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Professor Simon J. Gaskell

Biography

BSc,PhD, Bristol; MRC Postdoctoral Fellow, University of Glasgow; Principal Research Officer, Tenovus Institute for Cancer Research, University of Wales College of Medicine; Professor of Experimental Medicine and Pharmacology, Baylor College of Medicine, Houston (USA).

Research interests

The research interests of my group, in the Michael Barber Centre for Mass Spectrometry, involve the development and application of state-of-the-art mass spectrometry, with particular reference to applications in the biomedical sciences.  In recent years, a major effort has been devoted to proteomics, an area of “post-genome science” that has been enabled by the international efforts to sequence the genomes of many organisms, including man.  Proteomics involves the qualitative and quantitative determination of the protein compositions of cells, with attention to the characterisation of the protein/protein complexes that are the real biochemical machinery.  The Michael Barber Centre hosts, in collaboration with the Department of Biomolecular Sciences, the Leukaemia Research Fund National Proteomics Facility.  The strongly interdisciplinary nature of our research is further emphasised by our participation in the Consortium for Post-Genome Science, a heavily funded programme involving UMIST, the Universities of Liverpool and Manchester, and the Daresbury Laboratory.  Within the Consortium, we lead the Third-Generation Proteomics project which is funding the purchase of a 9.4 tesla Fourier-transform ion cylotron resonance mass spectrometer.  

The chemist’s contribution to research such as this must be based on a clear understanding of the instrumentation used for mass spectrometry and of the gas-phase ion chemistry that is integral to this suite of analytical techniques.  Thus, for example, we are concerned with aspects of instrument development (such as the exploitation of surface-induced decomposition in tandem mass spectrometry).  In addition, much effort is directed towards studies of peptide ion fragmentation and this has enabled us to propose general mechanisms of charge-directed ion cleavages.

Based on such fundamental understanding of our analytical chemical techniques, we are able to contribute to the elucidation of problems of fundamental biological and clinical importance.  Working with colleagues at the Manchester Royal Infirmary, for example, we have shown for the first time that the oxidation of low density lipoprotein (LDL) from human blood may result in the formation of lipid-protein conjugates that may influence the uptake of LDL by the arterial wall.  In collaboration with researchers from the University of Houston and the University of North Carolina, Chapel Hill, we have studied the inhibition of a critical functional protein from Escherichia coli by synthetic antibiotics. 

Recent publications - for a full list, see the Publications page

1. Wright JC, Sugden D, Francis-McIntyre S, Riba-Garcia I, Gaskell SJ, Grigoriev IV, Baker SE, Beynon RJ, Hubbard SJ. Exploiting proteomic data for genome annotation and gene model validation in Aspergillus niger.  BMC Genomics 2009, in press.
2. Hart SR, Lau KW, Hao Z, Broadhead R, Portman N, Hühmer A, Gull K, McKean PG,
   Hubbard SJ, Gaskell SJ.  Analysis of the trypanosome flagellar proteome using a combined electron transfer/collisionally activated dissociation strategy.  J Am Soc Mass Spectrom 2009; 20: 167-175.
3. Doherty M, Hammond D, Clague M, Gaskell SJ, Beynon RJ.  Turnover of the human proteome: determination of intracellular stability by dynamic SILAC.  J Proteome Res 2009; 8: 104-112.
4. Riba Garcia I,  Giles K, Bateman RH, Gaskell SJ. Studies of peptide a- and b-type fragment ions using stable isotope labeling and integrated ion mobility/tandem mass spectrometry.  J Am Soc Mass Spectrom 2008; 19: 1781-1787.
5. Tyler RK, Chu MLH, Johnson H, McKenzie EA, Gaskell SJ, Eyers PA.  Phosphoregulation of human Mps1 kinase.  Biochem J 2000; 417:173-181.
6. Laurent N, Haddoub R, Voglmeir J, Wong SCC, Gaskell SJ, Flitsch S.  SPOT synthesis of peptide arrays on self-assembled monolayers and their evaluation as enzyme substrates.  ChemBioChem 2008; 9: 2592-2596.
7. Hart SR, Gaskell SJ.  Methods of proteome analysis: challenges and opportunities.  SEB Exp Biol Ser 2008; 61: 37-64.
8. de la Luz-Hernández KR, Rojas-del Calvo L, Rabasa-Legón Y, Lage-Castellanos A, Castillo-Vitlloch A, Díaz J, Gaskell S.  J Proteomics 2008; 71: 133-147.
9. Eyers CE, Simpson DM, Wong SCC, Beynon RJ, Gaskell SJ. QCAL - a novel standard for assessing instrument conditions for protein analysis. J Am Soc Mass Spectrom 2008; 19: 1275-1280.
10. Johnson H, Wong SCC, Simpson DM, Beynon RJ, Gaskell SJ. Protein quantification by selective isolation and fragmentation of isotopic pairs using FT-ICR MS.  J Am Soc Mass Spectrom 2008; 19: 973-977.
11. Riba-Garcia I, Giles K, Bateman RH, Gaskell SJ.  Evidence for structural variants of a- and b-type peptide fragment Ions using combined ion mobility/mass spectrometry.  J Am Soc Mass Spectrom 2008; 19: 609-613.
12. Laurent N, Voglmeir J, Wright A, Blackburn J, Pham NT, Wong SCC, Gaskell SJ, Flitsch SL.  Enzymatic glycosylation of peptide arrays on gold surfaces.  ChemBioChem 2008; 9: 883-887.
13. Robertson DHL, Wong, SCC, Beynon RJ, Hurst JL, Gaskell SJ.  Observation of heterogeneous gene products by FT-ICR MS. J Am Soc Mass Spectrom 2008; 19: 103-110.