메뉴 건너뛰기




Volumn 4, Issue 1, 2013, Pages 82-91

Zinc biochemistry: From a single zinc enzyme to a key element of life

Author keywords

[No Author keywords available]

Indexed keywords

CARBONATE DEHYDRATASE; PROTEIN; ZINC; ZINC FINGER PROTEIN;

EID: 84879446511     PISSN: 21618313     EISSN: 21565376     Source Type: Journal    
DOI: 10.3945/an.112.003038     Document Type: Review
Times cited : (569)

References (97)
  • 1
    • 0002826692 scopus 로고
    • Etudes chimiques sur la vegetation
    • Raulin J. Etudes chimiques sur la vegetation. Ann Sci Nat Bot Biol Veg. 1869;11:92-299.
    • (1869) Ann Sci Nat Bot Biol Veg. , vol.11 , pp. 92-299
    • Raulin, J.1
  • 2
    • 0345541017 scopus 로고
    • The normal occurrence of zinc in biologic material
    • Lutz RE. The normal occurrence of zinc in biologic material. J Ind Hyg. 1926;8:127.
    • (1926) J Ind Hyg. , vol.8 , pp. 127
    • Lutz, R.E.1
  • 3
    • 53849109779 scopus 로고
    • The significance of zinc in the living organism
    • Drinker KA, Collier ES. The significance of zinc in the living organism. J Ind Hyg. 1926;8:257.
    • (1926) J Ind Hyg. , vol.8 , pp. 257
    • Drinker, K.A.1    Collier, E.S.2
  • 5
    • 0001152440 scopus 로고
    • Syndrome of iron deficiency anemia, hepatosplenomegaly, hypogonadism, dwarfism and geophagia
    • Prasad AS, Halsted JA, Nadimi M. Syndrome of iron deficiency anemia, hepatosplenomegaly, hypogonadism, dwarfism and geophagia. Am J Med. 1961;31:532-46.
    • (1961) Am J Med. , vol.31 , pp. 532-546
    • Prasad, A.S.1    Halsted, J.A.2    Nadimi, M.3
  • 6
    • 0021505337 scopus 로고
    • History and status of zinc in nutrition
    • O'Dell BL. History and status of zinc in nutrition. Fed Proc. 1984;43: 2821-2.
    • (1984) Fed Proc. , vol.43 , pp. 2821-2822
    • O'Dell, B.L.1
  • 7
    • 51149187338 scopus 로고
    • Carbonic anhydrase
    • Keilin D, Mann T. Carbonic anhydrase. Nature. 1939;144:442-3.
    • (1939) Nature. , vol.144 , pp. 442-443
    • Keilin, D.1    Mann, T.2
  • 8
    • 84862537820 scopus 로고    scopus 로고
    • Discovery of human zinc deficiency: 50 years later
    • Prasad AS. Discovery of human zinc deficiency: 50 years later. J Trace Elem Med Biol. 2012;26:66-9.
    • (2012) J Trace Elem Med Biol. , vol.26 , pp. 66-69
    • Prasad, A.S.1
  • 9
    • 0343349776 scopus 로고
    • Carboxypeptidase, a zinc metalloprotein
    • Vallee BL, Neurath H. Carboxypeptidase, a zinc metalloprotein. J Am Chem Soc. 1954;76:5006-7.
    • (1954) J Am Chem Soc. , vol.76 , pp. 5006-5007
    • Vallee, B.L.1    Neurath, H.2
  • 12
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller J, McLachlan AD, Klug A. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J. 1985;4:1609-14.
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 13
    • 0036853192 scopus 로고    scopus 로고
    • Structural characterization of the human proteome
    • Müller A, MacCallum RM, Sternberg MJ. Structural characterization of the human proteome. Genome Res. 2002;12:1625-41.
    • (2002) Genome Res. , vol.12 , pp. 1625-1641
    • Müller, A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 14
    • 33750928844 scopus 로고    scopus 로고
    • Structural zinc sites
    • Messerschmidt A, Bode W, Cygler M, editors. Chichester, UK: Wiley
    • Auld DS. Structural zinc sites. In: Messerschmidt A, Bode W, Cygler M, editors. Handbook of metalloproteins. Vol. 3. Chichester, UK: Wiley; 2004, p. 403-15.
    • (2004) Handbook of metalloproteins , vol.3 , pp. 403-415
    • Auld, D.S.1
  • 15
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: new insights into structural and functional diversity
    • Laity JH, Lee BM, Wright PE. Zinc finger proteins: new insights into structural and functional diversity. Curr Opin Struct Biol. 2001;11: 39-46.
    • (2001) Curr Opin Struct Biol. , vol.11 , pp. 39-46
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 17
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee BL, Auld DS. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry. 1990;29:5647-59.
    • (1990) Biochemistry. , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 20
    • 0035146853 scopus 로고    scopus 로고
    • Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation
    • Thunnissen MM, Nordlund P, Haeggström JZ. Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol. 2001;8:131-5.
    • (2001) Nat Struct Biol. , vol.8 , pp. 131-135
    • Thunnissen, M.M.1    Nordlund, P.2    Haeggström, J.Z.3
  • 21
    • 0032509320 scopus 로고    scopus 로고
    • Zinc fingers in Caenorhabditis elegans: Finding families and probing pathways
    • Clarke ND, Berg JM. Zinc fingers in Caenorhabditis elegans: Finding families and probing pathways. Science. 1998;282:2018-22.
    • (1998) Science. , vol.282 , pp. 2018-2022
    • Clarke, N.D.1    Berg, J.M.2
  • 22
    • 1342303474 scopus 로고    scopus 로고
    • Exploring the zinc proteome
    • Maret W. Exploring the zinc proteome. J Anal At Spectrom. 2004;19: 15-9.
    • (2004) J Anal At Spectrom. , vol.19 , pp. 15-19
    • Maret, W.1
  • 23
  • 24
    • 84896865791 scopus 로고    scopus 로고
    • Protein Data Bank, last accessed October 18
    • Protein Data Bank. http://www.rcsb.org, last accessed October 18, 2012.
    • (2012)
  • 26
    • 77953674718 scopus 로고    scopus 로고
    • Bioinformatics in bioinorganic chemistry
    • Bertini I, Cavallaro G. Bioinformatics in bioinorganic chemistry. Metallomics. 2010;2:39-51.
    • (2010) Metallomics. , vol.2 , pp. 39-51
    • Bertini, I.1    Cavallaro, G.2
  • 28
    • 57749112844 scopus 로고    scopus 로고
    • Zinc proteomics and the annotation of the human zinc proteome
    • Maret W. Zinc proteomics and the annotation of the human zinc proteome. Pure Appl Chem. 2008;80:2679-87.
    • (2008) Pure Appl Chem. , vol.80 , pp. 2679-2687
    • Maret, W.1
  • 29
    • 77952561593 scopus 로고    scopus 로고
    • Metalloproteomics, metalloproteomes, and the annotation of metalloproteins
    • Maret W. Metalloproteomics, metalloproteomes, and the annotation of metalloproteins. Metallomics. 2010;2:117-25.
    • (2010) Metallomics. , vol.2 , pp. 117-125
    • Maret, W.1
  • 30
    • 84881507393 scopus 로고    scopus 로고
    • Zinc and the zinc proteome
    • Banci L, guest editor. Sigel A, Sigel H, Sigel RKO, series editors. Metal ions in life sciences. Dordrecht, the Netherlands: Springer Science + Business Media B.V.
    • Maret W. Zinc and the zinc proteome. In: Banci L, guest editor. Metallomics and the cell. Sigel A, Sigel H, Sigel RKO, series editors. Metal ions in life sciences. Vol. 12. Dordrecht, the Netherlands: Springer Science + Business Media B.V.; 2013.
    • (2013) Metallomics and the cell , vol.12
    • Maret, W.1
  • 31
    • 1642263925 scopus 로고    scopus 로고
    • Protein Interface Zinc Sites
    • Messerschmidt A, Bode W, Cygler M, editors. Chichester, UK: Wiley
    • Maret W. Protein Interface Zinc Sites, In: Messerschmidt A, Bode W, Cygler M, editors. Handbook of metalloproteins Vol. 3. Chichester, UK: Wiley; 2004.
    • (2004) Handbook of metalloproteins , vol.3
    • Maret, W.1
  • 33
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee BL, Falchuk K. The biochemical basis of zinc physiology. Physiol Rev. 1993;73:79-118.
    • (1993) Physiol Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.2
  • 34
    • 80054737086 scopus 로고    scopus 로고
    • Minimal functional sites allow classification of zinc sites in proteins
    • Andreini C, Bertini I, Cavallaro G. Minimal functional sites allow classification of zinc sites in proteins. PLoS ONE. 2011;6:e26325.
    • (2011) PLoS ONE. , vol.6
    • Andreini, C.1    Bertini, I.2    Cavallaro, G.3
  • 35
    • 79960156125 scopus 로고    scopus 로고
    • Molecular and genetic features of zinc transporters in physiology and pathogenesis
    • Fukada T, Kambe T. Molecular and genetic features of zinc transporters in physiology and pathogenesis. Metallomics. 2011;3:662-74.
    • (2011) Metallomics. , vol.3 , pp. 662-674
    • Fukada, T.1    Kambe, T.2
  • 36
    • 67650050211 scopus 로고    scopus 로고
    • Mammalian zinc transporters: nutritional and physiologic regulation
    • Lichten LA, Cousins RJ. Mammalian zinc transporters: nutritional and physiologic regulation. Annu Rev Nutr. 2009;29:153-76.
    • (2009) Annu Rev Nutr. , vol.29 , pp. 153-176
    • Lichten, L.A.1    Cousins, R.J.2
  • 37
    • 0035693722 scopus 로고    scopus 로고
    • Eukaryotic zinc transporters and their regulation
    • Gaither LA, Eide DJ. Eukaryotic zinc transporters and their regulation. Biometals. 2001;14:251-70.
    • (2001) Biometals. , vol.14 , pp. 251-270
    • Gaither, L.A.1    Eide, D.J.2
  • 39
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter Yiip
    • Lu M, Chai J, Fu D. Structural basis for autoregulation of the zinc transporter Yiip. Nat Struct Mol Biol. 2009;16:1063-7.
    • (2009) Nat Struct Mol Biol. , vol.16 , pp. 1063-1067
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 40
    • 34447105299 scopus 로고    scopus 로고
    • Understanding the mechanism of zinc-sensing by metal-responsive element binding transcription factor-1 (MTF-1)
    • Laity JH, Andrews GK. Understanding the mechanism of zinc-sensing by metal-responsive element binding transcription factor-1 (MTF-1). Arch Biochem Biophys. 2007;463:201-10.
    • (2007) Arch Biochem Biophys. , vol.463 , pp. 201-210
    • Laity, J.H.1    Andrews, G.K.2
  • 41
  • 43
    • 48249086955 scopus 로고    scopus 로고
    • Human metallothionein metallomics
    • Li Y, Maret W. Human metallothionein metallomics. J Anal At Spectrom. 2008;23:1055-62.
    • (2008) J Anal At Spectrom. , vol.23 , pp. 1055-1062
    • Li, Y.1    Maret, W.2
  • 44
    • 0023937834 scopus 로고
    • Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
    • Arseniev A, Schultze B, Wörgötter E, Braun W, Wagner G, Vasak M, Kägi JHR, Wüthrich K. Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J Mol Biol. 1988;201:637-57.
    • (1988) J Mol Biol. , vol.201 , pp. 637-657
    • Arseniev, A.1    Schultze, B.2    Wörgötter, E.3    Braun, W.4    Wagner, G.5    Vasak, M.6    Kägi, J.H.R.7    Wüthrich, K.8
  • 46
    • 34848847551 scopus 로고    scopus 로고
    • The nanomolar and picomolar Zn(II) binding properties of metallothionein
    • Kreżel A, Maret W. The 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
  • 47
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothionein confer redox activity on zinc clusters
    • Maret W, Vallee BL. Thiolate ligands in metallothionein confer redox activity on zinc clusters. Proc Natl Acad Sci U S A. 1998;95:3478-82.
    • (1998) Proc Natl Acad Sci U S A. , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 48
    • 84865270893 scopus 로고    scopus 로고
    • The stoichiometric transition from Zn6Cu1-metallothionein to Zn7-metallothionein underlies the up-regulation of metallothionein (MT) expression
    • Alvarez L, Gonzales-Iglesias H, Garcia M, Gosh S, Sanz-Medel A, Coca-Prados M. The stoichiometric transition from Zn6Cu1-metallothionein to Zn7-metallothionein underlies the up-regulation of metallothionein (MT) expression. J Biol Chem. 2012;287:28456-69.
    • (2012) J Biol Chem. , vol.287 , pp. 28456-28469
    • Alvarez, L.1    Gonzales-Iglesias, H.2    Garcia, M.3    Gosh, S.4    Sanz-Medel, A.5    Coca-Prados, M.6
  • 49
    • 0017361007 scopus 로고
    • Copper-thionein from fetal bovine liver
    • Hartmann HJ, Weser U. Copper-thionein from fetal bovine liver. Biochim Biophys Acta. 1977;491:211-22.
    • (1977) Biochim Biophys Acta. , vol.491 , pp. 211-222
    • Hartmann, H.J.1    Weser, U.2
  • 50
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Uchida Y, Takio K, Titani K, Ihara Y, Tomonaga M. The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein. Neuron. 1991;7:337-47.
    • (1991) Neuron. , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 51
    • 40949108071 scopus 로고    scopus 로고
    • Thionein/metallothionein control Zn(II) availability and the activity of enzymes
    • Kreżel A, Maret W. Thionein/metallothionein control Zn(II) availability and the activity of enzymes. J Biol Inorg Chem. 2008;13:401-9.
    • (2008) J Biol Inorg Chem. , vol.13 , pp. 401-409
    • Krezel, A.1    Maret, W.2
  • 52
    • 33947276403 scopus 로고    scopus 로고
    • Different redox states of metallothionein/thionein in biological tissues
    • Kreżel A, Maret W. Different redox states of metallothionein/thionein in biological tissues. Biochem J. 2007;402:551-8.
    • (2007) Biochem J. , vol.402 , pp. 551-558
    • Krezel, A.1    Maret, W.2
  • 53
    • 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;281:681-7.
    • (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
  • 54
    • 59449095419 scopus 로고    scopus 로고
    • Molecular aspects of human cellular zinc homeostasis: redox control of zinc potentials and zinc signals
    • Maret W. Molecular aspects of human cellular zinc homeostasis: redox control of zinc potentials and zinc signals. Biometals. 2009;22:149-57.
    • (2009) Biometals. , vol.22 , pp. 149-157
    • Maret, W.1
  • 55
    • 1642389890 scopus 로고    scopus 로고
    • Zinc and sulfur: a critical biological partnership
    • Maret W. Zinc and sulfur: a critical biological partnership. Biochemistry. 2004;43:3301-9.
    • (2004) Biochemistry. , vol.43 , pp. 3301-3309
    • Maret, W.1
  • 56
    • 0015239110 scopus 로고
    • Metal complexes of phosphoglucomutase in vivo
    • Peck EJ, Ray WJ. Metal complexes of phosphoglucomutase in vivo. J Biol Chem. 1971;246:1160-7.
    • (1971) J Biol Chem. , vol.246 , pp. 1160-1167
    • Peck, E.J.1    Ray, W.J.2
  • 58
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • Simons TJB. Intracellular free zinc and zinc buffering in human red blood cells. J Membr Biol. 1991;123:63-71.
    • (1991) J Membr Biol. , vol.123 , pp. 63-71
    • Simons, T.J.B.1
  • 59
    • 33745029895 scopus 로고    scopus 로고
    • Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor
    • Bozym RA, Thompson RB, Stoddard AK, Fierke CA. Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor. ACS Chem Biol. 2006;1:103-11.
    • (2006) ACS Chem Biol. , vol.1 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 60
    • 33751223540 scopus 로고    scopus 로고
    • Zinc buffering capacity of a eukaryotic cell at physiological pH
    • Kreżel A, Maret W. Zinc buffering capacity of a eukaryotic cell at physiological pH. J Inorg Biol Chem. 2006;11:1049-62.
    • (2006) J Inorg Biol Chem. , vol.11 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 64
    • 34447106867 scopus 로고    scopus 로고
    • The zinc/thiolate redox biochemistry of metallothionein and the control of zinc ion fluctuations in cell signaling
    • Kreżel A, Hao Q, Maret W. The zinc/thiolate redox biochemistry of metallothionein and the control of zinc ion fluctuations in cell signaling. Arch Biochem Biophys. 2007;463:188-200.
    • (2007) Arch Biochem Biophys. , vol.463 , pp. 188-200
    • Krezel, A.1    Hao, Q.2    Maret, W.3
  • 65
    • 70350680995 scopus 로고    scopus 로고
    • Coordination dynamics of zinc in proteins
    • Maret W, Li Y. Coordination dynamics of zinc in proteins. Chem Rev. 2009;109:4682-707.
    • (2009) Chem Rev. , vol.109 , pp. 4682-4707
    • Maret, W.1    Li, Y.2
  • 67
    • 77952566927 scopus 로고    scopus 로고
    • Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis
    • Colvin RA, Holmes WR, Fontaine CP, Maret W. Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis. Metallomics. 2010;2:306-17.
    • (2010) Metallomics. , vol.2 , pp. 306-317
    • Colvin, R.A.1    Holmes, W.R.2    Fontaine, C.P.3    Maret, W.4
  • 69
    • 84867812919 scopus 로고    scopus 로고
    • New sensors for quantitative measurement of mitochondrial Zn(2+)
    • Park JG, Qin Y, Galati DF, Palmer AE. New sensors for quantitative measurement of mitochondrial Zn(2+). ACS Chem Biol. 2012;7: 1636-40.
    • (2012) ACS Chem Biol. , vol.7 , pp. 1636-1640
    • Park, J.G.1    Qin, Y.2    Galati, D.F.3    Palmer, A.E.4
  • 70
    • 85054637697 scopus 로고    scopus 로고
    • The regulatory and signaling functions of zinc ions in human cellular physiology
    • Zalups R, Koropatnick J, editors. Boca Raton, FL: Taylor and Francis
    • Haase H, Maret W. The regulatory and signaling functions of zinc ions in human cellular physiology. In: Zalups R, Koropatnick J, editors. Cellular and molecular biology of metals. Boca Raton, FL: Taylor and Francis; 2009, p. 181-212.
    • (2009) Cellular and molecular biology of metals , pp. 181-212
    • Haase, H.1    Maret, W.2
  • 71
    • 67649229609 scopus 로고    scopus 로고
    • Transient fluctuations of intracellular zinc ions in cell proliferation
    • Li Y, Maret W. Transient fluctuations of intracellular zinc ions in cell proliferation. Exp Cell Res. 2009;315:2463-70.
    • (2009) Exp Cell Res. , vol.315 , pp. 2463-2470
    • Li, Y.1    Maret, W.2
  • 72
    • 0028860021 scopus 로고
    • Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels
    • Atar D, Backx PH, Appel MM, Gao WD, Marban E. Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels. J Biol Chem. 1995;270:2473-7.
    • (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
  • 73
    • 33645740498 scopus 로고    scopus 로고
    • 2+]i and metallothionein level of rat heart via restoration of cell redox cycle
    • 2+]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
  • 74
    • 79960398834 scopus 로고    scopus 로고
    • 2+ concentration, Slc39 (Zip), and metallothionein gene expression in primary pancreatic islet b-cells
    • 2+ concentration, Slc39 (Zip), and metallothionein gene expression in primary pancreatic islet b-cells. J Biol Chem. 2011;286:25778-89.
    • (2011) J Biol Chem. , vol.286 , pp. 25778-25789
    • Bellomo, E.A.1    Meur, G.2    Rutter, G.A.3
  • 76
    • 33646126495 scopus 로고    scopus 로고
    • Flow cytometric measurement of labile zinc in peripheral blood mononuclear cells
    • Haase H, Hebel S, Engelhardt G, Rink L. Flow cytometric measurement of labile zinc in peripheral blood mononuclear cells. Anal Biochem. 2006;352:222-30.
    • (2006) Anal Biochem. , vol.352 , pp. 222-230
    • Haase, H.1    Hebel, S.2    Engelhardt, G.3    Rink, L.4
  • 78
    • 0030746608 scopus 로고    scopus 로고
    • High-affinity inhibition of NMDA NR1-NR2A receptors
    • Paoletti P, Ascher P, Neyton J. High-affinity inhibition of NMDA NR1-NR2A receptors. J Neurosci. 1997;17:5711-25.
    • (1997) J Neurosci. , vol.17 , pp. 5711-5725
    • Paoletti, P.1    Ascher, P.2    Neyton, J.3
  • 79
    • 79960504449 scopus 로고    scopus 로고
    • Zinc in neurotransmission
    • Tóth K. Zinc in neurotransmission. Annu Rev Nutr. 2011;31:139-53.
    • (2011) Annu Rev Nutr. , vol.31 , pp. 139-153
    • Tóth, K.1
  • 80
    • 79952744484 scopus 로고    scopus 로고
    • Zinc transporter ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory
    • Sindreu C, Palmiter RD, Storm DR. Zinc transporter ZnT-3 regulates presynaptic Erk1/2 signaling and hippocampus-dependent memory. Proc Natl Acad Sci U S A. 2011;108:3366-70.
    • (2011) Proc Natl Acad Sci U S A. , vol.108 , pp. 3366-3370
    • Sindreu, C.1    Palmiter, R.D.2    Storm, D.R.3
  • 81
    • 84862306310 scopus 로고    scopus 로고
    • Zinc in specialized secretory tissues: roles in the pancreas, prostate, and mammary gland
    • Kelleher SL, McCormick NH, Velasquez V, Lopez V. Zinc in specialized secretory tissues: roles in the pancreas, prostate, and mammary gland. Adv Nutr. 2011;2:101-11.
    • (2011) Adv Nutr. , vol.2 , pp. 101-111
    • Kelleher, S.L.1    McCormick, N.H.2    Velasquez, V.3    Lopez, V.4
  • 82
    • 13244277917 scopus 로고    scopus 로고
    • Zinc-specific autometallographic in vivo selenium methods: tracing of zinc-enriched (ZEN) pathways, and pools of zinc ions in a multitude of other ZEN cells
    • Danscher G, Stoltenberg M. Zinc-specific autometallographic in vivo selenium methods: tracing of zinc-enriched (ZEN) pathways, and pools of zinc ions in a multitude of other ZEN cells. J Histochem Cytochem. 2005;53:141-53.
    • (2005) J Histochem Cytochem. , vol.53 , pp. 141-153
    • Danscher, G.1    Stoltenberg, M.2
  • 84
    • 61849121844 scopus 로고    scopus 로고
    • Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation
    • Hogstrand C, Kille P, Nicholson RI, Taylor KM. Zinc transporters and cancer: a potential role for ZIP7 as a hub for tyrosine kinase activation. Trends Mol Med. 2009;15:101-11.
    • (2009) Trends Mol Med. , vol.15 , pp. 101-111
    • Hogstrand, C.1    Kille, P.2    Nicholson, R.I.3    Taylor, K.M.4
  • 85
    • 84856998257 scopus 로고    scopus 로고
    • Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7
    • ra11
    • Taylor KM, Hiscox S, Nicholson RI, Hogstrand C, Kille P. Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. Sci Signal. 2012;5:ra11.
    • (2012) Sci Signal. , vol.5
    • Taylor, K.M.1    Hiscox, S.2    Nicholson, R.I.3    Hogstrand, C.4    Kille, P.5
  • 88
  • 89
    • 84863393278 scopus 로고    scopus 로고
    • Picomolar concentrations of free zinc(II) ions regulate receptor protein tyrosine phosphatase beta activity
    • Wilson M, Hogstrand C, Maret W. Picomolar concentrations of free zinc(II) ions regulate receptor protein tyrosine phosphatase beta 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
  • 91
    • 0021645190 scopus 로고
    • Zinc: what is its role in biology?
    • Williams RJP. Zinc: what is its role in biology? Endeavour. 1984;8:65-70.
    • (1984) Endeavour. , vol.8 , pp. 65-70
    • Williams, R.J.P.1
  • 92
    • 0030964915 scopus 로고    scopus 로고
    • Coordination dynamics of biological zinc clusters in metallothioneins and in the DNA-binding domain of the transcription factor Gal4
    • Maret W, Larsen KS, Vallee BL. Coordination dynamics of biological zinc clusters in metallothioneins and in the DNA-binding domain of the transcription factor Gal4. Proc Natl Acad Sci U S A. 1997;94: 2233-7.
    • (1997) Proc Natl Acad Sci U S A. , vol.94 , pp. 2233-2237
    • Maret, W.1    Larsen, K.S.2    Vallee, B.L.3
  • 93
    • 80755153625 scopus 로고    scopus 로고
    • Redox biochemistry of mammalian metallothioneins
    • Maret W. Redox biochemistry of mammalian metallothioneins. J Biol Inorg Chem. 2011;16:1079-86.
    • (2011) J Biol Inorg Chem. , vol.16 , pp. 1079-1086
    • Maret, W.1
  • 94
    • 84856994470 scopus 로고    scopus 로고
    • Amsterdam, the Netherlands: IOS Press
    • Rink L, editor. Zinc in human health. Amsterdam, the Netherlands: IOS Press; 2011.
    • (2011) Zinc in human health
    • Rink, L.1
  • 95
    • 79959997623 scopus 로고    scopus 로고
    • Metals on the move: zinc ions in cellular regulation and in the coordination dynamics of zinc proteins
    • MaretW. Metals on the move: zinc ions in cellular regulation and in the coordination dynamics of zinc proteins. Biometals. 2011;24:411-8.
    • (2011) Biometals. , vol.24 , pp. 411-418
    • Maret, W.1
  • 96
    • 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;43:363-9.
    • (2008) Exp Gerontol. , vol.43 , pp. 363-369
    • Maret, W.1
  • 97
    • 33646036991 scopus 로고    scopus 로고
    • Zinc requirements and the risks and benefits of zinc supplementation
    • Maret W, Sandstead HH. Zinc requirements and the risks and benefits of zinc supplementation. J Trace Elem Med Biol. 2006;20:3-18.
    • (2006) J Trace Elem Med Biol. , vol.20 , pp. 3-18
    • Maret, W.1    Sandstead, H.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.