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Volumn 27, Issue 5, 2016, Pages 1175-1187

NanoLuc: A Small Luciferase Is Brightening Up the Field of Bioluminescence

Author keywords

[No Author keywords available]

Indexed keywords

MEDICAL APPLICATIONS; MOLECULAR BIOLOGY; MOLECULAR IMAGING; PHOSPHORESCENCE; PLANTS (BOTANY); SYSTEM STABILITY;

EID: 84971342943     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/acs.bioconjchem.6b00112     Document Type: Review
Times cited : (383)

References (61)
  • 1
    • 84971307867 scopus 로고    scopus 로고
    • Review of Bioluminescence for Engineers and Scientists in Biophotonics
    • Widder, E. A. and Falls, B. (2014) Review of Bioluminescence for Engineers and Scientists in Biophotonics IEEE J. Sel. Top. Quantum Electron. 20, 232 10.1109/JSTQE.2013.2284434
    • (2014) IEEE J. Sel. Top. Quantum Electron. , vol.20 , pp. 232
    • Widder, E.A.1    Falls, B.2
  • 2
    • 85034835826 scopus 로고    scopus 로고
    • Chapter 1. A History of Bioluminescence and Chemiluminescence from Ancient Times to the Present
    • pp, The Royal Society of Chemistry
    • Roda, A. (2011) Chapter 1. A History of Bioluminescence and Chemiluminescence from Ancient Times to the Present, in Chemiluminescence and Bioluminescence: Past, Present and Future, pp 1-50, The Royal Society of Chemistry.
    • (2011) Chemiluminescence and Bioluminescence: Past, Present and Future , pp. 1-50
    • Roda, A.1
  • 3
    • 84907546569 scopus 로고    scopus 로고
    • Engineering an enhanced, thermostable, monomeric bacterial luciferase gene as a reporter in plant protoplasts
    • Cui, B., Zhang, L., Song, Y., Wei, J., Li, C., Wang, T., Wang, Y., Zhao, T., and Shen, X. (2014) Engineering an enhanced, thermostable, monomeric bacterial luciferase gene as a reporter in plant protoplasts PLoS One 9, e107885 10.1371/journal.pone.0107885
    • (2014) PLoS One , vol.9 , pp. e107885
    • Cui, B.1    Zhang, L.2    Song, Y.3    Wei, J.4    Li, C.5    Wang, T.6    Wang, Y.7    Zhao, T.8    Shen, X.9
  • 5
    • 0000446257 scopus 로고
    • The Energy Source for Bioluminescence in an Isolated System
    • McElroy, W. D. (1947) The Energy Source for Bioluminescence in an Isolated System Proc. Natl. Acad. Sci. U. S. A. 33, 342-345 10.1073/pnas.33.11.342
    • (1947) Proc. Natl. Acad. Sci. U. S. A. , vol.33 , pp. 342-345
    • McElroy, W.D.1
  • 7
    • 79959493880 scopus 로고    scopus 로고
    • Bioluminescence: The First 3000 Years
    • Lee, J. (2008) Bioluminescence: the First 3000 Years J. Sib. Fed. Univ., Chem. 3, 194-205
    • (2008) J. Sib. Fed. Univ., Chem. , vol.3 , pp. 194-205
    • Lee, J.1
  • 8
    • 39049098131 scopus 로고    scopus 로고
    • Firefly luminescence: A historical perspective and recent developments
    • Fraga, H. (2008) Firefly luminescence: a historical perspective and recent developments Photochem. Photobiol. Sci. 7, 146-158 10.1039/b719181b
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 146-158
    • Fraga, H.1
  • 9
    • 33644611917 scopus 로고    scopus 로고
    • Discovery of green fluorescent protein
    • Shimomura, O. (2005) Discovery of green fluorescent protein Methods Biochem. Anal. 47, 1-13 10.1002/0471739499.ch1
    • (2005) Methods Biochem. Anal. , vol.47 , pp. 1-13
    • Shimomura, O.1
  • 10
    • 0024585366 scopus 로고
    • In memoriam Dr Marlene DeLuca. 1987 O. M. Smith Lecture. Firefly luciferase: Mechanism of action, cloning and expression of the active enzyme
    • Kricka, L. J. and Leach, F. R. (1989) In memoriam Dr Marlene DeLuca. 1987 O. M. Smith Lecture. Firefly luciferase: mechanism of action, cloning and expression of the active enzyme J. Biolumin. Chemilumin. 3, 1-5 10.1002/bio.1170030102
    • (1989) J. Biolumin. Chemilumin. , vol.3 , pp. 1-5
    • Kricka, L.J.1    Leach, F.R.2
  • 11
    • 0016710446 scopus 로고
    • Oplophorus oxyluciferin and a model luciferin compound biologically active with Oplophorus luciferase
    • Yamaguchi, I. (1975) Oplophorus oxyluciferin and a model luciferin compound biologically active with Oplophorus luciferase Biochem. J. 151, 9-15 10.1042/bj1510009
    • (1975) Biochem. J. , vol.151 , pp. 9-15
    • Yamaguchi, I.1
  • 12
    • 0017582130 scopus 로고
    • Purification and properties of Renilla reniformis luciferase
    • Matthews, J. C., Hori, K., and Cormier, M. J. (1977) Purification and properties of Renilla reniformis luciferase Biochemistry 16, 85-91 10.1021/bi00620a014
    • (1977) Biochemistry , vol.16 , pp. 85-91
    • Matthews, J.C.1    Hori, K.2    Cormier, M.J.3
  • 14
    • 25144443146 scopus 로고    scopus 로고
    • Dual luciferase assay system for rapid assessment of gene expression in Saccharomyces cerevisiae
    • McNabb, D. S., Reed, R., and Marciniak, R. A. (2005) Dual luciferase assay system for rapid assessment of gene expression in Saccharomyces cerevisiae Eukaryotic Cell 4, 1539-1549 10.1128/EC.4.9.1539-1549.2005
    • (2005) Eukaryotic Cell , vol.4 , pp. 1539-1549
    • McNabb, D.S.1    Reed, R.2    Marciniak, R.A.3
  • 15
    • 0017810342 scopus 로고
    • Properties and reaction mechanism of the bioluminescence system of the deep-sea shrimp Oplophorus gracilorostris
    • Shimomura, O., Masugi, T., Johnson, F. H., and Haneda, Y. (1978) Properties and reaction mechanism of the bioluminescence system of the deep-sea shrimp Oplophorus gracilorostris Biochemistry 17, 994-998 10.1021/bi00599a008
    • (1978) Biochemistry , vol.17 , pp. 994-998
    • Shimomura, O.1    Masugi, T.2    Johnson, F.H.3    Haneda, Y.4
  • 16
    • 0000274364 scopus 로고
    • Chemical Mechanisms in Bioluminescence
    • Mccapra, F. (1976) Chemical Mechanisms in Bioluminescence Acc. Chem. Res. 9, 201-208 10.1021/ar50102a001
    • (1976) Acc. Chem. Res. , vol.9 , pp. 201-208
    • McCapra, F.1
  • 17
    • 84899679316 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli: Advances and challenges
    • Rosano, G. L. and Ceccarelli, E. A. (2014) Recombinant protein expression in Escherichia coli: advances and challenges Front. Microbiol. 5, 172 10.3389/fmicb.2014.00172
    • (2014) Front. Microbiol. , vol.5 , pp. 172
    • Rosano, G.L.1    Ceccarelli, E.A.2
  • 18
    • 60449098993 scopus 로고    scopus 로고
    • Progress and prospects: The design and production of plasmid vectors
    • Gill, D. R., Pringle, I. A., and Hyde, S. C. (2009) Progress and prospects: the design and production of plasmid vectors Gene Ther. 16, 165-171 10.1038/gt.2008.183
    • (2009) Gene Ther. , vol.16 , pp. 165-171
    • Gill, D.R.1    Pringle, I.A.2    Hyde, S.C.3
  • 19
    • 84971364005 scopus 로고    scopus 로고
    • Promega, Ed. () Promega Corporation, Madison, WI. URL
    • Promega, Ed. (2016) Promega Corporation, Madison, WI. URL: https://www.promega.com/products/reporter-assays-and-transfection/reporter-assays/nanoluc-luciferase-redefining-reporter-assays/.
    • (2016)
  • 23
    • 84944720532 scopus 로고    scopus 로고
    • Quick preparation of nanoluciferase-based tracers for novel bioluminescent receptor-binding assays of protein hormones: Using erythropoietin as a model
    • Song, G., Wu, Q. P., Xu, T., Liu, Y. L., Xu, Z. G., Zhang, S. F., and Guo, Z. Y. (2015) Quick preparation of nanoluciferase-based tracers for novel bioluminescent receptor-binding assays of protein hormones: Using erythropoietin as a model J. Photochem. Photobiol., B 153, 311-316 10.1016/j.jphotobiol.2015.10.014
    • (2015) J. Photochem. Photobiol., B , vol.153 , pp. 311-316
    • Song, G.1    Wu, Q.P.2    Xu, T.3    Liu, Y.L.4    Xu, Z.G.5    Zhang, S.F.6    Guo, Z.Y.7
  • 24
    • 84949309355 scopus 로고    scopus 로고
    • Multiplex detection of protein-protein interactions using a next generation luciferase reporter
    • Verhoef, L. G., Mattioli, M., Ricci, F., Li, Y. C., and Wade, M. (2016) Multiplex detection of protein-protein interactions using a next generation luciferase reporter Biochim. Biophys. Acta, Mol. Cell Res. 1863, 284-292 10.1016/j.bbamcr.2015.11.031
    • (2016) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1863 , pp. 284-292
    • Verhoef, L.G.1    Mattioli, M.2    Ricci, F.3    Li, Y.C.4    Wade, M.5
  • 25
    • 84914172814 scopus 로고    scopus 로고
    • An ultrasensitive system for measuring the USPs and OTULIN activity using Nanoluc as a reporter
    • Chen, Y., Wang, L., Cheng, X., Ge, X., and Wang, P. (2014) An ultrasensitive system for measuring the USPs and OTULIN activity using Nanoluc as a reporter Biochem. Biophys. Res. Commun. 455, 178-183 10.1016/j.bbrc.2014.10.139
    • (2014) Biochem. Biophys. Res. Commun. , vol.455 , pp. 178-183
    • Chen, Y.1    Wang, L.2    Cheng, X.3    Ge, X.4    Wang, P.5
  • 26
    • 84919363188 scopus 로고    scopus 로고
    • Quantitative measurement of cell membrane receptor internalization by the nanoluciferase reporter: Using the G protein-coupled receptor RXFP3 as a model
    • Liu, Y., Song, G., Shao, X. X., Liu, Y. L., and Guo, Z. Y. (2015) Quantitative measurement of cell membrane receptor internalization by the nanoluciferase reporter: Using the G protein-coupled receptor RXFP3 as a model Biochim. Biophys. Acta, Biomembr. 1848, 688-694 10.1016/j.bbamem.2014.11.026
    • (2015) Biochim. Biophys. Acta, Biomembr. , vol.1848 , pp. 688-694
    • Liu, Y.1    Song, G.2    Shao, X.X.3    Liu, Y.L.4    Guo, Z.Y.5
  • 27
    • 84954323945 scopus 로고    scopus 로고
    • Application of the novel bioluminescent ligand-receptor binding assay to relaxin-RXFP1 system for interaction studies
    • Wu, Q. P., Zhang, L., Shao, X. X., Wang, J. H., Gao, Y., Xu, Z. G., Liu, Y. L., and Guo, Z. Y. (2016) Application of the novel bioluminescent ligand-receptor binding assay to relaxin-RXFP1 system for interaction studies Amino Acids 48, 1099-1107 10.1007/s00726-015-2146-3
    • (2016) Amino Acids , vol.48 , pp. 1099-1107
    • Wu, Q.P.1    Zhang, L.2    Shao, X.X.3    Wang, J.H.4    Gao, Y.5    Xu, Z.G.6    Liu, Y.L.7    Guo, Z.Y.8
  • 29
    • 84876285416 scopus 로고    scopus 로고
    • A convenient luminescence assay of ferroportin internalization to study its interaction with hepcidin
    • Song, G., Jiang, Q., Xu, T., Liu, Y. L., Xu, Z. G., and Guo, Z. Y. (2013) A convenient luminescence assay of ferroportin internalization to study its interaction with hepcidin FEBS J. 280, 1773-1781 10.1111/febs.12192
    • (2013) FEBS J. , vol.280 , pp. 1773-1781
    • Song, G.1    Jiang, Q.2    Xu, T.3    Liu, Y.L.4    Xu, Z.G.5    Guo, Z.Y.6
  • 30
    • 84887824237 scopus 로고    scopus 로고
    • A novel ultrasensitive bioluminescent receptor-binding assay of INSL3 through chemical conjugation with nanoluciferase
    • Zhang, L., Song, G., Xu, T., Wu, Q. P., Shao, X. X., Liu, Y. L., Xu, Z. G., and Guo, Z. Y. (2013) A novel ultrasensitive bioluminescent receptor-binding assay of INSL3 through chemical conjugation with nanoluciferase Biochimie 95, 2454-2459 10.1016/j.biochi.2013.09.008
    • (2013) Biochimie , vol.95 , pp. 2454-2459
    • Zhang, L.1    Song, G.2    Xu, T.3    Wu, Q.P.4    Shao, X.X.5    Liu, Y.L.6    Xu, Z.G.7    Guo, Z.Y.8
  • 31
    • 84908025956 scopus 로고    scopus 로고
    • Nanoluciferase as a novel quantitative protein fusion tag: Application for overexpression and bioluminescent receptor-binding assays of human leukemia inhibitory factor
    • He, S. X., Song, G., Shi, J. P., Guo, Y. Q., and Guo, Z. Y. (2014) Nanoluciferase as a novel quantitative protein fusion tag: Application for overexpression and bioluminescent receptor-binding assays of human leukemia inhibitory factor Biochimie 106, 140-148 10.1016/j.biochi.2014.08.012
    • (2014) Biochimie , vol.106 , pp. 140-148
    • He, S.X.1    Song, G.2    Shi, J.P.3    Guo, Y.Q.4    Guo, Z.Y.5
  • 32
    • 84936890798 scopus 로고    scopus 로고
    • A highly sensitive assay of IRE1 activity using the small luciferase NanoLuc: Evaluation of ALS-related genetic and pathological factors
    • Hikiji, T., Norisada, J., Hirata, Y., Okuda, K., Nagasawa, H., Ishigaki, S., Sobue, G., Kiuchi, K., and Oh-hashi, K. (2015) A highly sensitive assay of IRE1 activity using the small luciferase NanoLuc: Evaluation of ALS-related genetic and pathological factors Biochem. Biophys. Res. Commun. 463, 881-887 10.1016/j.bbrc.2015.05.132
    • (2015) Biochem. Biophys. Res. Commun. , vol.463 , pp. 881-887
    • Hikiji, T.1    Norisada, J.2    Hirata, Y.3    Okuda, K.4    Nagasawa, H.5    Ishigaki, S.6    Sobue, G.7    Kiuchi, K.8    Oh-Hashi, K.9
  • 33
    • 84902863883 scopus 로고    scopus 로고
    • A sensitive assay for the biosynthesis and secretion of MANF using NanoLuc activity
    • Norisada, J., Hirata, Y., Amaya, F., Kiuchi, K., and Oh-hashi, K. (2014) A sensitive assay for the biosynthesis and secretion of MANF using NanoLuc activity Biochem. Biophys. Res. Commun. 449, 483-489 10.1016/j.bbrc.2014.05.031
    • (2014) Biochem. Biophys. Res. Commun. , vol.449 , pp. 483-489
    • Norisada, J.1    Hirata, Y.2    Amaya, F.3    Kiuchi, K.4    Oh-Hashi, K.5
  • 34
    • 84940544060 scopus 로고    scopus 로고
    • The Vaginal Acquisition and Dissemination of HIV-1 Infection in a Novel Transgenic Mouse Model Is Facilitated by Coinfection with Herpes Simplex Virus 2 and Is Inhibited by Microbicide Treatment
    • Seay, K., Khajoueinejad, N., Zheng, J. H., Kiser, P., Ochsenbauer, C., Kappes, J. C., Herold, B., and Goldstein, H. (2015) The Vaginal Acquisition and Dissemination of HIV-1 Infection in a Novel Transgenic Mouse Model Is Facilitated by Coinfection with Herpes Simplex Virus 2 and Is Inhibited by Microbicide Treatment J. Virol. 89, 9559-9570 10.1128/JVI.01326-15
    • (2015) J. Virol. , vol.89 , pp. 9559-9570
    • Seay, K.1    Khajoueinejad, N.2    Zheng, J.H.3    Kiser, P.4    Ochsenbauer, C.5    Kappes, J.C.6    Herold, B.7    Goldstein, H.8
  • 35
    • 84952926946 scopus 로고    scopus 로고
    • High-Throughput Humanized Mouse Models for Evaluation of HIV-1 Therapeutics and Pathogenesis
    • Thomas, T., Seay, K., Zheng, J. H., Zhang, C., Ochsenbauer, C., Kappes, J. C., and Goldstein, H. (2016) High-Throughput Humanized Mouse Models for Evaluation of HIV-1 Therapeutics and Pathogenesis Methods Mol. Biol. 1354, 221-235 10.1007/978-1-4939-3046-3-15
    • (2016) Methods Mol. Biol. , vol.1354 , pp. 221-235
    • Thomas, T.1    Seay, K.2    Zheng, J.H.3    Zhang, C.4    Ochsenbauer, C.5    Kappes, J.C.6    Goldstein, H.7
  • 37
    • 84971336101 scopus 로고    scopus 로고
    • World Health Organization () URL
    • World Health Organization (2015) URL: http://www.who.int/topics/malaria/en/.
    • (2015)
  • 38
    • 84911937900 scopus 로고    scopus 로고
    • Plasmodium falciparum transfected with ultra bright NanoLuc luciferase offers high sensitivity detection for the screening of growth and cellular trafficking inhibitors
    • Azevedo, M. F., Nie, C. Q., Elsworth, B., Charnaud, S. C., Sanders, P. R., Crabb, B. S., and Gilson, P. R. (2014) Plasmodium falciparum transfected with ultra bright NanoLuc luciferase offers high sensitivity detection for the screening of growth and cellular trafficking inhibitors PLoS One 9, e112571 10.1371/journal.pone.0112571
    • (2014) PLoS One , vol.9 , pp. e112571
    • Azevedo, M.F.1    Nie, C.Q.2    Elsworth, B.3    Charnaud, S.C.4    Sanders, P.R.5    Crabb, B.S.6    Gilson, P.R.7
  • 39
    • 84896404489 scopus 로고    scopus 로고
    • Comparison of firefly luciferase and NanoLuc luciferase for biophotonic labeling of group A Streptococcus
    • Loh, J. M. and Proft, T. (2014) Comparison of firefly luciferase and NanoLuc luciferase for biophotonic labeling of group A Streptococcus Biotechnol. Lett. 36, 829-834 10.1007/s10529-013-1423-z
    • (2014) Biotechnol. Lett. , vol.36 , pp. 829-834
    • Loh, J.M.1    Proft, T.2
  • 40
    • 84949036024 scopus 로고    scopus 로고
    • Validation of Mitochondrial Gene Delivery in Liver and Skeletal Muscle via Hydrodynamic Injection Using an Artificial Mitochondrial Reporter DNA Vector
    • Yasuzaki, Y., Yamada, Y., Ishikawa, T., and Harashima, H. (2015) Validation of Mitochondrial Gene Delivery in Liver and Skeletal Muscle via Hydrodynamic Injection Using an Artificial Mitochondrial Reporter DNA Vector Mol. Pharmaceutics 12, 4311-4320 10.1021/acs.molpharmaceut.5b00511
    • (2015) Mol. Pharmaceutics , vol.12 , pp. 4311-4320
    • Yasuzaki, Y.1    Yamada, Y.2    Ishikawa, T.3    Harashima, H.4
  • 42
    • 84955072791 scopus 로고    scopus 로고
    • Self-Assembling NanoLuc Luciferase Fragments as Probes for Protein Aggregation in Living Cells
    • Zhao, J., Nelson, T. J., Vu, Q., Truong, T., and Stains, C. I. (2016) Self-Assembling NanoLuc Luciferase Fragments as Probes for Protein Aggregation in Living Cells ACS Chem. Biol. 11, 132-138 10.1021/acschembio.5b00758
    • (2016) ACS Chem. Biol. , vol.11 , pp. 132-138
    • Zhao, J.1    Nelson, T.J.2    Vu, Q.3    Truong, T.4    Stains, C.I.5
  • 43
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., Piston, D. W., and Johnson, C. H. (1999) A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins Proc. Natl. Acad. Sci. U. S. A. 96, 151-156 10.1073/pnas.96.1.151
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 44
    • 84858203893 scopus 로고    scopus 로고
    • Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling
    • Lohse, M. J., Nuber, S., and Hoffmann, C. (2012) Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling Pharmacol. Rev. 64, 299-336 10.1124/pr.110.004309
    • (2012) Pharmacol. Rev. , vol.64 , pp. 299-336
    • Lohse, M.J.1    Nuber, S.2    Hoffmann, C.3
  • 45
    • 33746300054 scopus 로고    scopus 로고
    • Materials for fluorescence resonance energy transfer analysis: Beyond traditional donor-acceptor combinations
    • Sapsford, K. E., Berti, L., and Medintz, I. L. (2006) Materials for fluorescence resonance energy transfer analysis: beyond traditional donor-acceptor combinations Angew. Chem., Int. Ed. 45, 4562-4589 10.1002/anie.200503873
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 4562-4589
    • Sapsford, K.E.1    Berti, L.2    Medintz, I.L.3
  • 46
    • 34547627492 scopus 로고    scopus 로고
    • Red-shifted Renilla reniformis luciferase variants for imaging in living subjects
    • Loening, A. M., Wu, A. M., and Gambhir, S. S. (2007) Red-shifted Renilla reniformis luciferase variants for imaging in living subjects Nat. Methods 4, 641-643 10.1038/nmeth1070
    • (2007) Nat. Methods , vol.4 , pp. 641-643
    • Loening, A.M.1    Wu, A.M.2    Gambhir, S.S.3
  • 47
    • 84935034436 scopus 로고    scopus 로고
    • HaloTag technology: A versatile platform for biomedical applications
    • England, C. G., Luo, H., and Cai, W. (2015) HaloTag technology: a versatile platform for biomedical applications Bioconjugate Chem. 26, 975-986 10.1021/acs.bioconjchem.5b00191
    • (2015) Bioconjugate Chem. , vol.26 , pp. 975-986
    • England, C.G.1    Luo, H.2    Cai, W.3
  • 49
    • 84955286419 scopus 로고    scopus 로고
    • Fluorophore-NanoLuc BRET Reporters Enable Sensitive in Vivo Optical Imaging and Flow Cytometry for Monitoring Tumorigenesis
    • Schaub, F. X., Reza, M. S., Flaveny, C. A., Li, W., Musicant, A. M., Hoxha, S., Guo, M., Cleveland, J. L., and Amelio, A. L. (2015) Fluorophore-NanoLuc BRET Reporters Enable Sensitive In Vivo Optical Imaging and Flow Cytometry for Monitoring Tumorigenesis Cancer Res. 75, 5023-5033 10.1158/0008-5472.CAN-14-3538
    • (2015) Cancer Res. , vol.75 , pp. 5023-5033
    • Schaub, F.X.1    Reza, M.S.2    Flaveny, C.A.3    Li, W.4    Musicant, A.M.5    Hoxha, S.6    Guo, M.7    Cleveland, J.L.8    Amelio, A.L.9
  • 50
    • 84923923826 scopus 로고    scopus 로고
    • A BRET-based homogeneous insulin assay using interacting domains in the primary binding site of the insulin receptor
    • Shigeto, H., Ikeda, T., Kuroda, A., and Funabashi, H. (2015) A BRET-based homogeneous insulin assay using interacting domains in the primary binding site of the insulin receptor Anal. Chem. 87, 2764-2770 10.1021/ac504063x
    • (2015) Anal. Chem. , vol.87 , pp. 2764-2770
    • Shigeto, H.1    Ikeda, T.2    Kuroda, A.3    Funabashi, H.4
  • 51
    • 75749126550 scopus 로고    scopus 로고
    • Bioluminescent imaging: A critical tool in pre-clinical oncology research
    • O'Neill, K., Lyons, S. K., Gallagher, W. M., Curran, K. M., and Byrne, A. T. (2010) Bioluminescent imaging: a critical tool in pre-clinical oncology research J. Pathol. 220, 317-327 10.1002/path.2656
    • (2010) J. Pathol. , vol.220 , pp. 317-327
    • O'Neill, K.1    Lyons, S.K.2    Gallagher, W.M.3    Curran, K.M.4    Byrne, A.T.5
  • 53
    • 84955714679 scopus 로고    scopus 로고
    • Detection of Brain Tumors and Systemic Metastases Using NanoLuc and Fluc for Dual Reporter Imaging
    • Germain-Genevois, C., Garandeau, O., and Couillaud, F. (2016) Detection of Brain Tumors and Systemic Metastases Using NanoLuc and Fluc for Dual Reporter Imaging Mol. Imaging Biol. 18, 62-69 10.1007/s11307-015-0864-2
    • (2016) Mol. Imaging Biol. , vol.18 , pp. 62-69
    • Germain-Genevois, C.1    Garandeau, O.2    Couillaud, F.3
  • 54
    • 84893508642 scopus 로고    scopus 로고
    • Stable, high-level expression of reporter proteins from improved alphavirus expression vectors to track replication and dissemination during encephalitic and arthritogenic disease
    • Sun, C., Gardner, C. L., Watson, A. M., Ryman, K. D., and Klimstra, W. B. (2014) Stable, high-level expression of reporter proteins from improved alphavirus expression vectors to track replication and dissemination during encephalitic and arthritogenic disease J. Virol. 88, 2035-2046 10.1128/JVI.02990-13
    • (2014) J. Virol. , vol.88 , pp. 2035-2046
    • Sun, C.1    Gardner, C.L.2    Watson, A.M.3    Ryman, K.D.4    Klimstra, W.B.5
  • 56
    • 84888024522 scopus 로고    scopus 로고
    • Highly sensitive real-time in vivo imaging of an influenza reporter virus reveals dynamics of replication and spread
    • Tran, V., Moser, L. A., Poole, D. S., and Mehle, A. (2013) Highly sensitive real-time in vivo imaging of an influenza reporter virus reveals dynamics of replication and spread J. Virol. 87, 13321-13329 10.1128/JVI.02381-13
    • (2013) J. Virol. , vol.87 , pp. 13321-13329
    • Tran, V.1    Moser, L.A.2    Poole, D.S.3    Mehle, A.4
  • 58
    • 0035874931 scopus 로고    scopus 로고
    • Limitations of the reporter green fluorescent protein under simulated tumor conditions
    • Coralli, C., Cemazar, M., Kanthou, C., Tozer, G. M., and Dachs, G. U. (2001) Limitations of the reporter green fluorescent protein under simulated tumor conditions Cancer Res. 61, 4784-4790
    • (2001) Cancer Res. , vol.61 , pp. 4784-4790
    • Coralli, C.1    Cemazar, M.2    Kanthou, C.3    Tozer, G.M.4    Dachs, G.U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.