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Volumn 1, Issue 1, 2004, Pages 61-66

Exploiting the 21st amino acid-purifying and labeling proteins by selenolate targeting

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; SELENOCYSTEINE;

EID: 13844304463     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth707     Document Type: Article
Times cited : (75)

References (34)
  • 1
    • 0038442808 scopus 로고    scopus 로고
    • Characterization of mammalian selenoproteomes
    • Kryukov, G.V. et al. Characterization of mammalian selenoproteomes. Science 300, 1439-1443 (2003).
    • (2003) Science , vol.300 , pp. 1439-1443
    • Kryukov, G.V.1
  • 2
    • 0030008330 scopus 로고    scopus 로고
    • Stadtman, T.C. Selenocysteine. Annu. Rev. Biochem. 65, 83–100 (1996).
    • (1996) Rev. Biochem , vol.65 , pp. 83-100
    • Stadtman, T.C.1
  • 3
    • 0025963803 scopus 로고
    • Selenocysteine: The 21st amino acid. Mol
    • Bock, A. et al. Selenocysteine: The 21st amino acid. Mol. Microbiol. 5, 515-520 (1991).
    • (1991) Microbiol , vol.5 , pp. 515-520
    • Bock, A.1
  • 5
    • 84988045454 scopus 로고    scopus 로고
    • Semisynthesis of proteins containing selenocysteine
    • Hondal, R.J. & Raines, R.T. Semisynthesis of proteins containing selenocysteine.
    • Hondal, R.J.1    Raines, R.T.2
  • 6
    • 84988042143 scopus 로고    scopus 로고
    • Methods Enzymol. 347, 70–83 (2002).
    • (2002) Methods Enzymol , vol.347 , pp. 70-83
  • 7
    • 0035958948 scopus 로고    scopus 로고
    • Preparation and properties of a selenium-containing catalytic antibody as type I deiodinase mimic
    • Lian, G. et al. Preparation and properties of a selenium-containing catalytic antibody as type I deiodinase mimic. J. Biol. Chem. 276, 28037-28041 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 28037-28041
    • Lian, G.1
  • 8
    • 0028326291 scopus 로고
    • The formation of diselenide bridges in proteins by incorporation of selenocysteine residues: Biosynthesis and characterization of (Se)2-thioredoxin
    • Muller, S. et al. The formation of diselenide bridges in proteins by incorporation of selenocysteine residues: Biosynthesis and characterization of (Se)2-thioredoxin. Biochemistry 33, 3404-3412 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3404-3412
    • Muller, S.1
  • 9
    • 0033536575 scopus 로고    scopus 로고
    • High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes
    • Arner, E.S.J., Sarioglu, H., Lottspeich, F., Holmgren, A. & Bock, A. High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes. J. Mol. Biol. 292, 10031016 (1999).
    • (1999) J. Mol. Biol , vol.292 , pp. 1003-1016
    • Arner, E.S.J.1    Sarioglu, H.2    Lottspeich, F.3    Holmgren, A.4    Bock, A.5
  • 10
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene
    • Gladyshev, V.N., Jeang, K-T. & Stadtman, T.C. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc. Natl Acad. Sa’. USA 93, 6146-6151 (1996).
    • (1996) Proc. Natl Acad. Sa’. USA , vol.93 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.-T.2    Stadtman, T.C.3
  • 11
    • 0032502720 scopus 로고    scopus 로고
    • Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue
    • Zhong, L., Arner, E.S.J., Ljung, J., Aslund, F. & Holmgren, A. Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. J. Biol. Chem. 273, 8581-8591 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 8581-8591
    • Zhong, L.1    Arner, E.S.J.2    Ljung, J.3    Aslund, F.4    Holmgren, A.5
  • 12
    • 0034705133 scopus 로고    scopus 로고
    • Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
    • Zhong, L., Arner, E.S.J. & Holmgren, A. Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proc. Natl. Acad. Sci. USA 97, 5854-5859 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5854-5859
    • Zhong, L.1    Arner, E.S.J.2    Holmgren, A.3
  • 13
    • 0032080238 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue
    • Nordberg, J., Zhong, L., Holmgren, A. & Arner, E.S.J. Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue. J. Biol. Chem. 273, 10835-10842 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 10835-10842
    • Nordberg, J.1    Zhong, L.2    Holmgren, A.3    Arner, E.S.J.4
  • 14
    • 0023730191 scopus 로고
    • Vasoactive intestinal polypeptide and related peptides. Isolation and chemistry
    • Mutt, V. Vasoactive intestinal polypeptide and related peptides. Isolation and chemistry. Ann. NY Acad. Sci. 527, 1-19 (1988).
    • (1988) Ann. NY Acad. Sci , vol.527 , pp. 1-19
    • Mutt, V.1
  • 15
    • 0024217479 scopus 로고
    • Synthesis, cloning and expression in Escherichia coli of artificial genes coding for biologically active elongated precursors of the vasoactive intestinal polypeptide
    • Simoncsits, A. et al. Synthesis, cloning and expression in Escherichia coli of artificial genes coding for biologically active elongated precursors of the vasoactive intestinal polypeptide. Eur. J. Biochem. 178, 343-350 (1988).
    • (1988) Eur. J. Biochem , vol.178 , pp. 343-350
    • Simoncsits, A.1
  • 16
    • 0024382841 scopus 로고
    • Antigenic and structural analysis of group II allergens (Der f II and Der p II) from house dust mites (Dermatophagoides spp)
    • Heymann, P.W., Chapman, M.D., Aalberse, R.C., Fox, J.W. & Platts-Mills, T.A. Antigenic and structural analysis of group II allergens (Der f II and Der p II) from house dust mites (Dermatophagoides spp). J. Allergy Clin. Immunol. 83, 10551067 (1989).
    • (1989) J. Allergy Clin. Immunol , vol.83 , pp. 1055-1067
    • Heymann, P.W.1    Chapman, M.D.2    Aalberse, R.C.3    Fox, J.W.4    Platts-Mills, T.A.5
  • 17
    • 0027302932 scopus 로고
    • Arsenical-based affinity chromatography of vicinal dithiol-containing proteins: Purification of L1210 leukemia cytoplasmic proteins and the recombinant rat c-erb Aß1 T3 receptor
    • Kalef, E., Walfish, P.G. & Gitler, C. Arsenical-based affinity chromatography of vicinal dithiol-containing proteins: Purification of L1210 leukemia cytoplasmic proteins and the recombinant rat c-erb Aß1 T3 receptor. Anal. Biochem. 212, 325-334 (1993).
    • (1993) Anal. Biochem , vol.212 , pp. 325-334
    • Kalef, E.1    Walfish, P.G.2    Gitler, C.3
  • 18
    • 0025763170 scopus 로고
    • Human plasma lecithin: Cholesterol acyltransferase. Preparation and use of immobilized p- aminophenylarsenoxide as a catalytic site-directed covalent ligand in enzyme purification
    • Zhou, G.Y., Jauhiainen, M., Stevenson, K. & Dolphin, P.J. Human plasma lecithin:cholesterol acyltransferase. Preparation and use of immobilized p- aminophenylarsenoxide as a catalytic site-directed covalent ligand in enzyme purification. J. Chromatogr. 568, 69-83 (1991).
    • (1991) J. Chromatogr , vol.568 , pp. 69-83
    • Zhou, G.Y.1    Jauhiainen, M.2    Stevenson, K.3    Dolphin, P.J.4
  • 19
    • 0026623536 scopus 로고
    • Iodophenylarsine oxide and arsenical affinity chromatography: New probes for dithiol proteins. Application to tubulins and to components of the insulin receptor-glucose transporter signal transduction pathway
    • Hoffman, R.D. & Lane, M.D. Iodophenylarsine oxide and arsenical affinity chromatography: New probes for dithiol proteins. Application to tubulins and to components of the insulin receptor-glucose transporter signal transduction pathway. J. Biol. Chem. 267, 14005-14011 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 14005-14011
    • Hoffman, R.D.1    Lane, M.D.2
  • 20
    • 0030697440 scopus 로고    scopus 로고
    • The path of unspecific incorporation of selenium in Escherichia coli. Arch
    • Muller, S., Heider, J. & Bock, A. The path of unspecific incorporation of selenium in Escherichia coli. Arch. Microbiol. 168, 421-427 (1997).
    • (1997) Microbiol , vol.168 , pp. 421-427
    • Muller, S.1    Heider, J.2    Bock, A.3
  • 21
    • 0023694907 scopus 로고
    • Pharmacology, molecular identification and functional characteristics of vasoactive intestinal peptide receptors in human breast cancer cells
    • Gespach, C., Bawab, W., de Cremoux, P. & Calvo, F. Pharmacology, molecular identification and functional characteristics of vasoactive intestinal peptide receptors in human breast cancer cells. Cancer Res. 48, 5079-5083 (1988).
    • (1988) Cancer Res , vol.48 , pp. 5079-5083
    • Gespach, C.1    Bawab, W.2    de Cremoux, P.3    Calvo, F.4
  • 22
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds
    • Gromer, S., Arscott, L.D., Williams, C.H., Jr, Schirmer, R.H. & Becker, K. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J. Biol. Chem. 273, 20096-20101 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 20096-20101
    • Arscott Williams Schirmer Becker, S.L.D.C.H.R.H.K.1
  • 23
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe, K. Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60, 523-533 (2003).
    • (2003) Appl. Microbiol. Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 24
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B.A., Adams, S.R. & Tsien, R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272 (1998).
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 25
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams, S.R. et al. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications. J. Am. Chem. Soc. 124, 6063-6076 (2002).
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6063-6076
    • Adams, S.R.1
  • 26
    • 0036121476 scopus 로고    scopus 로고
    • Recombinant expression of mammalian selenocysteine-containing thioredoxin reductase and other selenoproteins in Escherichia coli
    • Arner, E.S.J. Recombinant expression of mammalian selenocysteine-containing thioredoxin reductase and other selenoproteins in Escherichia coli. Methods Enzymol. 347, 226-235 (2002).
    • (2002) Methods Enzymol , vol.347 , pp. 226-235
    • Arner, E.S.J.1
  • 27
    • 0037811713 scopus 로고    scopus 로고
    • Loss of selenium from selenoproteins: Conversion of selenocysteine to dehydroalanine in vitro
    • Ma, S., Caprioli, R.M., Hill, K.E. & Burk, R.F. Loss of selenium from selenoproteins: Conversion of selenocysteine to dehydroalanine in vitro. J. Am. Soc. Mass Spectrom. 14, 593-600 (2003).
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 593-600
    • Ma, S.1    Caprioli, R.M.2    Hill, K.E.3    Burk, R.F.4
  • 28
    • 0037262667 scopus 로고    scopus 로고
    • Synthesis of target-specific radiolabeled peptides for diagnostic imaging
    • Fichna, J. & Janecka, A. Synthesis of target-specific radiolabeled peptides for diagnostic imaging. Bioconjug. Chem. 14, 3-17 (2003).
    • (2003) Bioconjug. Chem , vol.14 , pp. 3-17
    • Fichna, J.1    Janecka, A.2
  • 29
    • 0034911579 scopus 로고    scopus 로고
    • Recent progress in fluorine-18 labelled peptide radiopharmaceuticals
    • Okarvi, S.M. Recent progress in fluorine-18 labelled peptide radiopharmaceuticals. Eur. J. Nucl. Med. 28, 929-938 (2001).
    • (2001) Eur. J. Nucl. Med , vol.28 , pp. 929-938
    • Okarvi, S.M.1
  • 30
    • 0032884409 scopus 로고    scopus 로고
    • Stable one-step technetium-99m labeling of His-tagged recombinant proteins with a novel Tc(I)-carbonyl complex
    • Waibel, R. et al. Stable one-step technetium-99m labeling of His-tagged recombinant proteins with a novel Tc(I)-carbonyl complex. Nat. Biotechnol. 17, 897-901 (1999).
    • (1999) Nat. Biotechnol , vol.17 , pp. 897-901
    • Waibel, R.1
  • 31
    • 0035814333 scopus 로고    scopus 로고
    • Site-specific incorporation of fluorescent probes into protein: Hexahistidine-tag-mediated fluorescent labeling with (Ni2+: Nitrilotriacetic acid (n)-fluorochrome conjugates
    • 2+:nitrilotriacetic acid (n)-fluorochrome conjugates. J. Am. Chem. Soc. 123, 12123-12125 (2001).
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 12123-12125
    • Kapanidis, A.N.1    Ebright, Y.W.2    Ebright, R.H.3
  • 32
    • 0025284658 scopus 로고
    • Isolation of cDNA coding for the major mite allergen Der p II by IgE plaque immunoassay
    • Chua, K.Y. et al. Isolation of cDNA coding for the major mite allergen Der p II by IgE plaque immunoassay. Int. Arch. Allergy Appl. Immunol. 91, 118-123 (1990).
    • (1990) Int. Arch. Allergy Appl. Immunol , vol.91 , pp. 118-123
    • Chua, K.Y.1
  • 33
    • 0031773474 scopus 로고    scopus 로고
    • Preparation and assay of mammalian thioredoxin and thioredoxin reductase
    • Arner, E.S.J., Zhong, L. & Holmgren, A. Preparation and assay of mammalian thioredoxin and thioredoxin reductase. Methods Enzymol. 300, 226-239 (1999).
    • (1999) Methods Enzymol , vol.300 , pp. 226-239
    • Arner, E.S.J.1    Zhong, L.2    Holmgren, A.3
  • 34
    • 0015504841 scopus 로고
    • Isolation from porcine intestinal wall of a vasoactive octacosapeptide related to secretin and to glucagon
    • Said, S.I. & Mutt, V. Isolation from porcine intestinal wall of a vasoactive octacosapeptide related to secretin and to glucagon. Eur. J. Biochem. 28, 199204 (1972).
    • (1972) Eur. J. Biochem , vol.28 , pp. 199-204
    • Said, S.I.1    Mutt, V.2


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