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Volumn 8, Issue 2, 2005, Pages 161-170

Imbalance between pro-oxidant and pro-antioxidant functions of zinc in disease

Author keywords

Alzheimer's Disease; AP 1; Metallothionein thionein; NF B; Oxidative stress; p53; Zinc

Indexed keywords

ANTIOXIDANT; APOLIPOPROTEIN A1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; METALLOTHIONEIN; PROTEIN P53; ZINC FINGER PROTEIN;

EID: 32544452896     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2005-8209     Document Type: Review
Times cited : (65)

References (118)
  • 1
    • 0019497412 scopus 로고
    • A possible role of zinc in the pathology of dementia
    • F.M. Burnet, A possible role of zinc in the pathology of dementia, Lancet 1 (1981), 186-188.
    • (1981) Lancet , vol.1 , pp. 186-188
    • Burnet, F.M.1
  • 2
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • B.L. Vallee and K.H. Falchuk, The biochemical basis of zinc physiology, Physiol Rev 73 (1993), 79-118.
    • (1993) Physiol Rev , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 3
    • 20144377557 scopus 로고    scopus 로고
    • The neurobiology of zinc in health and disease
    • C.J. Frederickson, J.Y. Koh and A.I. Bush, The neurobiology of zinc in health and disease, Nat Rev Neurosci 6 (2005), 449-462.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 449-462
    • Frederickson, C.J.1    Koh, J.Y.2    Bush, A.I.3
  • 4
    • 0036308552 scopus 로고    scopus 로고
    • A novel member of a zinc transporter family is defective in Acrodermatitis enteropathica
    • K. Wang, B. Zhou, Y.M. Kuo, J. Zemansky and J. Gitschier, A novel member of a zinc transporter family is defective in Acrodermatitis enteropathica, Am J Hum Genet 71 (2002), 66-73.
    • (2002) Am J Hum Genet , vol.71 , pp. 66-73
    • Wang, K.1    Zhou, B.2    Kuo, Y.M.3    Zemansky, J.4    Gitschier, J.5
  • 6
    • 0242694859 scopus 로고    scopus 로고
    • Zinc is essential for brain development and function
    • H.H. Sandstead, Zinc is essential for brain development and function, J Trace Elem Exp Med 16 (2003), 165-173.
    • (2003) J Trace Elem Exp Med , vol.16 , pp. 165-173
    • Sandstead, H.H.1
  • 7
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • C.J. Frederickson, Neurobiology of zinc and zinc-containing neurons, Int Rev Neurobiol 31 (1989), 145-238.
    • (1989) Int Rev Neurobiol , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 8
    • 0035696287 scopus 로고    scopus 로고
    • Synaptically released zinc: Physiological functions and pathological effects
    • C.J. Frederickson and A.I. Bush, Synaptically released zinc: physiological functions and pathological effects, Biometals 14 (2001), 353-366.
    • (2001) Biometals , vol.14 , pp. 353-366
    • Frederickson, C.J.1    Bush, A.I.2
  • 9
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • A.I. Bush, The metallobiology of Alzheimer's disease, Trends Neurosci 26 (2003), 207-214.
    • (2003) Trends Neurosci , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 12
    • 1642389890 scopus 로고    scopus 로고
    • Zinc and sulfur: A critical biological partnership
    • W. Maret, Zinc and sulfur: a critical biological partnership, Biochemistry 43 (2004), 3301-3309.
    • (2004) Biochemistry , vol.43 , pp. 3301-3309
    • Maret, W.1
  • 13
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothionein confer redox activity on zinc clusters
    • W. Maret and B.L. Vallee, Thiolate ligands in metallothionein confer redox activity on zinc clusters, Proc Natl Acad Sci USA 95 (1998), 3478-3482.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 14
    • 0034866622 scopus 로고    scopus 로고
    • Redox control of zinc finger proteins: Mechanisms and role in gene regulation
    • S.H. Lee and W. Maret, Redox control of zinc finger proteins: mechanisms and role in gene regulation, Antioxid Redox Signal 3 (2001), 531-534.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 531-534
    • Lee, S.H.1    Maret, W.2
  • 15
    • 24344445329 scopus 로고    scopus 로고
    • Zinc coordination environments in proteins determine zinc functions
    • available on line 3 May 2005
    • W. Maret, Zinc coordination environments in proteins determine zinc functions, J Trace Elem Med Biol (2005), available on line 3 May 2005.
    • (2005) J Trace Elem Med Biol
    • Maret, W.1
  • 16
    • 18244377997 scopus 로고    scopus 로고
    • Keap1, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein
    • A.T. Dinkova-Kostova, W.D. Holtzclaw and N. Wakabayashi, Keap1, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein, Biochemistry 44 (2005), 6889-6899.
    • (2005) Biochemistry , vol.44 , pp. 6889-6899
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Wakabayashi, N.3
  • 17
    • 0001950228 scopus 로고    scopus 로고
    • The Glutathione Redox State and Zinc Mobilization from Metallothionein and other Proteins with Zinc/Sulfur Coordination Sites
    • C.A. Shaw, ed., Washington D.C.
    • W. Maret, The Glutathione Redox State and Zinc Mobilization from Metallothionein and other Proteins with Zinc/Sulfur Coordination Sites, in: Glutathione in the Nervous System, Taylor and Francis, C.A. Shaw, ed., Washington D.C., 1998, pp. 257-273.
    • (1998) Glutathione in the Nervous System, Taylor and Francis , pp. 257-273
    • Maret, W.1
  • 18
    • 0015239110 scopus 로고
    • Metal complexes of phosphoglucomutase in vivo
    • E.J. Peck, Jr. and W.J. Ray, Jr., Metal complexes of phosphoglucomutase in vivo, J Biol Chem 246 (1971), 1160-1167.
    • (1971) J Biol Chem , vol.246 , pp. 1160-1167
    • Peck Jr., E.J.1    Ray Jr., W.J.2
  • 19
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • T.J.B. Simons, Intracellular free zinc and zinc buffering in human red blood cells, J Membr Biol 123 (1991), 63-71.
    • (1991) J Membr Biol , vol.123 , pp. 63-71
    • Simons, T.J.B.1
  • 20
    • 0030961933 scopus 로고    scopus 로고
    • Study of the interactions of cadmium and zinc ions with cellular calcium homeostasis using 19F-NMR spectroscopy
    • J. Benters, U. Flögel, T. Schäfer, D. Leibfritz, S. Hechtenberg and D. Beyersmann, Study of the interactions of cadmium and zinc ions with cellular calcium homeostasis using 19F-NMR spectroscopy, Biochem 7322 (1997), 793-799.
    • (1997) Biochem , vol.7322 , pp. 793-799
    • Benters, J.1    Flögel, U.2    Schäfer, T.3    Leibfritz, D.4    Hechtenberg, S.5    Beyersmann, D.6
  • 21
    • 0028860021 scopus 로고
    • Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels
    • D. Atar, P.H. Backx, M.M. Appel, W.D. Gao and E. Marban, Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels, J Biol Chem 270 (1995), 2473-2477.
    • (1995) J Biol Chem , vol.270 , pp. 2473-2477
    • Atar, D.1    Backx, P.H.2    Appel, M.M.3    Gao, W.D.4    Marban, E.5
  • 23
    • 0031953881 scopus 로고    scopus 로고
    • Zinc and brain injury
    • D.W. Choi and J.Y. Koh, Zinc and brain injury, Annu Rev Neurosci 21 (1998), 347-375.
    • (1998) Annu Rev Neurosci , vol.21 , pp. 347-375
    • Choi, D.W.1    Koh, J.Y.2
  • 25
    • 0030979005 scopus 로고    scopus 로고
    • Oxidants increase intracellular free Zn2+ concentration in rabbit ventricular myocytes
    • B. Turan, H. Fliss and M. Désilets, Oxidants increase intracellular free Zn2+ concentration in rabbit ventricular myocytes, Am J Physiol 272 (1997), H2095-H2106.
    • (1997) Am J Physiol , vol.272
    • Turan, B.1    Fliss, H.2    Désilets, M.3
  • 26
    • 0033788519 scopus 로고    scopus 로고
    • Induction of neuronal apoptosis by thiol oxidation: Putative role of intracellular zinc release
    • E. Aizenman, A.K. Stout, K.A. Hartnett, K.E Dineley, B. McLaughlin and I.J. Reynolds, Induction of neuronal apoptosis by thiol oxidation: Putative role of intracellular zinc release, J Neurochem 75 (2000), 1878-1888.
    • (2000) J Neurochem , vol.75 , pp. 1878-1888
    • Aizenman, E.1    Stout, A.K.2    Hartnett, K.A.3    Dineley, K.E.4    McLaughlin, B.5    Reynolds, I.J.6
  • 28
    • 0345564814 scopus 로고    scopus 로고
    • Regulation of zinc homeostasis by inducible NO synthase-derived NO: Nuclear metallothionein translocation and intranuclear Zn2+ release
    • D.U. Spahl, D. Berendji-Grün, C.V. Suschek, V. Kolb-Bachofen and K.D. Kröncke, Regulation of zinc homeostasis by inducible NO synthase-derived NO: nuclear metallothionein translocation and intranuclear Zn2+ release, Proc Natl Acad Sci USA 100 (2003), 13952-13957.
    • (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
  • 29
    • 0021645190 scopus 로고
    • Zinc: What is its role in biology?
    • R.J.P. Williams, Zinc: what is its role in biology? Endeavour 8 (1984), 65-70.
    • (1984) Endeavour , vol.8 , pp. 65-70
    • Williams, R.J.P.1
  • 30
    • 0033514994 scopus 로고    scopus 로고
    • Inhibitory sites in enzymes: Zinc removal and reactivation by thionein
    • W. Maret, C. Jacob, B.L. Vallee and E.H. Fischer, Inhibitory sites in enzymes: zinc removal and reactivation by thionein, Proc Natl Acad Sci USA 96 (1999), 1936-1940.
    • (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
  • 31
    • 0035969898 scopus 로고    scopus 로고
    • Enzyme regulation by reversible zinc inhibition: Glycerol phosphate dehydrogenase as an example
    • W. Maret, C.A. Yetman and L.J. Jiang, Enzyme regulation by reversible zinc inhibition: glycerol phosphate dehydrogenase as an example, Chem Biol Interact 130-132 (2001), 893-903.
    • (2001) Chem Biol Interact , vol.130-132 , pp. 893-903
    • Maret, W.1    Yetman, C.A.2    Jiang, L.J.3
  • 32
    • 0037155880 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
    • I.G. Gazaryan, B.F. Krasnikov, G.A. Ashby, R.N. Thorneley, B.S. Kristal and A.M. Brown, Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase, J Biol Chem 277 (2002), 10064-10072.
    • (2002) J Biol Chem , vol.277 , pp. 10064-10072
    • Gazaryan, I.G.1    Krasnikov, B.F.2    Ashby, G.A.3    Thorneley, R.N.4    Kristal, B.S.5    Brown, A.M.6
  • 33
    • 0344010194 scopus 로고    scopus 로고
    • Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling
    • H. Haase and W. Maret, Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling, Exp Cell Res 291 (2003), 289-298.
    • (2003) Exp Cell Res , vol.291 , pp. 289-298
    • Haase, H.1    Maret, W.2
  • 35
    • 0030691761 scopus 로고    scopus 로고
    • Zinc inhibition of mitochondrial aconitase and its importance in citrate metabolism of prostate epithelial cells
    • L.C. Costello, Y. Liu, R.B. Franklin and M.C. Kennedy, Zinc inhibition of mitochondrial aconitase and its importance in citrate metabolism of prostate epithelial cells, J Biol Chem 272 (1997), 28875-28881.
    • (1997) J Biol Chem , vol.272 , pp. 28875-28881
    • Costello, L.C.1    Liu, Y.2    Franklin, R.B.3    Kennedy, M.C.4
  • 37
    • 0035956862 scopus 로고    scopus 로고
    • Zinc metallothionein imported into liver mitochondria modulates respiration
    • B. Ye, W. Maret and B.L. Vallee, Zinc metallothionein imported into liver mitochondria modulates respiration, Proc Natl Acad Sci USA 98 (2001), 2317-2322.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2317-2322
    • Ye, B.1    Maret, W.2    Vallee, B.L.3
  • 38
    • 0035861677 scopus 로고    scopus 로고
    • Zn(2+) induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria
    • D. Jiang, P.G. Sullivan, S.L. Sensi, O. Steward and J.H. Weiss, Zn(2+) induces permeability transition pore opening and release of pro-apoptotic peptides from neuronal mitochondria, J Biol Chem 276 (2001), 47524-47529.
    • (2001) J Biol Chem , vol.276 , pp. 47524-47529
    • Jiang, D.1    Sullivan, P.G.2    Sensi, S.L.3    Steward, O.4    Weiss, J.H.5
  • 39
    • 0025239795 scopus 로고
    • The physiological role of zinc as an antioxidant
    • T.M. Bray and W.J. Bettger, The physiological role of zinc as an antioxidant, Free Radic Biol Med 8 (1990), 281-291.
    • (1990) Free Radic Biol Med , vol.8 , pp. 281-291
    • Bray, T.M.1    Bettger, W.J.2
  • 40
    • 0034099055 scopus 로고    scopus 로고
    • The antioxidant properties of zinc
    • S.R. Powell, The antioxidant properties of zinc, J Nutr 130 (2000), 1447S-1454S.
    • (2000) J Nutr , vol.130
    • Powell, S.R.1
  • 42
    • 0028915120 scopus 로고
    • Zinc deficiency causes oxidative damage to proteins, lipids and DNA in rat testes
    • P.I. Oteiza, K.L. Olin, C.G. Fraga and C.L. Keen, Zinc deficiency causes oxidative damage to proteins, lipids and DNA in rat testes, J Nutr 125 (1995), 823-829.
    • (1995) J Nutr , vol.125 , pp. 823-829
    • Oteiza, P.I.1    Olin, K.L.2    Fraga, C.G.3    Keen, C.L.4
  • 43
    • 0037219351 scopus 로고    scopus 로고
    • Zinc takes the center stage: Its paradoxical role in Alzheimer's disease
    • M.P. Cuajungco and K.Y. Faget, Zinc takes the center stage: its paradoxical role in Alzheimer's disease, Brain Res Rev 41 (2003), 44-56.
    • (2003) Brain Res Rev , vol.41 , pp. 44-56
    • Cuajungco, M.P.1    Faget, K.Y.2
  • 44
    • 0038810225 scopus 로고    scopus 로고
    • A global view of the selectivity of zinc deprivation and excess on genes expressed in human THP-1 mononuclear cells
    • R.J. Cousins, R.K. Blanchard, M.P. Popp, L. Liu, J. Cao, J.B. Moore and C.L. Green, A global view of the selectivity of zinc deprivation and excess on genes expressed in human THP-1 mononuclear cells, Proc Natl Acad Sci USA 100 (2003), 6952-6957.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6952-6957
    • Cousins, R.J.1    Blanchard, R.K.2    Popp, M.P.3    Liu, L.4    Cao, J.5    Moore, J.B.6    Green, C.L.7
  • 45
    • 4344580481 scopus 로고    scopus 로고
    • Nutrient-gene interactions: A single nutrient and hundreds of target genes
    • H. Daniel and H.T. Dieck, Nutrient-gene interactions: a single nutrient and hundreds of target genes, Biol Chem 385 (2004), 571-583.
    • (2004) Biol Chem , vol.385 , pp. 571-583
    • Daniel, H.1    Dieck, H.T.2
  • 46
    • 0034024644 scopus 로고    scopus 로고
    • Zinc deficiency induces oxidative stress and AP-1 activation in 3T3 cells
    • P.I. Oteiza, M.S. Clegg, M.P. Zago and C.L. Keen, Zinc deficiency induces oxidative stress and AP-1 activation in 3T3 cells, Free Radic Biol Med 28 (2000), 1091-1099.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1091-1099
    • Oteiza, P.I.1    Clegg, M.S.2    Zago, M.P.3    Keen, C.L.4
  • 47
    • 0032955669 scopus 로고    scopus 로고
    • Antioxidant-like properties of zinc in activated endothelial cells
    • B. Hennig, P. Meerarani, M. Toborek and C.J. McClain, Antioxidant-like properties of zinc in activated endothelial cells, J Am Coll Nutr 18 (1999), 152-158.
    • (1999) J Am Coll Nutr , vol.18 , pp. 152-158
    • Hennig, B.1    Meerarani, P.2    Toborek, M.3    McClain, C.J.4
  • 49
    • 4344586103 scopus 로고    scopus 로고
    • Metal-responsive transcription factor-1 (MTF-1) selects different types of metal response elements at low vs. high zinc concentration
    • Y. Wang, I. Lorenzi, O. Georgiev and W. Schaffner, Metal-responsive transcription factor-1 (MTF-1) selects different types of metal response elements at low vs. high zinc concentration, Biol Chem 385 (2004), 623-632.
    • (2004) Biol Chem , vol.385 , pp. 623-632
    • Wang, Y.1    Lorenzi, I.2    Georgiev, O.3    Schaffner, W.4
  • 50
    • 0038637993 scopus 로고    scopus 로고
    • Zinc inhibition of cellular energy production: Implications for mitochondria and neurodegeneration
    • K.E. Dineley, T.V. Votyakova and I.J. Reynolds, Zinc inhibition of cellular energy production: implications for mitochondria and neurodegeneration, J Neurochem 85 (2003), 563-570.
    • (2003) J Neurochem , vol.85 , pp. 563-570
    • Dineley, K.E.1    Votyakova, T.V.2    Reynolds, I.J.3
  • 52
    • 0035826695 scopus 로고    scopus 로고
    • Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein
    • Y. Yang, W. Maret and B.L. Vallee, Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein, Proc Natl Acad Sci USA 98 (2001), 5556-5559.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5556-5559
    • Yang, Y.1    Maret, W.2    Vallee, B.L.3
  • 53
    • 0037008050 scopus 로고    scopus 로고
    • S-Nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation
    • Y. Chen, Y. Irie, W.M. Keung and W. Maret, S-Nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation, Biochemistry 41 (2002), 8360-8367.
    • (2002) Biochemistry , vol.41 , pp. 8360-8367
    • Chen, Y.1    Irie, Y.2    Keung, W.M.3    Maret, W.4
  • 55
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Y. Uchida, K. Takio, K. Titani, Y. Ihara and M. Tomonaga, The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein, Neuron 7 (1991), 337-347.
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 56
    • 0344394903 scopus 로고    scopus 로고
    • Zinc released from metallothionein-III may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury
    • J.Y. Lee, J.H. Kim, R.D. Palmiter and J.Y. Koh, Zinc released from metallothionein-III may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury, Exp Neurol 184 (2003), 337-347.
    • (2003) Exp Neurol , vol.184 , pp. 337-347
    • Lee, J.Y.1    Kim, J.H.2    Palmiter, R.D.3    Koh, J.Y.4
  • 57
    • 14644397252 scopus 로고    scopus 로고
    • Zn7metallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A
    • M. Knipp, G. Meloni, B. Roschitzki and M. Vasak, Zn7metallothionein-3 and the synaptic vesicle cycle: interaction of metallothionein-3 with the small GTPase Rab3A, Biochemistry 44 (2005), 3159-3165.
    • (2005) Biochemistry , vol.44 , pp. 3159-3165
    • Knipp, M.1    Meloni, G.2    Roschitzki, B.3    Vasak, M.4
  • 58
    • 0036941677 scopus 로고    scopus 로고
    • A distinct Cu(4)-thiolate cluster of human metallothionein-3 is located in the N-terminal domain
    • B. Roschitzki and M. Vasak, A distinct Cu(4)-thiolate cluster of human metallothionein-3 is located in the N-terminal domain, J Biol Inorg Chem 7 (2002), 611-616.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 611-616
    • Roschitzki, B.1    Vasak, M.2
  • 59
    • 0035693751 scopus 로고    scopus 로고
    • The role of zinc in caspase activation and apoptotic cell death
    • A.Q. Truong-Tran, J. Carter, R.E. Ruffin and P.D. Zalewski, The role of zinc in caspase activation and apoptotic cell death, Biometals 14 (2001), 315-330.
    • (2001) Biometals , vol.14 , pp. 315-330
    • Truong-Tran, A.Q.1    Carter, J.2    Ruffin, R.E.3    Zalewski, P.D.4
  • 60
    • 0035025062 scopus 로고    scopus 로고
    • A decrease in intracellular zinc level precedes the detection of early indicators of apoptosis in HL-60 cells
    • J.Y. Duffy, C.M. Miller, G.L. Rutschilling, G.M. Ridder, M.S. Clegg, C.L. Keen and G.P. Daston, A decrease in intracellular zinc level precedes the detection of early indicators of apoptosis in HL-60 cells, Apoptosis 6 (2001), 161-172.
    • (2001) Apoptosis , vol.6 , pp. 161-172
    • Duffy, J.Y.1    Miller, C.M.2    Rutschilling, G.L.3    Ridder, G.M.4    Clegg, M.S.5    Keen, C.L.6    Daston, G.P.7
  • 61
    • 0028922876 scopus 로고
    • The influence of zinc on apoptosis
    • F.W. Sunderman, Jr., The influence of zinc on apoptosis, Ann Clin Lab Sci 25 (1995), 134-142.
    • (1995) Ann Clin Lab Sci , vol.25 , pp. 134-142
    • Sunderman Jr., F.W.1
  • 62
    • 0030907004 scopus 로고    scopus 로고
    • A reappraisal of the role of zinc in life and death decisions of cells
    • P.J. Fraker and W.G. Telford, A reappraisal of the role of zinc in life and death decisions of cells, Proc Soc Exp Biol Med 215 (1997), 229-236.
    • (1997) Proc Soc Exp Biol Med , vol.215 , pp. 229-236
    • Fraker, P.J.1    Telford, W.G.2
  • 63
    • 0030855488 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis
    • D.K. Perry, M.J. Smyth, H.R. Stennicke, G.S. Salvesen, P. Duriez, G.G. Poirier and Y.A. Hannun, Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis, J Biol Chem 272 (1997), 18530-18533.
    • (1997) J Biol Chem , vol.272 , pp. 18530-18533
    • Perry, D.K.1    Smyth, M.J.2    Stennicke, H.R.3    Salvesen, G.S.4    Duriez, P.5    Poirier, G.G.6    Hannun, Y.A.7
  • 64
    • 17144377113 scopus 로고    scopus 로고
    • IAPs, RINGs and ubiquitylation
    • D.L. Vaux and J. Silke, IAPs, RINGs and ubiquitylation, Nat Rev Mol Cell Biol 6 (2005), 287-297.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 287-297
    • Vaux, D.L.1    Silke, J.2
  • 65
    • 11144249792 scopus 로고    scopus 로고
    • Physiological functions for brain NF-kappaB
    • M.K. Meffert and D. Baltimore, Physiological functions for brain NF-kappaB, Trends Neurosci 28 (2005), 37-43.
    • (2005) Trends Neurosci , vol.28 , pp. 37-43
    • Meffert, M.K.1    Baltimore, D.2
  • 66
    • 0033774342 scopus 로고    scopus 로고
    • The role of p53 in neuronal cell death
    • R.S. Morrison and Y. Kinoshita, The role of p53 in neuronal cell death, Cell Death Differ 7 (2000), 868-879.
    • (2000) Cell Death Differ , vol.7 , pp. 868-879
    • Morrison, R.S.1    Kinoshita, Y.2
  • 67
    • 0035971563 scopus 로고    scopus 로고
    • AP-1 proteins in the adult brain: Facts and fiction about effectors of neuroprotection and neurodegeneration
    • T. Herdegen and V. Waetzig, AP-1 proteins in the adult brain: facts and fiction about effectors of neuroprotection and neurodegeneration, Oncogene 20 (2001), 2424-2437.
    • (2001) Oncogene , vol.20 , pp. 2424-2437
    • Herdegen, T.1    Waetzig, V.2
  • 68
    • 0035696301 scopus 로고    scopus 로고
    • Functions of zinc in signaling, proliferation and differentiation of mammalian cells
    • D. Beyersmann and H. Haase, Functions of zinc in signaling, proliferation and differentiation of mammalian cells, BioMetals 14 (2001), 331-341.
    • (2001) BioMetals , vol.14 , pp. 331-341
    • Beyersmann, D.1    Haase, H.2
  • 69
    • 0029063792 scopus 로고
    • Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc
    • W. Maret, Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc, Neurochem Int 27 (1995), 111-117.
    • (1995) Neurochem Int , vol.27 , pp. 111-117
    • Maret, W.1
  • 70
    • 0034745011 scopus 로고    scopus 로고
    • Control of IkappaBalpha proteolysis by the ubiquitin-proteasome pathway
    • K. Tanaka, T. Kawakami, K. Tateishi, H. Yashiroda and T. Chiba, Control of IkappaBalpha proteolysis by the ubiquitin-proteasome pathway, Biochimie 83 (2001), 351-356.
    • (2001) Biochimie , vol.83 , pp. 351-356
    • Tanaka, K.1    Kawakami, T.2    Tateishi, K.3    Yashiroda, H.4    Chiba, T.5
  • 71
    • 3142612926 scopus 로고    scopus 로고
    • The RING-H2-finger protein APC11 as a target of hydrogen peroxide
    • T.S. Chang, W. Jeong, D.Y. Lee, C.S. Cho and S.G. Rhee, The RING-H2-finger protein APC11 as a target of hydrogen peroxide, Free Radic Biol Med 37 (2004), 521-530.
    • (2004) Free Radic Biol Med , vol.37 , pp. 521-530
    • Chang, T.S.1    Jeong, W.2    Lee, D.Y.3    Cho, C.S.4    Rhee, S.G.5
  • 72
    • 0026056918 scopus 로고
    • 2+ dependence, and differential half-site recognition
    • 2+ dependence, and differential half-site recognition, J Biol Chem 266 (1991), 252-260.
    • (1991) J Biol Chem , vol.266 , pp. 252-260
    • Zabel, U.1    Schreck, R.2    Baeuerle, P.A.3
  • 73
    • 0032518199 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B binding to DNA by chromium, cadmium, mercury, zinc, and arsenite in vitro: Evidence of a thiol mechanism
    • J.A. Shumilla, K.E. Wetterhahn and A. Barchowsky, Inhibition of NF-kappa B binding to DNA by chromium, cadmium, mercury, zinc, and arsenite in vitro: evidence of a thiol mechanism, Arch Biochem Biophys 349 (1998), 356-362.
    • (1998) Arch Biochem Biophys , vol.349 , pp. 356-362
    • Shumilla, J.A.1    Wetterhahn, K.E.2    Barchowsky, A.3
  • 74
    • 0036847701 scopus 로고    scopus 로고
    • Zinc inhibits nuclear factor-kappa B activation and sensitizes prostate cancer cells to cytotoxic agents
    • R.G. Uzzo, P. Leavis, W. Hatch, V.L. Gabai, N. Dulin, N. Zvartau and V.M. Kolenko, Zinc inhibits nuclear factor-kappa B activation and sensitizes prostate cancer cells to cytotoxic agents, Clin Cancer Res 8 (2002), 3579-3583.
    • (2002) Clin Cancer Res , vol.8 , pp. 3579-3583
    • Uzzo, R.G.1    Leavis, P.2    Hatch, W.3    Gabai, V.L.4    Dulin, N.5    Zvartau, N.6    Kolenko, V.M.7
  • 75
    • 0030754776 scopus 로고    scopus 로고
    • Zinc attenuates tumor necrosis factor-mediated activation of transcription factors in endothelial cells
    • P. Connell, V.M. Young, M. Toborek, D.A. Cohen, S. Barve, C.J. McClain and B. Hennig, Zinc attenuates tumor necrosis factor-mediated activation of transcription factors in endothelial cells, J Am Coll Nutr 16 (1997), 411-417.
    • (1997) J Am Coll Nutr , vol.16 , pp. 411-417
    • Connell, P.1    Young, V.M.2    Toborek, M.3    Cohen, D.A.4    Barve, S.5    McClain, C.J.6    Hennig, B.7
  • 76
    • 0037168653 scopus 로고    scopus 로고
    • Low intracellular zinc induces oxidative DNA damage, disrupts p53, NFκB, and AP1 DNA binding, and affects DNA repair in a rat glioma cell line
    • E. Ho and B.N. Ames, Low intracellular zinc induces oxidative DNA damage, disrupts p53, NFκB, and AP1 DNA binding, and affects DNA repair in a rat glioma cell line, Proc Natl Acad Sci USA 99 (2002), 16770-16775.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16770-16775
    • Ho, E.1    Ames, B.N.2
  • 77
    • 0035182280 scopus 로고    scopus 로고
    • Short-term zinc deficiency affects nuclear factor-kappab nuclear binding activity in rat testes
    • P.I. Oteiza, M.S. Clegg and C.L. Keen, Short-term zinc deficiency affects nuclear factor-kappab nuclear binding activity in rat testes, J Nutr 131 (2001), 21-26.
    • (2001) J Nutr , vol.131 , pp. 21-26
    • Oteiza, P.I.1    Clegg, M.S.2    Keen, C.L.3
  • 78
    • 0037072944 scopus 로고    scopus 로고
    • Low intracellular zinc impairs the translocation of activated NF-kappa B to the nuclei in human neuroblastoma IMR-32 cells
    • G.G. Mackenzie, M.P. Zago, C.L. Keen and P.I. Oteiza, Low intracellular zinc impairs the translocation of activated NF-kappa B to the nuclei in human neuroblastoma IMR-32 cells, J Biol Chem 277 (2002), 34610-34617.
    • (2002) J Biol Chem , vol.277 , pp. 34610-34617
    • Mackenzie, G.G.1    Zago, M.P.2    Keen, C.L.3    Oteiza, P.I.4
  • 79
    • 2442656756 scopus 로고    scopus 로고
    • Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein
    • H. Cao, J.S. Tuttle and P.I. Blackshear, Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein, J Biol Chem 279 (2004), 21489-21499.
    • (2004) J Biol Chem , vol.279 , pp. 21489-21499
    • Cao, H.1    Tuttle, J.S.2    Blackshear, P.I.3
  • 80
    • 11844251985 scopus 로고    scopus 로고
    • A20 inhibits NF-kappaB activation by dual ubiquitin-editing functions
    • K. Heyninck and R. Beyaert, A20 inhibits NF-kappaB activation by dual ubiquitin-editing functions, Trends Biochem Sci 30 (2005), 1-4.
    • (2005) Trends Biochem Sci , vol.30 , pp. 1-4
    • Heyninck, K.1    Beyaert, R.2
  • 81
    • 0141640785 scopus 로고    scopus 로고
    • Zinc modulates PPARγ signaling and activation of porcine endothelial cells
    • P. Meerarani, G. Reiterer, M. Toborek and B. Hennig, Zinc modulates PPARγ signaling and activation of porcine endothelial cells, J Nutr 133 (2003), 3058-3064.
    • (2003) J Nutr , vol.133 , pp. 3058-3064
    • Meerarani, P.1    Reiterer, G.2    Toborek, M.3    Hennig, B.4
  • 82
    • 3042700222 scopus 로고    scopus 로고
    • Peroxisome proliferator activated receptors alpha and gamma require zinc for their anti-inflammatory properties in porcine vascular endothelial cells
    • G. Reiterer, M. Toborek and B. Hennig, Peroxisome proliferator activated receptors alpha and gamma require zinc for their anti-inflammatory properties in porcine vascular endothelial cells, J Nutr 134 (2004), 1711-1715.
    • (2004) J Nutr , vol.134 , pp. 1711-1715
    • Reiterer, G.1    Toborek, M.2    Hennig, B.3
  • 83
    • 0034058549 scopus 로고    scopus 로고
    • The function of zinc metallothionein: A link between cellular zinc and redox state
    • W. Maret, The function of zinc metallothionein: a link between cellular zinc and redox state, J Nutr 130 (2000), 1455S-1458S.
    • (2000) J Nutr , vol.130
    • Maret, W.1
  • 84
    • 0038670762 scopus 로고    scopus 로고
    • The cellular zinc and redox states converge in the metallothionein/ thionein pair
    • W. Maret, The cellular zinc and redox states converge in the metallothionein/thionein pair, J Nutr 133 (2003), 1460S-1462S.
    • (2003) J Nutr , vol.133
    • Maret, W.1
  • 85
    • 0038150155 scopus 로고    scopus 로고
    • Zinc-induced NF-kappaB inhibition can be modulated by changes in the intracellular metallothionein level
    • C.H. Kim, J.H. Kim, J. Lee and Y.S. Ahn, Zinc-induced NF-kappaB inhibition can be modulated by changes in the intracellular metallothionein level, Toxicol Appl Pharmacol 190 (2003), 189-196.
    • (2003) Toxicol Appl Pharmacol , vol.190 , pp. 189-196
    • Kim, C.H.1    Kim, J.H.2    Lee, J.3    Ahn, Y.S.4
  • 86
    • 1942501608 scopus 로고    scopus 로고
    • Abrogation of nuclear factor-κB activation is involved in zinc inhibition of lipopolysaccharide-induced tumor necrosis factor-α production and liver injury
    • Z. Zhou, L. Wang, Z. Song, J.T. Saari, C.J. McClain and Y.J. Kang, Abrogation of nuclear factor-κB activation is involved in zinc inhibition of lipopolysaccharide-induced tumor necrosis factor-α production and liver injury, Am. J Pathol 164 (2004), 1547-1556.
    • (2004) Am. J Pathol , vol.164 , pp. 1547-1556
    • Zhou, Z.1    Wang, L.2    Song, Z.3    Saari, J.T.4    McClain, C.J.5    Kang, Y.J.6
  • 87
    • 3142691553 scopus 로고    scopus 로고
    • Metallothionein mediates the level and activity of nuclear factor kappaB in murine fibroblasts
    • H.L. Butcher, W.A. Kennette, O. Collins, R.K. Zalups and J. Koropatnick, Metallothionein mediates the level and activity of nuclear factor kappaB in murine fibroblasts, J Pharmacol Exp Ther 310 (2004), 589-598.
    • (2004) J Pharmacol Exp Ther , vol.310 , pp. 589-598
    • Butcher, H.L.1    Kennette, W.A.2    Collins, O.3    Zalups, R.K.4    Koropatnick, J.5
  • 88
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Y. Cho, S. Gorina, P.D. Jeffrey and N.P. Pavletich, Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations, Science 265 (1994), 346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 89
  • 90
    • 0034859507 scopus 로고    scopus 로고
    • Zinc binding and redox control of p53 structure and function
    • P. Hainaut and K. Mann, Zinc binding and redox control of p53 structure and function, Antioxid Redox Signal 3 (2001), 611-623.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 611-623
    • Hainaut, P.1    Mann, K.2
  • 91
    • 0038720319 scopus 로고    scopus 로고
    • Zinc deficiency induces oxidative DNA damage and increases p53 expression in human lung fibroblasts
    • E. Ho, C. Courtemanche and B.N. Ames, Zinc deficiency induces oxidative DNA damage and increases p53 expression in human lung fibroblasts, J Nutr 133 (2003), 2543-2548.
    • (2003) J Nutr , vol.133 , pp. 2543-2548
    • Ho, E.1    Courtemanche, C.2    Ames, B.N.3
  • 92
    • 0034824232 scopus 로고    scopus 로고
    • Zinc status affects p53, gadd45, and c-fos expression and caspase-3 activity in human bronchial epithelial cells
    • J.C. Fanzo, S.K. Reaves, L. Cui, L. Zhu, J.Y.J. Wu, Y.R. Wang and K.Y. Lei, Zinc status affects p53, gadd45, and c-fos expression and caspase-3 activity in human bronchial epithelial cells, Am J Physiol Cell Physiol 281 (2001), C751-757.
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Fanzo, J.C.1    Reaves, S.K.2    Cui, L.3    Zhu, L.4    Wu, J.Y.J.5    Wang, Y.R.6    Lei, K.Y.7
  • 93
    • 0036071295 scopus 로고    scopus 로고
    • P53 protein and p21 mRNA levels and caspase-3 activity are altered by zinc status in aortic endothelial cells
    • J.C. Fanzo, S.K. Reaves, L. Cui, L. Zhu, J.Y.J. Wu and K.Y. Lei, p53 protein and p21 mRNA levels and caspase-3 activity are altered by zinc status in aortic endothelial cells, Am J Physiol Cell Physiol 283 (2002), C631-C638.
    • (2002) Am J Physiol Cell Physiol , vol.283
    • Fanzo, J.C.1    Reaves, S.K.2    Cui, L.3    Zhu, L.4    Wu, J.Y.J.5    Lei, K.Y.6
  • 94
    • 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
    • C. Meplan, M.J. Richard and P. Hainaut, 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 19 (2000), 5227-5236.
    • (2000) Oncogene , vol.19 , pp. 5227-5236
    • Meplan, C.1    Richard, M.J.2    Hainaut, P.3
  • 95
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • E. Shaulian and M. Karin, AP-1 as a regulator of cell life and death, Nat Cell Biol 4 (2002), E131-136.
    • (2002) Nat Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 96
    • 0030006984 scopus 로고    scopus 로고
    • Extracellular zinc ions induces mitogen-activated protein kinase activity and protein tyrosine phosphorylation in bombesin-sensitive Swiss 3T3 fibroblasts
    • A. Hansson, Extracellular zinc ions induces mitogen-activated protein kinase activity and protein tyrosine phosphorylation in bombesin-sensitive Swiss 3T3 fibroblasts, Arch Biochem Biophys 328 (1996), 233-238.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 233-238
    • Hansson, A.1
  • 99
    • 0036850229 scopus 로고    scopus 로고
    • Extracellular zinc stimulates ERK-dependent activation of p21(Cip/WAF1) and inhibits proliferation of colorectal cancer cells
    • K.S. Park, Y. Ahn, J.A. Kim, M.S. Yun, B.L. Seong and K.Y. Choi, Extracellular zinc stimulates ERK-dependent activation of p21(Cip/WAF1) and inhibits proliferation of colorectal cancer cells, Br J Pharmacol 137 (2002), 597-607.
    • (2002) Br J Pharmacol , vol.137 , pp. 597-607
    • Park, K.S.1    Ahn, Y.2    Kim, J.A.3    Yun, M.S.4    Seong, B.L.5    Choi, K.Y.6
  • 101
    • 0001482329 scopus 로고    scopus 로고
    • Induction of an immediate early gene egr-1 by zinc through extracellular signal-regulated kinase activation in cortical culture: Its role in zinc-induced neuronal death
    • J.A. Park and J.Y. Koh, Induction of an immediate early gene egr-1 by zinc through extracellular signal-regulated kinase activation in cortical culture: its role in zinc-induced neuronal death, J Neurochem 73 (1999), 450-456.
    • (1999) J Neurochem , vol.73 , pp. 450-456
    • Park, J.A.1    Koh, J.Y.2
  • 102
    • 0035027723 scopus 로고    scopus 로고
    • Zn(2+) induces stimulation of the c-Jun N-terminal kinase signaling pathway through phosphoinositide 3-kinase
    • S.J. Eom, E.Y. Kim, J.E. Lee, H.J. Kang, J. Shim, S.U. Kim, B.J. Gwag and E.J. Choi, Zn(2+) induces stimulation of the c-Jun N-terminal kinase signaling pathway through phosphoinositide 3-kinase, Mol Pharmacol 59 (2001), 981-986.
    • (2001) Mol Pharmacol , vol.59 , pp. 981-986
    • Eom, S.J.1    Kim, E.Y.2    Lee, J.E.3    Kang, H.J.4    Shim, J.5    Kim, S.U.6    Gwag, B.J.7    Choi, E.J.8
  • 103
    • 0032907983 scopus 로고    scopus 로고
    • Inhibition of insulin-like growth factor-I mitogenic action by zinc chelation is associated with a decreased mitogen-activated protein kinase activation in RAT-1 fibroblasts
    • D. Lefebvre, C.M. Boney, J.M. Ketelslegers and J.P. Thissen, Inhibition of insulin-like growth factor-I mitogenic action by zinc chelation is associated with a decreased mitogen-activated protein kinase activation in RAT-1 fibroblasts, FEBS Lett 449 (1999), 284-288.
    • (1999) FEBS Lett , vol.449 , pp. 284-288
    • Lefebvre, D.1    Boney, C.M.2    Ketelslegers, J.M.3    Thissen, J.P.4
  • 104
    • 0034063878 scopus 로고    scopus 로고
    • The role of zinc in growth and cell proliferation
    • R.S. MacDonald, The role of zinc in growth and cell proliferation, J Nutr 130 (2000), 1500S-1508S.
    • (2000) J Nutr , vol.130
    • MacDonald, R.S.1
  • 105
    • 0014012502 scopus 로고
    • The reduced secretion of, and sensitivity to insulin in zinc-deficient rats
    • J. Quarterman, C.F. Mills and W.R. Humphries, The reduced secretion of, and sensitivity to insulin in zinc-deficient rats, Biochem Biophys Res Commun 25 (1966), 354-358.
    • (1966) Biochem Biophys Res Commun , vol.25 , pp. 354-358
    • Quarterman, J.1    Mills, C.F.2    Humphries, W.R.3
  • 106
    • 0035008149 scopus 로고    scopus 로고
    • Zinc has an insulin-like effect on glucose transport mediated by phosphoinositol-3-kinase and Akt in 3T3-L1 fibroblasts and adipocytes
    • X. Tang and N.F. Shay, Zinc has an insulin-like effect on glucose transport mediated by phosphoinositol-3-kinase and Akt in 3T3-L1 fibroblasts and adipocytes, J Nutr 131 (2001), 1414-1420.
    • (2001) J Nutr , vol.131 , pp. 1414-1420
    • Tang, X.1    Shay, N.F.2
  • 107
    • 24744446561 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases as targets of the combined insulinomimetic effects of zinc and oxidants
    • in press
    • H. Haase and W. Maret, Protein tyrosine phosphatases as targets of the combined insulinomimetic effects of zinc and oxidants, Biometals (2005), in press.
    • (2005) Biometals
    • Haase, H.1    Maret, W.2
  • 108
    • 0023611441 scopus 로고
    • Purified transcription factor AP-1 interacts with TPA-inducible enhancer elements
    • W. Lee, P. Mitchell and R. Tjian, Purified transcription factor AP-1 interacts with TPA-inducible enhancer elements, Cell 49 (1987), 741-752.
    • (1987) Cell , vol.49 , pp. 741-752
    • Lee, W.1    Mitchell, P.2    Tjian, R.3
  • 109
    • 0035834763 scopus 로고    scopus 로고
    • Phosphorylation is involved in the activation of metal-regulatory transcription factor 1 in response to metal ions
    • O. LaRochelle, V. Gagne, J. Charron, J.W. Soh and C. Seguin, Phosphorylation is involved in the activation of metal-regulatory transcription factor 1 in response to metal ions, J Biol Chem 276 (2001), 41879-41888.
    • (2001) J Biol Chem , vol.276 , pp. 41879-41888
    • LaRochelle, O.1    Gagne, V.2    Charron, J.3    Soh, J.W.4    Seguin, C.5
  • 110
    • 0023122946 scopus 로고
    • Metallothionein gene expression is regulated by serum factors and activators of protein kinase C
    • R.J. Imbra and M. Karin, Metallothionein gene expression is regulated by serum factors and activators of protein kinase C, Mol Cell Biol 7 (1987), 1358-1363.
    • (1987) Mol Cell Biol , vol.7 , pp. 1358-1363
    • Imbra, R.J.1    Karin, M.2
  • 112
    • 0034604723 scopus 로고    scopus 로고
    • Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content
    • L.T. Knapp and E. Klann, Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content, J Biol Chem 275 (2000), 24136-24145.
    • (2000) J Biol Chem , vol.275 , pp. 24136-24145
    • Knapp, L.T.1    Klann, E.2
  • 113
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • I. Korichneva, B. Hoyos, R. Chua, E. Levi and U. Hammerling, Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen, J Biol Chem 277 (2002), 44327-44331.
    • (2002) J Biol Chem , vol.277 , pp. 44327-44331
    • Korichneva, I.1    Hoyos, B.2    Chua, R.3    Levi, E.4    Hammerling, U.5
  • 114
    • 0023944916 scopus 로고
    • Zinc can increase the activity of protein kinase C and contributes to its binding to plasma membranes in T lymphocytes
    • P. Csermely, M. Szamel, K. Resch and J. Somogyi, Zinc can increase the activity of protein kinase C and contributes to its binding to plasma membranes in T lymphocytes, J Biol Chem 263 (1988), 6487-6490.
    • (1988) J Biol Chem , vol.263 , pp. 6487-6490
    • Csermely, P.1    Szamel, M.2    Resch, K.3    Somogyi, J.4
  • 115
    • 0026573869 scopus 로고
    • Pineal and retinal protein kinase C isoenzyme: Cooperative activation by calcium and zinc metallothionein
    • C.Z. Ou and M. Ebadi, Pineal and retinal protein kinase C isoenzyme: Cooperative activation by calcium and zinc metallothionein, J Pineal Res 12 (1992), 17-26.
    • (1992) J Pineal Res , vol.12 , pp. 17-26
    • Ou, C.Z.1    Ebadi, M.2
  • 116
    • 6344240735 scopus 로고    scopus 로고
    • Alterations in protein kinase C activity and processing during zinc-deficiency-induced cell death
    • S.S. Chou, M.S. Clegg, T.Y. Momma, B.J. Niles, J.Y. Duffy, G.P. Daston and C.L. Keen, Alterations in protein kinase C activity and processing during zinc-deficiency-induced cell death, Biochem J 383 (2004), 63-71.
    • (2004) Biochem J , vol.383 , pp. 63-71
    • Chou, S.S.1    Clegg, M.S.2    Momma, T.Y.3    Niles, B.J.4    Duffy, J.Y.5    Daston, G.P.6    Keen, C.L.7
  • 117
    • 3142759931 scopus 로고    scopus 로고
    • Secular trends in dietary intake in the United States
    • R.R. Briefel and C.L. Johnson, Secular trends in dietary intake in the United States, Annu. Rev Nutr 24 (2004), 401-431.
    • (2004) Annu. Rev Nutr , vol.24 , pp. 401-431
    • Briefel, R.R.1    Johnson, C.L.2
  • 118
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • T. Lu, Y. Pan, S.Y. Kao, C. Li, I. Kohane, J. Chan and B.A. Yankner, Gene regulation and DNA damage in the ageing human brain, Nature 429 (2004), 883-891.
    • (2004) Nature , vol.429 , pp. 883-891
    • Lu, T.1    Pan, Y.2    Kao, S.Y.3    Li, C.4    Kohane, I.5    Chan, J.6    Yankner, B.A.7


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