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Volumn 1847, Issue 11, 2015, Pages 1387-1400

The role of mitochondrial dysfunction in age-related diseases

Author keywords

Aging; Atherosclerosis; Immunity; Mitochondria; Neurodegeneration; Osteoporosis; Sirtuins; Stem cells

Indexed keywords

CARDIOLIPIN; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; PROTEOME; REACTIVE OXYGEN METABOLITE; SIRTUIN;

EID: 84941739003     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2015.05.021     Document Type: Article
Times cited : (171)

References (194)
  • 3
    • 1042301416 scopus 로고    scopus 로고
    • Characterization of superoxide-producing sites in isolated brain mitochondria
    • A.P. Kudin, N.Y. Bimpong-Buta, S. Vielhaber, C.E. Elger, and W.S. Kunz Characterization of superoxide-producing sites in isolated brain mitochondria J. Biol. Chem. 279 2004 4127 4135
    • (2004) J. Biol. Chem. , vol.279 , pp. 4127-4135
    • Kudin, A.P.1    Bimpong-Buta, N.Y.2    Vielhaber, S.3    Elger, C.E.4    Kunz, W.S.5
  • 4
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • J.F. Turrens Mitochondrial formation of reactive oxygen species J. Physiol. 552 2003 335 344
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 5
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • D. Harman The biologic clock: the mitochondria? J. Am. Geriatr. Soc. 20 1972 145 147
    • (1972) J. Am. Geriatr. Soc. , vol.20 , pp. 145-147
    • Harman, D.1
  • 6
    • 0027365312 scopus 로고
    • Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species
    • H.H. Ku, U.T. Brunk, and R.S. Sohal Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species Free Radic. Biol. Med. 15 1993 621 627
    • (1993) Free Radic. Biol. Med. , vol.15 , pp. 621-627
    • Ku, H.H.1    Brunk, U.T.2    Sohal, R.S.3
  • 7
    • 77956185904 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and mammalian healthspan
    • J. Wanagat, D. Dai, and P. Rabinovitch Mitochondrial oxidative stress and mammalian healthspan Mech. Ageing Dev. 131 2010 527 535
    • (2010) Mech. Ageing Dev. , vol.131 , pp. 527-535
    • Wanagat, J.1    Dai, D.2    Rabinovitch, P.3
  • 9
    • 0019186034 scopus 로고
    • Modification of mitochondrial respiration by aging and dietary restriction
    • R.H. Weindruch, M.K. Cheung, M.A. Verity, and R.L. Walford Modification of mitochondrial respiration by aging and dietary restriction Mech. Ageing Dev. 12 1980 375 392
    • (1980) Mech. Ageing Dev. , vol.12 , pp. 375-392
    • Weindruch, R.H.1    Cheung, M.K.2    Verity, M.A.3    Walford, R.L.4
  • 11
    • 84900534961 scopus 로고    scopus 로고
    • The biochemistry and cell biology of aging: Metabolic regulation through mitochondrial signaling
    • Y.C. Long, T.M. Tan, I. Takao, and B.L. Tang The biochemistry and cell biology of aging: metabolic regulation through mitochondrial signaling Am. J. Physiol. Endocrinol. Metab. 306 2014 E581 E591
    • (2014) Am. J. Physiol. Endocrinol. Metab. , vol.306 , pp. E581-E591
    • Long, Y.C.1    Tan, T.M.2    Takao, I.3    Tang, B.L.4
  • 12
    • 84940404091 scopus 로고    scopus 로고
    • Impaired mitophagy leads to cigarette smoke stress-induced cellular senescence: Implications for chronic obstructive pulmonary disease
    • (pii: fj.14-268276, Epub ahead of print)
    • T. Ahmad, I.K. Sundar, C.A. Lerner, J. Gerloff, A.M. Tormos, H. Yao, and I. Rahman Impaired mitophagy leads to cigarette smoke stress-induced cellular senescence: implications for chronic obstructive pulmonary disease FASEB J. 2015 (pii: fj.14-268276, Epub ahead of print)
    • (2015) FASEB J.
    • Ahmad, T.1    Sundar, I.K.2    Lerner, C.A.3    Gerloff, J.4    Tormos, A.M.5    Yao, H.6    Rahman, I.7
  • 13
    • 84896725752 scopus 로고    scopus 로고
    • Oxidative/nitrosative stress and immuno-inflammatory pathways in depression: Treatment implications
    • G. Anderson, and M. Maes Oxidative/nitrosative stress and immuno-inflammatory pathways in depression: treatment implications Curr. Pharm. Des. 20 2014 3812 3847
    • (2014) Curr. Pharm. Des. , vol.20 , pp. 3812-3847
    • Anderson, G.1    Maes, M.2
  • 15
    • 85043221259 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and insulin resistance: An update
    • M.K. Montgomery, and N. Turner Mitochondrial dysfunction and insulin resistance: an update Endocr. Connect. 4 2015 R1 R15
    • (2015) Endocr. Connect. , vol.4 , pp. R1-R15
    • Montgomery, M.K.1    Turner, N.2
  • 16
    • 84871830937 scopus 로고    scopus 로고
    • Intestinal barrier dysfunction links metabolic and inflammatory markers of aging to death in Drosophila
    • M. Rera, R.I. Clark, and D.W. Walker Intestinal barrier dysfunction links metabolic and inflammatory markers of aging to death in Drosophila Proc. Natl. Acad. Sci. U. S. A. 109 2012 21528 21533
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 21528-21533
    • Rera, M.1    Clark, R.I.2    Walker, D.W.3
  • 17
    • 57749092004 scopus 로고    scopus 로고
    • The pathology of atherosclerosis: Plaque development and plaque responses to medical treatment
    • W. Insull The pathology of atherosclerosis: plaque development and plaque responses to medical treatment Am. J. Med. 122 2009 S3 S14
    • (2009) Am. J. Med. , vol.122 , pp. S3-S14
    • Insull, W.1
  • 18
    • 6344285417 scopus 로고    scopus 로고
    • Endothelial cell superoxide generation: Regulation and relevance for cardiovascular pathophysiology
    • J.M. Li, and A.M. Shah Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology Am. J. Physiol. Regul. Integr. Comp. Physiol. 287 2004 R1014 R1030
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.287 , pp. R1014-R1030
    • Li, J.M.1    Shah, A.M.2
  • 19
    • 0035090379 scopus 로고    scopus 로고
    • Retention of oxidized LDL by extracellular matrix proteoglycans leads to its uptake by macrophages: An alternative approach to study lipoproteins cellular uptake
    • M. Kaplan, and M. Aviram Retention of oxidized LDL by extracellular matrix proteoglycans leads to its uptake by macrophages: an alternative approach to study lipoproteins cellular uptake Arterioscler. Thromb. Vasc. Biol. 21 2001 386 393
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 386-393
    • Kaplan, M.1    Aviram, M.2
  • 20
    • 33947512416 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in atherosclerosis
    • N.R. Madamanchi, and M.S. Runge Mitochondrial dysfunction in atherosclerosis Circ. Res. 100 2007 460 473
    • (2007) Circ. Res. , vol.100 , pp. 460-473
    • Madamanchi, N.R.1    Runge, M.S.2
  • 21
    • 0028103803 scopus 로고
    • Expression of heterologous human apolipoprotein e by J774 macrophages enhances cholesterol efflux to HDL3
    • T. Mazzone, and C. Reardon Expression of heterologous human apolipoprotein E by J774 macrophages enhances cholesterol efflux to HDL3 J. Lipid Res. 35 1994 1345 1353
    • (1994) J. Lipid Res. , vol.35 , pp. 1345-1353
    • Mazzone, T.1    Reardon, C.2
  • 22
    • 1942428112 scopus 로고    scopus 로고
    • Reverse cholesterol transport: High-density lipoprotein's magnificent mile
    • P.P. Toth Reverse cholesterol transport: high-density lipoprotein's magnificent mile Curr. Atheroscler. Rep. 5 2003 386 393
    • (2003) Curr. Atheroscler. Rep. , vol.5 , pp. 386-393
    • Toth, P.P.1
  • 23
    • 0023664723 scopus 로고
    • The role of sulfur-containing amino acids in superoxide production and modification of low density lipoprotein by arterial smooth muscle cells
    • J.W. Heinecke, H. Rosen, L.A. Suzuki, and A. Chait The role of sulfur-containing amino acids in superoxide production and modification of low density lipoprotein by arterial smooth muscle cells J. Biol. Chem. 262 1987 10098 10103
    • (1987) J. Biol. Chem. , vol.262 , pp. 10098-10103
    • Heinecke, J.W.1    Rosen, H.2    Suzuki, L.A.3    Chait, A.4
  • 24
    • 79955873404 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress significantly influences atherogenic risk and cytokine-induced oxidant production
    • C.M. Harrison, M. Pompilius, K.E. Pinkerton, and S.W. Ballinger Mitochondrial oxidative stress significantly influences atherogenic risk and cytokine-induced oxidant production Environ. Health Perspect. 119 2011 676 681
    • (2011) Environ. Health Perspect. , vol.119 , pp. 676-681
    • Harrison, C.M.1    Pompilius, M.2    Pinkerton, K.E.3    Ballinger, S.W.4
  • 26
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 28
    • 84907356094 scopus 로고    scopus 로고
    • LOX-1, mtDNA damage, and NLRP3 inflammasome activation in macrophages: Implications in atherogenesis
    • Z. Ding, S. Liu, X. Wang, Y. Dai, M. Khaidakov, X. Deng, Y. Fan, D. Xiang, and J.L. Mehta LOX-1, mtDNA damage, and NLRP3 inflammasome activation in macrophages: implications in atherogenesis Cardiovasc. Res. 103 2014 619 628
    • (2014) Cardiovasc. Res. , vol.103 , pp. 619-628
    • Ding, Z.1    Liu, S.2    Wang, X.3    Dai, Y.4    Khaidakov, M.5    Deng, X.6    Fan, Y.7    Xiang, D.8    Mehta, J.L.9
  • 30
    • 84862242000 scopus 로고    scopus 로고
    • The stability and activity of respiratory Complex II is cardiolipin-dependent
    • C.T. Schwall, V.L. Greenwood, and N.N. Alder The stability and activity of respiratory Complex II is cardiolipin-dependent Biochim. Biophys. Acta 1817 2012 1588 1596
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1588-1596
    • Schwall, C.T.1    Greenwood, V.L.2    Alder, N.N.3
  • 31
    • 0033984710 scopus 로고    scopus 로고
    • The effect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles
    • G. Paradies, G. Petrosillo, M. Pistolese, and F.M. Ruggiero The effect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles FEBS Lett. 466 2000 323 326
    • (2000) FEBS Lett. , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 35
    • 0019614894 scopus 로고
    • Ratio of central nervous system to body metabolism in vertebrates: Its constancy and functional basis
    • J.W. Mink, R.J. Blumenschine, and D.B. Adams Ratio of central nervous system to body metabolism in vertebrates: its constancy and functional basis Am. J. Physiol. 241 1981 R203 R212
    • (1981) Am. J. Physiol. , vol.241 , pp. R203-R212
    • Mink, J.W.1    Blumenschine, R.J.2    Adams, D.B.3
  • 36
    • 67349249403 scopus 로고    scopus 로고
    • The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1
    • A. Herrero-Mendez, A. Almeida, E. Fernández, C. Maestre, S. Moncada, and J.P. Bolaños The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1 Nat. Cell Biol. 11 2009 747 752
    • (2009) Nat. Cell Biol. , vol.11 , pp. 747-752
    • Herrero-Mendez, A.1    Almeida, A.2    Fernández, E.3    Maestre, C.4    Moncada, S.5    Bolaños, J.P.6
  • 39
    • 84907563036 scopus 로고    scopus 로고
    • Mitochondria-derived reactive oxygen species mediate caspase-dependent and -independent neuronal deaths
    • M.J. McManus, M.P. Murphy, and J.L. Franklin Mitochondria-derived reactive oxygen species mediate caspase-dependent and -independent neuronal deaths Mol. Cell. Neurosci. 63c 2014 13 23
    • (2014) Mol. Cell. Neurosci. , vol.63 C , pp. 13-23
    • McManus, M.J.1    Murphy, M.P.2    Franklin, J.L.3
  • 42
    • 0037314215 scopus 로고    scopus 로고
    • Neuronal degeneration and mitochondrial dysfunction
    • E.A. Schon, and G. Manfredi Neuronal degeneration and mitochondrial dysfunction J. Clin. Invest. 111 2003 303 312
    • (2003) J. Clin. Invest. , vol.111 , pp. 303-312
    • Schon, E.A.1    Manfredi, G.2
  • 43
    • 77956224679 scopus 로고    scopus 로고
    • The Alzheimer's disease mitochondrial cascade hypothesis
    • R.H. Swerdlow, J.M. Burns, and S.M. Khan The Alzheimer's disease mitochondrial cascade hypothesis J. Alzheimers Dis. 20 Suppl. 2 2010 S265 S279
    • (2010) J. Alzheimers Dis. , vol.20 , pp. S265-S279
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 44
    • 33750683018 scopus 로고    scopus 로고
    • Alzheimer's APP mangles mitochondria
    • M.T. Lin, and M.F. Beal Alzheimer's APP mangles mitochondria Nat Med, United States 2006 1241 1243
    • (2006) Nat Med, United States , pp. 1241-1243
    • Lin, M.T.1    Beal, M.F.2
  • 45
    • 79251584617 scopus 로고    scopus 로고
    • Mitochondrial γ-secretase participates in the metabolism of mitochondria-associated amyloid precursor protein
    • P.F. Pavlov, B. Wiehager, J. Sakai, S. Frykman, H. Behbahani, B. Winblad, and M. Ankarcrona Mitochondrial γ-secretase participates in the metabolism of mitochondria-associated amyloid precursor protein FASEB J. 25 2011 78 88
    • (2011) FASEB J. , vol.25 , pp. 78-88
    • Pavlov, P.F.1    Wiehager, B.2    Sakai, J.3    Frykman, S.4    Behbahani, H.5    Winblad, B.6    Ankarcrona, M.7
  • 46
    • 84901828447 scopus 로고    scopus 로고
    • Mitochondrial import and degradation of amyloid-β peptide
    • C.M. Pinho, P.F. Teixeira, and E. Glaser Mitochondrial import and degradation of amyloid-β peptide Biochim. Biophys. Acta 1837 2014 1069 1074
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 1069-1074
    • Pinho, C.M.1    Teixeira, P.F.2    Glaser, E.3
  • 47
    • 77956199031 scopus 로고    scopus 로고
    • A synergistic dysfunction of mitochondrial fission/fusion dynamics and mitophagy in Alzheimer's disease
    • R.X. Santos, S.C. Correia, X. Wang, G. Perry, M.A. Smith, P.I. Moreira, and X. Zhu A synergistic dysfunction of mitochondrial fission/fusion dynamics and mitophagy in Alzheimer's disease J. Alzheimers Dis. 20 Suppl. 2 2010 S401 S412
    • (2010) J. Alzheimers Dis. , vol.20 , pp. S401-S412
    • Santos, R.X.1    Correia, S.C.2    Wang, X.3    Perry, G.4    Smith, M.A.5    Moreira, P.I.6    Zhu, X.7
  • 51
    • 84865187620 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • A. Johri, and M.F. Beal Mitochondrial dysfunction in neurodegenerative diseases J. Pharmacol. Exp. Ther. 342 2012 619 630
    • (2012) J. Pharmacol. Exp. Ther. , vol.342 , pp. 619-630
    • Johri, A.1    Beal, M.F.2
  • 53
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis
    • D. Praticò, K. Uryu, S. Leight, J.Q. Trojanoswki, and V.M. Lee Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis J. Neurosci. 21 2001 4183 4187
    • (2001) J. Neurosci. , vol.21 , pp. 4183-4187
    • Praticò, D.1    Uryu, K.2    Leight, S.3    Trojanoswki, J.Q.4    Lee, V.M.5
  • 55
    • 0345701340 scopus 로고    scopus 로고
    • Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells
    • A. Gómez-Ramos, J. Díaz-Nido, M.A. Smith, G. Perry, and J. Avila Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells J. Neurosci. Res. 71 2003 863 870
    • (2003) J. Neurosci. Res. , vol.71 , pp. 863-870
    • Gómez-Ramos, A.1    Díaz-Nido, J.2    Smith, M.A.3    Perry, G.4    Avila, J.5
  • 56
    • 0034643895 scopus 로고    scopus 로고
    • Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells
    • H. Misonou, M. Morishima-Kawashima, and Y. Ihara Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells Biochemistry 39 2000 6951 6959
    • (2000) Biochemistry , vol.39 , pp. 6951-6959
    • Misonou, H.1    Morishima-Kawashima, M.2    Ihara, Y.3
  • 58
    • 0030016323 scopus 로고    scopus 로고
    • Increased risk of dementia in mothers of Alzheimer's disease cases: Evidence for maternal inheritance
    • S.D. Edland, J.M. Silverman, E.R. Peskind, D. Tsuang, E. Wijsman, and J.C. Morris Increased risk of dementia in mothers of Alzheimer's disease cases: evidence for maternal inheritance Neurology 47 1996 254 256
    • (1996) Neurology , vol.47 , pp. 254-256
    • Edland, S.D.1    Silverman, J.M.2    Peskind, E.R.3    Tsuang, D.4    Wijsman, E.5    Morris, J.C.6
  • 60
    • 3242668604 scopus 로고    scopus 로고
    • Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication
    • P.E. Coskun, M.F. Beal, and D.C. Wallace Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication Proc. Natl. Acad. Sci. U. S. A. 101 2004 10726 10731
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10726-10731
    • Coskun, P.E.1    Beal, M.F.2    Wallace, D.C.3
  • 62
    • 84922787347 scopus 로고    scopus 로고
    • Alzheimer's disease is associated with altered expression of genes involved in immune response and mitochondrial processes in astrocytes
    • S. Sekar, J. McDonald, L. Cuyugan, J. Aldrich, A. Kurdoglu, J. Adkins, and et al. Alzheimer's disease is associated with altered expression of genes involved in immune response and mitochondrial processes in astrocytes Neurobiol. Aging 36 2 2015 583 591
    • (2015) Neurobiol. Aging , vol.36 , Issue.2 , pp. 583-591
    • Sekar, S.1    McDonald, J.2    Cuyugan, L.3    Aldrich, J.4    Kurdoglu, A.5    Adkins, J.6
  • 63
    • 79955035120 scopus 로고    scopus 로고
    • Pseudogenes: Pseudo-functional or key regulators in health and disease?
    • R.C. Pink, K. Wicks, D.P. Caley, E.K. Punch, L. Jacobs, and D.R. Carter Pseudogenes: pseudo-functional or key regulators in health and disease? RNA 17 2011 792 798
    • (2011) RNA , vol.17 , pp. 792-798
    • Pink, R.C.1    Wicks, K.2    Caley, D.P.3    Punch, E.K.4    Jacobs, L.5    Carter, D.R.6
  • 64
    • 84888179383 scopus 로고    scopus 로고
    • Pseudogenes and their composers: Delving in the 'debris' of human genome
    • K. Sen, and T.C. Ghosh Pseudogenes and their composers: delving in the 'debris' of human genome Brief. Funct. Genomics 12 2013 536 547
    • (2013) Brief. Funct. Genomics , vol.12 , pp. 536-547
    • Sen, K.1    Ghosh, T.C.2
  • 66
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • J. Yao, R.W. Irwin, L. Zhao, J. Nilsen, R.T. Hamilton, and R.D. Brinton Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease Proc. Natl. Acad. Sci. U. S. A. 106 2009 14670 14675
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 68
    • 84893981123 scopus 로고    scopus 로고
    • Reduced levels of mitochondrial complex i subunit NDUFB8 and linked complex i + III oxidoreductase activity in the TgCRND8 mouse model of Alzheimer's disease
    • B.M. Francis, J. Yang, B.J. Song, S. Gupta, M. Maj, R.P. Bazinet, B. Robinson, and H.T. Mount Reduced levels of mitochondrial complex I subunit NDUFB8 and linked complex I + III oxidoreductase activity in the TgCRND8 mouse model of Alzheimer's disease J. Alzheimers Dis. 39 2014 347 355
    • (2014) J. Alzheimers Dis. , vol.39 , pp. 347-355
    • Francis, B.M.1    Yang, J.2    Song, B.J.3    Gupta, S.4    Maj, M.5    Bazinet, R.P.6    Robinson, B.7    Mount, H.T.8
  • 69
    • 70349422148 scopus 로고    scopus 로고
    • Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease
    • R.A. Quintanilla, and G.V. Johnson Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease Brain Res. Bull. 80 2009 242 247
    • (2009) Brain Res. Bull. , vol.80 , pp. 242-247
    • Quintanilla, R.A.1    Johnson, G.V.2
  • 70
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • L. Cui, H. Jeong, F. Borovecki, C.N. Parkhurst, N. Tanese, and D. Krainc Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration Cell 127 2006 59 69
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 71
    • 84893109080 scopus 로고    scopus 로고
    • A role for peroxisome proliferator-activated receptor γ coactivator 1 (PGC-1) in the regulation of cardiac mitochondrial phospholipid biosynthesis
    • L. Lai, M. Wang, O.J. Martin, T.C. Leone, R.B. Vega, X. Han, and D.P. Kelly A role for peroxisome proliferator-activated receptor γ coactivator 1 (PGC-1) in the regulation of cardiac mitochondrial phospholipid biosynthesis J. Biol. Chem. 289 2014 2250 2259
    • (2014) J. Biol. Chem. , vol.289 , pp. 2250-2259
    • Lai, L.1    Wang, M.2    Martin, O.J.3    Leone, T.C.4    Vega, R.B.5    Han, X.6    Kelly, D.P.7
  • 73
    • 57649210194 scopus 로고    scopus 로고
    • Impairing the mitochondrial fission and fusion balance: A new mechanism of neurodegeneration
    • A.B. Knott, and E. Bossy-Wetzel Impairing the mitochondrial fission and fusion balance: a new mechanism of neurodegeneration Ann. N. Y. Acad. Sci. 1147 2008 283 292
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 283-292
    • Knott, A.B.1    Bossy-Wetzel, E.2
  • 76
    • 33845933438 scopus 로고    scopus 로고
    • Mutant huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: Functional consequences
    • T. Milakovic, R.A. Quintanilla, and G.V. Johnson Mutant huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: functional consequences J. Biol. Chem. 281 2006 34785 34795
    • (2006) J. Biol. Chem. , vol.281 , pp. 34785-34795
    • Milakovic, T.1    Quintanilla, R.A.2    Johnson, G.V.3
  • 77
    • 33646136884 scopus 로고    scopus 로고
    • Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
    • D.T. Chang, G.L. Rintoul, S. Pandipati, and I.J. Reynolds Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons Neurobiol. Dis. 22 2006 388 400
    • (2006) Neurobiol. Dis. , vol.22 , pp. 388-400
    • Chang, D.T.1    Rintoul, G.L.2    Pandipati, S.3    Reynolds, I.J.4
  • 79
    • 29144468251 scopus 로고    scopus 로고
    • 3-Nitropropionic acid: A mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease
    • E. Brouillet, C. Jacquard, N. Bizat, and D. Blum 3-Nitropropionic acid: a mitochondrial toxin to uncover physiopathological mechanisms underlying striatal degeneration in Huntington's disease J. Neurochem. 95 2005 1521 1540
    • (2005) J. Neurochem. , vol.95 , pp. 1521-1540
    • Brouillet, E.1    Jacquard, C.2    Bizat, N.3    Blum, D.4
  • 82
    • 84884889978 scopus 로고    scopus 로고
    • Reprint of: Revisiting oxidative stress and mitochondrial dysfunction in the pathogenesis of Parkinson disease - Resemblance to the effect of amphetamine drugs of abuse
    • R. Perfeito, T. Cunha-Oliveira, and A.C. Rego Reprint of: revisiting oxidative stress and mitochondrial dysfunction in the pathogenesis of Parkinson disease - resemblance to the effect of amphetamine drugs of abuse Free Radic. Biol. Med. 62 2013 186 201
    • (2013) Free Radic. Biol. Med. , vol.62 , pp. 186-201
    • Perfeito, R.1    Cunha-Oliveira, T.2    Rego, A.C.3
  • 83
    • 71849084134 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • K.F. Winklhofer, and C. Haass Mitochondrial dysfunction in Parkinson's disease Biochim. Biophys. Acta 1802 2010 29 44
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 29-44
    • Winklhofer, K.F.1    Haass, C.2
  • 84
    • 79952164540 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease: Pathogenesis and neuroprotection
    • R.B. Mounsey, and P. Teismann Mitochondrial dysfunction in Parkinson's disease: pathogenesis and neuroprotection Park. Dis. 2011 2010 617472
    • (2010) Park. Dis. , vol.2011 , pp. 617472
    • Mounsey, R.B.1    Teismann, P.2
  • 85
    • 0037085288 scopus 로고    scopus 로고
    • Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors
    • H.J. Lee, S.Y. Shin, C. Choi, Y.H. Lee, and S.J. Lee Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors J. Biol. Chem. 277 2002 5411 5417
    • (2002) J. Biol. Chem. , vol.277 , pp. 5411-5417
    • Lee, H.J.1    Shin, S.Y.2    Choi, C.3    Lee, Y.H.4    Lee, S.J.5
  • 89
    • 55949128232 scopus 로고    scopus 로고
    • Emerging pathways in genetic Parkinson's disease: Autosomal-recessive genes in Parkinson's disease - A common pathway?
    • J.C. Fitzgerald, and H. Plun-Favreau Emerging pathways in genetic Parkinson's disease: autosomal-recessive genes in Parkinson's disease - a common pathway? FEBS J. 275 2008 5758 5766
    • (2008) FEBS J. , vol.275 , pp. 5758-5766
    • Fitzgerald, J.C.1    Plun-Favreau, H.2
  • 90
    • 84928499061 scopus 로고    scopus 로고
    • Parkinson's disease-implicated kinases in the brain; Insights into disease pathogenesis
    • N. Dzamko, J. Zhou, Y. Huang, and G.M. Halliday Parkinson's disease-implicated kinases in the brain; insights into disease pathogenesis Front. Mol. Neurosci. 7 2014 57
    • (2014) Front. Mol. Neurosci. , vol.7 , pp. 57
    • Dzamko, N.1    Zhou, J.2    Huang, Y.3    Halliday, G.M.4
  • 91
    • 77953682220 scopus 로고    scopus 로고
    • In a flurry of PINK, mitochondrial bioenergetics takes a leading role in Parkinson's disease
    • A.N. Murphy In a flurry of PINK, mitochondrial bioenergetics takes a leading role in Parkinson's disease EMBO Mol. Med. 1 2009 81 84
    • (2009) EMBO Mol. Med. , vol.1 , pp. 81-84
    • Murphy, A.N.1
  • 92
    • 2342431848 scopus 로고    scopus 로고
    • Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex i
    • C. Batandier, X. Leverve, and E. Fontaine Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I J. Biol. Chem. 279 2004 17197 17204
    • (2004) J. Biol. Chem. , vol.279 , pp. 17197-17204
    • Batandier, C.1    Leverve, X.2    Fontaine, E.3
  • 94
    • 33750350994 scopus 로고    scopus 로고
    • The role of protein aggregates in neuronal pathology: Guilty, innocent, or just trying to help?
    • S. Gispert-Sanchez, and G. Auburger The role of protein aggregates in neuronal pathology: guilty, innocent, or just trying to help? J. Neural Transm. Suppl. 70 2006 111 117
    • (2006) J. Neural Transm. Suppl. , vol.70 , pp. 111-117
    • Gispert-Sanchez, S.1    Auburger, G.2
  • 95
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • A.P. Pawar, K.F. Dubay, J. Zurdo, F. Chiti, M. Vendruscolo, and C.M. Dobson Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases J. Mol. Biol. 350 2005 379 392
    • (2005) J. Mol. Biol. , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 97
    • 0025770410 scopus 로고
    • Understanding osteoporosis
    • R. Marcus Understanding osteoporosis West. J. Med. 155 1991 53 60
    • (1991) West. J. Med. , vol.155 , pp. 53-60
    • Marcus, R.1
  • 98
    • 84908413236 scopus 로고    scopus 로고
    • Oxidative damage to osteoblasts can be alleviated by early autophagy through the endoplasmic reticulum stress pathway - Implications for the treatment of osteoporosis
    • Y.H. Yang, B. Li, X.F. Zheng, J.W. Chen, K. Chen, S.D. Jiang, and L.S. Jiang Oxidative damage to osteoblasts can be alleviated by early autophagy through the endoplasmic reticulum stress pathway - implications for the treatment of osteoporosis Free Radic. Biol. Med. 77 2014 10 20
    • (2014) Free Radic. Biol. Med. , vol.77 , pp. 10-20
    • Yang, Y.H.1    Li, B.2    Zheng, X.F.3    Chen, J.W.4    Chen, K.5    Jiang, S.D.6    Jiang, L.S.7
  • 102
    • 0031002026 scopus 로고    scopus 로고
    • Removal of osteoclast bone resorption products by transcytosis
    • J. Salo, P. Lehenkari, M. Mulari, K. Metsikko, and H.K. Vaananen Removal of osteoclast bone resorption products by transcytosis Science 276 1997 270 273
    • (1997) Science , vol.276 , pp. 270-273
    • Salo, J.1    Lehenkari, P.2    Mulari, M.3    Metsikko, K.4    Vaananen, H.K.5
  • 104
    • 0037673933 scopus 로고    scopus 로고
    • Control of osteoblast function and regulation of bone mass
    • S. Harada, and G.A. Rodan Control of osteoblast function and regulation of bone mass Nature 423 2003 349
    • (2003) Nature , vol.423 , pp. 349
    • Harada, S.1    Rodan, G.A.2
  • 105
    • 0022496620 scopus 로고
    • A three-dimensional ultrastructural study of osteoid-osteocytes in the tibia of chick embryos
    • C. Palumbo A three-dimensional ultrastructural study of osteoid-osteocytes in the tibia of chick embryos Cell Tissue Res. 246 1986 125 131
    • (1986) Cell Tissue Res. , vol.246 , pp. 125-131
    • Palumbo, C.1
  • 107
    • 0027199847 scopus 로고
    • Osteocytes, strain detection, bone modeling, and remodeling
    • L.E. Lanyon Osteocytes, strain detection, bone modeling, and remodeling Calcif. Tissue Int. 53 1993 S102 S107
    • (1993) Calcif. Tissue Int. , vol.53 , pp. S102-S107
    • Lanyon, L.E.1
  • 108
    • 0017642753 scopus 로고
    • The cellular basis of bone turnover and bone loss: A rebuttal of the osteocytic resorption - Bone flow theory
    • A.M. Parfitt The cellular basis of bone turnover and bone loss: a rebuttal of the osteocytic resorption - bone flow theory Clin. Orthop. Relat. Res. 1977 236 247
    • (1977) Clin. Orthop. Relat. Res. , pp. 236-247
    • Parfitt, A.M.1
  • 110
    • 84877354864 scopus 로고    scopus 로고
    • A novel role for the mitochondrial HTRA2/OMI protease in aging
    • S. Kang, T. Fernandes-Alnemri, and E.S. Alnemri A novel role for the mitochondrial HTRA2/OMI protease in aging Autophagy 9 2013 420 421
    • (2013) Autophagy , vol.9 , pp. 420-421
    • Kang, S.1    Fernandes-Alnemri, T.2    Alnemri, E.S.3
  • 112
    • 2642580016 scopus 로고    scopus 로고
    • Premature ageing in mice expressing defective mitochondrial DNA polymerase
    • A. Trifunovic, A. Wredenberg, M. Falkenberg, J.N. Spelbrink, and et al. Premature ageing in mice expressing defective mitochondrial DNA polymerase Nature 429 2004 417
    • (2004) Nature , vol.429 , pp. 417
    • Trifunovic, A.1    Wredenberg, A.2    Falkenberg, M.3    Spelbrink, J.N.4
  • 113
    • 0032865235 scopus 로고    scopus 로고
    • Mitochondrial DNA deletion associated oxidative stress and severe male osteoporosis
    • S.S. Varanasi, R.M. Francis, C.E. Berger, S.S. Papiha, and H.K. Datta Mitochondrial DNA deletion associated oxidative stress and severe male osteoporosis Osteoporos. Int. 10 1999 143 149
    • (1999) Osteoporos. Int. , vol.10 , pp. 143-149
    • Varanasi, S.S.1    Francis, R.M.2    Berger, C.E.3    Papiha, S.S.4    Datta, H.K.5
  • 114
    • 38349108752 scopus 로고    scopus 로고
    • Mitochondrial dysfunction as a cause of ageing
    • A. Trifunovic, and N.G. Larsson Mitochondrial dysfunction as a cause of ageing J. Intern. Med. 263 2008 167 178
    • (2008) J. Intern. Med. , vol.263 , pp. 167-178
    • Trifunovic, A.1    Larsson, N.G.2
  • 115
    • 75149129597 scopus 로고    scopus 로고
    • From estrogen-centric to aging and oxidative stress: A revised perspective of the pathogenesis of osteoporosis
    • S.C. Manolagas From estrogen-centric to aging and oxidative stress: a revised perspective of the pathogenesis of osteoporosis Endocr. Rev. 31 2010 266 300
    • (2010) Endocr. Rev. , vol.31 , pp. 266-300
    • Manolagas, S.C.1
  • 117
    • 22744447211 scopus 로고    scopus 로고
    • Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis
    • M. Giorgio, E. Migliaccio, F. Orsini, D. Paolucci, M. Moroni, C. Contursi, and et al. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis Cell 122 2 2005 221 233
    • (2005) Cell , vol.122 , Issue.2 , pp. 221-233
    • Giorgio, M.1    Migliaccio, E.2    Orsini, F.3    Paolucci, D.4    Moroni, M.5    Contursi, C.6
  • 120
    • 26444540441 scopus 로고    scopus 로고
    • Cholestane-3beta,5alpha,6beta-triol inhibits osteoblastic differentiation and promotes apoptosis of rat bone marrow stromal cells
    • H. Liu, L. Yuan, S. Xu, K. Wang, and T. Zhang Cholestane-3beta,5alpha,6beta-triol inhibits osteoblastic differentiation and promotes apoptosis of rat bone marrow stromal cells J. Cell. Biochem. 96 2005 198 208
    • (2005) J. Cell. Biochem. , vol.96 , pp. 198-208
    • Liu, H.1    Yuan, L.2    Xu, S.3    Wang, K.4    Zhang, T.5
  • 121
    • 84907518698 scopus 로고    scopus 로고
    • Adult stem cells and diseases of aging
    • L.B. Boyette, and R.S. Tuan Adult stem cells and diseases of aging J. Clin. Med. 3 2014 88 134
    • (2014) J. Clin. Med. , vol.3 , pp. 88-134
    • Boyette, L.B.1    Tuan, R.S.2
  • 122
    • 84896284170 scopus 로고    scopus 로고
    • Senescence in adipose-derived stem cells and its implications in nerve regeneration
    • C. Mantovani, G. Terenghi, and V. Magnaghi Senescence in adipose-derived stem cells and its implications in nerve regeneration Neural Regen. Res. 9 2014 10 15
    • (2014) Neural Regen. Res. , vol.9 , pp. 10-15
    • Mantovani, C.1    Terenghi, G.2    Magnaghi, V.3
  • 124
    • 84895788635 scopus 로고    scopus 로고
    • Human stem cell aging: Do mitochondrial DNA mutations have a causal role?
    • H.L. Baines, D.M. Turnbull, and L.C. Greaves Human stem cell aging: do mitochondrial DNA mutations have a causal role? Aging Cell 13 2014 201 205
    • (2014) Aging Cell , vol.13 , pp. 201-205
    • Baines, H.L.1    Turnbull, D.M.2    Greaves, L.C.3
  • 126
    • 84863102605 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein, stem cells, and atherosclerosis
    • H. Yang, A.S. Mohamed, and S.H. Zhou Oxidized low density lipoprotein, stem cells, and atherosclerosis Lipids Health Dis. 11 2012 85
    • (2012) Lipids Health Dis. , vol.11 , pp. 85
    • Yang, H.1    Mohamed, A.S.2    Zhou, S.H.3
  • 129
    • 79955698235 scopus 로고    scopus 로고
    • Accumulating mitochondrial DNA mutations drive premature hematopoietic aging phenotypes distinct from physiological stem cell aging
    • G.L. Norddahl, C.J. Pronk, M. Wahlestedt, G. Sten, J.M. Nygren, A. Ugale, M. Sigvardsson, and D. Bryder Accumulating mitochondrial DNA mutations drive premature hematopoietic aging phenotypes distinct from physiological stem cell aging Cell Stem Cell 8 2011 499 510
    • (2011) Cell Stem Cell , vol.8 , pp. 499-510
    • Norddahl, G.L.1    Pronk, C.J.2    Wahlestedt, M.3    Sten, G.4    Nygren, J.M.5    Ugale, A.6    Sigvardsson, M.7    Bryder, D.8
  • 130
    • 84882690377 scopus 로고    scopus 로고
    • Mitochondria localize to the cleavage furrow in mammalian cytokinesis
    • E.J. Lawrence, and C.A. Mandato Mitochondria localize to the cleavage furrow in mammalian cytokinesis PLoS One 8 2013 e72886
    • (2013) PLoS One , vol.8 , pp. e72886
    • Lawrence, E.J.1    Mandato, C.A.2
  • 131
    • 84910141948 scopus 로고    scopus 로고
    • Mitochondrial dynamics and inheritance during cell division, development and disease
    • P. Mishra, and D.C. Chan Mitochondrial dynamics and inheritance during cell division, development and disease Nat. Rev. Mol. Cell Biol. 15 2014 634 646
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 634-646
    • Mishra, P.1    Chan, D.C.2
  • 134
    • 84896306292 scopus 로고    scopus 로고
    • Mitochondrial function in pluripotent stem cells and cellular reprogramming
    • R. Bukowiecki, J. Adjaye, and A. Prigione Mitochondrial function in pluripotent stem cells and cellular reprogramming Gerontology 60 2014 174 182
    • (2014) Gerontology , vol.60 , pp. 174-182
    • Bukowiecki, R.1    Adjaye, J.2    Prigione, A.3
  • 136
    • 84872194038 scopus 로고    scopus 로고
    • Human embryonic stem cells commonly display large mitochondrial DNA deletions
    • L.V. Haute, C. Spits, M. Geens, S. Seneca, and K. Sermon Human embryonic stem cells commonly display large mitochondrial DNA deletions Nat. Biotechnol. 31 2013 20 23
    • (2013) Nat. Biotechnol. , vol.31 , pp. 20-23
    • Haute, L.V.1    Spits, C.2    Geens, M.3    Seneca, S.4    Sermon, K.5
  • 137
    • 84892492848 scopus 로고    scopus 로고
    • The aging signature: A hallmark of induced pluripotent stem cells?
    • L. Rohani, A.A. Johnson, A. Arnold, and A. Stolzing The aging signature: a hallmark of induced pluripotent stem cells? Aging Cell 13 2014 2 7
    • (2014) Aging Cell , vol.13 , pp. 2-7
    • Rohani, L.1    Johnson, A.A.2    Arnold, A.3    Stolzing, A.4
  • 140
    • 84896929687 scopus 로고    scopus 로고
    • Metabolic requirements for the maintenance of self-renewing stem cells
    • K. Ito, and T. Suda Metabolic requirements for the maintenance of self-renewing stem cells Nat. Rev. Mol. Cell Biol. 15 2014 243 256
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 243-256
    • Ito, K.1    Suda, T.2
  • 141
  • 142
    • 57649134966 scopus 로고    scopus 로고
    • Mitochondrial metabolism modulates differentiation and teratoma formation capacity in mouse embryonic stem cells
    • S.M. Schieke, M. Ma, L. Cao, J.P. McCoy Jr., C. Liu, N.F. Hensel, A.J. Barrett, M. Boehm, and T. Finkel Mitochondrial metabolism modulates differentiation and teratoma formation capacity in mouse embryonic stem cells J. Biol. Chem. 283 2008 28506 28512
    • (2008) J. Biol. Chem. , vol.283 , pp. 28506-28512
    • Schieke, S.M.1    Ma, M.2    Cao, L.3    McCoy, J.P.4    Liu, C.5    Hensel, N.F.6    Barrett, A.J.7    Boehm, M.8    Finkel, T.9
  • 143
    • 27744563079 scopus 로고    scopus 로고
    • The expression of mitochondrial DNA transcription factors during early cardiomyocyte in vitro differentiation from human embryonic stem cells
    • J.C. St John, J. Ramalho-Santos, H.L. Gray, P. Petrosko, V.Y. Rawe, C.S. Navara, C.R. Simerly, and G.P. Schatten The expression of mitochondrial DNA transcription factors during early cardiomyocyte in vitro differentiation from human embryonic stem cells Cloning Stem Cells 7 2005 141 153
    • (2005) Cloning Stem Cells , vol.7 , pp. 141-153
    • John, J.C.S.1    Ramalho-Santos, J.2    Gray, H.L.3    Petrosko, P.4    Rawe, V.Y.5    Navara, C.S.6    Simerly, C.R.7    Schatten, G.P.8
  • 144
    • 70349446465 scopus 로고    scopus 로고
    • Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation
    • E. Owusu-Ansah, and U. Banerjee Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation Nature 461 2009 537 541
    • (2009) Nature , vol.461 , pp. 537-541
    • Owusu-Ansah, E.1    Banerjee, U.2
  • 145
    • 84903449524 scopus 로고    scopus 로고
    • Interaction between ROS dependent DNA damage, mitochondria and p38 MAPK underlies senescence of human adult stem cells
    • A. Borodkina, A. Shatrova, P. Abushik, N. Nikolsky, and E. Burova Interaction between ROS dependent DNA damage, mitochondria and p38 MAPK underlies senescence of human adult stem cells Aging (Albany NY) 6 2014 481 495
    • (2014) Aging (Albany NY) , vol.6 , pp. 481-495
    • Borodkina, A.1    Shatrova, A.2    Abushik, P.3    Nikolsky, N.4    Burova, E.5
  • 146
    • 84901484906 scopus 로고    scopus 로고
    • TGF-beta1 induces senescence of bone marrow mesenchymal stem cells via increase of mitochondrial ROS production
    • J. Wu, J. Niu, X. Li, X. Wang, Z. Guo, and F. Zhang TGF-beta1 induces senescence of bone marrow mesenchymal stem cells via increase of mitochondrial ROS production BMC Dev. Biol. 14 2014 21
    • (2014) BMC Dev. Biol. , vol.14 , pp. 21
    • Wu, J.1    Niu, J.2    Li, X.3    Wang, X.4    Guo, Z.5    Zhang, F.6
  • 148
    • 77950630969 scopus 로고    scopus 로고
    • Growth factor erv1-like modulates to preserve mitochondrial dynamics and function in mouse embryonic stem cells
    • L.R. Todd, M.N. Damin, R. Gomathinayagam, S.R. Horn, A.R. Means, and U. Sankar Growth factor erv1-like modulates to preserve mitochondrial dynamics and function in mouse embryonic stem cells Mol. Biol. Cell 21 2010 1225 1236
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1225-1236
    • Todd, L.R.1    Damin, M.N.2    Gomathinayagam, R.3    Horn, S.R.4    Means, A.R.5    Sankar, U.6
  • 149
    • 84905741423 scopus 로고    scopus 로고
    • Stem cell aging: Mechanisms, regulators and therapeutic opportunities
    • J. Oh, Y.D. Lee, and A.J. Wagers Stem cell aging: mechanisms, regulators and therapeutic opportunities Nat. Med. 20 2014 870 880
    • (2014) Nat. Med. , vol.20 , pp. 870-880
    • Oh, J.1    Lee, Y.D.2    Wagers, A.J.3
  • 150
    • 84899860563 scopus 로고    scopus 로고
    • Miro1: New wheels for transferring mitochondria
    • G. Las, and O.S. Shirihai Miro1: new wheels for transferring mitochondria EMBO J. 33 2014 939 941
    • (2014) EMBO J. , vol.33 , pp. 939-941
    • Las, G.1    Shirihai, O.S.2
  • 151
    • 84907459327 scopus 로고    scopus 로고
    • Mitochondria regulate neutrophil activation by generating ATP for autocrine purinergic signaling
    • Y. Bao, C. Ledderose, T. Seier, A.F. Graf, B. Brix, E. Chong, and W.G. Junger Mitochondria regulate neutrophil activation by generating ATP for autocrine purinergic signaling J. Biol. Chem. 289 2014
    • (2014) J. Biol. Chem. , vol.289
    • Bao, Y.1    Ledderose, C.2    Seier, T.3    Graf, A.F.4    Brix, B.5    Chong, E.6    Junger, W.G.7
  • 154
    • 84926011028 scopus 로고    scopus 로고
    • Reactive oxygen species at the crossroads of inflammasome and inflammation
    • A. Harijith, D.L. Ebenezer, and V. Natarajan Reactive oxygen species at the crossroads of inflammasome and inflammation Front. Physiol. 5 2014 352
    • (2014) Front. Physiol. , vol.5 , pp. 352
    • Harijith, A.1    Ebenezer, D.L.2    Natarajan, V.3
  • 155
    • 84941733829 scopus 로고    scopus 로고
    • Antimicrobial resistance: Impact on clinical and economic outcomes and the need for new antimicrobials
    • A.K. Thabit, J.L. Crandon, and D.P. Nicolau Antimicrobial resistance: impact on clinical and economic outcomes and the need for new antimicrobials Expert Opin. Pharmacother. 2014 1 19
    • (2014) Expert Opin. Pharmacother. , pp. 1-19
    • Thabit, A.K.1    Crandon, J.L.2    Nicolau, D.P.3
  • 157
    • 84919488787 scopus 로고    scopus 로고
    • Neutralization of mitochondrial superoxide by superoxide dismutase 2 promotes bacterial clearance and regulates phagocyte numbers in zebrafish
    • E.M. Peterman, C. Sullivan, M.F. Goody, I. Rodriguez-Nunez, J.A. Yoder, and C.H. Kim Neutralization of mitochondrial superoxide by superoxide dismutase 2 promotes bacterial clearance and regulates phagocyte numbers in zebrafish Infect. Immun. 83 2015 430 440
    • (2015) Infect. Immun. , vol.83 , pp. 430-440
    • Peterman, E.M.1    Sullivan, C.2    Goody, M.F.3    Rodriguez-Nunez, I.4    Yoder, J.A.5    Kim, C.H.6
  • 158
    • 84873587763 scopus 로고    scopus 로고
    • Potentiating antibacterial activity by predictably enhancing endogenous microbial ROS production
    • M.P. Brynildsen, J.A. Winkler, C.S. Spina, I.C. MacDonald, and J.J. Collins Potentiating antibacterial activity by predictably enhancing endogenous microbial ROS production Nat. Biotechnol. 31 2013 160 165
    • (2013) Nat. Biotechnol. , vol.31 , pp. 160-165
    • Brynildsen, M.P.1    Winkler, J.A.2    Spina, C.S.3    MacDonald, I.C.4    Collins, J.J.5
  • 159
    • 84920181006 scopus 로고    scopus 로고
    • Antibacterial activity and mechanism of action of Monarda punctata essential oil and its main components against common bacterial pathogens in respiratory tract
    • H. Li, T. Yang, F.Y. Li, Y. Yao, and Z.M. Sun Antibacterial activity and mechanism of action of Monarda punctata essential oil and its main components against common bacterial pathogens in respiratory tract Int. J. Clin. Exp. Pathol. 7 2014 7389 7398
    • (2014) Int. J. Clin. Exp. Pathol. , vol.7 , pp. 7389-7398
    • Li, H.1    Yang, T.2    Li, F.Y.3    Yao, Y.4    Sun, Z.M.5
  • 160
    • 84911405863 scopus 로고    scopus 로고
    • 'Division of labour' in response to host oxidative burst drives a fatal Cryptococcus gattii outbreak
    • K. Voelz, S.A. Johnston, L.M. Smith, R.A. Hall, A. Idnurm, and R.C. May 'Division of labour' in response to host oxidative burst drives a fatal Cryptococcus gattii outbreak Nat. Commun. 5 2014 5194
    • (2014) Nat. Commun. , vol.5 , pp. 5194
    • Voelz, K.1    Johnston, S.A.2    Smith, L.M.3    Hall, R.A.4    Idnurm, A.5    May, R.C.6
  • 161
    • 84906874843 scopus 로고    scopus 로고
    • Mitochondrial dynamics and the innate antiviral immune response
    • M. Pourcelot, and D. Arnoult Mitochondrial dynamics and the innate antiviral immune response FEBS J. 281 2014 3791 3802
    • (2014) FEBS J. , vol.281 , pp. 3791-3802
    • Pourcelot, M.1    Arnoult, D.2
  • 162
    • 75949098312 scopus 로고    scopus 로고
    • Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway
    • C. Castanier, D. Garcin, A. Vazquez, and D. Arnoult Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway EMBO Rep. 11 2010 133 138
    • (2010) EMBO Rep. , vol.11 , pp. 133-138
    • Castanier, C.1    Garcin, D.2    Vazquez, A.3    Arnoult, D.4
  • 163
    • 84911192502 scopus 로고    scopus 로고
    • RNA viruses promote activation of the NLRP3 inflammasome through a RIP1-RIP3-DRP1 signaling pathway
    • X. Wang, W. Jiang, Y. Yan, T. Gong, J. Han, Z. Tian, and R. Zhou RNA viruses promote activation of the NLRP3 inflammasome through a RIP1-RIP3-DRP1 signaling pathway Nat. Immunol. 15 2014 1126 1133
    • (2014) Nat. Immunol. , vol.15 , pp. 1126-1133
    • Wang, X.1    Jiang, W.2    Yan, Y.3    Gong, T.4    Han, J.5    Tian, Z.6    Zhou, R.7
  • 165
    • 84876793270 scopus 로고    scopus 로고
    • An insight into the PB1F2 protein and its multifunctional role in enhancing the pathogenicity of the influenza A viruses
    • A.K. Chakrabarti, and G. Pasricha An insight into the PB1F2 protein and its multifunctional role in enhancing the pathogenicity of the influenza A viruses Virology 440 2013 97 104
    • (2013) Virology , vol.440 , pp. 97-104
    • Chakrabarti, A.K.1    Pasricha, G.2
  • 166
    • 84907319179 scopus 로고    scopus 로고
    • Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity
    • T. Yoshizumi, T. Ichinohe, O. Sasaki, H. Otera, S. Kawabata, K. Mihara, and T. Koshiba Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity Nat. Commun. 5 2014 4713
    • (2014) Nat. Commun. , vol.5 , pp. 4713
    • Yoshizumi, T.1    Ichinohe, T.2    Sasaki, O.3    Otera, H.4    Kawabata, S.5    Mihara, K.6    Koshiba, T.7
  • 167
    • 84921664520 scopus 로고    scopus 로고
    • SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome
    • C.S. Shi, H.Y. Qi, C. Boularan, N.N. Huang, M. Abu-Asab, J.H. Shelhamer, and J.H. Kehrl SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome J. Immunol. 193 2014 3080 3089
    • (2014) J. Immunol. , vol.193 , pp. 3080-3089
    • Shi, C.S.1    Qi, H.Y.2    Boularan, C.3    Huang, N.N.4    Abu-Asab, M.5    Shelhamer, J.H.6    Kehrl, J.H.7
  • 170
    • 84919460386 scopus 로고    scopus 로고
    • Contact-induced mitochondrial polarization supports HIV-1 virological synapse formation
    • E. Groppelli, S. Starling, and C. Jolly Contact-induced mitochondrial polarization supports HIV-1 virological synapse formation J. Virol. 89 2015 14 24
    • (2015) J. Virol. , vol.89 , pp. 14-24
    • Groppelli, E.1    Starling, S.2    Jolly, C.3
  • 171
    • 84898845550 scopus 로고    scopus 로고
    • Krebs cycle dysfunction shapes epigenetic landscape of chromatin: Novel insights into mitochondrial regulation of aging process
    • A. Salminen, K. Kaarniranta, M. Hiltunen, and A. Kauppinen Krebs cycle dysfunction shapes epigenetic landscape of chromatin: novel insights into mitochondrial regulation of aging process Cell. Signal. 26 2014 1598 1603
    • (2014) Cell. Signal. , vol.26 , pp. 1598-1603
    • Salminen, A.1    Kaarniranta, K.2    Hiltunen, M.3    Kauppinen, A.4
  • 172
    • 84919916896 scopus 로고    scopus 로고
    • Mitochondrial sirtuins: Emerging roles in metabolic regulations, energy homeostasis and diseases
    • P. Parihar, I. Solanki, M.L. Mansuri, and M.S. Parihar Mitochondrial sirtuins: emerging roles in metabolic regulations, energy homeostasis and diseases Exp. Gerontol. 61C 2015 130 141
    • (2015) Exp. Gerontol. , vol.61 C , pp. 130-141
    • Parihar, P.1    Solanki, I.2    Mansuri, M.L.3    Parihar, M.S.4
  • 173
    • 84901854646 scopus 로고    scopus 로고
    • Post-translational modification of mitochondria as a novel mode of regulation
    • A. Hofer, and T. Wenz Post-translational modification of mitochondria as a novel mode of regulation Exp. Gerontol. 56 2014 202 220
    • (2014) Exp. Gerontol. , vol.56 , pp. 202-220
    • Hofer, A.1    Wenz, T.2
  • 175
    • 84908343054 scopus 로고    scopus 로고
    • Disruption of SUMO-specific protease 2 induces mitochondria mediated neurodegeneration
    • J. Fu, H.M. Yu, S.Y. Chiu, A.J. Mirando, E.O. Maruyama, J.G. Cheng, and W. Hsu Disruption of SUMO-specific protease 2 induces mitochondria mediated neurodegeneration PLoS Genet. 10 2014 e1004579
    • (2014) PLoS Genet. , vol.10 , pp. e1004579
    • Fu, J.1    Yu, H.M.2    Chiu, S.Y.3    Mirando, A.J.4    Maruyama, E.O.5    Cheng, J.G.6    Hsu, W.7
  • 178
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: Regulation by sirtuins and implications for metabolic disease
    • J.C. Newman, W. He, and E. Verdin Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease J. Biol. Chem. 287 2012 42436 42443
    • (2012) J. Biol. Chem. , vol.287 , pp. 42436-42443
    • Newman, J.C.1    He, W.2    Verdin, E.3
  • 180
    • 84926628054 scopus 로고    scopus 로고
    • Mitochondrial sirtuins and their relationships with metabolic disease and cancer
    • S. Kumar, and D.B. Lombard Mitochondrial sirtuins and their relationships with metabolic disease and cancer Antioxid. Redox Signal. 22 12 2015 1060 1077
    • (2015) Antioxid. Redox Signal. , vol.22 , Issue.12 , pp. 1060-1077
    • Kumar, S.1    Lombard, D.B.2
  • 181
    • 84906656472 scopus 로고    scopus 로고
    • Mitochondrial acetylation and genetic models of Parkinson's disease
    • G. Auburger, S. Gispert, and M. Jendrach Mitochondrial acetylation and genetic models of Parkinson's disease Prog. Mol. Biol. Transl. Sci. 127 2014 155 182
    • (2014) Prog. Mol. Biol. Transl. Sci. , vol.127 , pp. 155-182
    • Auburger, G.1    Gispert, S.2    Jendrach, M.3
  • 182
    • 84909641972 scopus 로고    scopus 로고
    • SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis
    • Y. Zhu, Y. Yan, D.R. Principe, X. Zou, A. Vassilopoulos, and D. Gius SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis Cancer Metab. 2 2014 15
    • (2014) Cancer Metab. , vol.2 , pp. 15
    • Zhu, Y.1    Yan, Y.2    Principe, D.R.3    Zou, X.4    Vassilopoulos, A.5    Gius, D.6
  • 185
    • 84895744576 scopus 로고    scopus 로고
    • Regulation of MnSOD enzymatic activity by Sirt3 connects the mitochondrial acetylome signaling networks to aging and carcinogenesis
    • R. Tao, A. Vassilopoulos, L. Parisiadou, Y. Yan, and D. Gius Regulation of MnSOD enzymatic activity by Sirt3 connects the mitochondrial acetylome signaling networks to aging and carcinogenesis Antioxid. Redox Signal. 20 2014 1646 1654
    • (2014) Antioxid. Redox Signal. , vol.20 , pp. 1646-1654
    • Tao, R.1    Vassilopoulos, A.2    Parisiadou, L.3    Yan, Y.4    Gius, D.5
  • 186
    • 84877903301 scopus 로고    scopus 로고
    • Lysine deacetylases and mitochondrial dynamics in neurodegeneration
    • P. Guedes-Dias, and J.M. Oliveira Lysine deacetylases and mitochondrial dynamics in neurodegeneration Biochim. Biophys. Acta 1832 2013 1345 1359
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 1345-1359
    • Guedes-Dias, P.1    Oliveira, J.M.2
  • 188
    • 84895089601 scopus 로고    scopus 로고
    • Age-related decrease in the mitochondrial sirtuin deacetylase Sirt3 expression associated with ROS accumulation in the auditory cortex of the mimetic aging rat model
    • L. Zeng, Y. Yang, Y. Hu, Y. Sun, Z. Du, Z. Xie, T. Zhou, and W. Kong Age-related decrease in the mitochondrial sirtuin deacetylase Sirt3 expression associated with ROS accumulation in the auditory cortex of the mimetic aging rat model PLoS One 9 2014 e88019
    • (2014) PLoS One , vol.9 , pp. e88019
    • Zeng, L.1    Yang, Y.2    Hu, Y.3    Sun, Y.4    Du, Z.5    Xie, Z.6    Zhou, T.7    Kong, W.8
  • 190
    • 36249016246 scopus 로고    scopus 로고
    • A therapeutic role for sirtuins in diseases of aging?
    • C.H. Westphal, M.A. Dipp, and L. Guarente A therapeutic role for sirtuins in diseases of aging? Trends Biochem. Sci. 32 2007 555 560
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 555-560
    • Westphal, C.H.1    Dipp, M.A.2    Guarente, L.3
  • 191
    • 84903362440 scopus 로고    scopus 로고
    • Global changes in DNA methylation and hydroxymethylation in Alzheimer's disease human brain
    • N. Coppieters, B.V. Dieriks, C. Lill, R.L. Faull, M.A. Curtis, and M. Dragunow Global changes in DNA methylation and hydroxymethylation in Alzheimer's disease human brain Neurobiol. Aging 35 2014 1334 1344
    • (2014) Neurobiol. Aging , vol.35 , pp. 1334-1344
    • Coppieters, N.1    Dieriks, B.V.2    Lill, C.3    Faull, R.L.4    Curtis, M.A.5    Dragunow, M.6
  • 194
    • 84923269003 scopus 로고    scopus 로고
    • ATP-citrate lyase regulates cellular senescence via an AMPK- and p53-dependent pathway
    • J.H. Lee, H. Jang, S.M. Lee, J.E. Lee, J. Choi, T.W. Kim, E.J. Cho, and H.D. Youn ATP-citrate lyase regulates cellular senescence via an AMPK- and p53-dependent pathway FEBS J. 282 2 2015 361 371
    • (2015) FEBS J. , vol.282 , Issue.2 , pp. 361-371
    • Lee, J.H.1    Jang, H.2    Lee, S.M.3    Lee, J.E.4    Choi, J.5    Kim, T.W.6    Cho, E.J.7    Youn, H.D.8


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