메뉴 건너뛰기




Volumn 15, Issue 2, 2011, Pages 551-589

The redox basis of epigenetic modifications: From mechanisms to functional consequences

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYGLUTARIC ACID; 2 OXOGLUTARIC ACID; ADENOSINE DIPHOSPHATE RIBOSE; ALCOHOL; ASCORBIC ACID; DNA; DNA METHYLTRANSFERASE; ENZYME; GLUTATHIONE; GLYCOGEN SYNTHASE KINASE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEMETHYLASE; HISTONE METHYLTRANSFERASE; HOMOCYSTEINE; METHIONINE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PARACETAMOL; POLY(ADENOSINE DIPHOSPHATE RIBOSE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; RESVERATROL; RNA; S ADENOSYLMETHIONINE; SIRTUIN; SIRTUIN 1;

EID: 79959521749     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2010.3492     Document Type: Review
Times cited : (226)

References (353)
  • 1
    • 0036805853 scopus 로고    scopus 로고
    • Cytopathies involving mitochondrial complex II
    • DOI 10.1016/S0098-2997(02)00012-2, PII S0098299702000122
    • Ackrell BA. Cytopathies involving mitochondrial complex II. Mol Aspects Med 23: 369-384, 2002. (Pubitemid 35286652)
    • (2002) Molecular Aspects of Medicine , vol.23 , Issue.5 , pp. 369-384
    • Ackrell, B.A.C.1
  • 2
    • 57349166553 scopus 로고    scopus 로고
    • Hydroxyglutaric aciduria and malignant brain tumor: A case report and literature review
    • Aghili M, Zahedi F, and Rafiee E. Hydroxyglutaric aciduria and malignant brain tumor: a case report and literature review. J Neurooncol 91: 233-236, 2009.
    • (2009) J Neurooncol , vol.91 , pp. 233-236
    • Aghili, M.1    Zahedi, F.2    Rafiee, E.3
  • 3
    • 0034254857 scopus 로고    scopus 로고
    • NuRD and SIN3: Histone deacetylase complexes in development
    • DOI 10.1016/S0168-9525(00)02066-7, PII S0168952500020667
    • Ahringer J. NuRD and SIN3 histone deacetylase complexes in development. Trends Genet 16: 351-356, 2000. (Pubitemid 30628836)
    • (2000) Trends in Genetics , vol.16 , Issue.8 , pp. 351-356
    • Ahringer, J.1
  • 7
    • 33644875954 scopus 로고    scopus 로고
    • Neuronal protection by sirtuins in alzheimer's disease
    • Anekonda TS and Reddy PH. Neuronal protection by sirtuins in Alzheimer's disease. J Neurochem 96: 305-313, 2006.
    • (2006) J Neurochem , vol.96 , pp. 305-313
    • Anekonda, T.S.1    Reddy, P.H.2
  • 8
    • 72149084899 scopus 로고    scopus 로고
    • Peptidylarginine deiminase 4 and citrullination in health and disease
    • Anzilotti C, Pratesi F, Tommasi C, and Migliorini P. Peptidylarginine deiminase 4 and citrullination in health and disease. Autoimmun Rev 9: 158-160, 2010.
    • (2010) Autoimmun Rev , vol.9 , pp. 158-160
    • Anzilotti, C.1    Pratesi, F.2    Tommasi, C.3    Migliorini, P.4
  • 9
    • 84983711696 scopus 로고
    • Studies on the chemical nature of the substance inducing transformation of pneumococcal types: Induction of transformation by a desoxyribonucleic acid fraction isolated from pneumococcus type III
    • Avery OT, Macleod CM, and McCarty M. Studies on the chemical nature of the substance inducing transformation of pneumococcal types: induction of transformation by a desoxyribonucleic acid fraction isolated from pneumococcus type III. J Exp Med 79: 137-158, 1944.
    • (1944) J Exp Med , vol.79 , pp. 137-158
    • Avery, O.T.1    Macleod, C.M.2    McCarty, M.3
  • 11
    • 0038655454 scopus 로고    scopus 로고
    • A novel jmjC domain protein modulates heterochromatization in fission yeast
    • DOI 10.1128/MCB.23.12.4356-4370.2003
    • Ayoub N, Noma K, Isaac S, Kahan T, Grewal SI, and Cohen A. A novel jmjC domain protein modulates heterochromatization in fission yeast. Mol Cell Biol 23: 4356-4370, 2003. (Pubitemid 36666436)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.12 , pp. 4356-4370
    • Ayoub, N.1    Noma, K.-I.2    Isaac, S.3    Kahan, T.4    Grewal, S.I.S.5    Cohen, A.6
  • 12
    • 0036239879 scopus 로고    scopus 로고
    • Methionine synthase: A possible prime site of the ethanolic lesion in liver
    • DOI 10.1016/S0741-8329(01)00201-4, PII S0741832901002014
    • Barak AJ, Beckenhauer HC, and Tuma DJ. Methionine synthase. a possible prime site of the ethanolic lesion in liver. Alcohol 26: 65-67, 2002. (Pubitemid 34462228)
    • (2002) Alcohol , vol.26 , Issue.2 , pp. 65-67
    • Barak, A.J.1    Beckenhauer, H.C.2    Tuma, D.J.3
  • 14
    • 33847307112 scopus 로고    scopus 로고
    • Nitric oxide modulates oxygen sensing by hypoxia-inducible factor 1-dependent induction of prolyl hydroxylase 2
    • DOI 10.1074/jbc.M607065200
    • Berchner-Pfannschmidt U, Yamac H, Trinidad B, and Fandrey J. Nitric oxide modulates oxygen sensing by hypoxia-inducible factor 1-dependent induction of prolyl hydroxylase 2. J Biol Chem 282: 1788-1796, 2007. (Pubitemid 47076719)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 1788-1796
    • Berchner-Pfannschmidt, U.1    Yamac, H.2    Trinidad, B.3    Fandrey, J.4
  • 15
    • 0022634961 scopus 로고
    • Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of poly(ADP-ribose) polymerase
    • Berger SJ, Sudar DC, and Berger NA. Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of poly (ADP-ribose) polymerase. Biochem Biophys Res Commun 134: 227-232, 1986. (Pubitemid 16145323)
    • (1986) Biochemical and Biophysical Research Communications , vol.134 , Issue.1 , pp. 227-232
    • Berger, S.J.1    Sudar, D.C.2    Berger, N.A.3
  • 16
    • 0033753779 scopus 로고    scopus 로고
    • The DNA methyltransferases of mammals
    • Bestor TH. The DNA methyltransferases of mammals. Hum Mol Genet 9: 2395-2402, 2000.
    • (2000) Hum Mol Genet , vol.9 , pp. 2395-2402
    • Bestor, T.H.1
  • 17
    • 0033559510 scopus 로고    scopus 로고
    • Identification of a second major tumor-specific antigen recognized by CTLs on mouse mastocytoma P815
    • Bilsborough J, Van Pel A, Uyttenhove C, Boon T, and Van den Eynde BJ. Identification of a second major tumor-specific antigen recognized by CTLs on mouse mastocytoma P815. J Immunol 162: 3534-3540, 1999. (Pubitemid 29313606)
    • (1999) Journal of Immunology , vol.162 , Issue.6 , pp. 3534-3540
    • Bilsborough, J.1    Van Pel, A.2    Uyttenhove, C.3    Boon, T.4    Van Den Eynde, B.J.5
  • 18
    • 34249337761 scopus 로고    scopus 로고
    • Perceptions of epigenetics
    • DOI 10.1038/nature05913, PII NATURE05913
    • Bird A. Perceptions of epigenetics. Nature 447: 396-398, 2007. (Pubitemid 46816744)
    • (2007) Nature , vol.447 , Issue.7143 , pp. 396-398
    • Bird, A.1
  • 19
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast Sir2 and human SIRT1
    • DOI 10.1074/jbc.M205670200
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, and Sinclair DA. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 277: 45099-45107, 2002. (Pubitemid 36159111)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 20
    • 69249220176 scopus 로고    scopus 로고
    • DNA methylation and methyl-cpg binding proteins: Developmental requirements and function
    • Bogdanovic O and Veenstra GJ. DNA methylation and methyl-CpG binding proteins: developmental requirements and function. Chromosoma 118: 549-565, 2009.
    • (2009) Chromosoma , vol.118 , pp. 549-565
    • Bogdanovic, O.1    Veenstra, G.J.2
  • 21
    • 0342618710 scopus 로고    scopus 로고
    • Influence of histone acetylation on the modification of cytoplasmic and nuclear proteins by ADP-ribosylation in response to free radicals
    • DOI 10.1016/S0304-4165(96)00085-2, PII S0304416596000852
    • Bohm L, Schneeweiss FA, Sharan RN, and Feinendegen LE. Influence of histone acetylation on the modification of cytoplasmic and nuclear proteins by ADP-ribosylation in response to free radicals. Biochim Biophys Acta 1334: 149-154, 1997. (Pubitemid 27117516)
    • (1997) Biochimica et Biophysica Acta - General Subjects , vol.1334 , Issue.2-3 , pp. 149-154
    • Bohm, L.1    Schneeweiss, F.A.2    Sharan, R.N.3    Feinendegen, L.E.4
  • 22
    • 0015795009 scopus 로고
    • Cobalt compounds for the control of hypoxic stress
    • Brahmachari HD and Joseph S. Cobalt compounds for the control of hypoxic stress. Aerosp Med 44: 636-638, 1973.
    • (1973) Aerosp Med , vol.44 , pp. 636-638
    • Brahmachari, H.D.1    Joseph, S.2
  • 24
  • 25
    • 35248839988 scopus 로고    scopus 로고
    • Alpha-ketoglutarate is the precursor of L-2-hydroxyglutarate
    • Brunengraber H. Alpha-ketoglutarate is the precursor of L-2-hydroxyglutarate. J Inherit Metab Dis 30: 628, 2007.
    • (2007) J Inherit Metab Dis , vol.30 , pp. 628
    • Brunengraber, H.1
  • 26
    • 33745105118 scopus 로고    scopus 로고
    • Anaplerotic molecules: Current and future
    • DOI 10.1007/s10545-006-0320-1
    • Brunengraber H and Roe CR. Anaplerotic molecules: current and future. J Inherit Metab Dis 29: 327-331, 2006. (Pubitemid 43880628)
    • (2006) Journal of Inherited Metabolic Disease , vol.29 , Issue.2-3 , pp. 327-331
    • Brunengraber, H.1    Roe, C.R.2
  • 27
    • 18244390483 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
    • DOI 10.1002/ana.20474
    • Bubber P, Haroutunian V, Fisch G, Blass JP, and Gibson GE. Mitochondrial abnormalities in Alzheimer brain: mechanistic implications. Ann Neurol 57: 695-703, 2005. (Pubitemid 40628858)
    • (2005) Annals of Neurology , vol.57 , Issue.5 , pp. 695-703
    • Bubber, P.1    Haroutunian, V.2    Fisch, G.3    Blass, J.P.4    Gibson, G.E.5
  • 28
    • 0037352050 scopus 로고    scopus 로고
    • 2-oxo acid dehydrogenase complexes in redox regulation
    • Bunik VI. 2-Oxo acid dehydrogenase complexes in redox regulation. Eur J Biochem 270: 1036-1042, 2003.
    • (2003) Eur J Biochem , vol.270 , pp. 1036-1042
    • Bunik, V.I.1
  • 29
    • 61849157257 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Burns A and Iliffe S. Alzheimer's disease. BMJ 338: b158, 2009.
    • (2009) BMJ , vol.338
    • Burns, A.1    Iliffe, S.2
  • 30
    • 18844413584 scopus 로고    scopus 로고
    • Nitric oxide reverses desferrioxamine- and hypoxia-evoked HIF-1α accumulation - Implications for prolyl hydroxylase activity and iron
    • DOI 10.1016/j.yexcr.2005.02.018, PII S0014482705000844
    • Callapina M, Zhou J, Schnitzer S, Metzen E, Lohr C, Deitmer JW, and Brune B. Nitric oxide reverses desferrioxamine- and hypoxia-evoked HIF-1alpha accumulation - implications for prolyl hydroxylase activity and iron. Exp Cell Res 306: 274-284, 2005. (Pubitemid 40692790)
    • (2005) Experimental Cell Research , vol.306 , Issue.1 , pp. 274-284
    • Callapina, M.1    Zhou, J.2    Schnitzer, S.3    Metzen, E.4    Lohr, C.5    Deitmer, J.W.6    Brune, B.7
  • 33
    • 0035378322 scopus 로고    scopus 로고
    • Functional mitochondria are required for amyloid betamediated neurotoxicity
    • Cardoso SM, Santos S, Swerdlow RH, and Oliveira CR. Functional mitochondria are required for amyloid betamediated neurotoxicity. FASEB J 15: 1439-1441, 2001.
    • (2001) FASEB J , vol.15 , pp. 1439-1441
    • Cardoso, S.M.1    Santos, S.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 34
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • Castro L, Rodriguez M, and Radi R. Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. J Biol Chem 269: 29409-29415, 1994. (Pubitemid 24365085)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.47 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 36
    • 77950790835 scopus 로고    scopus 로고
    • Hepatoprotective effects of S-adenosyl-L-methionine against alcohol- and cytochrome P450 2E1-induced liver injury
    • Cederbaum AI. Hepatoprotective effects of S-adenosyl-L-methionine against alcohol- and cytochrome P450 2E1-induced liver injury. World J Gastroenterol 16: 1366-1376, 2010.
    • (2010) World J Gastroenterol , vol.16 , pp. 1366-1376
    • Cederbaum, A.I.1
  • 37
    • 70450239624 scopus 로고    scopus 로고
    • Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells
    • Cervera AM, Bayley JP, Devilee P, and McCreath KJ. Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells. Mol Cancer 8, 2009.
    • (2009) Mol Cancer , vol.8
    • Cervera, A.M.1    Bayley, J.P.2    Devilee, P.3    McCreath, K.J.4
  • 38
    • 0002160618 scopus 로고
    • Nicotinamide mononucleotide activation of new DNA-dependent poly-adenylic acid synthesizing nuclear enzyme
    • Chambon P, Weill JD, and Mandel P. Nicotinamide mononucleotide activation of new DNA-dependent poly-adenylic acid synthesizing nuclear enzyme. Biochem Biophys Res Commun 11: 39-43, 1963.
    • (1963) Biochem Biophys Res Commun , vol.11 , pp. 39-43
    • Chambon, P.1    Weill, J.D.2    Mandel, P.3
  • 39
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • DOI 10.1126/science.1145801
    • Chang B, Chen Y, Zhao Y, and Bruick RK. JMJD6 is a histone arginine demethylase. Science 318: 444-447, 2007. (Pubitemid 47614528)
    • (2007) Science , vol.318 , Issue.5849 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 40
    • 79959508911 scopus 로고    scopus 로고
    • PADI4 and tumourigenesis
    • Chang X and Fang K. PADI4 and tumourigenesis. Cancer Cell Int 10: 7, 2010.
    • (2010) Cancer Cell Int , vol.10 , pp. 7
    • Chang, X.1    Fang, K.2
  • 41
    • 33646576501 scopus 로고    scopus 로고
    • Nickel ions increase histone H3 lysine 9 dimethylation and induce transgene silencing
    • DOI 10.1128/MCB.26.10.3728-3737.2006
    • Chen H, Ke Q, Kluz T, Yan, Y, and Costa M. Nickel ions increase histone H3 lysine 9 dimethylation and induce transgene silencing. Mol Cell Biol 26: 3728-3737, 2006. (Pubitemid 43726391)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.10 , pp. 3728-3737
    • Chen, H.1    Ke, Q.2    Kluz, T.3    Yan, Y.4    Costa, M.5
  • 44
    • 77955170881 scopus 로고    scopus 로고
    • Hypoxiaregulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression
    • Chen Z, Li Y, Zhang H, Huang P, and Luthra R. Hypoxiaregulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression. Oncogene 29: 4362-4368, 2010.
    • (2010) Oncogene , vol.29 , pp. 4362-4368
    • Chen, Z.1    Li, Y.2    Zhang, H.3    Huang, P.4    Luthra, R.5
  • 45
    • 67349106068 scopus 로고    scopus 로고
    • MicroRNA-21 protects against the H(2)O(2)-induced injury on cardiac myocytes via its target gene PDCD4
    • Cheng Y, Liu X, Zhang S, Lin Y, Yang J, and Zhang C. MicroRNA-21 protects against the H(2)O(2)-induced injury on cardiac myocytes via its target gene PDCD4. J Mol Cell Cardiol 47: 5-14, 2009.
    • (2009) J Mol Cell Cardiol , vol.47 , pp. 5-14
    • Cheng, Y.1    Liu, X.2    Zhang, S.3    Lin, Y.4    Yang, J.5    Zhang, C.6
  • 47
    • 40649111338 scopus 로고    scopus 로고
    • Non-coding RNAs, epigenetics and complexity
    • Costa FF. Non-coding RNAs, epigenetics and complexity. Gene 410: 9-17, 2008.
    • (2008) Gene , vol.410 , pp. 9-17
    • Costa, F.F.1
  • 50
    • 0034682761 scopus 로고    scopus 로고
    • Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity
    • Cozzi A, Corsi B, Levi S, Santambrogio P, Albertini A, and Arosio P. Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity. J Biol Chem 275: 25122-25129, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 25122-25129
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Albertini, A.5    Arosio, P.6
  • 51
    • 77953737471 scopus 로고    scopus 로고
    • Ascorbate induces autophagy in pancreatic cancer
    • Cullen JJ. Ascorbate induces autophagy in pancreatic cancer. Autophagy 6: 421-422, 2010.
    • (2010) Autophagy , vol.6 , pp. 421-422
    • Cullen, J.J.1
  • 54
    • 0034720734 scopus 로고    scopus 로고
    • Base excision repair is impaired in mammalian cells lacking poly(ADP- ribose) polymerase-1
    • DOI 10.1021/bi0003442
    • Dantzer F, de La Rubia G, Menissier-De Murcia J, Hostomsky Z, de Murcia G, and Schreiber V. Base excision repair is impaired in mammalian cells lacking Poly(ADP-ribose) polymerase-1. Biochemistry 39: 7559-7569, 2000. (Pubitemid 30422075)
    • (2000) Biochemistry , vol.39 , Issue.25 , pp. 7559-7569
    • Dantzer, F.1    De La Rubia, G.2    Menissier-De Murcia, J.3    Hostomsky, Z.4    De Murcia, G.5    Schreiber, V.6
  • 55
    • 0032925999 scopus 로고    scopus 로고
    • Reduced levels of poly(adp-ribosyl)ation result in chromatin compaction and hypermethylation as shown by cell-by-cell computer-assisted quantitative analysis
    • de Capoa A, Febbo FR, Giovannelli F, Niveleau A, Zardo G, Marenzi S, and Caiafa P. Reduced levels of poly(ADP-ribosyl)ation result in chromatin compaction and hypermethylation as shown by cell-by-cell computer-assisted quantitative analysis. FASEB J 13: 89-93, 1999. (Pubitemid 29038278)
    • (1999) FASEB Journal , vol.13 , Issue.1 , pp. 89-93
    • De Capoa, A.1    Febbo, F.R.2    Giovannelli, F.3    Niveleau, A.4    Zardo, G.5    Marenzi, S.6    Caiafa, P.7
  • 56
    • 34250218580 scopus 로고    scopus 로고
    • Important roles of multiple sp1 binding sites and epigenetic modifications in the regulation of the methionine sulfoxide reductase B1 (MsrB1) promoter
    • De Luca A, Sacchetta P, Nieddu M, Di Ilio, C and Favaloro B. Important roles of multiple Sp1 binding sites and epigenetic modifications in the regulation of the methionine sulfoxide reductase B1 (MsrB1) promoter. BMC Mol Biol 8: 39, 2007.
    • (2007) BMC Mol Biol , vol.8 , pp. 39
    • De Luca, A.1    Sacchetta, P.2    Nieddu, M.3    Di Ilio, C.4    Favaloro, B.5
  • 57
    • 0022834642 scopus 로고
    • Modulation of chromatin superstructure induced by poly(ADP-ribose) synthesis and degradation
    • de Murcia G, Huletsky A, Lamarre D, Gaudreau A, Pouyet J, Daune M, and Poirier GG. Modulation of chromatin superstructure induced by poly(ADP-ribose) synthesis and degradation. J Biol Chem 261: 7011-7017, 1986. (Pubitemid 17219474)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.15 , pp. 7011-7017
    • De Murcia, G.1    Huletsky, A.2    Lamarres, D.3
  • 58
    • 50149097983 scopus 로고    scopus 로고
    • Hypoxia, HIF1 and glucose metabolism in the solid tumour
    • Denko NC. Hypoxia, HIF1 and glucose metabolism in the solid tumour. Nat Rev Cancer 8: 705-713, 2008.
    • (2008) Nat Rev Cancer , vol.8 , pp. 705-713
    • Denko, N.C.1
  • 59
    • 77952963702 scopus 로고    scopus 로고
    • H(2)O(2)-mediated cytotoxicity of pharmacologic ascorbate concentrations to neuroblastoma cells: Potential role of lactate and ferritin
    • Deubzer B, Mayer F, Kuci Z, Niewisch M, Merkel G, Handgretinger R, and Bruchelt G. H(2)O(2)-mediated cytotoxicity of pharmacologic ascorbate concentrations to neuroblastoma cells: potential role of lactate and ferritin. Cell Physiol Biochem 25: 767-774, 2010.
    • (2010) Cell Physiol Biochem , vol.25 , pp. 767-774
    • Deubzer, B.1    Mayer, F.2    Kuci, Z.3    Niewisch, M.4    Merkel, G.5    Handgretinger, R.6    Bruchelt, G.7
  • 61
    • 23944509075 scopus 로고    scopus 로고
    • The SETdomain protein superfamily: Protein lysine methyltrans-ferases
    • Dillon SC, Zhang X, Trievel RC, and Cheng X. The SETdomain protein superfamily: protein lysine methyltrans-ferases. Genome Biol 6: 227, 2005.
    • (2005) Genome Biol , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3    Cheng, X.4
  • 63
    • 0034109902 scopus 로고    scopus 로고
    • Epigenetic silencing of maspin gene expression in human breast cancers
    • DOI 10.1002/(SICI)1097-0215(20000315)85:6<805::AID-IJC12>3.0.CO;2-5
    • Domann FE, Rice JC, Hendrix MJ, and Futscher BW. Epigenetic silencing of maspin gene expression in human breast cancers. Int J Cancer 85: 805-810, 2000. (Pubitemid 30131470)
    • (2000) International Journal of Cancer , vol.85 , Issue.6 , pp. 805-810
    • Domann, F.E.1    Rice, J.C.2    Hendrix, M.J.C.3    Futscher, B.W.4
  • 64
    • 0035266127 scopus 로고    scopus 로고
    • Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species
    • Donald SP, Sun XY, Hu CA, Yu J, Mei JM, Valle D, and Phang JM. Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species. Cancer Res 61: 1810-1815, 2001. (Pubitemid 32691989)
    • (2001) Cancer Research , vol.61 , Issue.5 , pp. 1810-1815
    • Donald, S.P.1    Sun, X.-Y.2    Hu, C.-A.A.3    Yu, J.4    Mei, J.M.5    Valle, D.6    Phang, J.M.7
  • 65
    • 77952936173 scopus 로고    scopus 로고
    • Redox signaling, alkylation (carbonylation) of conserved cysteines inactivates class I histone deacetylases 1, 2, and 3 and antagonizes their transcriptional repressor function
    • Doyle, K and Fitzpatrick FA. Redox signaling, alkylation (carbonylation) of conserved cysteines inactivates class I histone deacetylases 1, 2, and 3 and antagonizes their transcriptional repressor function. J Biol Chem 285: 17417-17424, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 17417-17424
    • Doyle, K.1    Fitzpatrick, F.A.2
  • 66
    • 0023902956 scopus 로고
    • S-adenosyl-L-methionine synthetase and phospholipid methyltransferase are inhibited in human cirrhosis
    • Duce AM, Ortiz P, Cabrero C, and Mato JM. S-adenosyl-L-methionine synthetase and phospholipid methyltransferase are inhibited in human cirrhosis. Hepatology 8: 65-68, 1988. (Pubitemid 18092060)
    • (1988) Hepatology , vol.8 , Issue.1 , pp. 65-68
    • Duce, A.M.1    Ortiz, P.2    Cabrero, C.3    Mato, J.M.4
  • 71
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • DOI 10.1038/nature01048
    • Falnes PO, Johansen RF, and Seeberg E. AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature 419: 178-182, 2002. (Pubitemid 35025447)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 72
    • 77956402239 scopus 로고    scopus 로고
    • MicroRNA-210 regulates mitochondrial free radical response to hypoxia and krebs cycle in cancer cells by targeting iron sulfur cluster protein ISCU
    • Favaro E, Ramachandran A, McCormick R, Gee H, Blancher C, Crosby M, Devlin C, Blick C, Buffa F, Li JL, et al. MicroRNA-210 regulates mitochondrial free radical response to hypoxia and krebs cycle in cancer cells by targeting iron sulfur cluster protein ISCU. PLoS ONE 5: e10345, 2010.
    • (2010) PLoS ONE , vol.5
    • Favaro, E.1    Ramachandran, A.2    McCormick, R.3    Gee, H.4    Blancher, C.5    Crosby, M.6    Devlin, C.7    Blick, C.8    Buffa, F.9    Li, J.L.10
  • 74
    • 29244469466 scopus 로고    scopus 로고
    • The epigenetic progenitor origin of human cancer
    • DOI 10.1038/nrg1748
    • Feinberg AP, Ohlsson R, and Henikoff S. The epigenetic progenitor origin of human cancer. Nat Rev Genet 7: 21-33, 2006. (Pubitemid 41828945)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.1 , pp. 21-33
    • Feinberg, A.P.1    Ohlsson, R.2    Henikoff, S.3
  • 75
    • 0036024260 scopus 로고    scopus 로고
    • S-Adenosyl-L-methionine and mitochondrial reduced glutathione depletion in alcoholic liver disease
    • DOI 10.1016/S0741-8329(02)00229-X, PII S074183290200229X
    • Fernandez-Checa JC, Colell A, and Garcia-Ruiz C. S-Adenosyl-L-methionine and mitochondrial reduced glutathione depletion in alcoholic liver disease. Alcohol 27: 179-183, 2002. (Pubitemid 34876920)
    • (2002) Alcohol , vol.27 , Issue.3 , pp. 179-183
    • Fernandez-Checa, J.C.1    Colell, A.2    Garcia-Ruiz, C.3
  • 76
    • 52049087584 scopus 로고    scopus 로고
    • Leigh and leigh-like syndrome in children and adults
    • Finsterer J. Leigh and Leigh-like syndrome in children and adults. Pediatr Neurol 39: 223-235, 2008.
    • (2008) Pediatr Neurol , vol.39 , pp. 223-235
    • Finsterer, J.1
  • 77
    • 77950906905 scopus 로고    scopus 로고
    • Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents
    • Flashman E, Davies SL, Yeoh KK, and Schofield CJ. Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents. Biochem J 427: 135-142, 2010.
    • (2010) Biochem J , vol.427 , pp. 135-142
    • Flashman, E.1    Davies, S.L.2    Yeoh, K.K.3    Schofield, C.J.4
  • 78
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint DH, Tuminello JF, and Emptage MH. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 268: 22369-22376, 1993. (Pubitemid 23318282)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 79
    • 68749115479 scopus 로고    scopus 로고
    • New roles of flavoproteins in molecular cell biology: Histone demethylase LSD1 and chromatin
    • Forneris F, Battaglioli E, Mattevi A, and Binda C. New roles of flavoproteins in molecular cell biology: histone demethylase LSD1 and chromatin. FEBS J 276: 4304-4312, 2009.
    • (2009) FEBS J , vol.276 , pp. 4304-4312
    • Forneris, F.1    Battaglioli, E.2    Mattevi, A.3    Binda, C.4
  • 80
    • 16344368814 scopus 로고    scopus 로고
    • Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
    • DOI 10.1016/j.febslet.2005.03.015
    • Forneris F, Binda C, Vanoni MA, Mattevi A, and Battaglioli E. Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process. FEBS Lett 579: 2203-2207, 2005. (Pubitemid 40469693)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2203-2207
    • Forneris, F.1    Binda, C.2    Vanoni, M.A.3    Mattevi, A.4    Battaglioli, E.5
  • 81
    • 65549083102 scopus 로고    scopus 로고
    • The putative tumor suppressor microRNA-101 modulates the cancer epigenome by repressing the polycomb group protein EZH2
    • Friedman JM, Liang G, Liu CC, Wolff EM, Tsai YC, Ye W, Zhou X, and Jones PA. The putative tumor suppressor microRNA-101 modulates the cancer epigenome by repressing the polycomb group protein EZH2. Cancer Res 69: 2623-2629, 2009.
    • (2009) Cancer Res , vol.69 , pp. 2623-2629
    • Friedman, J.M.1    Liang, G.2    Liu, C.C.3    Wolff, E.M.4    Tsai, Y.C.5    Ye, W.6    Zhou, X.7    Jones, P.A.8
  • 82
    • 78651428138 scopus 로고    scopus 로고
    • The role of natural selection in the origin of life
    • Fry I. The Role of natural selection in the origin of life. Orig Life Evol Biosph 41: 3-16, 2011.
    • (2011) Orig Life Evol Biosph , vol.41 , pp. 3-16
    • Fry, I.1
  • 83
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (Sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • DOI 10.1006/bbrc.1999.0897
    • Frye RA. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 260: 273-279, 1999. (Pubitemid 29351819)
    • (1999) Biochemical and Biophysical Research Communications , vol.260 , Issue.1 , pp. 273-279
    • Frye, R.A.1
  • 84
    • 0037591867 scopus 로고    scopus 로고
    • Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression
    • DOI 10.1074/jbc.M302283200
    • Fujita N, Watanabe S, Ichimura T, Tsuruzoe S, Shinkai Y, Tachibana M, Chiba T, and Nakao M. Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 hetero-chromatic complex for DNA methylation-based transcriptional repression. J Biol Chem 278: 24132-24138, 2003. (Pubitemid 36830249)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 24132-24138
    • Fujita, N.1    Watanabe, S.2    Ichimura, T.3    Tsuruzoe, S.4    Shinkai, Y.5    Tachibana, M.6    Chiba, T.7    Nakao, M.8
  • 85
    • 0038412822 scopus 로고    scopus 로고
    • The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase
    • DOI 10.1093/nar/gkg332
    • Fuks F, Hurd PJ, Deplus R, and Kouzarides T. The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase. Nucleic Acids Res 31: 2305-2312, 2003. (Pubitemid 37442098)
    • (2003) Nucleic Acids Research , vol.31 , Issue.9 , pp. 2305-2312
    • Fuks, F.1    Hurd, P.J.2    Deplus, R.3    Kouzarides, T.4
  • 87
    • 33646548638 scopus 로고    scopus 로고
    • Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion
    • DOI 10.1021/bi060212u
    • Gantt SL, Gattis SG, and Fierke CA. Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry 45: 6170-6178, 2006. (Pubitemid 43727109)
    • (2006) Biochemistry , vol.45 , Issue.19 , pp. 6170-6178
    • Gantt, S.L.1    Gattis, S.G.2    Fierke, C.A.3
  • 88
    • 77951223432 scopus 로고    scopus 로고
    • The microtubule-associated histone deacetylase 6 (HDAC6) regulates epidermal growth factor receptor (EGFR) endocytic trafficking and degradation
    • Gao YS, Hubbert CC, and Yao TP. The microtubule-associated histone deacetylase 6 (HDAC6) regulates epidermal growth factor receptor (EGFR) endocytic trafficking and degradation. J Biol Chem 285: 11219-11226, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 11219-11226
    • Gao, Y.S.1    Hubbert, C.C.2    Yao, T.P.3
  • 89
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner PR and Fridovich I. Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266: 19328-19333, 1991. (Pubitemid 21908236)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.29 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 90
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner PR, Raineri I, Epstein LB, and White CW. Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem 270: 13399-13405, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 94
    • 0035213138 scopus 로고    scopus 로고
    • The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway
    • DOI 10.1086/324413
    • Gimenez-Roqueplo AP, Favier J, Rustin P, Mourad JJ, Plouin PF, Corvol P, Rotig A, and Jeunemaitre X. The R22 × mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway. Am J Hum Genet 69: 1186-1197, 2001. (Pubitemid 33124200)
    • (2001) American Journal of Human Genetics , vol.69 , Issue.6 , pp. 1186-1197
    • Gimenez-Roqueplo, A.-P.1    Favier, J.2    Rustin, P.3    Mourad, J.-J.4    Plouin, P.-F.5    Corvol, P.6    Rotig, A.7    Jeunemaitre, X.8
  • 96
    • 0025745413 scopus 로고
    • ADP-ribosylation of core histones and their acetylated subspecies
    • Golderer G and Grobner P. ADP-ribosylation of core histones and their acetylated subspecies. Biochem J 277(Pt 3): 607-610, 1991.
    • (1991) Biochem J , vol.277 , Issue.PART 3 , pp. 607-610
    • Golderer, G.1    Grobner, P.2
  • 97
    • 73149117308 scopus 로고    scopus 로고
    • Targeting histone demethylases in cancer therapy
    • Grant S. Targeting histone demethylases in cancer therapy. Clin Cancer Res 15: 7111-7113, 2009.
    • (2009) Clin Cancer Res , vol.15 , pp. 7111-7113
    • Grant, S.1
  • 98
    • 75449119103 scopus 로고    scopus 로고
    • Somatic mutations of IDH1 and IDH2 in the leukemic transformation of myeloproliferative neoplasms
    • Green A and Beer P. Somatic mutations of IDH1 and IDH2 in the leukemic transformation of myeloproliferative neoplasms. N Engl J Med 362: 369-370, 2010.
    • (2010) N Engl J Med , vol.362 , pp. 369-370
    • Green, A.1    Beer, P.2
  • 99
    • 58149267462 scopus 로고    scopus 로고
    • Nicotinamide restores cognition in alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of thr231-phosphotau
    • Green KN, Steffan JS, Martinez-Coria H, Sun X, Schreiber SS, Thompson LM, and LaFerla FM. Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau. J Neurosci 28: 11500-11510, 2008.
    • (2008) J Neurosci , vol.28 , pp. 11500-11510
    • Green, K.N.1    Steffan, J.S.2    Martinez-Coria, H.3    Sun, X.4    Schreiber, S.S.5    Thompson, L.M.6    LaFerla, F.M.7
  • 100
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • DOI 10.1016/j.jmb.2004.02.006, PII S0022283604001408
    • Gregoretti IV, Lee YM, and Goodson HV. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. JMol Biol 338: 17-31, 2004. (Pubitemid 38429783)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.1 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.-M.2    Goodson, H.V.3
  • 101
    • 77952236323 scopus 로고    scopus 로고
    • RNAi-dependent formation of heterochromatin and its diverse functions
    • Grewal SI. RNAi-dependent formation of heterochromatin and its diverse functions. Curr Opin Genet Dev 20: 134-141, 2010.
    • (2010) Curr Opin Genet Dev , vol.20 , pp. 134-141
    • Grewal, S.I.1
  • 103
    • 22744444561 scopus 로고    scopus 로고
    • Calorie restriction and SIR2 genes - Towards a mechanism
    • DOI 10.1016/j.mad.2005.03.013, PII S0047637405000795
    • Guarente L. Calorie restriction and SIR2 genes - towards a mechanism. Mech Ageing Dev 126: 923-928, 2005. (Pubitemid 41033172)
    • (2005) Mechanisms of Ageing and Development , vol.126 , Issue.9 SPEC. ISS. , pp. 923-928
    • Guarente, L.1
  • 104
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins - Emerging roles in physiology, aging, and calorie restriction
    • DOI 10.1101/gad.1467506
    • Haigis MC and Guarente LP. Mammalian sirtuins - emerging roles in physiology, aging, and calorie restriction. Genes Dev 20: 2913-2921, 2006. (Pubitemid 44771725)
    • (2006) Genes and Development , vol.20 , Issue.21 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 105
    • 77954345408 scopus 로고    scopus 로고
    • Genome-wide reprogramming in the mouse germ line entails the base excision repair pathway
    • Hajkova P, Jeffries SJ, Lee C, Miller N, Jackson SP, and Surani MA. Genome-wide reprogramming in the mouse germ line entails the base excision repair pathway. Science 329: 78-82, 2010.
    • (2010) Science , vol.329 , pp. 78-82
    • Hajkova, P.1    Jeffries, S.J.2    Lee, C.3    Miller, N.4    Jackson, S.P.5    Surani, M.A.6
  • 106
    • 55549139051 scopus 로고    scopus 로고
    • The expanding field of poly(ADP-ribosyl)ation reactions. "Protein modifications: Beyond the usual suspects" review series
    • Hakme A, Wong HK, Dantzer F, and Schreiber V. The expanding field of poly(ADP-ribosyl)ation reactions. "Protein modifications: beyond the usual suspects" Review Series. EMBO Rep 9: 1094-1100, 2008.
    • (2008) EMBO Rep , vol.9 , pp. 1094-1100
    • Hakme, A.1    Wong, H.K.2    Dantzer, F.3    Schreiber, V.4
  • 108
    • 65249164893 scopus 로고    scopus 로고
    • Ure(k)a! Sirtuins regulate mitochondria
    • Hallows WC, Smith BC, Lee S, and Denu JM. Ure(k)a! Sirtuins Regulate Mitochondria. Cell 137: 404-406, 2009.
    • (2009) Cell , vol.137 , pp. 404-406
    • Hallows, W.C.1    Smith, B.C.2    Lee, S.3    Denu, J.M.4
  • 110
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going?
    • DOI 10.1128/MMBR.00040-05
    • Hassa PO, Haenni SS, Elser M, and Hottiger MO. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? Microbiol Mol Biol Rev 70: 789-829, 2006. (Pubitemid 44484693)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.3 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 111
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPs, a small but powerful family of poly-ADP-ribose polymerases
    • DOI 10.2741/2909
    • Hassa PO and Hottiger MO. The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. Front Biosci 13: 3046-3082, 2008. (Pubitemid 351589219)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.8 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 112
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen A and Fridovich I. Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J Biol Chem 269: 29405-29408, 1994. (Pubitemid 24365084)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.47 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 113
    • 66249108936 scopus 로고    scopus 로고
    • Promoter targeted small RNAs induce long-term transcriptional gene silencing in human cells
    • Hawkins PG, Santoso S, Adams C, Anest V, and Morris KV. Promoter targeted small RNAs induce long-term transcriptional gene silencing in human cells. Nucleic Acids Res 37: 2984-2995, 2009.
    • (2009) Nucleic Acids Res , vol.37 , pp. 2984-2995
    • Hawkins, P.G.1    Santoso, S.2    Adams, C.3    Anest, V.4    Morris, K.V.5
  • 114
    • 0036105474 scopus 로고    scopus 로고
    • New view at C
    • DOI 10.1038/nm0502-445
    • Hediger MA. New view at C. Nat Med 8: 445-446, 2002. (Pubitemid 34546739)
    • (2002) Nature Medicine , vol.8 , Issue.5 , pp. 445-446
    • Hediger, M.A.1
  • 117
    • 38049056733 scopus 로고    scopus 로고
    • Energy metabolism, altered proteins, sirtuins and ageing: Converging mechanisms?
    • Hipkiss AR. Energy metabolism, altered proteins, sirtuins and ageing: converging mechanisms? Biogerontology 9: 49-55, 2008.
    • (2008) Biogerontology , vol.9 , pp. 49-55
    • Hipkiss, A.R.1
  • 119
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • DOI 10.1074/jbc.M304982200
    • Hirsila M, Koivunen P, Gunzler V, Kivirikko KI, and Myllyharju J. Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J Biol Chem 278: 30772-30780, 2003. (Pubitemid 36994584)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 120
    • 34548140496 scopus 로고    scopus 로고
    • An epigenetic perspective on the free radical theory of development
    • DOI 10.1016/j.freeradbiomed.2007.06.027, PII S0891584907004601
    • Hitchler MJ and Domann FE. An epigenetic perspective on the free radical theory of development. Free Radic Biol Med 43: 1023-1036, 2007. (Pubitemid 47302657)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.7 , pp. 1023-1036
    • Hitchler, M.J.1    Domann, F.E.2
  • 121
    • 67349240804 scopus 로고    scopus 로고
    • Metabolic defects provide a spark for the epigenetic switch in cancer
    • Hitchler MJ and Domann FE. Metabolic defects provide a spark for the epigenetic switch in cancer. Free Radic Biol Med 47: 115-127, 2009.
    • (2009) Free Radic Biol Med , vol.47 , pp. 115-127
    • Hitchler, M.J.1    Domann, F.E.2
  • 122
  • 123
    • 0023279926 scopus 로고
    • The inheritance of epigenetic defects
    • Holliday R. The inheritance of epigenetic defects. Science 238: 163-170, 1987. (Pubitemid 17139717)
    • (1987) Science , vol.238 , Issue.4824 , pp. 163-170
    • Holliday, R.1
  • 124
    • 0033306577 scopus 로고    scopus 로고
    • Transcriptional repression by REST: Recruitment of Sin3A and histone deacetylase to neuronal genes
    • DOI 10.1038/13165
    • Huang Y, Myers SJ, and Dingledine R. Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes. Nat Neurosci 2: 867-872, 1999. (Pubitemid 30602598)
    • (1999) Nature Neuroscience , vol.2 , Issue.10 , pp. 867-872
    • Huang, Y.1    Myers, S.J.2    Dingledine, R.3
  • 126
    • 33646819342 scopus 로고    scopus 로고
    • The plasma membrane redox system in aging
    • DOI 10.1016/j.arr.2006.03.005, PII S1568163706000341
    • Hyun DH, Hernandez JO, Mattson MP, and de Cabo R. The plasma membrane redox system in aging. Ageing Res Rev 5: 209-220, 2006. (Pubitemid 43766257)
    • (2006) Ageing Research Reviews , vol.5 , Issue.2 , pp. 209-220
    • Hyun, D.-H.1    Hernandez, J.O.2    Mattson, M.P.3    De Cabo, R.4
  • 127
    • 0024673303 scopus 로고
    • CpG methylation of the cAMP-responsive enhancer/promoter sequence TGACGT-CA abolishes specific factor binding as well as transcriptional activation
    • Iguchi-Ariga SM and Schaffner W. CpG methylation of the cAMP-responsive enhancer/promoter sequence TGACGT-CA abolishes specific factor binding as well as transcriptional activation. Genes Dev 3: 612-619, 1989.
    • (1989) Genes Dev , vol.3 , pp. 612-619
    • Iguchi-Ariga, S.M.1    Schaffner, W.2
  • 128
    • 67349255210 scopus 로고    scopus 로고
    • CpG islands - "A rough guide"
    • Illingworth RS and Bird AP. CpG islands - "a rough guide." FEBS Lett 583: 1713-1720, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 1713-1720
    • Illingworth, R.S.1    Bird, A.P.2
  • 129
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • DOI 10.1038/35001622
    • Imai S, Armstrong CM, Kaeberlein M, and Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800, 2000. (Pubitemid 30111843)
    • (2000) Nature , vol.403 , Issue.6771 , pp. 795-800
    • Imai, S.-I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 130
    • 68349110863 scopus 로고    scopus 로고
    • Epigenetics in hyperhomocysteinemic states. A special focus on uremia
    • Ingrosso D and Perna AF. Epigenetics in hyperhomocysteinemic states. A special focus on uremia. Biochim Biophys Acta 1790: 892-899, 2009.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 892-899
    • Ingrosso, D.1    Perna, A.F.2
  • 132
    • 0842308109 scopus 로고    scopus 로고
    • Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: Role of tyrosine nitration
    • DOI 10.1016/j.bbrc.2004.01.046
    • Ito K, Hanazawa T, Tomita K, Barnes PJ, and Adcock IM. Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: role of tyrosine nitration. Biochem Biophys Res Commun 315: 240-245, 2004. (Pubitemid 38175212)
    • (2004) Biochemical and Biophysical Research Communications , vol.315 , Issue.1 , pp. 240-245
    • Ito, K.1    Hanazawa, T.2    Tomita, K.3    Barnes, P.J.4    Adcock, I.M.5
  • 134
    • 38449104412 scopus 로고    scopus 로고
    • On the enzymatic properties of dnmt1: Specificity, processivity, mechanism of linear diffusion and allosteric regulation of the enzyme
    • Jeltsch A. On the enzymatic properties of Dnmt1: specificity, processivity, mechanism of linear diffusion and allosteric regulation of the enzyme. Epigenetics 1: 63-66, 2006.
    • (2006) Epigenetics , vol.1 , pp. 63-66
    • Jeltsch, A.1
  • 135
    • 77955918482 scopus 로고    scopus 로고
    • Reversible acetylation of PGC-1: Connecting energy sensors and effectors to guarantee metabolic flexibility
    • Jeninga EH, Schoonjans K, and Auwerx J. Reversible acetylation of PGC-1: connecting energy sensors and effectors to guarantee metabolic flexibility. Oncogene 29: 4617-4624, 2010.
    • (2010) Oncogene , vol.29 , pp. 4617-4624
    • Jeninga, E.H.1    Schoonjans, K.2    Auwerx, J.3
  • 136
    • 70350221895 scopus 로고    scopus 로고
    • Arsenicals produce stable progressive changes in DNA methylation patterns that are linked to malignant transformation of immortalized urothelial cells
    • Jensen TJ, Novak P, Wnek SM, Gandolfi AJ, and Futscher BW. Arsenicals produce stable progressive changes in DNA methylation patterns that are linked to malignant transformation of immortalized urothelial cells. Toxicol Appl Pharmacol 241: 221-229, 2009.
    • (2009) Toxicol Appl Pharmacol , vol.241 , pp. 221-229
    • Jensen, T.J.1    Novak, P.2    Wnek, S.M.3    Gandolfi, A.J.4    Futscher, B.W.5
  • 137
    • 59349117680 scopus 로고    scopus 로고
    • Epigenetic mediated transcriptional activation of WNT5A participates in arsenical-associated malignant transformation
    • Jensen TJ, Wozniak RJ, Eblin KE, Wnek SM, Gandolfi AJ, and Futscher BW. Epigenetic mediated transcriptional activation of WNT5A participates in arsenical-associated malignant transformation. Toxicol Appl Pharmacol 235: 39-46, 2009.
    • (2009) Toxicol Appl Pharmacol , vol.235 , pp. 39-46
    • Jensen, T.J.1    Wozniak, R.J.2    Eblin, K.E.3    Wnek, S.M.4    Gandolfi, A.J.5    Futscher, B.W.6
  • 138
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein T and Allis CD. Translating the histone code. Science 293: 1074-1080, 2001. (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 139
    • 0031984480 scopus 로고    scopus 로고
    • SET domain proteins modulate chromatin domains in eu- and heterochromatin
    • DOI 10.1007/s000180050127
    • Jenuwein T, Laible G, Dorn R, and Reuter G. SET domain proteins modulate chromatin domains in eu- and heterochromatin. Cell Mol Life Sci 54: 80-93, 1998. (Pubitemid 28048252)
    • (1998) Cellular and Molecular Life Sciences , vol.54 , Issue.1 , pp. 80-93
    • Jenuwein, T.1    Laible, G.2    Dorn, R.3    Reuter, G.4
  • 142
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, and Yao TP. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115: 727-738, 2003. (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 143
    • 72049121173 scopus 로고    scopus 로고
    • DNA methylation by dimethyl sulfoxide and methionine sulfoxide triggered by hydroxyl radical and implications for epigenetic modifications
    • Kawai K, Li YS, Song MF, and Kasai H. DNA methylation by dimethyl sulfoxide and methionine sulfoxide triggered by hydroxyl radical and implications for epigenetic modifications. Bioorg Med Chem Lett 20: 260-265, 2010.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 260-265
    • Kawai, K.1    Li, Y.S.2    Song, M.F.3    Kasai, H.4
  • 144
    • 34848888039 scopus 로고    scopus 로고
    • Role of transmethylation reactions in alcoholic liver disease
    • Kharbanda KK. Role of transmethylation reactions in alcoholic liver disease. World J Gastroenterol 13: 4947-4954, 2007. (Pubitemid 47496826)
    • (2007) World Journal of Gastroenterology , vol.13 , Issue.37 , pp. 4947-4954
    • Kharbanda, K.K.1
  • 146
    • 24044474409 scopus 로고    scopus 로고
    • Histone H3 modifications in rat hepatic stellate cells by ethanol
    • DOI 10.1093/alcalc/agh170
    • Kim JS and Shukla SD. Histone h3 modifications in rat hepatic stellate cells by ethanol. Alcohol Alcohol 40: 367-372, 2005. (Pubitemid 41222394)
    • (2005) Alcohol and Alcoholism , vol.40 , Issue.5 , pp. 367-372
    • Kim, J.-S.1    Shukla, S.D.2
  • 147
    • 33644978395 scopus 로고    scopus 로고
    • Acute in vivo effect of ethanol (binge drinking) on histone H3 modifications in rat tissues
    • Kim JS and Shukla SD. Acute in vivo effect of ethanol (binge drinking) on histone H3 modifications in rat tissues. Alcohol Alcohol 41: 126-132, 2006.
    • (2006) Alcohol Alcohol , vol.41 , pp. 126-132
    • Kim, J.S.1    Shukla, S.D.2
  • 148
    • 33746930794 scopus 로고    scopus 로고
    • Succinate dehydrogenase and fumarate hydratase: Linking mitochondrial dysfunction and cancer
    • DOI 10.1038/sj.onc.1209594, PII 1209594
    • King A, Selak MA, and Gottlieb E. Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer. Oncogene 25: 4675-4682, 2006. (Pubitemid 44187617)
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4675-4682
    • King, A.1    Selak, M.A.2    Gottlieb, E.3
  • 149
    • 72249115358 scopus 로고    scopus 로고
    • Niacin status impacts chromatin structure
    • Kirkland JB. Niacin status impacts chromatin structure. J Nutr 139: 2397-2401, 2009.
    • (2009) J Nutr , vol.139 , pp. 2397-2401
    • Kirkland, J.B.1
  • 150
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles HJ, Raval RR, Harris AL, and Ratcliffe PJ. Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res 63: 1764-1768, 2003. (Pubitemid 36460834)
    • (2003) Cancer Research , vol.63 , Issue.8 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 151
    • 33744475759 scopus 로고    scopus 로고
    • Control of AIF-mediated cell death by the functional interplay of SIRT1 and PARP-1 in response to DNA damage
    • Kolthur-Seetharam U, Dantzer F, McBurney MW, de Murcia G, and Sassone-Corsi P. Control of AIF-mediated cell death by the functional interplay of SIRT1 and PARP-1 in response to DNA damage. Cell Cycle 5: 873-877, 2006. (Pubitemid 44145583)
    • (2006) Cell Cycle , vol.5 , Issue.8 , pp. 873-877
    • Kolthur-Seetharam, U.1    Dantzer, F.2    McBurney, M.W.3    De Murcia, G.4    Sassone-Corsi, P.5
  • 152
    • 77949924512 scopus 로고    scopus 로고
    • IDH1 and IDH2 mutations in gliomas and the associated induction of hypoxia-inducible factor and production of 2-hydroxyglutarate
    • Komotar RJ, Starke RM, Sisti MB, and Connolly ES. IDH1 and IDH2 mutations in gliomas and the associated induction of hypoxia-inducible factor and production of 2-hydroxyglutarate. Neurosurgery 66: N20-N21, 2010.
    • (2010) Neurosurgery , vol.66
    • Komotar, R.J.1    Starke, R.M.2    Sisti, M.B.3    Connolly, E.S.4
  • 154
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • DOI 10.1016/j.cell.2007.02.005, PII S0092867407001845
    • Kouzarides T. Chromatin modifications and their function. Cell 128: 693-705, 2007. (Pubitemid 46273577)
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 156
    • 77952212771 scopus 로고    scopus 로고
    • RNA traffic control of chromatin complexes
    • Koziol MJ and Rinn JL. RNA traffic control of chromatin complexes. Curr Opin Genet Dev 20: 142-148, 2010.
    • (2010) Curr Opin Genet Dev , vol.20 , pp. 142-148
    • Koziol, M.J.1    Rinn, J.L.2
  • 157
    • 66149123748 scopus 로고    scopus 로고
    • The nuclear DNA base 5-hydroxymethylcytosine is present in purkinje neurons and the brain
    • Kriaucionis S and Heintz N. The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain. Science 324: 929-930, 2009.
    • (2009) Science , vol.324 , pp. 929-930
    • Kriaucionis, S.1    Heintz, N.2
  • 160
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • DOI 10.1002/(SICI)1521-1878(199808)20:8<615::AID-BIES4>3.0.CO;2-H
    • Kuo MH and Allis CD. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20: 615-626, 1998. (Pubitemid 28422221)
    • (1998) BioEssays , vol.20 , Issue.8 , pp. 615-626
    • Kuo, M.-H.1    Allis, C.D.2
  • 161
    • 77955630249 scopus 로고    scopus 로고
    • MicroRNA expression in human retinal pigment epithelial (ARPE-19) cells: Increased expression of microRNA-9 by N-(4-hydroxyphenyl)retinamide
    • Kutty RK, Samuel W, Jaworski C, Duncan T, Nagineni CN, Raghavachari N, Wiggert B, and Redmond TM. MicroRNA expression in human retinal pigment epithelial (ARPE-19) cells: increased expression of microRNA-9 by N-(4-hydroxyphenyl)retinamide. Mol Vis 16: 1475-1486, 2010.
    • (2010) Mol Vis , vol.16 , pp. 1475-1486
    • Kutty, R.K.1    Samuel, W.2    Jaworski, C.3    Duncan, T.4    Nagineni, C.N.5    Raghavachari, N.6    Wiggert, B.7    Redmond, T.M.8
  • 162
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • DOI 10.1038/35065132
    • Lachner M, O'Carroll D, Rea S, Mechtler K, and Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410: 116-120, 2001. (Pubitemid 32225847)
    • (2001) Nature , vol.410 , Issue.6824 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 163
    • 45849131304 scopus 로고    scopus 로고
    • Regulation of 14-3-3 sigma expression in human thyroid carcinoma is epigenetically regulated by aberrant cytosine methylation
    • Lal G, Padmanabha L, Provenzano M, Fitzgerald M, Weydert J, and Domann FE. Regulation of 14-3-3 sigma expression in human thyroid carcinoma is epigenetically regulated by aberrant cytosine methylation. Cancer Lett 267: 165-174, 2008.
    • (2008) Cancer Lett , vol.267 , pp. 165-174
    • Lal, G.1    Padmanabha, L.2    Provenzano, M.3    Fitzgerald, M.4    Weydert, J.5    Domann, F.E.6
  • 165
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
    • Landry J, Slama JT, and Sternglanz R. Role of NAD(+) in the deacetylase activity of the SIR2-like proteins. Biochem Biophys Res Commun 278: 685-690, 2000.
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 685-690
    • Landry, J.1    Slama, J.T.2    Sternglanz, R.3
  • 170
    • 67249116835 scopus 로고    scopus 로고
    • Targeting histone deacetylases for the treatment of disease
    • Lawless MW, Norris S, O'Byrne KJ, and Gray SG. Targeting histone deacetylases for the treatment of disease. J Cell Mol Med 13: 826-852, 2009.
    • (2009) J Cell Mol Med , vol.13 , pp. 826-852
    • Lawless, M.W.1    Norris, S.2    O'Byrne, K.J.3    Gray, S.G.4
  • 171
    • 72649087731 scopus 로고    scopus 로고
    • Functions and evolution of selenoprotein methionine sulfoxide reductases
    • Lee BC, Dikiy A, Kim HY, and Gladyshev VN. Functions and evolution of selenoprotein methionine sulfoxide reductases. Biochim Biophys Acta 1790: 1471-1477, 2009.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1471-1477
    • Lee, B.C.1    Dikiy, A.2    Kim, H.Y.3    Gladyshev, V.N.4
  • 172
    • 66349101408 scopus 로고    scopus 로고
    • X chromosome inactivation sparked by non-coding RNAs
    • Leeb M, Steffen PA, and Wutz A. X chromosome inactivation sparked by non-coding RNAs. RNA Biol 6: 94-99, 2009.
    • (2009) RNA Biol , vol.6 , pp. 94-99
    • Leeb, M.1    Steffen, P.A.2    Wutz, A.3
  • 173
    • 35148844229 scopus 로고    scopus 로고
    • Identification of MSRA gene on chromosome 8p as a candidate metastasis suppressor for human hepatitis B virus-positive hepatocellular carcinoma
    • Lei KF, Wang YF, Zhu XQ, Lu PC, Sun BS, Jia HL, Ren N, Ye QH, Sun HC, Wang L, et al. Identification of MSRA gene on chromosome 8p as a candidate metastasis suppressor for human hepatitis B virus-positive hepatocellular carcinoma. BMC Cancer 7: 172, 2007.
    • (2007) BMC Cancer , vol.7 , pp. 172
    • Lei, K.F.1    Wang, Y.F.2    Zhu, X.Q.3    Lu, P.C.4    Sun, B.S.5    Jia, H.L.6    Ren, N.7    Ye, Q.H.8    Sun, H.C.9    Wang, L.10
  • 174
    • 0030065081 scopus 로고    scopus 로고
    • Methyl-donor deficiency due to chemically induced glutathione depletion
    • Lertratanangkoon K, Orkiszewski RS, and Scimeca JM. Methyl-donor deficiency due to chemically induced glutathione depletion. Cancer Res 56: 995-1005, 1996. (Pubitemid 26065392)
    • (1996) Cancer Research , vol.56 , Issue.5 , pp. 995-1005
    • Lertratanangkoon, K.1    Orkiszewski, R.S.2    Scimeca, J.M.3
  • 176
    • 0030696188 scopus 로고    scopus 로고
    • Alterations of DNA methylation by glutathione depletion
    • DOI 10.1016/S0304-3835(97)00300-5, PII S0304383597003005
    • Lertratanangkoon K, Wu CJ, Savaraj N, and Thomas ML. Alterations of DNA methylation by glutathione depletion. Cancer Lett 120: 149-156, 1997. (Pubitemid 27496811)
    • (1997) Cancer Letters , vol.120 , Issue.2 , pp. 149-156
    • Lertratanangkoon, K.1    Wu, C.J.2    Savaraj, N.3    Thomas, M.L.4
  • 177
    • 67349203545 scopus 로고    scopus 로고
    • Losing and finding a way at C: New promise for pharmacologic ascorbate in cancer treatment
    • Levine M, Espey MG, and Chen Q. Losing and finding a way at C: new promise for pharmacologic ascorbate in cancer treatment. Free Radic Biol Med 47: 27-29, 2009.
    • (2009) Free Radic Biol Med , vol.47 , pp. 27-29
    • Levine, M.1    Espey, M.G.2    Chen, Q.3
  • 178
    • 67650135475 scopus 로고    scopus 로고
    • Alterations of histone modifications by cobalt compounds
    • Li Q, Ke Q, and Costa M. Alterations of histone modifications by cobalt compounds. Carcinogenesis 30: 1243-1251, 2009.
    • (2009) Carcinogenesis , vol.30 , pp. 1243-1251
    • Li, Q.1    Ke, Q.2    Costa, M.3
  • 180
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in saccharomyces cerevisiae
    • Lin SJ, Defossez PA, and Guarente L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289: 2126-2128, 2000.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 181
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • DOI 10.1016/S0955-0674(03)00006-1
    • Lin SJ and Guarente L. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr Opin Cell Biol 15: 241-246, 2003. (Pubitemid 36332200)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.2 , pp. 241-246
    • Lin, S.-J.1    Guarente, L.2
  • 183
    • 65249115670 scopus 로고    scopus 로고
    • Involvement of MicroRNAs in hydrogen peroxide-mediated gene regulation and cellular injury response in vascular smooth muscle cells
    • Lin Y, Liu X, Cheng Y, Yang J, Huo Y, and Zhang C. Involvement of MicroRNAs in hydrogen peroxide-mediated gene regulation and cellular injury response in vascular smooth muscle cells. J Biol Chem 284: 7903-7913, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 7903-7913
    • Lin, Y.1    Liu, X.2    Cheng, Y.3    Yang, J.4    Huo, Y.5    Zhang, C.6
  • 184
    • 61449158984 scopus 로고    scopus 로고
    • Histone deacetylase 11 regulates oligodendrocyte-specific gene expression and cell development in OL-1 oligodendroglia cells
    • Liu H, Hu Q, D'Ercole AJ, and Ye P. Histone deacetylase 11 regulates oligodendrocyte-specific gene expression and cell development in OL-1 oligodendroglia cells. Glia 57: 1-12, 2009.
    • (2009) Glia , vol.57 , pp. 1-12
    • Liu, H.1    Hu, Q.2    D'Ercole, A.J.3    Ye, P.4
  • 187
    • 56249120580 scopus 로고    scopus 로고
    • Proline oxidase, a p53-induced gene, targets COX-2/PGE2 signaling to induce apoptosis and inhibit tumor growth in colorectal cancers
    • Liu Y, Borchert GL, Surazynski A, and Phang JM. Proline oxidase, a p53-induced gene, targets COX-2/PGE2 signaling to induce apoptosis and inhibit tumor growth in colorectal cancers. Oncogene 27: 6729-6737, 2008.
    • (2008) Oncogene , vol.27 , pp. 6729-6737
    • Liu, Y.1    Borchert, G.L.2    Surazynski, A.3    Phang, J.M.4
  • 188
    • 0033067354 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis: Current concepts and controversies
    • Lu SC. Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J 13: 1169-1183, 1999. (Pubitemid 29300363)
    • (1999) FASEB Journal , vol.13 , Issue.10 , pp. 1169-1183
    • Lu, S.C.1
  • 189
    • 65049089113 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Lu SC. Regulation of glutathione synthesis. Mol Aspects Med 30: 42-59, 2009.
    • (2009) Mol Aspects Med , vol.30 , pp. 42-59
    • Lu, S.C.1
  • 190
    • 34548177451 scopus 로고    scopus 로고
    • Induction of specific micro RNA (miRNA) species by ROS-generating metal sulfates in primary human brain cells
    • DOI 10.1016/j.jinorgbio.2007.06.004, PII S0162013407001298
    • Lukiw WJ and Pogue AI. Induction of specific micro RNA (miRNA) species by ROS-generating metal sulfates in primary human brain cells. J Inorg Biochem 101: 1265-1269, 2007. (Pubitemid 47313522)
    • (2007) Journal of Inorganic Biochemistry , vol.101 , Issue.9 SPEC. ISS. , pp. 1265-1269
    • Lukiw, W.J.1    Pogue, A.I.2
  • 192
    • 77950841042 scopus 로고    scopus 로고
    • Transcriptional gene silencing through epigenetic changes mediated by non-coding RNAs
    • Malecova B and Morris KV. Transcriptional gene silencing through epigenetic changes mediated by non-coding RNAs. Curr Opin Mol Ther 12: 214-222, 2010.
    • (2010) Curr Opin Mol Ther , vol.12 , pp. 214-222
    • Malecova, B.1    Morris, K.V.2
  • 193
    • 77952536841 scopus 로고    scopus 로고
    • IDH1 and IDH2 gene mutations identify novel molecular subsets within de novo cytogenetically normal acute myeloid leukemia: A cancer and leukemia group B study
    • Marcucci G, Maharry K, Wu YZ, Radmacher MD, Mrozek K, Margeson D, Holland KB, Whitman SP, Becker H, Schwind S, et al. IDH1 and IDH2 gene mutations identify novel molecular subsets within De Novo cytogenetically normal acute myeloid leukemia: a cancer and leukemia group B study. J Clin Oncol 28: 2348-2355, 2010.
    • (2010) J Clin Oncol , vol.28 , pp. 2348-2355
    • Marcucci, G.1    Maharry, K.2    Wu, Y.Z.3    Radmacher, M.D.4    Mrozek, K.5    Margeson, D.6    Holland, K.B.7    Whitman, S.P.8    Becker, H.9    Schwind, S.10
  • 194
    • 0035313803 scopus 로고    scopus 로고
    • Histone acetyltransferases: Function, structure, and catalysis
    • DOI 10.1016/S0959-437X(00)00173-8
    • Marmorstein R and Roth SY. Histone acetyltransferases: function, structure, and catalysis. Curr Opin Genet Dev 11: 155-161, 2001. (Pubitemid 32209199)
    • (2001) Current Opinion in Genetics and Development , vol.11 , Issue.2 , pp. 155-161
    • Marmorstein, R.1    Roth, S.Y.2
  • 195
    • 34547919621 scopus 로고    scopus 로고
    • Class IIa histone deacetylases: Regulating the regulators
    • DOI 10.1038/sj.onc.1210613, PII 1210613
    • Martin M, Kettmann R, and Dequiedt F. Class IIa histone deacetylases: regulating the regulators. Oncogene 26: 5450-5467, 2007. (Pubitemid 47255927)
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5450-5467
    • Martin, M.1    Kettmann, R.2    Dequiedt, F.3
  • 196
    • 68949096744 scopus 로고    scopus 로고
    • Epigenetic differences in cortical neurons from a pair of monozygotic twins discordant for alzheimer's disease
    • Mastroeni D, McKee A, Grover A, Rogers J, and Coleman PD. Epigenetic differences in cortical neurons from a pair of monozygotic twins discordant for Alzheimer's disease. PLoS ONE 4: e6617, 2009.
    • (2009) PLoS ONE , vol.4
    • Mastroeni, D.1    McKee, A.2    Grover, A.3    Rogers, J.4    Coleman, P.D.5
  • 198
    • 3142523739 scopus 로고    scopus 로고
    • HIF-1: An oxygen and metal responsive transcription factor
    • Maxwell P and Salnikow K. HIF-1: an oxygen and metal responsive transcription factor. Cancer Biol Ther 3: 29-35, 2004. (Pubitemid 41342413)
    • (2004) Cancer Biology and Therapy , vol.3 , Issue.1 , pp. 29-35
    • Maxwell, P.1    Salnikow, K.2
  • 199
    • 40849086158 scopus 로고    scopus 로고
    • Identification of a p53-response element in the promoter of the proline oxidase gene
    • Maxwell SA and Kochevar GJ. Identification of a p53-response element in the promoter of the proline oxidase gene. Biochem Biophys Res Commun 369: 308-313, 2008.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 308-313
    • Maxwell, S.A.1    Kochevar, G.J.2
  • 201
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. Glutathione metabolism and its selective modification. J Biol Chem 263: 17205-17208, 1988. (Pubitemid 19029311)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.33 , pp. 17205-17208
    • Meister, A.1
  • 204
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1α by inhibition of prolyl hydroxylases
    • DOI 10.1091/mbc.E02-12-0791
    • Metzen E, Zhou J, Jelkmann W, Fandrey J, and Brune B. Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases. Mol Biol Cell 14: 3470-3481, 2003. (Pubitemid 37013142)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.8 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 205
    • 0033229699 scopus 로고    scopus 로고
    • Regulation of intracellular iron metabolism in human erythroid precursors by internalized extracellular ferritin
    • Meyron-Holtz EG, Vaisman B, Cabantchik ZI, Fibach E, Rouault TA, Hershko C, and Konijn AM. Regulation of intracellular iron metabolism in human erythroid precursors by internalized extracellular ferritin. Blood 94: 3205-3211, 1999. (Pubitemid 29512730)
    • (1999) Blood , vol.94 , Issue.9 , pp. 3205-3211
    • Meyron-Holtz, E.G.1    Vaisman, B.2    Cabantchik, Z.I.3    Fibach, E.4    Rouault, T.A.5    Hershko, C.6    Konijn, A.M.7
  • 206
    • 77953392974 scopus 로고    scopus 로고
    • Ascorbate inhibition of angiogenesis in aortic rings ex vivo and subcutaneous matrigel plugs in vivo
    • Mikirova NA, Casciari JJ, and Riordan NH. Ascorbate inhibition of angiogenesis in aortic rings ex vivo and subcutaneous Matrigel plugs in vivo. J Angiogenes Res 2: 2, 2010.
    • (2010) J Angiogenes Res , vol.2 , pp. 2
    • Mikirova, N.A.1    Casciari, J.J.2    Riordan, N.H.3
  • 207
    • 77954324820 scopus 로고    scopus 로고
    • Epigenetics. The seductive allure of behavioral epigenetics
    • Miller G. Epigenetics. The seductive allure of behavioral epigenetics. Science 329: 24-27, 2010.
    • (2010) Science , vol.329 , pp. 24-27
    • Miller, G.1
  • 208
    • 34548745142 scopus 로고    scopus 로고
    • Insights in the regulation of cholesterol 7α-hydroxylase gene reveal a target for modulating bile acid synthesis
    • DOI 10.1002/hep.21819
    • Mitro N, Godio C, De Fabiani E, Scotti E, Galmozzi A, Gilardi F, Caruso D, Vigil Chacon AB, and Crestani M. Insights in the regulation of cholesterol 7alpha-hydroxylase gene reveal a target for modulating bile acid synthesis. Hepatology 46: 885-897, 2007. (Pubitemid 47436134)
    • (2007) Hepatology , vol.46 , Issue.3 , pp. 885-897
    • Mitro, N.1    Godio, C.2    De Fabiani, E.3    Scotti, E.4    Galmozzi, A.5    Gilardi, F.6    Caruso, D.7    Chacon, A.B.V.8    Crestani, M.9
  • 210
    • 10044241543 scopus 로고    scopus 로고
    • Oxidative stress and cigarette smoke alter chromatin remodeling but differentially regulate NF-κB activation and proinflammatory cytokine release in alveolar epithelial cells
    • DOI 10.1096/fj.04-1506fje
    • Moodie FM, Marwick JA, Anderson CS, Szulakowski P, Biswas SK, Bauter MR, Kilty I, and Rahman I. Oxidative stress and cigarette smoke alter chromatin remodeling but differentially regulate NF-kappaB activation and proinflammatory cytokine release in alveolar epithelial cells. FASEB J 18: 1897-1899, 2004. (Pubitemid 39602276)
    • (2004) FASEB Journal , vol.18 , Issue.15 , pp. 1897-1899
    • Moodie, F.M.1    Marwick, J.A.2    Anderson, C.S.3    Szulakowski, P.4    Biswas, S.K.5    Bauter, M.R.6    Kilty, I.7    Rahman, I.8
  • 212
    • 77954758157 scopus 로고    scopus 로고
    • Polycomb group protein-mediated repression of transcription
    • Morey L and Helin K. Polycomb group protein-mediated repression of transcription. Trends Biochem Sci 35: 323-332, 2010.
    • (2010) Trends Biochem Sci , vol.35 , pp. 323-332
    • Morey, L.1    Helin, K.2
  • 214
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: Biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast N and Shi Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu Rev Biochem 79: 155-179, 2010.
    • (2010) Annu Rev Biochem , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 215
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • Muckenthaler MU, Galy B, and Hentze MW. Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network. Annu Rev Nutr 28: 197-213, 2008.
    • (2008) Annu Rev Nutr , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 216
    • 28644443925 scopus 로고    scopus 로고
    • Iron regulatory protein 1 as a sensor of reactive oxygen species
    • HNE and Further Lipid Peroxidation Products
    • Mueller S. Iron regulatory protein 1 as a sensor of reactive oxygen species. Biofactors 24: 171-181, 2005. (Pubitemid 41750540)
    • (2005) BioFactors , vol.24 , Issue.1-4 , pp. 171-181
    • Mueller, S.1
  • 218
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • DOI 10.1126/science.1060118
    • Nakayama J, Rice JC, Strahl BD, Allis CD, and Grewal SI. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292: 110-113, 2001. (Pubitemid 32289138)
    • (2001) Science , vol.292 , Issue.5514 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.S.5
  • 222
    • 34250359929 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, macroH2A, and contributes to silencing of the inactive X chromosome
    • DOI 10.1074/jbc.M610502200
    • Nusinow DA, Hernandez-Munoz I, Fazzio TG, Shah GM, Kraus WL, and Panning B. Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome. J Biol Chem 282: 12851-12859, 2007. (Pubitemid 47100579)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12851-12859
    • Nusinow, D.A.1    Hernandez-Munoz, I.2    Fazzio, T.G.3    Shah, G.M.4    Kraus, W.L.5    Panning, B.6
  • 223
    • 0031045306 scopus 로고    scopus 로고
    • Glycolytic pathway, redox state of NAD(P)-couples and energy metabolism in lens in galactose-fed rats: Effect of an aldose reductase inhibitor
    • DOI 10.1076/ceyr.16.1.34.5113
    • Obrosova I, Faller A, Burgan J, Ostrow E, and Williamson JR. Glycolytic pathway, redox state of NAD(P)-couples and energy metabolism in lens in galactose-fed rats: effect of an aldose reductase inhibitor. Curr Eye Res 16: 34-43, 1997. (Pubitemid 27085150)
    • (1997) Current Eye Research , vol.16 , Issue.1 , pp. 34-43
    • Obrosova, I.1    Faller, A.2    Burgan, J.3    Ostrow, E.4    Williamson, J.R.5
  • 224
    • 0033010213 scopus 로고    scopus 로고
    • Effect of dietary taurine supplementation on GSH and NAD(P)-redox status, lipid peroxidation, and energy metabolism in diabetic precataractous lens
    • Obrosova IG and Stevens MJ. Effect of dietary taurine supplementation on GSH and NAD(P)-redox status, lipid peroxidation, and energy metabolism in diabetic precataractous lens. Invest Ophthalmol Vis Sci 40: 680-688, 1999. (Pubitemid 29109446)
    • (1999) Investigative Ophthalmology and Visual Science , vol.40 , Issue.3 , pp. 680-688
    • Obrosova, I.G.1    Stevens, M.J.2
  • 225
    • 64949179184 scopus 로고    scopus 로고
    • Highdose vitamin C (ascorbic acid) therapy in the treatment of patients with advanced cancer
    • Ohno S, Ohno Y, Suzuki N, Soma G, and Inoue M. Highdose vitamin C (ascorbic acid) therapy in the treatment of patients with advanced cancer. Anticancer Res 29: 809-815, 2009.
    • (2009) Anticancer Res , vol.29 , pp. 809-815
    • Ohno, S.1    Ohno, Y.2    Suzuki, N.3    Soma, G.4    Inoue, M.5
  • 226
    • 0035146957 scopus 로고    scopus 로고
    • PFK-2/FBPase-2: Maker and breaker of the essential biofactor fructose-2,6-bisphosphate
    • DOI 10.1016/S0968-0004(00)01699-6, PII S0968000400016996
    • Okar DA, Manzano A, Navarro-Sabate A, Riera L, Bartrons R, and Lange AJ. PFK-2/FBPase-2: maker and breaker of the essential biofactor fructose-2,6-bisphosphate. Trends Biochem Sci 26: 30-35, 2001. (Pubitemid 32124707)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.1 , pp. 30-35
    • Okar, D.A.1    Lange, A.J.2    Manzano, A.3    Navarro-Sabate, A.4    Riera, L.5    Bartrons, R.6
  • 227
    • 45449114804 scopus 로고    scopus 로고
    • The colorful history of active DNA demethylation
    • DOI 10.1016/j.cell.2008.06.009, PII S0092867408007617
    • Ooi SK and Bestor TH. The colorful history of active DNA demethylation. Cell 133: 1145-1148, 2008. (Pubitemid 351852922)
    • (2008) Cell , vol.133 , Issue.7 , pp. 1145-1148
    • Ooi, S.K.T.1    Bestor, T.H.2
  • 228
    • 77956058729 scopus 로고    scopus 로고
    • Epigenetics and cardiovascular disease
    • Ordovas JM and Smith CE. Epigenetics and cardiovascular disease. Nat Rev Cardiol 7: 510-519, 2010.
    • (2010) Nat Rev Cardiol , vol.7 , pp. 510-519
    • Ordovas, J.M.1    Smith, C.E.2
  • 230
    • 0014455894 scopus 로고
    • Binding of ADP-ribose polymer with histone
    • Otake H, Miwa M, Fujimura S, and Sugimura T. Binding of ADP-ribose polymer with histone. J Biochem 65: 145-146, 1969.
    • (1969) J Biochem , vol.65 , pp. 145-146
    • Otake, H.1    Miwa, M.2    Fujimura, S.3    Sugimura, T.4
  • 231
    • 33751241119 scopus 로고    scopus 로고
    • Histone H3 lysine 56 acetylation: A new twist in the chromosome cycle
    • Ozdemir A, Masumoto H, Fitzjohn P, Verreault A, and Logie C. Histone H3 lysine 56 acetylation: a new twist in the chromosome cycle. Cell Cycle 5: 2602-2608, 2006. (Pubitemid 44785804)
    • (2006) Cell Cycle , vol.5 , Issue.22 , pp. 2602-2608
    • Ozdemir, A.1    Masumoto, H.2    Fitzjohn, P.3    Verreault, A.4    Logie, C.5
  • 232
    • 33847050240 scopus 로고    scopus 로고
    • Non-heme dioxygenases: Cellular sensors and regulators jelly rolled into one?
    • Ozer A and Bruick RK. Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? Nat Chem Biol 3: 144-153, 2007.
    • (2007) Nat Chem Biol , vol.3 , pp. 144-153
    • Ozer, A.1    Bruick, R.K.2
  • 233
    • 0036058194 scopus 로고    scopus 로고
    • Medulloblastoma in a child with the metabolic disease L-2-hydroxyglutaric aciduria
    • DOI 10.1159/000065097
    • Ozisik PA, Akalan N, Palaoglu S, and Topcu M. Medulloblastoma in a child with the metabolic disease L-2-hydroxyglutaric aciduria. Pediatr Neurosurg 37: 22-26, 2002. (Pubitemid 34920739)
    • (2002) Pediatric Neurosurgery , vol.37 , Issue.1 , pp. 22-26
    • Ozisik, P.A.1    Akalan, N.2    Palaoglu, S.3    Topcu, M.4
  • 234
    • 0015912073 scopus 로고
    • Enzymatic demethylation of calf thymus histones
    • Paik WK and Kim S. Enzymatic demethylation of calf thymus histones. Biochem Biophys Res Commun 51: 781-788, 1973.
    • (1973) Biochem Biophys Res Commun , vol.51 , pp. 781-788
    • Paik, W.K.1    Kim, S.2
  • 235
    • 34548527262 scopus 로고    scopus 로고
    • Distinct methylation patterns in histone H3 at Lys-4 and Lys-9 correlate with up- & down-regulation of genes by ethanol in hepatocytes
    • DOI 10.1016/j.lfs.2007.07.030, PII S0024320507005322
    • Pal-Bhadra M, Bhadra U, Jackson DE, Mamatha L, Park PH and Shukla SD. Distinct methylation patterns in histone H3 at Lys-4 and Lys-9 correlate with up- & down-regulation of genes by ethanol in hepatocytes. Life Sci 81: 979-987, 2007. (Pubitemid 47384784)
    • (2007) Life Sciences , vol.81 , Issue.12 , pp. 979-987
    • Pal-Bhadra, M.1    Bhadra, U.2    Jackson, D.E.3    Mamatha, L.4    Park, P.-H.5    Shukla, S.D.6
  • 236
    • 33846630894 scopus 로고    scopus 로고
    • Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro
    • DOI 10.1128/MCB.01223-06
    • Pan Y, Mansfield KD, Bertozzi CC, Rudenko V, Chan DA, Giaccia AJ, and Simon MC. Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro. Mol Cell Biol 27: 912-925, 2007. (Pubitemid 46174556)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.3 , pp. 912-925
    • Pan, Y.1    Mansfield, K.D.2    Bertozzi, C.C.3    Rudenko, V.4    Chan, D.A.5    Giaccia, A.J.6    Simon, M.C.7
  • 237
    • 33644850483 scopus 로고    scopus 로고
    • Proline oxidase, a proapoptotic gene, is induced by troglitazone: Evidence for both peroxisome proliferator-activated receptor γ-dependent and -independent mechanisms
    • DOI 10.1074/jbc.M507867200
    • Pandhare J, Cooper SK, and Phang JM. Proline oxidase, a proapoptotic gene, is induced by troglitazone: evidence for both peroxisome proliferator-activated receptor gamma-dependent and -independent mechanisms. J Biol Chem 281: 2044-2052, 2006. (Pubitemid 43845792)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 2044-2052
    • Pandhare, J.1    Cooper, S.K.2    Phang, J.M.3
  • 238
    • 77954573304 scopus 로고    scopus 로고
    • IDH1 and IDH2 mutation analysis in chronic- and blast-phase myeloproliferative neoplasms
    • Pardanani A, Lasho TL, Finke CM, Mai M, McClure RF, and Tefferi A. IDH1 and IDH2 mutation analysis in chronic- and blast-phase myeloproliferative neoplasms. Leukemia 24: 1146-1151, 2010.
    • (2010) Leukemia , vol.24 , pp. 1146-1151
    • Pardanani, A.1    Lasho, T.L.2    Finke, C.M.3    Mai, M.4    McClure, R.F.5    Tefferi, A.6
  • 240
    • 70349312354 scopus 로고    scopus 로고
    • ChIP-seq: Advantages and challenges of a maturing technology
    • Park PJ. ChIP-seq: advantages and challenges of a maturing technology. Nat Rev Genet 10: 669-680, 2009.
    • (2009) Nat Rev Genet , vol.10 , pp. 669-680
    • Park, P.J.1
  • 241
    • 66849143816 scopus 로고    scopus 로고
    • SDH mutations in tumorigenesis and inherited endocrine tumours: Lesson from the phaeochromocytoma-paraganglioma syndromes
    • Pasini B and Stratakis CA. SDH mutations in tumorigenesis and inherited endocrine tumours: lesson from the phaeochromocytoma-paraganglioma syndromes. J Intern Med 266: 19-42, 2009.
    • (2009) J Intern Med , vol.266 , pp. 19-42
    • Pasini, B.1    Stratakis, C.A.2
  • 243
    • 33646056352 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and cell senescence: Cause or consequence?
    • Passos JF, von Zglinicki T, and Saretzki G. Mitochondrial dysfunction and cell senescence: cause or consequence? Rejuvenation Res 9: 64-68, 2006.
    • (2006) Rejuvenation Res , vol.9 , pp. 64-68
    • Passos, J.F.1    Von Zglinicki, T.2    Saretzki, G.3
  • 244
    • 61849086820 scopus 로고    scopus 로고
    • The resistance of electrontransport chain fe-S clusters to oxidative damage during the reaction of peroxynitrite with mitochondrial complex II and rat-heart pericardium
    • Pearce LL, Martinez-Bosch S, Manzano EL, Winnica DE, Epperly MW, and Peterson J. The resistance of electrontransport chain Fe-S clusters to oxidative damage during the reaction of peroxynitrite with mitochondrial complex II and rat-heart pericardium. Nitric Oxide 20: 135-142, 2009.
    • (2009) Nitric Oxide , vol.20 , pp. 135-142
    • Pearce, L.L.1    Martinez-Bosch, S.2    Manzano, E.L.3    Winnica, D.E.4    Epperly, M.W.5    Peterson, J.6
  • 246
    • 53849096017 scopus 로고    scopus 로고
    • The metabolism of proline, a stress substrate, modulates carcinogenic pathways
    • Phang JM, Donald SP, Pandhare J, and Liu Y. The metabolism of proline, a stress substrate, modulates carcinogenic pathways. Amino Acids 35: 681-690, 2008.
    • (2008) Amino Acids , vol.35 , pp. 681-690
    • Phang, J.M.1    Donald, S.P.2    Pandhare, J.3    Liu, Y.4
  • 247
    • 0032546922 scopus 로고    scopus 로고
    • Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells
    • DOI 10.1074/jbc.273.25.15382
    • Picard V, Epsztejn S, Santambrogio P, Cabantchik ZI, and Beaumont C. Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells. J Biol Chem 273: 15382-15386, 1998. (Pubitemid 28298142)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15382-15386
    • Picard, V.1    Epsztejn, S.2    Santambrogio, P.3    Cabantchik, Z.I.4    Beaumont, C.5
  • 248
    • 30044443515 scopus 로고    scopus 로고
    • + depletion and reduced Sir2α deacetylase activity
    • DOI 10.1074/jbc.M506162200
    • Pillai JB, Isbatan A, Imai S, and Gupta MP. Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sir2alpha deacetylase activity. J Biol Chem 280: 43121-43130, 2005. (Pubitemid 43049278)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.52 , pp. 43121-43130
    • Pillai, J.B.1    Isbatan, A.2    Imai, S.-I.3    Gupta, M.P.4
  • 249
    • 33746880713 scopus 로고    scopus 로고
    • Preadaptation to efficient respiratory maintenance is essential both for maximal longevity and the retention of replicative potential in chronologically ageing yeast
    • DOI 10.1016/j.mad.2006.05.004, PII S0047637406001436
    • Piper PW, Harris NL, and MacLean M. Preadaptation to efficient respiratory maintenance is essential both for maximal longevity and the retention of replicative potential in chronologically ageing yeast. Mech Ageing Dev 127: 733-740, 2006. (Pubitemid 44188818)
    • (2006) Mechanisms of Ageing and Development , vol.127 , Issue.9 , pp. 733-740
    • Piper, P.W.1    Harris, N.L.2    MacLean, M.3
  • 251
    • 0037974679 scopus 로고    scopus 로고
    • Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: Modulation of enzyme activities by MnSOD
    • Powell CS and Jackson RM. Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD. Am J Physiol Lung Cell Mol Physiol 285: L189-L198, 2003. (Pubitemid 36736482)
    • (2003) American Journal of Physiology - Lung Cellular and Molecular Physiology , vol.285
    • Powell, C.S.1    Jackson, R.M.2
  • 253
    • 0030044251 scopus 로고    scopus 로고
    • Differential sensitivity of zinc finger transcription factors MTF-1, Sp1 and krox-20 to CpG methylation of their binding sites
    • Radtke F, Hug M, Georgiev O, Matsuo K, and Schaffner W. Differential sensitivity of zinc finger transcription factors MTF-1, Sp1 and Krox-20 to CpG methylation of their binding sites. Biol Chem Hoppe Seyler 377: 47-56, 1996. (Pubitemid 26056833)
    • (1996) Biological Chemistry Hoppe-Seyler , vol.377 , Issue.1 , pp. 47-56
    • Radtke, F.1    Hug, M.2    Georgiev, O.3    Matsuo, K.4    Schaffner, W.5
  • 254
    • 33750867930 scopus 로고    scopus 로고
    • Metabolic effects of aldose reductase inhibition during low-flow ischemia and reperfusion
    • Ramasamy R, TruebloodN, and Schaefer S. Metabolic effects of aldose reductase inhibition during low-flow ischemia and reperfusion. Am J Physiol 275(1 Pt 2): H195-H203, 1998.
    • (1998) Am J Physiol , vol.275 , Issue.1 PART 2
    • Ramasamy, R.1    Trueblood, N.2    Schaefer, S.3
  • 255
    • 0347419305 scopus 로고    scopus 로고
    • The molecular machinery of Keilin's respiratory chain
    • Rich PR. The molecular machinery of Keilin's respiratory chain. Biochem Soc Trans 31(Pt 6): 1095-1105, 2003. (Pubitemid 38030918)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1095-1105
    • Rich, P.R.1
  • 257
    • 34247868881 scopus 로고    scopus 로고
    • Inborn errors in the metabolism of glutathione
    • Ristoff E and Larsson A. Inborn errors in the metabolism of glutathione. Orphanet J Rare Dis 2: 16, 2007.
    • (2007) Orphanet J Rare Dis , vol.2 , pp. 16
    • Ristoff, E.1    Larsson, A.2
  • 258
    • 23844477888 scopus 로고    scopus 로고
    • The p53-induced gene-6 (proline oxidase) mediates apoptosis through a calcineurin-dependent pathway
    • DOI 10.1074/jbc.M504852200
    • Rivera A and Maxwell SA. The p53-induced gene-6 (proline oxidase) mediates apoptosis through a calcineurin-dependent pathway. J Biol Chem 280: 29346-29354, 2005. (Pubitemid 41161390)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.32 , pp. 29346-29354
    • Rivera, A.1    Maxwell, S.A.2
  • 260
    • 1642308537 scopus 로고    scopus 로고
    • Pol (ADP-ribosyl)ated chromatin domains: Access granted
    • DOI 10.1242/jcs.01080
    • Rouleau M, Aubin RA, and Poirier GG. Poly(ADP-ribosyl)ated chromatin domains: access granted. J Cell Sci 117(Pt 6): 815-825, 2004. (Pubitemid 38386940)
    • (2004) Journal of Cell Science , vol.117 , Issue.6 , pp. 815-825
    • Rouleau, M.1    Aubin, R.A.2    Poirier, G.G.3
  • 262
    • 0028857578 scopus 로고
    • Propionyl-L-carnitine-mediated improvement in contractile function of rat hearts oxidizing acetoacetate
    • Russell RR 3rd, Mommessin JI, and Taegtmeyer H. Propionyl-L-carnitine- mediated improvement in contractile function of rat hearts oxidizing acetoacetate. Am J Physiol 268(1 Pt 2): H441-H447, 1995.
    • (1995) Am J Physiol , vol.268 , Issue.1 PART 2
    • Russell III, R.R.1    Mommessin, J.I.2    Taegtmeyer, H.3
  • 263
    • 0026317455 scopus 로고
    • Pyruvate carboxylation prevents the decline in contractile function of rat hearts oxidizing acetoacetate
    • Russell RR 3rd and Taegtmeyer H. Pyruvate carboxylation prevents the decline in contractile function of rat hearts oxidizing acetoacetate. Am J Physiol 261(6 Pt 2): H1756-H1762, 1991.
    • (1991) Am J Physiol , vol.261 , Issue.6 PART 2
    • Russell III, R.R.1    Taegtmeyer, H.2
  • 266
    • 70350357467 scopus 로고    scopus 로고
    • Maintaining mammalian iron and oxygen homeostasis: Sensors, regulation, and cross-talk
    • Salahudeen AA and Bruick RK. Maintaining Mammalian iron and oxygen homeostasis: sensors, regulation, and cross-talk. Ann N Y Acad Sci 1177: 30-38, 2009.
    • (2009) Ann N y Acad Sci , vol.1177 , pp. 30-38
    • Salahudeen, A.A.1    Bruick, R.K.2
  • 267
    • 56949101056 scopus 로고    scopus 로고
    • SIRT1 regulates the ribosomal DNA locus: Epigenetic candles twinkle longevityinthe christmas tree
    • Salminen A and Kaarniranta K. SIRT1 regulates the ribosomal DNA locus: epigenetic candles twinkle longevityinthe Christmas tree. Biochem Biophys Res Commun 378: 6-9, 2009.
    • (2009) Biochem Biophys Res Commun , vol.378 , pp. 6-9
    • Salminen, A.1    Kaarniranta, K.2
  • 268
    • 0032877460 scopus 로고    scopus 로고
    • Nickel-induced transformation shifts the balance between HIF-1 and p53 transcription factors
    • DOI 10.1093/carcin/20.9.1819
    • Salnikow K, An WG, Melillo G, Blagosklonny MV, and Costa M. Nickel-induced transformation shifts the balance between HIF-1 and p53 transcription factors. Carcinogenesis 20: 1819-1823, 1999. (Pubitemid 29410563)
    • (1999) Carcinogenesis , vol.20 , Issue.9 , pp. 1819-1823
    • Salnikow, K.1    An, W.G.2    Melillo, G.3    Blagosklonny, M.V.4    Costa, M.5
  • 269
  • 270
    • 0036194785 scopus 로고    scopus 로고
    • + salvage pathway
    • Sandmeier JJ, Celic I, Boeke JD and Smith JS. Telomeric and rDNA silencing in Saccharomyces cerevisiae are dependent on a nuclear NAD(+) salvage pathway. Genetics 160: 877-889, 2002. (Pubitemid 34263455)
    • (2002) Genetics , vol.160 , Issue.3 , pp. 877-889
    • Sandmeier, J.J.1    Celic, I.2    Boeke, J.D.3    Smith, J.S.4
  • 273
    • 77954534436 scopus 로고    scopus 로고
    • Palmitoyl ascorbate-modified liposomes as nanoparticle platform for ascorbate-mediated cytotoxicity and paclitaxel co-delivery
    • Sawant RR, Vaze O, Rockwell K, and Torchilin VP. Palmitoyl ascorbate-modified liposomes as nanoparticle platform for ascorbate-mediated cytotoxicity and paclitaxel co-delivery. Eur J Pharm Biopharm 75: 321-326, 2010.
    • (2010) Eur J Pharm Biopharm , vol.75 , pp. 321-326
    • Sawant, R.R.1    Vaze, O.2    Rockwell, K.3    Torchilin, V.P.4
  • 275
    • 74049130225 scopus 로고    scopus 로고
    • Solving the dnmt2 enigma
    • Schaefer M and Lyko F. Solving the Dnmt2 enigma. Chromosoma 119: 35-40, 2010.
    • (2010) Chromosoma , vol.119 , pp. 35-40
    • Schaefer, M.1    Lyko, F.2
  • 278
    • 33745591371 scopus 로고    scopus 로고
    • Redox stress is not essential for the pseudo-hypoxic phenotype of succinate dehydrogenase deficient cells
    • DOI 10.1016/j.bbabio.2006.05.015, PII S0005272806001411
    • Selak MA, Duran RV, and Gottlieb E. Redox stress is not essential for the pseudo-hypoxic phenotype of succinate dehydrogenase deficient cells. Biochim Biophys Acta 1757: 567-572, 2006. (Pubitemid 43993873)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 567-572
    • Selak, M.A.1    Duran, R.V.2    Gottlieb, E.3
  • 280
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, and Casero RA. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119: 941-953, 2004. (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 281
    • 0021734287 scopus 로고
    • Characterization of two genes required for the position-effect control of yeast mating-type genes
    • Shore D, Squire M, and Nasmyth KA. Characterization of two genes required for the position-effect control of yeast mating-type genes. EMBO J 3: 2817-2823, 1984.
    • (1984) EMBO J , vol.3 , pp. 2817-2823
    • Shore, D.1    Squire, M.2    Nasmyth, K.A.3
  • 283
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith BC and Denu JM. Chemical mechanisms of histone lysine and arginine modifications. Biochim Biophys Acta 1789: 45-57, 2009.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 284
    • 53649086367 scopus 로고    scopus 로고
    • Mechanisms and molecular probes of sirtuins
    • Smith BC, Hallows WC, and Denu JM. Mechanisms and molecular probes of sirtuins. Chem Biol 15: 1002-1013, 2008.
    • (2008) Chem Biol , vol.15 , pp. 1002-1013
    • Smith, B.C.1    Hallows, W.C.2    Denu, J.M.3
  • 285
    • 36249005491 scopus 로고    scopus 로고
    • Succinate inhibition of α-ketoglutarate-dependent enzymes in a yeast model of paraganglioma
    • DOI 10.1093/hmg/ddm275
    • Smith EH, Janknecht R, and Maher LJ 3rd. Succinate inhibition of alpha-ketoglutarate-dependent enzymes in a yeast model of paraganglioma. Hum Mol Genet 16: 3136-3148, 2007. (Pubitemid 350131331)
    • (2007) Human Molecular Genetics , vol.16 , Issue.24 , pp. 3136-3148
    • Smith, E.H.1    Janknecht, R.2    Maher III, J.L.3
  • 288
    • 70349780606 scopus 로고    scopus 로고
    • The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors
    • Spannhoff A, Hauser AT, Heinke R, Sippl W, and Jung M. The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors. ChemMedChem 4: 1568-1582, 2009.
    • (2009) ChemMedChem , vol.4 , pp. 1568-1582
    • Spannhoff, A.1    Hauser, A.T.2    Heinke, R.3    Sippl, W.4    Jung, M.5
  • 290
    • 33645692860 scopus 로고    scopus 로고
    • D-2-hydroxyglutaric aciduria: Unravelling the biochemical pathway and the genetic defect
    • Struys EA. D-2-Hydroxyglutaric aciduria: unravelling the biochemical pathway and the genetic defect. J Inherit Metab Dis 29: 21-29, 2006.
    • (2006) J Inherit Metab Dis , vol.29 , pp. 21-29
    • Struys, E.A.1
  • 292
    • 77952744176 scopus 로고    scopus 로고
    • Natural antisense transcripts regulate gene expression in an epigenetic manner
    • Su WY, Xiong H, and Fang JY. Natural antisense transcripts regulate gene expression in an epigenetic manner. Biochem Biophys Res Commun 396: 177-181, 2010.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 177-181
    • Su, W.Y.1    Xiong, H.2    Fang, J.Y.3
  • 293
    • 67349119474 scopus 로고    scopus 로고
    • Modulation of histone methylation and MLH1 gene silencing by hexavalent chromium
    • Sun H, Zhou X, Chen H, Li Q, and Costa M. Modulation of histone methylation and MLH1 gene silencing by hexavalent chromium. Toxicol Appl Pharmacol 237: 258-266, 2009.
    • (2009) Toxicol Appl Pharmacol , vol.237 , pp. 258-266
    • Sun, H.1    Zhou, X.2    Chen, H.3    Li, Q.4    Costa, M.5
  • 294
    • 0031239784 scopus 로고    scopus 로고
    • Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene
    • DOI 10.1006/abbi.1997.0246
    • Sunden SL, Renduchintala MS, Park EI, Miklasz SD, and Garrow TA. Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene. Arch Biochem Biophys 345: 171-174, 1997. (Pubitemid 27374220)
    • (1997) Archives of Biochemistry and Biophysics , vol.345 , Issue.1 , pp. 171-174
    • Sunden, S.L.F.1    Renduchintala, M.S.2    Park, E.I.3    Miklasz, S.D.4    Garrow, T.A.5
  • 295
    • 43749098985 scopus 로고    scopus 로고
    • DNA methylation landscapes: Provocative insights from epigenomics
    • DOI 10.1038/nrg2341, PII NRG2341
    • Suzuki MM and Bird A. DNA methylation landscapes: provocative insights from epigenomics. Nat Rev Genet 9: 465-76, 2008. (Pubitemid 351693975)
    • (2008) Nature Reviews Genetics , vol.9 , Issue.6 , pp. 465-476
    • Suzuki, M.M.1    Bird, A.2
  • 301
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny JC, Dowd GJ, Huang J, Hilz H, and Moazed D. An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99: 735-745, 1999. (Pubitemid 30017644)
    • (1999) Cell , vol.99 , Issue.7 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 302
    • 70350634117 scopus 로고    scopus 로고
    • Living with iron (and oxygen): Questions and answers about iron homeostasis
    • Theil EC and Goss DJ. Living with iron (and oxygen): questions and answers about iron homeostasis. Chem Rev 109: 4568-4579, 2009.
    • (2009) Chem Rev , vol.109 , pp. 4568-4579
    • Theil, E.C.1    Goss, D.J.2
  • 303
    • 33751001725 scopus 로고    scopus 로고
    • Histone citrullination by protein arginine deiminase: Is arginine methylation a green light or a roadblock?
    • Thompson PR and Fast W. Histone citrullination by protein arginine deiminase: is arginine methylation a green light or a roadblock? ACS Chem Biol 1: 433-441, 2006.
    • (2006) ACS Chem Biol , vol.1 , pp. 433-441
    • Thompson, P.R.1    Fast, W.2
  • 304
    • 77950865121 scopus 로고    scopus 로고
    • Alpha-tocopheryl succinate promotes selective cell death induced by vitamin K3 in combination with ascorbate
    • Tomasetti M, Strafella E, Staffolani S, Santarelli L, Neuzil J, and Guerrieri R. alpha-Tocopheryl succinate promotes selective cell death induced by vitamin K3 in combination with ascorbate. Br J Cancer 102: 1224-1234, 2010.
    • (2010) Br J Cancer , vol.102 , pp. 1224-1234
    • Tomasetti, M.1    Strafella, E.2    Staffolani, S.3    Santarelli, L.4    Neuzil, J.5    Guerrieri, R.6
  • 306
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • DOI 10.1038/nature00908
    • Trewick SC, Henshaw TF, Hausinger RP, Lindahl T, and Sedgwick B. Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature 419: 174-178, 2002. (Pubitemid 35025446)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 307
    • 17644392469 scopus 로고    scopus 로고
    • Methylation: Lost in hydroxylation?
    • DOI 10.1038/sj.embor.7400379
    • Trewick SC, McLaughlin PJ, and Allshire RC Methylation: lost in hydroxylation? EMBO Rep 6: 315-320, 2005. (Pubitemid 40561622)
    • (2005) EMBO Reports , vol.6 , Issue.4 , pp. 315-320
    • Trewick, S.C.1    McLaughlin, P.J.2    Allshire, R.C.3
  • 308
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • DOI 10.1038/nature04433, PII NATURE04433
    • Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, and Zhang Y. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439: 811-816, 2006. (Pubitemid 43255695)
    • (2006) Nature , vol.439 , Issue.7078 , pp. 811-816
    • Tsukada, Y.-I.1    Fang, J.2    Erdjument-Bromage, H.3    Warren, M.E.4    Borchers, C.H.5    Tempst, P.6    Zhang, Y.7
  • 309
    • 2142829614 scopus 로고    scopus 로고
    • Regulation of chromatin structure and gene activity by poly(ADP-ribose) polymerases
    • DOI 10.1016/S0070-2153(03)01007-X, PII S007021530301007X
    • Tulin A, Chinenov Y, and Spradling A. Regulation of chromatin structure and gene activity by poly(ADP-ribose) polymerases. Curr Top Dev Biol 56: 55-83, 2003. (Pubitemid 137639483)
    • (2003) Current Topics in Developmental Biology , vol.56 , pp. 55-83
    • Tulin, A.1    Chinenov, Y.2    Spradling, A.3
  • 310
    • 33644777616 scopus 로고    scopus 로고
    • Drosophila poly(ADP-Ribose) glycohydrolase mediates chromatin structure and SIR2-dependent silencing
    • DOI 10.1534/genetics.105.049239
    • Tulin A, Naumova NM, Menon AK, and Spradling AC. Drosophila poly(ADP-ribose) glycohydrolase mediates chromatin structure and SIR2-dependent silencing. Genetics 172: 363-371, 2006. (Pubitemid 43345498)
    • (2006) Genetics , vol.172 , Issue.1 , pp. 363-371
    • Tulin, A.1    Naumova, N.M.2    Menon, A.K.3    Spradling, A.C.4
  • 311
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • DOI 10.1126/science.1078764
    • Tulin A and Spradling A. Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 299: 560-562, 2003. (Pubitemid 36135152)
    • (2003) Science , vol.299 , Issue.5606 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 315
    • 64449084807 scopus 로고    scopus 로고
    • L: 2-hydroxyglutaric aciduria, a disorder of metabolite repair
    • Van Schaftingen E, Rzem R, and Veiga-da-Cunha M. L: - 2-hydroxyglutaric aciduria, a disorder of metabolite repair. J Inherit Metab Dis 32: 135-142, 2009.
    • (2009) J Inherit Metab Dis , vol.32 , pp. 135-142
    • Van Schaftingen, E.1    Rzem, R.2    Veiga-Da-Cunha, M.3
  • 316
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the warburg effect: The metabolic requirements of cell proliferation
    • Vander Heiden MG, Cantley LC, and Thompson CB. 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
  • 319
    • 34247854781 scopus 로고    scopus 로고
    • Ascorbate deficiency results in impaired neutrophil apoptosis and clearance and is associated with up-regulation of hypoxia-inducible factor 1α
    • DOI 10.1189/jlb.0806541
    • Vissers MC and Wilkie RP. Ascorbate deficiency results in impaired neutrophil apoptosis and clearance and is associated with up-regulation of hypoxia-inducible factor 1alpha. J Leukoc Biol 81: 1236-1244, 2007. (Pubitemid 46702042)
    • (2007) Journal of Leukocyte Biology , vol.81 , Issue.5 , pp. 1236-1244
    • Vissers, M.C.M.1    Wilkie, R.P.2
  • 321
    • 0030940298 scopus 로고    scopus 로고
    • Histone acetylation: Chromatin in action
    • DOI 10.1016/S0968-0004(97)01016-5, PII S0968000497010165
    • Wade PA, Pruss D, and Wolffe AP. Histone acetylation: chromatin in action. Trends Biochem Sci 22: 128-132, 1997. (Pubitemid 27156942)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.4 , pp. 128-132
    • Wade, P.A.1    Pruss, D.2    Wolffe, A.P.3
  • 322
    • 57649178844 scopus 로고    scopus 로고
    • The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: A review
    • Wamelink MM, Struys EA, and Jakobs C. The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review. J Inherit Metab Dis 31: 703-717, 2008.
    • (2008) J Inherit Metab Dis , vol.31 , pp. 703-717
    • Wamelink, M.M.1    Struys, E.A.2    Jakobs, C.3
  • 324
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O. On the origin of cancer cells. Science 123: 309-314, 1956.
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 326
    • 79959520570 scopus 로고    scopus 로고
    • This reference has been deleted
    • This reference has been deleted.
  • 328
    • 60949102130 scopus 로고    scopus 로고
    • Dicer is regulated by cellular stresses and interferons
    • Wiesen JL and Tomasi TB. Dicer is regulated by cellular stresses and interferons. Mol Immunol 46: 1222-1228, 2009.
    • (2009) Mol Immunol , vol.46 , pp. 1222-1228
    • Wiesen, J.L.1    Tomasi, T.B.2
  • 329
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets?
    • Witt O, Deubzer HE, Milde T, and Oehme I. HDAC family: what are the cancer relevant targets? Cancer Lett 277: 8-21, 2009.
    • (2009) Cancer Lett , vol.277 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 330
    • 77954370016 scopus 로고    scopus 로고
    • Monomethylarsonous acid produces irreversible events resulting in malignant transformation of a human bladder cell line following 12 weeks of low-level exposure
    • Wnek SM, Jensen TJ, Severson PL, Futscher BW, and Gandolfi AJ. Monomethylarsonous acid produces irreversible events resulting in malignant transformation of a human bladder cell line following 12 weeks of low-level exposure. Toxicol Sci 116: 44-57, 2010.
    • (2010) Toxicol Sci , vol.116 , pp. 44-57
    • Wnek, S.M.1    Jensen, T.J.2    Severson, P.L.3    Futscher, B.W.4    Gandolfi, A.J.5
  • 331
    • 32844468049 scopus 로고    scopus 로고
    • Histone arginine methylation and its dynamic regulation
    • Wysocka J, Allis CD, and Coonrod S. Histone arginine methylation and its dynamic regulation. Front Biosci 11: 344-355, 2006. (Pubitemid 43253497)
    • (2006) Frontiers in Bioscience , vol.11 , pp. 344-355
    • Wysocka, J.1    Allis, C.D.2    Coonrod, S.3
  • 333
    • 0042092322 scopus 로고    scopus 로고
    • Analysis of specific lysine histone H3 and H4 acetylation and methylation status in clones of cells with a gene silenced by nickel exposure
    • DOI 10.1016/S0041-008X(03)00169-8
    • Yan Y, Kluz T, Zhang P, Chen HB, and Costa M. Analysis of specific lysine histone H3 and H4 acetylation and methylation status in clones of cells with a gene silenced by nickel exposure. Toxicol Appl Pharmacol 190: 272-277, 2003. (Pubitemid 36937217)
    • (2003) Toxicology and Applied Pharmacology , vol.190 , Issue.3 , pp. 272-277
    • Yan, Y.1    Kluz, T.2    Zhang, P.3    Chen, H.-B.4    Costa, M.5
  • 334
    • 33745728358 scopus 로고    scopus 로고
    • Cigarette smoke induces proinflammatory cytokine release by activation of NF-kappaB and posttranslational modifications of histone deacetylase in macrophages
    • Yang SR, Chida AS, Bauter MR, Shafiq N, Seweryniak K, Maggirwar SB, Kilty I, and Rahman I. Cigarette smoke induces proinflammatory cytokine release by activation of NF-kappaB and posttranslational modifications of histone deacetylase in macrophages. Am J Physiol Lung Cell Mol Physiol 291: L46-L57, 2006.
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.291
    • Yang, S.R.1    Chida, A.S.2    Bauter, M.R.3    Shafiq, N.4    Seweryniak, K.5    Maggirwar, S.B.6    Kilty, I.7    Rahman, I.8
  • 335
    • 77953669993 scopus 로고    scopus 로고
    • Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease
    • Ye H and Rouault TA. Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease. Biochemistry 49: 4945-4956, 2010.
    • (2010) Biochemistry , vol.49 , pp. 4945-4956
    • Ye, H.1    Rouault, T.A.2
  • 336
    • 34547870843 scopus 로고    scopus 로고
    • Homocysteine-mediated expression of SAHH, DNMTs, MBD2, and DNA hypomethylation potential pathogenic mechanism in VSMCs
    • DOI 10.1089/dna.2007.0584
    • Yideng J, Jianzhong Z, Ying H, Juan S, Jinge Z, Shenglan W, Xiaoqun H, and Shuren W. Homocysteine-mediated expression of SAHH, DNMTs, MBD2, and DNA hypomethylation potential pathogenic mechanism in VSMCs. DNA Cell Biol 26: 603-611, 2007. (Pubitemid 47263207)
    • (2007) DNA and Cell Biology , vol.26 , Issue.8 , pp. 603-611
    • Yideng, J.1    Jianzhong, Z.2    Ying, H.3    Juan, S.4    Jinge, Z.5    Shenglan, W.6    Xiaoqun, H.7    Shuren, W.8
  • 337
    • 41449110349 scopus 로고    scopus 로고
    • Homocysteine-mediated PPARα,γ DNA methylation and its potential pathogenic mechanism in monocytes
    • DOI 10.1089/dna.2007.0658
    • Yideng J, Zhihong L, Jiantuan X, Jun C, Guizhong L, and Shuren W. Homocysteine-mediated PPARalpha, gamma DNA methylation and its potential pathogenic mechanism in monocytes. DNA Cell Biol 27: 143-150, 2008. (Pubitemid 351457770)
    • (2008) DNA and Cell Biology , vol.27 , Issue.3 , pp. 143-150
    • Yideng, J.1    Zhihong, L.2    Jiantuan, X.3    Jun, C.4    Guizhong, L.5    Shuren, W.6
  • 338
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan J, Pu M, Zhang Z, and Lou Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 8: 1747-1753, 2009.
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 339
    • 34347252306 scopus 로고    scopus 로고
    • Overview: How is alcohol metabolized by the body?
    • Zakhari S. Overview: how is alcohol metabolized by the body? Alcohol Res Health 29: 245-254, 2006.
    • (2006) Alcohol Res Health , vol.29 , pp. 245-254
    • Zakhari, S.1
  • 340
    • 0032569020 scopus 로고    scopus 로고
    • The unmethylated state of CpG islands in mouse fibroblasts depends on the poly(ADP-ribosyl)ation process
    • DOI 10.1074/jbc.273.26.16517
    • Zardo G and Caiafa P. The unmethylated state of CpG islands in mouse fibroblasts depends on the poly(ADP-ribosyl)ation process. J Biol Chem 273: 16517-16520, 1998. (Pubitemid 28311436)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.26 , pp. 16517-16520
    • Zardo, G.1    Caiafa, P.2
  • 341
    • 0032883884 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribosyl)ation introduces an anomalous methylation pattern in transfected foreign DNA
    • Zardo G, Marenzi S, Perilli M, and Caiafa P. Inhibition of poly(ADP-ribosyl)ation introduces an anomalous methylation pattern in transfected foreign DNA. FASEB J 13: 1518-1522, 1999. (Pubitemid 29411784)
    • (1999) FASEB Journal , vol.13 , Issue.12 , pp. 1518-1522
    • Zardo, G.1    Marenzi, S.2    Perilli, M.3    Caiafa, P.4
  • 346
    • 0041589716 scopus 로고    scopus 로고
    • Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked?
    • DOI 10.1002/bies.10317
    • Zhang J. Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked? Bioessays 25: 808-814, 2003. (Pubitemid 36966382)
    • (2003) BioEssays , vol.25 , Issue.8 , pp. 808-814
    • Zhang, J.1
  • 347
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • DOI 10.1126/science.1069300
    • Zhang Q, Piston DW, and Goodman RH. Regulation of corepressor function by nuclear NADH. Science 295: 1895-1897, 2002. (Pubitemid 34214127)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3
  • 349
    • 0024996681 scopus 로고
    • The oxidative inactivation of mitochondrial electron transport chain components and ATPase
    • Zhang Y, Marcillat O, Giulivi C, Ernster L, and Davies KJ. The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J Biol Chem 265: 16330-16336, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 16330-16336
    • Zhang, Y.1    Marcillat, O.2    Giulivi, C.3    Ernster, L.4    Davies, K.J.5
  • 350
    • 0037165643 scopus 로고    scopus 로고
    • Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate- substrate-NO complex: Evidence for metal centred rearrangements
    • DOI 10.1016/S0014-5793(02)02520-6, PII S0014579302025206
    • Zhang Z, Ren J, Harlos K, McKinnon CH, Clifton IJ, and Schofield CJ. Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements. FEBS Lett 517: 7-12, 2002. (Pubitemid 34327621)
    • (2002) FEBS Letters , vol.517 , Issue.1-3 , pp. 7-12
    • Zhang, Z.1    Ren, J.-S.2    Harlos, K.3    McKinnon, C.H.4    Clifton, I.J.5    Schofield, C.J.6
  • 351
    • 64849098267 scopus 로고    scopus 로고
    • Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha
    • Zhao S, Lin Y, Xu W, Jiang W, Zha Z, Wang P, Yu W, Li Z, Gong L, Peng Y, et al. Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha. Science 324: 261-265, 2009.
    • (2009) Science , vol.324 , pp. 261-265
    • Zhao, S.1    Lin, Y.2    Xu, W.3    Jiang, W.4    Zha, Z.5    Wang, P.6    Yu, W.7    Li, Z.8    Gong, L.9    Peng, Y.10
  • 352
    • 61849137246 scopus 로고    scopus 로고
    • Effects of nickel, chromate, and arsenite on histone 3 lysine methylation
    • Zhou X, Li Q, Arita A, Sun H, and Costa M. Effects of nickel, chromate, and arsenite on histone 3 lysine methylation. Toxicol Appl Pharmacol 236: 78-84, 2009.
    • (2009) Toxicol Appl Pharmacol , vol.236 , pp. 78-84
    • Zhou, X.1    Li, Q.2    Arita, A.3    Sun, H.4    Costa, M.5
  • 353
    • 73349104113 scopus 로고    scopus 로고
    • Active DNA demethylation mediated by DNA glycosylases
    • Zhu JK. Active DNA demethylation mediated by DNA glycosylases. Annu Rev Genet 43: 143-166, 2009.
    • (2009) Annu Rev Genet , vol.43 , pp. 143-166
    • Zhu, J.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.