메뉴 건너뛰기




Volumn 19, Issue 11, 2008, Pages 2113-2119

Dual function labeling of biomolecules based on DsRed-monomer

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOMOLECULES; CALMODULIN; COPPER; FLUORESCENCE;

EID: 56749163793     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc800147k     Document Type: Article
Times cited : (4)

References (49)
  • 1
    • 13444267652 scopus 로고    scopus 로고
    • Protein localization studies in the age of 'Omics'
    • O'Rourke, N. A., Meyer, T., and Chandy, G. (2005) Protein localization studies in the age of 'Omics'. Curr. Opin. Chem. Biol. 9, 82-7.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 82-87
    • O'Rourke, N.A.1    Meyer, T.2    Chandy, G.3
  • 2
    • 18744401100 scopus 로고    scopus 로고
    • Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
    • Chen, I., Howarth, M., Lin, W., and Ting, A. Y. (2005) Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat. Methods 2, 99-104.
    • (2005) Nat. Methods , vol.2 , pp. 99-104
    • Chen, I.1    Howarth, M.2    Lin, W.3    Ting, A.Y.4
  • 3
    • 13844270303 scopus 로고    scopus 로고
    • Recent advances in gel-based proteome profiling techniques
    • Hu, Y., Huang, X., Chen, G. Y., and Yao, S. Q. (2004) Recent advances in gel-based proteome profiling techniques. Mol. Biotechnol. 28, 63-76.
    • (2004) Mol. Biotechnol , vol.28 , pp. 63-76
    • Hu, Y.1    Huang, X.2    Chen, G.Y.3    Yao, S.Q.4
  • 4
    • 4644320062 scopus 로고    scopus 로고
    • Targeted protein functionalization using His-tags
    • Meredith, G. D., Wu, H. Y., and Allbritton, N. L. (2004) Targeted protein functionalization using His-tags. Bioconjugate Chem. 15, 969-82.
    • (2004) Bioconjugate Chem , vol.15 , pp. 969-982
    • Meredith, G.D.1    Wu, H.Y.2    Allbritton, N.L.3
  • 5
    • 15244346042 scopus 로고    scopus 로고
    • Synthesis and self-alkylation of isotope-coded affinity tag reagents
    • Zhang, Z., Edwards, P. J., Roeske, R. W., and Guo, L. (2005) Synthesis and self-alkylation of isotope-coded affinity tag reagents. Bioconjugate Chem. 16, 458-64.
    • (2005) Bioconjugate Chem , vol.16 , pp. 458-464
    • Zhang, Z.1    Edwards, P.J.2    Roeske, R.W.3    Guo, L.4
  • 7
    • 34547218393 scopus 로고    scopus 로고
    • Identification of an orthogonal peptide binding motif for biarsenical multiuse affinity probes
    • Chen, B., Cao, H., Yan, P., Mayer, M. U., and Squier, T. C. (2007) Identification of an orthogonal peptide binding motif for biarsenical multiuse affinity probes. Bioconjugate Chem. 18, 1259-65.
    • (2007) Bioconjugate Chem , vol.18 , pp. 1259-1265
    • Chen, B.1    Cao, H.2    Yan, P.3    Mayer, M.U.4    Squier, T.C.5
  • 8
    • 2442679406 scopus 로고    scopus 로고
    • Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase
    • Tanaka, T., Kamiya, N., and Nagamune, T. (2004) Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase. Bioconjugate Chem. 15, 491-7.
    • (2004) Bioconjugate Chem , vol.15 , pp. 491-497
    • Tanaka, T.1    Kamiya, N.2    Nagamune, T.3
  • 9
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh, D. S. (2005) Making the most of affinity tags. Trends Biotechnol. 23, 316-20.
    • (2005) Trends Biotechnol , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 10
    • 0033819031 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo and in vitro using small peptide tags
    • Cull, M. G., and Schatz, P. J. (2000) Biotinylation of proteins in vivo and in vitro using small peptide tags. Methods Enzymol. 326, 430-40.
    • (2000) Methods Enzymol , vol.326 , pp. 430-440
    • Cull, M.G.1    Schatz, P.J.2
  • 14
    • 33847247484 scopus 로고    scopus 로고
    • A generic method for the production of recombinant proteins in Escherichia coli using a dual hexahistidine-maltose-binding protein affinity tag
    • Tropea, J. E., Cherry, S., Nallamsetty, S., Bignon, C., and Waugh, D. S. (2007) A generic method for the production of recombinant proteins in Escherichia coli using a dual hexahistidine-maltose-binding protein affinity tag. Methods Mol. Biol. 363, 1-19.
    • (2007) Methods Mol. Biol , vol.363 , pp. 1-19
    • Tropea, J.E.1    Cherry, S.2    Nallamsetty, S.3    Bignon, C.4    Waugh, D.S.5
  • 19
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson, G. H., and Lippincott-Schwartz, J. (2002) A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297, 1873-7.
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 20
    • 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, 6063-76.
    • (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
  • 21
    • 2542448230 scopus 로고    scopus 로고
    • Engineering green fluorescent protein as a dual functional tag
    • Paramban, R. I., Bugos, R. C., and Su, W. W. (2004) Engineering green fluorescent protein as a dual functional tag. Biotechnol. Bioeng. 86, 687-97.
    • (2004) Biotechnol. Bioeng , vol.86 , pp. 687-697
    • Paramban, R.I.1    Bugos, R.C.2    Su, W.W.3
  • 23
    • 0017734494 scopus 로고
    • Mechanism of quenching of fluorescein by anti-fluorescein IgG antibodies
    • Watt, R. M., and Voss, E. W. (1977) Mechanism of quenching of fluorescein by anti-fluorescein IgG antibodies. Immunochemistry 14, 533-51.
    • (1977) Immunochemistry , vol.14 , pp. 533-551
    • Watt, R.M.1    Voss, E.W.2
  • 24
    • 34247644884 scopus 로고    scopus 로고
    • Metal affinity-based purification of a red fluorescent protein
    • Rahimi, Y. (2007) Metal affinity-based purification of a red fluorescent protein. Chromatographia 65, 1612-1112.
    • (2007) Chromatographia , vol.65 , pp. 1612-1112
    • Rahimi, Y.1
  • 26
    • 33749075329 scopus 로고    scopus 로고
    • Anthozoa red fluorescent protein in biosensing
    • Shrestha, S., and Deo, S. K. (2006) Anthozoa red fluorescent protein in biosensing. Anal. Bioanal. Chem. 386, 515-24.
    • (2006) Anal. Bioanal. Chem , vol.386 , pp. 515-524
    • Shrestha, S.1    Deo, S.K.2
  • 28
    • 56749104366 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of non-natural variants of DsRed-monomer
    • in press
    • Goulding, A. M., Hunt, E. A., Shrestha, S., Dria, K., and Deo, S. K. (2008) Biochemical and spectroscopic characterization of non-natural variants of DsRed-monomer. Protein Eng. Des. Sel., in press.
    • (2008) Protein Eng. Des. Sel
    • Goulding, A.M.1    Hunt, E.A.2    Shrestha, S.3    Dria, K.4    Deo, S.K.5
  • 30
    • 0026750290 scopus 로고
    • The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains
    • Trewhella, J. (1992) The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains. Cell Calcium 13, 377-90.
    • (1992) Cell Calcium , vol.13 , pp. 377-390
    • Trewhella, J.1
  • 33
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • Babu, Y. S., Bugg, C. E., and Cook, W. J. (1988) Structure of calmodulin refined at 2.2 A resolution. J. Mol. Biol. 204, 191-204.
    • (1988) J. Mol. Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 34
    • 0036859953 scopus 로고    scopus 로고
    • Class-selective drug detection: Fluorescently-labeled calmodulin as the biorecognition element for phenothiazines and tricyclic antidepressants
    • Douglass, P. M., Salins, L. L., Dikici, E., and Daunert, S. (2002) Class-selective drug detection: fluorescently-labeled calmodulin as the biorecognition element for phenothiazines and tricyclic antidepressants. Bioconjugate Chem. 13, 1186-92.
    • (2002) Bioconjugate Chem , vol.13 , pp. 1186-1192
    • Douglass, P.M.1    Salins, L.L.2    Dikici, E.3    Daunert, S.4
  • 35
    • 0344413682 scopus 로고    scopus 로고
    • Drug detection based on the conformational changes of calmodulin and the fluorescence of its enhanced green fluorescent protein fusion partner
    • Dikici, E., Deo, S. K., and Daunert, S. (2003) Drug detection based on the conformational changes of calmodulin and the fluorescence of its enhanced green fluorescent protein fusion partner. Anal. Chim. Acta 500, 237-245.
    • (2003) Anal. Chim. Acta , vol.500 , pp. 237-245
    • Dikici, E.1    Deo, S.K.2    Daunert, S.3
  • 36
    • 0030726112 scopus 로고    scopus 로고
    • Rational design of a calcium sensing system based on induced conformational changes of calmodulin
    • Schauer-Vukasinovic, V., Cullen, L., and Daunert, S. (1997) Rational design of a calcium sensing system based on induced conformational changes of calmodulin. J. Am. Chem. Soc. 1119, 11102-11103.
    • (1997) J. Am. Chem. Soc , vol.1119 , pp. 11102-11103
    • Schauer-Vukasinovic, V.1    Cullen, L.2    Daunert, S.3
  • 37
    • 23044495862 scopus 로고    scopus 로고
    • Comparison of negative and positive ion electrospray ionization mass spectra of calmodulin and its complex with trifluoperazine
    • Watt, S. J., Oakley, A., Sheil, M. M., and Beck, J. L. (2005) Comparison of negative and positive ion electrospray ionization mass spectra of calmodulin and its complex with trifluoperazine. Rapid Commun. Mass Spectrom. 19, 2123-30.
    • (2005) Rapid Commun. Mass Spectrom , vol.19 , pp. 2123-2130
    • Watt, S.J.1    Oakley, A.2    Sheil, M.M.3    Beck, J.L.4
  • 39
    • 0035684295 scopus 로고    scopus 로고
    • Increase of bradykinin in plasma of patients undergoing cardiopulmonary bypass: The importance of lung exclusion
    • Cugno, M., Nussberger, J., Biglioli, P., Alamanni, F., Coppola, R., and Agostoni, A. (2001) Increase of bradykinin in plasma of patients undergoing cardiopulmonary bypass: the importance of lung exclusion. Chest 120, 1776-82.
    • (2001) Chest , vol.120 , pp. 1776-1782
    • Cugno, M.1    Nussberger, J.2    Biglioli, P.3    Alamanni, F.4    Coppola, R.5    Agostoni, A.6
  • 40
    • 0028287748 scopus 로고
    • Development of digoxigenin-labeled peptide: Application to chemiluminoenzyme immunoassay of bradykinin in inflamed tissues
    • Decarie, A., Drapeau, G., Closset, J., Couture, R., and Adam, A. (1994) Development of digoxigenin-labeled peptide: application to chemiluminoenzyme immunoassay of bradykinin in inflamed tissues. Peptides 15, 511-8.
    • (1994) Peptides , vol.15 , pp. 511-518
    • Decarie, A.1    Drapeau, G.2    Closset, J.3    Couture, R.4    Adam, A.5
  • 41
    • 0022958154 scopus 로고
    • Determination of bradykinin by enzyme immunoassay
    • Geiger, R., and Miska, W. (1986) Determination of bradykinin by enzyme immunoassay. Adv. Exp. Med. Biol. 198, 531-6.
    • (1986) Adv. Exp. Med. Biol , vol.198 , pp. 531-536
    • Geiger, R.1    Miska, W.2
  • 42
    • 0019426650 scopus 로고
    • Enzyme immunoassay of bradykinin using β-D-galactosidase as a labeling enzyme
    • Ueno, A., Oh-ishi, S., Kitagawa, T., and Katori, M. (1981) Enzyme immunoassay of bradykinin using β-D-galactosidase as a labeling enzyme. Biochem. Pharmacol. 30, 1659-64.
    • (1981) Biochem. Pharmacol , vol.30 , pp. 1659-1664
    • Ueno, A.1    Oh-ishi, S.2    Kitagawa, T.3    Katori, M.4
  • 43
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird, G. S., Zacharias, D. A., and Tsien, R. Y. (1999) Circular permutation and receptor insertion within green fluorescent proteins. Proc. Natl. Acad. Sci. U.S.A. 96, 11241-6.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 44
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • Miyawaki, A., Llopis, J., Heim, R., McCaffery, J. M., Adams, J. A., Ikura, M., and Tsien, R. Y. (1997) Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature 388, 882-7.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5    Ikura, M.6    Tsien, R.Y.7
  • 45
    • 33746879628 scopus 로고    scopus 로고
    • Single-cell resolution imaging of membrane-anchored hepatitis C virus NS3/4A protease activity
    • Martin, M. M., and Jean, F. (2006) Single-cell resolution imaging of membrane-anchored hepatitis C virus NS3/4A protease activity. Biol. Chem. 387, 1075-80.
    • (2006) Biol. Chem , vol.387 , pp. 1075-1080
    • Martin, M.M.1    Jean, F.2
  • 46
    • 38949084579 scopus 로고    scopus 로고
    • Using green and red fluorescent proteins to teach protein expression, purification, and crystallization
    • Wu Y., Z. Y., Song, J., Hu, X., Ding, Y., and Zhang, Z. (2008) Using green and red fluorescent proteins to teach protein expression, purification, and crystallization. Biochem. Mol. Biol. Educ. 36, 43-54.
    • (2008) Biochem. Mol. Biol. Educ , vol.36 , pp. 43-54
    • Wu, Y.Z.Y.1    Song, J.2    Hu, X.3    Ding, Y.4    Zhang, Z.5
  • 47
    • 33846143832 scopus 로고    scopus 로고
    • In vivo dynamics of enterovirus protease revealed by fluorescence resonance emission transfer (FRET) based on a novel FRET pair
    • Hsu, Y. Y., Liu, Y. N., Wang, W., Kao, F. J., and Kung, S. H. (2007) In vivo dynamics of enterovirus protease revealed by fluorescence resonance emission transfer (FRET) based on a novel FRET pair. Biochem. Biophys. Res. Commun. 353, 939-45.
    • (2007) Biochem. Biophys. Res. Commun , vol.353 , pp. 939-945
    • Hsu, Y.Y.1    Liu, Y.N.2    Wang, W.3    Kao, F.J.4    Kung, S.H.5
  • 48
    • 0037125999 scopus 로고    scopus 로고
    • A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins
    • Kohl, T., Heinze, K. G., Kuhlemann, R., Koltermann, A., and Schwille, P. (2002) A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins. Proc. Natl. Acad Sci. U.S.A. 99, 12161-6.
    • (2002) Proc. Natl. Acad Sci. U.S.A , vol.99 , pp. 12161-12166
    • Kohl, T.1    Heinze, K.G.2    Kuhlemann, R.3    Koltermann, A.4    Schwille, P.5
  • 49
    • 0035957110 scopus 로고    scopus 로고
    • Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer
    • Mizuno, H., Sawano, A., Eli, P., Hama, H., and Miyawaki, A. (2001) Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry 40, 2502-10.
    • (2001) Biochemistry , vol.40 , pp. 2502-2510
    • Mizuno, H.1    Sawano, A.2    Eli, P.3    Hama, H.4    Miyawaki, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.