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Volumn 19, Issue 9, 2013, Pages 1753-1764

Metallothioneins, ageing and cellular senescence: A future therapeutic target

Author keywords

Ageing; Cellular senescence; Inflammation; Metallothioneins; MT target therapeutic approach

Indexed keywords

HOMOCYSTEINE; METALLOTHIONEIN;

EID: 84876735812     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161213805219595     Document Type: Article
Times cited : (28)

References (175)
  • 1
    • 13944262937 scopus 로고    scopus 로고
    • Understanding the odd science of aging
    • Kirkwood TB. Understanding the odd science of aging. Cell 2005; 120: 437-47.
    • (2005) Cell , vol.120 , pp. 437-447
    • Kirkwood, T.B.1
  • 2
    • 34249672703 scopus 로고    scopus 로고
    • Biological aging is no longer an unsolved problem
    • Hayflick L. Biological aging is no longer an unsolved problem. Ann N Y Acad Sci 2007; 1100: 1-13.
    • (2007) Ann N Y Acad Sci , vol.1100 , pp. 1-13
    • Hayflick, L.1
  • 3
    • 78649350746 scopus 로고    scopus 로고
    • The aging stress response
    • Haigis MC, Yankner BA. The aging stress response. Mol Cell 2010; 40: 333-44.
    • (2010) Mol Cell , vol.40 , pp. 333-344
    • Haigis, M.C.1    Yankner, B.A.2
  • 4
    • 79952260454 scopus 로고    scopus 로고
    • The DNA damage response: Balancing the scale between cancer and ageing
    • Seviour EG, Lin SY. The DNA damage response: Balancing the scale between cancer and ageing. Aging (Albany NY) 2010; 2: 900-7.
    • (2010) Aging (Albany NY) , vol.2 , pp. 900-907
    • Seviour, E.G.1    Lin, S.Y.2
  • 5
    • 64949135819 scopus 로고    scopus 로고
    • Does damage to DNA and other macromolecules play a role in aging? If so, how?
    • Campisi J, Vijg J. Does damage to DNA and other macromolecules play a role in aging? If so, how? J Gerontol A Biol Sci Med Sci 2009; 64: 175-8.
    • (2009) J Gerontol A Biol Sci Med Sci , vol.64 , pp. 175-178
    • Campisi, J.1    Vijg, J.2
  • 6
    • 79251498807 scopus 로고    scopus 로고
    • Protein homeostasis and aging: The importance of exquisite quality control
    • Koga H, Kaushik S, Cuervo AM. Protein homeostasis and aging: The importance of exquisite quality control. Ageing Res Rev 2011; 10: 205-15.
    • (2011) Ageing Res Rev , vol.10 , pp. 205-215
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 7
    • 77956362155 scopus 로고    scopus 로고
    • Protein homeostasis and aging in neurodegeneration
    • Douglas PM, Dillin A. Protein homeostasis and aging in neurodegeneration. J Cell Biol 2010; 190: 719-29.
    • (2010) J Cell Biol , vol.190 , pp. 719-729
    • Douglas, P.M.1    Dillin, A.2
  • 8
    • 34548186667 scopus 로고    scopus 로고
    • Cellular senescence: When bad things happen to good cells
    • Campisi J, d'Adda di Fagagna F. Cellular senescence: when bad things happen to good cells. Nat Rev Mol Cell Biol 2007; 8: 729-40.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 729-740
    • Campisi, J.1    d'Adda di Fagagna, F.2
  • 9
    • 0029060897 scopus 로고
    • The function of metallothionein
    • Vallee BL. The function of metallothionein. Neurochem Int 1995; 27: 23-33.
    • (1995) Neurochem Int , vol.27 , pp. 23-33
    • Vallee, B.L.1
  • 10
    • 0034578489 scopus 로고    scopus 로고
    • Zinc, metallothioneins, immune responses, survival and ageing
    • Mocchegiani E, Muzzioli M, Giacconi R. Zinc, metallothioneins, immune responses, survival and ageing. Biogerontology 2000; 1: 133-43.
    • (2000) Biogerontology , vol.1 , pp. 133-143
    • Mocchegiani, E.1    Muzzioli, M.2    Giacconi, R.3
  • 11
    • 34848847551 scopus 로고    scopus 로고
    • Dual nanomolar and picomolar Zn(II) binding properties of metallothionein
    • Krezel A, Maret W. Dual nanomolar and picomolar Zn(II) binding properties of metallothionein. J Am Chem Soc 2007;129:10911-21.
    • (2007) J Am Chem Soc , vol.129 , pp. 10911-10921
    • Krezel, A.1    Maret, W.2
  • 12
    • 0021944046 scopus 로고
    • Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals
    • Thornalley PJ, Vasák M. Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim Biophys Acta 1985; 827: 36-44.
    • (1985) Biochim Biophys Acta , vol.827 , pp. 36-44
    • Thornalley, P.J.1    Vasák, M.2
  • 13
    • 34548512038 scopus 로고    scopus 로고
    • Cellular zinc and redox buffering capacity of metallothionein/thionein in health and disease
    • Maret W, Krezel A. Cellular zinc and redox buffering capacity of metallothionein/thionein in health and disease. Mol Med 2007; 13: 371-5.
    • (2007) Mol Med , vol.13 , pp. 371-375
    • Maret, W.1    Krezel, A.2
  • 15
    • 33947276403 scopus 로고    scopus 로고
    • Different redox states of metallothionein/ thionein in biological tissue
    • Krezel A, Maret W. Different redox states of metallothionein/ thionein in biological tissue. Biochem J 2007; 402: 551-8.
    • (2007) Biochem J , vol.402 , pp. 551-558
    • Krezel, A.1    Maret, W.2
  • 16
    • 0036239958 scopus 로고    scopus 로고
    • Recent studies on metallothionein: Protection against toxicity of heavy metals and oxygen free radicals
    • Sato M, Kondoh M. Recent studies on metallothionein: protection against toxicity of heavy metals and oxygen free radicals. Tohoku J Exp Med 2002;196: 9-22.
    • (2002) Tohoku J Exp Med , vol.196 , pp. 9-22
    • Sato, M.1    Kondoh, M.2
  • 17
    • 0030711622 scopus 로고    scopus 로고
    • Metallothionein accretion in human hepatic cells is linked to cellular proliferation
    • Studer R, Vogt CP, Cavigelli M, Hunziker PE, Kägi JH. Metallothionein accretion in human hepatic cells is linked to cellular proliferation. Biochem J 1997; 328: 63-7.
    • (1997) Biochem J , vol.328 , pp. 63-67
    • Studer, R.1    Vogt, C.P.2    Cavigelli, M.3    Hunziker, P.E.4    Kägi, J.H.5
  • 18
    • 0034213058 scopus 로고    scopus 로고
    • Zinc and immunoresistance to infection in aging: New biological tools
    • Mocchegiani E, Muzzioli M, Giacconi R. Zinc and immunoresistance to infection in aging: new biological tools. Trends Pharmacol Sci 2000; 21: 205-8.
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 205-208
    • Mocchegiani, E.1    Muzzioli, M.2    Giacconi, R.3
  • 19
    • 3042738968 scopus 로고    scopus 로고
    • Metal-responsive transcription factor-1 (MTF-1) is essential for embryonic liver development and heavy metal detoxification in the adult liver
    • Wang Y, Wimmer U, Lichtlen P, et al. Metal-responsive transcription factor-1 (MTF-1) is essential for embryonic liver development and heavy metal detoxification in the adult liver. FASEB J 2004; 18: 1071-79.
    • (2004) FASEB J , vol.18 , pp. 1071-1079
    • Wang, Y.1    Wimmer, U.2    Lichtlen, P.3
  • 20
    • 0035283151 scopus 로고    scopus 로고
    • The transcription factors MTF-1 and USF1 cooperate to regulate mouse metallothionein-I expression in response to the essential metal zinc in visceral endoderm cells during early development
    • Andrews GK, Lee DK, Ravindra R, et al. The transcription factors MTF-1 and USF1 cooperate to regulate mouse metallothionein-I expression in response to the essential metal zinc in visceral endoderm cells during early development. EMBO J 2001; 20: 1114-22.
    • (2001) EMBO J , vol.20 , pp. 1114-1122
    • Andrews, G.K.1    Lee, D.K.2    Ravindra, R.3
  • 22
    • 0016805058 scopus 로고
    • The induction of metallothionein in rat liver by zinc injection and restriction of food intake
    • Bremner I, Davies NT. The induction of metallothionein in rat liver by zinc injection and restriction of food intake. Biochem J 1975; 149: 733-38.
    • (1975) Biochem J , vol.149 , pp. 733-738
    • Bremner, I.1    Davies, N.T.2
  • 23
    • 0033990794 scopus 로고    scopus 로고
    • Regulation of metallothionein gene expression by oxidative stress and metal ions
    • Andrews GK. Regulation of metallothionein gene expression by oxidative stress and metal ions. Biochem Pharmacol 2000; 59: 95-104.
    • (2000) Biochem Pharmacol , vol.59 , pp. 95-104
    • Andrews, G.K.1
  • 24
    • 33645767663 scopus 로고    scopus 로고
    • Metallothionein isoform 2A expression is inducible and protects against ROS-mediated cell death in rotenone-treated HeLa cells
    • Reinecke F, Levanets O, Olivier Y, et al. Metallothionein isoform 2A expression is inducible and protects against ROS-mediated cell death in rotenone-treated HeLa cells. Biochem J 2006; 395: 405-15.
    • (2006) Biochem J , vol.395 , pp. 405-415
    • Reinecke, F.1    Levanets, O.2    Olivier, Y.3
  • 25
    • 42049101604 scopus 로고    scopus 로고
    • Metallothionein redox biology in the cytoprotective and cytotoxic functions of zinc
    • Maret W. Metallothionein redox biology in the cytoprotective and cytotoxic functions of zinc. Exp Gerontol 2008; 43: 363-69.
    • (2008) Exp Gerontol , vol.43 , pp. 363-369
    • Maret, W.1
  • 26
    • 0028351149 scopus 로고
    • Nitric oxide destroys zinc-sulfur clusters inducing zinc release from metallothionein and inhibition of the zinc finger-type yeast transcription activator LAC9
    • Kröncke KD, Fehsel K, Schmidt T, et al. Nitric oxide destroys zinc-sulfur clusters inducing zinc release from metallothionein and inhibition of the zinc finger-type yeast transcription activator LAC9. Biochem Biophys Res Commun 1994; 200: 1105-10.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 1105-1110
    • Kröncke, K.D.1    Fehsel, K.2    Schmidt, T.3
  • 27
    • 0037008050 scopus 로고    scopus 로고
    • S-nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation
    • Chen Y, Irie Y, Keung WM, Maret W. S-nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation. Biochemistry 2002 41: 8360-7.
    • (2002) Biochemistry , vol.41 , pp. 8360-8367
    • Chen, Y.1    Irie, Y.2    Keung, W.M.3    Maret, W.4
  • 28
    • 0028082427 scopus 로고
    • Oxidative metal release from metallothionein via zincthiol/ disulfide interchange
    • Maret W. Oxidative metal release from metallothionein via zincthiol/ disulfide interchange. Proc Natl Acad Sci USA 1994; 91: 237-41.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 237-241
    • Maret, W.1
  • 29
    • 0033514932 scopus 로고    scopus 로고
    • Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes
    • Jacob C, Maret W, Vallee BL. Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes. Proc Natl Acad Sci USA 1999; 96: 1910-14.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1910-1914
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 30
    • 0034859512 scopus 로고    scopus 로고
    • Catalytic oxidation of zinc/sulfur coordination sites in proteins by selenium compounds
    • Chen Y, Maret W. Catalytic oxidation of zinc/sulfur coordination sites in proteins by selenium compounds. Antioxid Redox Signal 2001; 3: 651-56.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 651-656
    • Chen, Y.1    Maret, W.2
  • 31
    • 27844457019 scopus 로고    scopus 로고
    • Thioredoxin and lipoic acid catalyze the denitrosation of low molecular weight and protein S-nitrosothiols
    • Stoyanovsky DA, Tyurina YY, Tyurin VA, et al. Thioredoxin and lipoic acid catalyze the denitrosation of low molecular weight and protein S-nitrosothiols. J Am Chem Soc 2005; 127:15815-23.
    • (2005) J Am Chem Soc , vol.127 , pp. 15815-15823
    • Stoyanovsky, D.A.1    Tyurina, Y.Y.2    Tyurin, V.A.3
  • 32
    • 33846019656 scopus 로고    scopus 로고
    • Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes
    • Sagher D, Brunell D, Brot N, Vallee BL, Weissbach H. Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes. J Biol Chem 2006; 281: 31184-87.
    • (2006) J Biol Chem , vol.281 , pp. 31184-31187
    • Sagher, D.1    Brunell, D.2    Brot, N.3    Vallee, B.L.4    Weissbach, H.5
  • 33
    • 33645740498 scopus 로고    scopus 로고
    • Selenium prevents diabetes-induced alterations in [Zn2+]i and metallothionein level of rat heart via restoration of cell redox cycle
    • Ayaz M, Turan B. Selenium prevents diabetes-induced alterations in [Zn2+]i and metallothionein level of rat heart via restoration of cell redox cycle. Am J Physiol Heart Circ Physiol 2006; 290: H1071-80.
    • (2006) Am J Physiol Heart Circ Physiol , vol.290
    • Ayaz, M.1    Turan, B.2
  • 34
    • 33750901634 scopus 로고    scopus 로고
    • Zinc coordination environments in proteins as redox sensors and signal transducers
    • Maret W. Zinc coordination environments in proteins as redox sensors and signal transducers. Antioxid Redox Signal 2006; 8:1419-41.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1419-1441
    • Maret, W.1
  • 36
    • 10744230660 scopus 로고    scopus 로고
    • Crosstalk between nitric oxide and zinc pathways to neuronal cell death involving mitochondrial dysfunction and p38-activated K+ channels
    • Bossy-Wetzel E, Talantova MV, Lee WD, et al. Crosstalk between nitric oxide and zinc pathways to neuronal cell death involving mitochondrial dysfunction and p38-activated K+ channels. Neuron 2004; 41: 351-65.
    • (2004) Neuron , vol.41 , pp. 351-365
    • Bossy-Wetzel, E.1    Talantova, M.V.2    Lee, W.D.3
  • 37
    • 33749831752 scopus 로고    scopus 로고
    • Intracellular zinc elevation measured with a "calcium-specific" indicator during ischemia and reperfusion in rat hippocampus: A question on calcium overload
    • Stork CJ, Li YV. Intracellular zinc elevation measured with a "calcium-specific" indicator during ischemia and reperfusion in rat hippocampus: a question on calcium overload. J Neurosci 2006; 26: 10430-37.
    • (2006) J Neurosci , vol.26 , pp. 10430-10437
    • Stork, C.J.1    Li, Y.V.2
  • 38
    • 0038399723 scopus 로고    scopus 로고
    • Role of metallothionein-III following central nervous system damage
    • Carrasco J, Penkowa M, Giralt M, et al. Role of metallothionein-III following central nervous system damage. Neurobiol Dis 2003; 13: 22-36.
    • (2003) Neurobiol Dis , vol.13 , pp. 22-36
    • Carrasco, J.1    Penkowa, M.2    Giralt, M.3
  • 39
    • 0034597712 scopus 로고    scopus 로고
    • Mechanisms for the formation of protein-bound homocysteine in human plasma
    • Togawa T, Sengupta S, Chen H, et al. Mechanisms for the formation of protein-bound homocysteine in human plasma. Biochem Biophys Res Commun 2000; 277: 668-74.
    • (2000) Biochem Biophys Res Commun , vol.277 , pp. 668-674
    • Togawa, T.1    Sengupta, S.2    Chen, H.3
  • 40
    • 33847624075 scopus 로고    scopus 로고
    • Targeting of metallothionein by L-homocysteine: A novel mechanism for disruption of zinc and redox homeostasis
    • Barbato JC, Catanescu O, Murray K, DiBello PM, Jacobsen DW. Targeting of metallothionein by L-homocysteine: a novel mechanism for disruption of zinc and redox homeostasis. Arterioscler Thromb Vasc Biol 2007; 27: 49-54.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 49-54
    • Barbato, J.C.1    Catanescu, O.2    Murray, K.3    DiBello, P.M.4    Jacobsen, D.W.5
  • 41
    • 33847680903 scopus 로고    scopus 로고
    • Homocysteinylation of metallothionein impairs intracellular redox homeostasis: The enemy within!
    • Colgan SM, Austin RC. Homocysteinylation of metallothionein impairs intracellular redox homeostasis: the enemy within! Arterioscler Thromb Vasc Biol 2007; 27: 8-11.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 8-11
    • Colgan, S.M.1    Austin, R.C.2
  • 42
    • 33749427563 scopus 로고    scopus 로고
    • Involvement of oxidative stress in the synthesis of metallothionein induced by mitochondrial inhibitors
    • Futakawa N, Kondoh M, Ueda S, et al. Involvement of oxidative stress in the synthesis of metallothionein induced by mitochondrial inhibitors. Biol Pharm Bull 2006; 29: 2016-20.
    • (2006) Biol Pharm Bull , vol.29 , pp. 2016-2020
    • Futakawa, N.1    Kondoh, M.2    Ueda, S.3
  • 44
    • 0034913884 scopus 로고    scopus 로고
    • Metallothionein inhibits doxorubicin-induced mitochondrial cytochrome c release and caspase-3 activation in cardiomyocytes
    • Wang GW, Klein JB, Kang YJ. Metallothionein inhibits doxorubicin-induced mitochondrial cytochrome c release and caspase-3 activation in cardiomyocytes. J Pharmacol Exp Ther 2001; 298:461-68.
    • (2001) J Pharmacol Exp Ther , vol.298 , pp. 461-468
    • Wang, G.W.1    Klein, J.B.2    Kang, Y.J.3
  • 45
    • 0031691375 scopus 로고    scopus 로고
    • Zinc ions prevent processing of caspase-3 during apoptosis induced by geranylgeraniol in HL-60 cells
    • Aiuchi T, Mihara S, Nakaya M, Masuda Y, Nakajo S, Nakaya K. Zinc ions prevent processing of caspase-3 during apoptosis induced by geranylgeraniol in HL-60 cells. J Biochem 1998; 124: 300-3.
    • (1998) J Biochem , vol.124 , pp. 300-303
    • Aiuchi, T.1    Mihara, S.2    Nakaya, M.3    Masuda, Y.4    Nakajo, S.5    Nakaya, K.6
  • 47
    • 77954681706 scopus 로고    scopus 로고
    • The missing zinc: P53 misfolding and cancer
    • Loh SN. The missing zinc: p53 misfolding and cancer. Metallomics 2010; 2: 442-49.
    • (2010) Metallomics , vol.2 , pp. 442-449
    • Loh, S.N.1
  • 50
    • 84866755324 scopus 로고    scopus 로고
    • Effect of aging on 5-hydroxymethylcytosine in brain mitochondria
    • Mar 22. doi.org/10.1016/j.neurobiolaging.2012.02.006
    • Dzitoyeva S, Chen H, Manev H. Effect of aging on 5-hydroxymethylcytosine in brain mitochondria. Neurobiol Aging 2012 Mar 22. doi.org/10.1016/j.neurobiolaging.2012.02.006
    • (2012) Neurobiol Aging
    • Dzitoyeva, S.1    Chen, H.2    Manev, H.3
  • 51
    • 0027204255 scopus 로고
    • A putative glutathione-binding site in CdZn-metallothionein identified by equilibrium binding and molecular-modelling studies
    • Brouwer M, Hoexum-Brouwer T, Cashon RE. A putative glutathione-binding site in CdZn-metallothionein identified by equilibrium binding and molecular-modelling studies. Biochem J 1993; 294: 219-25.
    • (1993) Biochem J , vol.294 , pp. 219-225
    • Brouwer, M.1    Hoexum-Brouwer, T.2    Cashon, R.E.3
  • 53
    • 0028082427 scopus 로고
    • Oxidative metal release from metallothionein via zincthiol/ disulfide interchange
    • Maret W. Oxidative metal release from metallothionein via zincthiol/ disulfide interchange. Proc Natl Acad Sci U S A 1994;91:237-41.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 237-241
    • Maret, W.1
  • 54
    • 0035956862 scopus 로고    scopus 로고
    • Zinc metallothionein imported into liver mitochondria modulates respiration
    • Ye B, Maret W, Vallee BL. Zinc metallothionein imported into liver mitochondria modulates respiration. Proc Natl Acad Sci USA 2001; 98:2317-22.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2317-2322
    • Ye, B.1    Maret, W.2    Vallee, B.L.3
  • 55
    • 1642298968 scopus 로고    scopus 로고
    • Metallothionein can function as a chaperone for zinc uptake transport into prostate and liver mitochondria
    • Costello LC, Guan Z, Franklin RB, Feng P. Metallothionein can function as a chaperone for zinc uptake transport into prostate and liver mitochondria. J Inorg Biochem 2004; 98:664-66.
    • (2004) J Inorg Biochem , vol.98 , pp. 664-666
    • Costello, L.C.1    Guan, Z.2    Franklin, R.B.3    Feng, P.4
  • 56
    • 19744375548 scopus 로고    scopus 로고
    • Metallothionein transfers zinc to mitochondrial aconitase through a direct interaction in mouse hearts
    • Feng W, Cai J, Pierce WM, et al. Metallothionein transfers zinc to mitochondrial aconitase through a direct interaction in mouse hearts. Biochem Biophys Res Commun 2005; 332: 853-58.
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 853-858
    • Feng, W.1    Cai, J.2    Pierce, W.M.3
  • 57
    • 33745512245 scopus 로고    scopus 로고
    • Mitochondrial aconitase and citrate metabolism in malignant and non-malignant human prostate tissues
    • Singh KK, Desouki MM, Franklin RB, Costello LC. Mitochondrial aconitase and citrate metabolism in malignant and non-malignant human prostate tissues. Mol Cancer 2006; 5: 14-18.
    • (2006) Mol Cancer , vol.5 , pp. 14-18
    • Singh, K.K.1    Desouki, M.M.2    Franklin, R.B.3    Costello, L.C.4
  • 58
    • 13344259905 scopus 로고    scopus 로고
    • Zinc causes loss of membrane potential and elevates reactive oxygen species in rat brain mitochondria
    • Dineley KE, Richards LL, Votyakova TV, Reynolds IJ. Zinc causes loss of membrane potential and elevates reactive oxygen species in rat brain mitochondria. Mitochondrion 2005; 5: 55-65.
    • (2005) Mitochondrion , vol.5 , pp. 55-65
    • Dineley, K.E.1    Richards, L.L.2    Votyakova, T.V.3    Reynolds, I.J.4
  • 59
    • 0001375517 scopus 로고
    • On the inhibition of mitochondrial electron transport by Zn(2+) ions
    • Kleiner D, von Jagow G. On the inhibition of mitochondrial electron transport by Zn(2+) ions. FEBS Lett 1972; 20: 229-32.
    • (1972) FEBS Lett , vol.20 , pp. 229-232
    • Kleiner, D.1    von Jagow, G.2
  • 60
    • 0033514994 scopus 로고    scopus 로고
    • Inhibitory sites in enzymes: Zinc removal and reactivation by thionein
    • Maret W, Jacob C, Vallee BL, Fischer EH. Inhibitory sites in enzymes: zinc removal and reactivation by thionein. Proc Natl Acad Sci USA 1999; 96: 1936-40.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1936-1940
    • Maret, W.1    Jacob, C.2    Vallee, B.L.3    Fischer, E.H.4
  • 61
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob C, Maret W, Vallee BL. Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc Natl Acad Sci USA 1998; 95: 3489-94.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 62
    • 0026698727 scopus 로고
    • Mitochondrial creatine kinase: A key enzyme of aerobic energy metabolism
    • Wyss M, Smeitink J, Wevers RA, Wallimann T. Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim Biophys Acta 1992; 1102:119-66.
    • (1992) Biochim Biophys Acta , vol.1102 , pp. 119-166
    • Wyss, M.1    Smeitink, J.2    Wevers, R.A.3    Wallimann, T.4
  • 63
    • 84555189166 scopus 로고    scopus 로고
    • Metallothioneins protect cytosolic creatine kinases against stress induced by nitrogen-based oxidants
    • Chen Z, Li J, Zhao TJ, et al. Metallothioneins protect cytosolic creatine kinases against stress induced by nitrogen-based oxidants. Biochem J 2012; 441: 623-32.
    • (2012) Biochem J , vol.441 , pp. 623-632
    • Chen, Z.1    Li, J.2    Zhao, T.J.3
  • 64
    • 20444403004 scopus 로고    scopus 로고
    • Gene expression profiles in the liver and kidney of metallothionein-null mice
    • Miura N, Koizumi S. Gene expression profiles in the liver and kidney of metallothionein-null mice. Biochem Biophys Res Commun 2005; 332: 949-55.
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 949-955
    • Miura, N.1    Koizumi, S.2
  • 65
    • 79251470797 scopus 로고    scopus 로고
    • The first long-lived mutants: Discovery of the insulin/ IGF-1 pathway for ageing
    • Kenyon C. The first long-lived mutants: discovery of the insulin/ IGF-1 pathway for ageing. Philos Trans R Soc Lond B Biol Sci 2011; 366: 9-16.
    • (2011) Philos Trans R Soc Lond B Biol Sci , vol.366 , pp. 9-16
    • Kenyon, C.1
  • 66
    • 33750600258 scopus 로고    scopus 로고
    • Novel roles for metallothionein-I + II (MT-I + II) in defense responses, neurogenesis, and tissue restoration after traumatic brain injury: Insights from global gene expression profiling in wild-type and MT-I + II knockout mice
    • Penkowa M, Cáceres M, Borup R, et al. Novel roles for metallothionein-I + II (MT-I + II) in defense responses, neurogenesis, and tissue restoration after traumatic brain injury: insights from global gene expression profiling in wild-type and MT-I + II knockout mice. J Neurosci Res 2006; 84:1452-74.
    • (2006) J Neurosci Res , vol.84 , pp. 1452-1474
    • Penkowa, M.1    Cáceres, M.2    Borup, R.3
  • 67
    • 70349669095 scopus 로고    scopus 로고
    • Ribosomal protein S6 kinase 1 signaling regulates mammalian life span
    • Selman C, Tullet JM, Wieser D, et al. Ribosomal protein S6 kinase 1 signaling regulates mammalian life span. Science 2009; 326: 140-44.
    • (2009) Science , vol.326 , pp. 140-144
    • Selman, C.1    Tullet, J.M.2    Wieser, D.3
  • 68
    • 0029987684 scopus 로고    scopus 로고
    • Metallothionein I and II protect against zinc deficiency and zinc toxicity in mice
    • Kelly EJ, Quaife CJ, Froelick GJ, Palmiter RD. Metallothionein I and II protect against zinc deficiency and zinc toxicity in mice. J Nutr 1996; 126:1782-90.
    • (1996) J Nutr , vol.126 , pp. 1782-1790
    • Kelly, E.J.1    Quaife, C.J.2    Froelick, G.J.3    Palmiter, R.D.4
  • 69
    • 0027204069 scopus 로고
    • Targeting and germ-line transmission of a null mutation at the metallothionein I and II loci in mouse
    • Michalska AE, Choo KH. Targeting and germ-line transmission of a null mutation at the metallothionein I and II loci in mouse. Proc Natl Acad Sci USA 1993; 90: 8088-92.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8088-8092
    • Michalska, A.E.1    Choo, K.H.2
  • 70
    • 0031892092 scopus 로고    scopus 로고
    • Obesity and hyperleptinemia in metallothionein (-I and-II) null mice
    • Beattie JH, Wood AM, Newman AM, et al. Obesity and hyperleptinemia in metallothionein (-I and-II) null mice. Proc Natl Acad Sci USA 1998; 95: 358-63.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 358-363
    • Beattie, J.H.1    Wood, A.M.2    Newman, A.M.3
  • 71
    • 32244433433 scopus 로고    scopus 로고
    • Metallothionein and liver cell regeneration
    • Cherian MG, Kang YJ. Metallothionein and liver cell regeneration. Exp Biol Med (Maywood) 2006; 231: 138-44.
    • (2006) Exp Biol Med (Maywood) , vol.231 , pp. 138-144
    • Cherian, M.G.1    Kang, Y.J.2
  • 72
    • 56349115845 scopus 로고    scopus 로고
    • Role of metallothionein in lung inflammation induced by ozone exposure in mice
    • Inoue K, Takano H, Kaewamatawong T, et al. Role of metallothionein in lung inflammation induced by ozone exposure in mice. Free Radic Biol Med 2008; 45:1714-22.
    • (2008) Free Radic Biol Med , vol.45 , pp. 1714-1722
    • Inoue, K.1    Takano, H.2    Kaewamatawong, T.3
  • 73
    • 72749118269 scopus 로고    scopus 로고
    • Metallothionein induces a regenerative reactive astrocyte phenotype via JAK/STAT and RhoA signalling pathways
    • Leung YK, Pankhurst M, Dunlop SA, et al. Metallothionein induces a regenerative reactive astrocyte phenotype via JAK/STAT and RhoA signalling pathways. Exp Neurol 2010; 221: 98-106.
    • (2010) Exp Neurol , vol.221 , pp. 98-106
    • Leung, Y.K.1    Pankhurst, M.2    Dunlop, S.A.3
  • 74
    • 42649144123 scopus 로고    scopus 로고
    • Metallothionein downregulation in very old age: A phenomenon associated with cellular senescence?
    • Malavolta M, Cipriano C, Costarelli L, et al. Metallothionein downregulation in very old age: a phenomenon associated with cellular senescence? Rejuvenation Res 2008; 11: 455-59.
    • (2008) Rejuvenation Res , vol.11 , pp. 455-459
    • Malavolta, M.1    Cipriano, C.2    Costarelli, L.3
  • 78
    • 3342976147 scopus 로고    scopus 로고
    • GenAge: A genomic and proteomic network map of human ageing
    • de Magalhães JP, Toussaint O. GenAge: a genomic and proteomic network map of human ageing. FEBS Lett 2004; 571: 243-47.
    • (2004) FEBS Lett , vol.571 , pp. 243-247
    • de Magalhães, J.P.1    Toussaint, O.2
  • 79
    • 44349118767 scopus 로고    scopus 로고
    • Human ApoD, an apolipoprotein up-regulated in neurodegenerative diseases, extends lifespan and increases stress resistance in Drosophila
    • Muffat J, Walker DW, Benzer S. Human ApoD, an apolipoprotein up-regulated in neurodegenerative diseases, extends lifespan and increases stress resistance in Drosophila. Proc Natl Acad Sci USA 2008; 105:7088-93.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7088-7093
    • Muffat, J.1    Walker, D.W.2    Benzer, S.3
  • 80
    • 33847169447 scopus 로고    scopus 로고
    • Protection of cells from oxidative stress by microsomal glutathione transferase 1
    • Siritantikorn A, Johansson K, Ahlen K, et al. Protection of cells from oxidative stress by microsomal glutathione transferase 1. Biochem Biophys Res Commun 2007; 355: 592-96.
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 592-596
    • Siritantikorn, A.1    Johansson, K.2    Ahlen, K.3
  • 81
    • 84860288746 scopus 로고    scopus 로고
    • Survival study of Metallothionein-1 transgenic mice and respective controls (C57BL/6J): Influence of a zinc-enriched environment
    • Malavolta M, Basso A, Piacenza F, et al. Survival study of Metallothionein-1 transgenic mice and respective controls (C57BL/6J): influence of a zinc-enriched environment. Rejuvenation Res 2012; 15:140-43.
    • (2012) Rejuvenation Res , vol.15 , pp. 140-143
    • Malavolta, M.1    Basso, A.2    Piacenza, F.3
  • 82
    • 33744456501 scopus 로고    scopus 로고
    • Metallothionein prolongs survival and antagonizes senescence-associated cardiomyocyte diastolic dysfunction: Role of oxidative stress
    • Yang X, Doser TA, Fang CX, et al. Metallothionein prolongs survival and antagonizes senescence-associated cardiomyocyte diastolic dysfunction: role of oxidative stress. FASEB J 2006; 20:1024-26.
    • (2006) FASEB J , vol.20 , pp. 1024-1026
    • Yang, X.1    Doser, T.A.2    Fang, C.X.3
  • 83
    • 21144434217 scopus 로고    scopus 로고
    • Extension of murine life span by overexpression of catalase targeted to mitochondria
    • Schriner SE, Linford NJ, Martin GM, et al. Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 2005; 308: 1909-11.
    • (2005) Science , vol.308 , pp. 1909-1911
    • Schriner, S.E.1    Linford, N.J.2    Martin, G.M.3
  • 84
    • 59749084724 scopus 로고    scopus 로고
    • Accelerated failure time models provide a useful statistical framework for aging research
    • Swindell WR. Accelerated failure time models provide a useful statistical framework for aging research. Exp Gerontol 2009; 44: 190-200.
    • (2009) Exp Gerontol , vol.44 , pp. 190-200
    • Swindell, W.R.1
  • 85
    • 64249107059 scopus 로고    scopus 로고
    • Evidence for cardiomyocyte renewal in humans
    • Bergmann O, Bhardwaj RD, Bernard S, et al. Evidence for cardiomyocyte renewal in humans. Science 2009; 324: 98-102.
    • (2009) Science , vol.324 , pp. 98-102
    • Bergmann, O.1    Bhardwaj, R.D.2    Bernard, S.3
  • 87
    • 33646128026 scopus 로고    scopus 로고
    • Nutrient-gene interaction in ageing and successful ageing. A single nutrient (zinc) and some target genes related to inflammatory/immune response
    • Mocchegiani E, Costarelli L, Giacconi R, et al. Nutrient-gene interaction in ageing and successful ageing. A single nutrient (zinc) and some target genes related to inflammatory/immune response. Mech Ageing Dev 2006; 127: 517-25.
    • (2006) Mech Ageing Dev , vol.127 , pp. 517-525
    • Mocchegiani, E.1    Costarelli, L.2    Giacconi, R.3
  • 88
    • 33644866812 scopus 로고    scopus 로고
    • Metallothionein disulfides are present in metallothionein-overexpressing transgenic mouse heart and increase under conditions of oxidative stress
    • Feng W, Benz FW, Cai J, Pierce WM, Kang YJ. Metallothionein disulfides are present in metallothionein-overexpressing transgenic mouse heart and increase under conditions of oxidative stress. J Biol Chem 2006; 281: 681-87.
    • (2006) J Biol Chem , vol.281 , pp. 681-687
    • Feng, W.1    Benz, F.W.2    Cai, J.3    Pierce, W.M.4    Kang, Y.J.5
  • 89
    • 80755153625 scopus 로고    scopus 로고
    • Redox biochemistry of mammalian metallothioneins
    • Maret W. Redox biochemistry of mammalian metallothioneins J Biol Inorg Chem 2011; 16:1079-1086
    • (2011) J Biol Inorg Chem , vol.16 , pp. 1079-1086
    • Maret, W.1
  • 90
    • 0035344459 scopus 로고    scopus 로고
    • Nitric oxide selectively releases metals from the amino-terminal domain of metallothioneins: Potential role at inflammatory sites
    • Zangger K, Oz G, Haslinger E, Kunert O, Armitage IM. Nitric oxide selectively releases metals from the amino-terminal domain of metallothioneins: potential role at inflammatory sites. FASEB J 2001; 15: 1303-05.
    • (2001) FASEB J , vol.15 , pp. 1303-1305
    • Zangger, K.1    Oz, G.2    Haslinger, E.3    Kunert, O.4    Armitage, I.M.5
  • 91
    • 0345564814 scopus 로고    scopus 로고
    • Regulation of zinc homeostasis by inducible NO synthase-derived NO: Nuclear metallothionein translocation and intranuclear Zn2+ release
    • Spahl DU, Berendji-Grün D, Suschek CV, Kolb-Bachofen V, Kröncke KD. Regulation of zinc homeostasis by inducible NO synthase-derived NO: nuclear metallothionein translocation and intranuclear Zn2+ release. Proc Natl Acad Sci USA 2003; 100:13952-57.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13952-13957
    • Spahl, D.U.1    Berendji-Grün, D.2    Suschek, C.V.3    Kolb-Bachofen, V.4    Kröncke, K.D.5
  • 92
    • 0042697664 scopus 로고    scopus 로고
    • Antagonistic pleiotropy, mortality source interactions, and the evolutionary theory of senescence
    • Williams PD, Day T. Antagonistic pleiotropy, mortality source interactions, and the evolutionary theory of senescence. Evolution 2003; 57:1478-88.
    • (2003) Evolution , vol.57 , pp. 1478-1488
    • Williams, P.D.1    Day, T.2
  • 93
    • 77953925098 scopus 로고    scopus 로고
    • Heat shock proteins in long-lived worms and mice with insulin/insulin-like signaling mutations
    • Swindell WR. Heat shock proteins in long-lived worms and mice with insulin/insulin-like signaling mutations. Aging (Albany NY) 2009; 1: 573-77.
    • (2009) Aging (Albany NY) , vol.1 , pp. 573-577
    • Swindell, W.R.1
  • 94
    • 58149235102 scopus 로고    scopus 로고
    • Over-expression of heat shock protein 70 in mice is associated with growth retardation, tu mor formation, and early death
    • Vanhooren V, Liu XE, Desmyter L, et al. Over-expression of heat shock protein 70 in mice is associated with growth retardation, tu mor formation, and early death. Rejuvenation Res 2008; 11: 1013-20.
    • (2008) Rejuvenation Res , vol.11 , pp. 1013-1020
    • Vanhooren, V.1    Liu, X.E.2    Desmyter, L.3
  • 95
    • 35449004475 scopus 로고    scopus 로고
    • Biological variability of transferrin saturation and unsaturated iron-binding capacity
    • Adams PC, Reboussin DM, Press RD, et al. Biological variability of transferrin saturation and unsaturated iron-binding capacity. Am J Med 2007; 120: 999. e1-7.
    • (2007) Am J Med , vol.120
    • Adams, P.C.1    Reboussin, D.M.2    Press, R.D.3
  • 96
    • 0036484319 scopus 로고    scopus 로고
    • Association between the MHC class I gene HFE polymorphisms and longevity: A study in Sicilian population
    • Lio D, Balistreri CR, Colonna-Romano G, et al. Association between the MHC class I gene HFE polymorphisms and longevity: a study in Sicilian population. Genes Immun 2002; 3: 20-4.
    • (2002) Genes Immun , vol.3 , pp. 20-24
    • Lio, D.1    Balistreri, C.R.2    Colonna-Romano, G.3
  • 98
    • 31044444489 scopus 로고    scopus 로고
    • Interrelationship among neutrophil efficiency, inflammation, antioxidant activity and zinc pool in very old age
    • Moroni F, Di Paolo ML, Rigo A, et al. Interrelationship among neutrophil efficiency, inflammation, antioxidant activity and zinc pool in very old age. Biogerontology 2005; 6: 271-81.
    • (2005) Biogerontology , vol.6 , pp. 271-281
    • Moroni, F.1    Di Paolo, M.L.2    Rigo, A.3
  • 99
    • 77952875418 scopus 로고    scopus 로고
    • Overexpression of metal-responsive transcription factor (MTF-1) in Drosophila melanogaster ameliorates life-span reductions associated with oxidative stress and metal toxicity
    • Bahadorani S, Mukai S, Egli D, Hilliker AJ. Overexpression of metal-responsive transcription factor (MTF-1) in Drosophila melanogaster ameliorates life-span reductions associated with oxidative stress and metal toxicity. Neurobiol Aging 2010; 31:1215-26.
    • (2010) Neurobiol Aging , vol.31 , pp. 1215-1226
    • Bahadorani, S.1    Mukai, S.2    Egli, D.3    Hilliker, A.J.4
  • 100
    • 36448984298 scopus 로고    scopus 로고
    • Gene expression profiling of long-lived dwarf mice: Longevity associated genes and relationships with diet, gender and aging
    • Swindell WR. Gene expression profiling of long-lived dwarf mice: longevity associated genes and relationships with diet, gender and aging. BMC Genomics 2007; 8: 353-58.
    • (2007) BMC Genomics , vol.8 , pp. 353-358
    • Swindell, W.R.1
  • 101
    • 0035082093 scopus 로고    scopus 로고
    • Longevity and heavy metal resistance in daf-2 and age-1 long-lived mutants of Caenorhabditis elegans
    • Barsyte D, Lovejoy DA, Lithgow GJ. Longevity and heavy metal resistance in daf-2 and age-1 long-lived mutants of Caenorhabditis elegans. FASEB J 2001; 15: 627-34.
    • (2001) FASEB J , vol.15 , pp. 627-634
    • Barsyte, D.1    Lovejoy, D.A.2    Lithgow, G.J.3
  • 102
    • 33748531801 scopus 로고    scopus 로고
    • Plasticity of neuroendocrine-thymus interactions during ontogeny and ageing: Role of zinc and arginine
    • Mocchegiani E, Santarelli L, Costarelli L, et al. Plasticity of neuroendocrine-thymus interactions during ontogeny and ageing: role of zinc and arginine. Ageing Res Rev 2006; 5: 281-309.
    • (2006) Ageing Res Rev , vol.5 , pp. 281-309
    • Mocchegiani, E.1    Santarelli, L.2    Costarelli, L.3
  • 103
    • 0030753690 scopus 로고    scopus 로고
    • Serum levels of insulin-like growth factor-I (IGF-I) and IGF-binding protein-3 in healthy centenarians: Relationship with plasma leptin and lipid concentration, insulin action and cognitive function
    • Paolisso G, Ammendola S, Del Buono A, et al. Serum levels of insulin-like growth factor-I (IGF-I) and IGF-binding protein-3 in healthy centenarians: relationship with plasma leptin and lipid concentration, insulin action and cognitive function. J Clin Endocrinol Metab 1997; 82: 2204-09.
    • (1997) J Clin Endocrinol Metab , vol.82 , pp. 2204-2209
    • Paolisso, G.1    Ammendola, S.2    Del Buono, A.3
  • 104
    • 0038637217 scopus 로고    scopus 로고
    • Polymorphic variants of insulin-like growth factor I (IGF-I) receptor and phosphoinositide 3-kinase genes affect IGF-I plasma levels and human longevity: Cues for an evolutionarily conserved mechanism of life span control
    • Bonafè M, Barbieri M, Marchegiani F, et al. Polymorphic variants of insulin-like growth factor I (IGF-I) receptor and phosphoinositide 3-kinase genes affect IGF-I plasma levels and human longevity: cues for an evolutionarily conserved mechanism of life span control. J Clin Endocrinol Metab 2003; 88: 3299-304.
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 3299-3304
    • Bonafè, M.1    Barbieri, M.2    Marchegiani, F.3
  • 105
    • 84863393278 scopus 로고    scopus 로고
    • Picomolar concentrations of free zinc(II) ions regulate receptor protein-tyrosine phosphatase β activity
    • Wilson M, Hogstrand C, Maret W. Picomolar concentrations of free zinc(II) ions regulate receptor protein-tyrosine phosphatase β activity. J Biol Chem 2012; 287: 9322-6.
    • (2012) J Biol Chem , vol.287 , pp. 9322-9326
    • Wilson, M.1    Hogstrand, C.2    Maret, W.3
  • 106
    • 84863347363 scopus 로고    scopus 로고
    • Inhibition of protein tyrosine phosphatase improves angiogenesis via enhancing Ang-1/Tie-2 signaling in diabetes
    • Chen JX, Tuo Q, Liao DF, Zeng H. Inhibition of protein tyrosine phosphatase improves angiogenesis via enhancing Ang-1/Tie-2 signaling in diabetes. Exp Diabetes Res 2012; 2012: 836759-63.
    • (2012) Exp Diabetes Res , vol.2012 , pp. 836759-836763
    • Chen, J.X.1    Tuo, Q.2    Liao, D.F.3    Zeng, H.4
  • 107
    • 34547836490 scopus 로고    scopus 로고
    • Polymorphisms in MT1a gene coding region are associated with longevity in Italian Central female population
    • Cipriano C, Malavolta M, Costarelli L, et al. Polymorphisms in MT1a gene coding region are associated with longevity in Italian Central female population. Biogerontology 2006; 7: 357-65.
    • (2006) Biogerontology , vol.7 , pp. 357-365
    • Cipriano, C.1    Malavolta, M.2    Costarelli, L.3
  • 108
    • 33745837058 scopus 로고    scopus 로고
    • Novel-209A/G MT2A polymorphism in old patients with type 2 diabetes and atherosclerosis: Relationship with inflammation (IL-6) and zinc
    • Giacconi R, Cipriano C, Muti E, et al. Novel-209A/G MT2A polymorphism in old patients with type 2 diabetes and atherosclerosis: relationship with inflammation (IL-6) and zinc. Biogerontology 2005; 6: 407-13.
    • (2005) Biogerontology , vol.6 , pp. 407-413
    • Giacconi, R.1    Cipriano, C.2    Muti, E.3
  • 109
    • 50549218525 scopus 로고
    • The limited in vitro lifetime of human diploid cell strains
    • Hayflick L. The limited in vitro lifetime of human diploid cell strains. Exp Cell Res 1965; 37: 614-36.
    • (1965) Exp Cell Res , vol.37 , pp. 614-636
    • Hayflick, L.1
  • 110
    • 13944270339 scopus 로고    scopus 로고
    • Senescent cells, tumor suppression, and organismal aging: Good citizens, bad neighbors
    • Campisi J. Senescent cells, tumor suppression, and organismal aging: good citizens, bad neighbors. Cell 2005; 120: 513-22.
    • (2005) Cell , vol.120 , pp. 513-522
    • Campisi, J.1
  • 111
    • 19544362405 scopus 로고    scopus 로고
    • Adult neurogenesis and repair of the adult CNS with neural progenitors, precursors, and stem cells
    • Emsley JG, Mitchell BD, Kempermann G, Macklis JD. Adult neurogenesis and repair of the adult CNS with neural progenitors, precursors, and stem cells. Prog Neurobiol 2005; 75: 321-41.
    • (2005) Prog Neurobiol , vol.75 , pp. 321-341
    • Emsley, J.G.1    Mitchell, B.D.2    Kempermann, G.3    Macklis, J.D.4
  • 112
    • 0242329884 scopus 로고    scopus 로고
    • p53 functions through stress-and promoter-specific recruitment of transcription initiation components before and after DNA damage
    • Espinosa JM, Verdun RE, Emerson BM. p53 functions through stress-and promoter-specific recruitment of transcription initiation components before and after DNA damage. Mol Cell 2003; 12: 1015-27.
    • (2003) Mol Cell , vol.12 , pp. 1015-1027
    • Espinosa, J.M.1    Verdun, R.E.2    Emerson, B.M.3
  • 113
    • 77954537044 scopus 로고    scopus 로고
    • Regulation of tumor suppressor p53 at the RNA level
    • Vilborg A, Wilhelm MT, Wiman KG. Regulation of tumor suppressor p53 at the RNA level. J Mol Med (Berl) 2010; 88: 645-52.
    • (2010) J Mol Med (Berl) , vol.88 , pp. 645-652
    • Vilborg, A.1    Wilhelm, M.T.2    Wiman, K.G.3
  • 115
    • 0034597536 scopus 로고    scopus 로고
    • Metalloregulation of the tumor suppressor protein p53: Zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells
    • Méplan C, Richard MJ, Hainaut P. Metalloregulation of the tumor suppressor protein p53: zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells. Oncogene 2000; 19:5227-36.
    • (2000) Oncogene , vol.19 , pp. 5227-5236
    • Méplan, C.1    Richard, M.J.2    Hainaut, P.3
  • 116
    • 0031978026 scopus 로고    scopus 로고
    • Modulation of p53 protein conformation and DNA-binding activity by intracellular chelation of zinc
    • Verhaegh GW, Parat MO, Richard MJ, Hainaut P. Modulation of p53 protein conformation and DNA-binding activity by intracellular chelation of zinc. Mol Carcinog 1998; 21:205-14.
    • (1998) Mol Carcinog , vol.21 , pp. 205-214
    • Verhaegh, G.W.1    Parat, M.O.2    Richard, M.J.3    Hainaut, P.4
  • 118
    • 0036385838 scopus 로고    scopus 로고
    • An essential role for functional telomeres in mouse germ cells during fertilization and early development
    • Liu L, Blasco M, Trimarchi J, Keefe D. An essential role for functional telomeres in mouse germ cells during fertilization and early development. Dev Biol 2002; 249:74-84.
    • (2002) Dev Biol , vol.249 , pp. 74-84
    • Liu, L.1    Blasco, M.2    Trimarchi, J.3    Keefe, D.4
  • 119
    • 0346256784 scopus 로고    scopus 로고
    • Metabolic analysis of senescent human fibroblasts reveals a role for AMP in cellular senescence
    • Zwerschke W, Mazurek S, Stöckl P, Hütter E, Eigenbrodt E, Jansen-Dürr P. Metabolic analysis of senescent human fibroblasts reveals a role for AMP in cellular senescence. Biochem J 2003; 376: 403-11.
    • (2003) Biochem J , vol.376 , pp. 403-411
    • Zwerschke, W.1    Mazurek, S.2    Stöckl, P.3    Hütter, E.4    Eigenbrodt, E.5    Jansen-Dürr, P.6
  • 120
  • 121
    • 21244431867 scopus 로고    scopus 로고
    • Mitochondria, telomeres and cell senescence
    • Passos JF, von Zglinicki T. Mitochondria, telomeres and cell senescence. Exp Gerontol 2005; 40: 466-72.
    • (2005) Exp Gerontol , vol.40 , pp. 466-472
    • Passos, J.F.1    von Zglinicki, T.2
  • 122
    • 0025279931 scopus 로고
    • Telomeres shorten during ageing of human fibroblasts
    • Harley CB, Futcher AB, Greider CW. Telomeres shorten during ageing of human fibroblasts. Nature 1990; 345: 458-60.
    • (1990) Nature , vol.345 , pp. 458-460
    • Harley, C.B.1    Futcher, A.B.2    Greider, C.W.3
  • 123
    • 56949097013 scopus 로고    scopus 로고
    • Restoring wtp53 activity in HIPK2 depleted MCF7 cells by modulating metallothionein and zinc
    • Puca R, Nardinocchi L, Bossi G, et al. Restoring wtp53 activity in HIPK2 depleted MCF7 cells by modulating metallothionein and zinc. Exp Cell Res 2009; 315: 67-75.
    • (2009) Exp Cell Res , vol.315 , pp. 67-75
    • Puca, R.1    Nardinocchi, L.2    Bossi, G.3
  • 124
    • 33846090789 scopus 로고    scopus 로고
    • Accumulation of senescent cells in mitotic tissue of aging primates
    • Jeyapalan JC, Ferreira M, Sedivy JM, Herbig U. Accumulation of senescent cells in mitotic tissue of aging primates. Mech Ageing Dev. 2007; 128: 36-44.
    • (2007) Mech Ageing Dev. , vol.128 , pp. 36-44
    • Jeyapalan, J.C.1    Ferreira, M.2    Sedivy, J.M.3    Herbig, U.4
  • 125
    • 67649657879 scopus 로고    scopus 로고
    • Accumulation of cells with short telomeres is associated with impaired zinc homeostasis and inflammation in old hypertensive participants
    • Cipriano C, Tesei S, Malavolta M, et al. Accumulation of cells with short telomeres is associated with impaired zinc homeostasis and inflammation in old hypertensive participants. J Gerontol A Biol Sci Med Sci 2009; 64:745-51.
    • (2009) J Gerontol A Biol Sci Med Sci , vol.64 , pp. 745-751
    • Cipriano, C.1    Tesei, S.2    Malavolta, M.3
  • 126
    • 77951652952 scopus 로고    scopus 로고
    • Metallothionein-I/II null cardiomyocytes are sensitive to Fusarium mycotoxin butenolide-induced cytotoxicity and oxidative DNA damage
    • Yang HY, Wang YM, Peng SQ. Metallothionein-I/II null cardiomyocytes are sensitive to Fusarium mycotoxin butenolide-induced cytotoxicity and oxidative DNA damage. Toxicon 2010; 55:1291-96.
    • (2010) Toxicon , vol.55 , pp. 1291-1296
    • Yang, H.Y.1    Wang, Y.M.2    Peng, S.Q.3
  • 128
    • 0030964277 scopus 로고    scopus 로고
    • The biology of replicative senescence
    • Campisi J. The biology of replicative senescence. Eur J Cancer 1997; 33: 703-09.
    • (1997) Eur J Cancer , vol.33 , pp. 703-709
    • Campisi, J.1
  • 129
    • 23244460597 scopus 로고    scopus 로고
    • Crucial role of p53-dependent cellular senescence in suppression of Pten-deficient tumorigenesis
    • Chen Z, Trotman LC, Shaffer D, et al. Crucial role of p53-dependent cellular senescence in suppression of Pten-deficient tumorigenesis. Nature 2005; 436: 725-30.
    • (2005) Nature , vol.436 , pp. 725-730
    • Chen, Z.1    Trotman, L.C.2    Shaffer, D.3
  • 130
    • 0141518574 scopus 로고    scopus 로고
    • Metallothionein (I+II) confers, via c-myc, immune plasticity in oldest mice: Model of partial hepatectomy/liver regeneration
    • Cipriano C, Giacconi R, Muzzioli M, et al. Metallothionein (I+II) confers, via c-myc, immune plasticity in oldest mice: model of partial hepatectomy/liver regeneration. Mech Ageing Dev 2003; 124: 877-86.
    • (2003) Mech Ageing Dev , vol.124 , pp. 877-886
    • Cipriano, C.1    Giacconi, R.2    Muzzioli, M.3
  • 131
    • 0029902680 scopus 로고    scopus 로고
    • Alterations in mRNA stability during rat liver regeneration
    • Kren BT, Trembley JH, Steer CJ. Alterations in mRNA stability during rat liver regeneration. Am J Physiol 1996; 270: G763-77.
    • (1996) Am J Physiol , vol.270
    • Kren, B.T.1    Trembley, J.H.2    Steer, C.J.3
  • 132
    • 77952105389 scopus 로고    scopus 로고
    • Inflammatory networks during cellular senescence: Causes and consequences
    • Freund A, Orjalo AV, Desprez PY, Campisi J. Inflammatory networks during cellular senescence: causes and consequences. Trends Mol Med 2010; 16: 238-46.
    • (2010) Trends Mol Med , vol.16 , pp. 238-246
    • Freund, A.1    Orjalo, A.V.2    Desprez, P.Y.3    Campisi, J.4
  • 134
    • 80855128461 scopus 로고    scopus 로고
    • Cellular senescence: A link between cancer and age-related degenerative disease?
    • Campisi J, Andersen JK, Kapahi P, Melov S. Cellular senescence: a link between cancer and age-related degenerative disease? Semin Cancer Biol 2011; 21:354-59.
    • (2011) Semin Cancer Biol , vol.21 , pp. 354-359
    • Campisi, J.1    Andersen, J.K.2    Kapahi, P.3    Melov, S.4
  • 135
    • 33746616991 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 is a critical downstream target of p53 in the induction of replicative senescence
    • Kortlever RM, Higgins PJ, Bernards R. Plasminogen activator inhibitor-1 is a critical downstream target of p53 in the induction of replicative senescence. Nat Cell Biol 2006; 8:877-84.
    • (2006) Nat Cell Biol , vol.8 , pp. 877-884
    • Kortlever, R.M.1    Higgins, P.J.2    Bernards, R.3
  • 137
    • 44649101304 scopus 로고    scopus 로고
    • Oncogeneinduced senescence relayed by an interleukin-dependent inflammatory network
    • Kuilman T, Michaloglou C, Vredeveld LC, et al. Oncogeneinduced senescence relayed by an interleukin-dependent inflammatory network. Cell 2008; 133: 1019-31.
    • (2008) Cell , vol.133 , pp. 1019-1031
    • Kuilman, T.1    Michaloglou, C.2    Vredeveld, L.C.3
  • 138
    • 7944223098 scopus 로고    scopus 로고
    • Ras-induced interleukin-8 expression plays a critical role in tumor growth and angiogenesis
    • Sparmann A, Bar-Sagi D. Ras-induced interleukin-8 expression plays a critical role in tumor growth and angiogenesis. Cancer Cell 2004; 6: 447-58.
    • (2004) Cancer Cell , vol.6 , pp. 447-458
    • Sparmann, A.1    Bar-Sagi, D.2
  • 139
    • 34447506658 scopus 로고    scopus 로고
    • Oncogenic Ras-induced secretion of IL6 is required for tumorigenesis
    • Ancrile B, Lim KH, Counter CM. Oncogenic Ras-induced secretion of IL6 is required for tumorigenesis. Genes Dev 2007; 21:1714-19.
    • (2007) Genes Dev , vol.21 , pp. 1714-1719
    • Ancrile, B.1    Lim, K.H.2    Counter, C.M.3
  • 140
    • 77950343306 scopus 로고    scopus 로고
    • IL-6 and MYC collaborate in plasma cell tumor formation in mice
    • Rutsch S, Neppalli VT, Shin DM, et al. IL-6 and MYC collaborate in plasma cell tumor formation in mice. Blood 2010; 115:1746-54.
    • (2010) Blood , vol.115 , pp. 1746-1754
    • Rutsch, S.1    Neppalli, V.T.2    Shin, D.M.3
  • 141
    • 18244378255 scopus 로고    scopus 로고
    • MtmRNA gene expression, via IL-6 and glucocorticoids, as potential genetic marker of immunosenescence: Lessons from very old mice and humans
    • Mocchegiani E, Giacconi R, Cipriano C, et al. MtmRNA gene expression, via IL-6 and glucocorticoids, as potential genetic marker of immunosenescence: lessons from very old mice and humans. Exp Gerontol 2002; 37: 349-57.
    • (2002) Exp Gerontol , vol.37 , pp. 349-357
    • Mocchegiani, E.1    Giacconi, R.2    Cipriano, C.3
  • 142
    • 0026793281 scopus 로고
    • Differential expression of metalloproteinase and tissue inhibitor of metalloproteinase genes in aged human fibroblasts
    • Millis AJ, Hoyle M, McCue HM, Martini H. Differential expression of metalloproteinase and tissue inhibitor of metalloproteinase genes in aged human fibroblasts. Exp Cell Res 1992; 201: 373-79.
    • (1992) Exp Cell Res , vol.201 , pp. 373-379
    • Millis, A.J.1    Hoyle, M.2    McCue, H.M.3    Martini, H.4
  • 143
    • 58349092595 scopus 로고    scopus 로고
    • Metallothionein is upregulated by hypoxia and stabilizes hypoxia-inducible factor in the kidney
    • Kojima I, Tanaka T, Inagi R, et al. Metallothionein is upregulated by hypoxia and stabilizes hypoxia-inducible factor in the kidney. Kidney Int 2009; 75: 268-77.
    • (2009) Kidney Int , vol.75 , pp. 268-277
    • Kojima, I.1    Tanaka, T.2    Inagi, R.3
  • 144
    • 33947129286 scopus 로고    scopus 로고
    • Cardiac overexpression of metallothionein attenuates chronic alcohol intake-induced cardiomyocyte contractile dysfunction
    • Li Q, Ren J. Cardiac overexpression of metallothionein attenuates chronic alcohol intake-induced cardiomyocyte contractile dysfunction. Cardiovasc Toxicol 2006; 6: 173-82.
    • (2006) Cardiovasc Toxicol , vol.6 , pp. 173-182
    • Li, Q.1    Ren, J.2
  • 145
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell 2006; 124: 471-84.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 146
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N, Sonenberg N. Upstream and downstream of mTOR. Genes Dev 2004; 18:1926-45.
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 147
    • 50549087736 scopus 로고    scopus 로고
    • Growth stimulation leads to cellular senescence when the cell cycle is blocked
    • Demidenko ZN, Blagosklonny MV. Growth stimulation leads to cellular senescence when the cell cycle is blocked. Cell Cycle 2008; 7:3355-61.
    • (2008) Cell Cycle , vol.7 , pp. 3355-3361
    • Demidenko, Z.N.1    Blagosklonny, M.V.2
  • 148
    • 20444363122 scopus 로고    scopus 로고
    • The coordinate regulation of the p53 and mTOR pathways in cells
    • Feng Z, Zhang H, Levine AJ, Jin S. The coordinate regulation of the p53 and mTOR pathways in cells. Proc Natl Acad Sci USA 2005; 102: 8204-09.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8204-8209
    • Feng, Z.1    Zhang, H.2    Levine, A.J.3    Jin, S.4
  • 150
    • 0034058549 scopus 로고    scopus 로고
    • The function of zinc metallothionein: A link between cellular zinc and redox state
    • Maret W. The function of zinc metallothionein: a link between cellular zinc and redox state. J Nutr 2000; 130: 1455S-1458S.
    • (2000) J Nutr , vol.130
    • Maret, W.1
  • 151
    • 0344441890 scopus 로고    scopus 로고
    • A DNA damage checkpoint response in telomere-initiated senescence
    • d'Adda di Fagagna F, Reaper PM, Clay-Farrace L, et al. A DNA damage checkpoint response in telomere-initiated senescence. Nature 2003; 426: 194-98.
    • (2003) Nature , vol.426 , pp. 194-198
    • d'Adda di Fagagna, F.1    Reaper, P.M.2    Clay-Farrace, L.3
  • 152
    • 2442511752 scopus 로고    scopus 로고
    • Telomere shortening triggers senescence of human cells through a pathway involving ATM, p53, and p21(CIP1), but not p16(INK4a)
    • Herbig U, Jobling WA, Chen BP, Chen DJ, Sedivy JM. Telomere shortening triggers senescence of human cells through a pathway involving ATM, p53, and p21(CIP1), but not p16(INK4a). Mol Cell 2004; 14: 501-13.
    • (2004) Mol Cell , vol.14 , pp. 501-513
    • Herbig, U.1    Jobling, W.A.2    Chen, B.P.3    Chen, D.J.4    Sedivy, J.M.5
  • 153
    • 33846937033 scopus 로고    scopus 로고
    • Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
    • Xue W, Zender L, Miething C, et al. Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas. Nature 2007; 445: 656-60.
    • (2007) Nature , vol.445 , pp. 656-660
    • Xue, W.1    Zender, L.2    Miething, C.3
  • 154
    • 0028856794 scopus 로고
    • Telomere length and replicative aging in human vascular tissues
    • Chang E, Harley CB. Telomere length and replicative aging in human vascular tissues. Proc Natl Acad Sci USA 1995; 92: 11190-94.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11190-11194
    • Chang, E.1    Harley, C.B.2
  • 155
    • 66449084405 scopus 로고    scopus 로고
    • p38alpha and p38gamma mediate oncogenic ras-induced senescence through differential mechanisms
    • Kwong J, Hong L, Liao R, Deng Q, Han J, Sun P. p38alpha and p38gamma mediate oncogenic ras-induced senescence through differential mechanisms. J Biol Chem 2009; 284: 11237-46.
    • (2009) J Biol Chem , vol.284 , pp. 11237-11246
    • Kwong, J.1    Hong, L.2    Liao, R.3    Deng, Q.4    Han, J.5    Sun, P.6
  • 156
    • 84857020239 scopus 로고    scopus 로고
    • Micronutrient (Zn, Cu, Fe)-gene interactions in ageing and inflammatory age-related diseases: Implications for treatments
    • Mocchegiani E, Costarelli L, Giacconi R, Piacenza F, Basso A, Malavolta M. Micronutrient (Zn, Cu, Fe)-gene interactions in ageing and inflammatory age-related diseases: implications for treatments. Ageing Res Rev 2012; 11: 297-319.
    • (2012) Ageing Res Rev , vol.11 , pp. 297-319
    • Mocchegiani, E.1    Costarelli, L.2    Giacconi, R.3    Piacenza, F.4    Basso, A.5    Malavolta, M.6
  • 157
    • 80055113353 scopus 로고    scopus 로고
    • Activation of Sirt1 by resveratrol inhibits TNF-β induced inflammation in fibroblasts
    • Zhu X, Liu Q, Wang M, et al. Activation of Sirt1 by resveratrol inhibits TNF-β induced inflammation in fibroblasts. PLoS One 2011; 6: e27081.
    • (2011) PLoS One , vol.6
    • Zhu, X.1    Liu, Q.2    Wang, M.3
  • 158
    • 84859520675 scopus 로고    scopus 로고
    • Involvement of sirtuins in life-span and aging related diseases
    • Mahlknecht U, Zschoernig B. Involvement of sirtuins in life-span and aging related diseases. Adv Exp Med Biol 2012; 739: 252-61.
    • (2012) Adv Exp Med Biol , vol.739 , pp. 252-261
    • Mahlknecht, U.1    Zschoernig, B.2
  • 159
    • 71849090002 scopus 로고    scopus 로고
    • Dual role of Zn2+ in maintaining structural integrity and suppressing deacetylase activity of SIRT1
    • Chen L, Feng Y, Zhou Y, et al. Dual role of Zn2+ in maintaining structural integrity and suppressing deacetylase activity of SIRT1. J Inorg Biochem 2010; 104:180-85.
    • (2010) J Inorg Biochem , vol.104 , pp. 180-185
    • Chen, L.1    Feng, Y.2    Zhou, Y.3
  • 160
    • 35349011597 scopus 로고    scopus 로고
    • Sirt1 modulates premature senescence-like phenotype in human endothelial cells
    • Ota H, Akishita M, Eto M, Iijima K, Kaneki M, Ouchi Y. Sirt1 modulates premature senescence-like phenotype in human endothelial cells. J Mol Cell Cardiol 2007; 43: 571-79.
    • (2007) J Mol Cell Cardiol , vol.43 , pp. 571-579
    • Ota, H.1    Akishita, M.2    Eto, M.3    Iijima, K.4    Kaneki, M.5    Ouchi, Y.6
  • 161
    • 79952455618 scopus 로고    scopus 로고
    • TOR signaling never gets old: Aging, longevity and TORC1 activity
    • Evans DS, Kapahi P, Hsueh WC, Kockel L. TOR signaling never gets old: aging, longevity and TORC1 activity. Ageing Res Rev 2011; 10: 225-37.
    • (2011) Ageing Res Rev , vol.10 , pp. 225-237
    • Evans, D.S.1    Kapahi, P.2    Hsueh, W.C.3    Kockel, L.4
  • 162
    • 58349088356 scopus 로고    scopus 로고
    • Metallothionein: A new soldier in the fight against chronic renal hypoxia?
    • Bauer R. Metallothionein: a new soldier in the fight against chronic renal hypoxia? Kidney Int 2009; 75: 257-59.
    • (2009) Kidney Int , vol.75 , pp. 257-259
    • Bauer, R.1
  • 163
    • 84855886815 scopus 로고    scopus 로고
    • Dietary restriction in rats and mice: A meta-analysis and review of the evidence for genotype-dependent effects on lifespan
    • Swindell WR. Dietary restriction in rats and mice: a meta-analysis and review of the evidence for genotype-dependent effects on lifespan. Ageing Res Rev 2012; 11: 254-70.
    • (2012) Ageing Res Rev , vol.11 , pp. 254-270
    • Swindell, W.R.1
  • 165
    • 4344609497 scopus 로고    scopus 로고
    • Microarray profiling of progesteroneregulated endometrial genes during the rhesus monkey secretory phase
    • Ace CI, Okulicz WC. Microarray profiling of progesteroneregulated endometrial genes during the rhesus monkey secretory phase. Reprod Biol Endocrinol 2004; 2: 54-58.
    • (2004) Reprod Biol Endocrinol , vol.2 , pp. 54-58
    • Ace, C.I.1    Okulicz, W.C.2
  • 166
    • 41949125616 scopus 로고    scopus 로고
    • Pennington CALERIE Team. Is caloric restriction associated with development of eating-disorder symptoms? Results from the CALERIE trial
    • Williamson DA, Martin CK, Anton SD, et al. Pennington CALERIE Team. Is caloric restriction associated with development of eating-disorder symptoms? Results from the CALERIE trial. Health Psychol 2008; 27: S32-42.
    • (2008) Health Psychol , vol.27
    • Williamson, D.A.1    Martin, C.K.2    Anton, S.D.3
  • 167
    • 84859816154 scopus 로고    scopus 로고
    • Caloric restriction alters the metabolic response to a mixed-meal: Results from a randomized, controlled trial
    • Huffman KM, Redman LM, Landerman LR, et al. Caloric restriction alters the metabolic response to a mixed-meal: results from a randomized, controlled trial. PLoS One 2012; 7: e28190.
    • (2012) PLoS One , vol.7
    • Huffman, K.M.1    Redman, L.M.2    Landerman, L.R.3
  • 168
    • 84863404830 scopus 로고    scopus 로고
    • CALERIE Study Group. Approaches for quantifying energy intake and % calorie restriction during calorie restriction interventions in humans: The multicenter CALERIE study
    • Racette SB, Das SK, Bhapkar M, et al. CALERIE Study Group. Approaches for quantifying energy intake and % calorie restriction during calorie restriction interventions in humans: the multicenter CALERIE study. Am J Physiol Endocrinol Metab 2012; 302: E441-8.
    • (2012) Am J Physiol Endocrinol Metab , vol.302
    • Racette, S.B.1    Das, S.K.2    Bhapkar, M.3
  • 169
    • 84864017471 scopus 로고    scopus 로고
    • Caloric Restriction may reverse age-related autonomic decline in humans
    • Apr 17. doi: 10.1111/j.1474-9726.2012.00825.x
    • Stein PK, Soare A, Meyer TE, Cangemi R, Holloszy JO, Fontana L. Caloric Restriction may reverse age-related autonomic decline in humans. Aging Cell 2012 Apr 17. doi: 10.1111/j.1474-9726.2012.00825.x.
    • (2012) Aging Cell
    • Stein, P.K.1    Soare, A.2    Meyer, T.E.3    Cangemi, R.4    Holloszy, J.O.5    Fontana, L.6
  • 170
    • 0018821441 scopus 로고
    • Comparison of the zinc binding domains in the 7S nerve growth factor and the zincinsulin hexamer
    • Dunn MF, Pattison SE, Storm MC, Quiel E. Comparison of the zinc binding domains in the 7S nerve growth factor and the zincinsulin hexamer. Biochemistry 1980: 19: 718-25.
    • (1980) Biochemistry , vol.19 , pp. 718-725
    • Dunn, M.F.1    Pattison, S.E.2    Storm, M.C.3    Quiel, E.4
  • 171
    • 24344488003 scopus 로고    scopus 로고
    • Fluctuations of cellular, available zinc modulate insulin signaling via inhibition of protein tyrosine phosphatases
    • Haase H, Maret W. Fluctuations of cellular, available zinc modulate insulin signaling via inhibition of protein tyrosine phosphatases. J Trace Elem Med Biol 2005; 19: 37-42.
    • (2005) J Trace Elem Med Biol , vol.19 , pp. 37-42
    • Haase, H.1    Maret, W.2
  • 172
    • 79551632441 scopus 로고    scopus 로고
    • Application of phi29 motor pRNA for targeted therapeutic delivery of siRNA silencing metallothionein-IIA and survivin in ovarian cancers
    • Tarapore P, Shu Y, Guo P, Ho SM. Application of phi29 motor pRNA for targeted therapeutic delivery of siRNA silencing metallothionein-IIA and survivin in ovarian cancers. Mol Ther 2011; 19: 386-94.
    • (2011) Mol Ther , vol.19 , pp. 386-394
    • Tarapore, P.1    Shu, Y.2    Guo, P.3    Ho, S.M.4
  • 173
    • 38449118426 scopus 로고    scopus 로고
    • Metallothionein is upregulated under hypoxia and promotes the survival of human prostate cancer cells
    • Yamasaki M, Nomura T, Sato F, Mimata H. Metallothionein is upregulated under hypoxia and promotes the survival of human prostate cancer cells. Oncol Rep 2007; 18: 1145-53.
    • (2007) Oncol Rep , vol.18 , pp. 1145-1153
    • Yamasaki, M.1    Nomura, T.2    Sato, F.3    Mimata, H.4
  • 174
    • 42649142261 scopus 로고    scopus 로고
    • Zinc, metallothioneins, longevity: Effect of zinc supplementation on antioxidant response: A Zincage study
    • Mocchegiani E; Zincage Consortium. Zinc, metallothioneins, longevity: effect of zinc supplementation on antioxidant response: a Zincage study. Rejuvenation Res 2008; 11:419-23.
    • (2008) Rejuvenation Res , vol.11 , pp. 419-423
    • Mocchegiani, E.1
  • 175
    • 84862532394 scopus 로고    scopus 로고
    • Zinc supplementation augments in vivo antitumor effect of chemotherapy by restoring p53 function
    • Sep 19. doi: 10.1002/ijc.26441
    • Margalit O, Simon AJ, Yakubov E, et al. Zinc supplementation augments in vivo antitumor effect of chemotherapy by restoring p53 function. Int J Cancer 2011 Sep 19. doi: 10.1002/ijc.26441.
    • (2011) Int J Cancer
    • Margalit, O.1    Simon, A.J.2    Yakubov, E.3


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