    • Racker, E.1
  • 53
    • 68149148549 scopus 로고    scopus 로고
    • Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma Cells
    • 1:CAS:528:DC%2BD1MXptFClurw%3D 10.1007/s10571-009-9398-y 19350381
    • Rhein, V., Baysang, G., Rao, S., Meier, F., Bonert, A., Muller-Spahn, F., et al. (2009). Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma Cells. Cellular and Molecular Neurobiology, 29, 1063-1071.
    • (2009) Cellular and Molecular Neurobiology , vol.29 , pp. 1063-1071
    • Rhein, V.1    Baysang, G.2    Rao, S.3    Meier, F.4    Bonert, A.5    Muller-Spahn, F.6
  • 54
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • 1:CAS:528:DC%2BD28XhtVyktbbN 10.1038/nature05291 17051204
    • Rubinsztein, D. C. (2006). The roles of intracellular protein-degradation pathways in neurodegeneration. Nature, 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 55
    • 0025832755 scopus 로고
    • Assessment of the mitochondrial respiratory chain
    • 1:STN:280:DyaK3M3nvVKgsQ%3D%3D 10.1016/0140-6736(91)90057-V 1676118
    • Rustin, P., Chretien, D., Bourgeron, T., Wucher, A., Saudubray, J. M., Rotig, A., et al. (1991). Assessment of the mitochondrial respiratory chain. Lancet, 338, 60.
    • (1991) Lancet , vol.338 , pp. 60
    • Rustin, P.1    Chretien, D.2    Bourgeron, T.3    Wucher, A.4    Saudubray, J.M.5    Rotig, A.6
  • 56
    • 78651423598 scopus 로고    scopus 로고
    • Microautophagy of cytosolic proteins by late endosomes
    • 1:CAS:528:DC%2BC3MXjtFeqtLg%3D 10.1016/j.devcel.2011.02.011
    • Sahu, R., Kaushik, S., Clement, C. C., Cannizzo, E. S., Scharf, B., Follenzi, A., et al. (2011). Microautophagy of cytosolic proteins by late endosomes. Developmental Cell, 20(3), 405-406.
    • (2011) Developmental Cell , vol.20 , Issue.3 , pp. 405-406
    • Sahu, R.1    Kaushik, S.2    Clement, C.C.3    Cannizzo, E.S.4    Scharf, B.5    Follenzi, A.6
  • 59
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • 1:CAS:528:DC%2BD2sXht1ykt7g%3D 10.1021/bi602508x 17274631
    • Sazanov, L. A. (2007). Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry, 46, 2275-2288.
    • (2007) Biochemistry , vol.46 , pp. 2275-2288
    • Sazanov, L.A.1
  • 60
    • 0037036115 scopus 로고    scopus 로고
    • Nuclear activators and coactivators in mammalian mitochondrial biogenesis
    • 1:CAS:528:DC%2BD38XjvVejsrw%3D 10.1016/S0167-4781(02)00343-3 12031478
    • Scarpulla, R. C. (2002). Nuclear activators and coactivators in mammalian mitochondrial biogenesis. Biochimica et Biophysica Acta, 1576(1-2), 1-14.
    • (2002) Biochimica et Biophysica Acta , vol.1576 , Issue.1-2 , pp. 1-14
    • Scarpulla, R.C.1
  • 61
    • 79957960940 scopus 로고    scopus 로고
    • Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network
    • 1:CAS:528:DC%2BC3MXntV2lsL4%3D 10.1016/j.bbamcr.2010.09.019 3035754 20933024
    • Scarpulla, R. C. (2011). Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network. Biochimica et Biophysica Acta, 1813(7), 1269-1278.
    • (2011) Biochimica et Biophysica Acta , vol.1813 , Issue.7 , pp. 1269-1278
    • Scarpulla, R.C.1
  • 62
    • 0015880897 scopus 로고
    • The morphology of various types of cell death in prenatal tissues
    • 1:STN:280:DyaE287jtVCksA%3D%3D 10.1002/tera.1420070306 4807128
    • Schweichel, J. U., & Merker, H. J. (1973). The morphology of various types of cell death in prenatal tissues. Teratology, 7, 253-266.
    • (1973) Teratology , vol.7 , pp. 253-266
    • Schweichel, J.U.1    Merker, H.J.2
  • 63
    • 60349093657 scopus 로고    scopus 로고
    • The role of Abeta-induced calcium dysregulation in the pathogenesis of Alzheimer's disease
    • 1:CAS:528:DC%2BD1MXhvVCku7g%3D
    • Small, D. H., Gasperini, R., Vincent, A. J., Hung, A. C., & Foa, L. (2009). The role of Abeta-induced calcium dysregulation in the pathogenesis of Alzheimer's disease. Journal of Alzheimers Disease, 16, 225-233.
    • (2009) Journal of Alzheimers Disease , vol.16 , pp. 225-233
    • Small, D.H.1    Gasperini, R.2    Vincent, A.J.3    Hung, A.C.4    Foa, L.5
  • 64
    • 0016334871 scopus 로고
    • Controls of citrate synthase. Life
    • 1:CAS:528:DyaE2MXht1SmsL0%3D
    • Srere, P. A. (1974). Controls of citrate synthase. Life. Science, 15, 1695-1710.
    • (1974) Science , vol.15 , pp. 1695-1710
    • Srere, P.A.1
  • 65
    • 0032747486 scopus 로고    scopus 로고
    • Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death
    • 1:CAS:528:DyaK1MXnvVKisrc%3D 10.1016/S0002-9440(10)65460-0 10550301
    • Stadelmann, C., Deckwerth, T. L., Srinivasan, A., Bancher, C., Brück, W., Jellinger, K., et al. (1999). Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death. American Journal of Pathology, 155(5), 1459-1466.
    • (1999) American Journal of Pathology , vol.155 , Issue.5 , pp. 1459-1466
    • Stadelmann, C.1    Deckwerth, T.L.2    Srinivasan, A.3    Bancher, C.4    Brück, W.5    Jellinger, K.6
  • 66
    • 78650328444 scopus 로고    scopus 로고
    • Autophagy basics
    • 1:CAS:528:DC%2BC3MXpslWgtA%3D%3D 10.1111/j.1348-0421.2010.00271.x 21175768
    • Tanida, I. (2011). Autophagy basics. Microbiology and Immunology, 55, 1-11.
    • (2011) Microbiology and Immunology , vol.55 , pp. 1-11
    • Tanida, I.1
  • 69
    • 33749543406 scopus 로고    scopus 로고
    • Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular β-amyloid-induced inhibition of complex IV and limit apoptosis
    • 1:CAS:528:DC%2BD28XhtVahsLbK 10.1074/jbc.M602533200 16887805
    • Veereshwarayya, V., Kumar, P., Rosen, K. M., Mestril, R., & Querfurth, H. W. (2006). Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular β-amyloid-induced inhibition of complex IV and limit apoptosis. Journal of Biological Chemistry, 281, 29468-29478.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 29468-29478
    • Veereshwarayya, V.1    Kumar, P.2    Rosen, K.M.3    Mestril, R.4    Querfurth, H.W.5
  • 70
    • 0036792096 scopus 로고    scopus 로고
    • Amyloid beta-peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling
    • 1:CAS:528:DC%2BD38XnvFGgsr0%3D 10.1073/pnas.172504199
    • Vitolo, O. V., Sant'Angelo, A., Costanzo, V., Battaglia, F., Arancio, O., & Shelanski, M. (2002). Amyloid beta-peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling. Proceedings of the National Academy of Sciences, 99(20), 13217-13221.
    • (2002) Proceedings of the National Academy of Sciences , vol.99 , Issue.20 , pp. 13217-13221
    • Vitolo, O.V.1    Sant'Angelo, A.2    Costanzo, V.3    Battaglia, F.4    Arancio, O.5    Shelanski, M.6
  • 71
    • 81355132716 scopus 로고    scopus 로고
    • Resistance exercise enhances the molecular signaling of mitochondrial biogenesis induced by endurance exercise in human skeletal muscle
    • 1:CAS:528:DC%2BC3MXhsFCmurfN 10.1152/japplphysiol.00086.2011 21836044
    • Wang, L., Mascher, H., Psilander, N., Blomstrand, E., & Sahlin, K. (2011). Resistance exercise enhances the molecular signaling of mitochondrial biogenesis induced by endurance exercise in human skeletal muscle. Journal of Applied Physiology, 111, 1335-1344.
    • (2011) Journal of Applied Physiology , vol.111 , pp. 1335-1344
    • Wang, L.1    Mascher, H.2    Psilander, N.3    Blomstrand, E.4    Sahlin, K.5
  • 72
    • 77951241263 scopus 로고    scopus 로고
    • Cross-talk between mitochondrial malate dehydrogenase and the cytochrome bc1 complex
    • 1:CAS:528:DC%2BC3cXjvFajtLc%3D 10.1074/jbc.M109.085787 20075069
    • Wang, Q., Yu, L., & Yu, C. A. (2010). Cross-talk between mitochondrial malate dehydrogenase and the cytochrome bc1 complex. Journal of Biological Chemistry, 285(14), 10408-10414.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.14 , pp. 10408-10414
    • Wang, Q.1    Yu, L.2    Yu, C.A.3
  • 73
    • 29044443820 scopus 로고    scopus 로고
    • Physicochemical characteristics of soluble oligomeric Aβ and their pathologic role in Alzheimer's disease
    • 1:CAS:528:DC%2BD28Xks1Wkug%3D%3D 10.1179/016164105X49436
    • Watson, D., Castano, E., Kokjohn, T. A., Kuo, Y. M., Lyubchenko, Y., et al. (2005). Physicochemical characteristics of soluble oligomeric Aβ and their pathologic role in Alzheimer's disease. Journal of Neurology Research, 27, 869-881.
    • (2005) Journal of Neurology Research , vol.27 , pp. 869-881
    • Watson, D.1    Castano, E.2    Kokjohn, T.A.3    Kuo, Y.M.4    Lyubchenko, Y.5
  • 74
    • 84875246546 scopus 로고    scopus 로고
    • Regulation of mitochondrial biogenesis and PGC-1α under cellular stress
    • 1:CAS:528:DC%2BC3sXitlams7k%3D 10.1016/j.mito.2013.01.006 23347985
    • Wenz, T. (2013). Regulation of mitochondrial biogenesis and PGC-1α under cellular stress. Mitochondrion, 13(2), 134-142.
    • (2013) Mitochondrion , vol.13 , Issue.2 , pp. 134-142
    • Wenz, T.1
  • 75
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
    • 1:CAS:528:DyaK28Xlt1yltr0%3D 10.1038/382685a0 8751438
    • Yan, S. D., Chen, X., Fu, J., Chen, M., & Zhu, H. (1996). RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease. Nature, 382, 685-691.
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3    Chen, M.4    Zhu, H.5
  • 76
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy - A novel beta-amyloid peptide-generating pathway activated in Alzheimer's disease
    • 1:CAS:528:DC%2BD2MXhtFWitrjI 10.1083/jcb.200505082 16203860
    • Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J. H., et al. (2005). Macroautophagy - A novel beta-amyloid peptide-generating pathway activated in Alzheimer's disease. Journal of Cell Biology, 171(1), 87-98.
    • (2005) Journal of Cell Biology , vol.171 , Issue.1 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3    Peterhoff, C.M.4    Schmidt, S.D.5    Lee, J.H.6
  • 77
    • 77953812778 scopus 로고    scopus 로고
    • AMP-activated protein kinase mediates activity-dependent regulation of peroxisome proliferator-activated receptor gamma coactivator-1alpha and nuclear respiratory factor 1 expression in rat visual cortical neurons
    • 1:CAS:528:DC%2BC3cXnvVOmsr8%3D 10.1016/j.neuroscience.2010.04.063 20438809
    • Yu, L., & Yang, S. J. (2010). AMP-activated protein kinase mediates activity-dependent regulation of peroxisome proliferator-activated receptor gamma coactivator-1alpha and nuclear respiratory factor 1 expression in rat visual cortical neurons. Neuroscience, 169(1), 23-38.
    • (2010) Neuroscience , vol.169 , Issue.1 , pp. 23-38
    • Yu, L.1    Yang, S.J.2
  • 78
    • 0032551697 scopus 로고    scopus 로고
    • Manganese inhibits mitochondrial aconitase: A mechanism of manganese neurotoxicity
    • 1:CAS:528:DyaK1cXksVyru7g%3D 10.1016/S0006-8993(98)00481-8
    • Zheng, W., Ren, S., & Graziano, J. H. (1998). Manganese inhibits mitochondrial aconitase: A mechanism of manganese neurotoxicity. Brain Reseach, 799(2), 334-342.
    • (1998) Brain Reseach , vol.799 , Issue.2 , pp. 334-342
    • Zheng, W.1    Ren, S.2    Graziano, J.H.3
  • 79
    • 84887387419 scopus 로고    scopus 로고
    • After the banquet: Mitochondrial biogenesis, mitophagy and cell survival
    • Zhu, J., Wang, K. Z. Q., & Chu, C. T. (2013). After the banquet: Mitochondrial biogenesis, mitophagy and cell survival. Autophagy, 9(9), 1-14.
    • (2013) Autophagy , vol.9 , Issue.9 , pp. 1-14
    • Zhu, J.1    Wang, K.Z.Q.2    Chu, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.