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Volumn 15, Issue 6, 2014, Pages 436-456

Energizing genetics and epi-genetics: Role in the regulation of mitochondrial function

Author keywords

Chromatin; DNA modification; Energy metabolism; Histone modification; Mitochondrial biogenesis; Transcription

Indexed keywords

2 OXOGLUTARIC ACID; ENDONUCLEASE; ESTROGEN RELATED RECEPTOR ALPHA; HISTONE DEMETHYLASE; HISTONE METHYLTRANSFERASE; INITIATION FACTOR 2; MAMMALIAN TARGET OF RAPAMYCIN; MICRORNA; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL RNA; NUCLEAR RESPIRATORY FACTOR 1; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; SIRTUIN; SIRTUIN 1; SIRTUIN 3; SIRTUIN 6; SMALL UNTRANSLATED RNA; STEROL REGULATORY ELEMENT BINDING PROTEIN 1; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FKHRL1; TRANSCRIPTION FACTOR NRF1; TRIACYLGLYCEROL; UBIQUINONE; UNCOUPLING PROTEIN 1;

EID: 84921926094     PISSN: 13892029     EISSN: 18755488     Source Type: Journal    
DOI: 10.2174/138920291506150106151119     Document Type: Article
Times cited : (10)

References (224)
  • 1
    • 84863974539 scopus 로고    scopus 로고
    • Association between oxidative stress and macromolecular damage in elderly patients with age-related macular degeneration
    • Venza, I.; Visalli, M.; Cucinotta, M.; Teti, D.; Venza, M. Association between oxidative stress and macromolecular damage in elderly patients with age-related macular degeneration. Aging Clin. Exp. Res 2012, 24(1), 21-27.
    • (2012) Aging Clin. Exp. Res , vol.24 , Issue.1 , pp. 21-27
    • Venza, I.1    Visalli, M.2    Cucinotta, M.3    Teti, D.4    Venza, M.5
  • 2
    • 84874603374 scopus 로고    scopus 로고
    • Combined effects of cigarette smoking and alcohol consumption on antioxidant/ oxidant balance in age-related macular degeneration
    • Venza, I.; Visalli, M.; Oteri, R.; Teti, D.; Venza, M. Combined effects of cigarette smoking and alcohol consumption on antioxidant/ oxidant balance in age-related macular degeneration. Aging Clin. Exp. Res2012, 24(5), 530-536.
    • (2012) Aging Clin. Exp. Res , vol.24 , Issue.5 , pp. 530-536
    • Venza, I.1    Visalli, M.2    Oteri, R.3    Teti, D.4    Venza, M.5
  • 3
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell, PCoupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature, 1961, 191, 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 4
    • 77954859197 scopus 로고    scopus 로고
    • The role of mitochondria in the pathogenesis of type 2 diabetes
    • Patti, M. E.; Corvera, S. The role of mitochondria in the pathogenesis of type 2 diabetes. Endocr. Rev2010, 31(3), 364-395.
    • (2010) Endocr. Rev , vol.31 , Issue.3 , pp. 364-395
    • Patti, M.E.1    Corvera, S.2
  • 5
    • 84906656472 scopus 로고    scopus 로고
    • Mitochondrial acetylation and genetic models of Parkinson's disease
    • Auburger, G.; Gispert, S.; Jendrach, MMitochondrial acetylation and genetic models of Parkinson's disease. Prog. Mol. Biol. Transl. Sci2014, 127, 155-182.
    • (2014) Prog. Mol. Biol. Transl. Sci , vol.127 , pp. 155-182
    • Auburger, G.1    Gispert, S.2    Jendrach, M.3
  • 7
    • 84909619435 scopus 로고    scopus 로고
    • The regulation of mitochondrial dynamics
    • Hoppins, S. The regulation of mitochondrial dynamics. Curr. Opin. Cell Biol2014, 29, 46-52.
    • (2014) Curr. Opin. Cell Biol , vol.29 , pp. 46-52
    • Hoppins, S.1
  • 8
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann, B. Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol2010, 11(12), 872-884.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , Issue.12 , pp. 872-884
    • Westermann, B.1
  • 9
    • 42049114034 scopus 로고    scopus 로고
    • Transcriptional paradigms in mammalian mitochondrial biogenesis and function
    • Scarpulla, R.C. Transcriptional paradigms in mammalian mitochondrial biogenesis and function. Physiol. Rev2008, 88(2), 611-638.
    • (2008) Physiol. Rev , vol.88 , Issue.2 , pp. 611-638
    • Scarpulla, R.C.1
  • 10
    • 84865414333 scopus 로고    scopus 로고
    • Transcriptional integration of mitochondrial biogenesis
    • Scarpulla, R.C.; Vega, R.B.; Kelly, D.P. Transcriptional integration of mitochondrial biogenesis. Trends Endocrinol. Metab2012, 23(9), 459-466.
    • (2012) Trends Endocrinol. Metab , vol.23 , Issue.9 , pp. 459-466
    • Scarpulla, R.C.1    Vega, R.B.2    Kelly, D.P.3
  • 11
    • 84890774184 scopus 로고    scopus 로고
    • Hallmarks of a new era in mitochondrial biochemistry
    • Pagliarini, D.J.; Rutter, J. Hallmarks of a new era in mitochondrial biochemistry. Genes Dev2013, 27(24), 2615-2627.
    • (2013) Genes Dev , vol.27 , Issue.24 , pp. 2615-2627
    • Pagliarini, D.J.1    Rutter, J.2
  • 12
    • 0037154972 scopus 로고    scopus 로고
    • Epigenetic Codes for Heterochromatin Formation and Silencing: Rounding up the Usual Suspects
    • Richards, E.J.; Elgin, S.C.R. Epigenetic Codes for Heterochromatin Formation and Silencing: Rounding up the Usual Suspects. Cell, 2002, 108(4), 489-500.
    • (2002) Cell , vol.108 , Issue.4 , pp. 489-500
    • Richards, E.J.1    Elgin, S.C.R.2
  • 13
    • 34848903233 scopus 로고    scopus 로고
    • Role of histone and DNA methylation in gene regulation
    • Vaillant, I.; Paszkowski, J. Role of histone and DNA methylation in gene regulation. Curr. Opin. Plant Biol2007, 10(5), 528-533.
    • (2007) Curr. Opin. Plant Biol , vol.10 , Issue.5 , pp. 528-533
    • Vaillant, I.1    Paszkowski, J.2
  • 14
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • Lee, K.K.; Workman, J.L. Histone acetyltransferase complexes: one size doesn't fit all. Nat. Rev. Mol. Cell Biol2007, 8(4), 284-295.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , Issue.4 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 15
    • 77957666255 scopus 로고    scopus 로고
    • Histone Methyl Transferases and Demethylases; Can They Link Metabolism and Tran scription?
    • Teperino, R.; Schoonjans, K.; Auwerx, J. Histone Methyl Transferases and Demethylases; Can They Link Metabolism and Tran scription? Cell Metab2010, 12(4), 321-327.
    • (2010) Cell Metab , vol.12 , Issue.4 , pp. 321-327
    • Teperino, R.1    Schoonjans, K.2    Auwerx, J.3
  • 16
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature, 1997, 389(6649), 349-352.
    • (1997) Nature , vol.389 , Issue.6649 , pp. 349-352
    • Grunstein, M.1
  • 17
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin Modifications and Their Function
    • Kouzarides, TChromatin Modifications and Their Function. Cell, 2007, 128(4), 693-705.
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 18
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith, B.C.; Denu, J.M. Chemical mechanisms of histone lysine and arginine modifications. Biochim. Biophys. Acta, 2009, 1789(1), 45-57.
    • (2009) Biochim. Biophys. Acta , vol.1789 , Issue.1 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 19
    • 65549170303 scopus 로고    scopus 로고
    • Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with geneactivating epigenetic marks that coexist on the lysine tail
    • Brasacchio, D.; Okabe, J.; Tikellis, C.; Balcerczyk, A.; George, P.; Baker, E.K.; Calkin, A.C.; Brownlee, M.; Cooper, M.E.; El-Osta, A. Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with geneactivating epigenetic marks that coexist on the lysine tail. Diabetes, 2009, 58(5), 1229-1236.
    • (2009) Diabetes , vol.58 , Issue.5 , pp. 1229-1236
    • Brasacchio, D.1    Okabe, J.2    Tikellis, C.3    Balcerczyk, A.4    George, P.5    Baker, E.K.6    Calkin, A.C.7    Brownlee, M.8    Cooper, M.E.9    El-Osta, A.10
  • 20
    • 53349101264 scopus 로고    scopus 로고
    • Transient high glucose causes persistent epigenetic changes and altered gene expression during subsequent normoglycemia
    • El-Osta, A.; Brasacchio, D.; Yao, D.; Pocai, A.; Jones, P.L.; Roeder, R.G.; Cooper, M.E.; Brownlee, M. Transient high glucose causes persistent epigenetic changes and altered gene expression during subsequent normoglycemia. J. Exp. Med2008, 205(10), 2409-2417.
    • (2008) J. Exp. Med , vol.205 , Issue.10 , pp. 2409-2417
    • El-Osta, A.1    Brasacchio, D.2    Yao, D.3    Pocai, A.4    Jones, P.L.5    Roeder, R.G.6    Cooper, M.E.7    Brownlee, M.8
  • 21
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y.; Lan, F.; Matson, C.; Mulligan, P.; Whetstine, J.R.; Cole, P. A.; Casero, R.A. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell, 2004, 119(7), 941-953.
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7
  • 23
    • 37249024572 scopus 로고    scopus 로고
    • Structure and mechanism of lysinespecific demethylase enzymes
    • Anand, R.; Marmorstein, R. Structure and mechanism of lysinespecific demethylase enzymes. J. Biol. Chem2007, 282(49), 35425-35429.
    • (2007) J. Biol. Chem , vol.282 , Issue.49 , pp. 35425-35429
    • Anand, R.1    Marmorstein, R.2
  • 25
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 Is a Histone Arginine Demethylase
    • Chang, B.; Chen, Y.; Zhao, Y.; Bruick, R.K. JMJD6 Is a Histone Arginine Demethylase. Science, 2007, 318(5849), 444-447.
    • (2007) Science , vol.318 , Issue.5849 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 26
    • 70349663508 scopus 로고    scopus 로고
    • Conformational signals in the C-terminal domain of methionine adenosyltransferase I/III determine its nucleocytoplasmic distribution
    • Reytor, E.; Pérez-Miguelsanz, J.; Alvarez, L.; Pérez-Sala, D.; Pajares, M.A. Conformational signals in the C-terminal domain of methionine adenosyltransferase I/III determine its nucleocytoplasmic distribution. FASEB J2009, 23(10), 3347-3360.
    • (2009) FASEB J , vol.23 , Issue.10 , pp. 3347-3360
    • Reytor, E.1    Pérez-Miguelsanz, J.2    Alvarez, L.3    Pérez-Sala, D.4    Pajares, M.A.5
  • 27
    • 62349110317 scopus 로고    scopus 로고
    • Effects of insulin and glucose on cellular metabolic fluxes in homocysteine transsulfuration, remethylation, S-adenosylmethionine synthesis, and global deoxyribonucleic acid methylation
    • Chiang, E.P.; Wang, Y.C.; Chen, W.W.; Tang, F.Y. Effects of insulin and glucose on cellular metabolic fluxes in homocysteine transsulfuration, remethylation, S-adenosylmethionine synthesis, and global deoxyribonucleic acid methylation. J. Clin. Endocrinol. Metab2009, 94(3), 1017-1025.
    • (2009) J. Clin. Endocrinol. Metab , vol.94 , Issue.3 , pp. 1017-1025
    • Chiang, E.P.1    Wang, Y.C.2    Chen, W.W.3    Tang, F.Y.4
  • 28
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative Phosphorylation at the fin de siècle
    • Saraste, M. Oxidative Phosphorylation at the fin de siècle. Science, 1999, 283(5407), 1488-1493.
    • (1999) Science , vol.283 , Issue.5407 , pp. 1488-1493
    • Saraste, M.1
  • 29
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • Bordone, L.; Guarente, L. Calorie restriction, SIRT1 and metabolism: understanding longevity. Nat. Rev. Mol. Cell Biol2005, 6(4), 298-305.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , Issue.4 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 30
    • 84902685602 scopus 로고    scopus 로고
    • Krebs cycle intermediates regulate DNA and histone methylation: Epigenetic impact on the aging process
    • Salminen, A.; Kauppinen, A.; Hiltunen, M.; Kaarniranta, KKrebs cycle intermediates regulate DNA and histone methylation: epigenetic impact on the aging process. Ageing Res. Rev2014, 16, 45-65.
    • (2014) Ageing Res. Rev , vol.16 , pp. 45-65
    • Salminen, A.1    Kauppinen, A.2    Hiltunen, M.3    Kaarniranta, K.4
  • 31
    • 57349151485 scopus 로고    scopus 로고
    • N. The JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress
    • Polytarchou, C.; Pfau, R.; Hatziapostolou, M.; Tsichlis, P. NThe JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress. Mol. Cell. Biol2008, 28(24), 7451-7464.
    • (2008) Mol. Cell. Biol , vol.28 , Issue.24 , pp. 7451-7464
    • Polytarchou, C.1    Pfau, R.2    Hatziapostolou, M.3    Tsichlis, P.4
  • 32
    • 21344440000 scopus 로고    scopus 로고
    • Reactive Oxygen Species as Mediators of Cellular Senescence
    • Colavitti, R.; Finkel, T. Reactive Oxygen Species as Mediators of Cellular Senescence. IUBMB Life, 2005, 57(4-5), 277-281.
    • (2005) IUBMB Life , vol.57 , Issue.4-5 , pp. 277-281
    • Colavitti, R.1    Finkel, T.2
  • 33
  • 34
    • 0035968183 scopus 로고    scopus 로고
    • Modulation of mitochondrial function by hydrogen peroxide
    • Nulton-Persson, A.C.; Szweda, L.I. Modulation of mitochondrial function by hydrogen peroxide. J. Biol. Chem2001, 276(26), 23357-23361.
    • (2001) J. Biol. Chem , vol.276 , Issue.26 , pp. 23357-23361
    • Nulton-Persson, A.C.1    Szweda, L.I.2
  • 36
    • 58049206724 scopus 로고    scopus 로고
    • Targeted inactivation of MLL3 histone H3-Lys-4 methyltransferase activity in the mouse reveals vital roles for MLL3 in adipogenesis
    • Lee, J.; Saha, P.K.; Yang, Q.H.; Lee, S.; Park, J.Y.; Suh, Y.; Lee, S.K.; Chan, L.; Roeder, R.G.; Lee, J.W. Targeted inactivation of MLL3 histone H3-Lys-4 methyltransferase activity in the mouse reveals vital roles for MLL3 in adipogenesis. Proc. Natl. Acad. Sci. U S A, 2008, 105(49), 19229-19234.
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , Issue.49 , pp. 19229-19234
    • Lee, J.1    Saha, P.K.2    Yang, Q.H.3    Lee, S.4    Park, J.Y.5    Suh, Y.6    Lee, S.K.7    Chan, L.8    Roeder, R.G.9    Lee, J.W.10
  • 37
    • 48249127225 scopus 로고    scopus 로고
    • Epigenetic histone H3 lysine 9 methylation in metabolic memory and inflammatory phenotype of vascular smooth muscle cells in diabetes
    • Villeneuve, L.M.; Reddy, M.A.; Lanting, L.L.; Wang, M.; Meng, L.; Natarajan, R. Epigenetic histone H3 lysine 9 methylation in metabolic memory and inflammatory phenotype of vascular smooth muscle cells in diabetes. Proc. Natl. Acad. Sci. U S A, 2008, 105(26), 9047-9052.
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , Issue.26 , pp. 9047-9052
    • Villeneuve, L.M.1    Reddy, M.A.2    Lanting, L.L.3    Wang, M.4    Meng, L.5    Natarajan, R.6
  • 39
    • 64749111074 scopus 로고    scopus 로고
    • M.; Zhang, Y. Role of Jhdm2a in regulating metabolic gene expression and obesity resistance
    • Tateishi, K.; Okada, Y.; Kallin, E. M.; Zhang, YRole of Jhdm2a in regulating metabolic gene expression and obesity resistance. Nature, 2009, 458(7239), 757-761.
    • (2009) Nature , vol.458 , Issue.7239 , pp. 757-761
    • Tateishi, K.1    Okada, Y.2    Kallin, E.3
  • 40
    • 0035787319 scopus 로고    scopus 로고
    • The beta-adrenergic receptors and the control of adipose tissue metabolism and thermogenesis
    • Collins, S.; Surwit, R. S. The beta-adrenergic receptors and the control of adipose tissue metabolism and thermogenesis. Recent Prog. Horm. Res2001, 56, 309-328.
    • (2001) Recent Prog. Horm. Res , vol.56 , pp. 309-328
    • Collins, S.1    Surwit, R.S.2
  • 41
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature, 1997, 389(6649), 349-352.
    • (1997) Nature , vol.389 , Issue.6649 , pp. 349-352
    • Grunstein, M.1
  • 42
    • 0027916769 scopus 로고
    • Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin
    • Lopez-Rodas, G.; Brosch, G.; Georgieva, E.I.; Sendra, R.; Franco, L.; Loidl, P. Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin. FEBS Lett1993, 317(3), 175-180.
    • (1993) FEBS Lett , vol.317 , Issue.3 , pp. 175-180
    • Lopez-Rodas, G.1    Brosch, G.2    Georgieva, E.I.3    Sendra, R.4    Franco, L.5    Loidl, P.6
  • 43
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: From sequence to function, regulation, and clinical implication
    • Yang, X.J.; Gregoire, S. Class II histone deacetylases: from sequence to function, regulation, and clinical implication. Mol. Cell. Biol2005, 25(8), 2873-2884.
    • (2005) Mol. Cell. Biol , vol.25 , Issue.8 , pp. 2873-2884
    • Yang, X.J.1    Gregoire, S.2
  • 46
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland, M.; Montgomery, R.L.; Olson, E.N. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat. Rev. Genet2009, 10(1), 32-42.
    • (2009) Nat. Rev. Genet , vol.10 , Issue.1 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 47
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray, S.G.; Ekstrom, T.J. The human histone deacetylase family. Exp. Cell Res2001, 262(2), 75-83.
    • (2001) Exp. Cell Res , vol.262 , Issue.2 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 48
    • 0034635987 scopus 로고    scopus 로고
    • Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases
    • Lu, J.; McKinsey, T.A.; Nicol, R.L.; Olson, E.N. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc. Natl. Acad. Sci. U S A, 2000, 97(8), 4070-4075.
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , Issue.8 , pp. 4070-4075
    • Lu, J.1    McKinsey, T.A.2    Nicol, R.L.3    Olson, E.N.4
  • 49
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti, I.V.; Lee, Y.M.; Goodson, H.V. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J. Mol. Biol2004, 338(1), 17-31.
    • (2004) J. Mol. Biol , vol.338 , Issue.1 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 51
    • 77952547233 scopus 로고    scopus 로고
    • Ten years of NAD-dependent SIR2 family deacetylases: Implications for metabolic diseases
    • Imai, S.; Guarente, L. Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases. Trends Pharmacol. Sci2010, 31(5), 212-220.
    • (2010) Trends Pharmacol. Sci , vol.31 , Issue.5 , pp. 212-220
    • Imai, S.1    Guarente, L.2
  • 52
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel, T.; Deng, C.X.; Mostoslavsky, R. Recent progress in the biology and physiology of sirtuins. Nature, 2009, 460(7255), 587-591.
    • (2009) Nature , vol.460 , Issue.7255 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 53
  • 54
    • 38649132337 scopus 로고    scopus 로고
    • Mitochondria--a nexus for aging, calorie restriction, and sirtuins?
    • Guarente, L. Mitochondria--a nexus for aging, calorie restriction, and sirtuins? Cell, 2008, 132(2), 171-176.
    • (2008) Cell , vol.132 , Issue.2 , pp. 171-176
    • Guarente, L.1
  • 55
    • 84858797950 scopus 로고    scopus 로고
    • Sirtuins as regulators of metabolism and healthspan
    • Houtkooper, R.H.; Pirinen, E.; Auwerx, J. Sirtuins as regulators of metabolism and healthspan. Nat. Rev. Mol. Cell Biol2012, 13(4), 225-238.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , Issue.4 , pp. 225-238
    • Houtkooper, R.H.1    Pirinen, E.2    Auwerx, J.3
  • 56
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R.APhylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun2000, 273(2), 793-798.
    • (2000) Biochem. Biophys. Res. Commun , vol.273 , Issue.2 , pp. 793-798
    • Frye, R.A.1
  • 57
    • 34250365395 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
    • Tanno, M.; Sakamoto, J.; Miura, T.; Shimamoto, K.; Horio, Y. Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J. Biol. Chem2007, 282(9), 6823-6832.
    • (2007) J. Biol. Chem , vol.282 , Issue.9 , pp. 6823-6832
    • Tanno, M.1    Sakamoto, J.2    Miura, T.3    Shimamoto, K.4    Horio, Y.5
  • 61
    • 0036929765 scopus 로고    scopus 로고
    • Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes
    • Pandey, R.; Muller, A.; Napoli, C.A.; Selinger, D.A.; Pikaard, C.S.; Richards, E.J.; Bender, J.; Mount, D.W.; Jorgensen, R.A. Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes. Nucleic. Acids Res2002, 30(23), 5036-5055.
    • (2002) Nucleic. Acids Res , vol.30 , Issue.23 , pp. 5036-5055
    • Pandey, R.1    Muller, A.2    Napoli, C.A.3    Selinger, D.A.4    Pikaard, C.S.5    Richards, E.J.6    Bender, J.7    Mount, D.W.8    Jorgensen, R.A.9
  • 62
    • 0037242383 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases
    • Utley, R.T.; Cote, J. The MYST family of histone acetyltransferases. Curr. Top. Microbiol. Immunol2003, 274, 203-236.
    • (2003) Curr. Top. Microbiol. Immunol , vol.274 , pp. 203-236
    • Utley, R.T.1    Cote, J.2
  • 63
    • 34547896549 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases and their intimate links to cancer
    • Avvakumov, N.; Cote, J. The MYST family of histone acetyltransferases and their intimate links to cancer. Oncogene, 2007, 26(37), 5395-5407.
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5395-5407
    • Avvakumov, N.1    Cote, J.2
  • 64
    • 0032076229 scopus 로고    scopus 로고
    • Conjunction dysfunction: CBP/p300 in human disease
    • Giles, R.H.; Peters, D.J.; Breuning, M.H. Conjunction dysfunction: CBP/p300 in human disease. Trends Genet1998, 14(5), 178-183.
    • (1998) Trends Genet , vol.14 , Issue.5 , pp. 178-183
    • Giles, R.H.1    Peters, D.J.2    Breuning, M.H.3
  • 66
    • 33646145721 scopus 로고    scopus 로고
    • Circadian regulator CLOCK is a histone acetyltransferase
    • Doi, M.; Hirayama, J.; Sassone-Corsi, P. Circadian regulator CLOCK is a histone acetyltransferase. Cell, 2006, 125(3), 497-508.
    • (2006) Cell , vol.125 , Issue.3 , pp. 497-508
    • Doi, M.1    Hirayama, J.2    Sassone-Corsi, P.3
  • 67
    • 0034615669 scopus 로고    scopus 로고
    • The SRC family of nuclear receptor coactivators
    • Leo, C.; Chen, J.D. The SRC family of nuclear receptor coactivators. Gene, 2000, 245(1), 1-11.
    • (2000) Gene , vol.245 , Issue.1 , pp. 1-11
    • Leo, C.1    Chen, J.D.2
  • 68
    • 84906262848 scopus 로고    scopus 로고
    • Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development
    • Karmodiya, K.; Anamika, K.; Muley, V.; Pradhan, S.J.; Bhide, Y.; Galande, S. Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development. Sci. Rep2014, 4, 6076.
    • (2014) Sci. Rep , vol.4 , pp. 6076
    • Karmodiya, K.1    Anamika, K.2    Muley, V.3    Pradhan, S.J.4    Bhide, Y.5    Galande, S.6
  • 69
    • 84902649601 scopus 로고    scopus 로고
    • Class Ispecific histone deacetylase inhibitor MS-275 overrides TRAILresistance in melanoma cells by downregulating c-FLIP
    • Venza, I.; Visalli, M.; Oteri, R.; Teti, D.; Venza, M. Class Ispecific histone deacetylase inhibitor MS-275 overrides TRAILresistance in melanoma cells by downregulating c-FLIP. Int. Immunopharmacol2014, 21(2), 439-446.
    • (2014) Int. Immunopharmacol , vol.21 , Issue.2 , pp. 439-446
    • Venza, I.1    Visalli, M.2    Oteri, R.3    Teti, D.4    Venza, M.5
  • 70
    • 67649238355 scopus 로고    scopus 로고
    • Butyrate improves insulin sensitivity and increases energy expenditure in mice
    • Gao, Z.; Yin, J.; Zhang, J.; Ward, R.E.; Martin, R.J.; Lefevre, M.; Cefalu, W.T.; Ye, J. Butyrate improves insulin sensitivity and increases energy expenditure in mice. Diabetes, 2009, 58(7), 1509-1517.
    • (2009) Diabetes , vol.58 , Issue.7 , pp. 1509-1517
    • Gao, Z.1    Yin, J.2    Zhang, J.3    Ward, R.E.4    Martin, R.J.5    Lefevre, M.6    Cefalu, W.T.7    Ye, J.8
  • 71
    • 79955579989 scopus 로고    scopus 로고
    • J. The microbiome and butyrate regulate energy metabolism and autophagy in the mammalian colon
    • Donohoe, D.R.; Garge, N.; Zhang, X.; Sun, W.; O'Connell, T.M.; Bunger, M. K.; Bultman, S. JThe microbiome and butyrate regulate energy metabolism and autophagy in the mammalian colon. Cell Metab2011, 13(5), 517-526.
    • (2011) Cell Metab , vol.13 , Issue.5 , pp. 517-526
    • Donohoe, D.R.1    Garge, N.2    Zhang, X.3    Sun, W.4    O'Connell, T.M.5    Bunger, M.K.6    Bultman, S.7
  • 74
    • 75649135910 scopus 로고    scopus 로고
    • Deconstructing repression: Evolving models of co-repressor action
    • Perissi, V.; Jepsen, K.; Glass, C.K.; Rosenfeld, M.G. Deconstructing repression: evolving models of co-repressor action. Nat. Rev. Genet2010, 11(2), 109-123.
    • (2010) Nat. Rev. Genet , vol.11 , Issue.2 , pp. 109-123
    • Perissi, V.1    Jepsen, K.2    Glass, C.K.3    Rosenfeld, M.G.4
  • 76
    • 1942518840 scopus 로고    scopus 로고
    • PPARs and the complex journey to obesity
    • Evans, R.M.; Barish, G.D.; Wang, Y.X. PPARs and the complex journey to obesity. Nat. Med2004, 10(4), 355-361.
    • (2004) Nat. Med , vol.10 , Issue.4 , pp. 355-361
    • Evans, R.M.1    Barish, G.D.2    Wang, Y.X.3
  • 77
    • 50649097541 scopus 로고    scopus 로고
    • Fat and beyond: The diverse biology of PPARgamma
    • Tontonoz, P.; Spiegelman, B.M. Fat and beyond: the diverse biology of PPARgamma. Annu. Rev. Biochem2008, 77, 289-312.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 289-312
    • Tontonoz, P.1    Spiegelman, B.M.2
  • 78
    • 1942518840 scopus 로고    scopus 로고
    • PPARs and the complex journey to obesity
    • Evans, R.M.; Barish, G.D.; Wang, Y.-X. PPARs and the complex journey to obesity. Nat. Med2004, 10(4), 355-361.
    • (2004) Nat. Med , vol.10 , Issue.4 , pp. 355-361
    • Evans, R.M.1    Barish, G.D.2    Wang, Y.-X.3
  • 80
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers, J.T.; Lerin, C.; Haas, W.; Gygi, S.P.; Spiegelman, B.M.; Puigserver, P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature, 2005, 434(7029), 113-118.
    • (2005) Nature , vol.434 , Issue.7029 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 81
    • 34547906123 scopus 로고    scopus 로고
    • Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1
    • Rodgers, J.T.; Puigserver, P. Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1. Proc. Natl. Acad. Sci. U S A, 2007, 104(31), 12861-12866.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , Issue.31 , pp. 12861-12866
    • Rodgers, J.T.1    Puigserver, P.2
  • 83
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • Purushotham, A.; Schug, T.T.; Xu, Q.; Surapureddi, S.; Guo, X.; Li, X. Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab2009, 9(4), 327-338.
    • (2009) Cell Metab , vol.9 , Issue.4 , pp. 327-338
    • Purushotham, A.1    Schug, T.T.2    Xu, Q.3    Surapureddi, S.4    Guo, X.5    Li, X.6
  • 91
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi, T.; Wang, F.; Stieren, E.; Tong, Q. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem2005, 280(14), 13560-13567.
    • (2005) J. Biol. Chem , vol.280 , Issue.14 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 92
    • 70349208608 scopus 로고    scopus 로고
    • P. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
    • Sundaresan, N.R.; Gupta, M.; Kim, G.; Rajamohan, S.B.; Isbatan, A.; Gupta, M. PSirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest2009, 119(9), 2758-2771.
    • (2009) J. Clin. Invest , vol.119 , Issue.9 , pp. 2758-2771
    • Sundaresan, N.R.1    Gupta, M.2    Kim, G.3    Rajamohan, S.B.4    Isbatan, A.5    Gupta, M.6
  • 93
    • 55749084738 scopus 로고    scopus 로고
    • X.; Finkel, T. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • Ahn, B.H.; Kim, H.S.; Song, S.; Lee, I.H.; Liu, J.; Vassilopoulos, A.; Deng, C. X.; Finkel, TA role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc. Natl. Acad. Sci. U S A, 2008, 105(38), 14447-14452.
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , Issue.38 , pp. 14447-14452
    • Ahn, B.H.1    Kim, H.S.2    Song, S.3    Lee, I.H.4    Liu, J.5    Vassilopoulos, A.6    Deng, C.7
  • 95
    • 84867421344 scopus 로고    scopus 로고
    • Transcriptional control of cardiac fuel metabolism and mitochondrial function
    • Leone, T.C.; Kelly, D.P. Transcriptional control of cardiac fuel metabolism and mitochondrial function. Cold Spring Harb. Symp. Quant. Biol2011, 76, 175-182.
    • (2011) Cold Spring Harb. Symp. Quant. Biol , vol.76 , pp. 175-182
    • Leone, T.C.1    Kelly, D.P.2
  • 96
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria: In sickness and in health
    • Nunnari, J.; Suomalainen, AMitochondria: in sickness and in health. Cell, 2012, 148(6), 1145-1159.
    • (2012) Cell , vol.148 , Issue.6 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 97
    • 84860192261 scopus 로고    scopus 로고
    • Identification of a molecular component of the mitochondrial acetyltransferase programme: A novel role for GCN5L1
    • Scott, I.; Webster, B.R.; Li, J.H.; Sack, M.N. Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1. Biochem. J2012, 443(3), 655-661.
    • (2012) Biochem. J , vol.443 , Issue.3 , pp. 655-661
    • Scott, I.1    Webster, B.R.2    Li, J.H.3    Sack, M.N.4
  • 98
    • 33744534726 scopus 로고    scopus 로고
    • GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha
    • Lerin, C.; Rodgers, J.T.; Kalume, D.E.; Kim, S.H.; Pandey, A.; Puigserver, P. GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1alpha. Cell Metab2006, 3(6), 429-438.
    • (2006) Cell Metab , vol.3 , Issue.6 , pp. 429-438
    • Lerin, C.1    Rodgers, J.T.2    Kalume, D.E.3    Kim, S.H.4    Pandey, A.5    Puigserver, P.6
  • 100
    • 84888854875 scopus 로고    scopus 로고
    • Impact of DNA methyltransferases on the epigenetic regulation of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) receptor expression in malignant melanoma
    • Venza, M.; Visalli, M.; Catalano, T.; Fortunato, C.; Oteri, R.; Teti, D.; Venza, I. Impact of DNA methyltransferases on the epigenetic regulation of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) receptor expression in malignant melanoma. Biochem. Biophys. Res. Commun2013, 441(4), 743-750.
    • (2013) Biochem. Biophys. Res. Commun , vol.441 , Issue.4 , pp. 743-750
    • Venza, M.1    Visalli, M.2    Catalano, T.3    Fortunato, C.4    Oteri, R.5    Teti, D.6    Venza, I.7
  • 102
    • 77956095231 scopus 로고    scopus 로고
    • Active DNA demethylation: Many roads lead to Rome
    • Wu, S.C.; Zhang, Y. Active DNA demethylation: many roads lead to Rome. Nat. Rev. Mol. Cell Biol2010, 11(9), 607-620.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , Issue.9 , pp. 607-620
    • Wu, S.C.1    Zhang, Y.2
  • 105
    • 84859002909 scopus 로고    scopus 로고
    • Parallel mechanisms of epigenetic reprogramming in the germline
    • Hackett, J.A.; Zylicz, J.J.; Surani, M.A. Parallel mechanisms of epigenetic reprogramming in the germline. Trends Genet2012, 28(4), 164-174.
    • (2012) Trends Genet , vol.28 , Issue.4 , pp. 164-174
    • Hackett, J.A.1    Zylicz, J.J.2    Surani, M.A.3
  • 106
    • 84881397528 scopus 로고    scopus 로고
    • PPARgamma-induced PARylation promotes local DNA demethylation by production of 5-hydroxymethylcytosine
    • Fujiki, K.; Shinoda, A.; Kano, F.; Sato, R.; Shirahige, K.; Murata, M. PPARgamma-induced PARylation promotes local DNA demethylation by production of 5-hydroxymethylcytosine. Nat. Commun2013, 4, 2262.
    • (2013) Nat. Commun , vol.4 , pp. 2262
    • Fujiki, K.1    Shinoda, A.2    Kano, F.3    Sato, R.4    Shirahige, K.5    Murata, M.6
  • 111
    • 84883393151 scopus 로고    scopus 로고
    • Alteration of genic 5-hydroxymethylcytosine patterning in olfactory neurons correlates with changes in gene expression and cell identity
    • Colquitt, B.M.; Allen, W.E.; Barnea, G.; Lomvardas, S. Alteration of genic 5-hydroxymethylcytosine patterning in olfactory neurons correlates with changes in gene expression and cell identity. Proc. Natl. Acad. Sci. U S A, 2013, 110(36), 14682-14687.
    • (2013) Proc. Natl. Acad. Sci. U S A , vol.110 , Issue.36 , pp. 14682-14687
    • Colquitt, B.M.1    Allen, W.E.2    Barnea, G.3    Lomvardas, S.4
  • 112
    • 84885794483 scopus 로고    scopus 로고
    • Higher 5-hydroxymethyl-cytosine identifies immortal DNA strand chromosomes in asymmetrically self-renewing distributed stem cells
    • Huh, Y.H.; Cohen, J.; Sherley, J.L. Higher 5-hydroxymethyl-cytosine identifies immortal DNA strand chromosomes in asymmetrically self-renewing distributed stem cells. Proc. Natl. Acad. Sci. U S A, 2013, 110(42), 16862-16867.
    • (2013) Proc. Natl. Acad. Sci. U S A , vol.110 , Issue.42 , pp. 16862-16867
    • Huh, Y.H.1    Cohen, J.2    Sherley, J.L.3
  • 114
    • 67149123375 scopus 로고    scopus 로고
    • Epigenetic regulation of adipocyte differentiation by a Rho guanine nucleotide exchange factor, WGEF
    • Horii, T.; Morita, S.; Kimura, M.; Hatada, I. Epigenetic regulation of adipocyte differentiation by a Rho guanine nucleotide exchange factor, WGEF. PLoS One, 2009, 4(6), e5809.
    • (2009) PLoS One , vol.4 , Issue.6
    • Horii, T.1    Morita, S.2    Kimura, M.3    Hatada, I.4
  • 115
    • 84859222932 scopus 로고    scopus 로고
    • Periconceptional maternal micronutrient supplementation is associated with widespread gender related changes in the epigenome: A study of a unique resource in the Gambia
    • Khulan, B.; Cooper, W.N.; Skinner, B.M.; Bauer, J.; Owens, S.; Prentice, A.M.; Belteki, G.; Constancia, M.; Dunger, D.; Affara, N. A. Periconceptional maternal micronutrient supplementation is associated with widespread gender related changes in the epigenome: a study of a unique resource in the Gambia. Hum. Mol. Genet2012, 21(9), 2086-2101.
    • (2012) Hum. Mol. Genet , vol.21 , Issue.9 , pp. 2086-2101
    • Khulan, B.1    Cooper, W.N.2    Skinner, B.M.3    Bauer, J.4    Owens, S.5    Prentice, A.M.6    Belteki, G.7    Constancia, M.8    Dunger, D.9    Affara, N.A.10
  • 117
    • 69149087790 scopus 로고    scopus 로고
    • Non-CpG methylation of the PGC-1alpha promoter through DNMT3B controls mitochondrial density
    • Barres, R.; Osler, M.E.; Yan, J.; Rune, A.; Fritz, T.; Caidahl, K.; Krook, A.; Zierath, J.R. Non-CpG methylation of the PGC-1alpha promoter through DNMT3B controls mitochondrial density. Cell Metab2009, 10(3), 189-198.
    • (2009) Cell Metab , vol.10 , Issue.3 , pp. 189-198
    • Barres, R.1    Osler, M.E.2    Yan, J.3    Rune, A.4    Fritz, T.5    Caidahl, K.6    Krook, A.7    Zierath, J.R.8
  • 118
    • 84899128768 scopus 로고    scopus 로고
    • Exercise prevents maternal high-fat dietinduced hypermethylation of the Pgc-1alpha gene and agedependent metabolic dysfunction in the offspring
    • Laker, R.C.; Lillard, T.S.; Okutsu, M.; Zhang, M.; Hoehn, K.L.; Connelly, J.J.; Yan, Z. Exercise prevents maternal high-fat dietinduced hypermethylation of the Pgc-1alpha gene and agedependent metabolic dysfunction in the offspring. Diabetes, 2014, 63(5), 1605-1611.
    • (2014) Diabetes , vol.63 , Issue.5 , pp. 1605-1611
    • Laker, R.C.1    Lillard, T.S.2    Okutsu, M.3    Zhang, M.4    Hoehn, K.L.5    Connelly, J.J.6    Yan, Z.7
  • 119
    • 0035177597 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A (mtTFA) and diabetes
    • Choi, Y.S.; Kim, S.; Pak, Y.K. Mitochondrial transcription factor A (mtTFA) and diabetes. Diabetes Res. Clin. Pract2001, 54 Suppl 2, S3-9.
    • (2001) Diabetes Res. Clin. Pract , vol.54 , pp. S3-S9
    • Choi, Y.S.1    Kim, S.2    Pak, Y.K.3
  • 120
    • 1842610582 scopus 로고    scopus 로고
    • NRF-2 transcription factor is essential in promoting human Tomm70 gene expression
    • Blesa, J.R.; Hernández, J.M.; Hernández-Yago, J. NRF-2 transcription factor is essential in promoting human Tomm70 gene expression. Mitochondrion, 2004, 3(5), 251-259.
    • (2004) Mitochondrion , vol.3 , Issue.5 , pp. 251-259
    • Blesa, J.R.1    Hernández, J.M.2    Hernández-Yago, J.3
  • 122
    • 14044261409 scopus 로고    scopus 로고
    • Alternative usages of multiple promoters of the acetyl-CoA carboxylase beta gene are related to differential transcriptional regulation in human and rodent tissues
    • Oh, S.Y.; Lee, M.Y.; Kim, J.M.; Yoon, S.; Shin, S.; Park, Y.N.; Ahn, Y.H.; Kim, K.S. Alternative usages of multiple promoters of the acetyl-CoA carboxylase beta gene are related to differential transcriptional regulation in human and rodent tissues. J. Biol. Chem2005, 280(7), 5909-5916.
    • (2005) J. Biol. Chem , vol.280 , Issue.7 , pp. 5909-5916
    • Oh, S.Y.1    Lee, M.Y.2    Kim, J.M.3    Yoon, S.4    Shin, S.5    Park, Y.N.6    Ahn, Y.H.7    Kim, K.S.8
  • 123
    • 77952060999 scopus 로고    scopus 로고
    • A. Role of Ucp1 enhancer methylation and chromatin remodelling in the control of Ucp1 expression in murine adipose tissue
    • Shore, A.; Karamitri, A.; Kemp, P.; Speakman, J. R.; Lomax, M. ARole of Ucp1 enhancer methylation and chromatin remodelling in the control of Ucp1 expression in murine adipose tissue. Diabetologia, 2010, 53(6), 1164-1173.
    • (2010) Diabetologia , vol.53 , Issue.6 , pp. 1164-1173
    • Shore, A.1    Karamitri, A.2    Kemp, P.3    Speakman, J.R.4    Lomax, M.5
  • 124
    • 0029121358 scopus 로고
    • Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor
    • Cavailles, V.; Dauvois, S.; L'Horset, F.; Lopez, G.; Hoare, S.; Kushner, P.J.; Parker, M.G. Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. EMBO J1995, 14(15), 3741-3751.
    • (1995) EMBO J , vol.14 , Issue.15 , pp. 3741-3751
    • Cavailles, V.1    Dauvois, S.2    L'Horset, F.3    Lopez, G.4    Hoare, S.5    Kushner, P.J.6    Parker, M.G.7
  • 126
    • 36549039059 scopus 로고    scopus 로고
    • G RIP140 directs histone and DNA methylation to silence Ucp1 expression in white adipocytes
    • Kiskinis, E.; Hallberg, M.; Christian, M.; Olofsson, M.; Dilworth, S. M.; White, R.; Parker, M. GRIP140 directs histone and DNA methylation to silence Ucp1 expression in white adipocytes. EMBO J2007, 26(23), 4831-4840.
    • (2007) EMBO J , vol.26 , Issue.23 , pp. 4831-4840
    • Kiskinis, E.1    Hallberg, M.2    Christian, M.3    Olofsson, M.4    Dilworth, S.M.5    White, R.6    Parker, M.7
  • 127
    • 79952749156 scopus 로고    scopus 로고
    • MDNA methyltransferase 1, cytosine methylation, and cytosine hydroxymethylation in mammalian mitochondria
    • Shock, L.S.; Thakkar, P.V.; Peterson, E.J.; Moran, R. G.; Taylor, S. MDNA methyltransferase 1, cytosine methylation, and cytosine hydroxymethylation in mammalian mitochondria. Proc. Natl. Acad. Sci. U S A, 2011, 108(9), 3630-3635.
    • (2011) Proc. Natl. Acad. Sci. U S A , vol.108 , Issue.9 , pp. 3630-3635
    • Shock, L.S.1    Thakkar, P.V.2    Peterson, E.J.3    Moran, R.G.4    Taylor, S.5
  • 128
    • 84891533924 scopus 로고    scopus 로고
    • JMitochondrial DNMT3A and DNA methylation in skeletal muscle and CNS of transgenic mouse models of ALS
    • Wong, M.; Gertz, B.; Chestnut, B. A.; Martin, L. JMitochondrial DNMT3A and DNA methylation in skeletal muscle and CNS of transgenic mouse models of ALS. Front. Cell. Neurosci2013, 7, 279.
    • (2013) Front. Cell. Neurosci , vol.7 , pp. 279
    • Wong, M.1    Gertz, B.2    Chestnut, B.A.3    Martin, L.4
  • 130
    • 40949126440 scopus 로고    scopus 로고
    • SMitochondrial complex III regulates hypoxic activation of HIF
    • Klimova, T.; Chandel, N. SMitochondrial complex III regulates hypoxic activation of HIF. Cell Death Differ2008, 15(4), 660-666.
    • (2008) Cell Death Differ , vol.15 , Issue.4 , pp. 660-666
    • Klimova, T.1    Chandel, N.2
  • 131
    • 84881344097 scopus 로고    scopus 로고
    • Phenotypic switching induced by damaged matrix is associated with DNA methyltransferase 3A (DNMT3A) activity and nuclear localization in smooth muscle cells (SMC)
    • Jiang, J.X.; Aitken, K.J.; Sotiropolous, C.; Kirwan, T.; Panchal, T.; Zhang, N.; Pu, S.; Wodak, S.; Tolg, C.; Bagli, D.J. Phenotypic switching induced by damaged matrix is associated with DNA methyltransferase 3A (DNMT3A) activity and nuclear localization in smooth muscle cells (SMC). PLoS One, 2013, 8(8), e69089.
    • (2013) PLoS One , vol.8 , Issue.8
    • Jiang, J.X.1    Aitken, K.J.2    Sotiropolous, C.3    Kirwan, T.4    Panchal, T.5    Zhang, N.6    Pu, S.7    Wodak, S.8    Tolg, C.9    Bagli, D.J.10
  • 132
    • 84864341714 scopus 로고    scopus 로고
    • The obesity-related peptide leptin sensitizes cardiac mitochondria to calcium-induced permeability transition pore opening and apoptosis
    • Martinez-Abundis, E.; Rajapurohitam, V.; Haist, J.V.; Gan, X.T.; Karmazyn, M. The obesity-related peptide leptin sensitizes cardiac mitochondria to calcium-induced permeability transition pore opening and apoptosis. PLoS One, 2012, 7(7), e41612.
    • (2012) PLoS One , vol.7 , Issue.7
    • Martinez-Abundis, E.1    Rajapurohitam, V.2    Haist, J.V.3    Gan, X.T.4    Karmazyn, M.5
  • 133
    • 84864941472 scopus 로고    scopus 로고
    • Obesity, Inflammation and Acute Myocardial Infarction - Expression of leptin, IL-6 and high sensitivity-CRP in Chennai based population
    • Rajendran, K.; Devarajan, N.; Ganesan, M.; Ragunathan, MObesity, Inflammation and Acute Myocardial Infarction - Expression of leptin, IL-6 and high sensitivity-CRP in Chennai based population. Thromb. J2012, 10(1), 13.
    • (2012) Thromb. J , vol.10 , Issue.1 , pp. 13
    • Rajendran, K.1    Devarajan, N.2    Ganesan, M.3    Ragunathan, M.4
  • 135
    • 33847367675 scopus 로고    scopus 로고
    • Non-genomic transgenerational inheritance of disease risk
    • Gluckman, P.D.; Hanson, M.A.; Beedle, A.S. Non-genomic transgenerational inheritance of disease risk. Bioessays, 2007, 29(2), 145-154.
    • (2007) Bioessays , vol.29 , Issue.2 , pp. 145-154
    • Gluckman, P.D.1    Hanson, M.A.2    Beedle, A.S.3
  • 138
    • 84893470415 scopus 로고    scopus 로고
    • Paternally induced transgenerational inheritance of susceptibility to diabetes in mammals
    • Wei, Y.; Yang, C.R.; Wei, Y.P.; Zhao, Z.A.; Hou, Y.; Schatten, H.; Sun, Q.Y. Paternally induced transgenerational inheritance of susceptibility to diabetes in mammals Proc. Natl. Acad. Sci. U S A, 2014, 111(5), 1873-1878
    • (2014) Proc. Natl. Acad. Sci. U S A , vol.111 , Issue.5 , pp. 1873-1878
    • Wei, Y.1    Yang, C.R.2    Wei, Y.P.3    Zhao, Z.A.4    Hou, Y.5    Schatten, H.6    Sun, Q.Y.7
  • 140
    • 33845744837 scopus 로고    scopus 로고
    • Initiation and beyond: Multiple functions of the human mitochondrial transcription machinery
    • Bonawitz, N.D.; Clayton, D.A.; Shadel, G.S. Initiation and beyond: multiple functions of the human mitochondrial transcription machinery. Mol. Cell, 2006, 24, 813-825.
    • (2006) Mol. Cell , vol.24 , pp. 813-825
    • Bonawitz, N.D.1    Clayton, D.A.2    Shadel, G.S.3
  • 141
    • 84877056321 scopus 로고    scopus 로고
    • TWINKLE is an essential mitochondrial helicase required for synthesis of nascent D-loop strands and complete mtDNA replication
    • Milenkovic, D.; Matic, S.; Kuhl, I.; Ruzzenente, B.; Freyer, C.; Jemt, E.; Park, C.B.; Falkenberg, M.; Larsson, N. G. TWINKLE is an essential mitochondrial helicase required for synthesis of nascent D-loop strands and complete mtDNA replication. Hum. Mol. Genet2013, 22(10), 1983-1993.
    • (2013) Hum. Mol. Genet , vol.22 , Issue.10 , pp. 1983-1993
    • Milenkovic, D.1    Matic, S.2    Kuhl, I.3    Ruzzenente, B.4    Freyer, C.5    Jemt, E.6    Park, C.B.7    Falkenberg, M.8    Larsson, N.G.9
  • 142
    • 84893317772 scopus 로고    scopus 로고
    • NReplication factors transiently associate with mtDNA at the mitochondrial inner membrane to facilitate replication
    • Rajala, N.; Gerhold, J.M.; Martinsson, P.; Klymov, A.; Spelbrink, J. NReplication factors transiently associate with mtDNA at the mitochondrial inner membrane to facilitate replication. Nucleic Acids Res2013, 42(2), 952-967.
    • (2013) Nucleic Acids Res , vol.42 , Issue.2 , pp. 952-967
    • Rajala, N.1    Gerhold, J.M.2    Martinsson, P.3    Klymov, A.4    Spelbrink, J.5
  • 143
    • 79952461851 scopus 로고    scopus 로고
    • The core human mitochondrial transcription initiation complex: It only takes two to tango
    • Shutt, T.E.; Bestwick, M.; Shadel, G.S. The core human mitochondrial transcription initiation complex: It only takes two to tango. Transcription, 2011, 2(2), 55-59.
    • (2011) Transcription , vol.2 , Issue.2 , pp. 55-59
    • Shutt, T.E.1    Bestwick, M.2    Shadel, G.S.3
  • 147
    • 33847656213 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A (TFAM): Roles in maintenance of mtDNA and cellular functions
    • Kang, D.; Kim, S.H.; Hamasaki, N. Mitochondrial transcription factor A (TFAM): roles in maintenance of mtDNA and cellular functions. Mitochondrion, 2007, 7(1-2), 39-44.
    • (2007) Mitochondrion , vol.7 , Issue.1-2 , pp. 39-44
    • Kang, D.1    Kim, S.H.2    Hamasaki, N.3
  • 148
    • 7644237446 scopus 로고    scopus 로고
    • Architectural role of mitochondrial transcription factor A in maintenance of human mitochondrial DNA
    • Kanki, T.; Ohgaki, K.; Gaspari, M.; Gustafsson, C.M.; Fukuoh, A.; Sasaki, N.; Hamasaki, N.; Kang, D. Architectural role of mitochondrial transcription factor A in maintenance of human mitochondrial DNA. Mol. Cell. Biol2004, 24(22), 9823-9834.
    • (2004) Mol. Cell. Biol , vol.24 , Issue.22 , pp. 9823-9834
    • Kanki, T.1    Ohgaki, K.2    Gaspari, M.3    Gustafsson, C.M.4    Fukuoh, A.5    Sasaki, N.6    Hamasaki, N.7    Kang, D.8
  • 150
    • 0033762782 scopus 로고    scopus 로고
    • GImpaired insulin secretion and beta-cell loss in tissue-specific knockout mice with mitochondrial diabetes
    • Silva, J. P.; Kohler, M.; Graff, C.; Oldfors, A.; Magnuson, M. A.; Berggren, P. O.; Larsson, N. GImpaired insulin secretion and beta-cell loss in tissue-specific knockout mice with mitochondrial diabetes. Nat. Genet2000, 26(3), 336-340.
    • (2000) Nat. Genet , vol.26 , Issue.3 , pp. 336-340
    • Silva, J.P.1    Kohler, M.2    Graff, C.3    Oldfors, A.4    Magnuson, M.A.5    Berggren, P.O.6    Larsson, N.7
  • 152
    • 84876428871 scopus 로고    scopus 로고
    • Aberrant Schwann cell lipid metabolism linked to mitochondrial deficits leads to axon degeneration and neuropathy
    • Viader, A.; Sasaki, Y.; Kim, S.; Strickland, A.; Workman, C.S.; Yang, K.; Gross, R.W.; Milbrandt, J. Aberrant Schwann cell lipid metabolism linked to mitochondrial deficits leads to axon degeneration and neuropathy. Neuron, 2013, 77(5), 886-898.
    • (2013) Neuron , vol.77 , Issue.5 , pp. 886-898
    • Viader, A.1    Sasaki, Y.2    Kim, S.3    Strickland, A.4    Workman, C.S.5    Yang, K.6    Gross, R.W.7    Milbrandt, J.8
  • 154
    • 84864308607 scopus 로고    scopus 로고
    • Mitochondrial DNA nucleoid structure
    • Bogenhagen, D.F. Mitochondrial DNA nucleoid structure. Biochim. Biophys. Acta, 2012, 1819(9-10), 914-920.
    • (2012) Biochim. Biophys. Acta , vol.1819 , Issue.9-10 , pp. 914-920
    • Bogenhagen, D.F.1
  • 155
    • 84882835838 scopus 로고    scopus 로고
    • mtDNA makes a U-turn for the mitochondrial nucleoid
    • Kukat, C.; Larsson, N.G. mtDNA makes a U-turn for the mitochondrial nucleoid. Trends Cell. Biol2013, 23(9), 457-463.
    • (2013) Trends Cell. Biol , vol.23 , Issue.9 , pp. 457-463
    • Kukat, C.1    Larsson, N.G.2
  • 156
    • 84864293013 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A regulates mitochondrial transcription initiation, DNA packaging, and genome copy number
    • Campbell, C.T.; Kolesar, J.E.; Kaufman, B.A. Mitochondrial transcription factor A regulates mitochondrial transcription initiation, DNA packaging, and genome copy number. Biochim. Biophys. Acta, 2012, 1819(9-10), 921-929.
    • (2012) Biochim. Biophys. Acta , vol.1819 , Issue.9-10 , pp. 921-929
    • Campbell, C.T.1    Kolesar, J.E.2    Kaufman, B.A.3
  • 157
    • 80555128721 scopus 로고    scopus 로고
    • The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA
    • Ngo, H.B.; Kaiser, J.T.; Chan, D.C.C. The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA. Nat. Struct. Mol. Biol2014, 18, 1290-1296.
    • (2014) Nat. Struct. Mol. Biol , vol.18 , pp. 1290-1296
    • Ngo, H.B.1    Kaiser, J.T.2    Chan, D.C.C.3
  • 159
    • 84864310340 scopus 로고    scopus 로고
    • Matrix proteases in mitochondrial DNA function
    • Matsushima, Y.; Kaguni, L.S. Matrix proteases in mitochondrial DNA function. Biochim. Biophys. Acta, 2012, 1819(9-10), 1080-1087.
    • (2012) Biochim. Biophys. Acta , vol.1819 , Issue.9-10 , pp. 1080-1087
    • Matsushima, Y.1    Kaguni, L.S.2
  • 160
    • 84872271398 scopus 로고    scopus 로고
    • Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease
    • Lu, B.; Lee, J.; Nie, X.; Li, M.; Morozov, Y.I.; Venkatesh, S.; Bogenhagen, D.F.; Temiakov, D.; Suzuki, C.K. Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease. Mol. Cell, 2013, 49(1), 121-132.
    • (2013) Mol. Cell , vol.49 , Issue.1 , pp. 121-132
    • Lu, B.1    Lee, J.2    Nie, X.3    Li, M.4    Morozov, Y.I.5    Venkatesh, S.6    Bogenhagen, D.F.7    Temiakov, D.8    Suzuki, C.K.9
  • 161
    • 78649842154 scopus 로고    scopus 로고
    • Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)
    • Matsushima, Y.; Goto, Y.; Kaguni, L.S. Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM). Proc. Natl. Acad. Sci. U S A, 2010, 107(43), 18410-18415.
    • (2010) Proc. Natl. Acad. Sci. U S A , vol.107 , Issue.43 , pp. 18410-18415
    • Matsushima, Y.1    Goto, Y.2    Kaguni, L.S.3
  • 163
    • 77954859197 scopus 로고    scopus 로고
    • The role of mitochondria in the pathogenesis of type 2 diabetes
    • Patti, M.E.; Corvera, S. The role of mitochondria in the pathogenesis of type 2 diabetes. Endocr. Rev2010, 31, 364-395.
    • (2010) Endocr. Rev , vol.31 , pp. 364-395
    • Patti, M.E.1    Corvera, S.2
  • 165
    • 21244477127 scopus 로고    scopus 로고
    • Exercise stimulates Pgc-1alpha transcription in skeletal muscle through activation of the p38 MAPK pathway
    • Akimoto, T.; Pohnert, S.C.; Li, P.; Zhang, M.; Gumbs, C.; Rosenberg, P.B.; Williams, R.S.; Yan, Z. Exercise stimulates Pgc-1alpha transcription in skeletal muscle through activation of the p38 MAPK pathway. J. Biol. Chem2005, 280(20), 19587-19593.
    • (2005) J. Biol. Chem , vol.280 , Issue.20 , pp. 19587-19593
    • Akimoto, T.1    Pohnert, S.C.2    Li, P.3    Zhang, M.4    Gumbs, C.5    Rosenberg, P.B.6    Williams, R.S.7    Yan, Z.8
  • 166
    • 35648937073 scopus 로고    scopus 로고
    • Skeletal muscle fiber-type switching, exercise intolerance, and myopathy in PGC-1alpha muscle-specific knock-out animals
    • Handschin, C.; Chin, S.; Li, P.; Liu, F.; Maratos-Flier, E.; Lebrasseur, N.K.; Yan, Z.; Spiegelman, B.M. Skeletal muscle fiber-type switching, exercise intolerance, and myopathy in PGC-1alpha muscle-specific knock-out animals. J. Biol. Chem2007, 282(41), 30014-30021.
    • (2007) J. Biol. Chem , vol.282 , Issue.41 , pp. 30014-30021
    • Handschin, C.1    Chin, S.2    Li, P.3    Liu, F.4    Maratos-Flier, E.5    Lebrasseur, N.K.6    Yan, Z.7    Spiegelman, B.M.8
  • 168
    • 34547545892 scopus 로고    scopus 로고
    • AMPactivated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha
    • Jager, S.; Handschin, C.; St-Pierre, J.; Spiegelman, B.M. AMPactivated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha. Proc. Natl. Acad. Sci. U S A, 2007, 104(29), 12017-12022.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , Issue.29 , pp. 12017-12022
    • Jager, S.1    Handschin, C.2    St-Pierre, J.3    Spiegelman, B.M.4
  • 169
  • 170
    • 36749081539 scopus 로고    scopus 로고
    • mTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex
    • Cunningham, J.T.; Rodgers, J.T.; Arlow, D.H.; Vazquez, F.; Mootha, V.K.; Puigserver, P. mTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex. Nature, 2007, 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
  • 173
    • 0019444843 scopus 로고
    • tRNA punctuation model of RNA processing in human mitochondria
    • Ojala, D.; Montoya, J.; Attardi, G. tRNA punctuation model of RNA processing in human mitochondria. Nature, 1981, 290(5806), 470-474.
    • (1981) Nature , vol.290 , Issue.5806 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 174
    • 84897527933 scopus 로고    scopus 로고
    • Initial steps in RNA processing and ribosome assembly occur at mitochondrial DNA nucleoids
    • Bogenhagen, D.F.; Martin, D.W.; Koller, A. Initial steps in RNA processing and ribosome assembly occur at mitochondrial DNA nucleoids. Cell Metab2014, 19(4), 618-629.
    • (2014) Cell Metab , vol.19 , Issue.4 , pp. 618-629
    • Bogenhagen, D.F.1    Martin, D.W.2    Koller, A.3
  • 175
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • Holzmann, J.; Frank, P.; Loffler, E.; Bennett, K.L.; Gerner, C.; Rossmanith, W. RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell, 2008, 135(3), 462-474.
    • (2008) Cell , vol.135 , Issue.3 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Loffler, E.3    Bennett, K.L.4    Gerner, C.5    Rossmanith, W.6
  • 178
    • 84875307449 scopus 로고    scopus 로고
    • Human mitochondrial RNA decay mediated by PNPase-hSuv3 complex takes place in distinct foci
    • Borowski, L.S.; Dziembowski, A.; Hejnowicz, M.S.; Stepien, P.P.; Szczesny, R.J. Human mitochondrial RNA decay mediated by PNPase-hSuv3 complex takes place in distinct foci. Nucleic Acids Res2013, 41(2), 1223-1240.
    • (2013) Nucleic Acids Res , vol.41 , Issue.2 , pp. 1223-1240
    • Borowski, L.S.1    Dziembowski, A.2    Hejnowicz, M.S.3    Stepien, P.P.4    Szczesny, R.J.5
  • 179
    • 84902436539 scopus 로고    scopus 로고
    • Helicase SUV3, polynucleotide phosphorylase, and mitochondrial polyadenylation polymerase form a transient complex to modulate mitochondrial mRNA polyadenylated tail lengths in response to energetic changes
    • Wang, D.D.; Guo, X.E.; Modrek, A.S.; Chen, C.F.; Chen, P.L.; Lee, W.H. Helicase SUV3, polynucleotide phosphorylase, and mitochondrial polyadenylation polymerase form a transient complex to modulate mitochondrial mRNA polyadenylated tail lengths in response to energetic changes. J. Biol. Chem2014, 289(24), 16727-16735.
    • (2014) J. Biol. Chem , vol.289 , Issue.24 , pp. 16727-16735
    • Wang, D.D.1    Guo, X.E.2    Modrek, A.S.3    Chen, C.F.4    Chen, P.L.5    Lee, W.H.6
  • 180
    • 55249119103 scopus 로고    scopus 로고
    • Role of SUV3 helicase in maintaining mitochondrial homeostasis in human cells
    • Khidr, L.; Wu, G.; Davila, A.; Procaccio, V.; Wallace, D.; Lee, W. H.C.P. Role of SUV3 helicase in maintaining mitochondrial homeostasis in human cells. J. Biol. Chem2008, 283, 27064-27073.
    • (2008) J. Biol. Chem , vol.283 , pp. 27064-27073
    • Khidr, L.1    Wu, G.2    Davila, A.3    Procaccio, V.4    Wallace, D.5    Lee, W.H.C.P.6
  • 182
    • 84869822219 scopus 로고    scopus 로고
    • LRPPRC/SLIRP suppresses PNPasemediated mRNA decay and promotes polyadenylation in human mitochondria
    • Chujo, T.; Ohira, T.; Sakaguchi, Y.; Goshima, N.; Nomura, N.; Nagao, A.; Suzuki, T. LRPPRC/SLIRP suppresses PNPasemediated mRNA decay and promotes polyadenylation in human mitochondria. Nucleic. Acids Res2012, 40(16), 8033-8047.
    • (2012) Nucleic. Acids Res , vol.40 , Issue.16 , pp. 8033-8047
    • Chujo, T.1    Ohira, T.2    Sakaguchi, Y.3    Goshima, N.4    Nomura, N.5    Nagao, A.6    Suzuki, T.7
  • 183
    • 84878408163 scopus 로고    scopus 로고
    • The leucine-rich pentatricopeptide repeatcontaining protein (LRPPRC) does not activate transcription in mammalian mitochondria
    • Harmel, J.; Ruzzenente, B.; Terzioglu, M.; Spahr, H.; Falkenberg, M.; Larsson, N.G. The leucine-rich pentatricopeptide repeatcontaining protein (LRPPRC) does not activate transcription in mammalian mitochondria. J. Biol. Chem2013, 288(22), 15510-15519.
    • (2013) J. Biol. Chem , vol.288 , Issue.22 , pp. 15510-15519
    • Harmel, J.1    Ruzzenente, B.2    Terzioglu, M.3    Spahr, H.4    Falkenberg, M.5    Larsson, N.G.6
  • 185
    • 84899852363 scopus 로고    scopus 로고
    • Functional genomic analysis of human mitochondrial RNA processing
    • Wolf, A.R.; Mootha, V.K. Functional genomic analysis of human mitochondrial RNA processing. Cell Rep2014, 7(3), 918-931.
    • (2014) Cell Rep , vol.7 , Issue.3 , pp. 918-931
    • Wolf, A.R.1    Mootha, V.K.2
  • 186
    • 0347444723 scopus 로고    scopus 로고
    • MicroRNAs: Genomics, biogenesis, mechanism, and function
    • Bartel, D.P. MicroRNAs: genomics, biogenesis, mechanism, and function. Cell, 2004, 116(2), 281-297.
    • (2004) Cell , vol.116 , Issue.2 , pp. 281-297
    • Bartel, D.P.1
  • 188
    • 84875309966 scopus 로고    scopus 로고
    • AThe mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression
    • Antonicka, H.; Sasarman, F.; Nishimura, T.; Paupe, V.; Shoubridge, E. AThe mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression. Cell Metab2013, 17, 386-398.
    • (2013) Cell Metab , vol.17 , pp. 386-398
    • Antonicka, H.1    Sasarman, F.2    Nishimura, T.3    Paupe, V.4    Shoubridge, E.5
  • 189
    • 80755169463 scopus 로고    scopus 로고
    • Human mitochondrial tRNAs: Biogenesis, function, structural aspects, and diseases
    • Suzuki, T.; Nagao, AHuman mitochondrial tRNAs: biogenesis, function, structural aspects, and diseases. Annu. Rev. Genet2011, 45, 299-329.
    • (2011) Annu. Rev. Genet , vol.45 , pp. 299-329
    • Suzuki, T.1    Nagao, A.2
  • 190
    • 0025666322 scopus 로고
    • A mutation in the tRNA(Leu)(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies
    • Goto, Y.; Nonaka, I.; Horai, S. A mutation in the tRNA(Leu)(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature, 1990, 348(6302), 651-653.
    • (1990) Nature , vol.348 , Issue.6302 , pp. 651-653
    • Goto, Y.1    Nonaka, I.2    Horai, S.3
  • 192
    • 84902869185 scopus 로고    scopus 로고
    • High-frequency involved hearing loss caused by novel mitochondrial DNA mutation in 16S ribosomal RNA gene
    • Abe, S.; Nagano, M.; Nishio, S.Y.; Kumakawa, K.; Usami, S. High-frequency involved hearing loss caused by novel mitochondrial DNA mutation in 16S ribosomal RNA gene. Otol. Neurotol2014, 35(6), 1087-1090.
    • (2014) Otol. Neurotol , vol.35 , Issue.6 , pp. 1087-1090
    • Abe, S.1    Nagano, M.2    Nishio, S.Y.3    Kumakawa, K.4    Usami, S.5
  • 193
    • 79251600222 scopus 로고    scopus 로고
    • Mitochondrial 12S rRNA mutations associated with aminoglycoside ototoxicity
    • Guan, M.X. Mitochondrial 12S rRNA mutations associated with aminoglycoside ototoxicity. Mitochondrion, 2010, 11(2), 237-245.
    • (2010) Mitochondrion , vol.11 , Issue.2 , pp. 237-245
    • Guan, M.X.1
  • 196
    • 84886684284 scopus 로고    scopus 로고
    • Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are positioned to modify nascent rRNA in foci near the mitochondrial DNA nucleoid
    • Lee, K.W.; Okot-Kotber, C.; LaComb, J.F.; Bogenhagen, D.F. Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are positioned to modify nascent rRNA in foci near the mitochondrial DNA nucleoid. J. Biol. Chem2013, 288(43), 31386-31399.
    • (2013) J. Biol. Chem , vol.288 , Issue.43 , pp. 31386-31399
    • Lee, K.W.1    Okot-Kotber, C.2    LaComb, J.F.3    Bogenhagen, D.F.4
  • 197
    • 84864319440 scopus 로고    scopus 로고
    • Mechanism of protein biosynthesis in mammalian mitochondria
    • Christian, B.E.; Spremulli, L.L. Mechanism of protein biosynthesis in mammalian mitochondria. Biochim. Biophys. Acta2012, 1819(9-10), 1035-1054.
    • (2012) Biochim. Biophys. Acta , vol.1819 , Issue.9-10 , pp. 1035-1054
    • Christian, B.E.1    Spremulli, L.L.2
  • 198
    • 84905820302 scopus 로고    scopus 로고
    • Making proteins in the powerhouse
    • Hallberg, B.M.; Larsson, N.G. Making proteins in the powerhouse. Cell Metab2014, 20(2), 226-240.
    • (2014) Cell Metab , vol.20 , Issue.2 , pp. 226-240
    • Hallberg, B.M.1    Larsson, N.G.2
  • 199
    • 77952472152 scopus 로고    scopus 로고
    • Mitochondrial translation and beyond: Processes implicated in combined oxidative phosphorylation deficiencies
    • Smits, P.; Smeitink, J.; van den Heuvel, L. Mitochondrial translation and beyond: processes implicated in combined oxidative phosphorylation deficiencies. J. Biomed. Biotechnol2010, 2010, 737385.
    • (2010) J. Biomed. Biotechnol , vol.2010
    • Smits, P.1    Smeitink, J.2    van den Heuvel, L.3
  • 202
    • 84859474843 scopus 로고    scopus 로고
    • Ribonucleoprotein Y-boxbinding protein-1 regulates mitochondrial oxidative phosphorylation (OXPHOS) protein expression after serum stimulation through binding to OXPHOS mRNA
    • Matsumoto, S.; Uchiumi, T.; Tanamachi, H.; Saito, T.; Yagi, M.; Takazaki, S.; Kanki, T.; Kang, D. Ribonucleoprotein Y-boxbinding protein-1 regulates mitochondrial oxidative phosphorylation (OXPHOS) protein expression after serum stimulation through binding to OXPHOS mRNA. Biochem. J2012, 443, 573-584.
    • (2012) Biochem. J , vol.443 , pp. 573-584
    • Matsumoto, S.1    Uchiumi, T.2    Tanamachi, H.3    Saito, T.4    Yagi, M.5    Takazaki, S.6    Kanki, T.7    Kang, D.8
  • 203
    • 84896716062 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria-a regulatory hub in metabolism, stress, and disease
    • Harbauer, A.B.; Zahedi, R.P.; Sickmann, A.; Pfanner, N.; Meisinger, C. The protein import machinery of mitochondria-a regulatory hub in metabolism, stress, and disease. Cell Metab2014, 19(3), 357-372.
    • (2014) Cell Metab , vol.19 , Issue.3 , pp. 357-372
    • Harbauer, A.B.1    Zahedi, R.P.2    Sickmann, A.3    Pfanner, N.4    Meisinger, C.5
  • 206
    • 33750986200 scopus 로고    scopus 로고
    • A new function in translocation for the mitochondrial i-AAA protease Yme1: Import of polynucleotide phosphorylase into the intermembrane space
    • Rainey, R.N.; Glavin, J.D.; Chen, H.W.; French, S.W.; Teitell, M. A.; Koehler, C.M. A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space. Mol. Cell. Biol2006, 26(22), 8488-8497.
    • (2006) Mol. Cell. Biol , vol.26 , Issue.22 , pp. 8488-8497
    • Rainey, R.N.1    Glavin, J.D.2    Chen, H.W.3    French, S.W.4    Teitell, M.A.5    Koehler, C.M.6
  • 210
    • 0141856299 scopus 로고    scopus 로고
    • The role of the 3' untranslated region in mRNA sorting to the vicinity of mitochondria is conserved from yeast to human cells
    • Sylvestre, J.; Margeot, A.; Jacq, C.; Dujardin, G.; Corral-Debrinski, MThe role of the 3' untranslated region in mRNA sorting to the vicinity of mitochondria is conserved from yeast to human cells. Mol. Biol. Cell, 2003, 14(9), 3848-3856.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.9 , pp. 3848-3856
    • Sylvestre, J.1    Margeot, A.2    Jacq, C.3    Dujardin, G.4    Corral-Debrinski, M.5
  • 211
    • 84882847104 scopus 로고    scopus 로고
    • Mitochondrial DNA methylation as a next-generation biomarker and diagnostic tool
    • Iacobazzi, V.; Castegna, A.; Infantino, V.; Andria, GMitochondrial DNA methylation as a next-generation biomarker and diagnostic tool. Mol. Genet. Metab2013, 110(1-2), 25-34.
    • (2013) Mol. Genet. Metab , vol.110 , Issue.1-2 , pp. 25-34
    • Iacobazzi, V.1    Castegna, A.2    Infantino, V.3    Andria, G.4
  • 212
    • 84882889657 scopus 로고    scopus 로고
    • The control region of mitochondrial DNA shows an unusual CpG and non-CpG methylation pattern
    • Bellizzi, D.; D'Aquila, P.; Scafone, T.; Giordano, M.; Riso, V.; Riccio, A.; Passarino, GThe control region of mitochondrial DNA shows an unusual CpG and non-CpG methylation pattern. DNA Res2013, 20(6), 537-547.
    • (2013) DNA Res , vol.20 , Issue.6 , pp. 537-547
    • Bellizzi, D.1    D'Aquila, P.2    Scafone, T.3    Giordano, M.4    Riso, V.5    Riccio, A.6    Passarino, G.7
  • 214
    • 84858000196 scopus 로고    scopus 로고
    • MicroRNAs in inflammation and immune responses
    • Contreras, J.; Rao, D.S. MicroRNAs in inflammation and immune responses. Leukemia, 2011, 26(3), 404-413.
    • (2011) Leukemia , vol.26 , Issue.3 , pp. 404-413
    • Contreras, J.1    Rao, D.S.2
  • 215
    • 84858776574 scopus 로고    scopus 로고
    • MicroRNAs in metabolism and metabolic disorders
    • Rottiers, V.; Naar, A.M. MicroRNAs in metabolism and metabolic disorders. Nat. Rev. Mol. Cell Biol2012, 13(4), 239-250.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , Issue.4 , pp. 239-250
    • Rottiers, V.1    Naar, A.M.2
  • 216
    • 84896916887 scopus 로고    scopus 로고
    • Identification of microRNA expression patterns in cutaneous and uveal melanoma cell lines
    • Venza, M.; Dell'Aversana, C.; Visalli, M.; Altucci, L.; Teti, D.; Venza, I. Identification of microRNA expression patterns in cutaneous and uveal melanoma cell lines. Tumori, 2014, 100(1), e4-7.
    • (2014) Tumori , vol.100 , Issue.1
    • Venza, M.1    Dell'Aversana, C.2    Visalli, M.3    Altucci, L.4    Teti, D.5    Venza, I.6
  • 219
    • 77955170881 scopus 로고    scopus 로고
    • Hypoxiaregulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression
    • Chen, Z.; Li, Y.; Zhang, H.; Huang, P.; Luthra, RHypoxiaregulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression. Oncogene, 2010, 29(30), 4362-4368.
    • (2010) Oncogene , vol.29 , Issue.30 , pp. 4362-4368
    • Chen, Z.1    Li, Y.2    Zhang, H.3    Huang, P.4    Luthra, R.5
  • 222
    • 84899103245 scopus 로고    scopus 로고
    • MicroRNA-149 inhibits PARP-2 and promotes mitochondrial biogenesis via SIRT-1/PGC-1alpha network in skeletal muscle
    • Mohamed, J.S.; Hajira, A.; Pardo, P.S.; Boriek, A.M. MicroRNA-149 inhibits PARP-2 and promotes mitochondrial biogenesis via SIRT-1/PGC-1alpha network in skeletal muscle. Diabetes, 2014, 63(5), 1546-1559.
    • (2014) Diabetes , vol.63 , Issue.5 , pp. 1546-1559
    • Mohamed, J.S.1    Hajira, A.2    Pardo, P.S.3    Boriek, A.M.4


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