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
2024 Awarded the Biochemical Society Centenary Award for 2025.
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