Author

P. Eyers

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

Biology Disciplines

Click to filter author papers

Biochemistry· 5 Evolutionary Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:human· 7 Approach:experimental assay· 6 Assay:proteomics· 5 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 2 Research Focus:chromatin & epigenetic regulation· 2 Organism:Arabidopsis· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

D. P. Byrne· 4 shared C. Eyers· 3 shared N. Kannan· 3 shared S. Shrestha· 3 shared D. Byrne· 2 shared R. Bayliss· 2 shared S. Katiyar· 2 shared A. Basle· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

4 shared papersBiochemistry

D. P. Byrne

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Regulation of Human PINK1 ubiquitin kinase by Serine167, Serine228 and Cysteine412 phosphorylation

A. Waddell, H. Ojha, S. Agarwal, C. Clarke, A. Terriente-Felix, H. Zhou, P. Kakade, A. Knebel, A. Shaw, R. Gourlay, J. Varghese, R. Soares, R. Toth, T. Macartney, P. Eyers, , M. Muqit

This study identifies phosphorylation sites in hPINK1 that regulate its activation and ubiquitin interaction, revealing a novel inhibitory mechanism involving pCys412.

bioRxiv · Mar 31, 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

A single bacterial sulfatase is required for metabolism of colonic mucin O-glycans and intestinal colonization by a symbiotic human gut bacterium

A. S. Luis, C. Jin, G. Vasconcelos Pereira, R. W. P. Glowacki, S. Gugel, S. Singh, D. P. Byrne, N. A. Pudlo, J. A. London, A. Basle, M. Reihill, S. Oscarson, P. Eyers, M. Czjzek, G. Michel, , E. C. Martens

This study identifies a single sulfatase essential for colonic mucin O-glycan metabolism and intestinal colonization by Bacteroides thetaiotaomicron.

bioRxiv · Nov 20, 2020 · PreprintMicrobiology

A novel redox-active switch in Fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily

S. Shrestha, S. Katiyar, C. E. Sanz-Rodriguez, N. R. Kemppinen, H. W. Kim, R. Kadirvelraj, C. Panagos, N. Keyhaninejad, M. Colonna, P. Chopra, D. P. Byrne, G. J. Boons, E. V. Knaap, P. Eyers, A. S. Edison, , N. Kannan

This study identifies redox-sensitive cysteines in Fructosamine-3-kinases (FN3Ks) that regulate their activity and dimerization through disulfide bonds, revealing a novel redox regulatory mechanism in the protein kinase superfamily.

bioRxiv · Jan 13, 2020Biochemistry

An evolutionary-conserved redox regulatory mechanism in human Ser/Thr protein kinases

D. P. Byrne, S. Shrestha, N. Kannan, P. Eyers

The study identifies a conserved redox regulatory mechanism in human Ser/Thr kinases through cysteine oxidation in the activation segment.

bioRxiv · Mar 8, 2019 · PreprintBiochemistry

Covalent Aurora A regulation by the metabolic integrator coenzyme A

Y. Tsuchiya, D. Byrne, S. Burgess, J. Bormann, J. Bakovic, Y. Huang, A. Zhyvoloup, S. Peak-Chew, T. Tran, F. Bellany, A. Tabor, E. Chan, L. Guruprasad, O. Garifulin, V. Filonenko, , I. Gout

This study identifies a novel covalent inhibition mechanism of Aurora A kinase by coenzyme A, showing its regulation under oxidative stress and impact on meiotic spindle formation.

bioRxiv · Nov 14, 2018Biochemistry

New tools for evaluating protein tyrosine sulphation: Tyrosyl Protein Sulphotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors

P. Eyers, D. Byrne, P. Ngamlert, Y. Li, K. Ramakrishnan, C. Eyers, C. Wells, D. Drewry, W. Zuercher, N. Berry, D. Fernig

The paper develops a non-radioactive assay to quantify tyrosine sulphation by TPST1 and TPST2 and identifies RAF kinase inhibitors as potential TPST inhibitors.

bioRxiv · Apr 6, 2018Biochemistry