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Volumn 502, Issue 7472, 2013, Pages 489-498

The nexus of chromatin regulation and intermediary metabolism

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYBUTYRATE DEHYDROGENASE; 3 HYDROXYBUTYRIC ACID; 5 METHYLTETRAHYDROFOLATE HOMOCYSTEINE METHYLTRANSFERASE; 5 METHYLTETRAHYDROFOLIC ACID; 5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); ACETYL COENZYME A; ADENOSINE TRIPHOSPHATE CITRATE LYASE; ADENOSYLHOMOCYSTEINASE; GLYCINE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; HISTONE METHYLTRANSFERASE; HOMOCYSTEINE; ISOCITRATE DEHYDROGENASE 1; ISOCITRATE DEHYDROGENASE 2; KETONE BODY; METHIONINE; METHIONINE ADENOSYLTRANSFERASE; OXIDOREDUCTASE; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; SERINE DEHYDRATASE; SIRTUIN; THREONINE; THREONINE 3 DEHYDROGENASE; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84886812954     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12752     Document Type: Review
Times cited : (320)

References (116)
  • 1
    • 34249275353 scopus 로고    scopus 로고
    • Phenotypic plasticity and the epigenetics of human disease
    • Feinberg, A. P. Phenotypic plasticity and the epigenetics of human disease. Nature 447, 433-440 (2007).
    • (2007) Nature , vol.447 , pp. 433-440
    • Feinberg, A.P.1
  • 2
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li, B., Carey, M. & Workman, J. L. The role of chromatin during transcription. Cell 128, 707-719 (2007).
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 3
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D. & Allis, C. D. The language of covalent histone modifications. Nature 403, 41-45 (2000).
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 4
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S. L. The complex language of chromatin regulation during transcription. Nature 447, 407-412 (2007).
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 5
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. & Allis, C. D. Translating the histone code. Science 293, 1074-1080 (2001).
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 6
    • 0017331464 scopus 로고
    • Structure of chromatin
    • Kornberg, R. D. Structure of chromatin. Annu. Rev. Biochem. 46, 931-954 (1977).
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 931-954
    • Kornberg, R.D.1
  • 9
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function. Cell 128, 693-705 (2007).
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 10
    • 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 153, 56-69 (2013).
    • (2013) Cell , vol.153 , pp. 56-69
    • Kaelin, W.G.1    McKnight, S.L.2
  • 11
    • 84863534997 scopus 로고    scopus 로고
    • Metabolic regulation of epigenetics
    • Lu, C. & Thompson, C. B. Metabolic regulation of epigenetics. Cell Metab. 16, 9-17 (2012).
    • (2012) Cell Metab. , vol.16 , pp. 9-17
    • Lu, C.1    Thompson, C.B.2
  • 12
    • 84858796367 scopus 로고    scopus 로고
    • A two-way street: Reciprocal regulation of metabolism and signalling
    • Wellen, K. E. & Thompson, C. B. A two-way street: reciprocal regulation of metabolism and signalling. Nature Rev. Mol. Cell Biol. 13, 270-276 (2012).
    • (2012) Nature Rev. Mol. Cell Biol. , vol.13 , pp. 270-276
    • Wellen, K.E.1    Thompson, C.B.2
  • 13
    • 84856090681 scopus 로고    scopus 로고
    • Connecting threads: Epigenetics and metabolism
    • Katada, S., Imhof, A. & Sassone-Corsi, P. Connecting threads: epigenetics and metabolism. Cell 148, 24-28 (2012).
    • (2012) Cell , vol.148 , pp. 24-28
    • Katada, S.1    Imhof, A.2    Sassone-Corsi, P.3
  • 14
    • 77957666255 scopus 로고    scopus 로고
    • Histone methyl transferases and demethylases; Can they link metabolism and transcription?
    • Teperino, R., Schoonjans, K. & Auwerx, J. Histone methyl transferases and demethylases; can they link metabolism and transcription? Cell Metab. 12, 321-327 (2010).
    • (2010) Cell Metab. , vol.12 , pp. 321-327
    • Teperino, R.1    Schoonjans, K.2    Auwerx, J.3
  • 15
    • 34249337761 scopus 로고    scopus 로고
    • Perceptions of epigenetics
    • Bird, A. Perceptions of epigenetics. Nature 447, 396-398 (2007).
    • (2007) Nature , vol.447 , pp. 396-398
    • Bird, A.1
  • 16
    • 38349100549 scopus 로고    scopus 로고
    • Epigenetic events in mammalian germ-cell development: Reprogramming and beyond
    • Sasaki, H. & Matsui, Y. Epigenetic events in mammalian germ-cell development: reprogramming and beyond. Nature Rev. Genet. 9, 129-140 (2008).
    • (2008) Nature Rev. Genet. , vol.9 , pp. 129-140
    • Sasaki, H.1    Matsui, Y.2
  • 17
    • 34249279527 scopus 로고    scopus 로고
    • Stability and flexibility of epigenetic gene regulation in mammalian development
    • Reik, W. Stability and flexibility of epigenetic gene regulation in mammalian development. Nature 447, 425-432 (2007).
    • (2007) Nature , vol.447 , pp. 425-432
    • Reik, W.1
  • 18
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • Hirschey, M. D. et al. SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 464, 121-125 (2010).
    • (2010) Nature , vol.464 , pp. 121-125
    • Hirschey, M.D.1
  • 19
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: Regulation by sirtuins and implications for metabolic disease
    • Newman, J. C., He, W. & Verdin, E. Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease. J. Biol. Chem. 287, 42436-42443 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 42436-42443
    • Newman, J.C.1    He, W.2    Verdin, E.3
  • 20
    • 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. 23, 467-476 (2012).
    • (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
  • 21
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profiling of histone methylations in the human genome
    • Barski, A. et al. High-resolution profiling of histone methylations in the human genome. Cell 129, 823-837 (2007).
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1
  • 22
    • 16344368814 scopus 로고    scopus 로고
    • Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
    • Forneris, F., Binda, C., Vanoni, M. A., Mattevi, A. & Battaglioli, E. Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process. FEBS Lett. 579, 2203-2207 (2005).
    • (2005) FEBS Lett. , vol.579 , pp. 2203-2207
    • Forneris, F.1    Binda, C.2    Vanoni, M.A.3    Mattevi, A.4    Battaglioli, E.5
  • 23
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • Loenarz, C. & Schofield, C. J. Expanding chemical biology of 2-oxoglutarate oxygenases. Nature Chem. Biol. 4, 152-156 (2008).
    • (2008) Nature Chem. Biol. , vol.4 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 24
    • 78650447665 scopus 로고    scopus 로고
    • β-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • Sakabe, K., Wang, Z. & Hart, G. W. β-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc. Natl Acad. Sci. USA 107, 19915-19920 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 25
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart, G. W. G., Housley, M. P. M. & Slawson, C. C. Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446, 1017-1022 (2007).
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.G.1    Housley, M.P.M.2    Slawson, C.C.3
  • 26
    • 84860184939 scopus 로고    scopus 로고
    • Bittersweet memories: Linking metabolism to epigenetics through O-GlcNAcylation
    • Hanover, J. A. J., Krause, M. W. M. & Love, D. C. D. Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation. Nature Rev. Mol. Cell Biol. 13, 312-321 (2012).
    • (2012) Nature Rev. Mol. Cell Biol. , vol.13 , pp. 312-321
    • Hanover, J.A.J.1    Krause, M.W.M.2    Love, D.C.D.3
  • 27
    • 84859512121 scopus 로고    scopus 로고
    • β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3
    • Fong, J. J. et al. β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3. J. Biol. Chem. 287, 12195-12203 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 12195-12203
    • Fong, J.J.1
  • 28
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
    • Rodgers, J. T. et al. Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1. Nature 434, 113-118 (2005).
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1
  • 29
    • 0027887302 scopus 로고
    • Functions for DNA methylation in vertebrates
    • Bird, A. P. Functions for DNA methylation in vertebrates. Cold Spring Harb. Symp. Quant. Biol. 58, 281-285 (1993).
    • (1993) Cold Spring Harb. Symp. Quant. Biol. , vol.58 , pp. 281-285
    • Bird, A.P.1
  • 30
    • 84886860116 scopus 로고    scopus 로고
    • TET enzymes, TDG and the dynamics of DNA demethylation
    • Kohli, R. M. & Zhang, Y. TET enzymes, TDG and the dynamics of DNA demethylation. Nature 502, 472-479 (2013).
    • (2013) Nature , vol.502 , pp. 472-479
    • Kohli, R.M.1    Zhang, Y.2
  • 31
    • 77957970301 scopus 로고    scopus 로고
    • Epigenetic modifications and human disease
    • Portela, A. & Esteller, M. Epigenetic modifications and human disease. Nature Biotechnol. 28, 1057-1068 (2010).
    • (2010) Nature Biotechnol. , vol.28 , pp. 1057-1068
    • Portela, A.1    Esteller, M.2
  • 32
    • 84876784115 scopus 로고    scopus 로고
    • Epigenetic flexibility in metabolic regulation: Disease cause and prevention?
    • Kirchner, H., Osler, M. E., Krook, A. & Zierath, J. R. Epigenetic flexibility in metabolic regulation: disease cause and prevention? Trends Cell Biol. 23, 203-209 (2013).
    • (2013) Trends Cell Biol. , vol.23 , pp. 203-209
    • Kirchner, H.1    Osler, M.E.2    Krook, A.3    Zierath, J.R.4
  • 33
    • 69149087790 scopus 로고    scopus 로고
    • Non-CpG methylation of the PGC-1α promoter through DNMT3B controls mitochondrial density
    • Barrès, R. et al. Non-CpG methylation of the PGC-1α promoter through DNMT3B controls mitochondrial density. Cell Metab. 10, 189-198 (2009).
    • (2009) Cell Metab. , vol.10 , pp. 189-198
    • Barrès, R.1
  • 34
    • 84876979205 scopus 로고    scopus 로고
    • Weight loss after gastric bypass surgery in human obesity remodels promoter methylation
    • Barrès, R. et al. Weight loss after gastric bypass surgery in human obesity remodels promoter methylation. Cell Rep. 3, 1020-1027 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 1020-1027
    • Barrès, R.1
  • 35
    • 84864010293 scopus 로고    scopus 로고
    • Nutrition and epigenetics: An interplay of dietary methyl donors, one-carbon metabolism and DNA methylation
    • Anderson, O. S., Sant, K. E. & Dolinoy, D. C. Nutrition and epigenetics: an interplay of dietary methyl donors, one-carbon metabolism and DNA methylation. J. Nutr. Biochem. 23, 853-859 (2012).
    • (2012) J. Nutr. Biochem. , vol.23 , pp. 853-859
    • Anderson, O.S.1    Sant, K.E.2    Dolinoy, D.C.3
  • 36
    • 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. et al. 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. 26, 1326-1338 (2012).
    • (2012) Genes Dev. , vol.26 , pp. 1326-1338
    • Xiao, M.1
  • 37
    • 33749052511 scopus 로고    scopus 로고
    • Rheostat control of gene expression by metabolites
    • Ladurner, A. G. Rheostat control of gene expression by metabolites. Mol. Cell 24, 1-11 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 1-11
    • Ladurner, A.G.1
  • 38
    • 4143147468 scopus 로고    scopus 로고
    • Metabolic enzymes and coenzymes in transcription-a direct link between metabolism and transcription?
    • Shi, Y. & Shi, Y. Metabolic enzymes and coenzymes in transcription-a direct link between metabolism and transcription? Trends Genet. 20, 445-452 (2004).
    • (2004) Trends Genet. , vol.20 , pp. 445-452
    • Shi, Y.1    Shi, Y.2
  • 39
    • 72049125350 scopus 로고    scopus 로고
    • Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
    • Dang, L. et al. Cancer-associated IDH1 mutations produce 2-hydroxyglutarate. Nature 462, 739-744 (2009).
    • (2009) Nature , vol.462 , pp. 739-744
    • Dang, L.1
  • 40
    • 78751676934 scopus 로고    scopus 로고
    • KAT(ching) metabolism by the tail: Insight into the links between lysine acetyltransferases and metabolism
    • Albaugh, B. N., Arnold, K. M. & Denu, J. M. KAT(ching) metabolism by the tail: insight into the links between lysine acetyltransferases and metabolism. Chem Bio Chem 12, 290-298 (2011).
    • (2011) Chem Bio Chem , vol.12 , pp. 290-298
    • Albaugh, B.N.1    Arnold, K.M.2    Denu, J.M.3
  • 41
    • 84876217035 scopus 로고    scopus 로고
    • Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways
    • Rardin, M. J. et al. Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways. Proc. Natl Acad. Sci. USA 110, 6601-6606(2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 6601-6606
    • Rardin, M.J.1
  • 42
    • 84872276165 scopus 로고    scopus 로고
    • Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
    • Hebert, A. S. et al. Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome. Mol. Cell 49, 186-199 (2012).
    • (2012) Mol. Cell , vol.49 , pp. 186-199
    • Hebert, A.S.1
  • 43
    • 33747591416 scopus 로고    scopus 로고
    • Metabolic cycles as an underlying basis of biological oscillations
    • Tu, B. P. & McKnight, S. L. Metabolic cycles as an underlying basis of biological oscillations. Nature Rev. Mol. Cell Biol. 7, 696-701 (2006).
    • (2006) Nature Rev. Mol. Cell Biol. , vol.7 , pp. 696-701
    • Tu, B.P.1    McKnight, S.L.2
  • 44
    • 36749067297 scopus 로고    scopus 로고
    • Cyclic changes in metabolic state during the life of a yeast cell
    • Tu, B. P. et al. Cyclic changes in metabolic state during the life of a yeast cell. Proc. Natl Acad. Sci. USA 104, 16886-16891 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16886-16891
    • Tu, B.P.1
  • 45
    • 57049152851 scopus 로고    scopus 로고
    • Catalysis and substrate selection by histone/protein lysine acetyltransferases
    • Berndsen, C. E. & Denu, J. M. Catalysis and substrate selection by histone/protein lysine acetyltransferases. Curr. Opin. Struct. Biol. 18, 682-689 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 682-689
    • Berndsen, C.E.1    Denu, J.M.2
  • 46
    • 79955960768 scopus 로고    scopus 로고
    • Acetyl-CoA induces cell growth and proliferation by promoting the acetylation of histones at growth genes
    • Cai, L., Sutter, B. M., Li, B. & Tu, B. P. Acetyl-CoA induces cell growth and proliferation by promoting the acetylation of histones at growth genes. Mol. Cell 42, 426-437 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 426-437
    • Cai, L.1    Sutter, B.M.2    Li, B.3    Tu, B.P.4
  • 47
    • 33745557847 scopus 로고    scopus 로고
    • Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription
    • Takahashi, H., McCaffery, J. M., Irizarry, R. A. & Boeke, J. D. Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Mol. Cell 23, 207-217 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 207-217
    • Takahashi, H.1    McCaffery, J.M.2    Irizarry, R.A.3    Boeke, J.D.4
  • 48
    • 66249105703 scopus 로고    scopus 로고
    • ATP-citrate lyase links cellular metabolism to histone acetylation
    • Wellen, K. E. et al. ATP-citrate lyase links cellular metabolism to histone acetylation. Science 324, 1076-1080 (2009).
    • (2009) Science , vol.324 , pp. 1076-1080
    • Wellen, K.E.1
  • 49
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • Haigis, M. C. & Guarente, L. P. Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction. Genes Dev. 20, 2913-2921 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 51
    • 84455188711 scopus 로고    scopus 로고
    • +, a circadian metabolite with an epigenetic twist
    • +, a circadian metabolite with an epigenetic twist. Endocrinology 153, 1-5 (2012).
    • (2012) Endocrinology , vol.153 , pp. 1-5
    • Sassone-Corsi, P.1
  • 53
    • 47549088250 scopus 로고    scopus 로고
    • +-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control
    • +-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control. Cell 134, 329-340 (2008).
    • (2008) Cell , vol.134 , pp. 329-340
    • Nakahata, Y.1
  • 54
    • 43049169926 scopus 로고    scopus 로고
    • Epigenetic control of rDNA loci in response to intracellular energy status
    • Murayama, A. et al. Epigenetic control of rDNA loci in response to intracellular energy status. Cell 133, 627-639 (2008).
    • (2008) Cell , vol.133 , pp. 627-639
    • Murayama, A.1
  • 55
    • 41349090663 scopus 로고    scopus 로고
    • SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
    • Michishita, E. et al. SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature 452, 492-496 (2008).
    • (2008) Nature , vol.452 , pp. 492-496
    • Michishita, E.1
  • 56
    • 58149090925 scopus 로고    scopus 로고
    • SIRT6 links histone H3 lysine 9 deacetylation to NF-κB-dependent gene expression and organismal life span
    • Kawahara, T. L. A. et al. SIRT6 links histone H3 lysine 9 deacetylation to NF-κB-dependent gene expression and organismal life span. Cell 136, 62-74 (2009).
    • (2009) Cell , vol.136 , pp. 62-74
    • Kawahara, T.L.A.1
  • 57
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky, R. et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 124, 315-329 (2006).
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1
  • 58
    • 84858000209 scopus 로고    scopus 로고
    • The sirtuin SIRT6 regulates lifespan in male mice
    • Kanfi, Y. et al. The sirtuin SIRT6 regulates lifespan in male mice. Nature 483, 218-221 (2012).
    • (2012) Nature , vol.483 , pp. 218-221
    • Kanfi, Y.1
  • 59
    • 0014621744 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver
    • Veech, R. L. R., Eggleston, L. V. L. & Krebs, H. A. H. The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem. J. 115, 609-619 (1969).
    • (1969) Biochem. J. , vol.115 , pp. 609-619
    • Veech, R.L.R.1    Eggleston, L.V.L.2    Krebs, H.A.H.3
  • 60
    • 84255198350 scopus 로고    scopus 로고
    • The cAMP/PKA pathway rapidly activates SIRT1 to promote fatty acid oxidation independently of changes in NAD
    • Gerhart-Hines, Z. et al. The cAMP/PKA pathway rapidly activates SIRT1 to promote fatty acid oxidation independently of changes in NAD. Mol. Cell 44, 851-863 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 851-863
    • Gerhart-Hines, Z.1
  • 61
    • 84862022077 scopus 로고    scopus 로고
    • + precursor nicotinamide riboside enhances oxidative metabolism and protects against high-fat diet-induced obesity
    • + precursor nicotinamide riboside enhances oxidative metabolism and protects against high-fat diet-induced obesity. Cell Metab. 15, 838-847 (2012).
    • (2012) Cell Metab. , vol.15 , pp. 838-847
    • Cantó, C.1
  • 62
    • 84874721105 scopus 로고    scopus 로고
    • Evidence for a common mechanism of SIRT1 regulation by allosteric activators
    • Hubbard, B. P. et al. Evidence for a common mechanism of SIRT1 regulation by allosteric activators. Science 339, 1216-1219 (2013).
    • (2013) Science , vol.339 , pp. 1216-1219
    • Hubbard, B.P.1
  • 63
    • 84877309874 scopus 로고    scopus 로고
    • Rejuvenating SIRT1 activators
    • Gut, P. & Verdin, E. Rejuvenating SIRT1 activators. Cell Metab. 17, 635-637 (2013).
    • (2013) Cell Metab. , vol.17 , pp. 635-637
    • Gut, P.1    Verdin, E.2
  • 64
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie, D. G. D., Ross, F. A. F. & Hawley, S. A. S. AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nature Rev. Mol. Cell Biol. 13, 251-262 (2012).
    • (2012) Nature Rev. Mol. Cell Biol. , vol.13 , pp. 251-262
    • Hardie, D.G.D.1    Ross, F.A.F.2    Hawley, S.A.S.3
  • 65
    • 77956294919 scopus 로고    scopus 로고
    • Signaling kinase AMPK activates stress-promoted transcription via histone H2B phosphorylation
    • Bungard, D. et al. Signaling kinase AMPK activates stress-promoted transcription via histone H2B phosphorylation. Science 329, 1201-1205 (2010).
    • (2010) Science , vol.329 , pp. 1201-1205
    • Bungard, D.1
  • 66
    • 33747195353 scopus 로고    scopus 로고
    • Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors
    • Takahashi, K. & Yamanaka, S. Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell 126, 663-676 (2006).
    • (2006) Cell , vol.126 , pp. 663-676
    • Takahashi, K.1    Yamanaka, S.2
  • 67
    • 78149487692 scopus 로고    scopus 로고
    • Pluripotency and cellular reprogramming: Facts, hypotheses, unresolved issues
    • Hanna, J. H., Saha, K. & Jaenisch, R. Pluripotency and cellular reprogramming: facts, hypotheses, unresolved issues. Cell 143, 508-525 (2010).
    • (2010) Cell , vol.143 , pp. 508-525
    • Hanna, J.H.1    Saha, K.2    Jaenisch, R.3
  • 68
    • 84886859638 scopus 로고    scopus 로고
    • Chromatin dynamics during cellular reprogramming
    • Apostolou, E. & Hochedlinger, K. Chromatin dynamics during cellular reprogramming. Nature 502, 462-471 (2013).
    • (2013) Nature , vol.502 , pp. 462-471
    • Apostolou, E.1    Hochedlinger, K.2
  • 69
    • 67749140110 scopus 로고    scopus 로고
    • Dependence of mouse embryonic stem cells on threonine catabolism
    • Wang, J. et al. Dependence of mouse embryonic stem cells on threonine catabolism. Science 325, 435-439 (2009).
    • (2009) Science , vol.325 , pp. 435-439
    • Wang, J.1
  • 70
    • 84872160110 scopus 로고    scopus 로고
    • Influence of threonine metabolism on S-adenosylmethionine and histone methylation
    • Shyh-Chang, N. et al. Influence of threonine metabolism on S-adenosylmethionine and histone methylation. Science 339, 222-226 (2013).
    • (2013) Science , vol.339 , pp. 222-226
    • Shyh-Chang, N.1
  • 71
    • 80053144962 scopus 로고    scopus 로고
    • A decade of exploring the cancer epigenome-biological and translational implications
    • Baylin, S. B. & Jones, P. A. A decade of exploring the cancer epigenome-biological and translational implications. Nature Rev. Cancer 11, 726-734 (2011).
    • (2011) Nature Rev. Cancer , vol.11 , pp. 726-734
    • Baylin, S.B.1    Jones, P.A.2
  • 72
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: The metabolic requirements of cell proliferation
    • Vander Heiden, M. G., Cantley, L. C. & Thompson, C. B. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 324, 1029-1033 (2009).
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 73
    • 77956674635 scopus 로고    scopus 로고
    • Evidence for an alternative glycolytic pathway in rapidly proliferating cells
    • Vander Heiden, M. G. et al. Evidence for an alternative glycolytic pathway in rapidly proliferating cells. Science 329, 1492-1499 (2010).
    • (2010) Science , vol.329 , pp. 1492-1499
    • Vander Heiden, M.G.1
  • 74
    • 84867606428 scopus 로고    scopus 로고
    • Hotspot mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma
    • Sturm, D. et al. Hotspot mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma. Cancer Cell 22, 425-437 (2012).
    • (2012) Cancer Cell , vol.22 , pp. 425-437
    • Sturm, D.1
  • 75
    • 84858796263 scopus 로고    scopus 로고
    • IDH1 mutation is sufficient to establish the glioma hypermethylator phenotype
    • Turcan, S. et al. IDH1 mutation is sufficient to establish the glioma hypermethylator phenotype. Nature 483, 479-483 (2012).
    • (2012) Nature , vol.483 , pp. 479-483
    • Turcan, S.1
  • 76
    • 77956265489 scopus 로고    scopus 로고
    • IDH mutations in glioma and acute myeloid leukemia
    • Dang, L., Jin, S. & Su, S. M. IDH mutations in glioma and acute myeloid leukemia. Trends Mol. Med. 16, 387-397 (2010).
    • (2010) Trends Mol. Med. , vol.16 , pp. 387-397
    • Dang, L.1    Jin, S.2    Su, S.M.3
  • 77
    • 48649087037 scopus 로고    scopus 로고
    • Inhibition of histone-deacetylase activity by short-chain fatty acids and some polyphenol metabolites formed in the colon
    • Waldecker, M., Kautenburger, T., Daumann, H., Busch, C. & Schrenk, D. Inhibition of histone-deacetylase activity by short-chain fatty acids and some polyphenol metabolites formed in the colon. J. Nutr. Biochem. 19, 587-593 (2008).
    • (2008) J. Nutr. Biochem. , vol.19 , pp. 587-593
    • Waldecker, M.1    Kautenburger, T.2    Daumann, H.3    Busch, C.4    Schrenk, D.5
  • 78
    • 0019940133 scopus 로고
    • Utilization of nutrients by isolated epithelial cells of the rat colon
    • Roediger, W. E. Utilization of nutrients by isolated epithelial cells of the rat colon. Gastroenterology 83, 424-429 (1982).
    • (1982) Gastroenterology , vol.83 , pp. 424-429
    • Roediger, W.E.1
  • 79
    • 35848936502 scopus 로고    scopus 로고
    • Dietary modulation of colon cancer risk
    • Kim, Y. S. & Milner, J. A. Dietary modulation of colon cancer risk. J. Nutr. 137, 2576S-2579S (2007).
    • (2007) J. Nutr. , vol.137
    • Kim, Y.S.1    Milner, J.A.2
  • 80
    • 84870389262 scopus 로고    scopus 로고
    • The Warburg effect dictates the mechanism of butyrate-mediated histone acetylation and cell proliferation
    • Donohoe, D. R. et al. The Warburg effect dictates the mechanism of butyrate-mediated histone acetylation and cell proliferation. Mol. Cell 48, 612-626 (2012).
    • (2012) Mol. Cell , vol.48 , pp. 612-626
    • Donohoe, D.R.1
  • 81
    • 33745301716 scopus 로고    scopus 로고
    • The effects of short-chain fatty acids on colon epithelial proliferation and survival depend on the cellular phenotype
    • Comalada, M. et al. The effects of short-chain fatty acids on colon epithelial proliferation and survival depend on the cellular phenotype. J. Cancer Res. Clin. Oncol. 132, 487-497 (2006).
    • (2006) J. Cancer Res. Clin. Oncol. , vol.132 , pp. 487-497
    • Comalada, M.1
  • 82
    • 33750110683 scopus 로고    scopus 로고
    • Fuel metabolism in starvation
    • Cahill, G. F. Fuel metabolism in starvation. Annu. Rev. Nutr. 26, 1-22 (2006).
    • (2006) Annu. Rev. Nutr. , vol.26 , pp. 1-22
    • Cahill, G.F.1
  • 83
    • 0034624968 scopus 로고    scopus 로고
    • D-β-hydroxybutyrate protects neurons in models of Alzheimer's and Parkinson's disease
    • Kashiwaya, Y. et al. D-β-hydroxybutyrate protects neurons in models of Alzheimer's and Parkinson's disease. Proc. Natl Acad. Sci. USA 97, 5440-5444 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5440-5444
    • Kashiwaya, Y.1
  • 84
    • 60749090581 scopus 로고    scopus 로고
    • The neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies
    • Maalouf, M., Rho, J. M. & Mattson, M. P. The neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies. Brain Res. Rev. 59, 293-315 (2009).
    • (2009) Brain Res. Rev. , vol.59 , pp. 293-315
    • Maalouf, M.1    Rho, J.M.2    Mattson, M.P.3
  • 85
    • 84872166360 scopus 로고    scopus 로고
    • Suppression of oxidative stress by β-hydroxybutyrate, an endogenous histone deacetylase inhibitor
    • Shimazu, T. et al. Suppression of oxidative stress by β-hydroxybutyrate, an endogenous histone deacetylase inhibitor. Science 339, 211-214 (2013).
    • (2013) Science , vol.339 , pp. 211-214
    • Shimazu, T.1
  • 86
    • 41349085806 scopus 로고    scopus 로고
    • Nutritional control of reproductive status in honeybees via DNA methylation
    • Kucharski, R., Maleszka, J., Foret, S. & Maleszka, R. Nutritional control of reproductive status in honeybees via DNA methylation. Science 319, 1827-1830 (2008).
    • (2008) Science , vol.319 , pp. 1827-1830
    • Kucharski, R.1    Maleszka, J.2    Foret, S.3    Maleszka, R.4
  • 87
    • 23044514669 scopus 로고    scopus 로고
    • Epigenetic differences arise during the lifetime of monozygotic twins
    • Fraga, M. F. M. et al. Epigenetic differences arise during the lifetime of monozygotic twins. Proc. Natl Acad. Sci. USA 102, 10604-10609 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 10604-10609
    • Fraga, M.F.M.1
  • 88
    • 84855956247 scopus 로고    scopus 로고
    • Epigenetics and the environment: Emerging patterns and implications
    • Feil, R. & Fraga, M. F. Epigenetics and the environment: emerging patterns and implications. Nature Rev. Genet. 13, 97-109 (2011).
    • (2011) Nature Rev. Genet. , vol.13 , pp. 97-109
    • Feil, R.1    Fraga, M.F.2
  • 89
    • 29144453326 scopus 로고    scopus 로고
    • Intensive diabetes treatment and cardiovascular disease in patients with type 1 diabetes
    • Nathan, D. M. et al. Intensive diabetes treatment and cardiovascular disease in patients with type 1 diabetes. N. Engl. J. Med. 353, 2643-2653 (2005).
    • (2005) N. Engl. J. Med. , vol.353 , pp. 2643-2653
    • Nathan, D.M.1
  • 90
    • 45149133036 scopus 로고    scopus 로고
    • Intensive blood glucose control and vascular outcomes in patients with type 2 diabetes
    • Patel, A. et al. Intensive blood glucose control and vascular outcomes in patients with type 2 diabetes. N. Engl. J. Med. 358, 2560-2572 (2008).
    • (2008) N. Engl. J. Med. , vol.358 , pp. 2560-2572
    • Patel, A.1
  • 92
    • 80053559849 scopus 로고    scopus 로고
    • Genome-wide analysis distinguishes hyperglycemia regulated epigenetic signatures of primary vascular cells
    • Pirola, L. et al. Genome-wide analysis distinguishes hyperglycemia regulated epigenetic signatures of primary vascular cells. Genome Res. 21, 1601-1615 (2011).
    • (2011) Genome Res. , vol.21 , pp. 1601-1615
    • Pirola, L.1
  • 93
    • 48249127225 scopus 로고    scopus 로고
    • Epigenetic histone H3 lysine 9 methylation in metabolic memory and inflammatory phenotype of vascular smooth muscle cells in diabetes
    • Villeneuve, L. M. et al. Epigenetic histone H3 lysine 9 methylation in metabolic memory and inflammatory phenotype of vascular smooth muscle cells in diabetes. Proc. Natl Acad. Sci. USA 105, 9047-9052 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9047-9052
    • Villeneuve, L.M.1
  • 94
    • 65549170303 scopus 로고    scopus 로고
    • Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with gene-activating epigenetic marks that coexist on the lysine tail
    • Brasacchio, D. et al. Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with gene-activating epigenetic marks that coexist on the lysine tail. Diabetes 58, 1229-1236 (2009).
    • (2009) Diabetes , vol.58 , pp. 1229-1236
    • Brasacchio, D.1
  • 95
    • 84876673669 scopus 로고    scopus 로고
    • Intergenerational programming of metabolic disease: Evidence from human populations and experimental animal models
    • Patti, M.-E. Intergenerational programming of metabolic disease: evidence from human populations and experimental animal models. Cell. Mol. Life Sci. 70, 1597-1608 (2013).
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 1597-1608
    • Patti, M.-E.1
  • 96
    • 33847769732 scopus 로고    scopus 로고
    • Anthropometric measures in middle age after exposure to famine during gestation: Evidence from the Dutch famine
    • Stein, A. D. et al. Anthropometric measures in middle age after exposure to famine during gestation: evidence from the Dutch famine. Am. J. Clin. Nutr. 85, 869-876 (2007).
    • (2007) Am. J. Clin. Nutr. , vol.85 , pp. 869-876
    • Stein, A.D.1
  • 97
    • 34250781054 scopus 로고    scopus 로고
    • Transgenerational response to nutrition, early life circumstances and longevity
    • Kaati, G., Bygren, L. O., Pembrey, M. & Sjöström, M. Transgenerational response to nutrition, early life circumstances and longevity. Eur. J. Hum. Genet. 15, 784-790 (2007).
    • (2007) Eur. J. Hum. Genet. , vol.15 , pp. 784-790
    • Kaati, G.1    Bygren, L.O.2    Pembrey, M.3    Sjöström, M.4
  • 98
    • 32944469027 scopus 로고    scopus 로고
    • Preconceptional fasting of fathers alters serum glucose in offspring of mice
    • Anderson, L. M. et al. Preconceptional fasting of fathers alters serum glucose in offspring of mice. Nutrition 22, 327-331 (2006).
    • (2006) Nutrition , vol.22 , pp. 327-331
    • Anderson, L.M.1
  • 99
    • 78650446334 scopus 로고    scopus 로고
    • Paternally induced transgenerational environmental reprogramming of metabolic gene expression in mammals
    • Carone, B. R. et al. Paternally induced transgenerational environmental reprogramming of metabolic gene expression in mammals. Cell 143, 1084-1096 (2010).
    • (2010) Cell , vol.143 , pp. 1084-1096
    • Carone, B.R.1
  • 100
    • 0032699670 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor α mediates the adaptive response to fasting
    • Kersten, S. et al. Peroxisome proliferator-activated receptor α mediates the adaptive response to fasting. J. Clin. Invest. 103, 1489-1498 (1999).
    • (1999) J. Clin. Invest. , vol.103 , pp. 1489-1498
    • Kersten, S.1
  • 101
    • 77958596171 scopus 로고    scopus 로고
    • Chronic high-fat diet in fathers programs β-cell dysfunction in female rat offspring
    • Ng, S.-F. et al. Chronic high-fat diet in fathers programs β-cell dysfunction in female rat offspring. Nature 467, 963-966 (2010).
    • (2010) Nature , vol.467 , pp. 963-966
    • Ng, S.-F.1
  • 102
    • 84865790047 scopus 로고    scopus 로고
    • An integrated encyclopedia of DNA elements in the human genome
    • ENCODE Project Consortium.
    • ENCODE Project Consortium. An integrated encyclopedia of DNA elements in the human genome. Nature 489, 57-74 (2012).
    • (2012) Nature , vol.489 , pp. 57-74
  • 103
    • 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 148, 46-57 (2012).
    • (2012) Cell , vol.148 , pp. 46-57
    • Rando, T.A.1    Chang, H.Y.2
  • 104
    • 20144363712 scopus 로고    scopus 로고
    • A potential decline in life expectancy in the United States in the 21st century
    • Olshansky, S. J. et al. A potential decline in life expectancy in the United States in the 21st century. N. Engl. J. Med. 352, 1138-1145 (2005).
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1138-1145
    • Olshansky, S.J.1
  • 106
    • 84886808679 scopus 로고    scopus 로고
    • Chromatin proteins and modifications as drug targets
    • Helin, K. & Dhanak, D. Chromatin proteins and modifications as drug targets. Nature 502, 480-488 (2013).
    • (2013) Nature , vol.502 , pp. 480-488
    • Helin, K.1    Dhanak, D.2
  • 107
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • Zhang, Q., Piston, D. W. & Goodman, R. H. Regulation of corepressor function by nuclear NADH. Science 295, 1895-1897 (2002).
    • (2002) Science , vol.295 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3
  • 108
    • 84858030373 scopus 로고    scopus 로고
    • Fluorescence imaging of cellular metabolites with RNA
    • Paige, J. S., Nguyen-Duc, T., Song, W. & Jaffrey, S. R. Fluorescence imaging of cellular metabolites with RNA. Science 335, 1194 (2012).
    • (2012) Science , vol.335 , pp. 1194
    • Paige, J.S.1    Nguyen-Duc, T.2    Song, W.3    Jaffrey, S.R.4
  • 109
    • 84868024193 scopus 로고    scopus 로고
    • A genetically encoded metabolite sensor for malonyl-CoA
    • Ellis, J. M. & Wolfgang, M. J. A genetically encoded metabolite sensor for malonyl-CoA. Chem. Biol. 19, 1333-1339 (2012).
    • (2012) Chem. Biol. , vol.19 , pp. 1333-1339
    • Ellis, J.M.1    Wolfgang, M.J.2
  • 110
    • 79953732149 scopus 로고    scopus 로고
    • A fluorescent reporter of AMPK activity and cellular energy stress
    • Tsou, P., Bin, B., Zheng, Hsu, C.-H., Sasaki, A. T. & Cantley, L. C. A fluorescent reporter of AMPK activity and cellular energy stress. Cell Metab. 13, 476-486 (2011).
    • (2011) Cell Metab. , vol.13 , pp. 476-486
    • Tsou, P.1    Bin, B.2    Zheng Hsu, C.-H.3    Sasaki, A.T.4    Cantley, L.C.5
  • 111
    • 67649255876 scopus 로고    scopus 로고
    • A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • Niethammer, P., Grabher, C., Look, A. T. & Mitchison, T. J. A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 459, 996-999 (2009).
    • (2009) Nature , vol.459 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 112
    • 77950200010 scopus 로고    scopus 로고
    • The genetics of ageing
    • Kenyon, C. J. The genetics of ageing. Nature 464, 504-512 (2010).
    • (2010) Nature , vol.464 , pp. 504-512
    • Kenyon, C.J.1
  • 113
    • 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. 22, 42-49 (2012).
    • (2012) Trends Cell Biol. , vol.22 , pp. 42-49
    • Han, S.1    Brunet, A.2
  • 114
    • 81555214034 scopus 로고    scopus 로고
    • Transgenerational epigenetic inheritance of longevity in Caenorhabditis elegans
    • Greer, E. L. et al. Transgenerational epigenetic inheritance of longevity in Caenorhabditis elegans. Nature 479, 365-371 (2011).
    • (2011) Nature , vol.479 , pp. 365-371
    • Greer, E.L.1
  • 115
    • 77951176737 scopus 로고    scopus 로고
    • Extending healthy life span-from yeast to humans
    • Fontana, L., Partridge, L. & Longo, V. D. Extending healthy life span-from yeast to humans. Science 328, 321-326 (2010).
    • (2010) Science , vol.328 , pp. 321-326
    • Fontana, L.1    Partridge, L.2    Longo, V.D.3
  • 116
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • Bordone, L. & Guarente, L. Calorie restriction, SIRT1 and metabolism: understanding longevity. Nature Rev. Mol. Cell Biol. 6, 298-305 (2005).
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2


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