Alison E. ASHCROFT

Alison ASHCROFT is Professor of Biomolecular Mass Spectrometry in the Astbury Centre for Structural Molecular Biology and Faculty of Biological Sciences at the University of Leeds. She obtained her Ph.D. in Organic Chemistry from the University of Manchester (UK) and, after post-doctoral work in Switzerland followed by 14 years as a mass spectrometrist in industry, joined the University of Leeds in 1997.
Her research is focussed on using mass spectrometry to study protein folding, function and aggregation, and also mapping the assembly pathways of non-covalently bound macromolecular protein complexes. Of specific interest are membrane proteins, amyloidogenic protein aggregation and virus capsid assembly.
Her current instrumental development interests lie in the use of ion mobility spectrometry coupled to mass spectrometry to separate and characterise co-populated protein species.


Address:

Astbury Centre for Structural Molecular Biology,
Faculty of Biological Sciences,
Astbury Building,
University of Leeds,
Leeds, LS2 9JT , UK.
Mail : a.e.ashcroft(at)leeds.ac.uk
Lab Web page: http://www.personal.leeds.ac.uk/~fbsmaspe/index.html
Personal Web page: http://www.astbury.leeds.ac.uk/people/staffpage.php?StaffID=AEA

Selected Articles:

  1. H. Venter, A. E. Ashcroft, J. N. Keen, P. J. F. Henderson, R. B. Herbert (2002). Molecular dissection of membrane transport proteins: mass spectrometry and sequence determination of the galactose-H+ symport protein, GalP, of Escherichia coli and quantitative assay of the incorporation of [ring-2-13C]histidine and 15NH3. Biochem. J., 363, 243-252.
  2. D. P. Smith, K. Giles, R. H. Bateman, S. E. Radford, A. E. Ashcroft (2007). Monitoring co-populated conformational states during protein folding events using electrospray ionisation-ion mobility spectrometry–mass spectrometry. J. Am. Soc. Mass Spectrom., 18, 2180-2190
  3. D. P. Smith, T. W. Knapman, I. Campuzano, R. W. Malham, J. T. Berryman, S. E. Radford, A. E. Ashcroft (2009). Deciphering drift time measurements from travelling wave ion mobility spectrometry-mass spectrometry studies. European J. Mass Spectrom., 15, 113-130.
  4. L. N. Jones, S. A. Baldwin, P. J. F. Henderson, A. E. Ashcroft (2010). Defining topological features of membrane proteins by electrospray ionisation-mass spectrometry. Rapid Commun. Mass Spectrom., 24, 276-284.
  5. D. P. Smith, S. E. Radford, A. E. Ashcroft (2010). Elongated oligomers in β2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc. Nat. Acad. Sci. USA, 107, 6794-6798.
  6. T. W. Knapman, V. L. Morton, P. G. Stockley, N. J. Stonehouse, A. E. Ashcroft (2010). Determining the topology of macromolecular protein complexes. Rapid Commun. Mass Spectrom., 24, 3033–3042.
  7. A. C. Leney, L. M. McMorran, S. E. Radford, A. E. Ashcroft (2012). Amphipathic polymers facilitate the study of functional membrane proteins in the gas phase. Anal. Chem., 84, 9841-9847.
  8. T. W. Knapman, N. M. Valette, S. L. Warriner, A. E. Ashcroft (2013). Ion mobility spectrometry-mass spectrometry of intrinsically unfolded proteins: trying to put order into disorder. Curr. Anal. Chem., 9, 181-191, 2013.

Selected Reviews:

  1. V. L. Morton, P. G. Stockley, N. J. Stonehouse, A. E. Ashcroft (2008). Insights into virus capsid assembly using non-covalent mass spectrometry. Mass Spectrom. Rev., 27, 575-595.
  2. A. E. Ashcroft (2010). Mass spectrometry and the amyloid problem – how far can we go in the gas phase? (Critical Review). J. Am. Soc. Mass Spectrom., 21, 1087-1096.
  3. L. A. Woods, S. E. Radford, A. E. Ashcroft (2013). Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly. Biochemica Biophysica Acta: Proteins and Proteomics, on-line, doi: 10.1016/j.bbapap.2012.10.002.