2023
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. doi:10.1021/acs.jproteome.3c00425DOI: 10.1021/acs.jproteome.3c00425
Po, A., & Eyers, C. E. (2023). Top-Down Proteomics and the Challenges of True Proteoform Characterization.. Journal of proteome research. doi:10.1021/acs.jproteome.3c00416DOI: 10.1021/acs.jproteome.3c00416
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.87958DOI: 10.7554/elife.87958
Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms (Preprint)
DOI: 10.1101/2023.10.05.561145
Considerations for defining+80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond (Journal article)
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/d3cc02909cDOI: 10.1039/d3cc02909c
Collings, K., Boisdon, C., Sham, T. -T., Skinley, K., Oh, H. -K., Prince, T., . . . Maher, S. (n.d.). Attaching protein-adsorbing silica particles to the surface of cotton substrates for bioaerosol capture including SARS-CoV-2. Nature Communications, 14(1). doi:10.1038/s41467-023-40696-xDOI: 10.1038/s41467-023-40696-x
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.87958.1DOI: 10.7554/elife.87958.1
Neves, L. X., Wilson, R. A., Brownridge, P., Holman, S. W. W., Harman, V. M. M., Eyers, C. E. E., . . . Castro-Borges, W. (2023). Dissection of schistosome tissues under LC-MS compatible preservative conditions for quantitative proteomics. RAPID COMMUNICATIONS IN MASS SPECTROMETRY. doi:10.1002/rcm.9523DOI: 10.1002/rcm.9523
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/BCJ20220474DOI: 10.1042/BCJ20220474
2022
Want to Publish in <i>JPR</i>? This Is What You Need to Know! (Journal article)
Yates, J. R., Cristea, I. M., Dong, M. -Q., Eyers, C. E., LaBaer, J., Li, J. V., . . . Slavov, N. (2022). Want to Publish in <i>JPR</i>? This Is What You Need to Know!. JOURNAL OF PROTEOME RESEARCH, 21(12), 2837-2839. doi:10.1021/acs.jproteome.2c00704DOI: 10.1021/acs.jproteome.2c00704
Hunter, J. E., Campbell, A. E., Butterworth, J. A., Sellier, H., Hannaway, N. L., Luli, S., . . . Perkins, N. D. (2022). Mutation of the RelA(p65) Thr505 phosphosite disrupts the DNA replication stress response leading to CHK1 inhibitor resistance. BIOCHEMICAL JOURNAL, 479(19), 2087-2113. doi:10.1042/BCJ20220089DOI: 10.1042/BCJ20220089
Hunter, J. E., Campbell, A. E., Hannaway, N. L., Kerridge, S., Luli, S., Butterworth, J. A., . . . Perkins, N. D. (2022). Regulation of CHK1 inhibitor resistance by a c-Rel and USP1 dependent pathway. BIOCHEMICAL JOURNAL, 479(19), 2063-2086. doi:10.1042/BCJ20220102DOI: 10.1042/BCJ20220102
Hunter, J. E., Campbell, A. E., Kerridge, S., Fraser, C., Hannaway, N. L., Luli, S., . . . Perkins, N. D. (2022). Up-regulation of the PI3K/AKT and RHO/RAC/PAK signalling pathways in CHK1 inhibitor resistant E?-Myc lymphoma cells. BIOCHEMICAL JOURNAL, 479(19), 2131-2151. doi:10.1042/BCJ20220103DOI: 10.1042/BCJ20220103
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.2022.111073DOI: 10.1016/j.celrep.2022.111073
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/s41467-022-31109-6DOI: 10.1038/s41467-022-31109-6
Kalyuzhnyy, A., Eyers, P. A., Eyers, C. E., Bowler-Barnett, E., Martin, M. J., Sun, Z., . . . Jones, A. R. (2022). Profiling the Human Phosphoproteome to Estimate the True Extent of Protein Phosphorylation. JOURNAL OF PROTEOME RESEARCH, 21(6), 1510-1524. doi:10.1021/acs.jproteome.2c00131DOI: 10.1021/acs.jproteome.2c00131
Exploring the conformational landscape and stability of Aurora A using ion-mobility mass spectrometry and molecular modelling (Journal article)
Tomlinson, L. J., Batchelor, M., Sarsby, J., Byrne, D. P., Brownridge, P., Bayliss, R., . . . Eyers, C. E. (2022). Exploring the conformational landscape and stability of Aurora A using ion-mobility mass spectrometry and molecular modelling. Journal of the American Society for Mass Spectrometry. doi:10.1021/jasms.1c00271DOI: 10.1021/jasms.1c00271
2021
Campion, R., Bloxam, L., Burrow, K., Brownridge, P. J., Pentland, D. R., Thomas, P., . . . Morgan, A. (2021). Proteomic analysis of dietary restriction in yeast reveals a role for Hsp26 in replicative lifespan extension. BIOCHEMICAL JOURNAL, 478(24), 4153-4167. doi:10.1042/BCJ20210432DOI: 10.1042/BCJ20210432
Eyers, C. E. (2021). "What's in a Name?": Considerations for Identifying Preferred Reviewers. JOURNAL OF PROTEOME RESEARCH, 20(10), 4625-4626. doi:10.1021/acs.jproteome.1c00667DOI: 10.1021/acs.jproteome.1c00667
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-wDOI: 10.1038/s41467-021-25796-w
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.abf6685DOI: 10.1126/scisignal.abf6685
Campbell, A. E., Franco, C. F., Ling-I, S., Corbin, E. K., Perkins, S., Kalyuzhnyy, A., . . . Eyers, C. E. (2021). Temporal modulation of the NF-kappa B ReIA network in response to different types of DNA damage. Biochemical Journal, 478(3), 533-551. doi:10.1042/BCJ20200627DOI: 10.1042/BCJ20200627
2020
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.aax2713DOI: 10.1126/scisignal.aax2713
Use of the Polo-like kinase 4 (PLK4) inhibitor centrinone to investigate intracellular signalling networks using SILAC-based phosphoproteomics (Journal article)
Byrne, D. P., Clarke, C. J., Brownridge, P. J., Kalyuzhnyy, A., Perkins, S., Campbell, A., . . . Eyers, C. E. (2020). Use of the Polo-like kinase 4 (PLK4) inhibitor centrinone to investigate intracellular signalling networks using SILAC-based phosphoproteomics. The Biochemical journal, 477(13), 2451-2475. doi:10.1042/bcj20200309DOI: 10.1042/bcj20200309
Use of the Polo-like kinase 4 (PLK4) inhibitor centrinone to investigate intracellular signaling networks using SILAC-based phosphoproteomics (Preprint)
DOI: 10.1101/2020.05.22.110767
Neves, L. X., Wilson, R. A., Brownridge, P., Harman, V. M., Holman, S. W., Beynon, R. J., . . . Castro-Borges, W. (2020). Quantitative Proteomics of Enriched Esophageal and Gut Tissues from the Human Blood Fluke <i>Schistosoma mansoni</i> Pinpoints Secreted Proteins for Vaccine Development. JOURNAL OF PROTEOME RESEARCH, 19(1), 314-326. doi:10.1021/acs.jproteome.9b00531DOI: 10.1021/acs.jproteome.9b00531
Tsuchiya, Y., Byrne, D. P., Burgess, S. G., Bormann, J., Bakovic, J., Huang, Y., . . . Gout, I. (2020). Covalent Aurora A regulation by the metabolic integrator coenzyme A. REDOX BIOLOGY, 28. doi:10.1016/j.redox.2019.101318DOI: 10.1016/j.redox.2019.101318
Tomlinson, L. J., Coldron, A. K. M. C., Eyers, P. A., & Eyers, C. E. (2020). Determination of Phosphohistidine Stoichiometry in Histidine Kinases by Intact Mass Spectrometry. HISTIDINE PHOSPHORYLATION, 2077, 83-91. doi:10.1007/978-1-4939-9884-5_6DOI: 10.1007/978-1-4939-9884-5_6
High-Throughput Characterization of Histidine Phosphorylation Sites Using UPAX and Tandem Mass Spectrometry (Chapter)
Hardman, G., & Eyers, C. E. (2020). High-Throughput Characterization of Histidine Phosphorylation Sites Using UPAX and Tandem Mass Spectrometry. In HISTIDINE PHOSPHORYLATION (Vol. 2077, pp. 225-235). doi:10.1007/978-1-4939-9884-5_15DOI: 10.1007/978-1-4939-9884-5_15
Histidine Phosphorylation Methods and Protocols Preface (Chapter)
Eyers, C. E. (2020). Histidine Phosphorylation Methods and Protocols Preface. In HISTIDINE PHOSPHORYLATION (Vol. 2077, pp. V). Retrieved from https://www.webofscience.com/
Tomlinson, L. J., & Eyers, C. E. (2020). Ion Mobility-Mass Spectrometry to Evaluate the Effects of Protein Modification or Small Molecule Binding on Protein Dynamics. ION MOBILITY-MASS SPECTROMETRY: METHODS AND PROTOCOLS, 2084, 179-190. doi:10.1007/978-1-0716-0030-6_11DOI: 10.1007/978-1-0716-0030-6_11
2019
Hardman, G., Perkins, S., Brownridge, P., Clarke, C., Byrne, D., Campbell, A., . . . Eyers, C. (2019). Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation. The EMBO Journal, 38(21). doi:10.15252/embj.2018100847DOI: 10.15252/embj.2018100847
Gray, C. J., Migas, L. G., Barran, P. E., Pagel, K., Seeberger, P. H., Eyers, C. E., . . . Flitsch, S. L. (2019). Advancing Solutions to the Carbohydrate Sequencing Challenge. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 141(37), 14463-14479. doi:10.1021/jacs.9b06406DOI: 10.1021/jacs.9b06406
Vonderach, M., Byrne, D. P., Barran, P. E., Eyers, P. A., & Eyers, C. E. (2019). DNA Binding and Phosphorylation Regulate the Core Structure of the NF-B p50 Transcription Factor. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 30(1), 128-138. doi:10.1007/s13361-018-1984-0DOI: 10.1007/s13361-018-1984-0
Myoblast Phosphoproteomics as a Tool to Investigate Global Signaling Events During Myogenesis. (Journal article)
Jones, F. K., Hardman, G. E., Ferries, S., Eyers, C. E., & Pisconti, A. (2019). Myoblast Phosphoproteomics as a Tool to Investigate Global Signaling Events During Myogenesis. MYOGENESIS, 2019 EDITION, 1889, 301-317. doi:10.1007/978-1-4939-8897-6_18DOI: 10.1007/978-1-4939-8897-6_18
2018
Foulkes, D. M., Byrne, D. P., Yeung, W., Shrestha, S., Bailey, F. P., Ferries, S., . . . Eyers, P. A. (2018). Covalent inhibitors of EGFR family protein kinases induce degradation of human Tribbles 2 (TRIB2) pseudokinase in cancer cells. SCIENCE SIGNALING, 11(549), 14 pages. doi:10.1126/scisignal.aat7951DOI: 10.1126/scisignal.aat7951
Byrne, D. P., Li, Y., Ramakrishnan, K., Barsukov, I. L., Yates, E. A., Eyers, C. E., . . . Eyers, P. A. (2018). New tools for carbohydrate sulfation analysis: heparan sulfate 2-O-sulfotransferase (HS2ST) is a target for small-molecule protein kinase inhibitors. BIOCHEMICAL JOURNAL, 475(15), 2417-2433. doi:10.1042/BCJ20180265DOI: 10.1042/BCJ20180265
Byrne, D. P., Li, Y., Ngamlert, P., Ramakrishnan, K., Eyers, C. E., Wells, C., . . . Eyers, P. A. (2018). New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors. BIOCHEMICAL JOURNAL, 475(15), 2435-2455. doi:10.1042/BCJ20180266DOI: 10.1042/BCJ20180266
Jarnuczak, A. F., Albornoz, M. G., Eyers, C. E., Grant, C. M., & Hubbard, S. J. (2018). A quantitative and temporal map of proteostasis during heat shock in <i>Saccharomyces cerevisiae</i>. MOLECULAR OMICS, 14(1), 37-52. doi:10.1039/c7mo00050bDOI: 10.1039/c7mo00050b
Eyers, C. E., Vonderach, M., Ferries, S., Jeacock, K., & Eyers, P. A. (2018). Understanding protein-drug interactions using ion mobility-mass spectrometry. CURRENT OPINION IN CHEMICAL BIOLOGY, 42, 167-176. doi:10.1016/j.cbpa.2017.12.013DOI: 10.1016/j.cbpa.2017.12.013
2017
Bury, L., Coelho, P. A., Simeone, A., Ferries, S., Eyers, C. E., Eyers, P. A., . . . Glover, D. M. (2017). Plk4 and Aurora A cooperate in the initiation of acentriolar spindle assembly in mammalian oocytes. JOURNAL OF CELL BIOLOGY, 216(11), 3571-3590. doi:10.1083/jcb.201606077DOI: 10.1083/jcb.201606077
Ferries., Perkins, S., Brownridge., Campbell, A., Eyers, P., Jones, A., & Eyers, C. E. (2017). Evaluation of Parameters for Confident Phosphorylation Site Localization using an Orbitrap Fusion Tribrid Mass Spectrometer. Journal of Proteome Research, 16(9), 3448-3459. doi:10.1021/acs.jproteome.7b00337DOI: 10.1021/acs.jproteome.7b00337
Smith, F. D., Esseltine, J. L., Nygren, P. J., Veesler, D., Byrne, D. P., Vonderach, M., . . . Scott, J. D. (2017). Local protein kinase A action proceeds through intact holoenzymes. Science, 356(6344), 1288-1293. doi:10.1126/science.aaj1669DOI: 10.1126/science.aaj1669
Gray, C., Schindler, B., Migas, L., Picmanova, M., Allouche, A., Green, A., . . . Flitsch, S. (2017). Bottom-up elucidation of glycosidic bond stereochemistry. Analytical Chemistry, 89(08), 4540-4549. doi:10.1021/acs.analchem.6b04998DOI: 10.1021/acs.analchem.6b04998
Gray, C. J., Sanchez-Ruiz, A., Sardzikova, I., Ahmed, Y. A., Miller, R. L., Reyes Martinez, J. E., . . . Flitsch, S. L. (2017). Label-Free Discovery Array Platform for the Characterization of Glycan Binding Proteins and Glycoproteins. ANALYTICAL CHEMISTRY, 89(8), 4444-4451. doi:10.1021/acs.analchem.6b04122DOI: 10.1021/acs.analchem.6b04122
Bennett, R. J., Simpson, D. M., Holman, S. W., Ryan, S., Brownridge, P., Eyers, C. E., . . . Beynon, R. J. (2017). DOSCATs: Double standards for protein quantification. Scientific Reports, 7. doi:10.1038/srep45570DOI: 10.1038/srep45570
2016
Skimming, D., Dastgheib, S., Baffi, T., Byrne, D., Ferries, S., Scott, S., . . . Kannan, N. (2016). KinView: A visual comparative sequence analysis tool for integrated kinome research. Molecular BioSystems, (12), 3651-3665. doi:10.1039/C6MB00466KDOI: 10.1039/C6MB00466K
Barone, G., Staples, C., Ganesh, A., Patterson, K., Byrne, D., Myers, K., . . . Collis, S. (2016). Human CDK18 promotes replication stress signaling and genome stability. Nucleic Acids Research, 44(18), 8772-8785. doi:10.1093/nar/gkw615DOI: 10.1093/nar/gkw615
Byrne, D. P., Vonderach, M., Ferries, S., Brownridge, P. J., Eyers, C. E., & Eyers, P. A. (2016). cAMP-dependent protein kinase (PKA) complexes probed by complementary differential scanning fluorimetry and ion mobility-mass spectrometry. BIOCHEMICAL JOURNAL, 473, 3159-3175. doi:10.1042/BCJ20160648DOI: 10.1042/bcj20160648
Jarnuczak, A. F., Lee, D. C. H., Lawless, C., Holman, S. W., Eyers, C. E., & Hubbard, S. J. (2016). Analysis of Intrinsic Peptide Detectability via Integrated Label-Free and SRM-Based Absolute Quantitative Proteomics. JOURNAL OF PROTEOME RESEARCH, 15(9), 2945-2959. doi:10.1021/acs.jproteome.6b00048DOI: 10.1021/acs.jproteome.6b00048
Mackenzie, R. J., Lawless, C., Holman, S., Lanthaler, K., Beynon, R. J., Grant, C. M., . . . Eyers, C. E. (2016). Absolute protein quantification of the yeast chaperome under conditions of heat shock. Proteomics, 16(15-16), 2128-2140. doi:10.1002/pmic.201500503DOI: 10.1002/pmic.201500503
Gray, C. J., Thomas, B., Upton, R., Migas, L. G., Eyers, C. E., Barran, P. E., & Flitsch, S. L. (2016). Applications of ion mobility mass spectrometry for high throughput, high resolution glycan analysis. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1860(8), 1688-1709. doi:10.1016/j.bbagen.2016.02.003DOI: 10.1016/j.bbagen.2016.02.003
lanucara, F., lam, C., Mann, J., Monie, T., Colombo, S., Holman, S., . . . Eyers, C. E. (2016). Dynamic phosphorylation of RelA on Ser42 and Ser45 in response to TNFα stimulation regulates DNA binding and transcription. Open Biology, 6(7). doi:10.1098/rsob.160055DOI: 10.1098/rsob.160055
RePLiCal: A QconCAT Protein for Retention Time Standardization in Proteomics Studies (Journal article)
Holman, S. W., McLean, L., & Eyers, C. E. (2016). RePLiCal: A QconCAT Protein for Retention Time Standardization in Proteomics Studies. JOURNAL OF PROTEOME RESEARCH, 15(3), 1090-1102. doi:10.1021/acs.jproteome.5b00988DOI: 10.1021/acs.jproteome.5b00988
Lawless, C., Holman, S. W., Brownridge, P., Lanthaler, K., Harman, V. M., Watkins, R., . . . Hubbard, S. J. (2016). Direct and Absolute Quantification of over 1800 Yeast Proteins via Selected Reaction Monitoring. Molecular and Cellular Proteomics, 15(4), 1309-1322. doi:10.1074/mcp.M115.054288DOI: 10.1074/mcp.M115.054288
2015
Strzelecka, D., Holman, S. W., & Eyers, C. E. (2015). Evaluation of dimethyl sulfoxide (DMSO) as a mobile phase additive during top 3 label-free quantitative proteomics. INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 391, 157-160. doi:10.1016/j.ijms.2015.07.004DOI: 10.1016/j.ijms.2015.07.004
In honour of Professor Simon Gaskell's 65th birthday (Journal article)
Eyers, C. E., & Wysocki, V. H. (2015). In honour of Professor Simon Gaskell's 65th birthday. INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 391, 1. doi:10.1016/j.ijms.2015.10.013DOI: 10.1016/j.ijms.2015.10.013
Mass spectrometry for structural analysis and quantification of the Major Urinary Proteins of the house mouse (Journal article)
Beynon, R. J., Armstrong, S. D., Claydon, A. J., Davidson, A. J., Eyers, C. E., Langridge, J. I., . . . Woolerton, Y. E. (2015). Mass spectrometry for structural analysis and quantification of the Major Urinary Proteins of the house mouse. INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 391, 146-156. doi:10.1016/j.ijms.2015.07.026DOI: 10.1016/j.ijms.2015.07.026
Focus on Quantitative Proteomics (Journal article)
Lilley, K. S., Beynon, R. J., Eyers, C. E., & Hubbard, S. J. (2015). Focus on Quantitative Proteomics. PROTEOMICS, 15(18), 3101-3103. doi:10.1002/pmic.201570163DOI: 10.1002/pmic.201570163
Jamuczak, A. E., Eyers, C. E., Schwartz, J. -M., Grant, C. M., & Hubbard, S. J. (2015). Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in <i>Saccharomyces cerevisiae</i>. PROTEOMICS, 15(18), 3126-3139. doi:10.1002/pmic.201400527DOI: 10.1002/pmic.201400527
Protein Structure (Journal article)
Barran, P., Cooper, H., & Eyers, C. (2015). Protein Structure. PROTEOMICS, 15(16), 2731-2732. doi:10.1002/pmic.201570143DOI: 10.1002/pmic.201570143
The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner (Journal article)
Bailey, F., Byrne, D., Oruganty, K., Eyers, C., Novotny, C. J., Shokat, K. M., . . . Eyers, P. (2015). The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner. Biochemical Journal, 467(1), 47-62. doi:10.1042/BJ20141441DOI: 10.1042/BJ20141441
2014
Eukaryotic Elongation Factor 2 Kinase Activity Is Controlled by Multiple Inputs from Oncogenic Signaling (Journal article)
Wang, X., Regufe da Mota, S., Rui, L., Moore, C. E., XIe, J., Lanucara, F., . . . Proud, C. G. (2014). Eukaryotic Elongation Factor 2 Kinase Activity Is Controlled by Multiple Inputs from Oncogenic Signaling. Molecular and Cellular Biology, 34(22), 4088-4103. doi:10.1128/MCB.01035-14DOI: 10.1128/MCB.01035-14
Chawner, R., Holman, S. W., Gaskell, S. J., & Eyers, C. E. (2014). Peptide scrambling during collision-induced dissociation is influenced by N-terminal residue basicity. Journal of the American Society of Mass Spectrometry, 25(11), 1927-1938. doi:10.1021/jasms.8b04652DOI: 10.1021/jasms.8b04652
Gonzalez-Sanchez, M. -B., Lanucara, F., Hardman, G. E., & Eyers, C. E. (2014). Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer. INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 367, 28-34. doi:10.1016/j.ijms.2014.04.015DOI: 10.1016/j.ijms.2014.04.015
Probing the exposure of the phosphate group in modified amino acids and peptides by ion-molecule reactions with triethoxyborane in Fourier transform ion cyclotron resonance mass spectrometry (Journal article)
Lanucara, F., Fornarini, S., Eyers, C. E., & Crestoni, M. E. (2014). Probing the exposure of the phosphate group in modified amino acids and peptides by ion-molecule reactions with triethoxyborane in Fourier transform ion cyclotron resonance mass spectrometry. RAPID COMMUNICATIONS IN MASS SPECTROMETRY, 28(10), 1107-1116. doi:10.1002/rcm.6884DOI: 10.1002/rcm.6884
Discrimination of epimeric glycans and glycopeptides using IM-MS and its potential for carbohydrate sequencing (vol 6, pg 65, 2014) (Journal article)
Both, P., Green, A. P., Gray, C. J., Sardzik, R., Voglmeir, J., Fontana, C., . . . Eyers, C. E. (2014). Discrimination of epimeric glycans and glycopeptides using IM-MS and its potential for carbohydrate sequencing (vol 6, pg 65, 2014). NATURE CHEMISTRY, 6(4), 368. doi:10.1038/NCHEM.1901DOI: 10.1038/NCHEM.1901
Lanucara, F., Lee, D. C. H., & Eyers, C. E. (2014). Unblocking the Sink: Improved CID-Based Analysis of Phosphorylated Peptides by Enzymatic Removal of the Basic <i>C</i>-Terminal Residue. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 25(2), 214-225. doi:10.1007/s13361-013-0770-2DOI: 10.1007/s13361-013-0770-2
Discrimination of epimeric glycans and glycopeptides using IM-MS and its potential for carbohydrate sequencing (Journal article)
Both, P., Green, A. P., Gray, C. J., Sardzik, R., Voglmeir, J., Fontana, C., . . . Eyers, C. E. (2014). Discrimination of epimeric glycans and glycopeptides using IM-MS and its potential for carbohydrate sequencing. NATURE CHEMISTRY, 6(1), 65-74. doi:10.1038/NCHEM.1817DOI: 10.1038/NCHEM.1817
Quantitative Proteomics Preface (Chapter)
Eyers, C. E. (2014). Quantitative Proteomics Preface. In QUANTITATIVE PROTEOMICS (Vol. 1, pp. V-VII). Retrieved from https://www.webofscience.com/
Lanucara, F., Holman, S. W., Gray, C. J., & Eyers, C. E. (2014). The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics. NATURE CHEMISTRY, 6(4), 281-294. doi:10.1038/NCHEM.1889DOI: 10.1038/NCHEM.1889
2013
ChemInform Abstract: Enzymatic Reactions on Immobilized Substrates (Journal article)
Gray, C. J., Weissenborn, M. J., Eyers, C. E., & Flitsch, S. L. (2013). ChemInform Abstract: Enzymatic Reactions on Immobilized Substrates. ChemInform, 44(40). doi:10.1002/chin.201340262DOI: 10.1002/chin.201340262
Enzymatic reactions on immobilised substrates (Journal article)
Gray, C. J., Weissenborn, M. J., Eyers, C. E., & Flitsch, S. L. (2013). Enzymatic reactions on immobilised substrates. CHEMICAL SOCIETY REVIEWS, 42(15), 6378-6405. doi:10.1039/c3cs60018aDOI: 10.1039/c3cs60018a
Attempting to rewrite <i>History</i>: challenges with the analysis of histidine-phosphorylated peptides (Journal article)
Gonzalez-Sanchez, M. -B., Lanucara, F., Helm, M., & Eyers, C. E. (2013). Attempting to rewrite <i>History</i>: challenges with the analysis of histidine-phosphorylated peptides. BIOCHEMICAL SOCIETY TRANSACTIONS, 41, 1089-1095. doi:10.1042/BST20130072DOI: 10.1042/BST20130072
The nitrosated bile acid DNA lesion <i>O</i><SUP>6</SUP>-carboxymethylguanine is a substrate for the human DNA repair protein <i>O</i><SUP>6</SUP>-methylguanine-DNA methyltransferase (Journal article)
Senthong, P., Millington, C. L., Wilkinson, O. J., Marriott, A. S., Watson, A. J., Reamtong, O., . . . Povey, A. C. (2013). The nitrosated bile acid DNA lesion <i>O</i><SUP>6</SUP>-carboxymethylguanine is a substrate for the human DNA repair protein <i>O</i><SUP>6</SUP>-methylguanine-DNA methyltransferase. NUCLEIC ACIDS RESEARCH, 41(5), 3047-3055. doi:10.1093/nar/gks1476DOI: 10.1093/nar/gks1476
A novel approach to the analysis of SUMOylation with the independent use of trypsin and elastase digestion followed by database searching utilising consecutive residue addition to lysine (Journal article)
Chicooree, N., Griffiths, J. R., Connolly, Y., Tan, C. -T., Malliri, A., Eyers, C. E., & Smith, D. L. (2013). A novel approach to the analysis of SUMOylation with the independent use of trypsin and elastase digestion followed by database searching utilising consecutive residue addition to lysine. RAPID COMMUNICATIONS IN MASS SPECTROMETRY, 27(1), 127-134. doi:10.1002/rcm.6425DOI: 10.1002/rcm.6425
Top-down mass spectrometry for the analysis of combinatorial post-translational modifications (Journal article)
Lanucara, F., & Eyers, C. E. (2013). Top-down mass spectrometry for the analysis of combinatorial post-translational modifications. MASS SPECTROMETRY REVIEWS, 32(1), 27-42. doi:10.1002/mas.21348DOI: 10.1002/mas.21348
2012
Dual purpose <i>S</i>-trityl-linkers for glycoarray fabrication on both polystyrene and gold (Journal article)
Wehner, J. W., Weissenborn, M. J., Hartmann, M., Gray, C. J., Sardzik, R., Eyers, C. E., . . . Lindhorst, T. K. (2012). Dual purpose <i>S</i>-trityl-linkers for glycoarray fabrication on both polystyrene and gold. ORGANIC & BIOMOLECULAR CHEMISTRY, 10(44), 8919-8926. doi:10.1039/c2ob26118aDOI: 10.1039/c2ob26118a
QconCAT Standard for Calibration of Ion Mobility-Mass Spectrometry Systems (Journal article)
Chawner, R., McCullough, B., Giles, K., Barran, P. E., Gaskell, S. J., & Eyers, C. E. (2012). QconCAT Standard for Calibration of Ion Mobility-Mass Spectrometry Systems. JOURNAL OF PROTEOME RESEARCH, 11(11), 5564-5572. doi:10.1021/pr3005327DOI: 10.1021/pr3005327
The N-Methylated Peptide SEN304 Powerfully Inhibits Aβ(1-42) Toxicity by Perturbing Oligomer Formation (Journal article)
Amijee, H., Bate, C., Williams, A., Virdee, J., Jeggo, R., Spanswick, D., . . . Doig, A. J. (2012). The N-Methylated Peptide SEN304 Powerfully Inhibits Aβ(1-42) Toxicity by Perturbing Oligomer Formation. BIOCHEMISTRY, 51(42), 8338-8352. doi:10.1021/bi300415vDOI: 10.1021/bi300415v
The use of selected reaction monitoring in quantitative proteomics (Journal article)
Holman, S. W., Sims, P. F. G., & Eyers, C. E. (2012). The use of selected reaction monitoring in quantitative proteomics. BIOANALYSIS, 4(14), 1763-1786. doi:10.4155/BIO.12.126DOI: 10.4155/BIO.12.126
Weissenborn, M. J., Wehner, J. W., Gray, C. J., Sardzik, R., Eyers, C. E., Lindhorst, T. K., & Flitsch, S. L. (2012). Formation of carbohydrate-functionalised polystyrene and glass slides and their analysis by MALDI-TOF MS. BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY, 8, 753-762. doi:10.3762/bjoc.8.86DOI: 10.3762/bjoc.8.86
The influence of a C-terminal basic residue on peptide fragmentation pathways (Journal article)
Chawner, R., Eyers, C. E., & Gaskell, S. J. (2012). The influence of a C-terminal basic residue on peptide fragmentation pathways. INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 316, 284-291. doi:10.1016/j.ijms.2012.02.017DOI: 10.1016/j.ijms.2012.02.017
Proposal for a common nomenclature for peptide fragment ions generated following sequence scrambling during collision-induced dissociation (Journal article)
Chawner, R., Gaskell, S. J., & Eyers, C. E. (2012). Proposal for a common nomenclature for peptide fragment ions generated following sequence scrambling during collision-induced dissociation. RAPID COMMUNICATIONS IN MASS SPECTROMETRY, 26(2), 205-206. doi:10.1002/rcm.5294DOI: 10.1002/rcm.5294
The Nitrosated Bile Acid DNA Lesion, <i>O</i><SUP>6</SUP>-carboxymethylguanine, Is a Substrate for Human <i>O</i><SUP>6</SUP>-alkylguanine DNA Alkyltransferase (Conference Paper)
Senthong, P., Williams, D. M., Wilkinson, O., Millington, C., Marriott, A., Watson, A. J., . . . Povey, A. C. (2012). The Nitrosated Bile Acid DNA Lesion, <i>O</i><SUP>6</SUP>-carboxymethylguanine, Is a Substrate for Human <i>O</i><SUP>6</SUP>-alkylguanine DNA Alkyltransferase. In ENVIRONMENTAL AND MOLECULAR MUTAGENESIS Vol. 53 (pp. S36). Retrieved from https://www.webofscience.com/
2011
Absolute Quantification of the Glycolytic Pathway in Yeast: DEPLOYMENT OF A COMPLETE QconCAT APPROACH (Journal article)
Carroll, K. M., Simpson, D. M., Eyers, C. E., Knight, C. G., Brownridge, P., Dunn, W. B., . . . Beynon, R. J. (2011). Absolute Quantification of the Glycolytic Pathway in Yeast: DEPLOYMENT OF A COMPLETE QconCAT APPROACH. MOLECULAR & CELLULAR PROTEOMICS, 10(12). doi:10.1074/mcp.M111.007633DOI: 10.1074/mcp.M111.007633
CONSeQuence: Prediction of Reference Peptides for Absolute Quantitative Proteomics Using Consensus Machine Learning Approaches (Journal article)
Eyers, C. E., Lawless, C., Wedge, D. C., Lau, K. W., Gaskell, S. J., & Hubbard, S. J. (2011). CONSeQuence: Prediction of Reference Peptides for Absolute Quantitative Proteomics Using Consensus Machine Learning Approaches. MOLECULAR & CELLULAR PROTEOMICS, 10(11). doi:10.1074/mcp.M110.003384DOI: 10.1074/mcp.M110.003384
Drummond, S. P., Hildyard, J., Firczuk, H., Reamtong, O., Li, N., Kannambath, S., . . . McCarthy, J. E. G. (2011). Diauxic shift-dependent relocalization of decapping activators Dhh1 and Pat1 to polysomal complexes. NUCLEIC ACIDS RESEARCH, 39(17), 7764-7774. doi:10.1093/nar/gkr474DOI: 10.1093/nar/gkr474
Identification of a Lacosamide Binding Protein Using an Affinity Bait and Chemical Reporter Strategy: 14-3-3 ζ (Journal article)
Park, K. D., Kim, D., Reamtong, O., Eyers, C., Gaskell, S. J., Liu, R., & Kohn, H. (2011). Identification of a Lacosamide Binding Protein Using an Affinity Bait and Chemical Reporter Strategy: 14-3-3 ζ. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 133(29), 11320-11330. doi:10.1021/ja2034156DOI: 10.1021/ja2034156
MASS SPECTROMETRIC-BASED QUANTITATIVE PROTEOMICS USING SILAC (Journal article)
Lanucara, F., & Eyers, C. E. (2011). MASS SPECTROMETRIC-BASED QUANTITATIVE PROTEOMICS USING SILAC. METHODS IN ENZYMOLOGY, VOL 500, 500, 133-150. doi:10.1016/B978-0-12-385118-5.00008-6DOI: 10.1016/B978-0-12-385118-5.00008-6
QUANTIFICATION OF PROTEINS AND THEIR MODIFICATIONS USING QCONCAT TECHNOLOGY (Journal article)
Carroll, K. M., Lanucara, F., & Eyers, C. E. (2011). QUANTIFICATION OF PROTEINS AND THEIR MODIFICATIONS USING QCONCAT TECHNOLOGY. METHODS IN ENZYMOLOGY, VOL 500, 500, 113-131. doi:10.1016/B978-0-12-385118-5.00007-4DOI: 10.1016/B978-0-12-385118-5.00007-4
2010
Analysis of Post-translational Modifications by LC-MS/MS (Journal article)
Johnson, H., & Eyers, C. E. (2010). Analysis of Post-translational Modifications by LC-MS/MS. LC-MS/MS IN PROTEOMICS: METHODS AND APPLICATIONS, 658, 93-108. doi:10.1007/978-1-60761-780-8_5DOI: 10.1007/978-1-60761-780-8_5
2009
Rigorous determination of the stoichiometry of protein phosphorylation using mass spectrometry (Journal article)
Johnson, H., Eyers, C. E., Eyers, P. A., Beynon, R. J., & Gaskell, S. J. (2009). Rigorous determination of the stoichiometry of protein phosphorylation using mass spectrometry. Journal of the American Society for Mass Spectrometry, 20(12), 2211-2220. doi:10.1016/j.jasms.2009.08.009DOI: 10.1016/j.jasms.2009.08.009
Park, K. D., Morieux, P., Salome, C., Cotten, S. W., Reamtong, O., Eyers, C., . . . Kohn, H. (2009). Lacosamide Isothiocyanate-Based Agents: Novel Agents To Target and Identify Lacosamide Receptors. JOURNAL OF MEDICINAL CHEMISTRY, 52(21), 6897-6911. doi:10.1021/jm9012054DOI: 10.1021/jm9012054
2008
QCAL—a novel standard for assessing instrument conditions for proteome analysis (Journal article)
Eyers, C., Simpson, D. M., Wong, C. C. S., Beynon, R. J., & Gaskell, S. J. (2008). QCAL—a novel standard for assessing instrument conditions for proteome analysis. Journal of the American Society for Mass Spectrometry, 19(9), 1275-1280. doi:10.1016/j.jasms.2008.05.019DOI: 10.1016/j.jasms.2008.05.019
Eyers, C. E., & Reamtong, O. (2008). All systems are go.. Genome biology, 9(5), 307. doi:10.1186/gb-2008-9-5-307DOI: 10.1186/gb-2008-9-5-307
Mass Spectrometry to Identify Posttranslational Modifications (Journal article)
Eyers, C. E., & Gaskell, S. J. (n.d.). Mass Spectrometry to Identify Posttranslational Modifications. Unknown Journal, 1-34. doi:10.1002/9780470048672.wecb469DOI: 10.1002/9780470048672.wecb469
2007
Peptide Detectability following ESI Mass Spectrometry: Prediction using Genetic Programming (Conference Paper)
Wedge, D. C., Kell, D. B., Gaskell, S. J., Lau, K. W., Hubbard, S. J., & Eyers, C. (2007). Peptide Detectability following ESI Mass Spectrometry: Prediction using Genetic Programming. In GECCO 2007: GENETIC AND EVOLUTIONARY COMPUTATION CONFERENCE, VOL 1 AND 2 (pp. 2219-+). Retrieved from https://www.webofscience.com/
Proteomic analysis of the adaptation of the host NSO myeloma cell line to a protein-free medium (Journal article)
De La Luz-Hernández, K. R., Rojas-Del Calvo, L., Victores-Sarasola, S., Lage-Castellanos, A., Eyers, C., Hart, S., . . . Gaskell, S. (2007). Proteomic analysis of the adaptation of the host NSO myeloma cell line to a protein-free medium. Biotecnologia Aplicada, 24(3-4), 215-223.
2005
The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ (Journal article)
Eyers, C. E., McNeill, H., Knebel, A., Morrice, N., Arthur, S. J. C., Cuenda, A., & Cohen, P. (2005). The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ. BIOCHEMICAL JOURNAL, 389, 127-135. doi:10.1042/BJ20050387DOI: 10.1042/BJ20050387
Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer (Journal article)
Fraga, M. F., Ballestar, E., Villar-Garea, A., Boix-Chornet, M., Espada, J., Schotta, G., . . . Esteller, M. (2005). Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. NATURE GENETICS, 37(4), 391-400. doi:10.1038/ng1531DOI: 10.1038/ng1531
2003
The characterization of protein post-translational modifications by mass spectrometry (Journal article)
Schweppe, R. E., Haydon, C. E., Lewis, T. S., Resing, K. A., & Ahn, N. G. (2003). The characterization of protein post-translational modifications by mass spectrometry. ACCOUNTS OF CHEMICAL RESEARCH, 36(6), 453-461. doi:10.1021/ar020143lDOI: 10.1021/ar020143l
Identification of novel phosphorylation sites on <i>Xenopus laevis</i> aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography (Journal article)
Haydon, C. E., Eyers, P. A., Aveline-Wolf, L. D., Resing, K. A., Maller, J. L., & Ahn, N. G. (2003). Identification of novel phosphorylation sites on <i>Xenopus laevis</i> aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography. MOLECULAR & CELLULAR PROTEOMICS, 2(10), 1055-1067. doi:10.1074/mcp.M300054-MCP200DOI: 10.1074/mcp.M300054-MCP200
2002
Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways (Journal article)
Knebel, A., Haydon, C. E., Morrice, N., & Cohen, P. (2002). Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways. BIOCHEMICAL JOURNAL, 367, 525-532. doi:10.1042/BJ20020916DOI: 10.1042/BJ20020916
Identification of a phosphorylation site on skeletal muscle myosin light chain kinase that becomes phosphorylated during muscle contraction (Journal article)
Haydon, C. E., Watt, P. W., Morrice, N., Knebel, A., Gaestel, M., & Cohen, P. (2002). Identification of a phosphorylation site on skeletal muscle myosin light chain kinase that becomes phosphorylated during muscle contraction. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 397(2), 224-231. doi:10.1006/abbi.2001.2625DOI: 10.1006/abbi.2001.2625
