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] Her research publications list her either as Claire E Haydon (her maiden name) or Claire E Eyers (from 2005).
Following her PhD in Dundee, Eyers joined the group of Professor Natalie Ahn in the USA, and was awarded an Outstanding Postdoctoral Fellow Award (Pacific/Mountain Affiliate) of the American Heart Association (2004), held at the University of Colorado Boulder.[3] 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,[4][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]
In 2022, Eyers was appointed to the Liverpool City Region Local Enterprise Partnership (LEP) Health and Life Sciences sub-board which aims to support the growth of the Health and Life Sciences sectors in the local area as well as providing support and access to the extensive knowledge and expertise across the Liverpool City region.[28][29]
^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. PMID24651194.
^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. PMID23863184.
^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. PMID11795875.
