메뉴 건너뛰기




Volumn , Issue , 2008, Pages 3-26

Metallothionein structure and reactivity

Author keywords

Copper; Metal cluster reactivity; Metal thiolate cluster; Metallothionein; Structure dynamics; Three dimensional structure; Zinc

Indexed keywords


EID: 84969662816     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1142/9789812778949_0001     Document Type: Chapter
Times cited : (7)

References (89)
  • 1
    • 0023937834 scopus 로고
    • Three-dimensional structure of rabbit liver Cd7metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
    • Arseniev A, Schultze P, Wörgötter E, et al. Three-dimensional structure of rabbit liver Cd7metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J Mol Biol 1988; 201: 637-657.
    • (1988) J Mol Biol , vol.201 , pp. 637-657
    • Arseniev, A.1    Schultze, P.2    Wörgötter, E.3
  • 2
    • 0024426560 scopus 로고
    • Proton NMR studies of the cobalt(II)- metallothionein system
    • Bertini I, Luchinat C, Messori L, Vašák M. Proton NMR studies of the cobalt(II)- metallothionein system. J Am Chem Soc 1989; 111: 7296-7300.
    • (1989) J Am Chem Soc , vol.111 , pp. 7296-7300
    • Bertini, I.1    Luchinat, C.2    Messori, L.3    Vašák, M.4
  • 3
    • 0034669776 scopus 로고    scopus 로고
    • Molecular-dynamics simulation of the beta domain of metallothionein with a semi-empirical treatment of the metal core
    • Berweger CD, Thiel W, van Gunsteren WF. Molecular-dynamics simulation of the beta domain of metallothionein with a semi-empirical treatment of the metal core. Proteins 2000; 41: 299-315.
    • (2000) Proteins , vol.41 , pp. 299-315
    • Berweger, C.D.1    Thiel, W.2    van Gunsteren, W.F.3
  • 4
    • 0002599375 scopus 로고    scopus 로고
    • Metallothionein: Molecular evolution and classification
    • Klaassen C (ed.), Birkhäuser Verlag, Basel
    • Binz PA, Kägi JHR. Metallothionein: Molecular evolution and classification. In: Klaassen C (ed.), Metallothionein IV, Birkhäuser Verlag, Basel, 1999, pp. 7-13.
    • (1999) Metallothionein IV , pp. 7-13
    • Binz, P.A.1    Kägi, J.H.R.2
  • 5
    • 0032127497 scopus 로고    scopus 로고
    • Structural characterization of Cu(I) and Zn(II) sites in neuronal-growth-inhibitory factor by extended X-ray absorption fine structure (EXAFS)
    • Bogumil R, Faller P, Binz PA, et al. Structural characterization of Cu(I) and Zn(II) sites in neuronal-growth-inhibitory factor by extended X-ray absorption fine structure (EXAFS). Eur J Biochem 1998; 255: 172-177.
    • (1998) Eur J Biochem , vol.255 , pp. 172-177
    • Bogumil, R.1    Faller, P.2    Binz, P.A.3
  • 6
    • 0026454919 scopus 로고
    • Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2
    • Braun W, Vašák M, Robbins AH, et al. Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2. Proc Natl Acad Sci USA 1992; 89: 10124-10128.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10124-10128
    • Braun, W.1    Vašák, M.2    Robbins, A.H.3
  • 7
    • 11844293463 scopus 로고    scopus 로고
    • The crystal structure of yeast copper thionein: The solution of a long-lasting enigma
    • Calderone V, Dolderer B, Hartmann HJ, et al. The crystal structure of yeast copper thionein: The solution of a long-lasting enigma. Proc Natl Acad Sci USA 2005; 102: 51-56.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 51-56
    • Calderone, V.1    Dolderer, B.2    Hartmann, H.J.3
  • 8
    • 0037008050 scopus 로고    scopus 로고
    • Nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation
    • Chen Y, Irie Y, Keung WM, Maret WS. Nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation. Biochemistry 2002; 41: 8360-8367.
    • (2002) Biochemistry , vol.41 , pp. 8360-8367
    • Chen, Y.1    Irie, Y.2    Keung, W.M.3    Maret, W.S.4
  • 9
    • 0345276580 scopus 로고    scopus 로고
    • Metallothioneins in human tumors and potential roles in carcinogenesis
    • Cherian G, Jayasurya A, Bay BH. Metallothioneins in human tumors and potential roles in carcinogenesis. Mutat Res 2003; 533: 201-209.
    • (2003) Mutat Res , vol.533 , pp. 201-209
    • Cherian, G.1    Jayasurya, A.2    Bay, B.H.3
  • 10
    • 33748417843 scopus 로고    scopus 로고
    • Mutation at Glu23 eliminates the neuron growth inhibitory activity of human metallothionein-3
    • Ding ZC, Teng XC, Cai B, et al. Mutation at Glu23 eliminates the neuron growth inhibitory activity of human metallothionein-3. Biochem Biophys Res Commun 2006; 349: 674-682.
    • (2006) Biochem Biophys Res Commun , vol.349 , pp. 674-682
    • Ding, Z.C.1    Teng, X.C.2    Cai, B.3
  • 11
    • 35348921706 scopus 로고    scopus 로고
    • Effect of alpha-domain substitution on the structure, property and function of human neuronal growth inhibitory factor
    • Ding ZC, Zheng Q, Cai B, et al. Effect of alpha-domain substitution on the structure, property and function of human neuronal growth inhibitory factor. J Biol Inorg Chem 2007; 12: 1173-1179.
    • (2007) J Biol Inorg Chem , vol.12 , pp. 1173-1179
    • Ding, Z.C.1    Zheng, Q.2    Cai, B.3
  • 12
    • 34247326875 scopus 로고    scopus 로고
    • Coordination of three and four Cu(I) to the α- and ß- domain of vertebrate Zn-metallothionein-1, respectively, induces significant structural changes
    • Dolderer B, Echner H, Beck A, et al. Coordination of three and four Cu(I) to the α- and ß- domain of vertebrate Zn-metallothionein-1, respectively, induces significant structural changes. FEBS J 2007; 274: 2349-2362.
    • (2007) FEBS J , vol.274 , pp. 2349-2362
    • Dolderer, B.1    Echner, H.2    Beck, A.3
  • 13
    • 33749604240 scopus 로고    scopus 로고
    • Metallothionein-3 is a component of a multiprotein complex in the mouse brain
    • El Ghazi I, Martin BL, Armitage IM. Metallothionein-3 is a component of a multiprotein complex in the mouse brain. Exp Biol Med (Maywood) 2006; 231: 1500-1506.
    • (2006) Exp Biol Med (Maywood) , vol.231 , pp. 1500-1506
    • El Ghazi, I.1    Martin, B.L.2    Armitage, I.M.3
  • 14
    • 0028263925 scopus 로고
    • Enhanced neurotrophic activity in Alzheimer’s disease cortex is not associated with down-regulation of metallothionein-III (GIF)
    • Erickson JC, Sewell AK, Jensen LT, et al. Enhanced neurotrophic activity in Alzheimer’s disease cortex is not associated with down-regulation of metallothionein-III (GIF). Brain Res 1994; 649: 297-304.
    • (1994) Brain Res , vol.649 , pp. 297-304
    • Erickson, J.C.1    Sewell, A.K.2    Jensen, L.T.3
  • 16
    • 0033520117 scopus 로고    scopus 로고
    • Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters
    • Faller P, Hasler DW, Zerbe O, et al. Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters. Biochemistry 1999; 38: 10158-10167.
    • (1999) Biochemistry , vol.38 , pp. 10158-10167
    • Faller, P.1    Hasler, D.W.2    Zerbe, O.3
  • 17
    • 17444437606 scopus 로고    scopus 로고
    • Distinct metal-thiolate clusters in the N-terminal domain of neuronal growth inhibitory factor
    • Faller P, Vašák M. Distinct metal-thiolate clusters in the N-terminal domain of neuronal growth inhibitory factor. Biochemistry 1997; 36: 13341-13348.
    • (1997) Biochemistry , vol.36 , pp. 13341-13348
    • Faller, P.1    Vašák, M.2
  • 19
    • 0023821683 scopus 로고
    • 113Cd NMR studies on metal-thiolate cluster formation in rabbit Cd(II)-metallothionein: Evidence for a pH dependence
    • 113Cd NMR studies on metal-thiolate cluster formation in rabbit Cd(II)-metallothionein: Evidence for a pH dependence. Biochemistry 1988; 27: 7163-7166.
    • (1988) Biochemistry , vol.27 , pp. 7163-7166
    • Good, M.1    Hollenstein, R.2    Sadler, P.J.3    Vašák, M.4
  • 20
    • 0025796617 scopus 로고
    • Metal selectivity of clusters in rabbit liver metallothionein
    • Good M, Hollenstein R, Vašák M. Metal selectivity of clusters in rabbit liver metallothionein. Eur J Biochem 1991; 197: 655-659.
    • (1991) Eur J Biochem , vol.197 , pp. 655-659
    • Good, M.1    Hollenstein, R.2    Vašák, M.3
  • 22
    • 0032552960 scopus 로고    scopus 로고
    • Metal-thiolate clusters in the C-terminal domain of human neuronal growth inhibitory factor (GIF)
    • Hasler DW, Faller P, Vašák M. Metal-thiolate clusters in the C-terminal domain of human neuronal growth inhibitory factor (GIF). Biochemistry 1998; 37: 14966-14973.
    • (1998) Biochemistry , vol.37 , pp. 14966-14973
    • Hasler, D.W.1    Faller, P.2    Vašák, M.3
  • 23
    • 0034727640 scopus 로고    scopus 로고
    • Effect of the two conserved prolines of human growth inhibitory factor (metallothionein-3) on its biological activity and structure fluctuation: Comparison with a mutant protein
    • Hasler DW, Jensen LT, Zerbe O, et al. Effect of the two conserved prolines of human growth inhibitory factor (metallothionein-3) on its biological activity and structure fluctuation: Comparison with a mutant protein. Biochemistry 2000; 39: 14567-14575.
    • (2000) Biochemistry , vol.39 , pp. 14567-14575
    • Hasler, D.W.1    Jensen, L.T.2    Zerbe, O.3
  • 24
    • 0028358324 scopus 로고
    • The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression
    • Heuchel R, Radtke F, Georgiev O, et al. The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression. EMBO J 1994; 13: 2870-2875.
    • (1994) EMBO J , vol.13 , pp. 2870-2875
    • Heuchel, R.1    Radtke, F.2    Georgiev, O.3
  • 25
    • 0035872463 scopus 로고    scopus 로고
    • Roles of the metallothionein family of proteins in the central nervous system
    • Hidalgo J, Aschner M, Zatta P, Vašák M. Roles of the metallothionein family of proteins in the central nervous system. Brain Res Bull 2001; 55: 133-145.
    • (2001) Brain Res Bull , vol.55 , pp. 133-145
    • Hidalgo, J.1    Aschner, M.2    Zatta, P.3    Vašák, M.4
  • 26
    • 11244270832 scopus 로고    scopus 로고
    • Expression of neuronal growth inhibitory factor (metallothionein-III) in the salivary gland
    • Irie Y, Mori F, Keung WM, et al. Expression of neuronal growth inhibitory factor (metallothionein-III) in the salivary gland. Physiol Res 2004; 53: 719-723.
    • (2004) Physiol Res , vol.53 , pp. 719-723
    • Irie, Y.1    Mori, F.2    Keung, W.M.3
  • 27
    • 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: 3489-3494.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 28
    • 0032584078 scopus 로고    scopus 로고
    • The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase
    • Jiang LJ, Maret W, Vallee BL. The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase. Proc Natl Acad Sci USA 1998; 95: 3483-3488.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3483-3488
    • Jiang, L.J.1    Maret, W.2    Vallee, B.L.3
  • 29
    • 0023781524 scopus 로고
    • Biochemistry of metallothionein
    • Kägi JHR, Schaffer A. Biochemistry of metallothionein. Biochemistry 1988; 27: 8509-8515.
    • (1988) Biochemistry , vol.27 , pp. 8509-8515
    • Kägi, J.H.R.1    Schaffer, A.2
  • 30
    • 0001593597 scopus 로고
    • Metallothionein: A cadmium- and zinc-containing protein from equine renal cortex
    • Kägi JHR, Vallee B. Metallothionein: A cadmium- and zinc-containing protein from equine renal cortex. J Biol Chem 1960; 235: 3460-3465.
    • (1960) J Biol Chem , vol.235 , pp. 3460-3465
    • Kägi, J.H.R.1    Vallee, B.2
  • 31
    • 0023696141 scopus 로고
    • Overexpression of metallothionein confers resistance to anticancer drugs
    • Kelley SL, Basu A, Teicher BA, et al. Overexpression of metallothionein confers resistance to anticancer drugs. Science 1988; 241: 1813-1815.
    • (1988) Science , vol.241 , pp. 1813-1815
    • Kelley, S.L.1    Basu, A.2    Teicher, B.A.3
  • 32
    • 34548128309 scopus 로고    scopus 로고
    • 2] anticancer complexes: Trans-Pt(II) complexes retain their N-donor ligands
    • 2] anticancer complexes: trans-Pt(II) complexes retain their N-donor ligands. J Med Chem 2007; 50: 4075-4086.
    • (2007) J Med Chem , vol.50 , pp. 4075-4086
    • Knipp, M.1    Karotki, A.V.2    Chesnov, S.3
  • 33
    • 14644397252 scopus 로고    scopus 로고
    • Zn7metallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A
    • Knipp M, Meloni G, Roschitzki B, Vašák M. Zn7metallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A. Biochemistry 2005; 44: 3159-3165.
    • (2005) Biochemistry , vol.44 , pp. 3159-3165
    • Knipp, M.1    Meloni, G.2    Roschitzki, B.3    Vašák, M.4
  • 34
    • 34447106867 scopus 로고    scopus 로고
    • The zinc/thiolate redox biochemistry of metallothionein and the control of zinc ion fluctuations in cell signaling
    • Kre¸z˙el 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
    • Kre¸zel, A.1    Hao, Q.2    Maret, W.3
  • 35
    • 34848847551 scopus 로고    scopus 로고
    • Dual nanomolar and picomolar Zn(II) binding properties of metallothionein
    • Kre¸z˙el A, Maret W. Dual nanomolar and picomolar Zn(II) binding properties of metallothionein. JAm Chem Soc 2007; 129: 10911-10921.
    • (2007) JAm Chem Soc , vol.129 , pp. 10911-10921
    • Kre¸zel, A.1    Maret, W.2
  • 36
    • 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
    • Kroncke 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: 1105-1110.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 1105-1110
    • Kroncke, K.D.1    Fehsel, K.2    Schmidt, T.3
  • 37
    • 0021845412 scopus 로고
    • Formation and characterization of aurothioneins: Au, Zn, Cd-thionein, Au, Cd-thionein, and (thiomalato-Au)chi-thionein
    • Laib JE, Shaw CF, Petering DH, et al. Formation and characterization of aurothioneins: Au, Zn, Cd-thionein, Au, Cd-thionein, and (thiomalato-Au)chi-thionein. Biochemistry 1985; 24: 1977-1986.
    • (1985) Biochemistry , vol.24 , pp. 1977-1986
    • Laib, J.E.1    Shaw, C.F.2    Petering, D.H.3
  • 38
    • 0031595147 scopus 로고    scopus 로고
    • 2+ removal from Zn metallothionein by nitrilotriacetate are associated with differential reactivity of the two metal clusters
    • 2+ removal from Zn metallothionein by nitrilotriacetate are associated with differential reactivity of the two metal clusters. J Inorg Biochem 1998; 70: 187-194.
    • (1998) J Inorg Biochem , vol.70 , pp. 187-194
    • Li, H.1    Otvos, J.D.2
  • 39
    • 0030052798 scopus 로고    scopus 로고
    • Activation of the complete mouse metallothionein gene locus in the maternal deciduum
    • Liang L, Fu K, Lee DK, et al. Activation of the complete mouse metallothionein gene locus in the maternal deciduum. Mol Reprod Dev 1996; 43: 25-37.
    • (1996) Mol Reprod Dev , vol.43 , pp. 25-37
    • Liang, L.1    Fu, K.2    Lee, D.K.3
  • 40
    • 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. JNutr 2000; 130: 1455S-1458S.
    • (2000) JNutr , vol.130 , pp. 1455S-1458S
    • Maret, W.1
  • 41
    • 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 USA 1998; 95: 3478-3482.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 42
    • 33947463103 scopus 로고
    • A cadmium protein from equine kidney cortex
    • Margoshes M, Vallee BL. A cadmium protein from equine kidney cortex. JAm Chem Soc 1957; 79: 4813-4814.
    • (1957) JAm Chem Soc , vol.79 , pp. 4813-4814
    • Margoshes, M.1    Vallee, B.L.2
  • 43
    • 0040853145 scopus 로고
    • Factors affecting stabilities of chelate, macrocyclic and macrobicyclic complexes in solution
    • Martell AE, Hancock RD, Motekaitis RJ. Factors affecting stabilities of chelate, macrocyclic and macrobicyclic complexes in solution. Coord Chem Rev 1994; 133: 39-65.
    • (1994) Coord Chem Rev , vol.133 , pp. 39-65
    • Martell, A.E.1    Hancock, R.D.2    Motekaitis, R.J.3
  • 44
    • 0027994282 scopus 로고
    • Metallothionein III is expressed in neurons that sequester zinc in synaptic vesicles
    • Masters BA, Quaife J, Erickson JC, et al. Metallothionein III is expressed in neurons that sequester zinc in synaptic vesicles. J Neuro sci 1994; 14: 5844-5857.
    • (1994) J Neuro sci , vol.14 , pp. 5844-5857
    • Masters, B.A.1    Quaife, J.2    Erickson, J.C.3
  • 46
    • 33744959629 scopus 로고    scopus 로고
    • Organization and assembly of metal-thiolate clusters in epithelium-specific metallothionein-4
    • Meloni G, Zovo K, Kazantseva J, et al. Organization and assembly of metal-thiolate clusters in epithelium-specific metallothionein-4. J Biol Chem 2006; 281: 14588-14595.
    • (2006) J Biol Chem , vol.281 , pp. 14588-14595
    • Meloni, G.1    Zovo, K.2    Kazantseva, J.3
  • 47
    • 28844456522 scopus 로고    scopus 로고
    • Gold nanocluster formation using metallothionein: Mass spectrometry and electron microscopy
    • Mercogliano CP, DeRosier DJ. Gold nanocluster formation using metallothionein: Mass spectrometry and electron microscopy. J Mol Biol 2006; 355: 211-223.
    • (2006) J Mol Biol , vol.355 , pp. 211-223
    • Mercogliano, C.P.1    DeRosier, D.J.2
  • 48
    • 0025163762 scopus 로고
    • Amide proton exchange in human metallothionein-2 measured by nuclear magnetic resonance spectroscopy
    • Messerle BA, Bos M, Schaffer A, et al. Amide proton exchange in human metallothionein-2 measured by nuclear magnetic resonance spectroscopy. J Mol Biol 1990a; 214: 781-786.
    • (1990) J Mol Biol , vol.214 , pp. 781-786
    • Messerle, B.A.1    Bos, M.2    Schaffer, A.3
  • 49
    • 0025180337 scopus 로고
    • 113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy
    • 113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy. J Mol Biol 1990b; 214:765-779.
    • (1990) J Mol Biol , vol.214 , pp. 765-779
    • Messerle, B.A.1    Schaffer, A.2    Vašák, M.3
  • 50
    • 0034053364 scopus 로고    scopus 로고
    • Induction, regulation, degradation, and biological significance of mammalian metallothioneins
    • Miles AT, Hawksworth GM, Beattie JH, Rodilla V. Induction, regulation, degradation, and biological significance of mammalian metallothioneins. Crit Rev Biochem Mol Biol 2000; 35: 35-70.
    • (2000) Crit Rev Biochem Mol Biol , vol.35 , pp. 35-70
    • Miles, A.T.1    Hawksworth, G.M.2    Beattie, J.H.3    Rodilla, V.4
  • 51
    • 0001024754 scopus 로고    scopus 로고
    • '- dithio-bis(2-nitrobenzoate) (DTNB) and aurothiomalate (AuSTm)
    • '- dithio-bis(2-nitrobenzoate) (DTNB) and aurothiomalate (AuSTm). Inorg Chem 1999; 38: 5655-5659.
    • (1999) Inorg Chem , vol.38 , pp. 5655-5659
    • Muñoz, A.1    Petering, D.H.2    Shaw, C.F.3
  • 52
    • 0023258490 scopus 로고
    • Immunohistochemical localization of metallothionein in cell nucleus and cytoplasm of fetal human liver and kidney and its changes during development
    • Nartey NO, Banerjee D, Cherian MG. Immunohistochemical localization of metallothionein in cell nucleus and cytoplasm of fetal human liver and kidney and its changes during development. Pathology 1987; 19: 233-238.
    • (1987) Pathology , vol.19 , pp. 233-238
    • Nartey, N.O.1    Banerjee, D.2    Cherian, M.G.3
  • 53
    • 34249912942 scopus 로고    scopus 로고
    • Structural prediction of the beta-domain of metallothionein-3 by molecular dynamics simulation
    • Ni FY, Cai B, Ding ZC, et al. Structural prediction of the beta-domain of metallothionein-3 by molecular dynamics simulation. Proteins 2007; 68: 255-266.
    • (2007) Proteins , vol.68 , pp. 255-266
    • Ni, F.Y.1    Cai, B.2    Ding, Z.C.3
  • 54
    • 0021829810 scopus 로고
    • Distinct metal-binding configurations in metallothionein
    • Nielson KB, Atkin CL, Winge DR. Distinct metal-binding configurations in metallothionein. J Biol Chem 1985; 260: 5342-5350.
    • (1985) J Biol Chem , vol.260 , pp. 5342-5350
    • Nielson, K.B.1    Atkin, C.L.2    Winge, D.R.3
  • 55
    • 0021046411 scopus 로고
    • Order of metal binding in metallothionein
    • Nielson KB, Winge DR. Order of metal binding in metallothionein. J Biol Chem 1983; 258: 13063-13069.
    • (1983) J Biol Chem , vol.258 , pp. 13063-13069
    • Nielson, K.B.1    Winge, D.R.2
  • 56
    • 0021356888 scopus 로고
    • Preferential binding of copper to the beta domain of metallothionein
    • Nielson KB, Winge DR. Preferential binding of copper to the beta domain of metallothionein. JBiol Chem 1984; 259: 4941-4946.
    • (1984) JBiol Chem , vol.259 , pp. 4941-4946
    • Nielson, K.B.1    Winge, D.R.2
  • 57
    • 0000119940 scopus 로고
    • Structure of the metal clusters in rabbit liver metallothionein
    • Otvos JD, Armitage IM. Structure of the metal clusters in rabbit liver metallothionein. Proc Natl Acad Sci USA 1980; 77: 7094-7098.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7094-7098
    • Otvos, J.D.1    Armitage, I.M.2
  • 58
    • 0004205702 scopus 로고
    • Dynamic aspects of metallothionein structure
    • Suzuki KT, Imura N, Kimura M (eds.), Birkhäuser Verlag, Basel
    • Otvos JD, Liu X, Li H, et al. Dynamic aspects of metallothionein structure. In: Suzuki KT, Imura N, Kimura M (eds.), Metallothionein III, Birkhäuser Verlag, Basel, 1993, pp. 57-74.
    • (1993) Metallothionein III , pp. 57-74
    • Otvos, J.D.1    Liu, X.2    Li, H.3
  • 59
    • 0035949634 scopus 로고    scopus 로고
    • Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: Metallothionein-3
    • Öz G, Zangger K, Armitage IM. Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: Metallothionein-3. Biochemistry 2001; 40: 11433-11441.
    • (2001) Biochemistry , vol.40 , pp. 11433-11441
    • Öz, G.1    Zangger, K.2    Armitage, I.M.3
  • 60
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter RD. The elusive function of metallothioneins. Proc Natl Acad Sci USA 1998; 95: 8428-8430.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 61
    • 0037076545 scopus 로고    scopus 로고
    • Brain-specific metallothionein-3 has higher metalbinding capacity than ubiquitous metallothioneins and binds metals noncooperatively
    • Palumaa P, Eriste E, Njunkova O, et al. Brain-specific metallothionein-3 has higher metalbinding capacity than ubiquitous metallothioneins and binds metals noncooperatively. Biochemistry 2002; 41: 6158-6163.
    • (2002) Biochemistry , vol.41 , pp. 6158-6163
    • Palumaa, P.1    Eriste, E.2    Njunkova, O.3
  • 64
    • 0026784356 scopus 로고
    • Spectroscopic studies on metal distribution in Co(II)/Zn(II) mixed-metal clusters in rabbit liver metallothionein 2
    • Pountney DL, Vašák M. Spectroscopic studies on metal distribution in Co(II)/Zn(II) mixed-metal clusters in rabbit liver metallothionein 2. Eur J Biochem 1992; 209: 335-341.
    • (1992) Eur J Biochem , vol.209 , pp. 335-341
    • Pountney, D.L.1    Vašák, M.2
  • 65
    • 0028289610 scopus 로고
    • Induction of a new metallothionein isoform (MT-IV) occurs during differentiation of stratified squamous epithelia
    • Quaife CJ, Findley SD, Erickson JC, et al. Induction of a new metallothionein isoform (MT-IV) occurs during differentiation of stratified squamous epithelia. Biochemistry 1994; 33: 7250-7259.
    • (1994) Biochemistry , vol.33 , pp. 7250-7259
    • Quaife, C.J.1    Findley, S.D.2    Erickson, J.C.3
  • 66
    • 0026047966 scopus 로고
    • Refined crystal structure of Cd, Zn metallothionein at 2.0 Â resolution
    • Robbins AH, McRee DE, Williamson M, et al. Refined crystal structure of Cd, Zn metallothionein at 2.0 Â resolution. J Mol Biol 1991; 221: 1269-1293.
    • (1991) J Mol Biol , vol.221 , pp. 1269-1293
    • Robbins, A.H.1    McRee, D.E.2    Williamson, M.3
  • 67
    • 0032504163 scopus 로고    scopus 로고
    • Modulation of DNA binding of a Tramtrack zinc finger peptide by the metallothionein-thionein conjugate pair
    • Roesijadi G, Bogumil R, Vašák M. Kägi JH. Modulation of DNA binding of a Tramtrack zinc finger peptide by the metallothionein-thionein conjugate pair. J Biol Chem 1998; 273: 17425-17432.
    • (1998) J Biol Chem , vol.273 , pp. 17425-17432
    • Roesijadi, G.1    Bogumil, R.2    Vašák, M.3    Kägi, J.H.4
  • 68
    • 0036189730 scopus 로고    scopus 로고
    • Advances in the structure and chemistry of metallothioneins
    • Romero-Isart N, Vašák M. Advances in the structure and chemistry of metallothioneins. J Inorg Biochem 2002; 88: 388-396.
    • (2002) J Inorg Biochem , vol.88 , pp. 388-396
    • Romero-Isart, N.1    Vašák, M.2
  • 69
    • 0036941677 scopus 로고    scopus 로고
    • A distinct Cu4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain
    • Roschitzki B, Vašák M. A distinct Cu4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain. J Biol Inorg Chem 2002; 7: 611-616.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 611-616
    • Roschitzki, B.1    Vašák, M.2
  • 70
    • 0041525416 scopus 로고    scopus 로고
    • Redox labile site in a Zn4 cluster of Cu4, Zn4-metallothionein-3
    • Roschitzki B, Vašák M. Redox labile site in a Zn4 cluster of Cu4, Zn4-metallothionein-3. Biochemistry 2003; 42: 9822-9828.
    • (2003) Biochemistry , vol.42 , pp. 9822-9828
    • Roschitzki, B.1    Vašák, M.2
  • 71
    • 0035202113 scopus 로고    scopus 로고
    • Expression domains in the skin of genes affected by the nude mutation and identified by gene expression profiling
    • Schlake T, Boehm T. Expression domains in the skin of genes affected by the nude mutation and identified by gene expression profiling. Mech Dev 2001; 109: 419-422.
    • (2001) Mech Dev , vol.109 , pp. 419-422
    • Schlake, T.1    Boehm, T.2
  • 72
    • 0023821870 scopus 로고
    • Conformation of Cd7-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy
    • Schultze P, Wörgötter E, Braun W, et al. Conformation of Cd7-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy. J Mol Biol 1988; 203: 251-268.
    • (1988) J Mol Biol , vol.203 , pp. 251-268
    • Schultze, P.1    Wörgötter, E.2    Braun, W.3
  • 73
    • 0026346245 scopus 로고
    • Ligand substitution and sulfhydryl reactivity of metallothionein
    • Shaw III CF, Savas MM, Petering DH. Ligand substitution and sulfhydryl reactivity of metallothionein. Methods Enzymol 1991; 205: 401-414.
    • (1991) Methods Enzymol , vol.205 , pp. 401-414
    • Shaw III, C.F.1    Savas, M.M.2    Petering, D.H.3
  • 74
    • 0035260711 scopus 로고    scopus 로고
    • Localization, regulation, and function of metallothionein-III/growth inhibitory factor in the brain
    • Sogawa CA, Asanuma M, Sogawa N, et al. Localization, regulation, and function of metallothionein-III/growth inhibitory factor in the brain. Acta Med Okayama 2001; 55: 1-9.
    • (2001) Acta Med Okayama , vol.55 , pp. 1-9
    • Sogawa, C.A.1    Asanuma, M.2    Sogawa, N.3
  • 75
    • 0343148504 scopus 로고
    • Metallothioneins
    • Stillman MJ. Metallothioneins. Coord Chem Rev 1995; 144: 461-511.
    • (1995) Coord Chem Rev , vol.144 , pp. 461-511
    • Stillman, M.J.1
  • 76
    • 0344688221 scopus 로고    scopus 로고
    • Trace elements in human physiology and pathology, Copper
    • Tapiero H, Townsend DM, Tew KD. Trace elements in human physiology and pathology, Copper. Biomed Pharmacother 2003; 57: 386-398.
    • (2003) Biomed Pharmacother , vol.57 , pp. 386-398
    • Tapiero, H.1    Townsend, D.M.2    Tew, K.D.3
  • 78
    • 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, Vašák 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    Vašák, M.2
  • 79
    • 2642579155 scopus 로고    scopus 로고
    • Functional differentiation in the mammalian metallothionein gene family: Metal binding features of mouse MT4 and comparison with its paralog MT1
    • Tio L, Villarreal L, Atrian S, Capdevila M. Functional differentiation in the mammalian metallothionein gene family: Metal binding features of mouse MT4 and comparison with its paralog MT1. J Biol Chem 2004; 279: 24403-24413.
    • (2004) J Biol Chem , vol.279 , pp. 24403-24413
    • Tio, L.1    Villarreal, L.2    Atrian, S.3    Capdevila, M.4
  • 80
    • 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, et al. The growth inhibitory factor that is deficient in the Alzheimer’s disease brain is a 68 amino acid metallothionein-like protein. Neuron 1991; 7: 337-347.
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3
  • 81
    • 0000699884 scopus 로고
    • Spectroscopic studies on cobalt(II) metallothionein: Evidence for pseudotetrahedral coordination
    • Vašák M. Spectroscopic studies on cobalt(II) metallothionein: Evidence for pseudotetrahedral coordination. J Am Chem Soc 1980; 102: 3953-3955.
    • (1980) J Am Chem Soc , vol.102 , pp. 3953-3955
    • Vašák, M.1
  • 82
    • 0037627500 scopus 로고
    • Metal thiolate clusters in cobalt(II)-metallothionein
    • Vašák M. Kagi JH. Metal thiolate clusters in cobalt(II)-metallothionein. Proc Natl Acad Sci USA 1981; 78: 6709-6713.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6709-6713
    • Vašák, M.1    Kagi, J.H.2
  • 83
    • 33744963136 scopus 로고    scopus 로고
    • Metallothioneins
    • King RB (ed.), 2nd ed., John Wiley & Sons, New York
    • Vašák M. Romero-Isart N. Metallothioneins. In: King RB (ed.), Encyclopedia of Inorganic Chemistry, 2nd ed., John Wiley & Sons, New York, 2005, pp. 3208-3221.
    • (2005) Encyclopedia of Inorganic Chemistry , pp. 3208-3221
    • Vašák, M.1    Romero-Isart, N.2
  • 84
    • 31444449685 scopus 로고    scopus 로고
    • Solution structure and dynamics of human metallothionein-3 (MT-3)
    • Wang H, Zhang Q, Cai B, et al. Solution structure and dynamics of human metallothionein-3 (MT-3). FEBS Lett 2006; 580: 795-800.
    • (2006) FEBS Lett , vol.580 , pp. 795-800
    • Wang, H.1    Zhang, Q.2    Cai, B.3
  • 85
    • 0020478923 scopus 로고
    • Domain nature of metallothionein
    • Winge DR, Miklossy KA. Domain nature of metallothionein. J Biol Chem 1982; 257: 3471-3476.
    • (1982) J Biol Chem , vol.257 , pp. 3471-3476
    • Winge, D.R.1    Miklossy, K.A.2
  • 86
    • 0028958526 scopus 로고
    • Covalent sequestration of melphalan by metallothionein and selective alkylation of cysteines
    • Yu X, Wu Z, Fenselau C. Covalent sequestration of melphalan by metallothionein and selective alkylation of cysteines. Biochemistry 1995; 34: 3377-3385.
    • (1995) Biochemistry , vol.34 , pp. 3377-3385
    • Yu, X.1    Wu, Z.2    Fenselau, C.3
  • 87
    • 0029865427 scopus 로고    scopus 로고
    • A binding site for chlorambucil on metallothionein
    • Zaia J, Jiang LC, Han MS, et al. A binding site for chlorambucil on metallothionein. Biochemistry 1996; 35: 2830-2835.
    • (1996) Biochemistry , vol.35 , pp. 2830-2835
    • Zaia, J.1    Jiang, L.C.2    Han, M.S.3
  • 88
    • 0035344459 scopus 로고    scopus 로고
    • Nitric oxide selectively releases metals from the aminoterminal domain of metallothioneins: Potential role at inflammatory sites
    • Zangger K, Öz G, Haslinger E, et al. Nitric oxide selectively releases metals from the aminoterminal domain of metallothioneins: Potential role at inflammatory sites. FASEB J 2001; 15: 1303-1305.
    • (2001) FASEB J , vol.15 , pp. 1303-1305
    • Zangger, K.1    Öz, G.2    Haslinger, E.3
  • 89
    • 0342614962 scopus 로고    scopus 로고
    • Three-dimensional solution structure of mouse Cd7-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy
    • Zangger K, Öz G, Otvos JD, Armitage IM. Three-dimensional solution structure of mouse Cd7-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy. Protein Sci 1999; 8: 2630-2638.
    • (1999) Protein Sci , vol.8 , pp. 2630-2638
    • Zangger, K.1    Öz, G.2    Otvos, J.D.3    Armitage, I.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.