Author

D. A. Sykes

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Pharmacology & Toxicology· 2 Bioengineering· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Approach:biophysical modeling· 2 Research Focus:drug response / drug discovery· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

C. R. Harwood· 3 shared D. B. Veprintsev· 3 shared D. Veprintsev· 2 shared E. J. Koers· 2 shared S. J. Briddon· 2 shared A. Hensley· 1 shared A. Kaur· 1 shared A. McAlinden· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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3 shared papersBiochemistry

C. R. Harwood

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Probing drug-target engagement of soluble Gαi1 protein using the SolThermoBRET thermal shift assay

O. Brod, D. Plevako, T. Perera, P. Hompluem, E. J. Koers, M. Hilbert, D. A. Sykes, D. Veprintsev

This paper introduces a high-throughput BRET-based thermal shift assay to measure protein stability and ligand interactions with Gi1 protein without purification.

bioRxiv · Feb 15, 2024 · PreprintBiophysics

Agonist efficacy at the B2AR is driven by agonist-induced differences in receptor affinity for the Gs protein, not ligand binding kinetics.

C. R. Harwood, D. A. Sykes, T. Redfern-Nichols, G. Ladds, S. J. Briddon, D. Veprintsev

This study shows that agonist efficacy at the {beta}2AR is determined by differences in receptor affinity for Gs protein, not ligand binding kinetics.

bioRxiv · Jan 5, 2024 · PreprintPharmacology & Toxicology

Ablation of Proliferating Osteoblast Lineage Cells After Fracture Leads to Atrophic Nonunion in a Mouse Model

K. R. Hixon, J. A. McKenzie, D. A. Sykes, S. Yoneda, A. Hensley, E. G. Buettmann, H. Zheng, D. Skouteris, A. McAlinden, A. N. Miller, M. J. Silva

This study shows that ablating proliferating osteoblast lineage cells after fracture in mice leads to atrophic nonunion, providing a new model for studying this condition.

Journal of Bone and Mineral Research · Nov 1, 2021Peer-reviewedBioengineering

Exploring the kinetic selectivity of drugs targeting the β1-adrenoceptor

D. A. Sykes, M. Jimenez Roses, J. Reilly, R. A. Fairhurst, S. J. Charlton, D. B. Veprintsev

This study investigates the kinetic selectivity of drugs targeting the β1-adrenoceptor, finding that hydrophobic interactions dominate ligand binding kinetics over combined polar and hydrophobic interactions.

bioRxiv · Aug 31, 2021Pharmacology & Toxicology

ThermoBRET: a ligand-engagement nanoscale thermostability assay applied to GPCRs

B. L. Hoare, D. N. Tippett, A. Kaur, S. A. Cullum, T. Miljus, E. J. Koers, C. R. Harwood, N. Dijon, N. D. Holliday, D. A. Sykes, D. B. Veprintsev

ThermoBRET quantifies GPCR thermostability using BRET without labelled ligands, revealing ligand effects on protein unfolding in non-purified samples.

bioRxiv · Aug 5, 2020Biochemistry

Functional solubilisation of the β2-adrenoceptor (β2AR) using Diisobutylene maleic acid (DIBMA).

C. R. Harwood, D. A. Sykes, B. Hoare, F. M. Heydenreich, R. Uddin, D. R. Poyner, S. J. Briddon, D. B. Veprintsev

This paper demonstrates the functional solubilisation of the β2-adrenoceptor using DIBMA, showing improved thermal stability compared to detergent-based methods.

bioRxiv · Jun 29, 2020Biochemistry