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Volumn 5, Issue 1, 2014, Pages 52-62

New nucleophilic mechanisms of ROS-dependent epigenetic modifications: Comparison of aging and cancer

Author keywords

DNA methylation; Histone modification; Nucleophilic mechanisms; ROS

Indexed keywords


EID: 85016326735     PISSN: None     EISSN: 21525250     Source Type: Journal    
DOI: 10.14336/AD.2014.050052     Document Type: Article
Times cited : (99)

References (74)
  • 1
    • 84907181279 scopus 로고    scopus 로고
    • Nucleophilic mechanism of ROS/RNS signaling in cancer epigenetic modifications
    • Afanas'ev I (2012). Nucleophilic mechanism of ROS/RNS signaling in cancer epigenetic modifications. Am J Biomed Sci, 4: 285-306.
    • (2012) Am J Biomed Sci , vol.4 , pp. 285-306
    • Afanas'ev, I.1
  • 3
    • 7944227724 scopus 로고    scopus 로고
    • On mechanism of superoxide signaling under physiological and pathophysiological conditions
    • Afanas'ev IB (2005). On mechanism of superoxide signaling under physiological and pathophysiological conditions. Med Hypotheses, 64: 127-9.
    • (2005) Med Hypotheses , vol.64 , pp. 127-129
    • Afanas'ev, I.B.1
  • 4
    • 33645242717 scopus 로고    scopus 로고
    • Competition between superoxide and hydrogen peroxide signaling in heterolytic enzymatic processes
    • Afanas'ev IB (2006). Competition between superoxide and hydrogen peroxide signaling in heterolytic enzymatic processes. Med Hypotheses, 66: 1125-8.
    • (2006) Med Hypotheses , vol.66 , pp. 1125-1128
    • Afanas'ev, I.B.1
  • 5
    • 35848932278 scopus 로고    scopus 로고
    • Signaling functions of free radicals superoxide & nitric oxide under physiological & pathological conditions
    • Afanas'ev IB (2007). Signaling functions of free radicals superoxide & nitric oxide under physiological & pathological conditions. Mol Biotechnol, 37: 2-4.
    • (2007) Mol Biotechnol , vol.37 , pp. 2-4
    • Afanas'ev, I.B.1
  • 6
    • 84877093000 scopus 로고    scopus 로고
    • Balancing reactive oxygen species in the epigenome: NADPH oxidases as target and perpetrator
    • Nov 5
    • Hayes P, Knaus UG (2012). Balancing reactive oxygen species in the epigenome: NADPH oxidases as target and perpetrator. Antioxid Redox Signal, Nov 5.
    • (2012) Antioxid Redox Signal
    • Hayes, P.1    Knaus, U.G.2
  • 7
    • 84863206202 scopus 로고    scopus 로고
    • Norepinephrine causes epigenetic repression of PKC [varepsilon] gene in rodent hearts by activating Nox1-dependent reactive oxygen species production
    • Xiong F, Xiao D, Zhang L (2012). Norepinephrine causes epigenetic repression of PKC [varepsilon] gene in rodent hearts by activating Nox1-dependent reactive oxygen species production. FASEB J, 26: 2753-63.
    • (2012) FASEB J , vol.26 , pp. 2753-2763
    • Xiong, F.1    Xiao, D.2    Zhang, L.3
  • 8
    • 84862950110 scopus 로고    scopus 로고
    • Hypoxia-derived oxidative stress mediates epigenetic repression of PKCe gene in foetal rat hearts
    • Patterson AJ, Xiao D, Xiong F, Dixon B, Zhang (2012). Hypoxia-derived oxidative stress mediates epigenetic repression of PKCe gene in foetal rat hearts. Cardiovasc Res, 93: 302-10.
    • (2012) Cardiovasc Res , vol.93 , pp. 302-310
    • Patterson, A.J.1    Xiao, D.2    Xiong, F.3    Dixon, B.Z.4
  • 10
    • 84859987864 scopus 로고    scopus 로고
    • Reactive oxygen species in cancer: Comparison with aging
    • Afanas'ev I (2011). Reactive oxygen species in cancer: Comparison with aging. Aging & Disease, 2: 219-30.
    • (2011) Aging & Disease , vol.2 , pp. 219-230
    • Afanas'ev, I.1
  • 11
    • 57249103576 scopus 로고    scopus 로고
    • Epigenetic changes induced by reactive oxygen species in hepatocellular carcinoma: methylation of the E-cadherin promoter
    • Lim SO, Gu LM, Kim MS, Kim HS, Park JN, Park CK, Cho JW, Park YM, Jung G (2008). Epigenetic changes induced by reactive oxygen species in hepatocellular carcinoma: methylation of the E-cadherin promoter. Gastroenterology,135: 2128-40.
    • (2008) Gastroenterology , vol.135 , pp. 2128-2140
    • Lim, S.O.1    Gu, L.M.2    Kim, M.S.3    Kim, H.S.4    Park, J.N.5    Park, C.K.6    Cho, J.W.7    Park, Y.M.8    Jung, G.9
  • 13
    • 77952959173 scopus 로고    scopus 로고
    • Downregulation of catalase by reactive oxygen species via hypermethylation of CpG island II on the catalase promoter
    • Min JY, Lim SO, Jung G (2010). Downregulation of catalase by reactive oxygen species via hypermethylation of CpG island II on the catalase promoter. FEBS Lett, 584: 2427-32.
    • (2010) FEBS Lett , vol.584 , pp. 2427-2432
    • Min, J.Y.1    Lim, S.O.2    Jung, G.3
  • 14
    • 84860269756 scopus 로고    scopus 로고
    • Epigenetic changes induced by oxidative stress in colorectal cancer cells: methylation of tumor suppressor RUNX3
    • Kang KA, Zhang R, Kim GY, Bae SC, Hyun JW (2012). Epigenetic changes induced by oxidative stress in colorectal cancer cells: methylation of tumor suppressor RUNX3. Tumour Biol, 33: 403-12.
    • (2012) Tumour Biol , vol.33 , pp. 403-412
    • Kang, K.A.1    Zhang, R.2    Kim, G.Y.3    Bae, S.C.4    Hyun, J.W.5
  • 18
    • 84867340549 scopus 로고    scopus 로고
    • Silencing of glutathione peroxidase 3 through DNA hypermethylation is associated with lymph node metastasis in gastric carcinomas
    • Peng DF, Hu TL, Schneider BG, Chen Z, Xu ZK, El-Rifai W (2012). Silencing of glutathione peroxidase 3 through DNA hypermethylation is associated with lymph node metastasis in gastric carcinomas. PloS One,7: e46214.
    • (2012) PloS One , vol.7
    • Peng, D.F.1    Hu, T.L.2    Schneider, B.G.3    Chen, Z.4    Xu, Z.K.5    El-Rifai, W.6
  • 19
    • 84878660136 scopus 로고    scopus 로고
    • Oxidative stress causes epigenetic alteration SDX1 expression in colorectal cancer cells
    • Zhang R, Kang KA, Kim KC, Na SY, Chang WY, Kim GY, Kim HS, Hyun JW (2013). Oxidative stress causes epigenetic alteration SDX1 expression in colorectal cancer cells. Gene, 524: 214-9.
    • (2013) Gene , vol.524 , pp. 214-219
    • Zhang, R.1    Kang, K.A.2    Kim, K.C.3    Na, S.Y.4    Chang, W.Y.5    Kim, G.Y.6    Kim, H.S.7    Hyun, J.W.8
  • 20
    • 39449091629 scopus 로고    scopus 로고
    • Silencing of DUOX NADPH oxidases by promoter hypermethylation in lung cancer
    • Luxen S, Belinsky SA, Knaus UG (2008). Silencing of DUOX NADPH oxidases by promoter hypermethylation in lung cancer. Cancer Res, 68: 1037-45.
    • (2008) Cancer Res , vol.68 , pp. 1037-1045
    • Luxen, S.1    Belinsky, S.A.2    Knaus, U.G.3
  • 22
    • 84862758303 scopus 로고    scopus 로고
    • Involvement of insulin-induced reversible chromatin remodeling in altering the expression of oxidative stress-responsible genes under hyperglycemia in 3T3-L1 preadipocytes
    • Gupta J, Kikoo (2012). Involvement of insulin-induced reversible chromatin remodeling in altering the expression of oxidative stress-responsible genes under hyperglycemia in 3T3-L1 preadipocytes. Gene, 504:181-91.
    • (2012) Gene , vol.504 , pp. 181-191
    • Gupta, J.K.1
  • 26
    • 52949144622 scopus 로고    scopus 로고
    • DNA methylation: its role in cancer development and therapy
    • Kurkjian C, Kummar S, Murgo AJ (2008). DNA methylation: its role in cancer development and therapy. Curr Probl Cancer, 32:187-235.
    • (2008) Curr Probl Cancer , vol.32 , pp. 187-235
    • Kurkjian, C.1    Kummar, S.2    Murgo, A.J.3
  • 27
    • 80052037691 scopus 로고    scopus 로고
    • Epigenetic regulation of caloric restriction in aging
    • Li Y, Daniel M, Tollefsbol TO (2011). Epigenetic regulation of caloric restriction in aging. BMC Med, 9: 98.
    • (2011) BMC Med , vol.9 , pp. 98
    • Li, Y.1    Daniel, M.2    Tollefsbol, T.O.3
  • 28
    • 40949142846 scopus 로고    scopus 로고
    • Mechanisms underlying caloric restriction and lifespan regulation: implications for vascular aging
    • Ungvari Z, Parrado-Fernandez C, Csiszar A, de Cabo R (2008). Mechanisms underlying caloric restriction and lifespan regulation: implications for vascular aging. Circ Res,102: 519-28.
    • (2008) Circ Res , vol.102 , pp. 519-528
    • Ungvari, Z.1    Parrado-Fernandez, C.2    Csiszar, A.3    de Cabo, R.4
  • 29
    • 80052037691 scopus 로고    scopus 로고
    • Epigenetic regulation of caloric restriction in aging
    • Li Y, Daniel M, Tollefsbol TO (2011). Epigenetic regulation of caloric restriction in aging. BMC Med, 9: 98.
    • (2011) BMC Med , vol.9 , pp. 98
    • Li, Y.1    Daniel, M.2    Tollefsbol, T.O.3
  • 30
    • 85019172173 scopus 로고    scopus 로고
    • Honeybeers and cells lines as models of DNA methylation and aging in response to diet
    • Ford D (2012). Honeybeers and cells lines as models of DNA methylation and aging in response to diet. Exp Gerontol, pii: S0531-5565(12) 00200-8.
    • (2012) Exp Gerontol
    • Ford, D.1
  • 32
    • 0036066957 scopus 로고    scopus 로고
    • Oxidative stress and TNF-alpha induce histone acetylation and NF-kappaB/AP-1 activation in alveolar epithelial cells: potential mechanism in gene transcription in lung inflammation
    • Rahman I, Gilmour PS, Jimenez LA, MacNee W (2002). Oxidative stress and TNF-alpha induce histone acetylation and NF-kappaB/AP-1 activation in alveolar epithelial cells: potential mechanism in gene transcription in lung inflammation. Mol Cell Biochem, 234-235 (1-2): 239-48.
    • (2002) Mol Cell Biochem , vol.234-235 , Issue.1-2 , pp. 239-248
    • Rahman, I.1    Gilmour, P.S.2    Jimenez, L.A.3    MacNee, W.4
  • 33
    • 0037372312 scopus 로고    scopus 로고
    • Histone acetylation regulates epithelial IL-8 release mediated by oxidative stress from environmental particles
    • Gilmour PS, Rahman I, Donaldson K, MacNee W(2003). Histone acetylation regulates epithelial IL-8 release mediated by oxidative stress from environmental particles. Am J Physiol Lung Cell Mol. Physiol, 284: L533-40.
    • (2003) Am J Physiol Lung Cell Mol. Physiol , vol.284 , pp. L533-L540
    • Gilmour, P.S.1    Rahman, I.2    Donaldson, K.3    MacNee, W.4
  • 34
    • 0037423725 scopus 로고    scopus 로고
    • The effect of oxidative stress on histone acetylation and IL-8 release
    • Tomita K, Barnes PJ, Adcock IM (2003). The effect of oxidative stress on histone acetylation and IL-8 release. Biochem Biophys Res Commun, 301: 572-7.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 572-577
    • Tomita, K.1    Barnes, P.J.2    Adcock, I.M.3
  • 35
    • 35548943647 scopus 로고    scopus 로고
    • Thalidomide induces gamma-globin gene expression through increased reactive oxygen species-mediated p38 MAPK signaling and histone H4 acetylation in adult erythropoiesis
    • Aerbajinai W, Zhu J, Gao Z, Chin K, Rodgers GP (2007). Thalidomide induces gamma-globin gene expression through increased reactive oxygen species-mediated p38 MAPK signaling and histone H4 acetylation in adult erythropoiesis. Blood, 110: 2864-71.
    • (2007) Blood , vol.110 , pp. 2864-2871
    • Aerbajinai, W.1    Zhu, J.2    Gao, Z.3    Chin, K.4    Rodgers, G.P.5
  • 36
    • 84867300941 scopus 로고    scopus 로고
    • Glucose depletion activates mmu-miR-4661-5p expression though oxidative stress and inhibition histone deacetylation
    • Druz A, Betenbaugh M, Shiloach J (2012). Glucose depletion activates mmu-miR-4661-5p expression though oxidative stress and inhibition histone deacetylation. Nucleic Acids Res, 40: 7291-7302.
    • (2012) Nucleic Acids Res , vol.40 , pp. 7291-7302
    • Druz, A.1    Betenbaugh, M.2    Shiloach, J.3
  • 37
    • 77956652170 scopus 로고    scopus 로고
    • Evidence for the role of oxidative stress in the acetylation of histone H3 by ethanol in rat hepatocytes
    • Choudhury M, Park PH, Jackson D, Shukla SD (2010). Evidence for the role of oxidative stress in the acetylation of histone H3 by ethanol in rat hepatocytes. Alcohol, 44: 531-40.
    • (2010) Alcohol , vol.44 , pp. 531-540
    • Choudhury, M.1    Park, P.H.2    Jackson, D.3    Shukla, S.D.4
  • 38
    • 79951941912 scopus 로고    scopus 로고
    • GCN5 regulates the superoxide-generating system in leukocytes via controlling gp91-phox gene expression
    • Kikuchi H, Kuribayashi F, Kiwaki, Takami Y, Nakayama T (2011). GCN5 regulates the superoxide-generating system in leukocytes via controlling gp91-phox gene expression. J Immunol, 186: 3015-3022.
    • (2011) J Immunol , vol.186 , pp. 3015-3022
    • Kikuchi, H.1    Kuribayashi, F.K.2    Takami, Y.3    Nakayama, T.4
  • 39
    • 14044255703 scopus 로고    scopus 로고
    • Oxidative stress is involved in inhibition of copper on histone acetylation in cells
    • Lin C, Kang J, Zheng R (2005). Oxidative stress is involved in inhibition of copper on histone acetylation in cells. Chem Biol Interact,151:167-76.
    • (2005) Chem Biol Interact , vol.151 , pp. 167-176
    • Lin, C.1    Kang, J.2    Zheng, R.3
  • 40
    • 0042591402 scopus 로고    scopus 로고
    • Nickel-induced hypoacetylation: the role of reactive oxygen species
    • Kang J, Zhang Y, Chen J, Chen H, Lin C, Wang Q, Ou Y (2003). Nickel-induced hypoacetylation: the role of reactive oxygen species. Toxicol Sci,74: 279-86.
    • (2003) Toxicol Sci , vol.74 , pp. 279-286
    • Kang, J.1    Zhang, Y.2    Chen, J.3    Chen, H.4    Lin, C.5    Wang, Q.6    Ou, Y.7
  • 41
    • 15744370742 scopus 로고    scopus 로고
    • Curcumin-induced histone hypoacetylation: the role of reactive oxygen species
    • Kang J, Chen J, Shi Y, Jia J, Zhang Y (2005). Curcumin-induced histone hypoacetylation: the role of reactive oxygen species. Biochem Pharmacol, 69: 1205-13.
    • (2005) Biochem Pharmacol , vol.69 , pp. 1205-1213
    • Kang, J.1    Chen, J.2    Shi, Y.3    Jia, J.4    Zhang, Y.5
  • 42
    • 84859643953 scopus 로고    scopus 로고
    • Anti-leukemia activity of chaetocin via death receptor-dependent apoptosis and dual modulation of the histone methyltransferase SUV39H1
    • Chaib H, Nebbioso A, Prebet T, Castellano R, Garbit S, Restouin A, Vey N, Altucci L, Collette Y (2012). Anti-leukemia activity of chaetocin via death receptor-dependent apoptosis and dual modulation of the histone methyltransferase SUV39H1. Leukemia, 26: 662-74.
    • (2012) Leukemia , vol.26 , pp. 662-674
    • Chaib, H.1    Nebbioso, A.2    Prebet, T.3    Castellano, R.4    Garbit, S.5    Restouin, A.6    Vey, N.7    Altucci, L.8    Collette, Y.9
  • 43
    • 69449107940 scopus 로고    scopus 로고
    • Histone deacetylase-2 is a key regulator of diabetes-and transforming growth factor-beta1-induced renal injury
    • Noh H, Oh EY, Seo JY, Yu MR, Kim YO, Ha H, Lee HB (2009). Histone deacetylase-2 is a key regulator of diabetes-and transforming growth factor-beta1-induced renal injury. Am J Physiol Renal Physiol, 297: F729-39.
    • (2009) Am J Physiol Renal Physiol , vol.297 , pp. F729-F739
    • Noh, H.1    Oh, E.Y.2    Seo, J.Y.3    Yu, M.R.4    Kim, Y.O.5    Ha, H.6    Lee, H.B.7
  • 44
    • 58149359833 scopus 로고    scopus 로고
    • Oxidative stress causes IL8 promoter hyperacetylation in cystic fibrosis airway cell models
    • Bartling TR, Drumm ML (2009). Oxidative stress causes IL8 promoter hyperacetylation in cystic fibrosis airway cell models. Am J Respir Cell Mol Biol, 40, 58-65.
    • (2009) Am J Respir Cell Mol Biol , vol.40 , pp. 58-65
    • Bartling, T.R.1    Drumm, M.L.2
  • 45
    • 15744370742 scopus 로고    scopus 로고
    • Curcumin-induced histone hypoacetylation: the role of reactive oxygen species
    • Kang J, Chen J, Shi Y, Jia J, Zhang Y (2005). Curcumin-induced histone hypoacetylation: the role of reactive oxygen species. Biochem Pharmacol, 69: 1205-13.
    • (2005) Biochem Pharmacol , vol.69 , pp. 1205-1213
    • Kang, J.1    Chen, J.2    Shi, Y.3    Jia, J.4    Zhang, Y.5
  • 46
    • 33845340834 scopus 로고    scopus 로고
    • Chronic protein kinase B (PKB/c-akt) activation leads to apoptosis induced by oxidative stress-mediated Foxo3a transcriptional up-regulation
    • Van Gorp AGM, Pomeranz KM, Birkenkamp KU, Hui RC-Y, Lam EW-F, Coffer PJ (2006). Chronic protein kinase B (PKB/c-akt) activation leads to apoptosis induced by oxidative stress-mediated Foxo3a transcriptional up-regulation. Cancer Res, 66: 10760 - 9.
    • (2006) Cancer Res , vol.66 , pp. 10760-10769
    • Van Gorp, A.G.M.1    Pomeranz, K.M.2    Birkenkamp, K.U.3    Hui, R.C-Y.4    Lam, E.W-F.5    Coffer, P.J.6
  • 48
    • 84864389133 scopus 로고    scopus 로고
    • Involvement of the up-regulated FoxO1 expression in follicular granulosa cell apoptosis induced by oxidative stress
    • Shen M, Lin F, Zhang J, Tang Y, Chen W-K, Liu H (2012). Involvement of the up-regulated FoxO1 expression in follicular granulosa cell apoptosis induced by oxidative stress. J Biol Chem, 287: 25727-40.
    • (2012) J Biol Chem , vol.287 , pp. 25727-25740
    • Shen, M.1    Lin, F.2    Zhang, J.3    Tang, Y.4    Chen, W-K.5    Liu, H.6
  • 50
    • 79953186624 scopus 로고    scopus 로고
    • FoxO transcription factors promote cardiomyocyte survival upon induction of oxidative stress
    • Sengupta A, Molkentin JD, Paik J-H, DePinho RA, Yutzey KE (2011). FoxO transcription factors promote cardiomyocyte survival upon induction of oxidative stress. J Biol Chem, 286: 7468 - 78.
    • (2011) J Biol Chem , vol.286 , pp. 7468-7478
    • Sengupta, A.1    Molkentin, J.D.2    Paik, J-H.3    DePinho, R.A.4    Yutzey, K.E.5
  • 53
    • 84860743760 scopus 로고    scopus 로고
    • FOXOs and sirtuins in vascular growth, maintenance, and aging
    • Oellerich MF, Potente M (2012). FOXOs and sirtuins in vascular growth, maintenance, and aging. Circ Res,110: 1238-51.
    • (2012) Circ Res , vol.110 , pp. 1238-1251
    • Oellerich, M.F.1    Potente, M.2
  • 55
    • 79957979314 scopus 로고    scopus 로고
    • Tumor suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Chen Y, Zhang J, Lin Y, Lei Q, Guan KL, Zhao S, Xiong (2011). Tumor suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep,12: 534-41.
    • (2011) EMBO Rep , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5    Zhao, S.X.6
  • 56
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang F, Nguyen M, Qin FX, Tong Q (2007). SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell, 6: 505-14.
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 57
    • 79959541505 scopus 로고    scopus 로고
    • Acetylation of MnSOD directs enzymatic activity responding to cellular nutrition status or oxidative stress
    • Miller O, Park SH, KIM HS, Jiang H, Coleman MC, Spitz DR, Gius D (2011). Acetylation of MnSOD directs enzymatic activity responding to cellular nutrition status or oxidative stress. Aging (Albany NY), 3: 102-7.
    • (2011) Aging (Albany NY) , vol.3 , pp. 102-107
    • Miller, O.1    Park, S.H.2    K.I.M, H.S.3    Jiang, H.4    Coleman, M.C.5    Spitz, D.R.6    Gius, D.7
  • 58
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu X, Brown K, Hirschey MD, Verdin E, Chen D (2010). Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab 2010; 12: 662-667.
    • (2010) Cell Metab 2010 , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 59
    • 80053007221 scopus 로고    scopus 로고
    • The regulation of aging and longevity: a new and complex role of p53
    • Feng Z, Lin M, Wu R (2011). The regulation of aging and longevity: a new and complex role of p53. Genes & Cancer, 2: 443-52.
    • (2011) Genes & Cancer , vol.2 , pp. 443-452
    • Feng, Z.1    Lin, M.2    Wu, R.3
  • 60
    • 80052762810 scopus 로고    scopus 로고
    • High-fat diet increases and the polyphenol, S17834, decreases acetylation of the sirtuin-1-dependent lysine-382 on p53 and apoptotic signaling in atherosclerotic lesion-prone aortic endothelium of normal mice
    • Xu S, Jiang B, Shi C, Bachschmid MM, Zang M, Verbeuren tJ, Cohen RA (2011). High-fat diet increases and the polyphenol, S17834, decreases acetylation of the sirtuin-1-dependent lysine-382 on p53 and apoptotic signaling in atherosclerotic lesion-prone aortic endothelium of normal mice. J Cardiovasc Pharmacol, 58: 263-271.
    • (2011) J Cardiovasc Pharmacol , vol.58 , pp. 263-271
    • Xu, S.1    Jiang, B.2    Shi, C.3    Bachschmid, M.M.4    Zang, M.5    Verbeuren, tJ.6    Cohen, R.A.7
  • 61
    • 80855144458 scopus 로고    scopus 로고
    • "Relax and Repair" to restrain aging
    • Krishnan V, Liu B, Zhou Z (2011). "Relax and Repair" to restrain aging. Aging (Albany NY), 3: 943-54.
    • (2011) Aging (Albany NY) , vol.3 , pp. 943-954
    • Krishnan, V.1    Liu, B.2    Zhou, Z.3
  • 63
    • 79959506318 scopus 로고    scopus 로고
    • Acetylation of H4K12 in porcine oocytes during in vitro aging: potential role of ooplasmic reactive oxygen species
    • Cui MS, Wang XL, Tang DW, Zhang J, Liu Y, Zeng SM (2011). Acetylation of H4K12 in porcine oocytes during in vitro aging: potential role of ooplasmic reactive oxygen species. Theriogenology, 75: 638-46.
    • (2011) Theriogenology , vol.75 , pp. 638-646
    • Cui, M.S.1    Wang, X.L.2    Tang, D.W.3    Zhang, J.4    Liu, Y.5    Zeng, S.M.6
  • 64
    • 84871367411 scopus 로고    scopus 로고
    • Preventive effects of epigallocatechin-3-o-gallate against replicative senescence associated with p53 acetylation in human dermal fibroblasts
    • Han DW, Lee MH, Kim B, Lee JJ, Hyon SH, Park JC (2012). Preventive effects of epigallocatechin-3-o-gallate against replicative senescence associated with p53 acetylation in human dermal fibroblasts. Oxid Med Cell Longev, Article ID 850684, 13 pages.
    • (2012) Oxid Med Cell Longev , pp. 13
    • Han, D.W.1    Lee, M.H.2    Kim, B.3    Lee, J.J.4    Hyon, S.H.5    Park, J.C.6
  • 65
    • 84875291091 scopus 로고    scopus 로고
    • Resveratrol induces premature senescence in lung cancer cells via ROS-mediated DNA damage
    • Luo H, Yang A, Schulte BA, Wargovich MJ, Wang GY (2013). Resveratrol induces premature senescence in lung cancer cells via ROS-mediated DNA damage. PLoS One, 8: e60065.
    • (2013) PLoS One , vol.8
    • Luo, H.1    Yang, A.2    Schulte, B.A.3    Wargovich, M.J.4    Wang, G.Y.5
  • 66
    • 78149465728 scopus 로고    scopus 로고
    • Epigenetic enhancement of p66She during cellular replicative or premature senescence
    • Zhang W, Ji W, Yang L, Xu Y, Yang J, Zhuang Z (2010). Epigenetic enhancement of p66She during cellular replicative or premature senescence. Toxicology, 278:189-94.
    • (2010) Toxicology , vol.278 , pp. 189-194
    • Zhang, W.1    Ji, W.2    Yang, L.3    Xu, Y.4    Yang, J.5    Zhuang, Z.6
  • 67
    • 0023176797 scopus 로고
    • Kinetic and catalytic mechanism of HhaI methyltransferase
    • Wu LC, Santi DV (1987). Kinetic and catalytic mechanism of HhaI methyltransferase. J Biol Chem, 262: 4778-86.
    • (1987) J Biol Chem , vol.262 , pp. 4778-4786
    • Wu, L.C.1    Santi, D.V.2
  • 68
    • 0035877609 scopus 로고    scopus 로고
    • The mechanism of DNA cytosine-5 methylation. Kinetic and mutational dissection of hhai methyltransferase
    • Vilkaitis G, Merkiene E, Serva S, Weinhold E, Klimauskas S (2001). The mechanism of DNA cytosine-5 methylation. Kinetic and mutational dissection of hhai methyltransferase. J Biol Chem, 276: 20924-34.
    • (2001) J Biol Chem , vol.276 , pp. 20924-20934
    • Vilkaitis, G.1    Merkiene, E.2    Serva, S.3    Weinhold, E.4    Klimauskas, S.5
  • 69
    • 79956001873 scopus 로고    scopus 로고
    • Direct observation of cytosine flipping and covalent catalysis in a DNA methyltransferase
    • Gerasimaite R, Merkiene E, Klimasauskas S (2011). Direct observation of cytosine flipping and covalent catalysis in a DNA methyltransferase. Nucleic Acids Res, 39: 377-80.
    • (2011) Nucleic Acids Res , vol.39 , pp. 377-380
    • Gerasimaite, R.1    Merkiene, E.2    Klimasauskas, S.3
  • 70
    • 0033603555 scopus 로고    scopus 로고
    • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
    • Tanner KG, Trievel RC, Kuo M-H, Howard RM, Berger SL, Allis CD, Marmorstein, Denu JM (1999). Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator. J Biol Chem, 274: 18157-60.
    • (1999) J Biol Chem , vol.274 , pp. 18157-18160
    • Tanner, K.G.1    Trievel, R.C.2    Kuo, M.-H.3    Howard, R.M.4    Berger, S.L.5    Allis, C.D.6    Marmorstein, D.J.M.7
  • 73
    • 84867174932 scopus 로고    scopus 로고
    • Enhanced free radical status of cancer cells: Success and failure of prooxidant/antioxidant treatment, Current Signal Transduction Therapy
    • Afanas'ev I (2012). Enhanced free radical status of cancer cells: Success and failure of prooxidant/antioxidant treatment, Current Signal Transduction Therapy, 7: 228-36.
    • (2012) , vol.7 , pp. 228-236
    • Afanas'ev, I.1
  • 74
    • 63849285200 scopus 로고    scopus 로고
    • Superoxide and nitric oxide in senescence and aging
    • Afanas'ev I (2009). Superoxide and nitric oxide in senescence and aging. Front Biosci. 14: 3899-912.
    • (2009) Front Biosci , vol.14 , pp. 3899-3912
    • Afanas'ev, I.1


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