메뉴 건너뛰기




Volumn 112, Issue , 2017, Pages 36-48

Role of glutathione in the regulation of epigenetic mechanisms in disease

Author keywords

DNA methylation; Epigenetics; Glutathione; Histone; MicroRNAs; Rare diseases; S adenosylmethionine; S glutathionylation

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; DNA; GLUTAREDOXIN; GLUTATHIONE; HISTONE; UNTRANSLATED RNA; MICRORNA; S ADENOSYLMETHIONINE;

EID: 85024486710     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2017.07.008     Document Type: Review
Times cited : (88)

References (195)
  • 1
    • 65049087578 scopus 로고    scopus 로고
    • Role of nuclear glutathione as a key regulator of cell proliferation
    • Pallardo, F.V., Markovic, J., Garcia, J.L., Vina, J., Role of nuclear glutathione as a key regulator of cell proliferation. Mol. Asp. Med. 30:1–2 (2009), 77–85.
    • (2009) Mol. Asp. Med. , vol.30 , Issue.1-2 , pp. 77-85
    • Pallardo, F.V.1    Markovic, J.2    Garcia, J.L.3    Vina, J.4
  • 3
    • 78649560974 scopus 로고    scopus 로고
    • Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield
    • Vivancos, P.D., Dong, Y., Ziegler, K., Markovic, J., Pallardo, F.V., Pellny, T.K., Verrier, P.J., Foyer, C.H., Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield. Plant J. 64:5 (2010), 825–838.
    • (2010) Plant J. , vol.64 , Issue.5 , pp. 825-838
    • Vivancos, P.D.1    Dong, Y.2    Ziegler, K.3    Markovic, J.4    Pallardo, F.V.5    Pellny, T.K.6    Verrier, P.J.7    Foyer, C.H.8
  • 4
    • 34547110841 scopus 로고    scopus 로고
    • Glutathione is recruited into the nucleus in early phases of cell proliferation
    • Markovic, J., Borras, C., Ortega, A., Sastre, J., Vina, J., Pallardo, F.V., Glutathione is recruited into the nucleus in early phases of cell proliferation. J. Biol. Chem. 282:28 (2007), 20416–20424.
    • (2007) J. Biol. Chem. , vol.282 , Issue.28 , pp. 20416-20424
    • Markovic, J.1    Borras, C.2    Ortega, A.3    Sastre, J.4    Vina, J.5    Pallardo, F.V.6
  • 7
    • 79959521749 scopus 로고    scopus 로고
    • The redox basis of epigenetic modifications: from mechanisms to functional consequences
    • Cyr, A.R., Domann, F.E., The redox basis of epigenetic modifications: from mechanisms to functional consequences. Antioxid. Redox Signal. 15:2 (2011), 551–589.
    • (2011) Antioxid. Redox Signal. , vol.15 , Issue.2 , pp. 551-589
    • Cyr, A.R.1    Domann, F.E.2
  • 11
    • 69349098474 scopus 로고    scopus 로고
    • Epigenetics: definition, mechanisms and clinical perspective
    • Dupont, C., Armant, D.R., Brenner, C.A., Epigenetics: definition, mechanisms and clinical perspective. Semin. Reprod. Med. 27:5 (2009), 351–357.
    • (2009) Semin. Reprod. Med. , vol.27 , Issue.5 , pp. 351-357
    • Dupont, C.1    Armant, D.R.2    Brenner, C.A.3
  • 12
    • 84925267221 scopus 로고    scopus 로고
    • Epigenetic inheritance: histone bookmarks across generations
    • Campos, E.I., Stafford, J.M., Reinberg, D., Epigenetic inheritance: histone bookmarks across generations. Trends Cell Biol. 24 (2014), 664–674.
    • (2014) Trends Cell Biol. , vol.24 , pp. 664-674
    • Campos, E.I.1    Stafford, J.M.2    Reinberg, D.3
  • 13
    • 84897139220 scopus 로고    scopus 로고
    • Transgenerational epigenetic inheritance: myths and mechanisms
    • Heard, E., Martienssen, R.A., Transgenerational epigenetic inheritance: myths and mechanisms. Cell 157:1 (2014), 95–109.
    • (2014) Cell , vol.157 , Issue.1 , pp. 95-109
    • Heard, E.1    Martienssen, R.A.2
  • 14
    • 84885151895 scopus 로고    scopus 로고
    • Paternal obesity initiates metabolic disturbances in two generations of mice with incomplete penetrance to the F2 generation and alters the transcriptional profile of testis and sperm microRNA content
    • Fullston, T., Ohlsson Teague, E.M., Palmer, N.O., DeBlasio, M.J., Mitchell, M., Corbett, M., Print, C.G., Owens, J.A., Lane, M., Paternal obesity initiates metabolic disturbances in two generations of mice with incomplete penetrance to the F2 generation and alters the transcriptional profile of testis and sperm microRNA content. FASEB J. 27:10 (2013), 4226–4243.
    • (2013) FASEB J. , vol.27 , Issue.10 , pp. 4226-4243
    • Fullston, T.1    Ohlsson Teague, E.M.2    Palmer, N.O.3    DeBlasio, M.J.4    Mitchell, M.5    Corbett, M.6    Print, C.G.7    Owens, J.A.8    Lane, M.9
  • 15
    • 84860576380 scopus 로고    scopus 로고
    • Smoking induces differential miRNA expression in human spermatozoa: a potential transgenerational epigenetic concern?
    • Marczylo, E.L., Amoako, A.A., Konje, J.C., Gant, T.W., Marczylo, T.H., Smoking induces differential miRNA expression in human spermatozoa: a potential transgenerational epigenetic concern?. Epigenetics 7:5 (2012), 432–439.
    • (2012) Epigenetics , vol.7 , Issue.5 , pp. 432-439
    • Marczylo, E.L.1    Amoako, A.A.2    Konje, J.C.3    Gant, T.W.4    Marczylo, T.H.5
  • 17
    • 84858439628 scopus 로고    scopus 로고
    • Cancer epigenomics: beyond genomics
    • Sandoval, J., Esteller, M., Cancer epigenomics: beyond genomics. Curr. Opin. Genet. Dev. 22:1 (2012), 50–55.
    • (2012) Curr. Opin. Genet. Dev. , vol.22 , Issue.1 , pp. 50-55
    • Sandoval, J.1    Esteller, M.2
  • 18
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones, P.A., Baylin, S.B., The epigenomics of cancer. Cell 128:4 (2007), 683–692.
    • (2007) Cell , vol.128 , Issue.4 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 21
    • 80052461558 scopus 로고    scopus 로고
    • Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
    • Ito, S., Shen, L., Dai, Q., Wu, S.C., Collins, L.B., Swenberg, J.A., He, C., Zhang, Y., Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science 333:6047 (2011), 1300–1303.
    • (2011) Science , vol.333 , Issue.6047 , pp. 1300-1303
    • Ito, S.1    Shen, L.2    Dai, Q.3    Wu, S.C.4    Collins, L.B.5    Swenberg, J.A.6    He, C.7    Zhang, Y.8
  • 25
    • 79954457998 scopus 로고    scopus 로고
    • Genome-wide analysis of 5-hydroxymethylcytosine distribution reveals its dual function in transcriptional regulation in mouse embryonic stem cells
    • Wu, H., D'Alessio, A.C., Ito, S., Wang, Z., Cui, K., Zhao, K., Sun, Y.E., Zhang, Y., Genome-wide analysis of 5-hydroxymethylcytosine distribution reveals its dual function in transcriptional regulation in mouse embryonic stem cells. Genes Dev. 25:7 (2011), 679–684.
    • (2011) Genes Dev. , vol.25 , Issue.7 , pp. 679-684
    • Wu, H.1    D'Alessio, A.C.2    Ito, S.3    Wang, Z.4    Cui, K.5    Zhao, K.6    Sun, Y.E.7    Zhang, Y.8
  • 26
    • 84874655393 scopus 로고    scopus 로고
    • Dynamics of 5-methylcytosine and 5-hydroxymethylcytosine during germ cell reprogramming
    • Yamaguchi, S., Hong, K., Liu, R., Inoue, A., Shen, L., Zhang, K., Zhang, Y., Dynamics of 5-methylcytosine and 5-hydroxymethylcytosine during germ cell reprogramming. Cell Res. 23:3 (2013), 329–339.
    • (2013) Cell Res. , vol.23 , Issue.3 , pp. 329-339
    • Yamaguchi, S.1    Hong, K.2    Liu, R.3    Inoue, A.4    Shen, L.5    Zhang, K.6    Zhang, Y.7
  • 27
    • 84937538653 scopus 로고    scopus 로고
    • Regulation of the epigenome by Vitamin C
    • Young, J.I., Züchner, S., Wang, G., Regulation of the epigenome by Vitamin C. Ann. Rev. Nutr. 35:1 (2015), 545–564.
    • (2015) Ann. Rev. Nutr. , vol.35 , Issue.1 , pp. 545-564
    • Young, J.I.1    Züchner, S.2    Wang, G.3
  • 28
    • 84987933236 scopus 로고    scopus 로고
    • Chiral antioxidant-based gold nanoclusters reprogram DNA epigenetic patterns
    • 33436-33436
    • Ma, Y., Fu, H., Zhang, C., Cheng, S., Gao, J., Wang, Z., Jin, W., Conde, J., Cui, D., Chiral antioxidant-based gold nanoclusters reprogram DNA epigenetic patterns. Sci. Rep., 6(1), 2016 33436-33436.
    • (2016) Sci. Rep. , vol.6 , Issue.1
    • Ma, Y.1    Fu, H.2    Zhang, C.3    Cheng, S.4    Gao, J.5    Wang, Z.6    Jin, W.7    Conde, J.8    Cui, D.9
  • 29
    • 3042767202 scopus 로고    scopus 로고
    • MicroRNAs: small RNAs with a big role in gene regulation
    • He, L., Hannon, G.J., MicroRNAs: small RNAs with a big role in gene regulation. Nat. Rev. Genet. 5:7 (2004), 522–531.
    • (2004) Nat. Rev. Genet. , vol.5 , Issue.7 , pp. 522-531
    • He, L.1    Hannon, G.J.2
  • 30
    • 60149099385 scopus 로고    scopus 로고
    • Evolution and functions of long noncoding RNAs
    • Ponting, C.P., Oliver, P.L., Reik, W., Evolution and functions of long noncoding RNAs. Cell 136:4 (2009), 629–641.
    • (2009) Cell , vol.136 , Issue.4 , pp. 629-641
    • Ponting, C.P.1    Oliver, P.L.2    Reik, W.3
  • 31
    • 33645321647 scopus 로고    scopus 로고
    • MicroRNAs in cell proliferation, cell death, and tumorigenesis
    • Hwang, H.W., Mendell, J.T., MicroRNAs in cell proliferation, cell death, and tumorigenesis. Br. J. Cancer 94:6 (2006), 776–780.
    • (2006) Br. J. Cancer , vol.94 , Issue.6 , pp. 776-780
    • Hwang, H.W.1    Mendell, J.T.2
  • 32
    • 77957361864 scopus 로고    scopus 로고
    • Targeting microRNAs in cancer: rationale, strategies and challenges
    • Garzon, R., Marcucci, G., Croce, C.M., Targeting microRNAs in cancer: rationale, strategies and challenges. Nat. Rev. Drug Discov. 9:10 (2010), 775–789.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , Issue.10 , pp. 775-789
    • Garzon, R.1    Marcucci, G.2    Croce, C.M.3
  • 33
    • 54549108798 scopus 로고    scopus 로고
    • MicroRNAs to Nanog, Oct4 and Sox2 coding regions modulate embryonic stem cell differentiation
    • Tay, Y., Zhang, J., Thomson, A.M., Lim, B., Rigoutsos, I., MicroRNAs to Nanog, Oct4 and Sox2 coding regions modulate embryonic stem cell differentiation. Nature 455:7216 (2008), 1124–1128.
    • (2008) Nature , vol.455 , Issue.7216 , pp. 1124-1128
    • Tay, Y.1    Zhang, J.2    Thomson, A.M.3    Lim, B.4    Rigoutsos, I.5
  • 34
    • 34547441263 scopus 로고    scopus 로고
    • Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR
    • Lytle, J.R., Yario, T.A., Steitz, J.A., Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR. Proc. Natl. Acad. Sci. USA 104:23 (2007), 9667–9672.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.23 , pp. 9667-9672
    • Lytle, J.R.1    Yario, T.A.2    Steitz, J.A.3
  • 35
    • 36749026906 scopus 로고    scopus 로고
    • Switching from repression to activation: microRNAs can up-regulate translation
    • Vasudevan, S., Tong, Y., Steitz, J.A., Switching from repression to activation: microRNAs can up-regulate translation. Science 318:5858 (2007), 1931–1934.
    • (2007) Science , vol.318 , Issue.5858 , pp. 1931-1934
    • Vasudevan, S.1    Tong, Y.2    Steitz, J.A.3
  • 36
    • 84885185272 scopus 로고    scopus 로고
    • Regulation of the Nrf2 antioxidant pathway by microRNAs: new players in micromanaging redox homeostasis
    • Cheng, X., Ku, C.H., Siow, R.C., Regulation of the Nrf2 antioxidant pathway by microRNAs: new players in micromanaging redox homeostasis. Free Radic. Biol. Med. 64 (2013), 4–11.
    • (2013) Free Radic. Biol. Med. , vol.64 , pp. 4-11
    • Cheng, X.1    Ku, C.H.2    Siow, R.C.3
  • 37
    • 84885175767 scopus 로고    scopus 로고
    • Redox regulation of microRNAs in health and disease
    • J.F.H.
    • Siow, R.C., H, J.F., Redox regulation of microRNAs in health and disease. Free Radic. Biol. Med. 64 (2013), 1–3.
    • (2013) Free Radic. Biol. Med. , vol.64 , pp. 1-3
    • Siow, R.C.1
  • 39
    • 77952212771 scopus 로고    scopus 로고
    • RNA traffic control of chromatin complexes
    • Koziol, M.J., Rinn, J.L., RNA traffic control of chromatin complexes. Curr. Opin. Genet. Dev. 20:2 (2010), 142–148.
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , Issue.2 , pp. 142-148
    • Koziol, M.J.1    Rinn, J.L.2
  • 41
    • 80053045739 scopus 로고    scopus 로고
    • Molecular mechanisms of long noncoding RNAs
    • Wang, K.C., Chang, H.Y., Molecular mechanisms of long noncoding RNAs. Mol. Cell 43:6 (2011), 904–914.
    • (2011) Mol. Cell , vol.43 , Issue.6 , pp. 904-914
    • Wang, K.C.1    Chang, H.Y.2
  • 43
    • 84960435106 scopus 로고    scopus 로고
    • Critical link between epigenetics and transcription factors in the induction of autoimmunity: a comprehensive review
    • Wu, H., Zhao, M., Yoshimura, A., Chang, C., Lu, Q., Critical link between epigenetics and transcription factors in the induction of autoimmunity: a comprehensive review. Clin. Rev. Allergy Immunol. 50:3 (2016), 333–344.
    • (2016) Clin. Rev. Allergy Immunol. , vol.50 , Issue.3 , pp. 333-344
    • Wu, H.1    Zhao, M.2    Yoshimura, A.3    Chang, C.4    Lu, Q.5
  • 44
    • 34250820438 scopus 로고    scopus 로고
    • Chromatin dynamics and the preservation of genetic information
    • Downs, J.A., Nussenzweig, M.C., Nussenzweig, A., Chromatin dynamics and the preservation of genetic information. Nature 447:7147 (2007), 951–958.
    • (2007) Nature , vol.447 , Issue.7147 , pp. 951-958
    • Downs, J.A.1    Nussenzweig, M.C.2    Nussenzweig, A.3
  • 45
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D., Allis, C.D., The language of covalent histone modifications. Nature 403:6765 (2000), 41–45.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 46
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T., Allis, C.D., Translating the histone code. Science 293:5532 (2001), 1074–1080.
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 47
    • 84866072106 scopus 로고    scopus 로고
    • A simple histone code opens many paths to epigenetics
    • Sneppen, K., Dodd, I.B., A simple histone code opens many paths to epigenetics. PLoS Comput. Biol., 8(8), 2012, e1002643.
    • (2012) PLoS Comput. Biol. , vol.8 , Issue.8 , pp. e1002643
    • Sneppen, K.1    Dodd, I.B.2
  • 48
    • 84942422655 scopus 로고    scopus 로고
    • Progress in epigenetic histone modification analysis by mass spectrometry for clinical investigations
    • Önder, Ö., Sidoli, S., Carroll, M., Garcia, B.A., Progress in epigenetic histone modification analysis by mass spectrometry for clinical investigations. Expert Rev. Proteom. 12:5 (2015), 499–517.
    • (2015) Expert Rev. Proteom. , vol.12 , Issue.5 , pp. 499-517
    • Önder, Ö.1    Sidoli, S.2    Carroll, M.3    Garcia, B.A.4
  • 52
    • 23044460521 scopus 로고    scopus 로고
    • Epigenetics, histone H3 variants, and the inheritance of chromatin states
    • Henikoff, S., McKittrick, E., Ahmad, K., Epigenetics, histone H3 variants, and the inheritance of chromatin states. Cold Spring Harb. Symp. Quant. Biol. 69 (2004), 235–243.
    • (2004) Cold Spring Harb. Symp. Quant. Biol. , vol.69 , pp. 235-243
    • Henikoff, S.1    McKittrick, E.2    Ahmad, K.3
  • 53
    • 1242342240 scopus 로고    scopus 로고
    • Histone H3.3 is enriched in covalent modifications associated with active chromatin
    • McKittrick, E., Gafken, P.R., Ahmad, K., Henikoff, S., Histone H3.3 is enriched in covalent modifications associated with active chromatin. Proc. Natl. Acad. Sci. USA 101:6 (2004), 1525–1530.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.6 , pp. 1525-1530
    • McKittrick, E.1    Gafken, P.R.2    Ahmad, K.3    Henikoff, S.4
  • 54
    • 33646239638 scopus 로고    scopus 로고
    • Histone H3 variants and their potential role in indexing mammalian genomes: the “H3 barcode hypothesis”
    • Hake, S.B., Allis, C.D., Histone H3 variants and their potential role in indexing mammalian genomes: the “H3 barcode hypothesis”. Proc. Natl. Acad. Sci. USA 103:17 (2006), 6428–6435.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.17 , pp. 6428-6435
    • Hake, S.B.1    Allis, C.D.2
  • 55
    • 0346731045 scopus 로고    scopus 로고
    • Forming facultative heterochromatin: silencing of an X chromosome in mammalian females
    • Chow, J.C., Brown, C.J., Forming facultative heterochromatin: silencing of an X chromosome in mammalian females. Cell. Mol. Life Sci. 60:12 (2003), 2586–2603.
    • (2003) Cell. Mol. Life Sci. , vol.60 , Issue.12 , pp. 2586-2603
    • Chow, J.C.1    Brown, C.J.2
  • 57
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M., Jenuwein, T., The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14:3 (2002), 286–298.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , Issue.3 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 58
    • 84904051400 scopus 로고    scopus 로고
    • Biochemical systems approaches for the analysis of histone modification readout
    • Soldi, M., Bremang, M., Bonaldi, T., Biochemical systems approaches for the analysis of histone modification readout. Biochim. Biophys. Acta 1839:8 (2014), 657–668.
    • (2014) Biochim. Biophys. Acta , vol.1839 , Issue.8 , pp. 657-668
    • Soldi, M.1    Bremang, M.2    Bonaldi, T.3
  • 59
    • 84908616466 scopus 로고    scopus 로고
    • Posttranslational modifications of human histone H3: an update
    • Xu, Y.M., Du, J.Y., Lau, A.T., Posttranslational modifications of human histone H3: an update. Proteomics 14:17–18 (2014), 2047–2060.
    • (2014) Proteomics , vol.14 , Issue.17-18 , pp. 2047-2060
    • Xu, Y.M.1    Du, J.Y.2    Lau, A.T.3
  • 60
    • 4043112183 scopus 로고    scopus 로고
    • Oxidative damage to methyl-CpG sequences inhibits the binding of the methyl-CpG binding domain (MBD) of methyl-CpG binding protein 2 (MeCP2)
    • Valinluck, V., Tsai, H.H., Rogstad, D.K., Burdzy, A., Bird, A., Sowers, L.C., Oxidative damage to methyl-CpG sequences inhibits the binding of the methyl-CpG binding domain (MBD) of methyl-CpG binding protein 2 (MeCP2). Nucleic Acids Res. 32:14 (2004), 4100–4108.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.14 , pp. 4100-4108
    • Valinluck, V.1    Tsai, H.H.2    Rogstad, D.K.3    Burdzy, A.4    Bird, A.5    Sowers, L.C.6
  • 61
    • 4143070452 scopus 로고    scopus 로고
    • Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression
    • Rahman, I., Marwick, J., Kirkham, P., Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression. Biochem. Pharmacol. 68:6 (2004), 1255–1267.
    • (2004) Biochem. Pharmacol. , vol.68 , Issue.6 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 62
    • 78650270964 scopus 로고    scopus 로고
    • Beyond genetics: epigenetic code in chronic kidney disease
    • Dwivedi, R.S., Herman, J.G., McCaffrey, T.A., Raj, D.S., Beyond genetics: epigenetic code in chronic kidney disease. Kidney Int. 79:1 (2011), 23–32.
    • (2011) Kidney Int. , vol.79 , Issue.1 , pp. 23-32
    • Dwivedi, R.S.1    Herman, J.G.2    McCaffrey, T.A.3    Raj, D.S.4
  • 64
    • 84875755814 scopus 로고    scopus 로고
    • Influence of metabolism on epigenetics and disease
    • Kaelin, W.G. Jr., McKnight, S.L., Influence of metabolism on epigenetics and disease. Cell 153:1 (2013), 56–69.
    • (2013) Cell , vol.153 , Issue.1 , pp. 56-69
    • Kaelin, W.G.1    McKnight, S.L.2
  • 65
    • 84904610478 scopus 로고    scopus 로고
    • Maintenance of glutathione levels and its importance in epigenetic regulation
    • 88-88
    • Garcia-Gimenez, J.L., Pallardo, F.V., Maintenance of glutathione levels and its importance in epigenetic regulation. Front. Pharmacol., 5, 2014 88-88.
    • (2014) Front. Pharmacol. , vol.5
    • Garcia-Gimenez, J.L.1    Pallardo, F.V.2
  • 66
    • 84978196149 scopus 로고    scopus 로고
    • Oxidative stress signaling to chromatin in health and disease
    • Kreuz, S., Fischle, W., Oxidative stress signaling to chromatin in health and disease. Epigenomics 8:6 (2016), 843–862.
    • (2016) Epigenomics , vol.8 , Issue.6 , pp. 843-862
    • Kreuz, S.1    Fischle, W.2
  • 67
    • 77953539483 scopus 로고    scopus 로고
    • Differences among allelic variants of human glutathione transferase A2-2 in the activation of azathioprine
    • Zhang, W., Moden, O., Mannervik, B., Differences among allelic variants of human glutathione transferase A2-2 in the activation of azathioprine. Chem. Biol. Interact. 186:2 (2010), 110–117.
    • (2010) Chem. Biol. Interact. , vol.186 , Issue.2 , pp. 110-117
    • Zhang, W.1    Moden, O.2    Mannervik, B.3
  • 68
    • 84895817996 scopus 로고    scopus 로고
    • DNA methylation, a hand behind neurodegenerative diseases
    • Lu, H., Liu, X., Deng, Y., Qing, H., DNA methylation, a hand behind neurodegenerative diseases. Front. Aging Neurosci., 5, 2013, 85.
    • (2013) Front. Aging Neurosci. , vol.5 , pp. 85
    • Lu, H.1    Liu, X.2    Deng, Y.3    Qing, H.4
  • 69
    • 85014064108 scopus 로고    scopus 로고
    • The diverse roles of glutathione-associated cell resistance against hypericin photodynamic therapy
    • Theodossiou, T.A., Olsen, C.E., Jonsson, M., Kubin, A., Hothersall, J.S., Berg, K., The diverse roles of glutathione-associated cell resistance against hypericin photodynamic therapy. Redox Biol. 12 (2017), 191–197.
    • (2017) Redox Biol. , vol.12 , pp. 191-197
    • Theodossiou, T.A.1    Olsen, C.E.2    Jonsson, M.3    Kubin, A.4    Hothersall, J.S.5    Berg, K.6
  • 72
    • 84884417889 scopus 로고    scopus 로고
    • Pleiotropic effects of methionine adenosyltransferases deregulation as determinants of liver cancer progression and prognosis
    • Frau, M., Feo, F., Pascale, R.M., Pleiotropic effects of methionine adenosyltransferases deregulation as determinants of liver cancer progression and prognosis. J. Hepatol. 59:4 (2013), 830–841.
    • (2013) J. Hepatol. , vol.59 , Issue.4 , pp. 830-841
    • Frau, M.1    Feo, F.2    Pascale, R.M.3
  • 74
    • 84897424236 scopus 로고    scopus 로고
    • Morphine induces redox-based changes in global dna methylation and retrotransposon transcription by inhibition of excitatory amino acid transporter type 3-mediated cysteine uptake
    • Trivedi, M., Shah, J., Hodgson, N., Byun, H.M., Deth, R., Morphine induces redox-based changes in global dna methylation and retrotransposon transcription by inhibition of excitatory amino acid transporter type 3-mediated cysteine uptake. Mol. Pharmacol. 85:5 (2014), 747–757.
    • (2014) Mol. Pharmacol. , vol.85 , Issue.5 , pp. 747-757
    • Trivedi, M.1    Shah, J.2    Hodgson, N.3    Byun, H.M.4    Deth, R.5
  • 75
    • 84979521132 scopus 로고    scopus 로고
    • Enhanced GSH synthesis by Bisphenol A exposure promoted DNA methylation process in the testes of adult rare minnow Gobiocypris rarus
    • Yuan, C., Zhang, Y., Liu, Y., Zhang, T., Wang, Z., Enhanced GSH synthesis by Bisphenol A exposure promoted DNA methylation process in the testes of adult rare minnow Gobiocypris rarus. Aquat. Toxicol. 178 (2016), 99–105.
    • (2016) Aquat. Toxicol. , vol.178 , pp. 99-105
    • Yuan, C.1    Zhang, Y.2    Liu, Y.3    Zhang, T.4    Wang, Z.5
  • 76
    • 84949551883 scopus 로고    scopus 로고
    • Epigenetic effects of casein-derived opioid peptides in SH-SY5Y human neuroblastoma cells
    • Trivedi, M.S., Hodgson, N.W., Walker, S.J., Trooskens, G., Nair, V., Deth, R.C., Epigenetic effects of casein-derived opioid peptides in SH-SY5Y human neuroblastoma cells. Nutr. Metab., 12, 2015, 54.
    • (2015) Nutr. Metab. , vol.12 , pp. 54
    • Trivedi, M.S.1    Hodgson, N.W.2    Walker, S.J.3    Trooskens, G.4    Nair, V.5    Deth, R.C.6
  • 78
    • 0027536144 scopus 로고
    • Restriction endonucleases and modification methylases
    • Anderson, J.E., Restriction endonucleases and modification methylases. Curr. Opin. Struct. Biol. 3 (1993), 24–30.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 24-30
    • Anderson, J.E.1
  • 79
    • 65049089113 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Lu, S.C., Regulation of glutathione synthesis. Mol. Asp. Med. 30:1–2 (2009), 42–59.
    • (2009) Mol. Asp. Med. , vol.30 , Issue.1-2 , pp. 42-59
    • Lu, S.C.1
  • 80
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • Feng, Q., Wang, H., Ng, H.H., Erdjument-Bromage, H., Tempst, P., Struhl, K., Zhang, Y., Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr. Biol. 12:12 (2002), 1052–1058.
    • (2002) Curr. Biol. , vol.12 , Issue.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3    Erdjument-Bromage, H.4    Tempst, P.5    Struhl, K.6    Zhang, Y.7
  • 81
    • 0037020199 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of a SET domain protein methyltransferase
    • Trievel, R.C., Beach, B.M., Dirk, L.M., Houtz, R.L., Hurley, J.H., Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell 111:1 (2002), 91–103.
    • (2002) Cell , vol.111 , Issue.1 , pp. 91-103
    • Trievel, R.C.1    Beach, B.M.2    Dirk, L.M.3    Houtz, R.L.4    Hurley, J.H.5
  • 82
    • 77955616558 scopus 로고    scopus 로고
    • Compartmentalization of Mammalian folate-mediated one-carbon metabolism
    • Tibbetts, A.S., Appling, D.R., Compartmentalization of Mammalian folate-mediated one-carbon metabolism. Annu. Rev. Nutr. 30 (2010), 57–81.
    • (2010) Annu. Rev. Nutr. , vol.30 , pp. 57-81
    • Tibbetts, A.S.1    Appling, D.R.2
  • 84
    • 84875836819 scopus 로고    scopus 로고
    • The relationship between intracellular and plasma levels of folate and metabolites in the methionine cycle: a model
    • Duncan, T.M., Reed, M.C., Nijhout, H.F., The relationship between intracellular and plasma levels of folate and metabolites in the methionine cycle: a model. Mol. Nutr. Food Res. 57:4 (2013), 628–636.
    • (2013) Mol. Nutr. Food Res. , vol.57 , Issue.4 , pp. 628-636
    • Duncan, T.M.1    Reed, M.C.2    Nijhout, H.F.3
  • 85
    • 84878781935 scopus 로고    scopus 로고
    • How are mammalian methionine adenosyltransferases regulated in the liver? A focus on redox stress
    • Pajares, M.A., Álvarez, L., Pérez-Sala, D., How are mammalian methionine adenosyltransferases regulated in the liver? A focus on redox stress. FEBS Lett. 587:12 (2013), 1711–1716.
    • (2013) FEBS Lett. , vol.587 , Issue.12 , pp. 1711-1716
    • Pajares, M.A.1    Álvarez, L.2    Pérez-Sala, D.3
  • 87
    • 37149010874 scopus 로고    scopus 로고
    • Oxidative stress modulates DNA methylation during melanocyte anchorage blockade associated with malignant transformation
    • Campos, A.C., Molognoni, F., Melo, F.H., Galdieri, L.C., Carneiro, C.R., D'Almeida, V., Correa, M., Jasiulionis, M.G., Oxidative stress modulates DNA methylation during melanocyte anchorage blockade associated with malignant transformation. Neoplasia 9:12 (2007), 1111–1121.
    • (2007) Neoplasia , vol.9 , Issue.12 , pp. 1111-1121
    • Campos, A.C.1    Molognoni, F.2    Melo, F.H.3    Galdieri, L.C.4    Carneiro, C.R.5    D'Almeida, V.6    Correa, M.7    Jasiulionis, M.G.8
  • 88
    • 0019765119 scopus 로고
    • Depletion of glutathione by inhibition of biosynthesis
    • Griffith, O.W., Depletion of glutathione by inhibition of biosynthesis. Methods Enzymol. 77 (1981), 59–63.
    • (1981) Methods Enzymol. , vol.77 , pp. 59-63
    • Griffith, O.W.1
  • 89
    • 0014105888 scopus 로고
    • Enzyme-catalysed conjugations of glutathione with unsaturated compounds
    • Boyland, E., Chasseaud, L.F., Enzyme-catalysed conjugations of glutathione with unsaturated compounds. Biochem. J. 104:1 (1967), 95–102.
    • (1967) Biochem. J. , vol.104 , Issue.1 , pp. 95-102
    • Boyland, E.1    Chasseaud, L.F.2
  • 91
    • 0026026873 scopus 로고
    • The relationship between nuclear glutathione levels and resistance to melphalan in human ovarian tumour cells
    • Britten, R.A., Green, J.A., Broughton, C., Browning, P.G., White, R., Warenius, H.M., The relationship between nuclear glutathione levels and resistance to melphalan in human ovarian tumour cells. Biochem. Pharmacol. 41:4 (1991), 647–649.
    • (1991) Biochem. Pharmacol. , vol.41 , Issue.4 , pp. 647-649
    • Britten, R.A.1    Green, J.A.2    Broughton, C.3    Browning, P.G.4    White, R.5    Warenius, H.M.6
  • 93
    • 0029949621 scopus 로고    scopus 로고
    • Increased sensitivity to oxidative injury in chinese hamster ovary cells stably transfected with rat liver S-adenosylmethionine synthetase cDNA
    • Sanchez-Gongora, E., Pastorino, J.G., Alvarez, L., Pajares, M.A., Garcia, C., Vina, J.R., Mato, J.M., Farber, J.L., Increased sensitivity to oxidative injury in chinese hamster ovary cells stably transfected with rat liver S-adenosylmethionine synthetase cDNA. Biochem. J. 319:Pt 3 (1996), 767–773.
    • (1996) Biochem. J. , vol.319 , pp. 767-773
    • Sanchez-Gongora, E.1    Pastorino, J.G.2    Alvarez, L.3    Pajares, M.A.4    Garcia, C.5    Vina, J.R.6    Mato, J.M.7    Farber, J.L.8
  • 94
    • 0026699645 scopus 로고
    • Modulation of rat liver S-adenosylmethionine synthetase activity by glutathione
    • Pajares, M.A., Duran, C., Corrales, F., Pliego, M.M., Mato, J.M., Modulation of rat liver S-adenosylmethionine synthetase activity by glutathione. J. Biol. Chem. 267:25 (1992), 17598–17605.
    • (1992) J. Biol. Chem. , vol.267 , Issue.25 , pp. 17598-17605
    • Pajares, M.A.1    Duran, C.2    Corrales, F.3    Pliego, M.M.4    Mato, J.M.5
  • 95
    • 0030592716 scopus 로고    scopus 로고
    • Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione
    • Martinez-Chantar, M.L., Pajares, M.A., Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione. FEBS Lett. 397:2–3 (1996), 293–297.
    • (1996) FEBS Lett. , vol.397 , Issue.2-3 , pp. 293-297
    • Martinez-Chantar, M.L.1    Pajares, M.A.2
  • 97
    • 0038758127 scopus 로고    scopus 로고
    • Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol
    • Perez-Mato, I., Castro, C., Ruiz, F.A., Corrales, F.J., Mato, J.M., Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol. J. Biol. Chem. 274:24 (1999), 17075–17079.
    • (1999) J. Biol. Chem. , vol.274 , Issue.24 , pp. 17075-17079
    • Perez-Mato, I.1    Castro, C.2    Ruiz, F.A.3    Corrales, F.J.4    Mato, J.M.5
  • 98
    • 0032742177 scopus 로고    scopus 로고
    • In vivo regulation by glutathione of methionine adenosyltransferase S-nitrosylation in rat liver
    • Corrales, F.J., Ruiz, F., Mato, J.M., In vivo regulation by glutathione of methionine adenosyltransferase S-nitrosylation in rat liver. J. Hepatol. 31:5 (1999), 887–894.
    • (1999) J. Hepatol. , vol.31 , Issue.5 , pp. 887-894
    • Corrales, F.J.1    Ruiz, F.2    Mato, J.M.3
  • 99
    • 0036136732 scopus 로고    scopus 로고
    • S-Adenosylmethionine: a control switch that regulates liver function
    • Mato, J.M., Corrales, F.J., Lu, S.C., Avila, M.A., S-Adenosylmethionine: a control switch that regulates liver function. FASEB J. 16:1 (2002), 15–26.
    • (2002) FASEB J. , vol.16 , Issue.1 , pp. 15-26
    • Mato, J.M.1    Corrales, F.J.2    Lu, S.C.3    Avila, M.A.4
  • 100
    • 33645240777 scopus 로고    scopus 로고
    • Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation
    • Lindermayr, C., Saalbach, G., Bahnweg, G., Durner, J., Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation. J. Biol. Chem. 281:7 (2006), 4285–4291.
    • (2006) J. Biol. Chem. , vol.281 , Issue.7 , pp. 4285-4291
    • Lindermayr, C.1    Saalbach, G.2    Bahnweg, G.3    Durner, J.4
  • 104
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C., Kumar, C., Gnad, F., Nielsen, M.L., Rehman, M., Walther, T.C., Olsen, J.V., Mann, M., Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325:5942 (2009), 834–840.
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8
  • 105
    • 77957666255 scopus 로고    scopus 로고
    • Histone methyl transferases and demethylases; can they link metabolism and transcription?
    • Teperino, R., Schoonjans, K., Auwerx, J., Histone methyl transferases and demethylases; can they link metabolism and transcription?. Cell Metab. 12:4 (2010), 321–327.
    • (2010) Cell Metab. , vol.12 , Issue.4 , pp. 321-327
    • Teperino, R.1    Schoonjans, K.2    Auwerx, J.3
  • 106
    • 0027362756 scopus 로고
    • Prevention of bromobenzene toxicity by N-acetylmethionine: correlation between toxicity and the impairment in O- and S-methylation of bromothiocatechols
    • Lertratanangkoon, K., Scimeca, J.M., Prevention of bromobenzene toxicity by N-acetylmethionine: correlation between toxicity and the impairment in O- and S-methylation of bromothiocatechols. Toxicol. Appl. Pharmacol. 122:2 (1993), 191–199.
    • (1993) Toxicol. Appl. Pharmacol. , vol.122 , Issue.2 , pp. 191-199
    • Lertratanangkoon, K.1    Scimeca, J.M.2
  • 107
    • 0030065081 scopus 로고    scopus 로고
    • Methyl-donor deficiency due to chemically induced glutathione depletion
    • Lertratanangkoon, K., Orkiszewski, R.S., Scimeca, J.M., Methyl-donor deficiency due to chemically induced glutathione depletion. Cancer Res. 56:5 (1996), 995–1005.
    • (1996) Cancer Res. , vol.56 , Issue.5 , pp. 995-1005
    • Lertratanangkoon, K.1    Orkiszewski, R.S.2    Scimeca, J.M.3
  • 108
    • 0028999638 scopus 로고
    • Differential effects of depleting agents on cytoplasmic and nuclear non-protein sulphydryls: a fluorescence image cytometry study
    • Thomas, M., Nicklee, T., Hedley, D.W., Differential effects of depleting agents on cytoplasmic and nuclear non-protein sulphydryls: a fluorescence image cytometry study. Br. J. Cancer 72:1 (1995), 45–50.
    • (1995) Br. J. Cancer , vol.72 , Issue.1 , pp. 45-50
    • Thomas, M.1    Nicklee, T.2    Hedley, D.W.3
  • 109
    • 0028181392 scopus 로고
    • Modulation of gamma-glutamylcysteine synthetase large subunit mRNA expression by butylated hydroxyanisole
    • Borroz, K.I., Buetler, T.M., Eaton, D.L., Modulation of gamma-glutamylcysteine synthetase large subunit mRNA expression by butylated hydroxyanisole. Toxicol. Appl. Pharmacol. 126:1 (1994), 150–155.
    • (1994) Toxicol. Appl. Pharmacol. , vol.126 , Issue.1 , pp. 150-155
    • Borroz, K.I.1    Buetler, T.M.2    Eaton, D.L.3
  • 110
    • 0024444942 scopus 로고
    • Increase in endothelial cell glutathione and precursor amino acid uptake by diethyl maleate and hyperoxia
    • Deneke, S.M., Baxter, D.F., Phelps, D.T., Fanburg, B.L., Increase in endothelial cell glutathione and precursor amino acid uptake by diethyl maleate and hyperoxia. Am. J. Physiol. 257:4 Pt 1 (1989), L265–L271.
    • (1989) Am. J. Physiol. , vol.257 , Issue.4 , pp. L265-L271
    • Deneke, S.M.1    Baxter, D.F.2    Phelps, D.T.3    Fanburg, B.L.4
  • 111
    • 0024468830 scopus 로고
    • Erythrocytes fail to induce glutathione in response to diethyl maleate or hyperoxia
    • Phelps, D.T., Deneke, S.M., Baxter, D.F., Fanburg, B.L., Erythrocytes fail to induce glutathione in response to diethyl maleate or hyperoxia. Am. J. Physiol. 257:4 Pt 1 (1989), L272–L276.
    • (1989) Am. J. Physiol. , vol.257 , Issue.4 , pp. L272-L276
    • Phelps, D.T.1    Deneke, S.M.2    Baxter, D.F.3    Fanburg, B.L.4
  • 113
    • 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, Y.S., Song, M.F., Kasai, H., DNA methylation by dimethyl sulfoxide and methionine sulfoxide triggered by hydroxyl radical and implications for epigenetic modifications. Bioorg. Med. Chem. Lett. 20:1 (2010), 260–265.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.1 , pp. 260-265
    • Kawai, K.1    Li, Y.S.2    Song, M.F.3    Kasai, H.4
  • 114
    • 79959744436 scopus 로고    scopus 로고
    • DNA methylation in cancer development, diagnosis and therapy – multiple opportunities for genotoxic agents to act as methylome disruptors or remediators
    • Lewandowska, J., Bartoszek, A., DNA methylation in cancer development, diagnosis and therapy – multiple opportunities for genotoxic agents to act as methylome disruptors or remediators. Mutagenesis 26:4 (2011), 475–487.
    • (2011) Mutagenesis , vol.26 , Issue.4 , pp. 475-487
    • Lewandowska, J.1    Bartoszek, A.2
  • 116
    • 0019046891 scopus 로고
    • Effect of histone H3 sulfhydryl modifications on histone-histone interactions and nucleosome formation and structure
    • Lewis, P.N., Chiu, S.S., Effect of histone H3 sulfhydryl modifications on histone-histone interactions and nucleosome formation and structure. Eur. J. Biochem. 109:2 (1980), 369–376.
    • (1980) Eur. J. Biochem. , vol.109 , Issue.2 , pp. 369-376
    • Lewis, P.N.1    Chiu, S.S.2
  • 117
    • 0020554124 scopus 로고
    • Reversible changes in nucleosome structure and histone H3 accessibility in transcriptionally active and inactive states of rDNA chromatin
    • Prior, C.P., Cantor, C.R., Johnson, E.M., Littau, V.C., Allfrey, V.G., Reversible changes in nucleosome structure and histone H3 accessibility in transcriptionally active and inactive states of rDNA chromatin. Cell 34:3 (1983), 1033–1042.
    • (1983) Cell , vol.34 , Issue.3 , pp. 1033-1042
    • Prior, C.P.1    Cantor, C.R.2    Johnson, E.M.3    Littau, V.C.4    Allfrey, V.G.5
  • 118
    • 85011661322 scopus 로고    scopus 로고
    • Profiling of histone post-translational modifications in mouse brain with high-resolution top-down mass spectrometry
    • Zhou, M., Paša-Tolić, L., Stenoien, D.L., Profiling of histone post-translational modifications in mouse brain with high-resolution top-down mass spectrometry. J. Proteome Res. 16:2 (2017), 599–608.
    • (2017) J. Proteome Res. , vol.16 , Issue.2 , pp. 599-608
    • Zhou, M.1    Paša-Tolić, L.2    Stenoien, D.L.3
  • 119
    • 84885234013 scopus 로고    scopus 로고
    • Proteome-wide detection and quantitative analysis of irreversible cysteine oxidation using long column UPLC-pSRM
    • Lee, C.F., Paull, T.T., Person, M.D., Proteome-wide detection and quantitative analysis of irreversible cysteine oxidation using long column UPLC-pSRM. J. Proteome Res. 12:10 (2013), 4302–4315.
    • (2013) J. Proteome Res. , vol.12 , Issue.10 , pp. 4302-4315
    • Lee, C.F.1    Paull, T.T.2    Person, M.D.3
  • 120
    • 0028564741 scopus 로고
    • Homocysteinemia and schizophrenia as a case of methylation deficiency
    • Regland, B., Johansson, B.V., Gottfries, C.G., Homocysteinemia and schizophrenia as a case of methylation deficiency. J. Neural Transm. Gen. Sect. 98:2 (1994), 143–152.
    • (1994) J. Neural Transm. Gen. Sect. , vol.98 , Issue.2 , pp. 143-152
    • Regland, B.1    Johansson, B.V.2    Gottfries, C.G.3
  • 121
    • 29244464827 scopus 로고    scopus 로고
    • Altered glutathione redox state in schizophrenia
    • Yao, J.K., Leonard, S., Reddy, R., Altered glutathione redox state in schizophrenia. Dis. Markers 22:1–2 (2006), 83–93.
    • (2006) Dis. Markers , vol.22 , Issue.1-2 , pp. 83-93
    • Yao, J.K.1    Leonard, S.2    Reddy, R.3
  • 122
    • 40849116456 scopus 로고    scopus 로고
    • Aberrant DNA methylation associated with bipolar disorder identified from discordant monozygotic twins
    • Kuratomi, G., Iwamoto, K., Bundo, M., Kusumi, I., Kato, N., Iwata, N., Ozaki, N., Kato, T., Aberrant DNA methylation associated with bipolar disorder identified from discordant monozygotic twins. Mol. Psychiatry 13:4 (2008), 429–441.
    • (2008) Mol. Psychiatry , vol.13 , Issue.4 , pp. 429-441
    • Kuratomi, G.1    Iwamoto, K.2    Bundo, M.3    Kusumi, I.4    Kato, N.5    Iwata, N.6    Ozaki, N.7    Kato, T.8
  • 124
    • 15244348759 scopus 로고    scopus 로고
    • Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism
    • James, S.J., Cutler, P., Melnyk, S., Jernigan, S., Janak, L., Gaylor, D.W., Neubrander, J.A., Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism. Am. J. Clin. Nutr. 80:6 (2004), 1611–1617.
    • (2004) Am. J. Clin. Nutr. , vol.80 , Issue.6 , pp. 1611-1617
    • James, S.J.1    Cutler, P.2    Melnyk, S.3    Jernigan, S.4    Janak, L.5    Gaylor, D.W.6    Neubrander, J.A.7
  • 126
    • 84882417694 scopus 로고    scopus 로고
    • The 'golden age' of DNA methylation in neurodegenerative diseases
    • Fuso, A., The 'golden age' of DNA methylation in neurodegenerative diseases. Clin. Chem. Lab. Med. 51:3 (2013), 523–534.
    • (2013) Clin. Chem. Lab. Med. , vol.51 , Issue.3 , pp. 523-534
    • Fuso, A.1
  • 127
    • 84869413146 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis in homocystinuria patients with genetic remethylation defects
    • Richard, E., Desviat, L.R., Ugarte, M., Pérez, B., Oxidative stress and apoptosis in homocystinuria patients with genetic remethylation defects. J. Cell. Biochem. 114:1 (2013), 183–191.
    • (2013) J. Cell. Biochem. , vol.114 , Issue.1 , pp. 183-191
    • Richard, E.1    Desviat, L.R.2    Ugarte, M.3    Pérez, B.4
  • 128
    • 0034703084 scopus 로고    scopus 로고
    • Increase in plasma homocysteine associated with parallel increases in plasma S-adenosylhomocysteine and lymphocyte DNA hypomethylation
    • Yi, P., Melnyk, S., Pogribna, M., Pogribny, I.P., Hine, R.J., James, S.J., Increase in plasma homocysteine associated with parallel increases in plasma S-adenosylhomocysteine and lymphocyte DNA hypomethylation. J. Biol. Chem. 275:38 (2000), 29318–29323.
    • (2000) J. Biol. Chem. , vol.275 , Issue.38 , pp. 29318-29323
    • Yi, P.1    Melnyk, S.2    Pogribna, M.3    Pogribny, I.P.4    Hine, R.J.5    James, S.J.6
  • 129
    • 0035172715 scopus 로고    scopus 로고
    • Intracellular S-adenosylhomocysteine concentrations predict global DNA hypomethylation in tissues of methyl-deficient cystathionine beta-synthase heterozygous mice
    • Caudill, M.A., Wang, J.C., Melnyk, S., Pogribny, I.P., Jernigan, S., Collins, M.D., Santos-Guzman, J., Swendseid, M.E., Cogger, E.A., James, S.J., Intracellular S-adenosylhomocysteine concentrations predict global DNA hypomethylation in tissues of methyl-deficient cystathionine beta-synthase heterozygous mice. J. Nutr. 131:11 (2001), 2811–2818.
    • (2001) J. Nutr. , vol.131 , Issue.11 , pp. 2811-2818
    • Caudill, M.A.1    Wang, J.C.2    Melnyk, S.3    Pogribny, I.P.4    Jernigan, S.5    Collins, M.D.6    Santos-Guzman, J.7    Swendseid, M.E.8    Cogger, E.A.9    James, S.J.10
  • 130
    • 52049123592 scopus 로고    scopus 로고
    • Methylenetetrahydrofolate reductase, common polymorphisms, and relation to disease
    • Thomas, P., Fenech, M., Methylenetetrahydrofolate reductase, common polymorphisms, and relation to disease. Vitam. Horm. 79 (2008), 375–392.
    • (2008) Vitam. Horm. , vol.79 , pp. 375-392
    • Thomas, P.1    Fenech, M.2
  • 132
    • 84869413146 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis in homocystinuria patients with genetic remethylation defects
    • Richard, E., Desviat, L.R., Ugarte, M., Perez, B., Oxidative stress and apoptosis in homocystinuria patients with genetic remethylation defects. J. Cell. Biochem. 114:1 (2013), 183–191.
    • (2013) J. Cell. Biochem. , vol.114 , Issue.1 , pp. 183-191
    • Richard, E.1    Desviat, L.R.2    Ugarte, M.3    Perez, B.4
  • 133
    • 80755140110 scopus 로고    scopus 로고
    • Hypothesis: hyperhomocysteinemia is an indicator of oxidant stress
    • Hoffman, M., Hypothesis: hyperhomocysteinemia is an indicator of oxidant stress. Med. Hypotheses 77:6 (2011), 1088–1093.
    • (2011) Med. Hypotheses , vol.77 , Issue.6 , pp. 1088-1093
    • Hoffman, M.1
  • 134
    • 2942700001 scopus 로고    scopus 로고
    • 5,10-methylenetetrahydrofolate reductase (MTHFR) 677C->T and 1298A->C mutations are associated with DNA hypomethylation
    • Castro, R., Rivera, I., Ravasco, P., Camilo, M.E., Jakobs, C., Blom, H.J., de Almeida, I.T., 5,10-methylenetetrahydrofolate reductase (MTHFR) 677C->T and 1298A->C mutations are associated with DNA hypomethylation. J. Med. Genet. 41:6 (2004), 454–458.
    • (2004) J. Med. Genet. , vol.41 , Issue.6 , pp. 454-458
    • Castro, R.1    Rivera, I.2    Ravasco, P.3    Camilo, M.E.4    Jakobs, C.5    Blom, H.J.6    de Almeida, I.T.7
  • 135
    • 84991083721 scopus 로고    scopus 로고
    • Functional characterization of missense mutations in severe methylenetetrahydrofolate reductase deficiency using a human expression system
    • Burda, P., Suormala, T., Heuberger, D., Schafer, A., Fowler, B., Froese, D.S., Baumgartner, M.R., Functional characterization of missense mutations in severe methylenetetrahydrofolate reductase deficiency using a human expression system. J. Inherit. Metab. Dis. 40:2 (2017), 297–306.
    • (2017) J. Inherit. Metab. Dis. , vol.40 , Issue.2 , pp. 297-306
    • Burda, P.1    Suormala, T.2    Heuberger, D.3    Schafer, A.4    Fowler, B.5    Froese, D.S.6    Baumgartner, M.R.7
  • 136
    • 84875836627 scopus 로고    scopus 로고
    • Low dietary folate and methylenetetrahydrofolate reductase deficiency may lead to pregnancy complications through modulation of ApoAI and IFN-gamma in spleen and placenta, and through reduction of methylation potential
    • Mikael, L.G., Pancer, J., Jiang, X., Wu, Q., Caudill, M., Rozen, R., Low dietary folate and methylenetetrahydrofolate reductase deficiency may lead to pregnancy complications through modulation of ApoAI and IFN-gamma in spleen and placenta, and through reduction of methylation potential. Mol. Nutr. Food Res. 57:4 (2013), 661–670.
    • (2013) Mol. Nutr. Food Res. , vol.57 , Issue.4 , pp. 661-670
    • Mikael, L.G.1    Pancer, J.2    Jiang, X.3    Wu, Q.4    Caudill, M.5    Rozen, R.6
  • 137
    • 79960144827 scopus 로고    scopus 로고
    • Epigenetics: a new bridge between nutrition and health
    • Choi, S.W., Friso, S., Epigenetics: a new bridge between nutrition and health. Adv. Nutr. 1:1 (2010), 8–16.
    • (2010) Adv. Nutr. , vol.1 , Issue.1 , pp. 8-16
    • Choi, S.W.1    Friso, S.2
  • 138
    • 0036327615 scopus 로고    scopus 로고
    • Diet, methyl donors and DNA methylation: interactions between dietary folate, methionine and choline
    • Niculescu, M.D., Zeisel, S.H., Diet, methyl donors and DNA methylation: interactions between dietary folate, methionine and choline. J. Nutr. 132:8 Suppl (2002), 2333S–2335S.
    • (2002) J. Nutr. , vol.132 , Issue.8 , pp. 2333S-2335S
    • Niculescu, M.D.1    Zeisel, S.H.2
  • 140
    • 30744479491 scopus 로고    scopus 로고
    • Dietary choline deficiency alters global and gene-specific DNA methylation in the developing hippocampus of mouse fetal brains
    • Niculescu, M.D., Craciunescu, C.N., Zeisel, S.H., Dietary choline deficiency alters global and gene-specific DNA methylation in the developing hippocampus of mouse fetal brains. FASEB J. 20:1 (2006), 43–49.
    • (2006) FASEB J. , vol.20 , Issue.1 , pp. 43-49
    • Niculescu, M.D.1    Craciunescu, C.N.2    Zeisel, S.H.3
  • 141
    • 67650489669 scopus 로고    scopus 로고
    • Folic acid or combination of folic acid and vitamin B(12) prevents short-term arsenic trioxide-induced systemic and mitochondrial dysfunction and DNA damage
    • Majumdar, S., Mukherjee, S., Maiti, A., Karmakar, S., Das, A.S., Mukherjee, M., Nanda, A., Mitra, C., Folic acid or combination of folic acid and vitamin B(12) prevents short-term arsenic trioxide-induced systemic and mitochondrial dysfunction and DNA damage. Environ. Toxicol. 24:4 (2009), 377–387.
    • (2009) Environ. Toxicol. , vol.24 , Issue.4 , pp. 377-387
    • Majumdar, S.1    Mukherjee, S.2    Maiti, A.3    Karmakar, S.4    Das, A.S.5    Mukherjee, M.6    Nanda, A.7    Mitra, C.8
  • 142
  • 146
    • 56349142882 scopus 로고    scopus 로고
    • Abnormal transmethylation/transsulfuration metabolism and DNA hypomethylation among parents of children with autism
    • James, S.J., Melnyk, S., Jernigan, S., Hubanks, A., Rose, S., Gaylor, D.W., Abnormal transmethylation/transsulfuration metabolism and DNA hypomethylation among parents of children with autism. J. Autism Dev. Disord. 38:10 (2008), 1966–1975.
    • (2008) J. Autism Dev. Disord. , vol.38 , Issue.10 , pp. 1966-1975
    • James, S.J.1    Melnyk, S.2    Jernigan, S.3    Hubanks, A.4    Rose, S.5    Gaylor, D.W.6
  • 147
    • 84897111264 scopus 로고    scopus 로고
    • Methylomic analysis of monozygotic twins discordant for autism spectrum disorder and related behavioural traits
    • Wong, C.C., Meaburn, E.L., Ronald, A., Price, T.S., Jeffries, A.R., Schalkwyk, L.C., Plomin, R., Mill, J., Methylomic analysis of monozygotic twins discordant for autism spectrum disorder and related behavioural traits. Mol. Psychiatry 19:4 (2014), 495–503.
    • (2014) Mol. Psychiatry , vol.19 , Issue.4 , pp. 495-503
    • Wong, C.C.1    Meaburn, E.L.2    Ronald, A.3    Price, T.S.4    Jeffries, A.R.5    Schalkwyk, L.C.6    Plomin, R.7    Mill, J.8
  • 149
    • 77951116456 scopus 로고    scopus 로고
    • The ScanBrit randomised, controlled, single-blind study of a gluten- and casein-free dietary intervention for children with autism spectrum disorders
    • Whiteley, P., Haracopos, D., Knivsberg, A.M., Reichelt, K.L., Parlar, S., Jacobsen, J., Seim, A., Pedersen, L., Schondel, M., Shattock, P., The ScanBrit randomised, controlled, single-blind study of a gluten- and casein-free dietary intervention for children with autism spectrum disorders. Nutr. Neurosci. 13:2 (2010), 87–100.
    • (2010) Nutr. Neurosci. , vol.13 , Issue.2 , pp. 87-100
    • Whiteley, P.1    Haracopos, D.2    Knivsberg, A.M.3    Reichelt, K.L.4    Parlar, S.5    Jacobsen, J.6    Seim, A.7    Pedersen, L.8    Schondel, M.9    Shattock, P.10
  • 150
    • 84893871236 scopus 로고    scopus 로고
    • Nutriepigenetic regulation by folate-homocysteine-methionine axis: a review
    • Bhargava, S., Tyagi, S.C., Nutriepigenetic regulation by folate-homocysteine-methionine axis: a review. Mol. Cell. Biochem. 387:1–2 (2014), 55–61.
    • (2014) Mol. Cell. Biochem. , vol.387 , Issue.1-2 , pp. 55-61
    • Bhargava, S.1    Tyagi, S.C.2
  • 151
    • 23444438707 scopus 로고    scopus 로고
    • Oxidative stress levels are raised in chronic fatigue syndrome and are associated with clinical symptoms
    • Kennedy, G., Spence, V.A., McLaren, M., Hill, A., Underwood, C., Belch, J.J., Oxidative stress levels are raised in chronic fatigue syndrome and are associated with clinical symptoms. Free Radic. Biol. Med. 39:5 (2005), 584–589.
    • (2005) Free Radic. Biol. Med. , vol.39 , Issue.5 , pp. 584-589
    • Kennedy, G.1    Spence, V.A.2    McLaren, M.3    Hill, A.4    Underwood, C.5    Belch, J.J.6
  • 153
    • 84896525898 scopus 로고    scopus 로고
    • The emerging role of autoimmunity in myalgic encephalomyelitis/chronic fatigue syndrome (ME/cfs)
    • Morris, G., Berk, M., Galecki, P., Maes, M., The emerging role of autoimmunity in myalgic encephalomyelitis/chronic fatigue syndrome (ME/cfs). Mol. Neurobiol. 49:2 (2014), 741–756.
    • (2014) Mol. Neurobiol. , vol.49 , Issue.2 , pp. 741-756
    • Morris, G.1    Berk, M.2    Galecki, P.3    Maes, M.4
  • 154
    • 84905860167 scopus 로고    scopus 로고
    • DNA methylation modifications associated with chronic fatigue syndrome
    • de Vega, W.C., Vernon, S.D., McGowan, P.O., DNA methylation modifications associated with chronic fatigue syndrome. PLoS One, 9(8), 2014, e104757.
    • (2014) PLoS One , vol.9 , Issue.8 , pp. e104757
    • de Vega, W.C.1    Vernon, S.D.2    McGowan, P.O.3
  • 155
    • 34547870843 scopus 로고    scopus 로고
    • Homocysteine-mediated expression of SAHH, DNMTs, MBD2, and DNA hypomethylation potential pathogenic mechanism in VSMCs
    • Yideng, J., Jianzhong, Z., Ying, H., Juan, S., Jinge, Z., Shenglan, W., Xiaoqun, H., Shuren, W., Homocysteine-mediated expression of SAHH, DNMTs, MBD2, and DNA hypomethylation potential pathogenic mechanism in VSMCs. DNA Cell Biol. 26:8 (2007), 603–611.
    • (2007) DNA Cell Biol. , 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
  • 157
    • 0036326660 scopus 로고    scopus 로고
    • Elevation in S-adenosylhomocysteine and DNA hypomethylation: potential epigenetic mechanism for homocysteine-related pathology
    • James, S.J., Melnyk, S., Pogribna, M., Pogribny, I.P., Caudill, M.A., Elevation in S-adenosylhomocysteine and DNA hypomethylation: potential epigenetic mechanism for homocysteine-related pathology. J. Nutr. 132:8 Suppl (2002), 2361S–2366S.
    • (2002) J. Nutr. , vol.132 , Issue.8 , pp. 2361S-2366S
    • James, S.J.1    Melnyk, S.2    Pogribna, M.3    Pogribny, I.P.4    Caudill, M.A.5
  • 158
    • 0021865460 scopus 로고
    • Low content of hepatic reduced glutathione in patients with Wilson's disease
    • Summer, K.H., Eisenburg, J., Low content of hepatic reduced glutathione in patients with Wilson's disease. Biochem. Med. 34:1 (1985), 107–111.
    • (1985) Biochem. Med. , vol.34 , Issue.1 , pp. 107-111
    • Summer, K.H.1    Eisenburg, J.2
  • 160
    • 0347991793 scopus 로고    scopus 로고
    • Homocysteine and oxidative stress
    • Perna, A.F., Ingrosso, D., Santo, N.G. De, Homocysteine and oxidative stress. Amino Acids 25:3-4 (2003), 409–417.
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 409-417
    • Perna, A.F.1    Ingrosso, D.2    Santo, N.G.D.3
  • 162
    • 19044385595 scopus 로고    scopus 로고
    • Cystathionine beta synthase deficiency promotes oxidative stress, fibrosis, and steatosis in mice liver
    • Robert, K., Nehme, J., Bourdon, E., Pivert, G., Friguet, B., Delcayre, C., Delabar, J.M., Janel, N., Cystathionine beta synthase deficiency promotes oxidative stress, fibrosis, and steatosis in mice liver. Gastroenterology 128:5 (2005), 1405–1415.
    • (2005) Gastroenterology , vol.128 , Issue.5 , pp. 1405-1415
    • Robert, K.1    Nehme, J.2    Bourdon, E.3    Pivert, G.4    Friguet, B.5    Delcayre, C.6    Delabar, J.M.7    Janel, N.8
  • 163
    • 34047255417 scopus 로고    scopus 로고
    • DNA methylation status is not impaired in treated cystathionine beta-synthase (CBS) deficient patients
    • Heil, S.G., Riksen, N.P., Boers, G.H., Smulders, Y., Blom, H.J., DNA methylation status is not impaired in treated cystathionine beta-synthase (CBS) deficient patients. Mol. Genet. Metab. 91:1 (2007), 55–60.
    • (2007) Mol. Genet. Metab. , vol.91 , Issue.1 , pp. 55-60
    • Heil, S.G.1    Riksen, N.P.2    Boers, G.H.3    Smulders, Y.4    Blom, H.J.5
  • 165
    • 84859508314 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in Down syndrome
    • Pagano, G., Castello, G., Oxidative stress and mitochondrial dysfunction in Down syndrome. Adv. Exp. Med. Biol 724 (2012), 291–299.
    • (2012) Adv. Exp. Med. Biol , vol.724 , pp. 291-299
    • Pagano, G.1    Castello, G.2
  • 167
    • 0021485455 scopus 로고
    • Superoxide dismutase, glutathione peroxidase and lipoperoxidation in Down's syndrome fetal brain
    • Brooksbank, B.W., Balazs, R., Superoxide dismutase, glutathione peroxidase and lipoperoxidation in Down's syndrome fetal brain. Brain Res. 318:1 (1984), 37–44.
    • (1984) Brain Res. , vol.318 , Issue.1 , pp. 37-44
    • Brooksbank, B.W.1    Balazs, R.2
  • 168
    • 0023444192 scopus 로고
    • Transgenic mice with increased Cu/Zn-superoxide dismutase activity: animal model of dosage effects in Down syndrome
    • Epstein, C.J., Avraham, K.B., Lovett, M., Smith, S., Elroy-Stein, O., Rotman, G., Bry, C., Groner, Y., Transgenic mice with increased Cu/Zn-superoxide dismutase activity: animal model of dosage effects in Down syndrome. Proc. Natl. Acad. Sci. USA 84:22 (1987), 8044–8048.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , Issue.22 , pp. 8044-8048
    • Epstein, C.J.1    Avraham, K.B.2    Lovett, M.3    Smith, S.4    Elroy-Stein, O.5    Rotman, G.6    Bry, C.7    Groner, Y.8
  • 169
    • 0023880939 scopus 로고
    • Down's syndrome: a pathology involving the lack of balance of reactive oxygen species
    • Kedziora, J., Bartosz, G., Down's syndrome: a pathology involving the lack of balance of reactive oxygen species. Free Radic. Biol. Med. 4:5 (1988), 317–330.
    • (1988) Free Radic. Biol. Med. , vol.4 , Issue.5 , pp. 317-330
    • Kedziora, J.1    Bartosz, G.2
  • 170
    • 0035882353 scopus 로고    scopus 로고
    • Influence of age on activities of antioxidant enzymes and lipid peroxidation products in erythrocytes and neutrophils of Down syndrome patients
    • Muchova, J., Sustrova, M., Garaiova, I., Liptakova, A., Blazicek, P., Kvasnicka, P., Pueschel, S., Durackova, Z., Influence of age on activities of antioxidant enzymes and lipid peroxidation products in erythrocytes and neutrophils of Down syndrome patients. Free Radic. Biol. Med. 31:4 (2001), 499–508.
    • (2001) Free Radic. Biol. Med. , vol.31 , Issue.4 , pp. 499-508
    • Muchova, J.1    Sustrova, M.2    Garaiova, I.3    Liptakova, A.4    Blazicek, P.5    Kvasnicka, P.6    Pueschel, S.7    Durackova, Z.8
  • 172
    • 0034969415 scopus 로고    scopus 로고
    • Homocysteine metabolism in children with Down syndrome: in vitro modulation
    • Pogribna, M., Melnyk, S., Pogribny, I., Chango, A., Yi, P., James, S.J., Homocysteine metabolism in children with Down syndrome: in vitro modulation. Am. J. Hum. Genet. 69:1 (2001), 88–95.
    • (2001) Am. J. Hum. Genet. , vol.69 , Issue.1 , pp. 88-95
    • Pogribna, M.1    Melnyk, S.2    Pogribny, I.3    Chango, A.4    Yi, P.5    James, S.J.6
  • 175
    • 0030876935 scopus 로고    scopus 로고
    • Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction
    • Dahl, N., Pigg, M., Ristoff, E., Gali, R., Carlsson, B., Mannervik, B., Larsson, A., Board, P., Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum. Mol. Genet. 6:7 (1997), 1147–1152.
    • (1997) Hum. Mol. Genet. , vol.6 , Issue.7 , pp. 1147-1152
    • Dahl, N.1    Pigg, M.2    Ristoff, E.3    Gali, R.4    Carlsson, B.5    Mannervik, B.6    Larsson, A.7    Board, P.8
  • 176
    • 79954617745 scopus 로고    scopus 로고
    • Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification
    • Tew, K.D., Townsend, D.M., Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification. Drug. Metab. Rev. 43:2 (2011), 179–193.
    • (2011) Drug. Metab. Rev. , vol.43 , Issue.2 , pp. 179-193
    • Tew, K.D.1    Townsend, D.M.2
  • 177
    • 34247868881 scopus 로고    scopus 로고
    • Inborn errors in the metabolism of glutathione
    • Ristoff, E., Larsson, A., Inborn errors in the metabolism of glutathione. Orphanet. J. Rare Dis., 2, 2007, 16.
    • (2007) Orphanet. J. Rare Dis. , vol.2 , pp. 16
    • Ristoff, E.1    Larsson, A.2
  • 178
    • 85024490820 scopus 로고    scopus 로고
    • Epigenetic mechanisms of the aging human retina
    • 51–51
    • DeAngelis, M., Pennington, K., Epigenetic mechanisms of the aging human retina. J. Exp. Neurosci., 9(Suppl 2), 2016 51–51.
    • (2016) J. Exp. Neurosci. , vol.9
    • DeAngelis, M.1    Pennington, K.2
  • 181
    • 67649259174 scopus 로고    scopus 로고
    • “Shock and kill” effects of class I-selective histone deacetylase inhibitors in combination with the glutathione synthesis inhibitor buthionine sulfoximine in cell line models for HIV-1 quiescence
    • Savarino, A., Mai, A., Norelli, S., El Daker, S., Valente, S., Rotili, D., Altucci, L., Palamara, A.T., Garaci, E., “Shock and kill” effects of class I-selective histone deacetylase inhibitors in combination with the glutathione synthesis inhibitor buthionine sulfoximine in cell line models for HIV-1 quiescence. Retrovirology, 6, 2009, 52.
    • (2009) Retrovirology , vol.6 , pp. 52
    • Savarino, A.1    Mai, A.2    Norelli, S.3    El Daker, S.4    Valente, S.5    Rotili, D.6    Altucci, L.7    Palamara, A.T.8    Garaci, E.9
  • 182
    • 77953995002 scopus 로고    scopus 로고
    • Covalent histone modifications – miswritten, misinterpreted and mis-erased in human cancers
    • Chi, P., Allis, C.D., Wang, G.G., Covalent histone modifications – miswritten, misinterpreted and mis-erased in human cancers. Nat. Rev. Cancer 10:7 (2010), 457–469.
    • (2010) Nat. Rev. Cancer , vol.10 , Issue.7 , pp. 457-469
    • Chi, P.1    Allis, C.D.2    Wang, G.G.3
  • 183
    • 78049317185 scopus 로고    scopus 로고
    • Aging changes the chromatin configuration and histone methylation of mouse oocytes at germinal vesicle stage
    • Manosalva, I., Gonzalez, A., Aging changes the chromatin configuration and histone methylation of mouse oocytes at germinal vesicle stage. Theriogenology 74:9 (2010), 1539–1547.
    • (2010) Theriogenology , vol.74 , Issue.9 , pp. 1539-1547
    • Manosalva, I.1    Gonzalez, A.2
  • 184
    • 84902685602 scopus 로고    scopus 로고
    • Krebs cycle intermediates regulate DNA and histone methylation: epigenetic impact on the aging process
    • Salminen, A., Kauppinen, A., Hiltunen, M., Kaarniranta, K., Krebs cycle intermediates regulate DNA and histone methylation: epigenetic impact on the aging process. Ageing Res. Rev. 16 (2014), 45–65.
    • (2014) Ageing Res. Rev. , vol.16 , pp. 45-65
    • Salminen, A.1    Kauppinen, A.2    Hiltunen, M.3    Kaarniranta, K.4
  • 186
    • 85010392496 scopus 로고    scopus 로고
    • The histone modification code in the pathogenesis of autoimmune diseases
    • 2608605-2608605
    • Araki, Y., Mimura, T., The histone modification code in the pathogenesis of autoimmune diseases. Mediat. Inflamm., 2017, 2017 2608605-2608605.
    • (2017) Mediat. Inflamm. , vol.2017
    • Araki, Y.1    Mimura, T.2
  • 187
    • 84863430482 scopus 로고    scopus 로고
    • Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine
    • Kim, H.Y., Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine. Acta Biochim. Biophys. Sin. 44:7 (2012), 623–627.
    • (2012) Acta Biochim. Biophys. Sin. , vol.44 , Issue.7 , pp. 623-627
    • Kim, H.Y.1
  • 188
    • 84925708107 scopus 로고    scopus 로고
    • Post-translational modifications of histones that influence nucleosome dynamics
    • Bowman, G.D., Poirier, M.G., Post-translational modifications of histones that influence nucleosome dynamics. Chem. Rev. 115:6 (2015), 2274–2295.
    • (2015) Chem. Rev. , vol.115 , Issue.6 , pp. 2274-2295
    • Bowman, G.D.1    Poirier, M.G.2
  • 189
    • 84867300941 scopus 로고    scopus 로고
    • Glucose depletion activates mmu-miR-466h-5p expression through oxidative stress and inhibition of histone deacetylation
    • Druz, A., Betenbaugh, M., Shiloach, J., Glucose depletion activates mmu-miR-466h-5p expression through oxidative stress and inhibition of histone deacetylation. Nucleic Acids Res. 40:15 (2012), 7291–7302.
    • (2012) Nucleic Acids Res. , vol.40 , Issue.15 , pp. 7291-7302
    • Druz, A.1    Betenbaugh, M.2    Shiloach, J.3
  • 192
    • 84900018024 scopus 로고    scopus 로고
    • Rhythmic oscillations of the microRNA miR-96-5p play a neuroprotective role by indirectly regulating glutathione levels
    • Kinoshita, C., Aoyama, K., Matsumura, N., Kikuchi-Utsumi, K., Watabe, M., Nakaki, T., Rhythmic oscillations of the microRNA miR-96-5p play a neuroprotective role by indirectly regulating glutathione levels. Nat. Commun., 5, 2014, 3823.
    • (2014) Nat. Commun. , vol.5 , pp. 3823
    • Kinoshita, C.1    Aoyama, K.2    Matsumura, N.3    Kikuchi-Utsumi, K.4    Watabe, M.5    Nakaki, T.6
  • 193
    • 77953648439 scopus 로고    scopus 로고
    • Antioxidant N-acetyl-L-cysteine ameliorates symptoms of premature aging associated with the deficiency of the circadian protein BMAL1
    • Kondratov, R.V., Vykhovanets, O., Kondratova, A.A., Antoch, M.P., Antioxidant N-acetyl-L-cysteine ameliorates symptoms of premature aging associated with the deficiency of the circadian protein BMAL1. Aging 1:12 (2009), 979–987.
    • (2009) Aging , vol.1 , Issue.12 , pp. 979-987
    • Kondratov, R.V.1    Vykhovanets, O.2    Kondratova, A.A.3    Antoch, M.P.4
  • 195
    • 1642586763 scopus 로고    scopus 로고
    • Molecular biology of 5,10-methylenetetrahydrofolate reductase
    • Fodinger, M., Horl, W.H., Sunder-Plassmann, G., Molecular biology of 5,10-methylenetetrahydrofolate reductase. J. Nephrol. 13 (2000), 20–33.
    • (2000) J. Nephrol. , vol.13 , pp. 20-33
    • Fodinger, M.1    Horl, W.H.2    Sunder-Plassmann, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.