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Volumn 45, Issue 45, 2006, Pages 13641-13649

Functional characterization of iron-substituted tristetraprolin-2D (TTP-2D, NUP475-2D): RNA binding affinity and selectivity

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CLONING; ESCHERICHIA COLI; IRON COMPOUNDS; RNA; SUBSTITUTION REACTIONS;

EID: 33750986508     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060747n     Document Type: Article
Times cited : (41)

References (63)
  • 1
    • 0025051298 scopus 로고
    • Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein
    • Lai, W. S., Stumpo, D. J., and Blackshear, P. J. (1990) Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein, J. Biol. Chem. 265, 16556-16563.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16556-16563
    • Lai, W.S.1    Stumpo, D.J.2    Blackshear, P.J.3
  • 2
    • 0025001736 scopus 로고
    • A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence
    • DuBois, R. N., McLane, M. W., Ryder, K., Lau, L. F., and Nathans, D. (1990) A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence, J. Biol. Chem. 265, 19185-19191.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19185-19191
    • DuBois, R.N.1    McLane, M.W.2    Ryder, K.3    Lau, L.F.4    Nathans, D.5
  • 3
    • 0026031875 scopus 로고
    • The TIS11 primary response gene is a member of a gene family that encodes proteins with a highly conserved sequence containing an unusual Cys-His repeat
    • Varnum, B. C., Ma, Q. F., Chi, T. H., Fletcher, B., and Herschman, H. R. (1991) The TIS11 primary response gene is a member of a gene family that encodes proteins with a highly conserved sequence containing an unusual Cys-His repeat, Mol. Cell. Biol. 11, 1754-1758.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1754-1758
    • Varnum, B.C.1    Ma, Q.F.2    Chi, T.H.3    Fletcher, B.4    Herschman, H.R.5
  • 4
    • 0034625369 scopus 로고    scopus 로고
    • Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA
    • Lai, W. S., Carballo, E., Thorn, J. M., Kennington, E. A., and Blackshear, P. J. (2000) Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA, J. Biol. Chem. 275, 17827-17837.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17827-17837
    • Lai, W.S.1    Carballo, E.2    Thorn, J.M.3    Kennington, E.A.4    Blackshear, P.J.5
  • 5
    • 0037088665 scopus 로고    scopus 로고
    • Interactions of CCCH zinc finger proteins with mRNA: Non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs
    • Lai, W. S., Kennington, E. A., and Blackshear, P. J. (2002) Interactions of CCCH zinc finger proteins with mRNA: non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs, J. Biol. Chem. 277, 9606-9613.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9606-9613
    • Lai, W.S.1    Kennington, E.A.2    Blackshear, P.J.3
  • 6
    • 1542465947 scopus 로고    scopus 로고
    • Polymorphisms in the genes encoding members of the tristetraprolin family of human tandem CCCH zinc finger proteins
    • Blackshear, P. J., Phillips, R. S., Vazquez-Matias, J., and Mohrenweiser, H. (2003) Polymorphisms in the genes encoding members of the tristetraprolin family of human tandem CCCH zinc finger proteins, Prog. Nucleic Acid Res. Mol. Biol. 75, 43-68.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.75 , pp. 43-68
    • Blackshear, P.J.1    Phillips, R.S.2    Vazquez-Matias, J.3    Mohrenweiser, H.4
  • 8
    • 0030447656 scopus 로고    scopus 로고
    • Metal binding properties and secondary structure of the zinc-binding domain of Nup475
    • Worthington, M. T., Amann, B. T., Nathans, D., and Berg, J. M. (1996) Metal binding properties and secondary structure of the zinc-binding domain of Nup475, Proc. Natl. Acad. Sci. U.S.A. 93, 13754-13759.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13754-13759
    • Worthington, M.T.1    Amann, B.T.2    Nathans, D.3    Berg, J.M.4
  • 9
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • Carballo, E., Lai, W. S., and Blackshear, P. J. (1998) Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin, Science 281, 1001-1005.
    • (1998) Science , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 12
    • 0034653560 scopus 로고    scopus 로고
    • Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability
    • Carballo, E., Lai, W. S., and Blackshear, P. J. (2000) Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability, Blood 95, 1891-1899.
    • (2000) Blood , vol.95 , pp. 1891-1899
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 13
    • 0034073984 scopus 로고    scopus 로고
    • Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway
    • Stoecklin, G., Ming, X. F., Looser, R., and Moroni, C. (2000) Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway, Mol. Cell. Biol. 20, 3753-3763.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3753-3763
    • Stoecklin, G.1    Ming, X.F.2    Looser, R.3    Moroni, C.4
  • 14
    • 11844278314 scopus 로고    scopus 로고
    • Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay
    • Ogilvie, R. L., Abelson, M., Hau, H. H., Vlasova, I., Blackshear, P. J., and Bohjanen, P. R. (2005) Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay, J. Immunol. 174, 953-961.
    • (2005) J. Immunol. , vol.174 , pp. 953-961
    • Ogilvie, R.L.1    Abelson, M.2    Hau, H.H.3    Vlasova, I.4    Blackshear, P.J.5    Bohjanen, P.R.6
  • 15
    • 0038518201 scopus 로고    scopus 로고
    • Tristetraprolin binds to the COX-2 mRNA 3′ untranslated region in cancer cells
    • Boutaud, O., Dixon, D. A., Oates, J. A., and Sawaoka, H. (2003) Tristetraprolin binds to the COX-2 mRNA 3′ untranslated region in cancer cells, Adv. Exp. Med. Biol. 525, 157-160.
    • (2003) Adv. Exp. Med. Biol. , vol.525 , pp. 157-160
    • Boutaud, O.1    Dixon, D.A.2    Oates, J.A.3    Sawaoka, H.4
  • 16
    • 0037853195 scopus 로고    scopus 로고
    • Tristetraprolin binds to the 3′-untranslated region of cyclooxygenase-2 mRNA. A polyadenylation variant in a cancer cell line lacks the binding site
    • Sawaoka, H., Dixon, D. A., Oates, J. A., and Boutaud, O. (2003) Tristetraprolin binds to the 3′-untranslated region of cyclooxygenase-2 mRNA. A polyadenylation variant in a cancer cell line lacks the binding site, J. Biol. Chem. 278, 13928-13935.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13928-13935
    • Sawaoka, H.1    Dixon, D.A.2    Oates, J.A.3    Boutaud, O.4
  • 17
    • 16844362149 scopus 로고    scopus 로고
    • Post-transcriptional regulation in cancer
    • Audic, Y., and Hartley, R. S. (2004) Post-transcriptional regulation in cancer, Biol. Cell. 96, 479-498.
    • (2004) Biol. Cell , vol.96 , pp. 479-498
    • Audic, Y.1    Hartley, R.S.2
  • 18
    • 3042670643 scopus 로고    scopus 로고
    • Oxygen free radicals and the systemic inflammatory response
    • Closa, D., and Folch-Puy, E. (2004) Oxygen free radicals and the systemic inflammatory response, IUBMB Life 56, 185-191.
    • (2004) IUBMB Life , vol.56 , pp. 185-191
    • Closa, D.1    Folch-Puy, E.2
  • 19
    • 0141959075 scopus 로고    scopus 로고
    • Molecular targets in immune-mediated diseases: The case of tumour necrosis factor and rheumatoid arthritis
    • Campbell, I. K., Roberts, L. J., and Wicks, I. P. (2003) Molecular targets in immune-mediated diseases: the case of tumour necrosis factor and rheumatoid arthritis, Immunol. Cell Biol. 81, 354-366.
    • (2003) Immunol. Cell Biol. , vol.81 , pp. 354-366
    • Campbell, I.K.1    Roberts, L.J.2    Wicks, I.P.3
  • 20
    • 27944447260 scopus 로고    scopus 로고
    • Antibody treatments of inflammatory arthritis
    • Brown, M. A. (2005) Antibody treatments of inflammatory arthritis, Curr. Med. Chem. 12, 2943-2946.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 2943-2946
    • Brown, M.A.1
  • 21
    • 0038798677 scopus 로고    scopus 로고
    • A novel mechanism of tumor suppression by destabilizing AU-rich growth factor mRNA
    • Stoecklin, G., Gross, B., Ming, X. F., and Moroni, C. (2003) A novel mechanism of tumor suppression by destabilizing AU-rich growth factor mRNA, Oncogene. 22, 3554-3561.
    • (2003) Oncogene , vol.22 , pp. 3554-3561
    • Stoecklin, G.1    Gross, B.2    Ming, X.F.3    Moroni, C.4
  • 22
    • 0037073701 scopus 로고    scopus 로고
    • RNA binding properties of the AU-rich element-binding recombinant Nup475/TIS11/tristetraprolin protein
    • Worthington, M. T., Pelo, J. W., Sachedina, M. A., Applegate, J. L., Arseneau, K. O., and Pizarro, T. T. (2002) RNA binding properties of the AU-rich element-binding recombinant Nup475/TIS11/tristetraprolin protein, J. Biol. Chem. 277, 48558-48564.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48558-48564
    • Worthington, M.T.1    Pelo, J.W.2    Sachedina, M.A.3    Applegate, J.L.4    Arseneau, K.O.5    Pizarro, T.T.6
  • 23
    • 0033049125 scopus 로고    scopus 로고
    • Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA
    • Lai, W. S., Carballo, E., Strum, J. R., Kennington, E. A., Phillips, R. S., and Blackshear, P. J. (1999) Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA, Mol. Cell. Biol. 19, 4311-4323.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4311-4323
    • Lai, W.S.1    Carballo, E.2    Strum, J.R.3    Kennington, E.A.4    Phillips, R.S.5    Blackshear, P.J.6
  • 24
    • 0037472137 scopus 로고    scopus 로고
    • Selective RNA binding by a single CCCH zinc-binding domain from Nup475 (Tristetraprolin)
    • Michel, S. L. J., Guerrerio, A. L., and Berg, J. M. (2003) Selective RNA binding by a single CCCH zinc-binding domain from Nup475 (Tristetraprolin), Biochemistry 42, 4626-4630.
    • (2003) Biochemistry , vol.42 , pp. 4626-4630
    • Michel, S.L.J.1    Guerrerio, A.L.2    Berg, J.M.3
  • 25
    • 0038504080 scopus 로고    scopus 로고
    • Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates
    • Blackshear, P. J., Lai, W. S., Kennington, E. A., Brewer, G., Wilson, G. M., Guan, X., and Zhou, P. (2003) Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates, J. Biol. Chem. 278, 19947-19955.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19947-19955
    • Blackshear, P.J.1    Lai, W.S.2    Kennington, E.A.3    Brewer, G.4    Wilson, G.M.5    Guan, X.6    Zhou, P.7
  • 26
    • 3142615474 scopus 로고    scopus 로고
    • RNA sequence elements required for high affinity binding by the zinc finger domain of tristetraprolin: Conformational changes coupled to the bipartite nature of Au-rich MRNA-destabilizing motifs
    • Brewer, B. Y., Malicka, J., Blackshear, P. J., and Wilson, G. M. (2004) RNA sequence elements required for high affinity binding by the zinc finger domain of tristetraprolin: conformational changes coupled to the bipartite nature of Au-rich MRNA-destabilizing motifs, J. Biol. Chem. 279, 27870-27877.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27870-27877
    • Brewer, B.Y.1    Malicka, J.2    Blackshear, P.J.3    Wilson, G.M.4
  • 27
    • 1542364377 scopus 로고    scopus 로고
    • The design of functional DNA-binding proteins based on zinc finger domains
    • Jantz, D., Amann, B. T., Gatto, G. J., Jr., and Berg, J. M. (2004) The design of functional DNA-binding proteins based on zinc finger domains, Chem. Rev. 104, 789-799.
    • (2004) Chem. Rev. , vol.104 , pp. 789-799
    • Jantz, D.1    Amann, B.T.2    Gatto Jr., G.J.3    Berg, J.M.4
  • 28
    • 7244252846 scopus 로고    scopus 로고
    • Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: A zinc-dependent mRNA binding protein affected by posttranslational modifications
    • Cao, H. (2004) Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications, Biochemistry 43, 13724-13738.
    • (2004) Biochemistry , vol.43 , pp. 13724-13738
    • Cao, H.1
  • 29
    • 0037376557 scopus 로고    scopus 로고
    • Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases
    • Cao, H., Dzineku, F., and Blackshear, P. J. (2003) Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases, Arch. Biochem. Biophys. 412, 106-120.
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 106-120
    • Cao, H.1    Dzineku, F.2    Blackshear, P.J.3
  • 30
    • 0035871384 scopus 로고    scopus 로고
    • PIE-1 is a bifunctional protein that regulates maternal and zygotic gene expression in the embryonic germ line of Caenorhabditis elegans
    • Tenenhaus, C., Subramaniam, K., Dunn, M. A., and Seydoux, G. (2001) PIE-1 is a bifunctional protein that regulates maternal and zygotic gene expression in the embryonic germ line of Caenorhabditis elegans, Genes Dev. 15, 1031-1040.
    • (2001) Genes Dev. , vol.15 , pp. 1031-1040
    • Tenenhaus, C.1    Subramaniam, K.2    Dunn, M.A.3    Seydoux, G.4
  • 31
    • 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
  • 32
    • 1642389890 scopus 로고    scopus 로고
    • Zinc and sulfur: A critical biological partnership
    • Maret, W. (2004) Zinc and sulfur: a critical biological partnership, Biochemistry 43, 3301-3309.
    • (2004) Biochemistry , vol.43 , pp. 3301-3309
    • Maret, W.1
  • 33
    • 0036931270 scopus 로고    scopus 로고
    • Zinc fingers: Folds for many occasions
    • Matthews, J. M., and Sunde, M. (2002) Zinc fingers: folds for many occasions, IUBMB Life 54, 351-355.
    • (2002) IUBMB Life , vol.54 , pp. 351-355
    • Matthews, J.M.1    Sunde, M.2
  • 34
    • 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
  • 35
    • 0000957925 scopus 로고
    • On the metal-ion specificity of zinc finger proteins
    • Berg, J. M., and Merkle, D. L. (1989) On the metal-ion specificity of zinc finger proteins, J. Am. Chem. Soc. 111, 3759-3761.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3759-3761
    • Berg, J.M.1    Merkle, D.L.2
  • 36
    • 0021100320 scopus 로고
    • Xenopus transcription factor A requires zinc for binding to the 5 S RNA gene
    • Hanas, J. S., Hazuda, D. J., Bogenhagen, D. F., Wu, F. Y., and Wu, C. W. (1983) Xenopus transcription factor A requires zinc for binding to the 5 S RNA gene, J. Biol. Chem. 258, 14120-14125.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14120-14125
    • Hanas, J.S.1    Hazuda, D.J.2    Bogenhagen, D.F.3    Wu, F.Y.4    Wu, C.W.5
  • 37
    • 0029866985 scopus 로고    scopus 로고
    • In vivo and in vitro iron-replaced zinc finger generates free radicals and causes DNA damage
    • Conte, D., Narindrasorasak, S., and Sarkar, B. (1996) In vivo and in vitro iron-replaced zinc finger generates free radicals and causes DNA damage, J. Biol. Chem. 271, 5125-5130.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5125-5130
    • Conte, D.1    Narindrasorasak, S.2    Sarkar, B.3
  • 38
    • 0027537294 scopus 로고
    • A small single-"finger" peptide from the erythroid transcription factor GATA-1 binds specifically to DNA as a zinc or iron complex
    • Omichinski, J. G., Trainor, C., Evans, T., Gronenborn, A. M., Clore, G. M., and Felsenfeld, G. (1993) A small single-"finger" peptide from the erythroid transcription factor GATA-1 binds specifically to DNA as a zinc or iron complex, Proc. Natl. Acad. Sci. U.S.A. 90, 1676-1680.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1676-1680
    • Omichinski, J.G.1    Trainor, C.2    Evans, T.3    Gronenborn, A.M.4    Clore, G.M.5    Felsenfeld, G.6
  • 40
    • 0034871083 scopus 로고    scopus 로고
    • Zinc finger proteins as potential targets for toxic metal ions: Differential effects on structure and function
    • Hartwig, A. (2001) Zinc finger proteins as potential targets for toxic metal ions: differential effects on structure and function, Antioxid. Redox Signal 3, 625-34.
    • (2001) Antioxid. Redox Signal , vol.3 , pp. 625-634
    • Hartwig, A.1
  • 41
    • 0034873674 scopus 로고    scopus 로고
    • Oxidation of zinc-binding cysteine residues in transcription factor proteins
    • Wilcox, D. E., Schenk, A. D., Feldman, B. M., and Xu, Y. (2001) Oxidation of zinc-binding cysteine residues in transcription factor proteins, Antioxid. Redox Signaling 3, 549-564.
    • (2001) Antioxid. Redox Signaling , vol.3 , pp. 549-564
    • Wilcox, D.E.1    Schenk, A.D.2    Feldman, B.M.3    Xu, Y.4
  • 42
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups, Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 43
    • 0018416496 scopus 로고
    • Ellman's reagent: 5, 5′-dithiobis(2-nitrobenzoic acid) - A reexamination
    • Riddles, P. W., Blakeley, R. L., and Zerner, B. (1979) Ellman's reagent: 5, 5′-dithiobis(2-nitrobenzoic acid)-a reexamination, Anal. Biochem. 94, 75-81.
    • (1979) Anal. Biochem. , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 45
    • 0037435459 scopus 로고    scopus 로고
    • A Cys3His zinc-binding domain from Nup475/tristetraprolin: A novel fold with a disklike structure
    • Amann, B. T., Worthington, M. T., and Berg, J. M. (2003) A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure, Biochemistry 42, 217-221.
    • (2003) Biochemistry , vol.42 , pp. 217-221
    • Amann, B.T.1    Worthington, M.T.2    Berg, J.M.3
  • 46
    • 0021667647 scopus 로고
    • High spin cobalt(II) as a probe for the investigation of metalloproteins
    • Bertini, I., and Luchinat, C. (1984) High spin cobalt(II) as a probe for the investigation of metalloproteins, Adv. Inorg. Biochem. 6, 71-111.
    • (1984) Adv. Inorg. Biochem. , vol.6 , pp. 71-111
    • Bertini, I.1    Luchinat, C.2
  • 47
    • 0033593031 scopus 로고    scopus 로고
    • Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein
    • Berkovits, H. J., and Berg, J. M. (1999) Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein, Biochemistry 38, 16826-16830.
    • (1999) Biochemistry , vol.38 , pp. 16826-16830
    • Berkovits, H.J.1    Berg, J.M.2
  • 48
    • 3142615316 scopus 로고    scopus 로고
    • Spectroscopic determination of the thermodynamics of cobalt and zinc binding to GATA proteins
    • Ghering, A. B., Shokes, J. E., Scott, R. A., Omichinski, J. G., and Godwin, H. A. (2004) Spectroscopic determination of the thermodynamics of cobalt and zinc binding to GATA proteins, Biochemistry 43, 8346-8355.
    • (2004) Biochemistry , vol.43 , pp. 8346-8355
    • Ghering, A.B.1    Shokes, J.E.2    Scott, R.A.3    Omichinski, J.G.4    Godwin, H.A.5
  • 49
    • 0000685336 scopus 로고
    • Complexes of zinc finger peptides with Ni2+ and Fe2+
    • Krizek, B. A., and Berg, J. M. (1992) Complexes of zinc finger peptides with Ni2+ and Fe2+, Inorg. Chem. 31, 2984-2986.
    • (1992) Inorg. Chem. , vol.31 , pp. 2984-2986
    • Krizek, B.A.1    Berg, J.M.2
  • 50
    • 0013788501 scopus 로고
    • Rubredoxin: A new electron transfer protein from Clostridium pasteruianum
    • Lovenberg, W., and Sobel, B. E. (1965) Rubredoxin: A new electron transfer protein from Clostridium pasteruianum, Proc. Natl. Acad. Sci. U.S.A. 54, 193-199.
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 193-199
    • Lovenberg, W.1    Sobel, B.E.2
  • 52
    • 0014440788 scopus 로고
    • Further observations on the chemical nature of rubredoxin from Clostridium pasteurianum
    • Lovenberg, W., and Williams, W. M. (1969) Further observations on the chemical nature of rubredoxin from Clostridium pasteurianum, Biochemistry 8, 141-148.
    • (1969) Biochemistry , vol.8 , pp. 141-148
    • Lovenberg, W.1    Williams, W.M.2
  • 53
    • 0031694147 scopus 로고    scopus 로고
    • The de novo design of a rubredoxin-like Fe site
    • Farinas, E., and Regan, L. (1998) The de novo design of a rubredoxin-like Fe site, Protein Sci. 7, 1939-1946.
    • (1998) Protein Sci. , vol.7 , pp. 1939-1946
    • Farinas, E.1    Regan, L.2
  • 56
    • 20444495969 scopus 로고    scopus 로고
    • Multiple modes of RNA recognition by zinc finger proteins
    • Hall, T. M. (2005) Multiple modes of RNA recognition by zinc finger proteins, Curr. Opin. Struct. Biol. 15, 367-373.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 367-373
    • Hall, T.M.1
  • 57
    • 0036863118 scopus 로고    scopus 로고
    • Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover
    • Blackshear, P. J. (2002) Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover, Biochem. Soc. Trans. 30, 945-952.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 945-952
    • Blackshear, P.J.1
  • 58
    • 26644471490 scopus 로고    scopus 로고
    • Metal binding characteristics and role of iron oxidation in the ferric uptake regulator from Escherichia coli
    • Mills, S. A., and Marletta, M. A. (2005) Metal binding characteristics and role of iron oxidation in the ferric uptake regulator from Escherichia coli, Biochemistry 44, 13553-13559.
    • (2005) Biochemistry , vol.44 , pp. 13553-13559
    • Mills, S.A.1    Marletta, M.A.2
  • 59
    • 33745029895 scopus 로고    scopus 로고
    • Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor
    • Bozym, R. A., Thompson, R. B., Stoddard, A. K., and Fierke, C. A. (2006) Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor, ACS Chem. Biol. 7, 103-111.
    • (2006) ACS Chem. Biol. , vol.7 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 60
    • 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
  • 62
    • 0035986679 scopus 로고    scopus 로고
    • Metallochaperones: Bind and deliver
    • Rosenzweig, A. C. (2002) Metallochaperones: bind and deliver, Chem. Biol. 9, 673-677.
    • (2002) Chem. Biol. , vol.9 , pp. 673-677
    • Rosenzweig, A.C.1
  • 63
    • 11844257593 scopus 로고    scopus 로고
    • Coordinated remodeling of cellular metabolism during kon deficiency through targeted mRNA degradation
    • Puig, S., Askeland, E., and Thiele, D. I. (2005) Coordinated remodeling of cellular metabolism during kon deficiency through targeted mRNA degradation, Cell 120, 99-110.
    • (2005) Cell , vol.120 , pp. 99-110
    • Puig, S.1    Askeland, E.2    Thiele, D.I.3


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