메뉴 건너뛰기




Volumn 21, Issue 7, 2010, Pages 1341-1348

Detection of escherichia coli enoyl-ACP reductase using biarsenical-tetracysteine motif

Author keywords

[No Author keywords available]

Indexed keywords

BIARSENICAL REAGENT; CYSTEINE DERIVATIVE; ENHANCED GREEN FLUORESCENT PROTEIN; ENOYL ACYL CARRIER PROTEIN REDUCTASE (NADH); REAGENT; TETRACYSTEINE; UNCLASSIFIED DRUG;

EID: 77954869532     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc1001533     Document Type: Article
Times cited : (7)

References (47)
  • 1
    • 13444261101 scopus 로고    scopus 로고
    • Selective chemical labeling of proteins in living cells
    • Miller, L. W. and Cornish, V. W. (2005) Selective chemical labeling of proteins in living cells Curr. Opin. Chem. Biol. 9, 56-61
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 56-61
    • Miller, L.W.1    Cornish, V.W.2
  • 4
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • Heim, R., Prashert, D., and Tsien, R. Y. (1994) Wavelength mutations and posttranslational autoxidation of green fluorescent protein Proc. Natl. Acad. Sci. U.S.A. 91, 12501-12504
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12501-12504
    • Heim, R.1    Prashert, D.2    Tsien, R.Y.3
  • 6
    • 0030832226 scopus 로고    scopus 로고
    • On/off blinking and switching behaviour of single molecules of green fluorescent protein
    • Dickson, R. M., Cubitt, A. B., Tsien, R. Y., and Moerner, W. E. (1997) On/off blinking and switching behaviour of single molecules of green fluorescent protein Nature 388, 355-358
    • (1997) Nature , vol.388 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Tsien, R.Y.3    Moerner, W.E.4
  • 8
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein Annu. Rev. Biochem. 67, 509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 10
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N., Palmer, A. E., and Tsien, R. Y. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein Nat. Biotechnol. 22, 1567-1572
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 11
    • 29144446316 scopus 로고    scopus 로고
    • Improved fluorescent proteins for single-molecule research in molecular tracking and co-localization
    • Steinmeyer, R., Noskov, A., Krasel, C., Weber, I., Dees, C., and Harms, G. S. (2005) Improved fluorescent proteins for single-molecule research in molecular tracking and co-localization J. Fluoresc. 15, 707-721
    • (2005) J. Fluoresc. , vol.15 , pp. 707-721
    • Steinmeyer, R.1    Noskov, A.2    Krasel, C.3    Weber, I.4    Dees, C.5    Harms, G.S.6
  • 14
    • 0037225979 scopus 로고    scopus 로고
    • Immunofluorescent labeling of cancer marker Her2 and other cellular targets with semiconductor quantum dots
    • Wu, X., Liu, H., Liu, J., Haley, K. N., Treadway, J. A., Larson, J. P., Ge, N., Peale, F., and Bruchez, M. P. (2002) Immunofluorescent labeling of cancer marker Her2 and other cellular targets with semiconductor quantum dots Nat. Biotechnol. 21, 41-46
    • (2002) Nat. Biotechnol. , vol.21 , pp. 41-46
    • Wu, X.1    Liu, H.2    Liu, J.3    Haley, K.N.4    Treadway, J.A.5    Larson, J.P.6    Ge, N.7    Peale, F.8    Bruchez, M.P.9
  • 15
    • 65249177729 scopus 로고    scopus 로고
    • An improved cell-penetrating, caspase-activatable, near-infrared fluorescent peptide for apoptosis imaging
    • Maxwell, D., Chang, Q., Zhang, X., Barnett, E. M., and Piwnica-Worms, D. (2009) An improved cell-penetrating, caspase-activatable, near-infrared fluorescent peptide for apoptosis imaging Bioconjugate Chem. 20, 702-709
    • (2009) Bioconjugate Chem. , vol.20 , pp. 702-709
    • Maxwell, D.1    Chang, Q.2    Zhang, X.3    Barnett, E.M.4    Piwnica-Worms, D.5
  • 16
    • 45549102498 scopus 로고    scopus 로고
    • A drug-controllable tag for visualizing newly synthesized proteins in cells and whole animals
    • Lin, M. Z., Glenn, J. S., and Tsien, R. Y. (2008) A drug-controllable tag for visualizing newly synthesized proteins in cells and whole animals Proc. Natl. Acad. Sci. U.S.A. 105, 7744-7749
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7744-7749
    • Lin, M.Z.1    Glenn, J.S.2    Tsien, R.Y.3
  • 17
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler, A., Gendreizig, S., Gromemeyer, T., Pick, H., Vogel, H., and Johnsson, K. (2003) A general method for the covalent labeling of fusion proteins with small molecules in vivo Nat. Biotechnol. 21, 86-89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gromemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 19
    • 25144442659 scopus 로고    scopus 로고
    • Single-cell FRET imaging of transferrin receptor trafficking dynamics by Sfp-catalyzed, site-specific protein labeling
    • Yin, J., Lin, A. J., Buckett, P. D., Resnick, M. W., Golan, D. E., and Walsh, C. T. (2005) Single-cell FRET imaging of transferrin receptor trafficking dynamics by Sfp-catalyzed, site-specific protein labeling Chem. Biol. 12, 999-1006
    • (2005) Chem. Biol. , vol.12 , pp. 999-1006
    • Yin, J.1    Lin, A.J.2    Buckett, P.D.3    Resnick, M.W.4    Golan, D.E.5    Walsh, C.T.6
  • 20
    • 48249132422 scopus 로고    scopus 로고
    • An eight residue fragment of an acyl carrier protein suffices for post-translational introduction of fluorescent pantetheinyl arms in protein modification in vitro and in vivo
    • Zhou, Z., Koglin, A., Wang, Y., McMahon, A. P., and Walsh, C. T. (2008) An eight residue fragment of an acyl carrier protein suffices for post-translational introduction of fluorescent pantetheinyl arms in protein modification in vitro and in vivo J. Am. Chem. Soc. 130, 9925-9930
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9925-9930
    • Zhou, Z.1    Koglin, A.2    Wang, Y.3    McMahon, A.P.4    Walsh, C.T.5
  • 21
    • 3242754218 scopus 로고    scopus 로고
    • Specific labeling of cell surface proteins with chemically diverse compounds
    • George, N., Pick, H., Vogel, H., Johnsson, N., and Johnsson, K. (2004) Specific labeling of cell surface proteins with chemically diverse compounds J. Am. Chem. Soc. 126, 8896-8897
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8896-8897
    • George, N.1    Pick, H.2    Vogel, H.3    Johnsson, N.4    Johnsson, K.5
  • 22
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Grifin, B. A., Adams, S. R., Jones, J., and Tsien, R. Y. (2000) Fluorescent labeling of recombinant proteins in living cells with FlAsH Methods Enzymol. 327, 565-578
    • (2000) Methods Enzymol. , vol.327 , pp. 565-578
    • Grifin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 23
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R., and Tsien, R. Y. (1998) Specific covalent labeling of recombinant protein molecules inside live cells Science 281, 269-272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 24
    • 33646872862 scopus 로고    scopus 로고
    • Accumulation of FlAsH/Lumio green in active mitochondria can be reversed by beta-mercaptoethanol for specific staining of tetracysteine-tagged proteins
    • Langhorst, M. F., Genisyuerek, S., and Stuermer, C. A. O. (2006) Accumulation of FlAsH/Lumio green in active mitochondria can be reversed by beta-mercaptoethanol for specific staining of tetracysteine-tagged proteins Histochem. Cell Biol. 125, 743-747
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 743-747
    • Langhorst, M.F.1    Genisyuerek, S.2    Stuermer, C.A.O.3
  • 25
    • 35948932520 scopus 로고    scopus 로고
    • The biarsenical dye Lumio (TM) exhibits a reduced ability to specifically detect tetracysteine-containing proteins within live cells
    • Hearps, A. C., Pryor, M. J., Kuusisto, H. V., Rawlinson, S. M., Piller, S. C., and Jans, D. A. (2007) The biarsenical dye Lumio (TM) exhibits a reduced ability to specifically detect tetracysteine-containing proteins within live cells J. Fluoresc. 17, 593-597
    • (2007) J. Fluoresc. , vol.17 , pp. 593-597
    • Hearps, A.C.1    Pryor, M.J.2    Kuusisto, H.V.3    Rawlinson, S.M.4    Piller, S.C.5    Jans, D.A.6
  • 26
    • 9444247617 scopus 로고    scopus 로고
    • Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging
    • Andresen, M., Schmitz-Salue, R., and Jakobs, S. (2004) Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging Mol. Biol. Cell 15, 5616-5622
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5616-5622
    • Andresen, M.1    Schmitz-Salue, R.2    Jakobs, S.3
  • 27
    • 60549094701 scopus 로고    scopus 로고
    • Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins
    • Taguchi, Y., Shi, Z. D., Ruddy, B., Dorward, D. W., Greene, L., and Baron, G. S. (2009) Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins Mol. Biol. Cell 20, 233-244
    • (2009) Mol. Biol. Cell , vol.20 , pp. 233-244
    • Taguchi, Y.1    Shi, Z.D.2    Ruddy, B.3    Dorward, D.W.4    Greene, L.5    Baron, G.S.6
  • 29
    • 1442264894 scopus 로고    scopus 로고
    • A new protein conformation indicator based on biarsenical fluorescein with an extended benzoic acid moiety
    • Nakanishi, J., Maeda, M., and Umezawa, Y. (2004) A new protein conformation indicator based on biarsenical fluorescein with an extended benzoic acid moiety Anal. Sci. 20, 273-278
    • (2004) Anal. Sci. , vol.20 , pp. 273-278
    • Nakanishi, J.1    Maeda, M.2    Umezawa, Y.3
  • 30
    • 67649537863 scopus 로고    scopus 로고
    • Diversity in enoyl-acyl carrier protein reductases
    • Massengo-Tiassé, R. P. and Cronan, J. E. (2009) Diversity in enoyl-acyl carrier protein reductases Cell. Mol. Life Sci. 66, 1507-1517
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1507-1517
    • Massengo-Tiassé, R.P.1    Cronan, J.E.2
  • 31
    • 72049128855 scopus 로고    scopus 로고
    • Novel enoyl-ACP reductase (FabI) potential inhibitors of Escherichia coli from Chinese medicine monomers
    • Yao, J., Zhang, Q., Min, J., He, J., and Yu, Z. (2010) Novel enoyl-ACP reductase (FabI) potential inhibitors of Escherichia coli from Chinese medicine monomers Bioorg. Med. Chem. Lett. 20, 56-59
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 56-59
    • Yao, J.1    Zhang, Q.2    Min, J.3    He, J.4    Yu, Z.5
  • 32
    • 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., Campbell, R. E., Gross, L. A., Martin, B. R., Walkup, G. K., Yao, Y., Llopis, J., and Tsien, R. Y. (2002) 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) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 33
    • 4544303329 scopus 로고    scopus 로고
    • Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues
    • Wang, H. and Cronan, J. E. (2004) Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues J. Biol. Chem. 279, 34489-34495
    • (2004) J. Biol. Chem. , vol.279 , pp. 34489-34495
    • Wang, H.1    Cronan, J.E.2
  • 34
    • 49049101721 scopus 로고    scopus 로고
    • Biarsenical-tetracysteine motif as a fluorescent tag for detection in capillary electrophoresis
    • Kottegoda, S., Aoto, P. C., Sims, C. E., and Allbritton, N. L. (2008) Biarsenical-tetracysteine motif as a fluorescent tag for detection in capillary electrophoresis Anal. Chem. 80, 5358-5366
    • (2008) Anal. Chem. , vol.80 , pp. 5358-5366
    • Kottegoda, S.1    Aoto, P.C.2    Sims, C.E.3    Allbritton, N.L.4
  • 35
    • 56349158676 scopus 로고    scopus 로고
    • Epigallocatechin gallate is a slow-tight binding inhibitor of enoyl-ACP reductase from Plasmodium falciparum
    • Banerjee, T., Sharma, S. K., Surolia, N., and Surolia, A. (2008) Epigallocatechin gallate is a slow-tight binding inhibitor of enoyl-ACP reductase from Plasmodium falciparum Biochem. Biophys. Res. Commun. 377, 1238-1242
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 1238-1242
    • Banerjee, T.1    Sharma, S.K.2    Surolia, N.3    Surolia, A.4
  • 36
    • 4444303801 scopus 로고    scopus 로고
    • Detection of tetracysteine-tagged proteins using a biarsenical fluorescein derivative through dry microplate array gel electrophoresis
    • Feldman, G., Bogoev, R., Shevirov, J., Sartiel, A., and Margalit, L. (2004) Detection of tetracysteine-tagged proteins using a biarsenical fluorescein derivative through dry microplate array gel electrophoresis Electrophoresis 25, 2447-2451
    • (2004) Electrophoresis , vol.25 , pp. 2447-2451
    • Feldman, G.1    Bogoev, R.2    Shevirov, J.3    Sartiel, A.4    Margalit, L.5
  • 37
    • 33744928389 scopus 로고    scopus 로고
    • Aptamer-based detection and quantitative analysis of ricin using affinity probe capillary electrophoresis
    • Haes, A. J., Giordano, B. C., and Collins, G. E. (2006) Aptamer-based detection and quantitative analysis of ricin using affinity probe capillary electrophoresis Anal. Chem. 78, 3758-3764
    • (2006) Anal. Chem. , vol.78 , pp. 3758-3764
    • Haes, A.J.1    Giordano, B.C.2    Collins, G.E.3
  • 39
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 40
    • 0030589497 scopus 로고    scopus 로고
    • Negative staining of proteins in polyacrylamide gels with methyl trichloroacetate
    • Candiano, G., Porotto, M., Lanciotti, M., and Ghiggeri, G. M. (1996) Negative staining of proteins in polyacrylamide gels with methyl trichloroacetate Anal. Biochem. 243, 245-248
    • (1996) Anal. Biochem. , vol.243 , pp. 245-248
    • Candiano, G.1    Porotto, M.2    Lanciotti, M.3    Ghiggeri, G.M.4
  • 41
    • 23144451918 scopus 로고    scopus 로고
    • Quantitative detection of phosphoproteins by combination of two-dimensional difference gel electrophoresis and phosphospecific fluorescent staining
    • Stasyk, T., Morandel, S., Bakry, R., Feuerstein, I., Huck, C. W., Stecher, G., Bonn, G. K., and Huber, L. A. (2005) Quantitative detection of phosphoproteins by combination of two-dimensional difference gel electrophoresis and phosphospecific fluorescent staining Electrophoresis 26, 2850-2854
    • (2005) Electrophoresis , vol.26 , pp. 2850-2854
    • Stasyk, T.1    Morandel, S.2    Bakry, R.3    Feuerstein, I.4    Huck, C.W.5    Stecher, G.6    Bonn, G.K.7    Huber, L.A.8
  • 42
    • 0034802605 scopus 로고    scopus 로고
    • The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins
    • Stroffekova, K., Proenza, C., and Beam, K. G. (2001) The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins Pfluegers Arch. 442, 859-866
    • (2001) Pfluegers Arch. , vol.442 , pp. 859-866
    • Stroffekova, K.1    Proenza, C.2    Beam, K.G.3
  • 43
    • 17444432962 scopus 로고    scopus 로고
    • Thermodynamics of the As(III)-thiol interaction: Arsenite and monomethylarsenite complexes with glutathione, dihydrolipoic acid, and other thiol ligands
    • Spuches, A. M., Kruszyna, H. G., Rich, A. M., and Wilcox, D. E. (2005) Thermodynamics of the As(III)-thiol interaction: arsenite and monomethylarsenite complexes with glutathione, dihydrolipoic acid, and other thiol ligands Inorg. Chem. 44, 2964-2972
    • (2005) Inorg. Chem. , vol.44 , pp. 2964-2972
    • Spuches, A.M.1    Kruszyna, H.G.2    Rich, A.M.3    Wilcox, D.E.4
  • 44
    • 2442514066 scopus 로고    scopus 로고
    • Equilibrium characterization of the As(III)-cysteine and the As(III)-glutathione systems in aqueous solution
    • Rey, N. A., Howarth, O. W., and Pereira-Maia, E. C. (2004) Equilibrium characterization of the As(III)-cysteine and the As(III)-glutathione systems in aqueous solution J. Inorg. Biochem. 98, 1151-1159
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 1151-1159
    • Rey, N.A.1    Howarth, O.W.2    Pereira-Maia, E.C.3
  • 45
    • 53849114687 scopus 로고    scopus 로고
    • Cross-strand split Tetra-Cys motifs as structure sensors in a beta-sheet protein
    • Krishnan, B. and Gierasch, L. M. (2008) Cross-strand split Tetra-Cys motifs as structure sensors in a beta-sheet protein Chem. Biol. 15, 1104-1115
    • (2008) Chem. Biol. , vol.15 , pp. 1104-1115
    • Krishnan, B.1    Gierasch, L.M.2
  • 46
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans, B. N. G., Adams, S. R., Ellisman, M. H., and Tsien, R. Y. (2006) The fluorescent toolbox for assessing protein location and function Science 312, 217-224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.G.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.