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Volumn 43, Issue 12, 2004, Pages 3301-3309

Zinc and Sulfur: A Critical Biological Partnership

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; LIGAND; MAGNESIUM; METALLOTHIONEIN; RUBREDOXIN; SULFUR; UNCLASSIFIED DRUG; ZINC; ZINC FINGER PROTEIN; ZINC THIOLATE;

EID: 1642389890     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036340p     Document Type: Review
Times cited : (243)

References (122)
  • 1
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B. L., and Auld, D. S. (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins, Biochemistry 29, 5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 2
    • 0000282461 scopus 로고
    • Zinc: Biological Functions and Coordination Motifs
    • Vallee, B. L., and Auld, D. S. (1993) Zinc: Biological Functions and Coordination Motifs, Acc. Chem. Res. 26, 543-551.
    • (1993) Acc. Chem. Res. , vol.26 , pp. 543-551
    • Vallee, B.L.1    Auld, D.S.2
  • 3
    • 0021100320 scopus 로고
    • Xenopus transcription factor A requires zinc for binding to the 5S gene
    • Hanas, J. S., Hazuda, D., Bogenhagen, D. F., Wu, F. Y.-H., and Wu, C. W. (1983) Xenopus transcription factor A requires zinc for binding to the 5S gene, J. Biol. Chem. 258, 14120-14125.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14120-14125
    • Hanas, J.S.1    Hazuda, D.2    Bogenhagen, D.F.3    Wu, F.Y.-H.4    Wu, C.W.5
  • 4
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller, J., McLachlan, A. D., and Klug, A. (1985) Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes, EMBO J. 4, 1609-1614.
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 5
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • International Human Genome Sequencing Consortium (2001) Initial sequencing and analysis of the human genome, Nature 409, 860-921.
    • (2001) Nature , vol.409 , pp. 860-921
  • 6
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg, J. M., and Shi, Y. (1996) The galvanization of biology: A growing appreciation for the roles of zinc, Science 271, 1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 7
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity, J. H., Lee, B. M., and Wright, P. E. (2001) Zinc finger proteins: New insights into structural and functional diversity, Curr. Opin. Struct. Biol. 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
  • 8
    • 0030049613 scopus 로고    scopus 로고
    • Cytidine deaminase complexed to 3-deazacytidine: A "valence buffer" in zinc enzyme catalysis
    • Xiang, S., Short, S. A., Wolfenden, R., and Carter, C. W., Jr. (1996) Cytidine deaminase complexed to 3-deazacytidine: A "valence buffer" in zinc enzyme catalysis, Biochemistry 35, 1335-1341.
    • (1996) Biochemistry , vol.35 , pp. 1335-1341
    • Xiang, S.1    Short, S.A.2    Wolfenden, R.3    Carter Jr., C.W.4
  • 9
    • 0031244360 scopus 로고    scopus 로고
    • Enzyme-catalyzed methyl transfers to thiols: The role of zinc
    • Matthews, R. G., and Goulding, C. W. (1997) Enzyme-catalyzed methyl transfers to thiols: the role of zinc, Curr. Opin. Chem. Biol. 1, 332-339.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 332-339
    • Matthews, R.G.1    Goulding, C.W.2
  • 10
    • 0032587329 scopus 로고    scopus 로고
    • Zinc-catalyzed sulfur alkylation: Insights from protein farnesyltransferase
    • Hightower, K. E., and Fierke, C. A. (1999) Zinc-catalyzed sulfur alkylation: insights from protein farnesyltransferase, Curr. Opin. Chem. Biol. 3, 176-181.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 176-181
    • Hightower, K.E.1    Fierke, C.A.2
  • 11
    • 0027752816 scopus 로고
    • Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada
    • Myers, L. C., Verdine, G. L., and Wagner, G. (1993) Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada, Biochemistry 32, 14089-14094.
    • (1993) Biochemistry , vol.32 , pp. 14089-14094
    • Myers, L.C.1    Verdine, G.L.2    Wagner, G.3
  • 12
    • 0001657218 scopus 로고
    • Modeling the DNA methylphosphotriester repair site in Escherichia coli Ada. Why zinc and four cysteines?
    • Wilker, J. J., and Lippard, S. J. (1995) Modeling the DNA methylphosphotriester repair site in Escherichia coli Ada. Why zinc and four cysteines? J. Am. Chem. Soc. 117, 8682-8683.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8682-8683
    • Wilker, J.J.1    Lippard, S.J.2
  • 13
    • 0037389593 scopus 로고    scopus 로고
    • Synthetic modeling of zinc thiolates: Quantitative assessment of hydrogen bonding in modulating sulfur alkylation rates
    • Chiou, S.-J., Riordan, C. G., and Rheingold, A. L. (2003) Synthetic modeling of zinc thiolates: Quantitative assessment of hydrogen bonding in modulating sulfur alkylation rates, Proc. Natl. Acad. Sci. U.S.A. 100, 3695-3700.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3695-3700
    • Chiou, S.-J.1    Riordan, C.G.2    Rheingold, A.L.3
  • 14
    • 0037471640 scopus 로고    scopus 로고
    • Control of thiolate nucleophilicity and specificity in zinc metalloproteins by hydrogen bonding: Lessons from model compound studies
    • Smith, J. N., Shirin, Z., and Carrano, C. J. (2003) Control of thiolate nucleophilicity and specificity in zinc metalloproteins by hydrogen bonding: Lessons from model compound studies, J. Am. Chem. Soc. 125, 868-869.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 868-869
    • Smith, J.N.1    Shirin, Z.2    Carrano, C.J.3
  • 15
    • 0029787099 scopus 로고    scopus 로고
    • Zinc- and iron-rubredoxins from Clostridium pasteurianum at atomic resolution: A high-precision model of a ZnCys4 coordination unit in a protein
    • Dauter, Z., Wilson, K., Sieker, L., Moulis, J., and Meyer, J. (1996) Zinc- and iron-rubredoxins from Clostridium pasteurianum at atomic resolution: A high-precision model of a ZnCys4 coordination unit in a protein, Proc. Natl. Acad. Sci. U.S.A. 93, 8836-8840.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8836-8840
    • Dauter, Z.1    Wilson, K.2    Sieker, L.3    Moulis, J.4    Meyer, J.5
  • 16
    • 0037067059 scopus 로고    scopus 로고
    • Factors governing the protonation state of cysteines in proteins: An ab initio/CDM study
    • Dudev, T., and Lim, C. (2002) Factors governing the protonation state of cysteines in proteins: An ab initio/CDM study, J. Am. Chem. Soc. 124, 6759-6766.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6759-6766
    • Dudev, T.1    Lim, C.2
  • 17
    • 84962352816 scopus 로고    scopus 로고
    • 2+ Interactions: Thiol vs Thiolate Coordination
    • 2+ Interactions: Thiol vs. Thiolate Coordination, Proteins 49, 37-48.
    • (2002) Proteins , vol.49 , pp. 37-48
    • Simonson, T.1    Calimet, N.2
  • 18
    • 0030457336 scopus 로고    scopus 로고
    • Retention of thiol protons in two classes of protein zinc ion coordination centers
    • Fabris, D., Zaia, J., Hathout, Y., and Fenselau, C. (1996) Retention of thiol protons in two classes of protein zinc ion coordination centers, J. Am. Chem. Soc. 118, 12242-12243.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12242-12243
    • Fabris, D.1    Zaia, J.2    Hathout, Y.3    Fenselau, C.4
  • 19
    • 0035857417 scopus 로고    scopus 로고
    • Reactivity of Zinc Finger Cores: Analysis of Protein Packing and Electrostatic Screening
    • Maynard, A. T., and Covell, D. G. (2001) Reactivity of Zinc Finger Cores: Analysis of Protein Packing and Electrostatic Screening, J. Am. Chem. Soc. 123, 1047-1058.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1047-1058
    • Maynard, A.T.1    Covell, D.G.2
  • 20
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothionein confer redox activity on zinc clusters
    • Maret, W., and Vallee, B. L. (1998) Thiolate ligands in metallothionein confer redox activity on zinc clusters, Proc. Natl. Acad. Sci. U.S.A. 95, 3478-3482.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 21
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jacob, U., Muse, W., Eser, M., and Bardwell, J. C. A. (1999) Chaperone activity with a redox switch, Cell 96, 341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jacob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.A.4
  • 22
    • 0036810021 scopus 로고    scopus 로고
    • Redox-regulated molecular chaperones
    • Graf, P. C. F., and Jacob, U. (2002) Redox-regulated molecular chaperones, Cell. Mol. Life Sci. 59, 1624-1631.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1624-1631
    • Graf, P.C.F.1    Jacob, U.2
  • 23
    • 0141645618 scopus 로고    scopus 로고
    • The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor
    • Li, W., Bottrill, A. R., Bibb, M. J., Buttner, M. J., Paget, M. S. B., and Kleanthous, C. (2003) The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor, J. Mol. Biol. 333, 461-472.
    • (2003) J. Mol. Biol. , vol.333 , pp. 461-472
    • Li, W.1    Bottrill, A.R.2    Bibb, M.J.3    Buttner, M.J.4    Paget, M.S.B.5    Kleanthous, C.6
  • 24
    • 0032870929 scopus 로고    scopus 로고
    • Zinc finger of RPA, a non-DNA binding element, regulates its DNA binding activity through redox
    • Park, J.-S., Wang, M., Park, S.-J., and Lee, S.-H. (1999) Zinc finger of RPA, a non-DNA binding element, regulates its DNA binding activity through redox, J. Biol. Chem. 274, 29075-29080.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29075-29080
    • Park, J.-S.1    Wang, M.2    Park, S.-J.3    Lee, S.-H.4
  • 26
    • 0037143690 scopus 로고    scopus 로고
    • Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains
    • Kurek, I., Kawagoe, Y., Jacob-Wilk, D., Doblin, M., and Delmer, D. (2002) Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains, Proc. Natl. Acad. Sci. U.S.A. 99, 11109-11114.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11109-11114
    • Kurek, I.1    Kawagoe, Y.2    Jacob-Wilk, D.3    Doblin, M.4    Delmer, D.5
  • 27
    • 1642263925 scopus 로고    scopus 로고
    • Protein interface zinc sites: The role of zinc in the supramolecular assembly of proteins and in transient protein-protein interactions
    • (Messerschmidt, A., Ed.) Wiley, Chichester, U.K. (in press)
    • Maret, W. (2004) Protein interface zinc sites: the role of zinc in the supramolecular assembly of proteins and in transient protein-protein interactions, in Handbook of metalloproteins (Messerschmidt, A., Ed.) Wiley, Chichester, U.K. (in press).
    • (2004) Handbook of Metalloproteins
    • Maret, W.1
  • 28
    • 0036199685 scopus 로고    scopus 로고
    • Oxidation of the zinc-thiolate complex and uncoupling of endothelial nitric oxide synthase by peroxynitrite
    • Zou, M.-H., Shi, C., and Cohen, R. A. (2002) Oxidation of the zinc-thiolate complex and uncoupling of endothelial nitric oxide synthase by peroxynitrite, J. Clin. Invest. 109, 817-826.
    • (2002) J. Clin. Invest. , vol.109 , pp. 817-826
    • Zou, M.-H.1    Shi, C.2    Cohen, R.A.3
  • 29
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • Korichneva, I., Hoyos, B., Chua, R., Levi, E., and Hammerling, U. (2002) Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen, J. Biol. Chem. 277, 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
  • 30
    • 0034866622 scopus 로고    scopus 로고
    • Redox control of zinc finger proteins: Mechanisms and role in gene regulation
    • Lee, S.-H., and Maret, W. (2001) Redox control of zinc finger proteins: Mechanisms and role in gene regulation, Antioxid. Redox Signaling 3, 531-534.
    • (2001) Antioxid. Redox Signaling , vol.3 , pp. 531-534
    • Lee, S.-H.1    Maret, W.2
  • 31
    • 0020549413 scopus 로고
    • Latent and active human polymorphonuclear leukocyte collagenases
    • Macartney, H. W., and Tschesche, H. (1983) Latent and active human polymorphonuclear leukocyte collagenases, Eur. J. Biochem. 130, 71-78.
    • (1983) Eur. J. Biochem. , vol.130 , pp. 71-78
    • Macartney, H.W.1    Tschesche, H.2
  • 33
    • 9244222705 scopus 로고    scopus 로고
    • Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells
    • Tyagi, S. C., Kumar, S. G., and Borders, S. (1996) Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells, J. Cell. Biochem. 61, 139-151.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 139-151
    • Tyagi, S.C.1    Kumar, S.G.2    Borders, S.3
  • 35
    • 0033591844 scopus 로고    scopus 로고
    • Potential drugs against cervical cancer: Zinc-ejecting inhibitors of the human papillomavirus type 16 E6 oncoprotein
    • Beerheide, W., Bernard, H.-U., Tan, Y.-J., Ganeson, A., Rice, W. G., and Ting, A. E. (1999) Potential drugs against cervical cancer: Zinc-ejecting inhibitors of the human papillomavirus type 16 E6 oncoprotein, J. Nat. Cancer Inst. 91, 1211-1220.
    • (1999) J. Nat. Cancer Inst. , vol.91 , pp. 1211-1220
    • Beerheide, W.1    Bernard, H.-U.2    Tan, Y.-J.3    Ganeson, A.4    Rice, W.G.5    Ting, A.E.6
  • 37
    • 0030019808 scopus 로고    scopus 로고
    • The in vitro ejection of zinc from human immunodeficiency virus (HIV) type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity
    • Tummino, P. J., Scholten, J. D., Harvey, P. J., Holler, T. P., Maloney, L., Gogliotti, R., Domagala, J., and Hupe, D. (1996) The in vitro ejection of zinc from human immunodeficiency virus (HIV) type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity, Proc. Natl. Acad. Sci. U.S.A. 93, 969-973.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 969-973
    • Tummino, P.J.1    Scholten, J.D.2    Harvey, P.J.3    Holler, T.P.4    Maloney, L.5    Gogliotti, R.6    Domagala, J.7    Hupe, D.8
  • 38
    • 0037430396 scopus 로고    scopus 로고
    • Zinc-bound thiolate-disulfide exchange: A strategy for inhibiting metallo-β-lactamases
    • Boerzel, H., Koeckert, M., Bu, W. M., Spingler, B., and Lippard, S. J. (2003) Zinc-bound thiolate-disulfide exchange: A strategy for inhibiting metallo-β-lactamases, Inorg. Chem. 42, 1604-1615.
    • (2003) Inorg. Chem. , vol.42 , pp. 1604-1615
    • Boerzel, H.1    Koeckert, M.2    Bu, W.M.3    Spingler, B.4    Lippard, S.J.5
  • 39
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L., and Falchuk, K. H. (1993) The biochemical basis of zinc physiology, Physiol. Rev. 73, 79-118.
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 40
    • 0035693722 scopus 로고    scopus 로고
    • Eukaryotic zinc transporters and their regulation
    • Gaither, L. A., and Eide, D. J. (2001) Eukaryotic zinc transporters and their regulation, Biometals 14, 251-270.
    • (2001) Biometals , vol.14 , pp. 251-270
    • Gaither, L.A.1    Eide, D.J.2
  • 41
    • 0032509320 scopus 로고    scopus 로고
    • Zinc fingers in Caenorhabditis elegans: Finding families and probing pathways
    • Clarke, N. D., and Berg, J. M. (1998) Zinc fingers in Caenorhabditis elegans: Finding families and probing pathways, Science 282, 2018-2022.
    • (1998) Science , vol.282 , pp. 2018-2022
    • Clarke, N.D.1    Berg, J.M.2
  • 42
    • 0035696323 scopus 로고    scopus 로고
    • Bacterial zinc transporters and regulators
    • Hantke, K. (2001) Bacterial zinc transporters and regulators, Biometals 14, 239-249.
    • (2001) Biometals , vol.14 , pp. 239-249
    • Hantke, K.1
  • 44
    • 0001023773 scopus 로고
    • Metallocarboxypeptidases: Stability constants and enzymatic characteristics
    • Coleman, J. E., and Vallee, B. L. (1961) Metallocarboxypeptidases: Stability constants and enzymatic characteristics, J. Biol. Chem. 236, 2244-2249.
    • (1961) J. Biol. Chem. , vol.236 , pp. 2244-2249
    • Coleman, J.E.1    Vallee, B.L.2
  • 45
    • 0002106617 scopus 로고
    • Evolution, structure and chemical activity of class I metallothioneins: An overview
    • (Suzuki, K. T., Imura, N., and Kimura, M., Eds.), Birkhäuser, Basel, Switzerland
    • Kägi, J. H. R. (1993) Evolution, structure and chemical activity of class I metallothioneins: An overview, in Metallothionein III (Suzuki, K. T., Imura, N., and Kimura, M., Eds.) pp 29-55, Birkhäuser, Basel, Switzerland.
    • (1993) Metallothionein III , pp. 29-55
    • Kägi, J.H.R.1
  • 46
    • 33749034376 scopus 로고
    • Structure-reactivity relationships of metallothionein, a unique metal-binding protein
    • Otvos, J. D., Petering, D. H., and Shaw, C. F. (1989) Structure-reactivity relationships of metallothionein, a unique metal-binding protein, Comments Inorg. Chem. 1, 1-35.
    • (1989) Comments Inorg. Chem. , vol.1 , pp. 1-35
    • Otvos, J.D.1    Petering, D.H.2    Shaw, C.F.3
  • 48
    • 0022654324 scopus 로고
    • Metal binding to angiotensin converting enzyme: Implications for the metal binding site
    • Kleeman, S. G., Keung, W. M., and Riordan, J. F. (1986) Metal binding to angiotensin converting enzyme: Implications for the metal binding site, J. Inorg. Biochem. 26, 93-106.
    • (1986) J. Inorg. Biochem. , vol.26 , pp. 93-106
    • Kleeman, S.G.1    Keung, W.M.2    Riordan, J.F.3
  • 50
    • 1642363058 scopus 로고    scopus 로고
    • personal communication
    • Cha, J., and Auld, D. S. (2003) personal communication.
    • (2003)
    • Cha, J.1    Auld, D.S.2
  • 52
    • 0028948696 scopus 로고
    • Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc
    • Palmiter, R. D., and Findley, S. D. (1995) Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc, EMBO J. 14, 639-649.
    • (1995) EMBO J. , vol.14 , pp. 639-649
    • Palmiter, R.D.1    Findley, S.D.2
  • 53
    • 0015239110 scopus 로고
    • Metal complexes of phosphoglucomutase in vivo
    • Peck, E. J., Jr., and Ray, W. J., Jr. (1971) Metal complexes of phosphoglucomutase in vivo, J. Biol. Chem. 246, 1160-1167.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1160-1167
    • Peck Jr., E.J.1    Ray Jr., W.J.2
  • 54
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • Simons, T. J. B. (1991) Intracellular free zinc and zinc buffering in human red blood cells, J. Membr. Biol. 123, 63-71.
    • (1991) J. Membr. Biol. , vol.123 , pp. 63-71
    • Simons, T.J.B.1
  • 56
    • 0029028318 scopus 로고
    • 2+ in bovine milk and plasma
    • 2+ in bovine milk and plasma, J. Nutr. 125, 1904-1910.
    • (1995) J. Nutr. , vol.125 , pp. 1904-1910
    • Zhang, P.1    Allen, J.C.2
  • 57
    • 0028860021 scopus 로고
    • Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels
    • Atar, D., Backx, P. H., Appel, M. M., Gao, W. D., and Marban, E. (1995) Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels, J. Biol. Chem. 270, 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
  • 59
    • 0033514994 scopus 로고    scopus 로고
    • Inhibitory sites in enzymes: Zinc removal and reactivation by thionein
    • Maret, W., Jacob, C., Vallee, B. L., and Fischer, E. H. (1999) Inhibitory sites in enzymes: Zinc removal and reactivation by thionein, Proc. Natl. Acad. Sci. U.S.A. 96, 1936-1940.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1936-1940
    • Maret, W.1    Jacob, C.2    Vallee, B.L.3    Fischer, E.H.4
  • 60
    • 0037155880 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
    • Gazaryan, I. G., Krasnikov, B. F., Ashby, G. A., Thorneley, R. N. F., Kristal, B. S., and Brown, A. M. (2002) Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase, J. Biol. Chem. 277, 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.F.4    Kristal, B.S.5    Brown, A.M.6
  • 61
    • 0035969898 scopus 로고    scopus 로고
    • Enzyme regulation by reversible zinc inhibition: Glycerol phosphate dehydrogenase as an example
    • Maret, W., Yetman, C. A., and Jiang, L.-J. (2001) Enzyme regulation by reversible zinc inhibition: Glycerol phosphate dehydrogenase as an example, Chem.-Biol. Interact. 130-132, 891-901.
    • (2001) Chem.-Biol. Interact. , vol.130-132 , pp. 891-901
    • Maret, W.1    Yetman, C.A.2    Jiang, L.-J.3
  • 62
    • 0344010194 scopus 로고    scopus 로고
    • Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling
    • Haase, H., and Maret, W. (2003) Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling, Exp. Cell Res. 291, 289-298.
    • (2003) Exp. Cell Res. , vol.291 , pp. 289-298
    • Haase, H.1    Maret, W.2
  • 63
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten, C. E., and O'Halloran, T. V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis, Science 292, 2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 64
    • 33947463103 scopus 로고
    • A cadmium protein from equine kidney cortex
    • Margoshes, M., and Vallee, B. L. (1957) A cadmium protein from equine kidney cortex, J. Am. Chem. Soc. 79, 4813.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 4813
    • Margoshes, M.1    Vallee, B.L.2
  • 66
    • 0023937834 scopus 로고
    • Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
    • Arseniev, A., Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vašák, M., Kägi, J. H. R., and Wüthrich, K. (1988) Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance, J. Mol. Biol. 201, 637-657.
    • (1988) J. Mol. Biol. , vol.201 , pp. 637-657
    • Arseniev, A.1    Schultze, P.2    Wörgötter, E.3    Braun, W.4    Wagner, G.5    Vašák, M.6    Kägi, J.H.R.7    Wüthrich, K.8
  • 68
    • 0030959658 scopus 로고    scopus 로고
    • Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster
    • Bellon, S. F., Rodgers, K. K., Schatz, D. G., Coleman, J. E., and Steitz, T. A. (1997) Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster, Nat. Struct. Biol. 4, 586-591.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5
  • 69
    • 0025342571 scopus 로고
    • The DNA binding domain of GAL4 forms a binuclear metal ion complex
    • Pan, T., and Coleman, J. E. (1990) The DNA binding domain of GAL4 forms a binuclear metal ion complex, Biochemistry 29, 3023-3029.
    • (1990) Biochemistry , vol.29 , pp. 3023-3029
    • Pan, T.1    Coleman, J.E.2
  • 70
    • 0037020217 scopus 로고    scopus 로고
    • Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase
    • Zhang, X., Tamaru, H., Khan, S. I., Horton, J. R., Keefe, L. J., Selker, E. U., and Chen, X. (2002) Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase, Cell 111, 117-127.
    • (2002) Cell , vol.111 , pp. 117-127
    • Zhang, X.1    Tamaru, H.2    Khan, S.I.3    Horton, J.R.4    Keefe, L.J.5    Selker, E.U.6    Chen, X.7
  • 71
    • 1342303474 scopus 로고    scopus 로고
    • Exploring the zinc proteome
    • Maret, W. (2004) Exploring the zinc proteome, J. Anal. At. Spectrom. 19, 15-19.
    • (2004) J. Anal. At. Spectrom. , vol.19 , pp. 15-19
    • Maret, W.1
  • 73
    • 0000191704 scopus 로고
    • Metal binding and catalytic activity in bovine carbonic anhydrase
    • Lindskog, S., and Malmström, B. G. (1962) Metal binding and catalytic activity in bovine carbonic anhydrase, J. Biol. Chem. 237, 1129-1137.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1129-1137
    • Lindskog, S.1    Malmström, B.G.2
  • 74
    • 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, K. S., and Vallee, B. L. (1997) 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. 94, 2233-2237.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2233-2237
    • Maret, W.1    Larsen, K.S.2    Vallee, B.L.3
  • 75
    • 0004205702 scopus 로고
    • Dynamic aspects of metallothionein structure
    • (Suzuki, K. T., Imura, N., and Kimura, M., Eds.), Birkhäuser, Basel, Switzerland
    • Otvos, J. D., Liu, X., Li, H., Shen, G., and Basti, M. (1993) Dynamic aspects of metallothionein structure, in Metallothionein III (Suzuki, K. T., Imura, N., and Kimura, M., Eds.) pp 57-74, Birkhäuser, Basel, Switzerland.
    • (1993) Metallothionein III , pp. 57-74
    • Otvos, J.D.1    Liu, X.2    Li, H.3    Shen, G.4    Basti, M.5
  • 76
    • 0028082427 scopus 로고
    • Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange
    • Maret, W. (1994) Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange, Proc. Natl. Acad. Sci. U.S.A. 91, 237-241.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 237-241
    • Maret, W.1
  • 77
    • 0029063792 scopus 로고
    • Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc
    • Maret, W. (1995) Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc, Neurochem. Int. 27, 111-117.
    • (1995) Neurochem. Int. , vol.27 , pp. 111-117
    • Maret, W.1
  • 78
    • 0033514932 scopus 로고    scopus 로고
    • Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes
    • Jacob, C., Maret, W., and Vallee, B. L. (1999) Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes, Proc. Natl. Acad. Sci. U.S.A. 96, 1910-1914.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1910-1914
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 79
    • 0034845444 scopus 로고    scopus 로고
    • Catalytic selenols couple the redox cycles of metallothionein and glutathione
    • Chen, Y., and Maret, W. (2001) Catalytic selenols couple the redox cycles of metallothionein and glutathione, Eur. J. Biochem. 268, 3346-3353.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3346-3353
    • Chen, Y.1    Maret, W.2
  • 81
    • 0033788519 scopus 로고    scopus 로고
    • Induction of neuronal apoptosis by thiol oxidation: Putative role of intracellular zinc release
    • Aizenman, E., Stout, A. K., Hartnett, K. A., Dineley, K. E., McLaughlin, B., and Reynolds, I. J. (2000) Induction of neuronal apoptosis by thiol oxidation: Putative role of intracellular zinc release, J. Neurochem. 75, 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
  • 86
    • 0037008050 scopus 로고    scopus 로고
    • S-nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation
    • Chen, Y., Irie, Y., Keung, W. M., and Maret, W. (2002) S-Nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation, Biochemistry 41, 8360-8367.
    • (2002) Biochemistry , vol.41 , pp. 8360-8367
    • Chen, Y.1    Irie, Y.2    Keung, W.M.3    Maret, W.4
  • 87
  • 90
    • 0035826695 scopus 로고    scopus 로고
    • Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein
    • Yang, Y., Maret, W., and Vallee, B. L. (2001) Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein, Proc. Natl. Acad. Sci. U.S.A. 98, 5556-5559.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5556-5559
    • Yang, Y.1    Maret, W.2    Vallee, B.L.3
  • 91
    • 0033995621 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry of zinc, cadmium, and copper metallothioneins: Evidence for metal-binding cooperativity
    • Gehrig, P. M., You, C., Dallinger, R., Gruber, C., Brouwer, M., Kägi, J. H. R., and Hunziker, P. E. (2000) Electrospray ionization mass spectrometry of zinc, cadmium, and copper metallothioneins: Evidence for metal-binding cooperativity, Protein Sci. 9, 395-402.
    • (2000) Protein Sci. , vol.9 , pp. 395-402
    • Gehrig, P.M.1    You, C.2    Dallinger, R.3    Gruber, C.4    Brouwer, M.5    Kägi, J.H.R.6    Hunziker, P.E.7
  • 92
    • 0032584078 scopus 로고    scopus 로고
    • The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase
    • Jiang, L.-J., Maret, W., and Vallee, B. L. (1998) The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase, Proc. Natl. Acad. Sci. U.S.A. 95, 3483-3488.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3483-3488
    • Jiang, L.-J.1    Maret, W.2    Vallee, B.L.3
  • 93
    • 0019013769 scopus 로고
    • Reactivation in vitro of zinc-requiring apoenzymes by rat liver zinc-thionein
    • Udom, A. O., and Brady, F. O. (1980) Reactivation in vitro of zinc-requiring apoenzymes by rat liver zinc-thionein, Biochem. J. 187, 329-335.
    • (1980) Biochem. J. , vol.187 , pp. 329-335
    • Udom, A.O.1    Brady, F.O.2
  • 94
    • 0019085620 scopus 로고
    • Ligand substitution reactions of metallothioneins with EDTA and apo-carbonic anhydrase
    • Li, T. Y., Kraker, A. J., Shaw, C. F., III, and Petering, D. H. (1980) Ligand substitution reactions of metallothioneins with EDTA and apo-carbonic anhydrase, Proc. Natl. Acad. Sci. U.S.A. 77, 6334-6338.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 6334-6338
    • Li, T.Y.1    Kraker, A.J.2    Shaw III, C.F.3    Petering, D.H.4
  • 97
    • 0035814762 scopus 로고    scopus 로고
    • Stoichiometry in zinc ion transfer from metallothionein to zinc finger peptides
    • Hathout, Y., Fabris, D., and Fenselau, C. (2001) Stoichiometry in zinc ion transfer from metallothionein to zinc finger peptides, Int. J. Mass Spectrom. 204, 1-6.
    • (2001) Int. J. Mass Spectrom. , vol.204 , pp. 1-6
    • Hathout, Y.1    Fabris, D.2    Fenselau, C.3
  • 98
    • 0034646226 scopus 로고    scopus 로고
    • Zinc transfer potentials of the α- and β-clusters of metallothionein are affected by domain interactions in the whole molecule
    • Jiang, L.-J., Vašák, M., Vallee, B. L., and Maret, W. (2000) Zinc transfer potentials of the α- and β-clusters of metallothionein are affected by domain interactions in the whole molecule, Proc. Natl. Acad. Sci. U.S.A. 97, 2503-2508.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2503-2508
    • Jiang, L.-J.1    Vašák, M.2    Vallee, B.L.3    Maret, W.4
  • 100
    • 0027204255 scopus 로고
    • A putative glutathione-binding site in Cd,Zn-metallothionein identified by equilibrium binding and molecular modeling studies
    • Brouwer, M., Brouwer, T. H., and Cashon, R. E. (1993) A putative glutathione-binding site in Cd,Zn-metallothionein identified by equilibrium binding and molecular modeling studies, Biochem. J. 294, 219-225.
    • (1993) Biochem. J. , vol.294 , pp. 219-225
    • Brouwer, M.1    Brouwer, T.H.2    Cashon, R.E.3
  • 101
    • 0036312378 scopus 로고    scopus 로고
    • Qualitative characterization of biomolecular zinc complexes by collisionally induced dissociation
    • Alfonso, C., Hathout, Y., and Fenselau, C. (2002) Qualitative characterization of biomolecular zinc complexes by collisionally induced dissociation, J. Mass Spectrom. 37, 755-759.
    • (2002) J. Mass Spectrom. , vol.37 , pp. 755-759
    • Alfonso, C.1    Hathout, Y.2    Fenselau, C.3
  • 102
    • 0025719287 scopus 로고
    • Zinc transfer from transcription factor IIIA fingers to thionein clusters
    • Zeng, J., Vallee, B. L., and Kägi, J. H. R. (1991) Zinc transfer from transcription factor IIIA fingers to thionein clusters, Proc. Natl. Acad. Sci. U.S.A. 88, 9984-9988.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9984-9988
    • Zeng, J.1    Vallee, B.L.2    Kägi, J.H.R.3
  • 103
    • 0025976912 scopus 로고
    • Thionein (apometallothionein) can modulate DNA binding and transcription activation by zinc finger containing factor Sp1
    • Zeng, J., Heuchel, R., Schaffner, W., and Kägi, J. H. R. (1991) Thionein (apometallothionein) can modulate DNA binding and transcription activation by zinc finger containing factor Sp1, FEBS Lett. 279, 310-312.
    • (1991) FEBS Lett. , vol.279 , pp. 310-312
    • Zeng, J.1    Heuchel, R.2    Schaffner, W.3    Kägi, J.H.R.4
  • 104
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob, C., Maret, W., and Vallee, B. L. (1998) Control of zinc transfer between thionein, metallothionein, and zinc proteins, Proc. Natl. Acad. Sci. U.S.A. 95, 3489-3494.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 105
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter, R. D. (1998) The elusive function of metallothioneins, Proc. Natl. Acad. Sci. U.S.A. 95, 8428-8430.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 106
    • 0035956862 scopus 로고    scopus 로고
    • Zinc metallothionein imported into liver mitochondria modulates respiration
    • Ye, B., Maret, W., and Vallee, B. L. (2001) Zinc metallothionein imported into liver mitochondria modulates respiration, Proc. Natl. Acad. Sci. U.S.A. 98, 2317-2322.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2317-2322
    • Ye, B.1    Maret, W.2    Vallee, B.L.3
  • 108
    • 0034471629 scopus 로고    scopus 로고
    • Regulation of metallothionein gene expression and secretion in rat adipocytes differentiated from preadipocytes in primary culture
    • Trayhurn, P., Duncan, J. S., Wood, A. M., and Beattie, J. H. (2000) Regulation of metallothionein gene expression and secretion in rat adipocytes differentiated from preadipocytes in primary culture, Horm. Metab. Res. 32, 542-547.
    • (2000) Horm. Metab. Res. , vol.32 , pp. 542-547
    • Trayhurn, P.1    Duncan, J.S.2    Wood, A.M.3    Beattie, J.H.4
  • 109
    • 0008434168 scopus 로고    scopus 로고
    • Nuclear localization of metallothionein during cell proliferation and differentiation
    • Cherian, M. G., and Apostolova, M. D. (2000) Nuclear localization of metallothionein during cell proliferation and differentiation, Cell. Mol. Biol. 46, 347-356.
    • (2000) Cell. Mol. Biol. , vol.46 , pp. 347-356
    • Cherian, M.G.1    Apostolova, M.D.2
  • 110
    • 0034150290 scopus 로고    scopus 로고
    • Nuclear trafficking of metallothionein: Possible mechanisms and current knowledge
    • Ogra, Y., and Suzuki, K. T. (2000) Nuclear trafficking of metallothionein: Possible mechanisms and current knowledge, Cell. Mol. Biol. 46, 357-365.
    • (2000) Cell. Mol. Biol. , vol.46 , pp. 357-365
    • Ogra, Y.1    Suzuki, K.T.2
  • 111
    • 0027204069 scopus 로고
    • Targeting and germ line transmission of a null mutation at the metallothionein I and II loci in mouse
    • Michalska, A. E., and Choo, K. H. E. (1993) Targeting and germ line transmission of a null mutation at the metallothionein I and II loci in mouse, Proc. Natl. Acad. Sci. U.S.A. 90, 8088-8092.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8088-8092
    • Michalska, A.E.1    Choo, K.H.E.2
  • 113
    • 0033515626 scopus 로고    scopus 로고
    • Metallothionein is part of a zinc-scavenging mechanism for cell survival under conditions of extreme zinc deprivation
    • Suhy, D. A., Simon, K. D., Linzer, D. I. H., and O'Halloran, T. V. (1999) Metallothionein is part of a zinc-scavenging mechanism for cell survival under conditions of extreme zinc deprivation, J. Biol. Chem. 274, 9183-9192.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9183-9192
    • Suhy, D.A.1    Simon, K.D.2    Linzer, D.I.H.3    O'Halloran, T.V.4
  • 114
    • 0029987684 scopus 로고    scopus 로고
    • Metallothionein I and II protect against zinc deficiency and zinc toxicity in mice
    • Kelly, E. J., Quaife, C. J., Froelick, G. J., and Palmiter, R. D. (1996) Metallothionein I and II protect against zinc deficiency and zinc toxicity in mice, J. Nutr. 126, 1782-1790.
    • (1996) J. Nutr. , vol.126 , pp. 1782-1790
    • Kelly, E.J.1    Quaife, C.J.2    Froelick, G.J.3    Palmiter, R.D.4
  • 115
    • 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., and Tomonaga, M. (1991) The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein, Neuron 7, 337-347.
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 116
    • 0028932454 scopus 로고
    • Bioactivity of metallothionein-3 correlates with its novel β-domain sequence rather than metal binding properties
    • Sewell, A. K., Jensen, L. T., Erickson, J. C., Palmiter, R. D., and Winge, D. R. (1995) Bioactivity of metallothionein-3 correlates with its novel β-domain sequence rather than metal binding properties, Biochemistry 34, 4740-4747.
    • (1995) Biochemistry , vol.34 , pp. 4740-4747
    • Sewell, A.K.1    Jensen, L.T.2    Erickson, J.C.3    Palmiter, R.D.4    Winge, D.R.5
  • 117
    • 0034859756 scopus 로고    scopus 로고
    • Metal response element (MRE)-binding transcription factor-1 (MTF-1): Structure, function, and regulation
    • Giedroc, D. P., Chen, X., and Apuy, J. L. (2001) Metal response element (MRE)-binding transcription factor-1 (MTF-1): Structure, function, and regulation, Antioxid. Redox Signaling 3, 577-596.
    • (2001) Antioxid. Redox Signaling , vol.3 , pp. 577-596
    • Giedroc, D.P.1    Chen, X.2    Apuy, J.L.3
  • 118
    • 0035696187 scopus 로고    scopus 로고
    • Cellular zinc sensors: MTF-1 regulation of gene expression
    • Andrews, G. K. (2001) Cellular zinc sensors: MTF-1 regulation of gene expression, Biometals 14, 223-237.
    • (2001) Biometals , vol.14 , pp. 223-237
    • Andrews, G.K.1
  • 119
    • 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., Stark, G., Aguet, M., and Schaffner, W. (1994) The transcription factor MTF-1 is essential for basal and heavy-metal-induced metallothionein gene expression, EMBO J. 13, 2870-2875.
    • (1994) EMBO J. , vol.13 , pp. 2870-2875
    • Heuchel, R.1    Radtke, F.2    Georgiev, O.3    Stark, G.4    Aguet, M.5    Schaffner, W.6
  • 120
    • 1042289756 scopus 로고    scopus 로고
    • A novel cysteine cluster in human metal-responsive transcription factor 1 is required for heavy metal-induced transcriptional activation in vivo
    • Chen, X., Zhang, B., Harmon, P. M., Schaffner, W., Peterson, D. O., and Giedroc, D. P. (2004) A novel cysteine cluster in human metal-responsive transcription factor 1 is required for heavy metal-induced transcriptional activation in vivo, J. Biol. Chem. 279, 4515-4522.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4515-4522
    • Chen, X.1    Zhang, B.2    Harmon, P.M.3    Schaffner, W.4    Peterson, D.O.5    Giedroc, D.P.6
  • 122
    • 0001950228 scopus 로고    scopus 로고
    • The glutathione redox state and zinc mobilization from metallothionein and other proteins with zinc-sulfur coordination
    • (Shaw, C. A., Ed.), Taylor and Francis, Bristol, PA
    • Maret, W. (1997) The glutathione redox state and zinc mobilization from metallothionein and other proteins with zinc-sulfur coordination, in Glutathione in the nervous system (Shaw, C. A., Ed.) pp 257-273, Taylor and Francis, Bristol, PA.
    • (1997) Glutathione in the Nervous System , pp. 257-273
    • Maret, W.1


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