Author

L. A. Daly

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· 5 Evolutionary Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 5 Assay:proteomics· 4 Research Focus:chromatin & epigenetic regulation· 3 Approach:statistical model· 3 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1

Frequent Co-Authors

C. E. Eyers· 7 shared D. P. Byrne· 4 shared P. A. Eyers· 4 shared N. Kannan· 3 shared S. Shrestha· 3 shared A. R. Jones· 2 shared A. Venkat· 2 shared P. J. Brownridge· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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7 shared papersBiochemistry

C. E. Eyers

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms

G. Bendzunas, D. P. Byrne, S. Shrestha, L. A. Daly, S. O. Oswald, S. Katiyar, A. Venkat, W. Yeung, C. E. Eyers, P. A. Eyers, N. Kannan

This study investigates how redox regulation via cysteine oxidation controls BRSK1/2 kinase activity, revealing conserved mechanisms that modulate catalytic function through disulfide bond formation and salt bridge disruption.

bioRxiv · Oct 5, 2023 · PreprintBiochemistry

A bespoke analytical workflow for the confident identification of sulfopeptides and their discrimination from phosphopeptides

L. A. Daly, D. P. Byrne, S. Perkins, P. J. Brownridge, E. McDonnell, A. R. Jones, P. A. Eyers, C. E. Eyers

This study develops a mass spectrometry workflow to identify sulfotyrosine peptides and distinguish them from phosphotyrosine peptides, identifying 21 new sulfotyrosine-containing proteins.

bioRxiv · Jul 15, 2023 · PreprintBiochemistry

Mechanistic and evolutionary insights into isoform-specific 'supercharging' in DCLK family kinases

A. Venkat, G. Watterson, D. P. Byrne, B. O. Boyle, S. Shrestha, N. Gravel, E. E. Fairweather, L. A. Daly, C. Bunn, W. Yeung, I. Aggarwal, S. Katiyar, C. E. Eyers, P. Eyers, N. Kannan

This study investigates how isoform-specific variations in DCLK family kinases affect autoregulation through structural and functional analyses.

bioRxiv · Mar 29, 2023Evolutionary Biology

Evolutionary and cellular analysis of the dark pseudokinase PSKH2

D. P. Byrne, S. Shrestha, L. A. Daly, V. Marensi, K. Ramakrishnan, C. E. Eyers, N. Kannan, P. A. Eyers

This study investigates the evolutionary and cellular roles of the pseudokinase PSKH2, confirming its catalytic inactivity and identifying its mitochondrial localization and chaperone-dependent regulation.

bioRxiv · Sep 10, 2022Biochemistry

Mechanism of glycogen synthase inactivation and interaction with glycogenin

L. Marr, D. Biswas, L. A. Daly, C. Browning, S. Vial, D. P. Maskell, C. Hudson, J. Pollard, J. Bertrand, N. A. Ranson, H. Khatter, C. E. Eyers, K. Sakamoto, E. Zeqiraj

The paper describes the cryo-EM structure of phosphorylated glycogen synthase and its interaction with glycogenin, revealing mechanisms of GS autoinhibition and regulation.

bioRxiv · Nov 14, 2021Biochemistry

Oxygen-dependent changes in HIF binding partners and post-translational modifications regulate stability and transcriptional activity

L. A. Daly, P. J. Brownridge, V. See, C. E. Eyers

The paper investigates how oxygen levels affect HIF-1 and HIF-2 stability and activity through post-translational modifications and interactions, identifying novel oxygen-dependent PTMs and regulatory roles.

bioRxiv · Nov 12, 2020Biochemistry

Characterisation of protease activity during SARS-CoV-2 infection identifies novel viral cleavage sites and cellular targets with therapeutic potential

B. Meyer, J. Chiaravalli, S. Gellenoncourt, P. Brownridge, D. P. Bryne, L. A. Daly, A. Grauslys, M. Walter, F. Agou, L. A. Chakrabarti, C. S. Craik, C. E. Eyers, P. A. Eyers, Y. Gambin, A. R. Jones, , E. Emmott

This study identifies novel SARS-CoV-2 protease cleavage sites and cellular targets using mass spectrometry, showing that targeting these proteins can inhibit viral replication.

bioRxiv · Sep 16, 2020Microbiology