Sheena E Radford, OBE BSc PhD FMedSci FRS
PhD, University of Cambridge, 1987
BSc (Biochemistry), University of Birmingham, 1984
2021- Royal Society Research Professor
2014- Astbury Professor of Biophysics, University of Leeds
2012-2021 Director, Astbury Centre for Structural Molecular Biology, University of Leeds
2009-2012 Deputy Director, Astbury Centre for Structural Molecular Biology, University of Leeds
2004-2008 Co-founder and Co-director University Interdisciplinary Institute in Molecular Biophysics
2000- Professor of Structural Molecular Biology, University of Leeds
1998-2000 Reader in Structural Molecular Biology, University of Leeds
1996-2001 Supernumerary Research Fellow, Linacre College, Oxford
1995-1998 Lecturer, School of Biochemistry and Molecular Biology, University of Leeds
1992-1995 Senior Research Fellow, Linacre College, Oxford
1991-1995 Royal Society University Research Fellow, Oxford Centre for Molecular Sciences
1990-1992 EPA-Cephalosporin Junior Research Fellow, Linacre College, Oxford
1988-1991 Post-doctoral research, Inorganic Chemistry Laboratory, University of Oxford
1988 Post-doctoral research, Dyson Perrins Lab, University of Oxford
2022 Doctor Honoris causa Honorary Degree from the University of Liege.
2021 Royal Society 5-year Research Professorship.
2020 Membership of the Academia Europaea (MAE);
2020 Officer of the Order of the British Empire (OBE) for services to Molecular Biology;
2019 Election to Honorary Fellowship of St John’s College, Cambridge;
2017 Elected 2018 Fellow of the Biophysical Society for "Leadership in protein biophysics";
2015 The Rita and John Cornforth Award of the Royal Society of Chemistry, jointly with Professor Alison Ashcroft (University of Leeds);
2014 Honorary membership of the British Biophysical Society;
2014 Elected Fellow of the Royal Society (FRS);
2013 The Protein Society – Carl Branden award;
2010 Fellow of the Academy of Medical Sciences;
2009 Hites Award, American Society for Mass Spectrometry (joint with Professor Alison Ashcroft);
2007 Fellow of the European Molecular Biology Organisation (EMBO);
2005 Royal Society of Chemistry Astra-Zeneca prize: Proteins and Peptides;
2003 Fellow of the Royal Society of Chemistry;
2001-2006 BBSRC Professorial Fellow;
1996 The Biochemical Society - Colworth Medal;
1984 The University Science Faculty prize - University of Birmingham;
1983 Departmental prize – University of Birmingham;
1982 Departmental prize – University of Birmingham;
Link to all publications ->
- The folding of lysozyme involves partially structured intermediates and multiple pathways. Radford, S.E., Dobson, C.M. & Evans, P.A. (1992) Nature 358, 302-307
- Detection of transient protein folding populations by mass spectrometry. Miranker, A., Robinson, C.V., Radford, S.E., Aplin, R.T. & Dobson, C.M. (1993) Science 262, 896-899
- Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Booth, D.R., Sunde, M., Bellotti, V., Robinson, C.V., Hutchinson, W.L., Fraser, P.E., Hawkins, P.N., Dobson, C.M., Radford, S.E., Blake, C.C.F. & Pepys, M.B. (1997) Nature, 385, 787-793
- Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes. Aggeli, A., Bell, M., Boden, N., Keen, J., Knowles, P.F., McLeish, T.C.B., Pitkeathly, M. & Radford, S.E. (1997) Nature, 386, 259-262
- Rapid folding with and without populated intermediates in the homologous four helix proteins Im7 and Im9. Ferguson, N., Capaldi, A.P., James. R., Kleanthous, C. & Radford, S.E. (1999) J. Mol. Biol. 286, 1597-1608
- Partially unfolded states of β2-microglobulin and amyloidosis in vitro. McParland, V.J., Kad, N.M., Kalverda, A.P., Brown, A., Kerwin-Jones, P., Hunter, M.G., Sunde, M. & Radford, S.E. (2000) Biochemistry, 39, 8735-8746
- Ultra-rapid mixing experiments reveal that Im7 folds via an on-pathway intermediate. Capaldi, A.P., Shastry, M.C.R., Roder, H. & Radford, S.E. (2001) Nature Struct. Biol., 8, 68-72.
- Im7 folding mechanism: misfolding on the path to the native state. Capaldi, A.P., Kleanthous, C. & Radford, S.E. (2002) Nature Struct. Biol., 9, 209-216.
- Structural properties of an amyloid precursor of β2-microglobulin. McParland, V.J., Kalverda, A.P., Homans, S.W & Radford, S.E. Nature Struct. Biol. (2002), 9, 326-331
- Pulling geometry defines the mechanical resistance of a β-sheet protein. Brockwell, D.J., Paci, E., Zinober, R.C., Beddard, G.S., Olmsted, P.D., Smith, D.A., Perham, R.N. & Radford, S.E. (2003) Nature Struct. Biol., 10, 731-737
- Mechanically unfolding the small, topologically simple protein L. Brockwell, D.J., Beddard, G.S., Paci, E., West, D.K., Olmsted, P.D., Smith, D.A.M. & Radford, S.E. (2005) Biophys. J., 89, 506-519
- Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid. Gosal, W.S., Morten, I.J., Hewitt, E.W., Smith, D.A., Thomson, N.H. & Radford, S.E. (2005) J. Mol. Biol. 351, 850-864
- Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Jahn, T.R., Parker, M.J., Homans, S.W. & Radford, S.E. (2006) Nature Struct. and Molec. Biol. 13, 195-201
- Systematic analysis of nucleation-dependent polymerisation reveals new insights into the mechanism of amyloid self-assembly. Xue, W.F., Homans, S.W. & Radford, S.E. (2008) Proc. Natl. Acad. Sci. USA 105, 8926-8931
- The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints. Friel. C.T., Smith, D.A., Vendruscolo, M., Gsponer, J. & Radford, S.E. (2009) Nature Struct. and Molec. Biol. 16, 318-324
- Fibril fragmentation enhances amyloid cytotoxicity. Xue, W.F., Hellewell, A.L., Gosal, W.S., Homans, S.W., Hewitt, E.W. & Radford, S.E. (2009) J. Biol. Chem. 284, 34272-34282
- Elongated oligomers in β2-microglobulin amyloid assembly revealed by ion mobility spectrometry mass spectrometry. Smith, D.P., Radford, S.E. & Ashcroft, A.E. (2010) Proc. Natl. Acad. Sci. USA, 107, 6794-6798
- The transition state for the folding of an outer membrane protein. Huysmans, G., Baldwin, S.A., Brockwell, D.J. & Radford, S.E. (2010) Proc. Natl. Acad. Sci. USA, 107, 4099-4104
- Conformational conversion during amyloid formation at atomic resolution. Eichner, T., Kalverda, A.P., Thompson, G.S., Homans, S.W. & Radford, S.E. (2011) Molecular Cell 41, 161-172
- Ligand binding to distinct states diverts aggregation of an amyloid-forming protein. Woods, L.A., Platt, G.W., Hellewell, A.L., Hewitt, E.W., Homans, S.W., Ashcroft, A.E., Radford, S.E. (2011) Nature Chem. Biol. 7, 730-739
- Direct three-dimensional visualisation of membrane disruption by amyloid fibrils Milanesi, L., Sheynis, T., Xue, W.F., Orlova, E.V., Hellewell, A.L., Jelinek, R., Hewitt, E.W., Radford, S.E. & Saibil, H.R. (2012) Proc. Natl. Acad. Sci. USA, 109, 50, 20455-20460
- Site-specific identification of the A fibril-glycosaminoglycan interaction site using solid state NMR Madine, J., Pandya, M.J., Hicks, M.R., Rodger, A., Yates, E.A., Radford, S.E. & Middleton, D.A. (2012) Angewandte Chemie, 51, 13140-13143
- Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly Karamanos, T.K., Kalverda, A.P., Thompson, G.S & Radford S.E. (2014) Molecular Cell, 55, 214-226
- Energy landscapes of functional proteins are inherently risky Gershenson, A., Gierasch, L.M.*, Pastore, A. & Radford, S.E. (2014) Nature Chem. Biol., 10, 884-891
- How TriC folds tricky proteins Zhuravleva, A. * & Radford, S.E. * (2014) Cell 159, 1251-1252
- Screening and classifying small molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry Young, L.M., Saunders, J.C., Mahood, R.A., Revill, C.H., Foster R.J., Tu, L.-H., Raleigh, D.P., Radford, S.E. & Ashcroft, A.E. (2015) Nature Chemistry, 7, 1, 73-81
- Amyloid fibres: inert end- stage aggregates or key players in disease? Tipping, K.W., Van Oosten-Hawle, P., Hewitt, E.W. & Radford, S.E. (2015) Trends in Biochem. Sci., 40, 719-727
- Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM Iadanza, M.G., Higgins, A.J., Schiffrin, R., Calabrese, A.N., Brockwell, D.J., Ashcroft, A.E., Radford, S.E. & Ranson, N.A. (2016) Nature Comms., 7, 12865
- pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers Tipping, K.W., Karamanos, T.K., Jakhria, T., Iadanza, M.G., Goodchild, S.C., Tuma, R., Ranson, N.A., Hewitt, E.W. & Radford, S.E. (2015) PNAS, 112, 5691-5696
- Skp is a multivalent chaperone of outer membrane proteins Schiffrin, R., Calabrese, A.N., Devine, P.W.A., Harris, S.A., Ashcroft, A.E., Brockwell, D.J. & Radford, S.E. (2016) Nat. Struct. Mol. Biol. 23, 786-793
- Substrate protein folds while it is bound to the ATP-independent chaperone Spy Stull, F., Koldewey, P., Humes, J.R., Radford, S.E. & Bardwell, J.C.A. (2016) Nat. Struct. Mol. Biol. 1, 53-59
- An in vivo platform for identifying inhibitors of protein aggregation Saunders, J.C., Young, L.M., Mahood, R.A., Revill, C.H., Foster, R.J., Jackson, M.P., Smith, D.A.M., Ashcroft, A.E., Brockwell, D.J. & Radford, S.E. (2016) Nature Chem. Biol., 12, 94-101
- A new era for understanding amyloid structures and disease Iadanza, M.G., Jackson, M.P., Hewitt, E.W., Ranson, N.A. & Radford, S.E. (2018) Nature Rev. Mol. Cell. Biol., 19, 755–773
- The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism Iadanza. M.G., Silvers, R., Boardman, J., Smith, H.I., Karamanos, T.K., Debelouchina, G.T., Su, Y., Griffin, R.G., Ranson, N.A., & Radford, S.E. (2018) Nature Comms., 9, 4517 – 4527
- Structural mapping of oligomeric intermediates in an amyloid assembly pathway Karamanos, T.K., Jackson, M.P., Calabrese, A.N., Goodchild, S.C., Cawood, E.E., Thompson, G.S., Kalverda, A.P., Hewitt, E.W., & Radford, S.E. (2019) eLife 8, e46574