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Volumn 1, Issue 1, 2006, Pages 337-345

Bioluminescence resonance energy transfer (BRET) for the real-time detection of protein-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; PHOTOPROTEIN; PROTEIN;

EID: 34250637175     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.52     Document Type: Article
Times cited : (178)

References (24)
  • 1
    • 33646343978 scopus 로고    scopus 로고
    • Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)
    • Pfleger, K.D. & Eidne, K.A. Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). Nat. Methods 3, 165-174 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 165-174
    • Pfleger, K.D.1    Eidne, K.A.2
  • 2
    • 21344433619 scopus 로고    scopus 로고
    • Methods to monitor the quaternary structure of G-protein-coupled receptors
    • Milligan, G. & Bouvier, M. Methods to monitor the quaternary structure of G-protein-coupled receptors. FEBS J. 272, 2914-2925 (2005).
    • (2005) FEBS J , vol.272 , pp. 2914-2925
    • Milligan, G.1    Bouvier, M.2
  • 3
    • 0036696695 scopus 로고    scopus 로고
    • The use of resonance energy transfer in high-throughput screening: BRET versus FRET
    • Boute, N., Jockers, R. & Issad, T. The use of resonance energy transfer in high-throughput screening: BRET versus FRET. Trends Pharmacol. Sci. 23, 351-354 (2002).
    • (2002) Trends Pharmacol. Sci , vol.23 , pp. 351-354
    • Boute, N.1    Jockers, R.2    Issad, T.3
  • 4
    • 0742306811 scopus 로고    scopus 로고
    • New technologies: Bioluminescence resonance energy transfer (BRET) for the detection of real time interactions involving G-protein coupled receptors
    • Pfleger, K.D.G. & Eidne, K.A. New technologies: Bioluminescence resonance energy transfer (BRET) for the detection of real time interactions involving G-protein coupled receptors. Pituitary 6 141-151 (2003).
    • (2003) Pituitary , vol.6 , pp. 141-151
    • Pfleger, K.D.G.1    Eidne, K.A.2
  • 5
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • Wu, P. & Brand, L. Resonance energy transfer: Methods and applications. Anal. Biochem. 218, 1-13 (1994).
    • (1994) Anal. Biochem , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 6
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., Piston, D.W. & Johnson, C.H. A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. USA 96, 151-156. (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 7
    • 2342534555 scopus 로고    scopus 로고
    • The Arabidopsis repressor of light signaling, COP1, is regulated by nuclear exclusion: Mutational analysis by bioluminescence resonance energy transfer
    • Subramanian, C. et al. The Arabidopsis repressor of light signaling, COP1, is regulated by nuclear exclusion: Mutational analysis by bioluminescence resonance energy transfer. Proc. Natl. Acad. Sci. USA 101, 6798-6802 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6798-6802
    • Subramanian, C.1
  • 8
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S. et al. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. USA 97, 3684-3689 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3684-3689
    • Angers, S.1
  • 9
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer
    • Kroeger, K.M., Hanyaloglu, A.C., Seeber, R.M., Miles, L.E. & Eidne, K.A. Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276 12736-12743 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1    Hanyaloglu, A.C.2    Seeber, R.M.3    Miles, L.E.4    Eidne, K.A.5
  • 10
    • 13444269196 scopus 로고    scopus 로고
    • Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells
    • Pfleger, K.D.G. & Eidne, K.A. Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells. Biochem. J. 385, 625-637 (2005).
    • (2005) Biochem. J , vol.385 , pp. 625-637
    • Pfleger, K.D.G.1    Eidne, K.A.2
  • 11
    • 4444249880 scopus 로고    scopus 로고
    • α(v)β(3) Integrin interacts with the bransforming growth factor β (TGFβ) type II receptor to potentiate the proliferative effects of TGFβ1 in living human lung fibroblasts
    • Scaffidi, A.K. et al. α(v)β(3) Integrin interacts with the bransforming growth factor β (TGFβ) type II receptor to potentiate the proliferative effects of TGFβ1 in living human lung fibroblasts. J. Biol. Chem. 279, 37726-37733 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 37726-37733
    • Scaffidi, A.K.1
  • 12
    • 26944493862 scopus 로고    scopus 로고
    • Model for growth hormone receptor activation based on subunit rotation within a receptor dimer
    • Brown, R.J. et al. Model for growth hormone receptor activation based on subunit rotation within a receptor dimer. Nat. Struct. Mol. Biol. 12, 814-821 (2005).
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 814-821
    • Brown, R.J.1
  • 13
    • 10044273266 scopus 로고    scopus 로고
    • Development of a bioluminescence resonance energy-transfer assay for estrogen-like compound in vivo monitoring
    • Michelini, E., Mirasoli, M., Karp, M., Virta, M. & Roda, A. Development of a bioluminescence resonance energy-transfer assay for estrogen-like compound in vivo monitoring. Anal. Chem. 76, 7069-7076 (2004).
    • (2004) Anal. Chem , vol.76 , pp. 7069-7076
    • Michelini, E.1    Mirasoli, M.2    Karp, M.3    Virta, M.4    Roda, A.5
  • 14
    • 9644307891 scopus 로고    scopus 로고
    • Glucocorticoid ligands specify different interactions with NF-kappaB by allosteric effects on the glucocorticoid receptor DNA binding domain
    • Garside, H. et al. Glucocorticoid ligands specify different interactions with NF-kappaB by allosteric effects on the glucocorticoid receptor DNA binding domain. J. Biol. Chem. 279, 50050-50059 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 50050-50059
    • Garside, H.1
  • 15
    • 2442602269 scopus 로고    scopus 로고
    • Proximal, selective, and dynamic interactions between integrin alphaIIbbeta3 and protein tyrosine kinases in living cells
    • de Virgillo, M., Kiosses, W.B. & Shattil, S.J. Proximal, selective, and dynamic interactions between integrin alphaIIbbeta3 and protein tyrosine kinases in living cells. J. Cell. Biol. 165, 305-311 (2004).
    • (2004) J. Cell. Biol , vol.165 , pp. 305-311
    • de Virgillo, M.1    Kiosses, W.B.2    Shattil, S.J.3
  • 16
    • 4544348052 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation as a DNA damage-induced post-translational modification regulating poly(ADP-ribose) polymerase-1-topoisomerase I interaction
    • Yung, T.M., Sato, S. & Satoh, M.S. Poly(ADP-ribosyl)ation as a DNA damage-induced post-translational modification regulating poly(ADP-ribose) polymerase-1-topoisomerase I interaction. J. Biol. Chem. 279, 39686-39696 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 39686-39696
    • Yung, T.M.1    Sato, S.2    Satoh, M.S.3
  • 17
    • 23844538759 scopus 로고    scopus 로고
    • Src homology 3-domain growth factor receptor-bound 2-like (endophilin) interacting protein 1, a novel neuronal protein that regulates energy balance
    • Trevaskis, J. et al. Src homology 3-domain growth factor receptor-bound 2-like (endophilin) interacting protein 1, a novel neuronal protein that regulates energy balance. Endocrinology 146, 3757-3764 (2005).
    • (2005) Endocrinology , vol.146 , pp. 3757-3764
    • Trevaskis, J.1
  • 18
    • 0037928876 scopus 로고    scopus 로고
    • Oligomerization of transcriptional intermediary factor 1 regulators and interaction with ZNF74 nuclear matrix protein revealed by bioluminescence resonance energy transfer in living cells
    • Germain-Desprez, D., Bazinet, M., Bouvier, M. & Aubry, M. Oligomerization of transcriptional intermediary factor 1 regulators and interaction with ZNF74 nuclear matrix protein revealed by bioluminescence resonance energy transfer in living cells. J. Biol. Chem. 278, 22367-22373 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 22367-22373
    • Germain-Desprez, D.1    Bazinet, M.2    Bouvier, M.3    Aubry, M.4
  • 19
    • 0037384043 scopus 로고    scopus 로고
    • Oxytocin and vasopressin V1a and V2 receptors from constitutive homo- and heterodimers during biosynthesis
    • Terrillon, S. et al. Oxytocin and vasopressin V1a and V2 receptors from constitutive homo- and heterodimers during biosynthesis. Mol. Endocrinol. 17, 677-691 (2003).
    • (2003) Mol. Endocrinol , vol.17 , pp. 677-691
    • Terrillon, S.1
  • 20
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of β1- and β2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier, J.F., Salahpour, A., Angers, S., Breit, A. & Bouvier, M. Quantitative assessment of β1- and β2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J. Biol. Chem. 277, 44925-44931 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 21
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • Ayoub, M.A. et al. Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem. 277, 21522-21528 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1
  • 22
    • 24144488192 scopus 로고    scopus 로고
    • High-throughput screening of G protein-coupled receptor antagonists using a bioluminescence resonance energy transfer 1-based β-arrestin2 recruitment assay
    • Hamdan, F.F., Audet, M., Garneau, P., Pelletier, J. & Bouvier, M. High-throughput screening of G protein-coupled receptor antagonists using a bioluminescence resonance energy transfer 1-based β-arrestin2 recruitment assay. J. Biomol. Screen. 10, 463-475 (2005).
    • (2005) J. Biomol. Screen , vol.10 , pp. 463-475
    • Hamdan, F.F.1    Audet, M.2    Garneau, P.3    Pelletier, J.4    Bouvier, M.5
  • 23
    • 33747312516 scopus 로고    scopus 로고
    • Extended bioluminescence resonance energy transfer (eBRET) for monitoring prolonged protein-protein interactions in live cells
    • Advance online publication 21 February, doi: 10.1016/j.cellsig.2006.01.004
    • Pfleger, K.D. et al. Extended bioluminescence resonance energy transfer (eBRET) for monitoring prolonged protein-protein interactions in live cells. Cell. Signal; Advance online publication 21 February 2006 (doi: 10.1016/j.cellsig.2006.01.004).
    • (2006) Cell. Signal
    • Pfleger, K.D.1
  • 24
    • 28744450683 scopus 로고    scopus 로고
    • Noninvasive imaging of protein-protein interactions from live cells and living subjects using bioluminescence resonance energy transfer
    • De, A. & Gambhir, S.S. Noninvasive imaging of protein-protein interactions from live cells and living subjects using bioluminescence resonance energy transfer. FASEB J. 19, 2017-2019 (2005).
    • (2005) FASEB J , vol.19 , pp. 2017-2019
    • De, A.1    Gambhir, S.S.2


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