메뉴 건너뛰기




Volumn 389, Issue 4, 2009, Pages 563-568

Multiply mutated Gaussia luciferases provide prolonged and intense bioluminescence

Author keywords

Bioconjugation; Bioluminescence kinetics; Cell free protein synthesis; Gaussia luciferase; Non natural amino acids

Indexed keywords

AMINO ACID; AZIDE; GLYCINE; HOMOPROPARGLYGLYCINE; LUCIFERASE; UNCLASSIFIED DRUG;

EID: 70349751620     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.09.006     Document Type: Article
Times cited : (77)

References (29)
  • 1
    • 0036793192 scopus 로고    scopus 로고
    • It's not just about anatomy: in vivo bioluminescence imaging as an eyepiece into biology
    • Contag C.H., and Ross B.D. It's not just about anatomy: in vivo bioluminescence imaging as an eyepiece into biology. J. Magn. Reson. Imaging 16 (2002) 378-387
    • (2002) J. Magn. Reson. Imaging , vol.16 , pp. 378-387
    • Contag, C.H.1    Ross, B.D.2
  • 2
    • 41049117394 scopus 로고    scopus 로고
    • Applications of bioluminescence imaging to antiviral research and therapy: multiple luciferase enzymes and quantitation
    • Luker K.E., and Luker G.D. Applications of bioluminescence imaging to antiviral research and therapy: multiple luciferase enzymes and quantitation. Antiviral Res. 78 (2008) 179-187
    • (2008) Antiviral Res. , vol.78 , pp. 179-187
    • Luker, K.E.1    Luker, G.D.2
  • 3
    • 14044250981 scopus 로고    scopus 로고
    • Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo
    • Tannous B.A., Kim D.E., Fernandez J.L., Weissleder R., and Breakefield X.O. Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo. Mol. Ther. 11 (2005) 435-443
    • (2005) Mol. Ther. , vol.11 , pp. 435-443
    • Tannous, B.A.1    Kim, D.E.2    Fernandez, J.L.3    Weissleder, R.4    Breakefield, X.O.5
  • 4
    • 35348813658 scopus 로고    scopus 로고
    • Current state of imaging protein-protein interactions in vivo with genetically encoded reporters
    • Villalobos V., Naik S., and Piwnica-Worms D. Current state of imaging protein-protein interactions in vivo with genetically encoded reporters. Annu. Rev. Biomed. Eng. 9 (2007) 321-349
    • (2007) Annu. Rev. Biomed. Eng. , vol.9 , pp. 321-349
    • Villalobos, V.1    Naik, S.2    Piwnica-Worms, D.3
  • 6
    • 38949203326 scopus 로고    scopus 로고
    • Monitoring thiocyanate-degrading microbial community in relation to changes in process performance in mixed culture systems near washout
    • Lee C., Kim J., Do H., and Hwang S. Monitoring thiocyanate-degrading microbial community in relation to changes in process performance in mixed culture systems near washout. Water Res. 42 (2008) 1254-1262
    • (2008) Water Res. , vol.42 , pp. 1254-1262
    • Lee, C.1    Kim, J.2    Do, H.3    Hwang, S.4
  • 7
    • 0037039437 scopus 로고    scopus 로고
    • Optical imaging of Renilla luciferase reporter gene expression in living mice
    • Bhaumik S., and Gambhir S.S. Optical imaging of Renilla luciferase reporter gene expression in living mice. Proc. Natl. Acad. Sci. USA 99 (2002) 377-382
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 377-382
    • Bhaumik, S.1    Gambhir, S.S.2
  • 8
    • 0008380298 scopus 로고
    • Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli
    • de Wet J.R., Wood K.V., Helinski D.R., and DeLuca M. Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proc. Natl. Acad. Sci. USA 82 (1985) 7870-7873
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7870-7873
    • de Wet, J.R.1    Wood, K.V.2    Helinski, D.R.3    DeLuca, M.4
  • 9
    • 39049098131 scopus 로고    scopus 로고
    • Firefly luminescence: a historical perspective and recent developments
    • Fraga H. Firefly luminescence: a historical perspective and recent developments. Photochem. Photobiol. Sci. 7 (2008) 146-158
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 146-158
    • Fraga, H.1
  • 11
    • 44849130688 scopus 로고    scopus 로고
    • Cell-free metabolic engineering promotes high-level production of bioactive Gaussia princeps luciferase
    • Goerke A.R., Loening A.M., Gambhir S.S., and Swartz J.R. Cell-free metabolic engineering promotes high-level production of bioactive Gaussia princeps luciferase. Metab. Eng. 10 (2008) 187-200
    • (2008) Metab. Eng. , vol.10 , pp. 187-200
    • Goerke, A.R.1    Loening, A.M.2    Gambhir, S.S.3    Swartz, J.R.4
  • 12
    • 34548155475 scopus 로고    scopus 로고
    • Fusion of Gaussia luciferase to an engineered anti-carcinoembryonic antigen (CEA) antibody for in vivo optical imaging
    • Venisnik K.M., Olafsen T., Gambhir S.S., and Wu A.M. Fusion of Gaussia luciferase to an engineered anti-carcinoembryonic antigen (CEA) antibody for in vivo optical imaging. Mol. Imaging Biol. 9 (2007) 267-277
    • (2007) Mol. Imaging Biol. , vol.9 , pp. 267-277
    • Venisnik, K.M.1    Olafsen, T.2    Gambhir, S.S.3    Wu, A.M.4
  • 14
    • 43049142194 scopus 로고    scopus 로고
    • High yield cell-free production of integral membrane proteins without refolding or detergents
    • Wuu J.J., and Swartz J.R. High yield cell-free production of integral membrane proteins without refolding or detergents. Biochim. Biophys. Acta 1778 (2008) 1237-1250
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1237-1250
    • Wuu, J.J.1    Swartz, J.R.2
  • 15
    • 42549090557 scopus 로고    scopus 로고
    • Escherichia coli-based cell-free synthesis of virus-like particles
    • Bundy B.C., Franciszkowicz M.J., and Swartz J.R. Escherichia coli-based cell-free synthesis of virus-like particles. Biotechnol. Bioeng. 100 (2008) 28-37
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 28-37
    • Bundy, B.C.1    Franciszkowicz, M.J.2    Swartz, J.R.3
  • 17
    • 13944257292 scopus 로고    scopus 로고
    • In vivo incorporation of an alkyne into proteins in Escherichia coli
    • Deiters A., and Schultz P.G. In vivo incorporation of an alkyne into proteins in Escherichia coli. Bioorg. Med. Chem. Lett. 15 (2005) 1521-1524
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 1521-1524
    • Deiters, A.1    Schultz, P.G.2
  • 20
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett M.C., and Swartz J.R. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol. Bioeng. 86 (2004) 19-26
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 21
    • 0942286940 scopus 로고    scopus 로고
    • Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli
    • Kim D.M., and Swartz J.R. Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli. Biotechnol. Bioeng. 85 (2004) 122-129
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 122-129
    • Kim, D.M.1    Swartz, J.R.2
  • 22
    • 1542538048 scopus 로고    scopus 로고
    • Enhancing multiple disulfide bonded protein folding in a cell-free system
    • Yin G., and Swartz J.R. Enhancing multiple disulfide bonded protein folding in a cell-free system. Biotechnol. Bioeng. 86 (2004) 188-195
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 188-195
    • Yin, G.1    Swartz, J.R.2
  • 23
    • 38449099301 scopus 로고    scopus 로고
    • Development of cell-free protein synthesis platforms for disulfide bonded proteins
    • Goerke A.R., and Swartz J.R. Development of cell-free protein synthesis platforms for disulfide bonded proteins. Biotechnol. Bioeng. 99 (2008) 351-367
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 351-367
    • Goerke, A.R.1    Swartz, J.R.2
  • 24
    • 23244440886 scopus 로고    scopus 로고
    • An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
    • Calhoun K.A., and Swartz J.R. An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol. Prog. 21 (2005) 1146-1153
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1146-1153
    • Calhoun, K.A.1    Swartz, J.R.2
  • 25
    • 0033946807 scopus 로고    scopus 로고
    • Absolute calibration of luminometers with low-level light standards
    • O'Kane D.J., and Lee J. Absolute calibration of luminometers with low-level light standards. Methods Enzymol. 305 (2000) 87-96
    • (2000) Methods Enzymol. , vol.305 , pp. 87-96
    • O'Kane, D.J.1    Lee, J.2
  • 26
    • 3242811187 scopus 로고    scopus 로고
    • A fluorogenic probe for the copper(I)-catalyzed azide-alkyne ligation reaction: modulation of the fluorescence emission via 3(n, pi)-1(pi, pi) inversion
    • Zhou Z., and Fahrni C.J. A fluorogenic probe for the copper(I)-catalyzed azide-alkyne ligation reaction: modulation of the fluorescence emission via 3(n, pi)-1(pi, pi) inversion. J. Am. Chem. Soc. 126 (2004) 8862-8863
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8862-8863
    • Zhou, Z.1    Fahrni, C.J.2
  • 27
    • 36048997217 scopus 로고    scopus 로고
    • Identification of two catalytic domains in a luciferase secreted by the copepod Gaussia princeps
    • Inouye S., and Sahara Y. Identification of two catalytic domains in a luciferase secreted by the copepod Gaussia princeps. Biochem. Biophys. Res. Commun. 365 (2008) 96-101
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 96-101
    • Inouye, S.1    Sahara, Y.2
  • 28
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 29
    • 0017761354 scopus 로고
    • Substrate and substrate analogue binding properties of Renilla luciferase
    • Matthews J.C., Hori K., and Cormier M.J. Substrate and substrate analogue binding properties of Renilla luciferase. Biochemistry 16 (1977) 5217-5220
    • (1977) Biochemistry , vol.16 , pp. 5217-5220
    • Matthews, J.C.1    Hori, K.2    Cormier, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.