메뉴 건너뛰기




Volumn 16, Issue 1, 2014, Pages 45-65

Krebs cycle intermediates regulate DNA and histone methylation: Epigenetic impact on the aging process

Author keywords

Aging; Energy metabolism; Epigenetics; Krebs cycle; Methylation; Mitochondria

Indexed keywords

2 HYDROXYGLUTARIC ACID; 2 OXOGLUTARATE DEPENDENT DIOXYGENASE; 2 OXOGLUTARIC ACID; DIOXYGENASE; FUMARIC ACID; HISTONE DEMETHYLASE; KDM 2 PROTEIN; KDM 3 PROTEIN; KDM 4 PROTEIN; KDM 5 PROTEIN; KDM 6 PROTEIN; KDM 7 PROTEIN; OXOGLUTARATE DEHYDROGENASE; SUCCINATE DEHYDROGENASE; SUCCINIC ACID; UNCLASSIFIED DRUG; HISTONE;

EID: 84902685602     PISSN: 15681637     EISSN: 18729649     Source Type: Journal    
DOI: 10.1016/j.arr.2014.05.004     Document Type: Review
Times cited : (100)

References (347)
  • 4
    • 66149138053 scopus 로고    scopus 로고
    • The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence
    • Agger K., Cloos P.A., Rudkjaer L., Williams K., Andersen G., Christensen J., Helin K. The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence. Genes Dev. 2009, 23:1171-1176.
    • (2009) Genes Dev. , vol.23 , pp. 1171-1176
    • Agger, K.1    Cloos, P.A.2    Rudkjaer, L.3    Williams, K.4    Andersen, G.5    Christensen, J.6    Helin, K.7
  • 5
    • 80051679799 scopus 로고    scopus 로고
    • Long noncoding RNA, polycomb, and the ghosts haunting INK4b-ARF-INK4a expression
    • Aguilo F., Zhou M.M., Walsh M.J. Long noncoding RNA, polycomb, and the ghosts haunting INK4b-ARF-INK4a expression. Cancer Res. 2011, 71:5365-5369.
    • (2011) Cancer Res. , vol.71 , pp. 5365-5369
    • Aguilo, F.1    Zhou, M.M.2    Walsh, M.J.3
  • 9
    • 69049088683 scopus 로고    scopus 로고
    • Regulatory role of HIF-1α in the pathogenesis of age-related macular degeneration (AMD)
    • Arjamaa O., Nikinmaa M., Salminen A., Kaarniranta K. Regulatory role of HIF-1α in the pathogenesis of age-related macular degeneration (AMD). Ageing Res. Rev. 2009, 8:349-358.
    • (2009) Ageing Res. Rev. , vol.8 , pp. 349-358
    • Arjamaa, O.1    Nikinmaa, M.2    Salminen, A.3    Kaarniranta, K.4
  • 10
    • 84868156972 scopus 로고    scopus 로고
    • The histone demethylase PHF8 is essential for cytoskeleton dynamics
    • Asensio-Juan E., Gallego C., Martinez-Balbas M.A. The histone demethylase PHF8 is essential for cytoskeleton dynamics. Nucleic Acids Res. 2012, 40:9429-9440.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9429-9440
    • Asensio-Juan, E.1    Gallego, C.2    Martinez-Balbas, M.A.3
  • 11
    • 84871005673 scopus 로고    scopus 로고
    • The pathways of mitophagy for quality control and clearance of mitochondria
    • Ashrafi G., Schwarz T.L. The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differ. 2013, 20:31-42.
    • (2013) Cell Death Differ. , vol.20 , pp. 31-42
    • Ashrafi, G.1    Schwarz, T.L.2
  • 12
    • 84875424617 scopus 로고    scopus 로고
    • Emerging roles for chromatin as a signal integration and storage platform
    • Badeaux A.I., Shi Y. Emerging roles for chromatin as a signal integration and storage platform. Nat. Rev. Mol. Cell Biol. 2013, 14:211-224.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 211-224
    • Badeaux, A.I.1    Shi, Y.2
  • 15
    • 0035978878 scopus 로고    scopus 로고
    • Molecular mechanisms of ageing in connective tissues
    • Bailey A.J. Molecular mechanisms of ageing in connective tissues. Mech. Ageing Dev. 2001, 122:735-755.
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 735-755
    • Bailey, A.J.1
  • 17
    • 70649089277 scopus 로고    scopus 로고
    • A ketogenic diet increases succinic dehydrogenase (SDH) activity and recovers age-related decrease in numeric density of SDH-positive mitochondria in cerebellar Purkinje cells of late-adult rats
    • Balietti M., Giorgetti B., Di Stefano G., Casoli T., Platano D., Solazzi M., Bertoni-Freddari C., Aicardi G., Lattanzio F., Fattoretti P. A ketogenic diet increases succinic dehydrogenase (SDH) activity and recovers age-related decrease in numeric density of SDH-positive mitochondria in cerebellar Purkinje cells of late-adult rats. Micron 2010, 41:143-148.
    • (2010) Micron , vol.41 , pp. 143-148
    • Balietti, M.1    Giorgetti, B.2    Di Stefano, G.3    Casoli, T.4    Platano, D.5    Solazzi, M.6    Bertoni-Freddari, C.7    Aicardi, G.8    Lattanzio, F.9    Fattoretti, P.10
  • 18
    • 68549135295 scopus 로고    scopus 로고
    • Hypoxia-induced BNIP3 expression and mitophagy: in vivo comparison of the rat and the hypoxia-tolerant mole rat, Spalax ehrenbergi
    • Band M., Joel A., Hernandez A., Avivi A. Hypoxia-induced BNIP3 expression and mitophagy: in vivo comparison of the rat and the hypoxia-tolerant mole rat, Spalax ehrenbergi. FASEB J. 2009, 23:2327-2335.
    • (2009) FASEB J. , vol.23 , pp. 2327-2335
    • Band, M.1    Joel, A.2    Hernandez, A.3    Avivi, A.4
  • 19
    • 80054080265 scopus 로고    scopus 로고
    • Polycomb group proteins: repression in 3D
    • Bantignies F., Cavalli G. Polycomb group proteins: repression in 3D. Trends Genet. 2011, 27:454-464.
    • (2011) Trends Genet. , vol.27 , pp. 454-464
    • Bantignies, F.1    Cavalli, G.2
  • 20
    • 0142052858 scopus 로고    scopus 로고
    • Insulin/IGF-I-signaling pathway: an evolutionarily conserved mechanism of longevity from yeast to humans
    • Barbieri M., Bonafe M., Franceschi C., Paolisso G. Insulin/IGF-I-signaling pathway: an evolutionarily conserved mechanism of longevity from yeast to humans. Am. J. Physiol. Endocrinol. Metab. 2003, 285:E1064-E1071.
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.285
    • Barbieri, M.1    Bonafe, M.2    Franceschi, C.3    Paolisso, G.4
  • 22
    • 84875965163 scopus 로고    scopus 로고
    • Proliferation-dependent alterations of the DNA methylation landscape underlie hematopoietic stem cell aging
    • Beerman I., Bock C., Garrison B.S., Smith Z.D., Gu H., Meissner A., Rossi D.J. Proliferation-dependent alterations of the DNA methylation landscape underlie hematopoietic stem cell aging. Cell Stem Cell 2013, 12:413-425.
    • (2013) Cell Stem Cell , vol.12 , pp. 413-425
    • Beerman, I.1    Bock, C.2    Garrison, B.S.3    Smith, Z.D.4    Gu, H.5    Meissner, A.6    Rossi, D.J.7
  • 24
    • 79955483643 scopus 로고    scopus 로고
    • Hypoxia-induced angiogenesis is delayed in aging mouse brain
    • Benderro G.F., Lamanna J.C. Hypoxia-induced angiogenesis is delayed in aging mouse brain. Brain Res. 2011, 1389:50-60.
    • (2011) Brain Res. , vol.1389 , pp. 50-60
    • Benderro, G.F.1    Lamanna, J.C.2
  • 25
    • 0030577032 scopus 로고    scopus 로고
    • Age-dependent decrease in the activity of succinic dehydrogenase in rat CA1 pyramidal cells: a quantitative cytochemical study
    • Bertoni-Freddari C., Fattoretti P., Caselli U., Paoloni R., Meier-Ruge W. Age-dependent decrease in the activity of succinic dehydrogenase in rat CA1 pyramidal cells: a quantitative cytochemical study. Mech. Ageing Dev. 1996, 90:53-62.
    • (1996) Mech. Ageing Dev. , vol.90 , pp. 53-62
    • Bertoni-Freddari, C.1    Fattoretti, P.2    Caselli, U.3    Paoloni, R.4    Meier-Ruge, W.5
  • 26
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • Beyer S., Kristensen M.M., Jensen K.S., Johansen J.V., Staller P. The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J. Biol. Chem. 2008, 283:36542-36552.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36542-36552
    • Beyer, S.1    Kristensen, M.M.2    Jensen, K.S.3    Johansen, J.V.4    Staller, P.5
  • 27
    • 84870375316 scopus 로고    scopus 로고
    • Histone lysine methylation dynamics: establishment, regulation, and biological impact
    • Black J.C., Van Rechem C., Whetstine J.R. Histone lysine methylation dynamics: establishment, regulation, and biological impact. Mol. Cell 2012, 48:491-507.
    • (2012) Mol. Cell , vol.48 , pp. 491-507
    • Black, J.C.1    Van Rechem, C.2    Whetstine, J.R.3
  • 28
    • 84874801912 scopus 로고    scopus 로고
    • Answering the ultimate question what is the proximal cause of aging?
    • Blagosklonny M.V. Answering the ultimate question what is the proximal cause of aging?. Aging (Albany, NY) 2012, 4:861-877.
    • (2012) Aging (Albany, NY) , vol.4 , pp. 861-877
    • Blagosklonny, M.V.1
  • 29
    • 84888133742 scopus 로고    scopus 로고
    • Epigenetic changes in the progression of Alzheimer's disease
    • Bradley-Whitman M.A., Lovell M.A. Epigenetic changes in the progression of Alzheimer's disease. Mech. Ageing Dev. 2013, 134:486-495.
    • (2013) Mech. Ageing Dev. , vol.134 , pp. 486-495
    • Bradley-Whitman, M.A.1    Lovell, M.A.2
  • 32
    • 0032831589 scopus 로고    scopus 로고
    • Overhydroxylation of lysyl residues is the initial step for altered collagen cross-links and fibril architecture in fibrotic skin
    • Brinckmann J., Notbohm H., Tronnier M., Acil Y., Fietzek P.P., Schmeller W., Muller P.K., Bätge B. Overhydroxylation of lysyl residues is the initial step for altered collagen cross-links and fibril architecture in fibrotic skin. J. Invest. Dermatol. 1999, 113:617-621.
    • (1999) J. Invest. Dermatol. , vol.113 , pp. 617-621
    • Brinckmann, J.1    Notbohm, H.2    Tronnier, M.3    Acil, Y.4    Fietzek, P.P.5    Schmeller, W.6    Muller, P.K.7    Bätge, B.8
  • 33
    • 84876861651 scopus 로고    scopus 로고
    • Regulation of succinate-fuelled mitochondrial respiration in liver and skeletal muscle of hibernating thirteen-lined ground squirrels
    • Brown J.C., Chung D.J., Cooper A.N., Staples J.F. Regulation of succinate-fuelled mitochondrial respiration in liver and skeletal muscle of hibernating thirteen-lined ground squirrels. J. Exp. Biol. 2013, 216:1736-1743.
    • (2013) J. Exp. Biol. , vol.216 , pp. 1736-1743
    • Brown, J.C.1    Chung, D.J.2    Cooper, A.N.3    Staples, J.F.4
  • 35
    • 0036408866 scopus 로고    scopus 로고
    • Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species
    • Bunik V.I., Sievers C. Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur. J. Biochem. 2002, 269:5004-5015.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5004-5015
    • Bunik, V.I.1    Sievers, C.2
  • 36
    • 0037352050 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase complexes in redox regulation. Role of the lipoate residues and thioredoxin
    • Bunik V.I. 2-Oxo acid dehydrogenase complexes in redox regulation. Role of the lipoate residues and thioredoxin. Eur. J. Biochem. 2003, 270:1036-1042.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1036-1042
    • Bunik, V.I.1
  • 37
    • 70249150389 scopus 로고    scopus 로고
    • Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-kingdom comparison of the crossroad between energy production and nitrogen assimilation
    • Bunik V.I., Fernie A.R. Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-kingdom comparison of the crossroad between energy production and nitrogen assimilation. Biochem. J 2009, 422:405-421.
    • (2009) Biochem. J , vol.422 , pp. 405-421
    • Bunik, V.I.1    Fernie, A.R.2
  • 38
    • 77954950116 scopus 로고    scopus 로고
    • Progeria syndromes and ageing: what is the connection? Nat
    • Burtner C.R., Kennedy B.K. Progeria syndromes and ageing: what is the connection? Nat. Rev. Mol. Cell. Biol. 2010, 11:567-578.
    • (2010) Rev. Mol. Cell. Biol. , vol.11 , pp. 567-578
    • Burtner, C.R.1    Kennedy, B.K.2
  • 39
    • 68149100569 scopus 로고    scopus 로고
    • The role of epigenetics in aging and age-related diseases
    • Calvanese V., Lara E., Kahn A., Fraga M.F. The role of epigenetics in aging and age-related diseases. Ageing Res. Rev. 2009, 8:268-276.
    • (2009) Ageing Res. Rev. , vol.8 , pp. 268-276
    • Calvanese, V.1    Lara, E.2    Kahn, A.3    Fraga, M.F.4
  • 40
    • 33749246561 scopus 로고    scopus 로고
    • Epigenetic gene regulation in the bacterial world
    • Casadesus J., Low D. Epigenetic gene regulation in the bacterial world. Microbiol. Mol. Biol. Rev. 2006, 70:830-856.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 830-856
    • Casadesus, J.1    Low, D.2
  • 41
    • 84868593544 scopus 로고    scopus 로고
    • Kinetic analysis of iron-dependent histone demethylases: α-ketoglutarate substrate inhibition and potential relevance to the regulation of histone demethylation in cancer cells
    • Cascella B., Mirica L.M. Kinetic analysis of iron-dependent histone demethylases: α-ketoglutarate substrate inhibition and potential relevance to the regulation of histone demethylation in cancer cells. Biochemistry 2012, 51:8699-8701.
    • (2012) Biochemistry , vol.51 , pp. 8699-8701
    • Cascella, B.1    Mirica, L.M.2
  • 42
    • 84861912630 scopus 로고    scopus 로고
    • Programming of DNA methylation patterns
    • Cedar H., Bergman Y. Programming of DNA methylation patterns. Annu. Rev. Biochem. 2012, 81:97-117.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 97-117
    • Cedar, H.1    Bergman, Y.2
  • 43
    • 70450239624 scopus 로고    scopus 로고
    • Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells
    • Cervera A.M., Bayley J.P., Devilee P., McCreath K.J. Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells. Mol. Cancer 2009, 8:89.
    • (2009) Mol. Cancer , vol.8 , pp. 89
    • Cervera, A.M.1    Bayley, J.P.2    Devilee, P.3    McCreath, K.J.4
  • 44
    • 0032464203 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial function in skeletal muscle: effects of aging and exercise training
    • Chandwaney R., Leichtweis S., Leeuwenburgh C., Ji L.L. Oxidative stress and mitochondrial function in skeletal muscle: effects of aging and exercise training. Age (Omaha) 1998, 21:109-117.
    • (1998) Age (Omaha) , vol.21 , pp. 109-117
    • Chandwaney, R.1    Leichtweis, S.2    Leeuwenburgh, C.3    Ji, L.L.4
  • 45
    • 84862994335 scopus 로고    scopus 로고
    • Effect of aging on 5-hydroxymethylcytosine in the mouse hippocampus
    • Chen H., Dzitoyeva S., Manev H. Effect of aging on 5-hydroxymethylcytosine in the mouse hippocampus. Restor. Neurol. Neurosci. 2012, 30:237-245.
    • (2012) Restor. Neurol. Neurosci. , vol.30 , pp. 237-245
    • Chen, H.1    Dzitoyeva, S.2    Manev, H.3
  • 47
    • 84872953223 scopus 로고    scopus 로고
    • TET2 promotes histone O-GlcNAcylation during gene transcription
    • Chen Q., Chen Y., Bian C., Fujiki R., Yu X. TET2 promotes histone O-GlcNAcylation during gene transcription. Nature 2013, 493:561-564.
    • (2013) Nature , vol.493 , pp. 561-564
    • Chen, Q.1    Chen, Y.2    Bian, C.3    Fujiki, R.4    Yu, X.5
  • 50
    • 84879605512 scopus 로고    scopus 로고
    • Which way does the citric acid cycle turn during hypoxia? The critical role of α-ketoglutarate dehydrogenase complex
    • Chinopoulos C. Which way does the citric acid cycle turn during hypoxia? The critical role of α-ketoglutarate dehydrogenase complex. J. Neurosci. Res. 2013, 91:1030-1043.
    • (2013) J. Neurosci. Res. , vol.91 , pp. 1030-1043
    • Chinopoulos, C.1
  • 56
    • 0035150397 scopus 로고    scopus 로고
    • JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2β
    • Clissold P.M., Ponting C.P. JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2β. Trends Biochem. Sci. 2001, 26:7-9.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 7-9
    • Clissold, P.M.1    Ponting, C.P.2
  • 57
    • 43249102851 scopus 로고    scopus 로고
    • Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease
    • Cloos P.A., Christensen J., Agger K., Helin K. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. Genes Dev. 2008, 22:1115-1140.
    • (2008) Genes Dev. , vol.22 , pp. 1115-1140
    • Cloos, P.A.1    Christensen, J.2    Agger, K.3    Helin, K.4
  • 58
    • 34447543913 scopus 로고    scopus 로고
    • Cellular senescence in cancer and aging
    • Collado M., Blasco M.A., Serrano M. Cellular senescence in cancer and aging. Cell 2007, 130:223-233.
    • (2007) Cell , vol.130 , pp. 223-233
    • Collado, M.1    Blasco, M.A.2    Serrano, M.3
  • 60
    • 75349111140 scopus 로고    scopus 로고
    • Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria
    • Cimen H., Han M.J., Yang Y., Tong Q., Koc H., Koc E.C. Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry 2010, 49:304-311.
    • (2010) Biochemistry , vol.49 , pp. 304-311
    • Cimen, H.1    Han, M.J.2    Yang, Y.3    Tong, Q.4    Koc, H.5    Koc, E.C.6
  • 65
    • 84862831187 scopus 로고    scopus 로고
    • Gene networking and inflammatory pathway analysis in a JMJD3 knockdown human monocytic cell line
    • Das N.D., Jung K.H., Choi M.R., Yoon H.S., Kim S.H., Chai Y.G. Gene networking and inflammatory pathway analysis in a JMJD3 knockdown human monocytic cell line. Cell Biochem. Funct. 2012, 30:224-232.
    • (2012) Cell Biochem. Funct. , vol.30 , pp. 224-232
    • Das, N.D.1    Jung, K.H.2    Choi, M.R.3    Yoon, H.S.4    Kim, S.H.5    Chai, Y.G.6
  • 66
    • 70349303869 scopus 로고    scopus 로고
    • Predation between prokaryotes and the origin of eukaryotes
    • Davidov Y., Jurkevitch E. Predation between prokaryotes and the origin of eukaryotes. Bioessays 2009, 31:748-757.
    • (2009) Bioessays , vol.31 , pp. 748-757
    • Davidov, Y.1    Jurkevitch, E.2
  • 67
    • 79956330964 scopus 로고    scopus 로고
    • CpG islands and the regulation of transcription
    • Deaton A.M., Bird A. CpG islands and the regulation of transcription. Genes Dev. 2011, 25:1010-1022.
    • (2011) Genes Dev. , vol.25 , pp. 1010-1022
    • Deaton, A.M.1    Bird, A.2
  • 68
    • 0028467960 scopus 로고
    • 2-oxoglutarate-dependent dioxygenase and related enzymes: biochemical characterization
    • De Carolis E., De Luca V. 2-oxoglutarate-dependent dioxygenase and related enzymes: biochemical characterization. Phytochemistry 1994, 36:1093-1107.
    • (1994) Phytochemistry , vol.36 , pp. 1093-1107
    • De Carolis, E.1    De Luca, V.2
  • 69
  • 70
    • 68649090226 scopus 로고    scopus 로고
    • Regulation of mitochondrial dehydrogenases by calcium ions
    • Denton R.M. Regulation of mitochondrial dehydrogenases by calcium ions. Biochim. Biophys. Acta 2009, 1787:1309-1316.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1309-1316
    • Denton, R.M.1
  • 72
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G., Natoli G. The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 2007, 130:1083-1094.
    • (2007) Cell , vol.130 , pp. 1083-1094
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 74
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • Detmer S.A., Chan D.C. Functions and dysfunctions of mitochondrial dynamics. Nat. Rev. Mol. Cell Biol. 2007, 8:870-879.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 870-879
    • Detmer, S.A.1    Chan, D.C.2
  • 75
    • 80053355301 scopus 로고    scopus 로고
    • Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences the circadian clock
    • DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J., Panda S. Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences the circadian clock. Science 2011, 333:1881-1885.
    • (2011) Science , vol.333 , pp. 1881-1885
    • DiTacchio, L.1    Le, H.D.2    Vollmers, C.3    Hatori, M.4    Witcher, M.5    Secombe, J.6    Panda, S.7
  • 76
    • 79958036128 scopus 로고    scopus 로고
    • Successful aging and sustained good health in the naked mole rat: a long-lived mammalian model for biogerontology and biomedical research
    • Edrey Y.H., Hanes M., Pinto M., Mele J., Buffenstein R. Successful aging and sustained good health in the naked mole rat: a long-lived mammalian model for biogerontology and biomedical research. ILAR J. 2011, 52:41-53.
    • (2011) ILAR J. , vol.52 , pp. 41-53
    • Edrey, Y.H.1    Hanes, M.2    Pinto, M.3    Mele, J.4    Buffenstein, R.5
  • 77
    • 0037364314 scopus 로고    scopus 로고
    • A role for mitochondrial enzymes in inherited neoplasia and beyond
    • Eng C., Kiuru M., Fernandez M.J., Aaltonen L.A. A role for mitochondrial enzymes in inherited neoplasia and beyond. Nat. Rev. Cancer 2003, 3:193-202.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 193-202
    • Eng, C.1    Kiuru, M.2    Fernandez, M.J.3    Aaltonen, L.A.4
  • 79
    • 84873369257 scopus 로고    scopus 로고
    • RNA polymerase II progression through H3K27me3-enriched gene bodies requires JMJD3 histone demethylase
    • Estaras C., Fueyo R., Akizu N., Beltran S., Martinez-Balbas M.A. RNA polymerase II progression through H3K27me3-enriched gene bodies requires JMJD3 histone demethylase. Mol. Biol. Cell 2013, 24:351-360.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 351-360
    • Estaras, C.1    Fueyo, R.2    Akizu, N.3    Beltran, S.4    Martinez-Balbas, M.A.5
  • 81
    • 77950521594 scopus 로고    scopus 로고
    • PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
    • Feng W., Yonezawa M., Ye J., Jenuwein T., Grummt I. PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation. Nat. Struct. Mol. Biol. 2010, 17:445-450.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 445-450
    • Feng, W.1    Yonezawa, M.2    Ye, J.3    Jenuwein, T.4    Grummt, I.5
  • 82
    • 79960137178 scopus 로고    scopus 로고
    • The effects of the dietary polyphenol resveratrol on human healthy aging and lifespan
    • Fernandez A.F., Fraga M.F. The effects of the dietary polyphenol resveratrol on human healthy aging and lifespan. Epigenetics 2011, 6:870-874.
    • (2011) Epigenetics , vol.6 , pp. 870-874
    • Fernandez, A.F.1    Fraga, M.F.2
  • 83
    • 79959836522 scopus 로고    scopus 로고
    • Chromatin structure as a mediator of aging
    • Feser J., Tyler J. Chromatin structure as a mediator of aging. FEBS Lett. 2011, 585:2041-2048.
    • (2011) FEBS Lett. , vol.585 , pp. 2041-2048
    • Feser, J.1    Tyler, J.2
  • 84
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T., Holbrook N.J. Oxidants, oxidative stress and the biology of ageing. Nature 2000, 408:239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 86
  • 89
    • 84870152439 scopus 로고    scopus 로고
    • 5-Methylcytosine DNA demethylation: more than losing a methyl group
    • Franchini D.M., Schmitz K.M., Petersen-Mahrt S.K. 5-Methylcytosine DNA demethylation: more than losing a methyl group. Annu. Rev. Genet. 2012, 46:419-441.
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 419-441
    • Franchini, D.M.1    Schmitz, K.M.2    Petersen-Mahrt, S.K.3
  • 90
    • 84876057074 scopus 로고    scopus 로고
    • Indy mutants: live long and prosper
    • Frankel S., Rogina B. Indy mutants: live long and prosper. Front. Genet. 2012, 3:13.
    • (2012) Front. Genet. , vol.3 , pp. 13
    • Frankel, S.1    Rogina, B.2
  • 91
    • 36049022778 scopus 로고    scopus 로고
    • JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes
    • Frescas D., Guardavaccaro D., Bassermann F., Koyama-Nasu R., Pagano M. JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes. Nature 2007, 450:309-313.
    • (2007) Nature , vol.450 , pp. 309-313
    • Frescas, D.1    Guardavaccaro, D.2    Bassermann, F.3    Koyama-Nasu, R.4    Pagano, M.5
  • 92
    • 48949119155 scopus 로고    scopus 로고
    • Mitochondrial protein quality control: implications in ageing
    • Friguet B., Bulteau A.L., Petropoulos I. Mitochondrial protein quality control: implications in ageing. Biotechnol. J. 2008, 3:757-764.
    • (2008) Biotechnol. J. , vol.3 , pp. 757-764
    • Friguet, B.1    Bulteau, A.L.2    Petropoulos, I.3
  • 95
    • 78349297565 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications
    • Giacco F., Brownlee M. Oxidative stress and diabetic complications. Circ. Res. 2010, 107:1058-1070.
    • (2010) Circ. Res. , vol.107 , pp. 1058-1070
    • Giacco, F.1    Brownlee, M.2
  • 97
    • 71849095133 scopus 로고    scopus 로고
    • Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases
    • Gibson G.E., Starkov A., Blass J.P., Ratan R.R., Beal M.F. Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases. Biochim. Biophys. Acta 2010, 1802:122-134.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 122-134
    • Gibson, G.E.1    Starkov, A.2    Blass, J.P.3    Ratan, R.R.4    Beal, M.F.5
  • 98
    • 33747587608 scopus 로고    scopus 로고
    • Regulation of the INK4b-ARF-INK4a tumour suppressor locus: all for one or one for all
    • Gil J., Peters G. Regulation of the INK4b-ARF-INK4a tumour suppressor locus: all for one or one for all. Nat. Rev. Mol. Cell Biol. 2006, 7:667-677.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 667-677
    • Gil, J.1    Peters, G.2
  • 100
    • 77955651636 scopus 로고    scopus 로고
    • Epigenetic alterations in aging
    • Gonzalo S. Epigenetic alterations in aging. J. Appl. Physiol. 2010, 109:586-597.
    • (2010) J. Appl. Physiol. , vol.109 , pp. 586-597
    • Gonzalo, S.1
  • 101
    • 84883457895 scopus 로고    scopus 로고
    • Facts and controversies in our understanding of how caloric restriction impacts the mitochondrion
    • Gouspillou G., Hepple R.T. Facts and controversies in our understanding of how caloric restriction impacts the mitochondrion. Exp. Gerontol. 2013, 48:1075-1084.
    • (2013) Exp. Gerontol. , vol.48 , pp. 1075-1084
    • Gouspillou, G.1    Hepple, R.T.2
  • 102
    • 73749085370 scopus 로고    scopus 로고
    • Epigenetic factors in aging and longevity
    • Gravina S., Vijg J. Epigenetic factors in aging and longevity. Pflugers Arch. 2010, 459:247-258.
    • (2010) Pflugers Arch. , vol.459 , pp. 247-258
    • Gravina, S.1    Vijg, J.2
  • 103
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray M.W., Burger G., Lang B.F. Mitochondrial evolution. Science 1999, 283:1476-1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 104
    • 84859893371 scopus 로고    scopus 로고
    • Histone methylation: a dynamic mark in health, disease and inheritance
    • Greer E.L., Shi Y. Histone methylation: a dynamic mark in health, disease and inheritance. Nat. Rev. Genet. 2012, 13:343-357.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 343-357
    • Greer, E.L.1    Shi, Y.2
  • 107
    • 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, 132:171-176.
    • (2008) Cell , vol.132 , pp. 171-176
    • Guarente, L.1
  • 108
    • 0034626747 scopus 로고    scopus 로고
    • Genetic pathways that regulate ageing in model organisms
    • Guarente L., Kenyon C. Genetic pathways that regulate ageing in model organisms. Nature 2000, 408:255-262.
    • (2000) Nature , vol.408 , pp. 255-262
    • Guarente, L.1    Kenyon, C.2
  • 109
    • 79955538247 scopus 로고    scopus 로고
    • Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain
    • Guo J.U., Su Y., Zhong C., Ming G.L., Song H. Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain. Cell 2011, 145:423-434.
    • (2011) Cell , vol.145 , pp. 423-434
    • Guo, J.U.1    Su, Y.2    Zhong, C.3    Ming, G.L.4    Song, H.5
  • 110
    • 3543148408 scopus 로고    scopus 로고
    • Krebs cycle enzymes from livers of old mice are differentially regulated by caloric restriction
    • Hagopian K., Ramsey J.J., Weindruch R. Krebs cycle enzymes from livers of old mice are differentially regulated by caloric restriction. Exp. Gerontol. 2004, 39:1145-1154.
    • (2004) Exp. Gerontol. , vol.39 , pp. 1145-1154
    • Hagopian, K.1    Ramsey, J.J.2    Weindruch, R.3
  • 112
    • 84855321183 scopus 로고    scopus 로고
    • Histone methylation makes its mark on longevity
    • Han S., Brunet A. Histone methylation makes its mark on longevity. Trends Cell Biol. 2012, 22:42-49.
    • (2012) Trends Cell Biol. , vol.22 , pp. 42-49
    • Han, S.1    Brunet, A.2
  • 113
    • 84869159983 scopus 로고    scopus 로고
    • Stress-associated H3K4 methylation accumulates during postnatal development and aging of rhesus macaque brain
    • Han Y., Han D., Yan Z., Boyd-Kirkup J.D., Green C.D., Khaitovich P., Han J.D. Stress-associated H3K4 methylation accumulates during postnatal development and aging of rhesus macaque brain. Aging Cell 2012, 11:1055-1064.
    • (2012) Aging Cell , vol.11 , pp. 1055-1064
    • Han, Y.1    Han, D.2    Yan, Z.3    Boyd-Kirkup, J.D.4    Green, C.D.5    Khaitovich, P.6    Han, J.D.7
  • 115
    • 21644490218 scopus 로고    scopus 로고
    • Age-dependent alterations in mitochondrial enzymes in cortex, striatum and hippocampus of rat brain - potential role of l-carnitine
    • Haripriya D., Devi M.A., Kokilavani V., Sangeetha P., Panneerselvam C. Age-dependent alterations in mitochondrial enzymes in cortex, striatum and hippocampus of rat brain - potential role of l-carnitine. Biogerontology 2004, 5:355-364.
    • (2004) Biogerontology , vol.5 , pp. 355-364
    • Haripriya, D.1    Devi, M.A.2    Kokilavani, V.3    Sangeetha, P.4    Panneerselvam, C.5
  • 116
    • 77049308856 scopus 로고
    • Aging: a theory based on free radical and radiation chemistry
    • Harman D. Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 1956, 11:298-300.
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 117
    • 51349147548 scopus 로고    scopus 로고
    • Biological effects of 2-oxoglutarate with particular emphasis on the regulation of protein, mineral and lipid absorption/metabolism, muscle performance, kidney function, bone formation and cancerogenesis, all viewed from a healthy ageing perspective state of the art - review article
    • Harrison A.P., Pierzynowski S.G. Biological effects of 2-oxoglutarate with particular emphasis on the regulation of protein, mineral and lipid absorption/metabolism, muscle performance, kidney function, bone formation and cancerogenesis, all viewed from a healthy ageing perspective state of the art - review article. J. Physiol. Pharmacol. 2008, 59(Suppl. 1):91-106.
    • (2008) J. Physiol. Pharmacol. , vol.59 , Issue.Suppl. 1 , pp. 91-106
    • Harrison, A.P.1    Pierzynowski, S.G.2
  • 118
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes
    • Hausinger R.P. Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. Biol. 2004, 39:21-68.
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 119
    • 0026507897 scopus 로고
    • Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2
    • Hautala T., Byers M.G., Eddy R.L., Shows T.B., Kivirikko K.I., Myllylä R. Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2. Genomics 1992, 13:62-69.
    • (1992) Genomics , vol.13 , pp. 62-69
    • Hautala, T.1    Byers, M.G.2    Eddy, R.L.3    Shows, T.B.4    Kivirikko, K.I.5    Myllylä, R.6
  • 120
    • 55549147132 scopus 로고    scopus 로고
    • The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b)
    • He J., Kallin E.M., Tsukada Y., Zhang Y. The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b). Nat. Struct. Mol. Biol. 2008, 15:1169-1175.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1169-1175
    • He, J.1    Kallin, E.M.2    Tsukada, Y.3    Zhang, Y.4
  • 121
    • 84865421953 scopus 로고    scopus 로고
    • Mitochondrial sirtuins: regulators of protein acylation and metabolism
    • He W., Newman J.C., Wang M.Z., Ho L., Verdin E. Mitochondrial sirtuins: regulators of protein acylation and metabolism. Trends Endocrinol. Metab. 2012, 23:467-476.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 467-476
    • He, W.1    Newman, J.C.2    Wang, M.Z.3    Ho, L.4    Verdin, E.5
  • 122
    • 80052805267 scopus 로고    scopus 로고
    • Histone modification: cause or cog?
    • Henikoff S., Shilatifard A. Histone modification: cause or cog?. Trends Genet. 2011, 27:389-396.
    • (2011) Trends Genet. , vol.27 , pp. 389-396
    • Henikoff, S.1    Shilatifard, A.2
  • 124
    • 34047255064 scopus 로고    scopus 로고
    • Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates
    • Hewitson K.S., Lienard B.M., McDonough M.A., Clifton I.J., Butler D., Soares A.S., Oldham N.J., McNeill L.A., Schofield C.J. Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates. J. Biol. Chem. 2007, 282:3293-3301.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3293-3301
    • Hewitson, K.S.1    Lienard, B.M.2    McDonough, M.A.3    Clifton, I.J.4    Butler, D.5    Soares, A.S.6    Oldham, N.J.7    McNeill, L.A.8    Schofield, C.J.9
  • 126
    • 84872007491 scopus 로고    scopus 로고
    • Aberrant DNA methylation profiles in the premature aging disorders Hutchinson-Gilford progeria and Werner syndrome
    • Heyn H., Moran S., Esteller M. Aberrant DNA methylation profiles in the premature aging disorders Hutchinson-Gilford progeria and Werner syndrome. Epigenetics 2013, 8:28-33.
    • (2013) Epigenetics , vol.8 , pp. 28-33
    • Heyn, H.1    Moran, S.2    Esteller, M.3
  • 130
    • 36749082438 scopus 로고    scopus 로고
    • Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases
    • Hong S., Cho Y.W., Yu L.R., Yu H., Veenstra T.D., Ge K. Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:18439-18444.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18439-18444
    • Hong, S.1    Cho, Y.W.2    Yu, L.R.3    Yu, H.4    Veenstra, T.D.5    Ge, K.6
  • 131
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X. Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat. Struct. Mol. Biol. 2010, 17:38-43.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 134
    • 0027333040 scopus 로고
    • L-Glutamate dehydrogenases: distribution, properties and mechanism
    • Hudson R.C., Daniel R.M. l-Glutamate dehydrogenases: distribution, properties and mechanism. Comp. Biochem. Physiol. B 1993, 106:767-792.
    • (1993) Comp. Biochem. Physiol. B , vol.106 , pp. 767-792
    • Hudson, R.C.1    Daniel, R.M.2
  • 135
    • 84884251973 scopus 로고    scopus 로고
    • Collagen prolyl 3-hydroxylation: a major role for a minor post-translational modification? Connect
    • Hudson D.M., Eyre D.R. Collagen prolyl 3-hydroxylation: a major role for a minor post-translational modification? Connect. Tissue Res. 2013, 54:245-251.
    • (2013) Tissue Res. , vol.54 , pp. 245-251
    • Hudson, D.M.1    Eyre, D.R.2
  • 137
    • 84876694930 scopus 로고    scopus 로고
    • The role of genetics in the establishment and maintenance of the epigenome
    • Huidobro C., Fernandez A.F., Fraga M.F. The role of genetics in the establishment and maintenance of the epigenome. Cell. Mol. Life Sci. 2013, 70:1543-1573.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 1543-1573
    • Huidobro, C.1    Fernandez, A.F.2    Fraga, M.F.3
  • 138
    • 34248541922 scopus 로고    scopus 로고
    • Life and death: metabolic rate, membrane composition, and life span of animals
    • Hulbert A.J., Pamplona R., Buffenstein R., Buttemer W.A. Life and death: metabolic rate, membrane composition, and life span of animals. Physiol. Rev. 2007, 87:1175-1213.
    • (2007) Physiol. Rev. , vol.87 , pp. 1175-1213
    • Hulbert, A.J.1    Pamplona, R.2    Buffenstein, R.3    Buttemer, W.A.4
  • 139
    • 0033168449 scopus 로고    scopus 로고
    • Variation and evolution of the citric-acid cycle: a genomic perspective
    • Huynen M.A., Dandekar T., Bork P. Variation and evolution of the citric-acid cycle: a genomic perspective. Trends Microbiol. 1999, 7:281-291.
    • (1999) Trends Microbiol. , vol.7 , pp. 281-291
    • Huynen, M.A.1    Dandekar, T.2    Bork, P.3
  • 140
    • 67650828068 scopus 로고    scopus 로고
    • A comparative analysis of the cell biology of senescence and aging
    • Hwang E.S., Yoon G., Kang H.T. A comparative analysis of the cell biology of senescence and aging. Cell. Mol. Life Sci. 2009, 66:2503-2524.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2503-2524
    • Hwang, E.S.1    Yoon, G.2    Kang, H.T.3
  • 141
    • 84877929908 scopus 로고    scopus 로고
    • Control of the epithelial stem cell epigenome: the shaping of epithelial stem cell identity
    • Iglesias-Bartolome R., Callejas-Valera J.L., Gutkind J.S. Control of the epithelial stem cell epigenome: the shaping of epithelial stem cell identity. Curr. Opin. Cell Biol. 2013, 25:162-169.
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 162-169
    • Iglesias-Bartolome, R.1    Callejas-Valera, J.L.2    Gutkind, J.S.3
  • 142
    • 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. Sci. 2010, 31:212-220.
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 212-220
    • Imai, S.1    Guarente, L.2
  • 144
    • 84878239632 scopus 로고    scopus 로고
    • Heat shock protein 90 (Hsp90) selectively regulates the stability of KDM4B/JMJD2B histone demethylase
    • Ipenberg I., Guttmann-Raviv N., Khoury H.P., Kupershmit I., Ayoub N. Heat shock protein 90 (Hsp90) selectively regulates the stability of KDM4B/JMJD2B histone demethylase. J. Biol. Chem. 2013, 288:14681-14687.
    • (2013) J. Biol. Chem. , vol.288 , pp. 14681-14687
    • Ipenberg, I.1    Guttmann-Raviv, N.2    Khoury, H.P.3    Kupershmit, I.4    Ayoub, N.5
  • 146
    • 84892909863 scopus 로고    scopus 로고
    • Aging and epigenetic drift: a vicious cycle
    • Issa J.P. Aging and epigenetic drift: a vicious cycle. J. Clin. Invest. 2014, 124:24-29.
    • (2014) J. Clin. Invest. , vol.124 , pp. 24-29
    • Issa, J.P.1
  • 149
    • 84882267740 scopus 로고    scopus 로고
    • The regulation, localization, and functions of oxygen-sensing prolyl hydroxylase PHD3
    • Jaakkola P.M., Rantanen K. The regulation, localization, and functions of oxygen-sensing prolyl hydroxylase PHD3. Biol. Chem. 2013, 394:449-457.
    • (2013) Biol. Chem. , vol.394 , pp. 449-457
    • Jaakkola, P.M.1    Rantanen, K.2
  • 150
    • 0042886929 scopus 로고    scopus 로고
    • The mitochondrial theory of aging: dead or alive?
    • Jacobs H.T. The mitochondrial theory of aging: dead or alive?. Aging Cell 2003, 2:11-17.
    • (2003) Aging Cell , vol.2 , pp. 11-17
    • Jacobs, H.T.1
  • 152
    • 84866442827 scopus 로고    scopus 로고
    • Review: a meta-analysis of GWAS and age-associated diseases
    • Jeck W.R., Siebold A.P., Sharpless N.E. Review: a meta-analysis of GWAS and age-associated diseases. Aging Cell 2012, 11:727-731.
    • (2012) Aging Cell , vol.11 , pp. 727-731
    • Jeck, W.R.1    Siebold, A.P.2    Sharpless, N.E.3
  • 153
    • 84884906522 scopus 로고    scopus 로고
    • Paternal aging and associated intraindividual alterations of global sperm 5-methylcytosine and 5-hydroxymethylcytosine levels
    • Jenkins T.G., Aston K.I., Cairns B.R., Carrell D.T. Paternal aging and associated intraindividual alterations of global sperm 5-methylcytosine and 5-hydroxymethylcytosine levels. Fertil. Steril. 2013, 100:945-951.
    • (2013) Fertil. Steril. , vol.100 , pp. 945-951
    • Jenkins, T.G.1    Aston, K.I.2    Cairns, B.R.3    Carrell, D.T.4
  • 155
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science 2001, 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 157
    • 84879537717 scopus 로고    scopus 로고
    • Continuous aging of the human DNA methylome throughout the human lifespan
    • Johansson A., Enroth S., Gyllensten U. Continuous aging of the human DNA methylome throughout the human lifespan. PLoS ONE 2013, 8:e67378.
    • (2013) PLoS ONE , vol.8
    • Johansson, A.1    Enroth, S.2    Gyllensten, U.3
  • 160
    • 79955511101 scopus 로고    scopus 로고
    • Emerging models and paradigms for stem cell ageing
    • Jones D.L., Rando T.A. Emerging models and paradigms for stem cell ageing. Nat. Cell Biol. 2011, 13:506-512.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 506-512
    • Jones, D.L.1    Rando, T.A.2
  • 161
    • 84875754667 scopus 로고    scopus 로고
    • Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity
    • Jorgensen S., Schotta G., Sorensen C.S. Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity. Nucleic Acids Res. 2013, 41:2797-2806.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 2797-2806
    • Jorgensen, S.1    Schotta, G.2    Sorensen, C.S.3
  • 162
    • 77950602854 scopus 로고    scopus 로고
    • Histone deacetylase controls adult stem cell aging by balancing the expression of polycomb genes and jumonji domain containing 3
    • Jung J.W., Lee S., Seo M.S., Park S.B., Kurtz A., Kang S.K., Kang K.S. Histone deacetylase controls adult stem cell aging by balancing the expression of polycomb genes and jumonji domain containing 3. Cell. Mol. Life Sci. 2010, 67:1165-1176.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1165-1176
    • Jung, J.W.1    Lee, S.2    Seo, M.S.3    Park, S.B.4    Kurtz, A.5    Kang, S.K.6    Kang, K.S.7
  • 163
    • 84884471932 scopus 로고    scopus 로고
    • TET1 controls CNS 5-methylcytosine hydroxylation, active DNA demethylation, gene transcription, and memory formation
    • Kaas G.A., Zhong C., Eason D.E., Ross D.L., Vachhani R.V., Ming G.L., King J.R., Song H., Sweatt J.D. TET1 controls CNS 5-methylcytosine hydroxylation, active DNA demethylation, gene transcription, and memory formation. Neuron 2013, 79:1086-1093.
    • (2013) Neuron , vol.79 , pp. 1086-1093
    • Kaas, G.A.1    Zhong, C.2    Eason, D.E.3    Ross, D.L.4    Vachhani, R.V.5    Ming, G.L.6    King, J.R.7    Song, H.8    Sweatt, J.D.9
  • 164
    • 84875755814 scopus 로고    scopus 로고
    • Influence of metabolism on epigenetics and disease
    • Kaelin W.G., McKnight S.L. Influence of metabolism on epigenetics and disease. Cell 2013, 153:56-69.
    • (2013) Cell , vol.153 , pp. 56-69
    • Kaelin, W.G.1    McKnight, S.L.2
  • 165
    • 33646764620 scopus 로고    scopus 로고
    • Is there a molecular connection between hypoxia and aging?
    • Katschinski D.M. Is there a molecular connection between hypoxia and aging?. Exp. Gerontol. 2006, 41:482-484.
    • (2006) Exp. Gerontol. , vol.41 , pp. 482-484
    • Katschinski, D.M.1
  • 167
    • 33750030758 scopus 로고    scopus 로고
    • The regulation of INK4/ARF in cancer and aging
    • Kim W.Y., Sharpless N.E. The regulation of INK4/ARF in cancer and aging. Cell 2006, 127:265-275.
    • (2006) Cell , vol.127 , pp. 265-275
    • Kim, W.Y.1    Sharpless, N.E.2
  • 168
    • 33746930794 scopus 로고    scopus 로고
    • Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer
    • King A., Selak M.A., Gottlieb E. Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer. Oncogene 2006, 25:4675-4682.
    • (2006) Oncogene , vol.25 , pp. 4675-4682
    • King, A.1    Selak, M.A.2    Gottlieb, E.3
  • 169
    • 0024639221 scopus 로고
    • Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit
    • Kivirikko K.I., Myllylä R., Pihlajaniemi T. Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit. FASEB J. 1989, 3:1609-1617.
    • (1989) FASEB J. , vol.3 , pp. 1609-1617
    • Kivirikko, K.I.1    Myllylä, R.2    Pihlajaniemi, T.3
  • 170
    • 0031893340 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases and their protein disulfide isomerase subunit
    • Kivirikko K.I., Myllyharju J. Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. Matrix Biol. 1998, 16:357-368.
    • (1998) Matrix Biol. , vol.16 , pp. 357-368
    • Kivirikko, K.I.1    Myllyharju, J.2
  • 171
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose R.J., Kallin E.M., Zhang Y. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 2006, 7:715-727.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 172
    • 40349106009 scopus 로고    scopus 로고
    • A new role of the rDNA and nucleolus in the nucleus - rDNA instability maintains genome integrity
    • Kobayashi T.A. A new role of the rDNA and nucleolus in the nucleus - rDNA instability maintains genome integrity. Bioessays 2008, 30:267-272.
    • (2008) Bioessays , vol.30 , pp. 267-272
    • Kobayashi, T.A.1
  • 173
    • 0031579441 scopus 로고    scopus 로고
    • Functional characterization of the 5'-flanking region of the gene encoding human 2-oxoglutarate dehydrogenase
    • Koike K., Matsuo S. Functional characterization of the 5'-flanking region of the gene encoding human 2-oxoglutarate dehydrogenase. Gene 1997, 186:45-53.
    • (1997) Gene , vol.186 , pp. 45-53
    • Koike, K.1    Matsuo, S.2
  • 174
    • 33947520506 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF
    • Koivunen P., Hirsilä M., Remes A.M., Hassinen I.E., Kivirikko K.I., Myllyharju J. Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF. J. Biol. Chem. 2007, 282:4524-4532.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4524-4532
    • Koivunen, P.1    Hirsilä, M.2    Remes, A.M.3    Hassinen, I.E.4    Kivirikko, K.I.5    Myllyharju, J.6
  • 175
    • 84862104334 scopus 로고    scopus 로고
    • Alterations in histone H4 lysine 20 methylation: implications for cancer detection and prevention
    • Koturbash I., Simpson N.E., Beland F.A., Pogribny I.P. Alterations in histone H4 lysine 20 methylation: implications for cancer detection and prevention. Antioxid. Redox Signal. 2012, 17:365-374.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 365-374
    • Koturbash, I.1    Simpson, N.E.2    Beland, F.A.3    Pogribny, I.P.4
  • 176
    • 66149123748 scopus 로고    scopus 로고
    • The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain
    • Kriaucionis S., Heintz N. The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain. Science 2009, 324:929-930.
    • (2009) Science , vol.324 , pp. 929-930
    • Kriaucionis, S.1    Heintz, N.2
  • 177
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1α enhances hypoxic gene expression and tumor growth
    • Krieg A.J., Rankin E.B., Chan D., Razorenova O., Fernandez S., Giaccia A.J. Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1α enhances hypoxic gene expression and tumor growth. Membr. Cell Biol. 2010, 30:344-353.
    • (2010) Membr. Cell Biol. , vol.30 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 180
    • 0023873596 scopus 로고
    • Quantitative succinate dehydrogenase histochemistry in the hippocampus of aged rats
    • Kugler P., Vogel S., Gehm M. Quantitative succinate dehydrogenase histochemistry in the hippocampus of aged rats. Histochemistry 1988, 88:299-307.
    • (1988) Histochemistry , vol.88 , pp. 299-307
    • Kugler, P.1    Vogel, S.2    Gehm, M.3
  • 182
    • 11244351578 scopus 로고    scopus 로고
    • Supplementation of l-carnitine improves mitochondrial enzymes in heart and skeletal muscle of aged rats
    • Kumaran S., Subathra M., Balu M., Panneerselvam C. Supplementation of l-carnitine improves mitochondrial enzymes in heart and skeletal muscle of aged rats. Exp. Aging Res. 2005, 31:55-67.
    • (2005) Exp. Aging Res. , vol.31 , pp. 55-67
    • Kumaran, S.1    Subathra, M.2    Balu, M.3    Panneerselvam, C.4
  • 184
    • 54449091329 scopus 로고    scopus 로고
    • Early mitochondrial dysfunction in long-lived Mclk1+/- mice
    • Lapointe J., Hekimi S. Early mitochondrial dysfunction in long-lived Mclk1+/- mice. J. Biol. Chem. 2008, 283:26217-26227.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26217-26227
    • Lapointe, J.1    Hekimi, S.2
  • 186
    • 0016249048 scopus 로고
    • Changes in histone methylase activity of rat brain and liver with ageing
    • Lee C.T., Duerre J.A. Changes in histone methylase activity of rat brain and liver with ageing. Nature 1974, 251:240-242.
    • (1974) Nature , vol.251 , pp. 240-242
    • Lee, C.T.1    Duerre, J.A.2
  • 188
    • 58249123443 scopus 로고    scopus 로고
    • Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells
    • Lee S.H., Kim J., Kim W.H., Lee Y.M. Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells. Oncogene 2009, 28:184-194.
    • (2009) Oncogene , vol.28 , pp. 184-194
    • Lee, S.H.1    Kim, J.2    Kim, W.H.3    Lee, Y.M.4
  • 189
    • 35448984675 scopus 로고    scopus 로고
    • Nitrogen regulation in bacteria and archaea
    • Leigh J.A., Dodsworth J.A. Nitrogen regulation in bacteria and archaea. Annu. Rev. Microbiol. 2007, 61:349-377.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 349-377
    • Leigh, J.A.1    Dodsworth, J.A.2
  • 191
    • 80052037691 scopus 로고    scopus 로고
    • Epigenetic regulation of caloric restriction in aging
    • Li Y., Daniel M., Tollefsbol T.O. Epigenetic regulation of caloric restriction in aging. BMC Med. 2011, 9:98.
    • (2011) BMC Med. , vol.9 , pp. 98
    • Li, Y.1    Daniel, M.2    Tollefsbol, T.O.3
  • 192
    • 84857804808 scopus 로고    scopus 로고
    • The structure and allosteric regulation of mammalian glutamate dehydrogenase
    • Li M., Li C., Allen A., Stanley C.A., Smith T.J. The structure and allosteric regulation of mammalian glutamate dehydrogenase. Arch. Biochem. Biophys. 2012, 519:69-80.
    • (2012) Arch. Biochem. Biophys. , vol.519 , pp. 69-80
    • Li, M.1    Li, C.2    Allen, A.3    Stanley, C.A.4    Smith, T.J.5
  • 193
    • 84887022165 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial protein quality control in aging
    • Lionaki E., Tavernarakis N. Oxidative stress and mitochondrial protein quality control in aging. J. Proteomics 2013, 92:181-194.
    • (2013) J. Proteomics , vol.92 , pp. 181-194
    • Lionaki, E.1    Tavernarakis, N.2
  • 194
    • 79955513612 scopus 로고    scopus 로고
    • Manifestations and mechanisms of stem cell aging
    • Liu L., Rando T.A. Manifestations and mechanisms of stem cell aging. J. Cell Biol. 2011, 193:257-266.
    • (2011) J. Cell Biol. , vol.193 , pp. 257-266
    • Liu, L.1    Rando, T.A.2
  • 197
    • 84878738557 scopus 로고    scopus 로고
    • Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model
    • Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z. Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model. Nat. Commun. 2013, 4:1868.
    • (2013) Nat. Commun. , vol.4 , pp. 1868
    • Liu, B.1    Wang, Z.2    Zhang, L.3    Ghosh, S.4    Zheng, H.5    Zhou, Z.6
  • 198
    • 78650864017 scopus 로고    scopus 로고
    • Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases
    • Loenarz C., Schofield C.J. Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases. Trends Biochem. Sci. 2011, 36:7-18.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 7-18
    • Loenarz, C.1    Schofield, C.J.2
  • 200
    • 84885848767 scopus 로고    scopus 로고
    • Tudor: a versatile family of histone methylation 'readers'
    • Lu R., Wang G.G. Tudor: a versatile family of histone methylation 'readers'. Trends Biochem. Sci. 2013, 10.1016/j.tibs.2013.08.002.
    • (2013) Trends Biochem. Sci.
    • Lu, R.1    Wang, G.G.2
  • 203
    • 84870463217 scopus 로고    scopus 로고
    • JMJD2A promotes cellular transformation by blocking cellular senescence through transcriptional repression of the tumor suppressor CHD5
    • Mallette F.A., Richard S. JMJD2A promotes cellular transformation by blocking cellular senescence through transcriptional repression of the tumor suppressor CHD5. Cell Rep. 2012, 2:1233-1243.
    • (2012) Cell Rep. , vol.2 , pp. 1233-1243
    • Mallette, F.A.1    Richard, S.2
  • 204
    • 84859895529 scopus 로고    scopus 로고
    • RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites
    • Mallette F.A., Mattiroli F., Cui G., Young L.C., Hendzel M.J., Mer G., Sixma T.K., Richard S. RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J. 2012, 31:1865-1878.
    • (2012) EMBO J. , vol.31 , pp. 1865-1878
    • Mallette, F.A.1    Mattiroli, F.2    Cui, G.3    Young, L.C.4    Hendzel, M.J.5    Mer, G.6    Sixma, T.K.7    Richard, S.8
  • 205
    • 84860758536 scopus 로고    scopus 로고
    • Stochastic modulations of the pace and patterns of ageing: impacts on quasi-stochastic distributions of multiple geriatric pathologies
    • Martin G.M. Stochastic modulations of the pace and patterns of ageing: impacts on quasi-stochastic distributions of multiple geriatric pathologies. Mech. Ageing Dev. 2012, 133:107-111.
    • (2012) Mech. Ageing Dev. , vol.133 , pp. 107-111
    • Martin, G.M.1
  • 206
    • 84887902069 scopus 로고    scopus 로고
    • Medicinal chemistry of the epigenetic diet and caloric restriction
    • Martin S.L., Hardy T.M., Tollefsbol T.O. Medicinal chemistry of the epigenetic diet and caloric restriction. Curr. Med. Chem. 2013, 20:4050-4059.
    • (2013) Curr. Med. Chem. , vol.20 , pp. 4050-4059
    • Martin, S.L.1    Hardy, T.M.2    Tollefsbol, T.O.3
  • 208
    • 81155139577 scopus 로고    scopus 로고
    • The H3K27 demethylase UTX-1 regulates C. elegans lifespan in a germline-independent, insulin-dependent manner
    • Maures T.J., Greer E.L., Hauswirth A.G., Brunet A. The H3K27 demethylase UTX-1 regulates C. elegans lifespan in a germline-independent, insulin-dependent manner. Aging Cell 2011, 10:980-990.
    • (2011) Aging Cell , vol.10 , pp. 980-990
    • Maures, T.J.1    Greer, E.L.2    Hauswirth, A.G.3    Brunet, A.4
  • 209
  • 211
    • 41649101975 scopus 로고    scopus 로고
    • The mutant form of lamin A that causes Hutchinson-Gilford progeria is a biomarker of cellular aging in human skin
    • McClintock D., Ratner D., Lokuge M., Owens D.M., Gordon L.B., Collins F.S., Djabali K. The mutant form of lamin A that causes Hutchinson-Gilford progeria is a biomarker of cellular aging in human skin. PLoS ONE 2007, 2:e1269.
    • (2007) PLoS ONE , vol.2
    • McClintock, D.1    Ratner, D.2    Lokuge, M.3    Owens, D.M.4    Gordon, L.B.5    Collins, F.S.6    Djabali, K.7
  • 212
    • 84873349707 scopus 로고    scopus 로고
    • Correlated alterations in genome organization, histone methylation, and DNA-lamin A/C interactions in Hutchinson-Gilford progeria syndrome
    • McCord R.P., Nazario-Toole A., Zhang H., Chines P.S., Zhan Y., Erdos M.R., Collins F.S., Dekker J., Cao K. Correlated alterations in genome organization, histone methylation, and DNA-lamin A/C interactions in Hutchinson-Gilford progeria syndrome. Genome Res. 2013, 23:260-269.
    • (2013) Genome Res. , vol.23 , pp. 260-269
    • McCord, R.P.1    Nazario-Toole, A.2    Zhang, H.3    Chines, P.S.4    Zhan, Y.5    Erdos, M.R.6    Collins, F.S.7    Dekker, J.8    Cao, K.9
  • 214
    • 0026396728 scopus 로고
    • Age changes in chromatin: accumulative or programmed?
    • Medvedev Z.A., Medvedeva M.N. Age changes in chromatin: accumulative or programmed?. Ann. N. Y. Acad. Sci. 1991, 621:40-52.
    • (1991) Ann. N. Y. Acad. Sci. , vol.621 , pp. 40-52
    • Medvedev, Z.A.1    Medvedeva, M.N.2
  • 216
    • 84860586157 scopus 로고    scopus 로고
    • Mitochondrial regulation of epigenetics and its role in human diseases
    • Minocherhomji S., Tollefsbol T.O., Singh K.K. Mitochondrial regulation of epigenetics and its role in human diseases. Epigenetics 2012, 7:326-334.
    • (2012) Epigenetics , vol.7 , pp. 326-334
    • Minocherhomji, S.1    Tollefsbol, T.O.2    Singh, K.K.3
  • 218
    • 84876463939 scopus 로고    scopus 로고
    • Breathing-in epigenetic change with vitamin C
    • Monfort A., Wutz A. Breathing-in epigenetic change with vitamin C. EMBO Rep. 2013, 14:337-346.
    • (2013) EMBO Rep. , vol.14 , pp. 337-346
    • Monfort, A.1    Wutz, A.2
  • 220
    • 0142213541 scopus 로고    scopus 로고
    • Age-related increase in 4-hydroxynonenal adduction to rat heart α-ketoglutarate dehydrogenase does not cause loss of its catalytic activity
    • Moreau R., Heath S.H., Doneanu C.E., Lindsay J.G., Hagen T.M. Age-related increase in 4-hydroxynonenal adduction to rat heart α-ketoglutarate dehydrogenase does not cause loss of its catalytic activity. Antioxid. Redox Signal. 2003, 5:517-527.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 517-527
    • Moreau, R.1    Heath, S.H.2    Doneanu, C.E.3    Lindsay, J.G.4    Hagen, T.M.5
  • 221
    • 70349322563 scopus 로고    scopus 로고
    • Mammalian hibernation: differential gene expression and novel application of epigenetic controls
    • Morin P., Storey K.B. Mammalian hibernation: differential gene expression and novel application of epigenetic controls. Int. J. Dev. Biol. 2009, 53:433-442.
    • (2009) Int. J. Dev. Biol. , vol.53 , pp. 433-442
    • Morin, P.1    Storey, K.B.2
  • 222
    • 67651121563 scopus 로고    scopus 로고
    • Inhibition of succinate-linked respiration and complex II activity by hydrogen peroxide
    • Moser M.D., Matsuzaki S., Humphries K.M. Inhibition of succinate-linked respiration and complex II activity by hydrogen peroxide. Arch. Biochem. Biophys. 2009, 488:69-75.
    • (2009) Arch. Biochem. Biophys. , vol.488 , pp. 69-75
    • Moser, M.D.1    Matsuzaki, S.2    Humphries, K.M.3
  • 225
    • 84877704490 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, master regulators of the hypoxia response
    • Myllyharju J. Prolyl 4-hydroxylases, master regulators of the hypoxia response. Acta Physiol. (Oxf.) 2013, 208:148-165.
    • (2013) Acta Physiol. (Oxf.) , vol.208 , pp. 148-165
    • Myllyharju, J.1
  • 227
    • 67650065272 scopus 로고    scopus 로고
    • Increased prolyl 4-hydroxylase expression and differential regulation of hypoxia-inducible factors in the aged rat brain
    • Ndubuizu O.I., Chavez J.C., LaManna J.C. Increased prolyl 4-hydroxylase expression and differential regulation of hypoxia-inducible factors in the aged rat brain. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2009, 297:R158-R165.
    • (2009) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.297
    • Ndubuizu, O.I.1    Chavez, J.C.2    LaManna, J.C.3
  • 228
    • 34250643467 scopus 로고    scopus 로고
    • Ablation of de novo DNA methyltransferase Dnmt3a in the nervous system leads to neuromuscular defects and shortened lifespan
    • Nguyen S., Meletis K., Fu D., Jhaveri S., Jaenisch R. Ablation of de novo DNA methyltransferase Dnmt3a in the nervous system leads to neuromuscular defects and shortened lifespan. Dev. Dyn. 2007, 236:1663-1676.
    • (2007) Dev. Dyn. , vol.236 , pp. 1663-1676
    • Nguyen, S.1    Meletis, K.2    Fu, D.3    Jhaveri, S.4    Jaenisch, R.5
  • 229
    • 84860389035 scopus 로고    scopus 로고
    • 53BP1-mediated DNA double strand break repair: insert bad pun here
    • Noon A.T., Goodarzi A.A. 53BP1-mediated DNA double strand break repair: insert bad pun here. DNA Repair (Amst.) 2011, 10:1071-1076.
    • (2011) DNA Repair (Amst.) , vol.10 , pp. 1071-1076
    • Noon, A.T.1    Goodarzi, A.A.2
  • 231
    • 70449519969 scopus 로고    scopus 로고
    • Contribution of hypoxia to Alzheimer's disease: is HIF-1α a mediator of neurodegeneration?
    • Ogunshola O.O., Antoniou X. Contribution of hypoxia to Alzheimer's disease: is HIF-1α a mediator of neurodegeneration?. Cell. Mol. Life Sci. 2009, 66:3555-3563.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3555-3563
    • Ogunshola, O.O.1    Antoniou, X.2
  • 233
    • 84864461542 scopus 로고    scopus 로고
    • Rescue of aging-associated decline in Dnmt3a2 expression restores cognitive abilities
    • Oliveira A.M., Hemstedt T.J., Bading H. Rescue of aging-associated decline in Dnmt3a2 expression restores cognitive abilities. Nat. Neurosci. 2012, 15:1111-1113.
    • (2012) Nat. Neurosci. , vol.15 , pp. 1111-1113
    • Oliveira, A.M.1    Hemstedt, T.J.2    Bading, H.3
  • 234
    • 84867907645 scopus 로고    scopus 로고
    • The great unravelling: chromatin as a modulator of the aging process
    • O'Sullivan R.J., Karlseder J. The great unravelling: chromatin as a modulator of the aging process. Trends Biochem. Sci. 2012, 37:466-476.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 466-476
    • O'Sullivan, R.J.1    Karlseder, J.2
  • 235
    • 82355191783 scopus 로고    scopus 로고
    • Overproduction and secretion of α-ketoglutaric acid by microorganisms
    • Otto C., Yovkova V., Barth G. Overproduction and secretion of α-ketoglutaric acid by microorganisms. Appl. Microbiol. Biotechnol. 2011, 92:689-695.
    • (2011) Appl. Microbiol. Biotechnol. , vol.92 , pp. 689-695
    • Otto, C.1    Yovkova, V.2    Barth, G.3
  • 237
    • 79551623370 scopus 로고    scopus 로고
    • ANRIL, a long, noncoding RNA, is an unexpected major hotspot in GWAS
    • Pasmant E., Sabbagh A., Vidaud M., Bieche I. ANRIL, a long, noncoding RNA, is an unexpected major hotspot in GWAS. FASEB J. 2011, 25:444-448.
    • (2011) FASEB J. , vol.25 , pp. 444-448
    • Pasmant, E.1    Sabbagh, A.2    Vidaud, M.3    Bieche, I.4
  • 238
    • 84878260646 scopus 로고    scopus 로고
    • TETonic shift: biological roles of TET proteins in DNA demethylation and transcription
    • Pastor W.A., Aravind L., Rao A. TETonic shift: biological roles of TET proteins in DNA demethylation and transcription. Nat. Rev. Mol. Cell Biol. 2013, 14:341-356.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 341-356
    • Pastor, W.A.1    Aravind, L.2    Rao, A.3
  • 240
    • 84858059041 scopus 로고    scopus 로고
    • A meta-analysis of caloric restriction gene expression profiles to infer common signatures and regulatory mechanisms
    • Plank M., Wuttke D., van Dam S., Clarke S.A., de Magalhaes J.P. A meta-analysis of caloric restriction gene expression profiles to infer common signatures and regulatory mechanisms. Mol. Biosyst. 2012, 8:1339-1349.
    • (2012) Mol. Biosyst. , vol.8 , pp. 1339-1349
    • Plank, M.1    Wuttke, D.2    van Dam, S.3    Clarke, S.A.4    de Magalhaes, J.P.5
  • 242
    • 78449243068 scopus 로고    scopus 로고
    • Epigenetic regulation of the INK4b-ARF-INK4a locus: in sickness and in health
    • Popov N., Gil J. Epigenetic regulation of the INK4b-ARF-INK4a locus: in sickness and in health. Epigenetics 2010, 5:685-690.
    • (2010) Epigenetics , vol.5 , pp. 685-690
    • Popov, N.1    Gil, J.2
  • 243
    • 77955280094 scopus 로고    scopus 로고
    • The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation
    • Qiu J., Shi G., Jia Y., Li J., Wu M., Li J., Dong S., Wong J. The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation. Cell Res. 2010, 20:908-918.
    • (2010) Cell Res. , vol.20 , pp. 908-918
    • Qiu, J.1    Shi, G.2    Jia, Y.3    Li, J.4    Wu, M.5    Li, J.6    Dong, S.7    Wong, J.8
  • 244
    • 80052404569 scopus 로고    scopus 로고
    • Impaired hypoxic response in senescent mouse brain
    • Rabie T., Kunze R., Marti H.H. Impaired hypoxic response in senescent mouse brain. Int. J. Dev. Neurosci. 2011, 29:655-661.
    • (2011) Int. J. Dev. Neurosci. , vol.29 , pp. 655-661
    • Rabie, T.1    Kunze, R.2    Marti, H.H.3
  • 245
    • 80054959409 scopus 로고    scopus 로고
    • Revisiting the TCA cycle: signaling to tumor formation
    • Raimundo N., Baysal B.E., Shadel G.S. Revisiting the TCA cycle: signaling to tumor formation. Trends Mol. Med. 2011, 17:641-649.
    • (2011) Trends Mol. Med. , vol.17 , pp. 641-649
    • Raimundo, N.1    Baysal, B.E.2    Shadel, G.S.3
  • 247
    • 33745614062 scopus 로고    scopus 로고
    • Stem cells, ageing and the quest for immortality
    • Rando T.A. Stem cells, ageing and the quest for immortality. Nature 2006, 441:1080-1086.
    • (2006) Nature , vol.441 , pp. 1080-1086
    • Rando, T.A.1
  • 248
    • 84856090875 scopus 로고    scopus 로고
    • Aging, rejuvenation, and epigenetic reprogramming: resetting the aging clock
    • Rando T.A., Chang H.Y. Aging, rejuvenation, and epigenetic reprogramming: resetting the aging clock. Cell 2012, 148:46-57.
    • (2012) Cell , vol.148 , pp. 46-57
    • Rando, T.A.1    Chang, H.Y.2
  • 249
    • 81355146839 scopus 로고    scopus 로고
    • Lamin A farnesylation and aging
    • Reddy S., Comai L. Lamin A farnesylation and aging. Exp. Cell Res. 2012, 318:1-7.
    • (2012) Exp. Cell Res. , vol.318 , pp. 1-7
    • Reddy, S.1    Comai, L.2
  • 250
    • 0344321897 scopus 로고    scopus 로고
    • Impact of aging on DNA methylation
    • Richardson B. Impact of aging on DNA methylation. Ageing Res. Rev. 2003, 2:245-261.
    • (2003) Ageing Res. Rev. , vol.2 , pp. 245-261
    • Richardson, B.1
  • 251
    • 0034703017 scopus 로고    scopus 로고
    • Age-dependent defect in vascular endothelial growth factor expression is associated with reduced hypoxia-inducible factor 1 activity
    • Rivard A., Berthou-Soulie L., Principe N., Kearney M., Curry C., Branellec D., Semenza G.L., Isner J.M. Age-dependent defect in vascular endothelial growth factor expression is associated with reduced hypoxia-inducible factor 1 activity. J. Biol. Chem. 2000, 275:29643-29647.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29643-29647
    • Rivard, A.1    Berthou-Soulie, L.2    Principe, N.3    Kearney, M.4    Curry, C.5    Branellec, D.6    Semenza, G.L.7    Isner, J.M.8
  • 252
    • 84865562868 scopus 로고    scopus 로고
    • Hypoxia-induced DNA hypermethylation in human pulmonary fibroblasts is associated with Thy-1 promoter methylation and the development of a pro-fibrotic phenotype
    • Robinson C.M., Neary R., Levendale A., Watson C.J., Baugh J.A. Hypoxia-induced DNA hypermethylation in human pulmonary fibroblasts is associated with Thy-1 promoter methylation and the development of a pro-fibrotic phenotype. Respir. Res. 2012, 13:74.
    • (2012) Respir. Res. , vol.13 , pp. 74
    • Robinson, C.M.1    Neary, R.2    Levendale, A.3    Watson, C.J.4    Baugh, J.A.5
  • 254
    • 23644461909 scopus 로고    scopus 로고
    • Age-dependent increase of prolyl-4-hydroxylase domain (PHD) 3 expression in human and mouse heart
    • Rohrbach S., Simm A., Pregla R., Franke C., Katschinski D.M. Age-dependent increase of prolyl-4-hydroxylase domain (PHD) 3 expression in human and mouse heart. Biogerontology 2005, 6:165-171.
    • (2005) Biogerontology , vol.6 , pp. 165-171
    • Rohrbach, S.1    Simm, A.2    Pregla, R.3    Franke, C.4    Katschinski, D.M.5
  • 255
    • 43249114609 scopus 로고    scopus 로고
    • Caloric restriction counteracts age-dependent changes in prolyl-4-hydroxylase domain (PHD) 3 expression
    • Rohrbach S., Teichert S., Niemann B., Franke C., Katschinski D.M. Caloric restriction counteracts age-dependent changes in prolyl-4-hydroxylase domain (PHD) 3 expression. Biogerontology 2008, 9:169-176.
    • (2008) Biogerontology , vol.9 , pp. 169-176
    • Rohrbach, S.1    Teichert, S.2    Niemann, B.3    Franke, C.4    Katschinski, D.M.5
  • 257
    • 77952885778 scopus 로고    scopus 로고
    • Succinate dehydrogenase - assembly, regulation and role in human disease
    • Rutter J., Winge D.R., Schiffman J.D. Succinate dehydrogenase - assembly, regulation and role in human disease. Mitochondrion 2010, 10:393-401.
    • (2010) Mitochondrion , vol.10 , pp. 393-401
    • Rutter, J.1    Winge, D.R.2    Schiffman, J.D.3
  • 259
    • 84861461464 scopus 로고    scopus 로고
    • Axis of ageing: telomeres, p53 and mitochondria
    • Sahin E., DePinho R.A. Axis of ageing: telomeres, p53 and mitochondria. Nat. Rev. Mol. Cell Biol. 2012, 13:397-404.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 397-404
    • Sahin, E.1    DePinho, R.A.2
  • 260
    • 56949101056 scopus 로고    scopus 로고
    • SIRT1 regulates the ribosomal DNA locus: epigenetic candles twinkle longevity in the Christmas tree
    • Salminen A., Kaarniranta K. SIRT1 regulates the ribosomal DNA locus: epigenetic candles twinkle longevity in the Christmas tree. Biochem. Biophys. Res. Commun. 2009, 378:6-9.
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 6-9
    • Salminen, A.1    Kaarniranta, K.2
  • 261
    • 74449090245 scopus 로고    scopus 로고
    • Insulin/IGF-1 paradox of aging: regulation via AKT/IKK/NF-κB signaling
    • Salminen A., Kaarniranta K. Insulin/IGF-1 paradox of aging: regulation via AKT/IKK/NF-κB signaling. Cell. Signal. 2010, 22:573-577.
    • (2010) Cell. Signal. , vol.22 , pp. 573-577
    • Salminen, A.1    Kaarniranta, K.2
  • 262
    • 40949123149 scopus 로고    scopus 로고
    • Activation of innate immunity system during aging: NF-κB signaling is the molecular culprit of inflamm-aging
    • Salminen A., Huuskonen J., Ojala J., Kauppinen A., Kaarniranta K., Suuronen T. Activation of innate immunity system during aging: NF-κB signaling is the molecular culprit of inflamm-aging. Ageing Res. Rev. 2008, 7:83-105.
    • (2008) Ageing Res. Rev. , vol.7 , pp. 83-105
    • Salminen, A.1    Huuskonen, J.2    Ojala, J.3    Kauppinen, A.4    Kaarniranta, K.5    Suuronen, T.6
  • 263
    • 84856209016 scopus 로고    scopus 로고
    • Emerging role of NF-κB signaling in the induction of senescence-associated secretory phenotype (SASP)
    • Salminen A., Kauppinen A., Kaarniranta K. Emerging role of NF-κB signaling in the induction of senescence-associated secretory phenotype (SASP). Cell. Signal. 2012, 24:835-845.
    • (2012) Cell. Signal. , vol.24 , pp. 835-845
    • Salminen, A.1    Kauppinen, A.2    Kaarniranta, K.3
  • 264
    • 1342286842 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle and activation of glyoxylate cycle in the course of chronological aging of Saccharomyces cerevisiae. Compensatory role of succinate oxidation
    • Samokhvalov V., Ignatov V., Kondrashova M. Inhibition of Krebs cycle and activation of glyoxylate cycle in the course of chronological aging of Saccharomyces cerevisiae. Compensatory role of succinate oxidation. Biochimie 2004, 86:39-46.
    • (2004) Biochimie , vol.86 , pp. 39-46
    • Samokhvalov, V.1    Ignatov, V.2    Kondrashova, M.3
  • 265
    • 0037131426 scopus 로고    scopus 로고
    • Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging
    • Sarg B., Koutzamani E., Helliger W., Rundquist I., Lindner H.H. Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging. J. Biol. Chem. 2002, 277:39195-39201.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39195-39201
    • Sarg, B.1    Koutzamani, E.2    Helliger, W.3    Rundquist, I.4    Lindner, H.H.5
  • 266
  • 268
    • 26044471868 scopus 로고    scopus 로고
    • Efficacy of levo carnitine and alpha lipoic acid in ameliorating the decline in mitochondrial enzymes during aging
    • Savitha S., Sivarajan K., Haripriya D., Kokilavani V., Panneerselvam C. Efficacy of levo carnitine and alpha lipoic acid in ameliorating the decline in mitochondrial enzymes during aging. Clin. Nutr. 2005, 24:794-800.
    • (2005) Clin. Nutr. , vol.24 , pp. 794-800
    • Savitha, S.1    Sivarajan, K.2    Haripriya, D.3    Kokilavani, V.4    Panneerselvam, C.5
  • 269
    • 33646745137 scopus 로고    scopus 로고
    • Lamin A-dependent nuclear defects in human aging
    • Scaffidi P., Misteli T. Lamin A-dependent nuclear defects in human aging. Science 2006, 312:1059-1063.
    • (2006) Science , vol.312 , pp. 1059-1063
    • Scaffidi, P.1    Misteli, T.2
  • 270
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • Schofield C.J., Zhang Z. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 1999, 9:722-731.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 271
    • 0742305875 scopus 로고    scopus 로고
    • Repairing DNA-methylation damage
    • Sedgwick B. Repairing DNA-methylation damage. Nat. Rev. Mol. Cell Biol. 2004, 5:148-157.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 148-157
    • Sedgwick, B.1
  • 272
    • 77956092375 scopus 로고    scopus 로고
    • 2-Oxoglutarate oxygenases are inhibited by a range of transition metals
    • Sekirnik R., Rose N.R., Mecinovic J., Schofield C.J. 2-Oxoglutarate oxygenases are inhibited by a range of transition metals. Metallomics 2010, 2:397-399.
    • (2010) Metallomics , vol.2 , pp. 397-399
    • Sekirnik, R.1    Rose, N.R.2    Mecinovic, J.3    Schofield, C.J.4
  • 274
    • 77955351652 scopus 로고    scopus 로고
    • New insights into the role of mitochondria in aging: mitochondrial dynamics and more
    • Seo A.Y., Joseph A.M., Dutta D., Hwang J.C., Aris J.P., Leeuwenburgh C. New insights into the role of mitochondria in aging: mitochondrial dynamics and more. J. Cell Sci. 2010, 123:2533-2542.
    • (2010) J. Cell Sci. , vol.123 , pp. 2533-2542
    • Seo, A.Y.1    Joseph, A.M.2    Dutta, D.3    Hwang, J.C.4    Aris, J.P.5    Leeuwenburgh, C.6
  • 276
    • 3042829493 scopus 로고    scopus 로고
    • Hypoxic stress tolerance of the blind subterranean mole rat: expression of erythropoietin and hypoxia-inducible factor 1α
    • Shams I., Avivi A., Nevo E. Hypoxic stress tolerance of the blind subterranean mole rat: expression of erythropoietin and hypoxia-inducible factor 1α. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:9698-9703.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9698-9703
    • Shams, I.1    Avivi, A.2    Nevo, E.3
  • 277
    • 84855614902 scopus 로고    scopus 로고
    • Macrophages, meta-inflammation, and immuno-metabolism
    • Shapiro H., Lutaty A., Ariel A. Macrophages, meta-inflammation, and immuno-metabolism. ScientificWorldJournal 2011, 11:2509-2529.
    • (2011) ScientificWorldJournal , vol.11 , pp. 2509-2529
    • Shapiro, H.1    Lutaty, A.2    Ariel, A.3
  • 278
  • 279
    • 84879235514 scopus 로고    scopus 로고
    • 5-Hydroxymethylcytosine: generation, fate, and genomic distribution
    • Shen L., Zhang Y. 5-Hydroxymethylcytosine: generation, fate, and genomic distribution. Curr. Opin. Cell Biol. 2013, 25:289-296.
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 289-296
    • Shen, L.1    Zhang, Y.2
  • 280
    • 0033387202 scopus 로고    scopus 로고
    • The α-ketoglutarate dehydrogenase complex
    • Sheu K.F., Blass J.P. The α-ketoglutarate dehydrogenase complex. Ann. N. Y. Acad. Sci. 1999, 893:61-78.
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 61-78
    • Sheu, K.F.1    Blass, J.P.2
  • 281
    • 84880530231 scopus 로고    scopus 로고
    • Ten-eleven translocation 1 (Tet1) is regulated by O-linked N-acetylglucosamine transferase (Ogt) for target gene repression in mouse embryonic stem cells
    • Shi F.T., Kim H., Lu W., He Q., Liu D., Goodell M.A., Wan M., Songyang Z. Ten-eleven translocation 1 (Tet1) is regulated by O-linked N-acetylglucosamine transferase (Ogt) for target gene repression in mouse embryonic stem cells. J. Biol. Chem. 2013, 288:20776-20784.
    • (2013) J. Biol. Chem. , vol.288 , pp. 20776-20784
    • Shi, F.T.1    Kim, H.2    Lu, W.3    He, Q.4    Liu, D.5    Goodell, M.A.6    Wan, M.7    Songyang, Z.8
  • 282
    • 84861870951 scopus 로고    scopus 로고
    • The COMPASS family of histone H3K4 methylases: mechanisms of regulation in development and disease pathogenesis
    • Shilatifard A. The COMPASS family of histone H3K4 methylases: mechanisms of regulation in development and disease pathogenesis. Annu. Rev. Biochem 2012, 81:65-95.
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 65-95
    • Shilatifard, A.1
  • 284
    • 84873608154 scopus 로고    scopus 로고
    • Mechanisms that regulate stem cell aging and life span
    • Signer R.A., Morrison S.J. Mechanisms that regulate stem cell aging and life span. Cell Stem Cell 2013, 12:152-165.
    • (2013) Cell Stem Cell , vol.12 , pp. 152-165
    • Signer, R.A.1    Morrison, S.J.2
  • 285
    • 84876871047 scopus 로고    scopus 로고
    • Occupying chromatin: polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put
    • Simon J.A., Kingston R.E. Occupying chromatin: polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put. Mol. Cell 2013, 49:808-824.
    • (2013) Mol. Cell , vol.49 , pp. 808-824
    • Simon, J.A.1    Kingston, R.E.2
  • 286
    • 84874194072 scopus 로고    scopus 로고
    • DNA methylation: roles in mammalian development
    • Smith Z.D., Meissner A. DNA methylation: roles in mammalian development. Nat. Rev. Genet. 2013, 14:204-220.
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 204-220
    • Smith, Z.D.1    Meissner, A.2
  • 287
    • 79955921676 scopus 로고    scopus 로고
    • DNA methyltransferase controls stem cell aging by regulating BMI1 and EZH2 through microRNAs
    • So A.Y., Jung J.W., Lee S., Kim H.S., Kang K.S. DNA methyltransferase controls stem cell aging by regulating BMI1 and EZH2 through microRNAs. PLoS ONE 2011, 6:e19503.
    • (2011) PLoS ONE , vol.6
    • So, A.Y.1    Jung, J.W.2    Lee, S.3    Kim, H.S.4    Kang, K.S.5
  • 288
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • Sohal R.S., Weindruch R. Oxidative stress, caloric restriction, and aging. Science 1996, 273:59-63.
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 289
    • 36248971737 scopus 로고    scopus 로고
    • Control of key metabolic intersections in Bacillus subtilis
    • Sonenshein A.L. Control of key metabolic intersections in Bacillus subtilis. Nat. Rev. Microbiol. 2007, 5:917-927.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 917-927
    • Sonenshein, A.L.1
  • 290
    • 84884590688 scopus 로고    scopus 로고
    • Potential functional roles of DNA demethylation intermediates
    • Song C.X., He C. Potential functional roles of DNA demethylation intermediates. Trends Biochem. Sci. 2013, 10.1016/j.tibs.2013.07.003.
    • (2013) Trends Biochem. Sci.
    • Song, C.X.1    He, C.2
  • 291
    • 49349102919 scopus 로고    scopus 로고
    • Mitochondrial metabolism in hibernation and daily torpor: a review
    • Staples J.F., Brown J.C. Mitochondrial metabolism in hibernation and daily torpor: a review. J. Comp. Physiol. B 2008, 178:811-827.
    • (2008) J. Comp. Physiol. B , vol.178 , pp. 811-827
    • Staples, J.F.1    Brown, J.C.2
  • 293
    • 73149086166 scopus 로고    scopus 로고
    • Genes and gene expression modules associated with caloric restriction and aging in the laboratory mouse
    • Swindell W.R. Genes and gene expression modules associated with caloric restriction and aging in the laboratory mouse. BMC Genomics 2009, 10:585.
    • (2009) BMC Genomics , vol.10 , pp. 585
    • Swindell, W.R.1
  • 296
    • 64749111074 scopus 로고    scopus 로고
    • Role of Jhdm2a in regulating metabolic gene expression and obesity resistance
    • Tateishi K., Okada Y., Kallin E.M., Zhang Y. Role of Jhdm2a in regulating metabolic gene expression and obesity resistance. Nature 2009, 458:757-761.
    • (2009) Nature , vol.458 , pp. 757-761
    • Tateishi, K.1    Okada, Y.2    Kallin, E.M.3    Zhang, Y.4
  • 297
    • 78651086487 scopus 로고    scopus 로고
    • Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity
    • Tausendschön M., Dehne N., Brune B. Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity. Cytokine 2011, 53:256-262.
    • (2011) Cytokine , vol.53 , pp. 256-262
    • Tausendschön, M.1    Dehne, N.2    Brune, B.3
  • 298
    • 75349112375 scopus 로고    scopus 로고
    • Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging
    • Terman A., Kurz T., Navratil M., Arriaga E.A., Brunk U.T. Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging. Antioxid. Redox Signal. 2010, 12:503-535.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 503-535
    • Terman, A.1    Kurz, T.2    Navratil, M.3    Arriaga, E.A.4    Brunk, U.T.5
  • 300
    • 84884784742 scopus 로고    scopus 로고
    • Age-associated epigenetic drift: implications, and a case of epigenetic thrift?
    • Teschendorff A.E., West J., Beck S. Age-associated epigenetic drift: implications, and a case of epigenetic thrift?. Hum. Mol. Genet. 2013, 22:R7-R15.
    • (2013) Hum. Mol. Genet. , vol.22
    • Teschendorff, A.E.1    West, J.2    Beck, S.3
  • 301
    • 0021719299 scopus 로고
    • Age-related changes in the structure and function of chromatin: a review
    • Thakur M.K. Age-related changes in the structure and function of chromatin: a review. Mech. Ageing Dev. 1984, 27:263-286.
    • (1984) Mech. Ageing Dev. , vol.27 , pp. 263-286
    • Thakur, M.K.1
  • 303
    • 84861605111 scopus 로고    scopus 로고
    • Prenatal famine and genetic variation are independently and additively associated with DNA methylation at regulatory loci within IGF2/H19
    • Tobi E.W., Slagboom P.E., van Dongen J., Kremer D., Stein A.D., Putter H., Heijmans B.T., Lumey L.H. Prenatal famine and genetic variation are independently and additively associated with DNA methylation at regulatory loci within IGF2/H19. PLoS ONE 2012, 7:e37933.
    • (2012) PLoS ONE , vol.7
    • Tobi, E.W.1    Slagboom, P.E.2    van Dongen, J.3    Kremer, D.4    Stein, A.D.5    Putter, H.6    Heijmans, B.T.7    Lumey, L.H.8
  • 305
    • 33745252231 scopus 로고    scopus 로고
    • Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress
    • Tretter L., Adam-Vizi V. Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 2005, 360:2335-2345.
    • (2005) Philos. Trans. R. Soc. Lond. B: Biol. Sci. , vol.360 , pp. 2335-2345
    • Tretter, L.1    Adam-Vizi, V.2
  • 306
    • 38349108752 scopus 로고    scopus 로고
    • Mitochondrial dysfunction as a cause of ageing
    • Trifunovic A., Larsson N.G. Mitochondrial dysfunction as a cause of ageing. J. Intern. Med. 2008, 263:167-178.
    • (2008) J. Intern. Med. , vol.263 , pp. 167-178
    • Trifunovic, A.1    Larsson, N.G.2
  • 307
    • 84871268346 scopus 로고    scopus 로고
    • Consequences of the α-ketoglutarate dehydrogenase inhibition for neuronal metabolism and survival: implications for neurodegenerative diseases
    • Trofimova L.K., Araujo W.L., Strokina A.A., Fernie A.R., Bettendorff L., Bunik V.I. Consequences of the α-ketoglutarate dehydrogenase inhibition for neuronal metabolism and survival: implications for neurodegenerative diseases. Curr. Med. Chem. 2012, 19:5895-5906.
    • (2012) Curr. Med. Chem. , vol.19 , pp. 5895-5906
    • Trofimova, L.K.1    Araujo, W.L.2    Strokina, A.A.3    Fernie, A.R.4    Bettendorff, L.5    Bunik, V.I.6
  • 309
    • 77649152293 scopus 로고    scopus 로고
    • KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development
    • Tsukada Y., Ishitani T., Nakayama K.I. KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development. Genes Dev. 2010, 24:432-437.
    • (2010) Genes Dev. , vol.24 , pp. 432-437
    • Tsukada, Y.1    Ishitani, T.2    Nakayama, K.I.3
  • 310
    • 84863806968 scopus 로고    scopus 로고
    • Global heterochromatin loss: a unifying theory of aging?
    • Tsurumi A., Li W.X. Global heterochromatin loss: a unifying theory of aging?. Epigenetics 2012, 7:680-688.
    • (2012) Epigenetics , vol.7 , pp. 680-688
    • Tsurumi, A.1    Li, W.X.2
  • 311
    • 62449276460 scopus 로고    scopus 로고
    • Ndy1/KDM2B immortalizes mouse embryonic fibroblasts by repressing the Ink4a/Arf locus
    • Tzatsos A., Pfau R., Kampranis S.C., Tsichlis P.N. Ndy1/KDM2B immortalizes mouse embryonic fibroblasts by repressing the Ink4a/Arf locus. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:2641-2646.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2641-2646
    • Tzatsos, A.1    Pfau, R.2    Kampranis, S.C.3    Tsichlis, P.N.4
  • 312
    • 80053018047 scopus 로고    scopus 로고
    • Lysine-specific demethylase 2B (KDM2B)-let-7-enhancer of zester homolog 2 (EZH2) pathway regulates cell cycle progression and senescence in primary cells
    • Tzatsos A., Paskaleva P., Lymperi S., Contino G., Stoykova S., Chen Z., Wong K.K., Bardeesy N. Lysine-specific demethylase 2B (KDM2B)-let-7-enhancer of zester homolog 2 (EZH2) pathway regulates cell cycle progression and senescence in primary cells. J. Biol. Chem. 2011, 286:33061-33069.
    • (2011) J. Biol. Chem. , vol.286 , pp. 33061-33069
    • Tzatsos, A.1    Paskaleva, P.2    Lymperi, S.3    Contino, G.4    Stoykova, S.5    Chen, Z.6    Wong, K.K.7    Bardeesy, N.8
  • 314
    • 82955195630 scopus 로고    scopus 로고
    • Coordinated methyl-lysine erasure: structural and functional linkage of a Jumonji demethylase domain and a reader domain
    • Upadhyay A.K., Horton J.R., Zhang X., Cheng X. Coordinated methyl-lysine erasure: structural and functional linkage of a Jumonji demethylase domain and a reader domain. Curr. Opin. Struct. Biol. 2011, 21:750-760.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 750-760
    • Upadhyay, A.K.1    Horton, J.R.2    Zhang, X.3    Cheng, X.4
  • 315
    • 0032772689 scopus 로고    scopus 로고
    • Differential expression of human lysyl hydroxylase genes, lysine hydroxylation, and cross-linking of type I collagen during osteoblastic differentiation in vitro
    • Uzawa K., Grzesik W.J., Nishiura T., Kuznetsov S.A., Robey P.G., Brenner D.A., Yamauchi M. Differential expression of human lysyl hydroxylase genes, lysine hydroxylation, and cross-linking of type I collagen during osteoblastic differentiation in vitro. J. Bone Miner. Res. 1999, 14:1272-1280.
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 1272-1280
    • Uzawa, K.1    Grzesik, W.J.2    Nishiura, T.3    Kuznetsov, S.A.4    Robey, P.G.5    Brenner, D.A.6    Yamauchi, M.7
  • 316
    • 0015885681 scopus 로고
    • The 5-methylcytosine in DNA of rats. Tissue and age specificity and the changes induced by hydrocortisone and other agents
    • Vanyushin B.F., Nemirovsky L.E., Klimenko V.V., Vasiliev V.K., Belozersky A.N. The 5-methylcytosine in DNA of rats. Tissue and age specificity and the changes induced by hydrocortisone and other agents. Gerontologia 1973, 19:138-152.
    • (1973) Gerontologia , vol.19 , pp. 138-152
    • Vanyushin, B.F.1    Nemirovsky, L.E.2    Klimenko, V.V.3    Vasiliev, V.K.4    Belozersky, A.N.5
  • 317
    • 33744775719 scopus 로고    scopus 로고
    • Decreased collagen production in chronologically aged skin: roles of age-dependent alteration in fibroblast function and defective mechanical stimulation
    • Varani J., Dame M.K., Rittie L., Fligiel S.E., Kang S., Fisher G.J., Voorhees J.J. Decreased collagen production in chronologically aged skin: roles of age-dependent alteration in fibroblast function and defective mechanical stimulation. Am. J. Pathol. 2006, 168:1861-1868.
    • (2006) Am. J. Pathol. , vol.168 , pp. 1861-1868
    • Varani, J.1    Dame, M.K.2    Rittie, L.3    Fligiel, S.E.4    Kang, S.5    Fisher, G.J.6    Voorhees, J.J.7
  • 318
    • 84873635293 scopus 로고    scopus 로고
    • Genome instability and aging
    • Vijg J., Suh Y. Genome instability and aging. Annu. Rev. Physiol. 2013, 75:645-668.
    • (2013) Annu. Rev. Physiol. , vol.75 , pp. 645-668
    • Vijg, J.1    Suh, Y.2
  • 319
    • 2542497037 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes
    • Vranka J.A., Sakai L.Y., Bächinger H.P. Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J. Biol. Chem. 2004, 279:23615-23621.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23615-23621
    • Vranka, J.A.1    Sakai, L.Y.2    Bächinger, H.P.3
  • 320
    • 80052281488 scopus 로고    scopus 로고
    • Mitochondrial acetylation and diseases of aging
    • ID 234875
    • Wagner G.R., Payne R.M. Mitochondrial acetylation and diseases of aging. J. Aging Res. 2011, ID 234875.
    • (2011) J. Aging Res.
    • Wagner, G.R.1    Payne, R.M.2
  • 322
    • 84858604270 scopus 로고    scopus 로고
    • Metabolic reprogramming: a cancer hallmark even Warburg did not anticipate
    • Ward P.S., Thompson C.B. Metabolic reprogramming: a cancer hallmark even Warburg did not anticipate. Cancer Cell 2012, 21:297-308.
    • (2012) Cancer Cell , vol.21 , pp. 297-308
    • Ward, P.S.1    Thompson, C.B.2
  • 325
    • 77951240318 scopus 로고    scopus 로고
    • Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation
    • Wen H., Li J., Song T., Lu M., Kan P.Y., Lee M.G., Sha B., Shi X. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. J. Biol. Chem. 2010, 285:9322-9326.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9322-9326
    • Wen, H.1    Li, J.2    Song, T.3    Lu, M.4    Kan, P.Y.5    Lee, M.G.6    Sha, B.7    Shi, X.8
  • 327
    • 0023664725 scopus 로고
    • Genomic 5-methyldeoxycytidine decreases with age
    • Wilson V.L., Smith R.A., Ma S., Cutler R.G. Genomic 5-methyldeoxycytidine decreases with age. J. Biol. Chem. 1987, 262:9948-9951.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9948-9951
    • Wilson, V.L.1    Smith, R.A.2    Ma, S.3    Cutler, R.G.4
  • 328
    • 0033949848 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
    • Winder W.W., Holmes B.F., Rubink D.S., Jensen E.B., Chen M., Holloszy J.O. Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle. J. Appl. Physiol. 2000, 88:2219-2226.
    • (2000) J. Appl. Physiol. , vol.88 , pp. 2219-2226
    • Winder, W.W.1    Holmes, B.F.2    Rubink, D.S.3    Jensen, E.B.4    Chen, M.5    Holloszy, J.O.6
  • 331
    • 84875704850 scopus 로고    scopus 로고
    • Physiological consequences of complex II inhibition for aging, disease, and the mKATP channel
    • Wojtovich A.P., Smith C.O., Haynes C.M., Nehrke K.W., Brookes P.S. Physiological consequences of complex II inhibition for aging, disease, and the mKATP channel. Biochim. Biophys. Acta 2013, 1827:598-611.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 598-611
    • Wojtovich, A.P.1    Smith, C.O.2    Haynes, C.M.3    Nehrke, K.W.4    Brookes, P.S.5
  • 333
    • 84875799835 scopus 로고    scopus 로고
    • Fbxl10/Kdm2b recruits polycomb repressive complex 1 to CpG islands and regulates H2A ubiquitylation
    • Wu X., Johansen J.V., Helin K. Fbxl10/Kdm2b recruits polycomb repressive complex 1 to CpG islands and regulates H2A ubiquitylation. Mol. Cell 2013, 49:1134-1146.
    • (2013) Mol. Cell , vol.49 , pp. 1134-1146
    • Wu, X.1    Johansen, J.V.2    Helin, K.3
  • 334
    • 84862632865 scopus 로고    scopus 로고
    • Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors
    • Xiao M., Yang H., Xu W., Ma S., Lin H., Zhu H., Liu L., Liu Y., Yang C., Xu Y., Zhao S., Ye D., Xiong Y., Guan K.L. Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors. Genes Dev. 2012, 26:1326-1338.
    • (2012) Genes Dev. , vol.26 , pp. 1326-1338
    • Xiao, M.1    Yang, H.2    Xu, W.3    Ma, S.4    Lin, H.5    Zhu, H.6    Liu, L.7    Liu, Y.8    Yang, C.9    Xu, Y.10    Zhao, S.11    Ye, D.12    Xiong, Y.13    Guan, K.L.14
  • 336
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane K., Toumazou C., Tsukada Y., Erdjument-Bromage H., Tempst P., Wong J., Zhang Y. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell 2006, 125:483-495.
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1    Toumazou, C.2    Tsukada, Y.3    Erdjument-Bromage, H.4    Tempst, P.5    Wong, J.6    Zhang, Y.7
  • 338
    • 84883513587 scopus 로고    scopus 로고
    • Oncometabolites: linking altered metabolism with cancer
    • Yang M., Soga T., Pollard P.J. Oncometabolites: linking altered metabolism with cancer. J. Clin. Invest. 2013, 123:3652-3658.
    • (2013) J. Clin. Invest. , vol.123 , pp. 3652-3658
    • Yang, M.1    Soga, T.2    Pollard, P.J.3
  • 339
    • 20044371040 scopus 로고    scopus 로고
    • In the aging housefly aconitase is the only citric acid cycle enzyme to decline significantly
    • Yarian C.S., Sohal R.S. In the aging housefly aconitase is the only citric acid cycle enzyme to decline significantly. J. Bioenerg. Biomembr. 2005, 37:91-96.
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 91-96
    • Yarian, C.S.1    Sohal, R.S.2
  • 340
    • 28244454785 scopus 로고    scopus 로고
    • Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice
    • Yarian C.S., Toroser D., Sohal R.S. Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice. Mech. Ageing Dev. 2006, 127:79-84.
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 79-84
    • Yarian, C.S.1    Toroser, D.2    Sohal, R.S.3
  • 341
    • 0024578239 scopus 로고
    • The 2-oxo acid dehydrogenase complexes: recent advances
    • Yeaman S.J. The 2-oxo acid dehydrogenase complexes: recent advances. Biochem. J 1989, 257:625-632.
    • (1989) Biochem. J , vol.257 , pp. 625-632
    • Yeaman, S.J.1
  • 343
    • 84859746191 scopus 로고    scopus 로고
    • JMJD5, a Jumonji C (JmjC) domain-containing protein, negatively regulates osteoclastogenesis by facilitating NFATc1 protein degradation
    • Youn M.Y., Yokoyama A., Fujiyama-Nakamura S., Ohtake F., Minehata K., Yasuda H., Suzuki T., Kato S., Imai Y. JMJD5, a Jumonji C (JmjC) domain-containing protein, negatively regulates osteoclastogenesis by facilitating NFATc1 protein degradation. J. Biol. Chem. 2012, 287:12994-13004.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12994-13004
    • Youn, M.Y.1    Yokoyama, A.2    Fujiyama-Nakamura, S.3    Ohtake, F.4    Minehata, K.5    Yasuda, H.6    Suzuki, T.7    Kato, S.8    Imai, Y.9
  • 344
    • 84887037283 scopus 로고    scopus 로고
    • Aging-related genes in mesenchymal stem cells: a mini-review
    • Yu K.R., Kang K.S. Aging-related genes in mesenchymal stem cells: a mini-review. Gerontology 2013, 59:557-563.
    • (2013) Gerontology , vol.59 , pp. 557-563
    • Yu, K.R.1    Kang, K.S.2
  • 346
    • 77952795537 scopus 로고    scopus 로고
    • Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase
    • Zhou X., Sun H., Chen H., Zavadil J., Kluz T., Arita A., Costa M. Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase. Cancer Res. 2010, 70:4214-4221.
    • (2010) Cancer Res. , vol.70 , pp. 4214-4221
    • Zhou, X.1    Sun, H.2    Chen, H.3    Zavadil, J.4    Kluz, T.5    Arita, A.6    Costa, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.