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Outputs (6)

ThermoBRET: A Ligand-Engagement Nanoscale Thermostability Assay Applied to GPCRs** (2023)
Journal Article
Hoare, B. L., Tippett, D. N., Kaur, A., Cullum, S. A., Miljuš, T., Koers, E. J., …Veprintsev, D. B. (2024). ThermoBRET: A Ligand-Engagement Nanoscale Thermostability Assay Applied to GPCRs**. ChemBioChem, 25(2), Article e202300459. https://doi.org/10.1002/cbic.202300459

Measurements of membrane protein thermostability reflect ligand binding. Current thermostability assays often require protein purification or rely on pre-existing radiolabelled or fluorescent ligands, limiting their application to established targets... Read More about ThermoBRET: A Ligand-Engagement Nanoscale Thermostability Assay Applied to GPCRs**.

Kinetic analysis of endogenous β2-adrenoceptor-mediated cAMP GloSensorTM responses in HEK293 cells (2022)
Journal Article
Cullum, S. A., Veprintsev, D. B., & Hill, S. J. (2023). Kinetic analysis of endogenous β2-adrenoceptor-mediated cAMP GloSensorTM responses in HEK293 cells. British Journal of Pharmacology, 180(10), 1304-1315. https://doi.org/10.1111/bph.16008

Background and Aim: Standard pharmacological analysis of agonist activity utilises measurements of receptor-mediated responses at a set time-point, or at the peak response level, to characterise ligands. However, the occurrence of non-equilibrium con... Read More about Kinetic analysis of endogenous β2-adrenoceptor-mediated cAMP GloSensorTM responses in HEK293 cells.

Combined docking and machine learning identify key molecular determinants of ligand pharmacological activity on β2 adrenoceptor (2022)
Journal Article
Jiménez-Rosés, M., Morgan, B. A., Jimenez Sigstad, M., Tran, T. D. Z., Srivastava, R., Bunsuz, A., …Veprintsev, D. B. (2022). Combined docking and machine learning identify key molecular determinants of ligand pharmacological activity on β2 adrenoceptor. Pharmacology Research and Perspectives, 10(5), Article e00994. https://doi.org/10.1002/prp2.994

G protein-coupled receptors (GPCRs) are valuable therapeutic targets for many diseases. A central question of GPCR drug discovery is to understand what determines the agonism or antagonism of ligands that bind them. Ligands exert their action via the... Read More about Combined docking and machine learning identify key molecular determinants of ligand pharmacological activity on β2 adrenoceptor.

Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation (2019)
Journal Article
Mayer, D., Damberger, F. F., Samarasimhareddy, M., Feldmueller, M., Vuckovic, Z., Flock, T., …Veprintsev, D. B. (2019). Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation. Nature Communications, 10(1), 1-14. https://doi.org/10.1038/s41467-019-09204-y

Cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Despite high-resolution structural data of arrestins bound to phosphorylated receptor C-termi... Read More about Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation.

Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action (2014)
Journal Article
Karagöz, G. E., Duarte, A. M., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., …Rüdiger, S. G. (2014). Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action. Cell, 156(5), 963-974. https://doi.org/10.1016/j.cell.2014.01.037

Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly... Read More about Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action.