Research outputs
2025
An Optimized SP3 Sample Processing Workflow for In-Depth and Reproducible Phosphoproteomics.
Daly, L. A., Clarke, C. J., Oswald, S. O., Jankevics, A., Brownridge, P. J., Scheltema, R. A., & Eyers, C. E. (2025). An Optimized SP3 Sample Processing Workflow for In-Depth and Reproducible Phosphoproteomics.. Journal of proteome research, 24(8), 4300-4308. doi:10.1021/acs.jproteome.5c00220
Pervanadate-induced oxidation relieves autoinhibition of SRC protein tyrosine kinase
Redox regulation and dynamic control of brain-selective kinases BRSK1/2 in the AMPK family through cysteine-based mechanisms
Bendzunas, G. N., Byrne, D. P., Shrestha, S., Daly, L. A., Oswald, S. O., Katiyar, S., . . . Kannan, N. (2025). Redox regulation and dynamic control of brain-selective kinases BRSK1/2 in the AMPK family through cysteine-based mechanisms. eLife, 13. doi:10.7554/elife.92536.4
PSKH1 kinase activity is differentially modulated via allosteric binding of Ca<sup>2+</sup> sensor proteins.
Horne, C. R., Dite, T. A., Young, S. N., Mather, L. J., Dagley, L. F., Johnson, J. L., . . . Murphy, J. M. (2025). PSKH1 kinase activity is differentially modulated via allosteric binding of Ca<sup>2+</sup> sensor proteins.. Proceedings of the National Academy of Sciences of the United States of America, 122(8), e2420961122. doi:10.1073/pnas.2420961122
2024
PSKH1 kinase activity is differentially modulated via allosteric binding of Ca<sup>2+</sup>sensor proteins
Discovery of a Cushing’s syndrome protein kinase A mutant that biases signaling through type I AKAPs
Omar, M. H., Byrne, D. P., Shrestha, S., Lakey, T. M., Lee, K. -S., Lauer, S. M., . . . Scott, J. D. (2024). Discovery of a Cushing’s syndrome protein kinase A mutant that biases signaling through type I AKAPs. Science Advances, 10(8). doi:10.1126/sciadv.adl1258
2023
Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.
Daly, L. A., Byrne, D. P., Perkins, S., Brownridge, P. J., McDonnell, E., Jones, A. R., . . . Eyers, C. E. (2023). Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.. Journal of proteome research, 22(12), 3754-3772. doi:10.1021/acs.jproteome.3c00425
Mechanistic and evolutionary insights into isoform-specific 'supercharging' in DCLK family kinases.
Venkat, A., Watterson, G., Byrne, D. P., O'Boyle, B., Shrestha, S., Gravel, N., . . . Kannan, N. (2023). Mechanistic and evolutionary insights into isoform-specific 'supercharging' in DCLK family kinases.. eLife, 12, RP87958. doi:10.7554/elife.87958
Mechanistic and evolutionary insights into isoform-specific ‘supercharging’ in DCLK family kinases
Venkat, A., Watterson, G., Byrne, D. P., O'Boyle, B., Shrestha, S., Gravel, N., . . . Kannan, N. (2023). Mechanistic and evolutionary insights into isoform-specific ‘supercharging’ in DCLK family kinases. eLife, 12. doi:10.7554/elife.87958.3
Considerations for defining+80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond
Daly, L. A., Clarke, C. J., Po, A., Oswald, S. O., & Eyers, C. E. (2023). Considerations for defining+80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond. CHEMICAL COMMUNICATIONS, 59(77), 11484-11499. doi:10.1039/d3cc02909c
Mechanistic and evolutionary insights into isoform-specific 'supercharging' in DCLK family kinases.
Mechanistic and evolutionary insights into isoform-specific ‘supercharging’ in DCLK family kinases
Venkat, A., Watterson, G., Byrne, D. P., O’Boyle, B., Shrestha, S., Gravel, N., . . . Kannan, N. (2023). Mechanistic and evolutionary insights into isoform-specific ‘supercharging’ in DCLK family kinases. doi:10.7554/elife.87958.1
Evolutionary and cellular analysis of the 'dark' pseudokinase PSKH2
Byrne, D. P., Shrestha, S., Daly, L. A., Marensi, V., Ramakrishnan, K., Eyers, C. E., . . . Eyers, P. A. (2023). Evolutionary and cellular analysis of the 'dark' pseudokinase PSKH2. BIOCHEMICAL JOURNAL, 480(2), 141-160. doi:10.1042/BCJ20220474
TRIB2 as a potential target in AML resistant to target therapy
Marensi, V., Daly, L., Till, J. K., MacEwan, J. D., Eyers, E. C., & Eyers, A. P. (2023). TRIB2 as a potential target in AML resistant to target therapy. In BRITISH JOURNAL OF PHARMACOLOGY Vol. 180 (pp. 1270). Retrieved from https://www.webofscience.com/
2022
Mislocalization of protein kinase A drives pathology in Cushing?s syndrome
Omar, M. H., Byrne, D. P., Jones, K. N., Lakey, T. M., Collins, K. B., Lee, K. -S., . . . Scott, J. D. (2022). Mislocalization of protein kinase A drives pathology in Cushing?s syndrome. CELL REPORTS, 40(2). doi:10.1016/j.celrep.2022.111073
Mechanism of glycogen synthase inactivation and interaction with glycogenin
Marr, L., Biswas, D., Daly, L. A., Browning, C., Vial, S. C. M., Maskell, D. P., . . . Zeqiraj, E. (2022). Mechanism of glycogen synthase inactivation and interaction with glycogenin. NATURE COMMUNICATIONS, 13(1). doi:10.1038/s41467-022-31109-6
2021
Mechanism of glycogen synthase inactivation and interaction with glycogenin
Displacement of PKA catalytic subunit from AKAP signaling islands drives pathology in Cushing’s syndrome
Characterising proteolysis during SARS-CoV-2 infection identifies viral cleavage sites and cellular targets with therapeutic potential
Meyer, B., Chiaravalli, J., Gellenoncourt, S., Brownridge, P., Bryne, D. P., Daly, L. A., . . . Emmott, E. (2021). Characterising proteolysis during SARS-CoV-2 infection identifies viral cleavage sites and cellular targets with therapeutic potential. NATURE COMMUNICATIONS, 12(1). doi:10.1038/s41467-021-25796-w
Oxygen-dependent changes in binding partners and post-translational modifications regulate the abundance and activity of HIF-1 alpha/2 alpha
Daly, L. A., Brownridge, P. J., Batie, M., Rocha, S., See, V., & Eyers, C. E. (2021). Oxygen-dependent changes in binding partners and post-translational modifications regulate the abundance and activity of HIF-1 alpha/2 alpha. SCIENCE SIGNALING, 14(692). doi:10.1126/scisignal.abf6685
2020
The Role of Hypoxia-Inducible Factor Post-Translational Modifications in Regulating Its Localisation, Stability, and Activity
Albanese, A., Daly, L. A., Mennerich, D., Kietzmann, T., & See, V. (2021). The Role of Hypoxia-Inducible Factor Post-Translational Modifications in Regulating Its Localisation, Stability, and Activity. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 22(1). doi:10.3390/ijms22010268
The Role of Hypoxia-Inducible Factor Post-Translational Modifications in Regulating its Localisation, Stability and Activity
Albanese, A., Daly, L., Mennerich, D., Kietzmann, T., & Sée, V. (2020). The Role of Hypoxia-Inducible Factor Post-Translational Modifications in Regulating its Localisation, Stability and Activity. doi:10.20944/preprints202012.0112.v1
Aurora A regulation by reversible cysteine oxidation reveals evolutionarily conserved redox control of Ser/Thr protein kinase activity
Byrne, D. P., Shrestha, S., Galler, M., Cao, M., Daly, L. A., Campbell, A. E., . . . Eyers, P. A. (2020). Aurora A regulation by reversible cysteine oxidation reveals evolutionarily conserved redox control of Ser/Thr protein kinase activity. Science Signaling, 13(639). doi:10.1126/scisignal.aax2713
Identification and characterisation of the post-translational modifications that regulate the Hypoxia Inducible Factors, HIF-1α and HIF-2α
Daly, L. (2020). Identification and characterisation of the post-translational modifications that regulate the Hypoxia Inducible Factors, HIF-1α and HIF-2α.