Publications
Selected publications
- Characterising proteolysis during SARS-CoV-2 infection identifies viral cleavage sites and cellular targets with therapeutic potential (Journal article - 2021)
- Oxygen-dependent changes in binding partners and post-translational modifications regulate the abundance and activity of HIF-1 alpha/2 alpha (Journal article - 2021)
- Aurora A regulation by reversible cysteine oxidation reveals evolutionarily conserved redox control of Ser/Thr protein kinase activity (Journal article - 2020)
- Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation. (Journal article - 2019)
- DNA Binding and Phosphorylation Regulate the Core Structure of the NF-B p50 Transcription Factor (Journal article - 2019)
2024
Celebrating Women in Proteomics and Metabolomics.
Cristea, I. M., & Eyers, C. E. (2024). Celebrating Women in Proteomics and Metabolomics.. Journal of proteome research, 23(8), 2675-2679. doi:10.1021/acs.jproteome.4c00613
Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms
Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms
Bendzunas, G. N., Byrne, D. P., Shrestha, S., Daly, L. A., Oswald, S. O., Katiyar, S., . . . Kannan, N. (2024). Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms. doi:10.7554/elife.92536.3
Pyro(phospho)mania.
Eyers, C. E., & Clarke, C. J. (2024). Pyro(phospho)mania.. Nature chemical biology. doi:10.1038/s41589-024-01606-4
Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms
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
Mass Spectrometric Analysis of the Active Site Tryptic Peptide of Recombinant <i>O</i><sup>6</sup>-Methylguanine-DNA Methyltransferase Following Incubation with Human Colorectal DNA Reveals the Presence of an <i>O</i><sup>6</sup>-Alkylguanine Adductome.
Abdelhady, R., Senthong, P., Eyers, C. E., Reamtong, O., Cowley, E., Cannizzaro, L., . . . Povey, A. C. (2023). Mass Spectrometric Analysis of the Active Site Tryptic Peptide of Recombinant <i>O</i><sup>6</sup>-Methylguanine-DNA Methyltransferase Following Incubation with Human Colorectal DNA Reveals the Presence of an <i>O</i><sup>6</sup>-Alkylguanine Adductome.. Chemical research in toxicology, 36(12), 1921-1929. doi:10.1021/acs.chemrestox.3c00207
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
Top-Down Proteomics and the Challenges of True Proteoform Characterization.
Po, A., & Eyers, C. E. (2023). Top-Down Proteomics and the Challenges of True Proteoform Characterization.. Journal of proteome research, 22(12), 3663-3675. doi:10.1021/acs.jproteome.3c00416
MicroAge Mission: Examining the Effects of Microgravity and Electrical Stimulation on the Proteome of Human Tissue-Engineered Muscle Constructs
Jones, S., Shigdar, S., Hemmings, K., Hoettges, K., Henstock, J., McArdle, C., . . . McArdle, A. (2023). MicroAge Mission: Examining the Effects of Microgravity and Electrical Stimulation on the Proteome of Human Tissue-Engineered Muscle Constructs. Free Radical Biology and Medicine, 208, S55. doi:10.1016/j.freeradbiomed.2023.10.125
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. (n.d.). Mechanistic and evolutionary insights into isoform-specific ‘supercharging’ in DCLK family kinases. eLife, 12. doi:10.7554/elife.87958.3
18P AURKB inhibition radiosensitises NSCLC by altering mitotic fate
Egerton, K., Mitchell, T. A., Gravells, P., Katse, R., Fisher, M., Muthana, M., . . . Bryant, H. E. (2023). 18P AURKB inhibition radiosensitises NSCLC by altering mitotic fate. ESMO Open, 8(1), 101664. doi:10.1016/j.esmoop.2023.101664
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
Attaching protein-adsorbing silica particles to the surface of cotton substrates for bioaerosol capture including SARS-CoV-2
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-x
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.. bioRxiv. doi:10.1101/2023.03.29.534689
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
Mapping distinct vasodilator-induced phosphorylation patterns in human vascular smooth muscle: A quantitative phosphoproteomic approach
Sloniecka, M., Harris, J., Eyers, C., & Dart, C. (2023). Mapping distinct vasodilator-induced phosphorylation patterns in human vascular smooth muscle: A quantitative phosphoproteomic approach. Physiology, 38(S1). doi:10.1152/physiol.2023.38.s1.5732062
Dissection of schistosome tissues under LC-MS compatible preservative conditions for quantitative proteomics
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.9523
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
2022
Want to Publish in <i>JPR</i>? This Is What You Need to Know!
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.2c00704
Mutation of the RelA(p65) Thr505 phosphosite disrupts the DNA replication stress response leading to CHK1 inhibitor resistance
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/BCJ20220089
Regulation of CHK1 inhibitor resistance by a c-Rel and USP1 dependent pathway
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/BCJ20220102
Up-regulation of the PI3K/AKT and RHO/RAC/PAK signalling pathways in CHK1 inhibitor resistant E?-Myc lymphoma cells
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/BCJ20220103
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
Profiling the Human Phosphoproteome to Estimate the True Extent of Protein Phosphorylation
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.2c00131
Exploring the conformational landscape and stability of Aurora A using ion-mobility mass spectrometry and molecular modelling
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.1c00271
2021
Proteomic analysis of dietary restriction in yeast reveals a role for Hsp26 in replicative lifespan extension
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/BCJ20210432
Mechanism of glycogen synthase inactivation and interaction with glycogenin
Displacement of PKA catalytic subunit from AKAP signaling islands drives pathology in Cushing’s syndrome
"What's in a Name?": Considerations for Identifying Preferred Reviewers
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.1c00667
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
Temporal modulation of the NF-kappa B ReIA network in response to different types of DNA damage
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/BCJ20200627
2020
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
Use of the Polo-like kinase 4 (PLK4) inhibitor centrinone to investigate intracellular signalling networks using SILAC-based phosphoproteomics
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/bcj20200309
Use of the Polo-like kinase 4 (PLK4) inhibitor centrinone to investigate intracellular signaling networks using SILAC-based phosphoproteomics
Quantitative Proteomics of Enriched Esophageal and Gut Tissues from the Human Blood Fluke Schistosoma mansoni Pinpoints Secreted Proteins for Vaccine Development.
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.9b00531
Covalent Aurora A regulation by the metabolic integrator coenzyme A
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.2019.101318
Determination of Phosphohistidine Stoichiometry in Histidine Kinases by Intact Mass Spectrometry.
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_6
High-Throughput Characterization of Histidine Phosphorylation Sites Using UPAX and Tandem Mass Spectrometry
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_15
Histidine Phosphorylation Methods and Protocols Preface
Eyers, C. E. (2020). Histidine Phosphorylation Methods and Protocols Preface. In HISTIDINE PHOSPHORYLATION (Vol. 2077, pp. V). Retrieved from https://www.webofscience.com/
Ion Mobility-Mass Spectrometry to Evaluate the Effects of Protein Modification or Small Molecule Binding on Protein Dynamics.
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_11
Preface
Preface (2014). . Royal Society of Chemistry. doi:10.1039/9781782626985-fp005
2019
Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation.
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.2018100847
Advancing Solutions to the Carbohydrate Sequencing Challenge.
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.9b06406
DNA Binding and Phosphorylation Regulate the Core Structure of the NF-B p50 Transcription Factor
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/s13361-018-1984-0
Myoblast Phosphoproteomics as a Tool to Investigate Global Signaling Events During Myogenesis.
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_18
2018
Covalent Aurora A regulation by the metabolic integrator coenzyme A
Covalent inhibitors of EGFR family protein kinases induce degradation of human Tribbles 2 (TRIB2) pseudokinase in cancer cells
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.aat7951
New tools for carbohydrate sulfation analysis: heparan sulfate 2-O-sulfotransferase (HS2ST) is a target for small-molecule protein kinase inhibitors
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/BCJ20180265
New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors
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/BCJ20180266
A quantitative and temporal map of proteostasis during heat shock in <i>Saccharomyces cerevisiae</i>
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/c7mo00050b
Understanding protein-drug interactions using ion mobility-mass spectrometry
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.2017.12.013
2017
Plk4 and Aurora A cooperate in the initiation of acentriolar spindle assembly in mammalian oocytes
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.201606077
Evaluation of Parameters for Confident Phosphorylation Site Localization using an Orbitrap Fusion Tribrid Mass Spectrometer
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.7b00337
Local protein kinase A action proceeds through intact holoenzymes
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.aaj1669
Bottom-up elucidation of glycosidic bond stereochemistry
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.6b04998
Label-Free Discovery Array Platform for the Characterization of Glycan Binding Proteins and Glycoproteins
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.6b04122
DOSCATs: Double standards for protein quantification
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/srep45570
2016
KinView: A visual comparative sequence analysis tool for integrated kinome research
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/C6MB00466K
Human CDK18 promotes replication stress signaling and genome stability
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/gkw615
cAMP-dependent protein kinase (PKA) complexes probed by complementary differential scanning fluorimetry and ion mobility-mass spectrometry.
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/BCJ20160648
Analysis of Intrinsic Peptide Detectability via Integrated Label-Free and SRM-Based Absolute Quantitative Proteomics
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.6b00048
Absolute protein quantification of the yeast chaperome under conditions of heat shock.
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.201500503
Applications of ion mobility mass spectrometry for high throughput, high resolution glycan analysis
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.2016.02.003
Dynamic phosphorylation of RelA on Ser42 and Ser45 in response to TNFα stimulation regulates DNA binding and transcription
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.160055
RePLiCal: A QconCAT Protein for Retention Time Standardization in Proteomics Studies
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.5b00988
Direct and Absolute Quantification of over 1800 Yeast Proteins via Selected Reaction Monitoring
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.M115.054288
2015
Evaluation of dimethyl sulfoxide (DMSO) as a mobile phase additive during top 3 label-free quantitative proteomics
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.2015.07.004
In honour of Professor Simon Gaskell's 65th birthday
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.2015.10.013
Mass spectrometry for structural analysis and quantification of the Major Urinary Proteins of the house mouse
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.2015.07.026
Focus on Quantitative Proteomics
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.201570163
Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in <i>Saccharomyces cerevisiae</i>
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.201400527
Protein Structure
Barran, P., Cooper, H., & Eyers, C. (2015). Protein Structure. PROTEOMICS, 15(16), 2731-2732. doi:10.1002/pmic.201570143
The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner
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/BJ20141441
2014
Eukaryotic Elongation Factor 2 Kinase Activity Is Controlled by Multiple Inputs from Oncogenic Signaling
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.01035-14
Peptide scrambling during collision-induced dissociation is influenced by N-terminal residue basicity
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.8b04652
Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer
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.2014.04.015
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
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.6884
Discrimination of epimeric glycans and glycopeptides using IM-MS and its potential for carbohydrate sequencing (vol 6, pg 65, 2014)
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.1901
Quantitative Proteomics
Quantitative Proteomics (2014). (Vol. 1). doi:10.1039/9781782626985
Unblocking the Sink: Improved CID-Based Analysis of Phosphorylated Peptides by Enzymatic Removal of the Basic <i>C</i>-Terminal Residue
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/s13361-013-0770-2
Discrimination of epimeric glycans and glycopeptides using IM-MS and its potential for carbohydrate sequencing
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.1817
Quantitative Proteomics Preface
Eyers, C. E. (2014). Quantitative Proteomics Preface. In QUANTITATIVE PROTEOMICS (Vol. 1, pp. V-VII). Retrieved from https://www.webofscience.com/
The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics
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.1889
2013
ChemInform Abstract: Enzymatic Reactions on Immobilized Substrates
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.201340262
Enzymatic reactions on immobilised substrates
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/c3cs60018a
Attempting to rewrite <i>History</i>: challenges with the analysis of histidine-phosphorylated peptides
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/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
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/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
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.6425
CoPY - Census of the Proteome of Yeast: Quantification of the <i>S</i>. <i>cerevisiae</i> proteome
Lanthaler, K., Holman, S., Lawless, C., Watkins, R., Brownridge, P., Harman, V., . . . Beynon, R. (2013). CoPY - Census of the Proteome of Yeast: Quantification of the <i>S</i>. <i>cerevisiae</i> proteome. In YEAST Vol. 30 (pp. 188). Retrieved from https://www.webofscience.com/
Top-down mass spectrometry for the analysis of combinatorial post-translational modifications
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.21348
2012
Dual purpose <i>S</i>-trityl-linkers for glycoarray fabrication on both polystyrene and gold
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/c2ob26118a
QconCAT Standard for Calibration of Ion Mobility-Mass Spectrometry Systems
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/pr3005327
The N-Methylated Peptide SEN304 Powerfully Inhibits Aβ(1-42) Toxicity by Perturbing Oligomer Formation
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/bi300415v
The use of selected reaction monitoring in quantitative proteomics
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.12.126
Formation of carbohydrate-functionalised polystyrene and glass slides and their analysis by MALDI-TOF MS
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.8.86
The influence of a C-terminal basic residue on peptide fragmentation pathways
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.2012.02.017
Proposal for a common nomenclature for peptide fragment ions generated following sequence scrambling during collision-induced dissociation
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.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
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
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.M111.007633
CONSeQuence: Prediction of Reference Peptides for Absolute Quantitative Proteomics Using Consensus Machine Learning Approaches
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.M110.003384
Diauxic shift-dependent relocalization of decapping activators Dhh1 and Pat1 to polysomal complexes
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/gkr474
Identification of a Lacosamide Binding Protein Using an Affinity Bait and Chemical Reporter Strategy: 14-3-3 ζ
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/ja2034156
MASS SPECTROMETRIC-BASED QUANTITATIVE PROTEOMICS USING SILAC
Lanucara, F., & Eyers, C. E. (2011). MASS SPECTROMETRIC-BASED QUANTITATIVE PROTEOMICS USING SILAC. METHODS IN ENZYMOLOGY, VOL 500, 500, 133-150. doi:10.1016/B978-0-12-385118-5.00008-6
QUANTIFICATION OF PROTEINS AND THEIR MODIFICATIONS USING QCONCAT TECHNOLOGY
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/B978-0-12-385118-5.00007-4
2010
Analysis of Post-translational Modifications by LC-MS/MS
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_5
2009
Rigorous determination of the stoichiometry of protein phosphorylation using mass spectrometry
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.2009.08.009
Lacosamide Isothiocyanate-Based Agents: Novel Agents To Target and Identify Lacosamide Receptors
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/jm9012054
2008
QCAL—a novel standard for assessing instrument conditions for proteome analysis
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.2008.05.019
All systems are go.
Eyers, C. E., & Reamtong, O. (2008). All systems are go.. Genome biology, 9(5), 307. doi:10.1186/gb-2008-9-5-307
Mass Spectrometry to Identify Posttranslational Modifications
Eyers, C. E., & Gaskell, S. J. (n.d.). Mass Spectrometry to Identify Posttranslational Modifications. Unknown Journal, 1-34. doi:10.1002/9780470048672.wecb469
2007
Peptide Detectability following ESI Mass Spectrometry: Prediction using Genetic Programming
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
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
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/BJ20050387
Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
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/ng1531
2003
The characterization of protein post-translational modifications by mass spectrometry
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/ar020143l
Identification of novel phosphorylation sites on <i>Xenopus laevis</i> aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography
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-MCP200
2002
Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways
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/BJ20020916
Identification of a phosphorylation site on skeletal muscle myosin light chain kinase that becomes phosphorylated during muscle contraction
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.2001.2625