메뉴 건너뛰기




Volumn 40, Issue 3, 2006, Pages 355-367

Calcium-regulated photoproteins of marine coelenterates

Author keywords

Aequorin; Bioluminescence; Intracellular calcium; Molecular diagnosis; Obelin

Indexed keywords

COELENTERATA;

EID: 33747616483     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893306030022     Document Type: Review
Times cited : (35)

References (100)
  • 2
    • 34548576414 scopus 로고
    • Extraction, purification, and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O., Johnson F.H., Saiga Y. 1962. Extraction, purification, and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 59, 223-239.
    • (1962) J. Cell. Comp. Physiol. , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 3
    • 2042424647 scopus 로고
    • Extraction and properties of halistaurin, a bioluminescent protein from the hydromedusan, Halistaura
    • Shimomura O., Johnson F.H., Saiga Y. 1963. Extraction and properties of halistaurin, a bioluminescent protein from the hydromedusan, Halistaura. J. Cell. Comp. Physiol. 62, 9-15.
    • (1963) J. Cell. Comp. Physiol. , vol.62 , pp. 9-15
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 4
    • 0001919850 scopus 로고
    • Isolation and characterization of a photoprotein, "phialidin," and a spectrally unique green-fluorescent protein from the bioluminescent jellyfish Phialidium gregarium
    • Levine L.D., Ward W.W. 1982. Isolation and characterization of a photoprotein, "phialidin," and a spectrally unique green-fluorescent protein from the bioluminescent jellyfish Phialidium gregarium. Comp. Biochem. Physiol. 72B, 77-85.
    • (1982) Comp. Biochem. Physiol. , vol.72 B , pp. 77-85
    • Levine, L.D.1    Ward, W.W.2
  • 5
    • 0016293814 scopus 로고
    • Extraction, partial purification, and properties of obelin, the calcium-activated luminescent protein from hydroid Obelia geniculata
    • Campbell A.K. 1974. Extraction, partial purification, and properties of obelin, the calcium-activated luminescent protein from hydroid Obelia geniculata. Biochem. J. 143, 411-418.
    • (1974) Biochem. J. , vol.143 , pp. 411-418
    • Campbell, A.K.1
  • 8
    • 0041553754 scopus 로고
    • Physicochemical properties of obelin, photoprotein from the hydroid Obelia longissima
    • Bondar V.S., Trofimov K.P., Vysotski E.S. 1992. Physicochemical properties of obelin, photoprotein from the hydroid Obelia longissima. Biokhimiya. 57, 1481-1490.
    • (1992) Biokhimiya , vol.57 , pp. 1481-1490
    • Bondar, V.S.1    Trofimov, K.P.2    Vysotski, E.S.3
  • 9
    • 0015958207 scopus 로고
    • Extraction and purification of calcium-activated photoproteins from the ctenophores Mnemiopsis sp. and Beroe ovata
    • Ward W.W., Seliger H.H. 1974. Extraction and purification of calcium-activated photoproteins from the ctenophores Mnemiopsis sp. and Beroe ovata. Biochemistry. 13, 1491-1499.
    • (1974) Biochemistry , vol.13 , pp. 1491-1499
    • Ward, W.W.1    Seliger, H.H.2
  • 11
    • 0027464064 scopus 로고
    • 2+-activated photoprotein, clytin
    • 2+-activated photoprotein, clytin. FEBS Lett. 315, 343-346.
    • (1993) FEBS Lett. , vol.315 , pp. 343-346
    • Inouye, S.1    Tsuji, F.I.2
  • 13
    • 0008471011 scopus 로고
    • Cloning end expression of cDNA for obelin, calcium-activated photoprotein from the hydroid Obelia longissima
    • Illarionov B.A., Markova S.V., Bondar V.S.,Vysotski E.S., Gitelzon I.I. 1992. Cloning end expression of cDNA for obelin, calcium-activated photoprotein from the hydroid Obelia longissima. Dokl. Akad. Nauk. 326, 911-913.
    • (1992) Dokl. Akad. Nauk. , vol.326 , pp. 911-913
    • Illarionov, B.A.1    Markova, S.V.2    Bondar, V.S.3    Vysotski, E.S.4    Gitelzon, I.I.5
  • 16
    • 0025311949 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins: I. Relationships based on amino acid sequences
    • Moncrief N.D., Kretsinger R.H., Goodman M. 1990. Evolution of EF-hand calcium-modulated proteins: I. Relationships based on amino acid sequences. J. Mol. Evol. 30, 522-562.
    • (1990) J. Mol. Evol. , vol.30 , pp. 522-562
    • Moncrief, N.D.1    Kretsinger, R.H.2    Goodman, M.3
  • 19
    • 0028939743 scopus 로고
    • Cause of spectral variation in the luminescence of semisynthetic aequorins
    • Shimomura O. 1995. Cause of spectral variation in the luminescence of semisynthetic aequorins. Biochem. J. 306, 537-543.
    • (1995) Biochem. J. , vol.306 , pp. 537-543
    • Shimomura, O.1
  • 21
    • 0029027663 scopus 로고
    • Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution
    • Fisher A.J., Raushel F.M., Baldwin T.O., Rayment I. 1995. Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution. Biochemistry. 34, 6581-6586.
    • (1995) Biochemistry , vol.34 , pp. 6581-6586
    • Fisher, A.J.1    Raushel, F.M.2    Baldwin, T.O.3    Rayment, I.4
  • 22
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti E., Franks N.P., Brick P. 1996. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure. 4, 287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 23
    • 13444252278 scopus 로고    scopus 로고
    • Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole
    • Schultz L.W., Liu L., Cegielski M., Hastings J.W. 2005. Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole. Proc. Natl. Acad. Sci. USA. 102, 1378-1383.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1378-1383
    • Schultz, L.W.1    Liu, L.2    Cegielski, M.3    Hastings, J.W.4
  • 24
    • 0034682381 scopus 로고    scopus 로고
    • The crystal structure of the photoprotein aequorin at 2.3 angstrom resolution
    • Head J.F., Inouye S., Teranishi K., Shimomura O. 2000. The crystal structure of the photoprotein aequorin at 2.3 angstrom resolution. Nature. 405, 372-376.
    • (2000) Nature , vol.405 , pp. 372-376
    • Head, J.F.1    Inouye, S.2    Teranishi, K.3    Shimomura, O.4
  • 26
    • 0242362820 scopus 로고    scopus 로고
    • Atomic resolution structure of obelin: Soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine
    • Liu Z.J., Vysotski E.S., Deng L., Lee J., Rose J., Wang B.C. 2003. Atomic resolution structure of obelin: Soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine. Biochem. Biophys. Res. Commun. 311, 433-439.
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 433-439
    • Liu, Z.J.1    Vysotski, E.S.2    Deng, L.3    Lee, J.4    Rose, J.5    Wang, B.C.6
  • 29
    • 0026504431 scopus 로고
    • Two excited states in aequorin bioluminescence induced by tryptophan modification
    • Ohmiya Y., Ohashi M., Tsuji F.I. 1992. Two excited states in aequorin bioluminescence induced by tryptophan modification. FEBS Lett. 301, 197-201.
    • (1992) FEBS Lett. , vol.301 , pp. 197-201
    • Ohmiya, Y.1    Ohashi, M.2    Tsuji, F.I.3
  • 30
    • 0027447252 scopus 로고
    • 2+-binding photoprotein, aequorin, after histidine modification
    • 2+- binding photoprotein, aequorin, after histidine modification. FEBS Lett. 320, 267-270.
    • (1993) FEBS Lett. , vol.320 , pp. 267-270
    • Ohmiya, Y.1    Tsuji, F.I.2
  • 33
    • 0038522532 scopus 로고    scopus 로고
    • Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species
    • Vysotski E.S., Liu Z.J., Markova S.V., Blinks J.R., Deng L., Frank L.A., Herko M., Malikova N.P., Rose J.P., Wang B.C., Lee J. 2003. Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species. Biochemistry. 42, 6013-6024.
    • (2003) Biochemistry , vol.42 , pp. 6013-6024
    • Vysotski, E.S.1    Liu, Z.J.2    Markova, S.V.3    Blinks, J.R.4    Deng, L.5    Frank, L.A.6    Herko, M.7    Malikova, N.P.8    Rose, J.P.9    Wang, B.C.10    Lee, J.11
  • 34
    • 37049125208 scopus 로고
    • The chemiluminescence of a Cypridina luciferin analogue
    • McCapra F., Chang Y.C. 1967. The chemiluminescence of a Cypridina luciferin analogue. Chem. Commun. 19, 1011-1012.
    • (1967) Chem. Commun. , vol.19 , pp. 1011-1012
    • McCapra, F.1    Chang, Y.C.2
  • 35
    • 0030576862 scopus 로고    scopus 로고
    • Low-temperature photooxygenation of coelenterate luciferin analog synthesis and proof of 1.2-dioxetanone as luminescence intermediate
    • Usami K., Isobe M. 1996. Low-temperature photooxygenation of coelenterate luciferin analog synthesis and proof of 1.2-dioxetanone as luminescence intermediate. Tetrahedron. 52, 12061-12090.
    • (1996) Tetrahedron , vol.52 , pp. 12061-12090
    • Usami, K.1    Isobe, M.2
  • 36
    • 0033631829 scopus 로고    scopus 로고
    • Light-emitters involved in the luminescence of coelenterazine
    • Shimomura O., Teranishi K. 2000. Light-emitters involved in the luminescence of coelenterazine. Luminescence. 15, 51-58.
    • (2000) Luminescence , vol.15 , pp. 51-58
    • Shimomura, O.1    Teranishi, K.2
  • 37
    • 0037798055 scopus 로고    scopus 로고
    • Fluorescence properties of phenolate anions of coelenteramide analogues: The light-emitter structure in aequorin bioluminescence
    • Imai Y., Shibata T., Maki S., Niwa H., Ohashi M., Hirano T. 2001. Fluorescence properties of phenolate anions of coelenteramide analogues: The light-emitter structure in aequorin bioluminescence. Photochem. Photobiol. A: Chemistry. 146, 95-107.
    • (2001) Photochem. Photobiol. A: Chemistry , vol.146 , pp. 95-107
    • Imai, Y.1    Shibata, T.2    Maki, S.3    Niwa, H.4    Ohashi, M.5    Hirano, T.6
  • 38
    • 2942659225 scopus 로고    scopus 로고
    • 2+-regulated photoproteins: Structural insight into the bioluminescence mechanism
    • 2+-regulated photoproteins: Structural insight into the bioluminescence mechanism. Acc. Chem. Res. 37, 405-415.
    • (2004) Acc. Chem. Res. , vol.37 , pp. 405-415
    • Vysotski, E.S.1    Lee, J.2
  • 39
    • 0017334141 scopus 로고
    • Aequorin luminescence: Relation of light emission to calcium concentration - A calcium-independent component
    • Allen D.G., Blinks J.R., Prendergast F.G. 1977. Aequorin luminescence: Relation of light emission to calcium concentration - a calcium-independent component. Science. 195, 996-998.
    • (1977) Science , vol.195 , pp. 996-998
    • Allen, D.G.1    Blinks, J.R.2    Prendergast, F.G.3
  • 42
    • 13844278292 scopus 로고    scopus 로고
    • Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein
    • Stepanyuk G.A., Golz S., Markova S.V., Frank L.A., Lee J., Vysotski E.S. 2005. Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein. FEBS Lett. 579, 1008-1014.
    • (2005) FEBS Lett. , vol.579 , pp. 1008-1014
    • Stepanyuk, G.A.1    Golz, S.2    Markova, S.V.3    Frank, L.A.4    Lee, J.5    Vysotski, E.S.6
  • 45
    • 33747602294 scopus 로고
    • Isolation, properties, and applications of a calcium-sensitive photoprotein from the hydroid Obelia longissima
    • Bondar V.S., Vysotski E.S., Gamaley I.A., Kaulin A.B. 1990. Isolation, properties, and applications of a calcium-sensitive photoprotein from the hydroid Obelia longissima. Tsitologiya. 33, 57-66.
    • (1990) Tsitologiya , vol.33 , pp. 57-66
    • Bondar, V.S.1    Vysotski, E.S.2    Gamaley, I.A.3    Kaulin, A.B.4
  • 46
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures
    • Tsien R.Y. 1980. New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures. Biochemistry. 19, 2396-2404.
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 49
    • 23244444654 scopus 로고    scopus 로고
    • A new short-term toxicity assay using Aspergillus awamori with recombinant aequorin gene
    • Kozlova O., Zwinderman M., Christofi N. 2005. A new short-term toxicity assay using Aspergillus awamori with recombinant aequorin gene. BMC Microbiol. 5, 40.
    • (2005) BMC Microbiol. , vol.5 , pp. 40
    • Kozlova, O.1    Zwinderman, M.2    Christofi, N.3
  • 50
    • 0036451532 scopus 로고    scopus 로고
    • Aequorin-based functional assays for G-protein-coupled receptors, ion channels, and tyrosine kinase receptors
    • Dupriez V.J., Maes K., Le Poul E., Burgeon E., Detheux M. 2002. Aequorin-based functional assays for G-protein-coupled receptors, ion channels, and tyrosine kinase receptors. Receptors Channels. 8, 319-330.
    • (2002) Receptors Channels , vol.8 , pp. 319-330
    • Dupriez, V.J.1    Maes, K.2    Le Poul, E.3    Burgeon, E.4    Detheux, M.5
  • 52
    • 0024336003 scopus 로고
    • Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
    • Minta A., Kao J.P., Tsien R.Y. 1989. Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores. J. Biol. Chem. 264, 8171-8178.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8171-8178
    • Minta, A.1    Kao, J.P.2    Tsien, R.Y.3
  • 54
    • 0032514917 scopus 로고    scopus 로고
    • Direct monitoring of the calcium concentration in the sarcoplasmic and endoplasmic reticulum of skeletal muscle myotubes
    • Robert V., De Georgi F., Massimino M.L., Cantini M., Pozzan T. 1998. Direct monitoring of the calcium concentration in the sarcoplasmic and endoplasmic reticulum of skeletal muscle myotubes. J. Biol. Chem. 273, 30372-30378.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30372-30378
    • Robert, V.1    De Georgi, F.2    Massimino, M.L.3    Cantini, M.4    Pozzan, T.5
  • 55
    • 0033921091 scopus 로고    scopus 로고
    • Recombinant obelin: Cloning and expression of cDNA, purification and characterization as a calcium indicator
    • Illarionov B.A., Frank L.A., Illarionova V.A., Bondar V.S., Vysotski E.S., Blinks J.R. 2000. Recombinant obelin: Cloning and expression of cDNA, purification and characterization as a calcium indicator. Meth. Enzymol. 227, 223-249.
    • (2000) Meth. Enzymol. , vol.227 , pp. 223-249
    • Illarionov, B.A.1    Frank, L.A.2    Illarionova, V.A.3    Bondar, V.S.4    Vysotski, E.S.5    Blinks, J.R.6
  • 57
    • 0027233662 scopus 로고
    • Light-emitting properties of recombinant semi-synthetic aequorins and recombinant fluorescein-conjugated aequorin for measuring cellular calcium
    • Shimomura O., Musicki B., Kishi Y., Inouye S. 1993. Light-emitting properties of recombinant semi-synthetic aequorins and recombinant fluorescein-conjugated aequorin for measuring cellular calcium. Cell Calcium. 14, 373-378.
    • (1993) Cell Calcium , vol.14 , pp. 373-378
    • Shimomura, O.1    Musicki, B.2    Kishi, Y.3    Inouye, S.4
  • 63
    • 17644424638 scopus 로고    scopus 로고
    • CcbP, a calcium-binding protein from Anabaena sp. PCC 7120, provides evidence that calcium ions regulate heterocyst differentiation
    • Zhao Y., Shi Y., Zhao W., Huang X., Wang D., Brown N., Brand J., Zhao J. 2005. CcbP, a calcium-binding protein from Anabaena sp. PCC 7120, provides evidence that calcium ions regulate heterocyst differentiation. Proc. Natl. Acad. Sci. USA. 102, 5744-5748.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5744-5748
    • Zhao, Y.1    Shi, Y.2    Zhao, W.3    Huang, X.4    Wang, D.5    Brown, N.6    Brand, J.7    Zhao, J.8
  • 64
    • 0026552942 scopus 로고
    • Use of recombinant biotinylated aequorin in microtiter and membrane-based assays: Purification of recombinant apoaequorin from Escherichia coli
    • Stults N.L., Stocks H.N., Rivera H., Cray J., McCann R. O., O'Kane D., Cummings R.D., Cormier M.J., Smith D.F. 1992. Use of recombinant biotinylated aequorin in microtiter and membrane-based assays: Purification of recombinant apoaequorin from Escherichia coli. Biochemistry. 31, 1433-1442.
    • (1992) Biochemistry , vol.31 , pp. 1433-1442
    • Stults, N.L.1    Stocks, H.N.2    Rivera, H.3    Cray, J.4    McCann, R.O.5    O'Kane, D.6    Cummings, R.D.7    Cormier, M.J.8    Smith, D.F.9
  • 66
    • 0034073753 scopus 로고    scopus 로고
    • Site-specifically labeled photoprotein-thyroxine conjugates using aequorin mutants containing unique cysteine residues: Application for binding assays (part II)
    • Lewis J.C., Cullen L.C., Daunert S. 2000. Site-specifically labeled photoprotein-thyroxine conjugates using aequorin mutants containing unique cysteine residues: application for binding assays (part II). Bioconjug. Chem. 11, 140-145.
    • (2000) Bioconjug. Chem. , vol.11 , pp. 140-145
    • Lewis, J.C.1    Cullen, L.C.2    Daunert, S.3
  • 67
    • 0037099632 scopus 로고    scopus 로고
    • Bioluminescence immunoassay for cortisol using recombinant aequorin as a label
    • Mirasoli M., Deo S.K., Lewis J.C., Roda A., Daunert S. 2002. Bioluminescence immunoassay for cortisol using recombinant aequorin as a label. Anal. Biochem. 306, 204-211.
    • (2002) Anal. Biochem. , vol.306 , pp. 204-211
    • Mirasoli, M.1    Deo, S.K.2    Lewis, J.C.3    Roda, A.4    Daunert, S.5
  • 68
    • 0036683163 scopus 로고    scopus 로고
    • Determination of prostacyclin in plasma through a bioluminescent immunoassay for 6-keto-prostaglandin F1alpha: Implication of dosage in patients with primary pulmonary hypertension
    • Desai U.A., Deo S.K., Hyland K.V., Poon M., Daunert S. 2002. Determination of prostacyclin in plasma through a bioluminescent immunoassay for 6-keto-prostaglandin F1alpha: Implication of dosage in patients with primary pulmonary hypertension. Anal. Chem. 74, 3892-3898.
    • (2002) Anal. Chem. , vol.74 , pp. 3892-3898
    • Desai, U.A.1    Deo, S.K.2    Hyland, K.V.3    Poon, M.4    Daunert, S.5
  • 69
    • 1642578943 scopus 로고    scopus 로고
    • Bioluminescent immunoassay of thyrotropin and thyroxin using obelin as a label
    • Frank L.A., Petunin A.I., Vysotski E.C. 2004. Bioluminescent immunoassay of thyrotropin and thyroxin using obelin as a label. Anal. Biochem. 325, 240-246.
    • (2004) Anal. Biochem. , vol.325 , pp. 240-246
    • Frank, L.A.1    Petunin, A.I.2    Vysotski, E.C.3
  • 70
    • 28744451989 scopus 로고    scopus 로고
    • 2+-sensitive photoprotein obelin with immunoglobulins: Synthesis and applications as labels in immunochemical analysis
    • 2+-sensitive photoprotein obelin with immunoglobulins: Synthesis and applications as labels in immunochemical analysis. Bioorg. Khim. 30, 364-368.
    • (2004) Bioorg. Khim. , vol.30 , pp. 364-368
    • Frank, L.A.1    Petunin, A.I.2    Vysorski, E.S.3
  • 72
    • 0029986760 scopus 로고    scopus 로고
    • Luminometry: A novel bioluminescent immunoassay enhances the quantitation of mucosal and systematic antibody responses
    • Jackson R.J., Fujihashi K., Kiyono H., McGhee J.R. 1996. Luminometry: A novel bioluminescent immunoassay enhances the quantitation of mucosal and systematic antibody responses. J. Immunol. Methods. 190, 189-197.
    • (1996) J. Immunol. Methods. , vol.190 , pp. 189-197
    • Jackson, R.J.1    Fujihashi, K.2    Kiyono, H.3    McGhee, J.R.4
  • 73
    • 0025162392 scopus 로고
    • Bioluminescent immunoassay using a fusion protein of protein A and the photoprotein aequorin
    • Inouye S., Zenno S. 1990. Bioluminescent immunoassay using a fusion protein of protein A and the photoprotein aequorin. Biochem. Biophys. Res. Commun. 171, 169-174.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 169-174
    • Inouye, S.1    Zenno, S.2
  • 76
    • 0025228575 scopus 로고
    • Expression and secretion of aequorin as a chimeric antibody by means if a mammalian expression vector
    • Casadei J., Powel M.J., Kenten J.H. 1990. Expression and secretion of aequorin as a chimeric antibody by means if a mammalian expression vector. Proc. Natl. Acad. Sci. USA. 87, 2047-2051.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2047-2051
    • Casadei, J.1    Powel, M.J.2    Kenten, J.H.3
  • 77
    • 0035870163 scopus 로고    scopus 로고
    • An immunoassay for Leuenkephalin based on a C-terminal aequorin-peptide fusion
    • Deo S.K., Daunert S. 2001. An immunoassay for Leuenkephalin based on a C-terminal aequorin-peptide fusion. Anal. Chem. 73, 1903-1908.
    • (2001) Anal. Chem. , vol.73 , pp. 1903-1908
    • Deo, S.K.1    Daunert, S.2
  • 78
    • 0035012120 scopus 로고    scopus 로고
    • C-terminal and N-terminal fusions of aequorin with small peptides in immunoassay development
    • Deo S.K., Lewis J.C., Daunert S. 2001. C-terminal and N-terminal fusions of aequorin with small peptides in immunoassay development. Bioconjug. Chem. 12, 378-384.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 378-384
    • Deo, S.K.1    Lewis, J.C.2    Daunert, S.3
  • 80
    • 0037098939 scopus 로고    scopus 로고
    • Bacterial expression of in vivo-biotinylated aequorin for direct application to bioluminometric hybridization assays
    • Verhaegen M., Christopoulus T. 2002. Bacterial expression of in vivo-biotinylated aequorin for direct application to bioluminometric hybridization assays. Anal. Biochem. 306, 314-322.
    • (2002) Anal. Biochem. , vol.306 , pp. 314-322
    • Verhaegen, M.1    Christopoulus, T.2
  • 81
    • 0030589821 scopus 로고    scopus 로고
    • Quantitation of RT-PCR amplified cytokine mRNA by aequorin-based bioluminescence immunoassay
    • Xiao L., Chumfu Y., Nelson C.O., Holloway B.P., Udhayakumar V., Lal A.A. 1996. Quantitation of RT-PCR amplified cytokine mRNA by aequorin-based bioluminescence immunoassay. J. Immunol. Methods. 199, 139-147.
    • (1996) J. Immunol. Methods , vol.199 , pp. 139-147
    • Xiao, L.1    Chumfu, Y.2    Nelson, C.O.3    Holloway, B.P.4    Udhayakumar, V.5    Lal, A.A.6
  • 82
    • 0032004236 scopus 로고    scopus 로고
    • A flash-type bioluminescent immunoassay that is more sensitive than radioimaging: Quantitative detection of cytokine cDNA in activated and resting human cells
    • Actor J.K., Kuffner T., Dezzutti C.S., Hunter R.L., McNicholl J.M. 1998. A flash-type bioluminescent immunoassay that is more sensitive than radioimaging: quantitative detection of cytokine cDNA in activated and resting human cells. J. Immunol. Methods. 211, 65-67.
    • (1998) J. Immunol. Methods. , vol.211 , pp. 65-67
    • Actor, J.K.1    Kuffner, T.2    Dezzutti, C.S.3    Hunter, R.L.4    McNicholl, J.M.5
  • 83
    • 0031945655 scopus 로고    scopus 로고
    • Quantitative, competitive PCR assay for HIV-1 using a microplate-based detection system
    • Guenthner P.C., Hart C.E. 1998. Quantitative, competitive PCR assay for HIV-1 using a microplate-based detection system. Biotechniques. 24, 810-816.
    • (1998) Biotechniques , vol.24 , pp. 810-816
    • Guenthner, P.C.1    Hart, C.E.2
  • 84
    • 0032895682 scopus 로고    scopus 로고
    • A flexible bioluminescent-quantitative polymerase chain reaction assay for analysis of competitive PCR amplicons
    • Actor J.K., Limor J.R., Hunter R.L. 1999. A flexible bioluminescent- quantitative polymerase chain reaction assay for analysis of competitive PCR amplicons. J. Clin. Lab. Anal. 13, 40-47.
    • (1999) J. Clin. Lab. Anal. , vol.13 , pp. 40-47
    • Actor, J.K.1    Limor, J.R.2    Hunter, R.L.3
  • 85
    • 0033822545 scopus 로고    scopus 로고
    • Bioluminescent quantitation and detection of gene expression during infectious disease
    • Actor J.K. 2000. Bioluminescent quantitation and detection of gene expression during infectious disease. Comb. Chem. High Throughput Screen. 3, 277-288.
    • (2000) Comb. Chem. High Throughput Screen , vol.3 , pp. 277-288
    • Actor, J.K.1
  • 86
    • 0033831647 scopus 로고    scopus 로고
    • Quantitative and bioluminescent assay to measure efficacy of conventional and DNA vaccinations against Helicobacter pylory
    • Ozpolat B., Rao X.M., Lachman L.B., Osato M.S., Graham D.Y. 2000. Quantitative and bioluminescent assay to measure efficacy of conventional and DNA vaccinations against Helicobacter pylory. Comb. Chem. High Throughput Screen. 3, 289-302.
    • (2000) Comb. Chem. High Throughput Screen , vol.3 , pp. 289-302
    • Ozpolat, B.1    Rao, X.M.2    Lachman, L.B.3    Osato, M.S.4    Graham, D.Y.5
  • 87
    • 0033827591 scopus 로고    scopus 로고
    • Quantitation of Chlamidia trachomatis 16S rRNA using NASBA amplification and a bioluminescent microtiter plate assay
    • Song X., Coombes B.K., Mahony J.B. 2000. Quantitation of Chlamidia trachomatis 16S rRNA using NASBA amplification and a bioluminescent microtiter plate assay. Comb. Chem. High Throughput Screen. 3, 303-313.
    • (2000) Comb. Chem. High Throughput Screen , vol.3 , pp. 303-313
    • Song, X.1    Coombes, B.K.2    Mahony, J.B.3
  • 88
    • 0031945655 scopus 로고    scopus 로고
    • Quantitative, competitive PCR assay for HIV-1 using a microplate-based detection system
    • Guenthner P.C., Hart C.E. 1998. Quantitative, competitive PCR assay for HIV-1 using a microplate-based detection system. Biotechniques. 24, 810-816.
    • (1998) Biotechniques , vol.24 , pp. 810-816
    • Guenthner, P.C.1    Hart, C.E.2
  • 89
    • 0035253492 scopus 로고    scopus 로고
    • Enzyme-amplified aequorin-based bioluminometric hybridization assays
    • Laios E., Ioannou P.C., Christopoulus T.K. 2001. Enzyme-amplified aequorin-based bioluminometric hybridization assays. Anal. Chem. 73, 689-692.
    • (2001) Anal. Chem. , vol.73 , pp. 689-692
    • Laios, E.1    Ioannou, P.C.2    Christopoulus, T.K.3
  • 91
    • 23044495294 scopus 로고    scopus 로고
    • High-throughput double quantitative competitive polymerase chain reaction for determination of genetically modified organisms
    • Mavropoulou A.K., Ioannou P.C., Koraki T., Christopoulos T.K. 2005. High-throughput double quantitative competitive polymerase chain reaction for determination of genetically modified organisms. Anal. Chem. 77, 4785-4791.
    • (2005) Anal. Chem. , vol.77 , pp. 4785-4791
    • Mavropoulou, A.K.1    Ioannou, P.C.2    Koraki, T.3    Christopoulos, T.K.4
  • 93
    • 0042407892 scopus 로고    scopus 로고
    • Quenching of biotinylated aequorin bioluminescence by dye-labeled avidin conjugates: Application to homogeneous bioluminescence resonance energy transfer assays
    • Adamczyk M., Moore J.A., Shreder K. 2001. Quenching of biotinylated aequorin bioluminescence by dye-labeled avidin conjugates: Application to homogeneous bioluminescence resonance energy transfer assays. Organic Lett. 3, 1797-1800.
    • (2001) Organic Lett. , vol.3 , pp. 1797-1800
    • Adamczyk, M.1    Moore, J.A.2    Shreder, K.3
  • 94
    • 20444374787 scopus 로고    scopus 로고
    • Application of liposomal bioluminescent label in the development of a flow injection immunoanalytical system
    • Ho J. A., Huang M.-R. 2005. Application of liposomal bioluminescent label in the development of a flow injection immunoanalytical system. Anal. Chem. 77, 3431-3436.
    • (2005) Anal. Chem. , vol.77 , pp. 3431-3436
    • Ho, J.A.1    Huang, M.-R.2
  • 98
    • 0034658382 scopus 로고    scopus 로고
    • Bioluminescence detection of proteolytic bond cleavage by using recombinant aequorin
    • Deo S.K., Lewis J.C., Daunert S. 2000. Bioluminescence detection of proteolytic bond cleavage by using recombinant aequorin. Anal. Biochem. 281, 87-94.
    • (2000) Anal. Biochem. , vol.281 , pp. 87-94
    • Deo, S.K.1    Lewis, J.C.2    Daunert, S.3
  • 99
    • 0025793866 scopus 로고
    • A solid-phase assay for beta-1,4-galactosyltransferase activity in human serum using recombinant aequorin
    • Zatta P.F., Nyame K., Cormier M.J., Mattox S.A., Prieto P.A., Smith D.F., Cummings R.D. 1991. A solid-phase assay for beta-1,4-galactosyltransferase activity in human serum using recombinant aequorin. Anal. Biochem. 194, 185-191.
    • (1991) Anal. Biochem. , vol.194 , pp. 185-191
    • Zatta, P.F.1    Nyame, K.2    Cormier, M.J.3    Mattox, S.A.4    Prieto, P.A.5    Smith, D.F.6    Cummings, R.D.7
  • 100
    • 0029895889 scopus 로고    scopus 로고
    • A new bioluminescent assay for studies of protein G and protein A binding to IgG and IgM
    • Zatta P.F. 1996. A new bioluminescent assay for studies of protein G and protein A binding to IgG and IgM. J. Biochem. Biophys. Methods. 32, 7-13.
    • (1996) J. Biochem. Biophys. Methods , vol.32 , pp. 7-13
    • Zatta, P.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.