Claire E. Eyers

From Wikipedia, the free encyclopedia

Professor Claire Eyers

Claire Eyers (née Haydon) is a British biological mass spectrometrist who is professor of biological mass spectrometry at the University of Liverpool, where she heads up the Centre for Proteome Research.[1][failed verification] Her research publications list her either as Claire E Haydon (her maiden name) or Claire E Eyers (from 2005).

Early life and education[]

Eyers was born in London and educated at Putney High School[citation needed]. She was awarded a BSc Honours in Biochemistry with Industrial experience Rhône-Poulenc from the University of Bristol in 1998 prior to undertaking postgraduate studies in the MRC PPU[2][failed verification] at the University of Dundee where she was awarded a PhD in 2002 for her work on stress-activated protein kinases with Sir Philip Cohen[citation needed]. Her interests in protein phosphorylation and biological mass spectrometry have subsequently led to a series of professional appointments, including (in 2017) an Invited Member of the Scientific Advisory Group of the Human Proteome Organization (HUPO)[citation needed], the Editorial Board of Scientific Reports (2017–)[citation needed], and as an Executive committee & Trustee of the British Mass Spectrometry Society (2015–), for whom she was also Treasurer between 2016 and 2018[citation needed].

Career and research[]

Following her PhD in Dundee, Eyers joined the group of Professor Natalie Ahn[citation needed]in the USA, and was awarded an Outstanding Postdoctoral Fellow Award (Pacific/Mountain Affiliate) of the American Heart Association (2004)[citation needed], held at the University of Colorado Boulder[citation needed]. Subsequently, in 2005, she returned to the UK to take up a position with Professor Simon Gaskell as Deputy Head of the Michael Barber Centre for Mass Spectrometry at the University of Manchester[citation needed]. Her work in Manchester, a national and international centre of excellence for mass spectrometry best known for the development of fast atom bombardment (FAB)[citation needed], involved the development, refinement and application of strategies for protein quantification by mass spectrometry, and gas-phase characterisation of modified peptides and glycans. During her time in Manchester, she also contributed to securing the first bronze (2011) and subsequently silver (2013) Athena SWAN (Scientific Women's Academic Network) award for the School of Chemistry[citation needed]. In 2007, Eyers was awarded a personal Royal Society Dorothy Hodgkin Fellowship to set up her own research proteomics laboratory,[3][failed verification] and was promoted to Senior Lecturer in 2010[citation needed]. Since 2014, she has been the Professor of Biological Mass Spectrometry in the Faculty of Health and Life Sciences at the University of Liverpool[4][failed verification] and is currently Director of the Centre for Proteome Research.[5] She is currently Research and Impact Lead for the Institute of Integrative Biology at the University of Liverpool[citation needed], a founder member of the Workload Model Working Group, which oversaw a charter Gold ranking Athena SWAN award for the IIB in 2017, a first for the University of Liverpool.[6] Eyers sits on the Selection Committee for L'Oréal-UNESCO For Women in Science[citation needed], Professional Body Memberships and is a member of the Royal Society of Chemistry[citation needed], the American Society for Mass Spectrometry[citation needed], the British Society for Proteome Research (a member of the UK Biosciences Federation)[citation needed], the British Mass Spectrometry Society and the UK Biochemical Society.[7] Her expertise in protein phosphorylation and biological mass spectrometry have resulted in a number of professional appointments[citation needed]. She is currently Chair of BBSRC Committee D.[8] Alongside Professors Sabine Flitsch and Perdita Barran, Eyers is also Co-founder and Scientific Director of Bio-Shape Ltd[citation needed], a company specialising in the analysis of proteins, carbohydrates and their conjugates using mass spectrometry-based methods[citation needed].

Eyers' work in biological mass spectrometry focuses on the global and targeted analysis of post-translational modification on proteins[citation needed]. She has published over 70 research articles, has edited two books ('Quantitative Proteomics' published by RSC Press[9] and 'Histidine Phosphorylation: Methods and Protocols published by Springer Press [10]) and she currently holds two patents.[11] Her most cited publications[citation needed] focus on biochemical, structural, cellular and gas-phase studies of protein phosphorylation,[12] protein kinase complexes[13][14][15] and glycan conformation,[16][17][18] and several highly-accessed reviews[citation needed] on the subject of ion mobility mass spectrometry for biological molecules.[19][20][21][22][23] She is highly cited[citation needed] for her analysis of protein phosphorylation by mass spectrometry,[24][25] and in 2019 work in her lab led to the discovery that non-canonical protein phosphorylation on a broad range of amino acids, including Arg, Asp, Cys, Glu, His and Lys is widespread in human cells.[26] This work potentially opens up an entirely new field of 'non-canonical' protein phosphorylation analysis in prokaryotic and eukaryotic organisms, where protein phosphorylation represents a reversible switch that transmits intracellular signals in response to extracellular factors.[27]

Awards and honours[]

Eyers received the Outstanding Postdoctoral Fellow Award (Pacific/Mountain Affiliate) of the American Heart Association (2004),[citation needed] when working in the laboratory of Professor Natalie Ahn, at the University of Colorado Boulder. Eyers is the 2020 British Society for Proteome Research Named Lecturer.[28][failed verification] In her role as the BSPR Lecturer, Eyers will be presenting a series of lectures during 2020 and 2021 focused on phosphoproteomics and post translational modification analysis of proteins.

References[]

  1. ^ "Centre for Proteome Research – University of Liverpool".
  2. ^ "MRC PPUU – University of Dundee".
  3. ^ "Faculty of Health and Life Sciences – University of Liverpool".
  4. ^ "Faculty of Health and Life Sciences – University of Liverpool".
  5. ^ "Centre for Proteome Research – University of Liverpool".
  6. ^ "Athena SWAN – Institute of Integrative Biology – University of Liverpool".
  7. ^ "BMSS Committee | BMSS".
  8. ^ "BBSRC Panel D; BBSRC".
  9. ^ Quantitative Proteomics; RSC Press. New Developments in Mass Spectrometry. 2014. doi:10.1039/9781782626985. ISBN 978-1-84973-808-8.
  10. ^ Quantitative Proteomics; RSC Press. Methods in Molecular Biology. 2077. Springer. 2020. doi:10.1007/978-1-4939-9884-5. ISBN 978-1-4939-9883-8. S2CID 207988391.
  11. ^ "Google Scholar".
  12. ^ Ferries S, Perkins S, Brownridge PJ, Campbell A, Eyers PA, Jones AR, Eyers CE (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. PMID 28741359.
  13. ^ Vonderach M, Byrne DP, Barran PE, Eyers PA, Eyers CE (2019). "DNA Binding and Phosphorylation Regulate the Core Structure of the NF-κB p50 Transcription Factor". Journal of the American Society for Mass Spectrometry. 30 (1): 128–138. Bibcode:2019JASMS..30..128V. doi:10.1007/s13361-018-1984-0. PMC 6318249. PMID 29873020.
  14. ^ Smith FD, Esseltine JL, Nygren PJ, Veesler D, Byrne DP, Vonderach M, Strashnov I, Eyers CE, Eyers PA, Langeberg LK, Scott JD (2017). "Local protein kinase A action proceeds through intact holoenzymes". Science. 356 (6344): 1288–1293. Bibcode:2017Sci...356.1288S. doi:10.1126/science.aaj1669. PMC 5693252. PMID 28642438.
  15. ^ Byrne DP, Vonderach M, Ferries S, Brownridge PJ, Eyers CE, Eyers PA (2016). "cAMP-dependent protein kinase (PKA) complexes probed by complementary differential scanning fluorimetry and ion mobility-mass spectrometry". Biochemical Journal. 473 (19): 3159–75. doi:10.1042/BCJ20160648. PMC 5095912. PMID 27444646.
  16. ^ Gray CJ, Migas LG, Barran PE, Pagel K, Seeberger PH, Eyers CE, Boons GJ, Pohl NL, Compagnon I, Widmalm G, Flitsch SL (2019). "Advancing Solutions to the Carbohydrate Sequencing Challenge". Journal of the American Chemical Society. 141 (37): 14463–14479. doi:10.1021/jacs.9b06406. PMID 31403778.
  17. ^ Both P, Green AP, Gray CJ, Sardzík R, Voglmeir J, Fontana C, Austeri M, Rejzek M, Richardson D, Field RA, Widmalm G, Flitsch SL, Eyers CE (2014). "Discrimination of epimeric glycans and glycopeptides using IM-MS and its potential for carbohydrate sequencing". Nature Chemistry. 6 (1): 65–75. Bibcode:2014NatCh...6...65B. doi:10.1038/nchem.1817. PMID 24345949. S2CID 205292342.
  18. ^ Gray CJ, Schindler B, Migas LG, Pičmanová M, Allouche AR, Green AP, Mandal S, Motawia MS, Sánchez-Pérez R, Bjarnholt N, Moller BL, Rijs AM, Barran PE, Compagnon I, Eyers CE, Flitsch SL (2017). "Bottom-Up Elucidation of Glycosidic Bond Stereochemistry" (PDF). Analytical Chemistry. 89 (8): 4540–4549. doi:10.1021/acs.analchem.6b04998. hdl:2066/174591. PMID 28350444.
  19. ^ Eyers CE, Vonderach M, Ferries S, Jeacock K, Eyers PA (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. PMID 29331721.
  20. ^ Gray CJ, Thomas B, Upton R, Migas LG, Eyers CE, Barran PE, Flitsch SL (2016). "Applications of ion mobility mass spectrometry for high throughput, high resolution analysis". Biochimica et Biophysica Acta. 1860 (8): 1688–1709. doi:10.1016/j.bbagen.2016.02.003. PMID 26854953.
  21. ^ Lanucara F, Holman SW, Gray CJ, Eyers CE (2014). "The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics". Nature Chemistry. 6 (4): 281–294. Bibcode:2014NatCh...6..281L. doi:10.1038/nchem.1889. PMID 24651194.
  22. ^ Gonzalez-Sanchez MB, Lanucara F, Hardman GE, Eyers CE (2014). "Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer". International Journal of Mass Spectrometry. 367: 28–34. Bibcode:2014IJMSp.367...28G. doi:10.1016/j.ijms.2014.04.015. PMC 4375673. PMID 25844054.
  23. ^ Gonzalez-Sanchez MB, Lanucara F, Helm M, Eyers CE (2013). "Attempting to rewrite History: challenges with the analysis of histidine-phosphorylated peptides". Biochemical Society Transactions. 41 (4): 1089–1095. doi:10.1042/bst20130072. PMID 23863184.
  24. ^ Haydon CE, Eyers PA, Aveline-Wolf LD, Resing KA, Maller JL, Ahn NG (2003). "Identification of novel phosphorylation sites on Xenopus laevis 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. PMID 12885952.
  25. ^ Haydon CE, Watt PW, Morrice N, Knebel A, Gaestel M, Cohen P (2003). "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. PMID 11795875.
  26. ^ Hardman G, Perkins S, Brownridge PJ, Clarke CJ, Byrne DP, Campbell AE, Kalyuzhnyy A, Myall A, Eyers PA, Jones AR, Eyers CE (2019). "Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation". The EMBO Journal. 38 (21): e100847. doi:10.15252/embj.2018100847. PMC 6826212. PMID 31433507.
  27. ^ Hunter T (2012). "Why nature chose phosphate to modify proteins". Philosophical Transactions of the Royal Society B: Biological Sciences. 367 (1602): 2513–6. doi:10.1098/rstb.2012.0013. PMC 3415839. PMID 22889903.
  28. ^ "British Society for Proteome Research; BSPR".
Retrieved from ""