scholarly journals Supramolecular Control over Split-Luciferase Complementation

2016 ◽  
Vol 55 (31) ◽  
pp. 8899-8903 ◽  
Author(s):  
Ralph P. G. Bosmans ◽  
Jeroen M. Briels ◽  
Lech-Gustav Milroy ◽  
Tom F. A. de Greef ◽  
Maarten Merkx ◽  
...  
Keyword(s):  
Split Luciferase Complementation ◽  
Supramolecular Control ◽  
Split Luciferase

scholarly journals Supramolecular Control over Split-Luciferase Complementation

2016 ◽  
Vol 128 (31) ◽  
pp. 9045-9049 ◽  
Author(s):  
Ralph P. G. Bosmans ◽  
Jeroen M. Briels ◽  
Lech-Gustav Milroy ◽  
Tom F. A. de Greef ◽  
Maarten Merkx ◽  
...  
Keyword(s):  
Split Luciferase Complementation ◽  
Supramolecular Control ◽  
Split Luciferase

scholarly journals A Detection Method for GLUT4 Exocytosis Based on Spontaneous Split Luciferase Complementation

2019 ◽  
Vol 35 (8) ◽  
pp. 835-838 ◽  
Author(s):  
Mizuki ENDO ◽  
Masashi MIYASAKI ◽  
Qiaojing LI ◽  
Genki KAWAMURA ◽  
Takeaki OZAWA
Keyword(s):  
Detection Method ◽  
Split Luciferase Complementation ◽  
Split Luciferase

scholarly journals A Split Luciferase Complementation Assay for the Quantification of β-Arrestin2 Recruitment to Dopamine D2-Like Receptors

2020 ◽  
Vol 21 (17) ◽  
pp. 6103
Author(s):  
Lisa Forster ◽  
Lukas Grätz ◽  
Denise Mönnich ◽  
Günther Bernhardt ◽  
Steffen Pockes
Keyword(s):  
Kinase Inhibitors ◽  
Radioligand Binding ◽  
Binding Studies ◽  
Time Resolved ◽  
Protein Activation ◽  
Kinetic Information ◽  
Split Luciferase Complementation ◽  
Homogeneous Assay ◽  
Radioligand Binding Studies ◽  
Split Luciferase

Investigations on functional selectivity of GPCR ligands have become increasingly important to identify compounds with a potentially more beneficial side effect profile. In order to discriminate between individual signaling pathways, the determination of β-arrestin2 recruitment, in addition to G-protein activation, is of great value. In this study, we established a sensitive split luciferase-based assay with the ability to quantify β-arrestin2 recruitment to D2long and D3 receptors and measure time-resolved β-arrestin2 recruitment to the D2long receptor after agonist stimulation. We were able to characterize several standard (inverse) agonists as well as antagonists at the D2longR and D3R subtypes, whereas for the D4.4R, no β-arrestin2 recruitment was detected, confirming previous reports. Extensive radioligand binding studies and comparisons with the respective wild-type receptors confirm that the attachment of the Emerald luciferase fragment to the receptors does not affect the integrity of the receptor proteins. Studies on the involvement of GRK2/3 and PKC on the β-arrestin recruitment to the D2longR and D3R, as well as at the D1R using different kinase inhibitors, showed that the assay could also contribute to the elucidation of signaling mechanisms. Its broad applicability, which provides concentration-dependent and kinetic information on receptor/β-arrestin2 interactions, renders this homogeneous assay a valuable method for the identification of biased agonists.

scholarly journals A new split‐luciferase complementation assay identifies pentachlorophenol as an inhibitor of apoptosome formation

FEBS Open Bio ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 1194-1203 ◽  
Author(s):  
Amin Tashakor ◽  
Mahshid H‐Dehkordi ◽  
Enda O'Connell ◽  
Sergi Gomez Ganau ◽  
Rafael Gozalbes ◽  
...  
Keyword(s):  
Complementation Assay ◽  
Split Luciferase Complementation ◽  
Split Luciferase
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