Prof Sheena Radford, FMedSci, FRS

BSc, Birmingham, 1984; PhD, Cambridge, 1987.
Astbury Professor of Biophysics
School of Molecular and Cellular Biology

Contact: Astbury 10.122a, +44(0) 113 34 33170, email address for  

You can read more about Prof Radford, FMedSci, FRS's interests here:

Figure 1: (SER)

Figure 2: (SER)

Research Interests

Mechanisms of protein folding and misfolding in vitro and in vivo

The molecular details of how proteins fold from the linear amino acid sequence to their unique three-dimensional structures is one of the major challenges in biochemistry today. Although it has been known for more than forty years that proteins can fold to their native structures spontaneously in vitro, how this is achieved is still not understood in any great detail. The problem has recently become even more fascinating by the discovery that folding in the cell is is assisted by chaperone proteins and that misfolding events in vivo are responsible for several diseases.

Research into folding takes a multidisciplinary approach that crosses the boundaries between biochemistry, chemistry, medicine and physics and focuses on three major themes. The first uses an array of approaches to determine how the family of all-helical bacterial immunity proteins fold. In particular, the shape of the folding energy landscape, the structure of intermediates and the nature of the barriers that must be overcome to find the unique 3D fold of these proteins is being studied. In a parallel project we are investigating the role of protein misfolding in the onset of the amyloidogenic disease, haemodialysis-related amyloidosis. This disease affects more than 700,000 patients world-wide and is caused by the aggregation of the all-b-sheet protein b2-microglobulin into protein fibrils. We aim to elucidate the molecular mechanism of this, and other, diseases and to design therapies based on rational design or screening approaches. We are also developing new approaches to study folding. These involve using very fast methods of measuring folding on nsec and msec timescales, analysing the unfolding of proteins using the atomic force microscope, and watching the folding and unfolding of individual protein molecules in solution using single molecule fluorescence methods.

Our research integrates with activities within FBS in  Integrative Membrane Biology; Structural Molecular Biology and Neuroscience

Watch a lecture by Professor Radford discussing her work and celebrating her FRS award. Go to

One of the most fascinating questions in biology is how proteins are able to fold and assemble into complex, functional entities given just the information provided by the amino acid sequence. A related, equally important facet of the same fundamental question is how protein misfolding can lead to cellular dysfunction and disease. These issues are the major focus of my research and have been tackled using a broad range of techniques including protein chemistry, structural molecular biology and sophisticated biophysical methods.

Current major projects include:

  • Mechanism(s) of protein misfolding and assembly into amyloid

  • Membrane protein folding mechanisms and role of chaperones and the BAM complex

  • Stabilising proteins of therapeutic and industrial interest against aggregation

  • Method development (MS, NMR, single molecule methods)

Detailed research programme

  1. Mechanism(s) of protein mis-folding and assembly into amyloid

    A major project in the group focuses on using our knowledge of protein folding methods to develop new understandings of how proteins misfold and cause disease. Specifically, we are exploring the mechanism of onset of several human amyloid diseases, including Alzheimer’s, Machado-Joseph disease, type II diabetes and haemodialysis-related amyloidosis, caused by A?, ataxin 3, amylin and ?2-microglobulin, respectively. Our approach combines structural analysis of the species formed during aggregation obtained using fluorescence, single molecule methods (FRET and FCS), mass spectrometry and NMR, with detailed analysis of the kinetics of aggregation. In collaboration with Eric Hewitt and Patricija van Oosten Hawle (Astbury Centre for Structural Molecular Biology), analysis of the effects of the different species identified on cellular function and in C elegans are being investigated. Our aim is to derive a detailed molecular mechanism of the aggregation process from monomer to amyloid and to use the power of combinatorial chemistry combined with cell biological assays and structural analysis to find new therapies for these, and other, amyloid diseases.

    Highlights over recent years in this area have included using NMR and other biophysical methods to map the energy landscape for the formation of amyloid fibrils of ?2m (Fig. 1) of different morphological types, and analysis of the structure of amyloid fibrils using cryo-electron microscopy, with Helen Saibil (Birkbeck College, London) and solid state NMR (with Robert Griffin (Massachusetts Institute of Technology, USA). In addition, we have used solution NMR methods to determine the structure of the amyloidogenic precursor of ?2m and have shown that this species is not only highly amyloidogenic in itself, but it is also able to convert the non-amyloidogenic wild-type protein into a conformation able to self-assemble into amyloid at neutral pH. Reported in Molecular Cell in 2011 and 2014, this work revealed that conformational conversion is not restricted to prions but, instead, many proteins may possess the ability to convert a benign conformer to an amyloidogenic form by bimolecular collision. We are now continuing this work, extending the ideas found to other protein systems and using NMR to obtained more direct structural insights into the mechanism by which conformational conversion occurs, as well as the conformational properties of higher order oligomeric states.

    In parallel with this work, in a long-standing collaboration with Alison Ashcroft (Astbury Centre for Structural Molecular Biology), we are developing ion mobility mass spectrometry (IMS) coupled with mass spectrometry (MS) to identify and individually characterise the structural properties, population and stability of different oligomeric species of aggregation-prone sequences that are co-populated in the early stages of amyloid assembly. In addition, we are developing this approach to search for small molecules able to inhibit amyloid assembly and to determine their mechanism of action in detail. (Fig. 2). Published in Nature Chemistry, the methods developed, combined with an active collaboration with Dr Richard Foster (Medicinal Chemist, Astbury Centre for Structural Molecular Biology), provide novel small molecules and fragments for screening experiments:

    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., FosterR.J., Tu, L.-H., Raleigh, D.P., Radford, S.E. & Ashcroft, A.E. (2015) Nature Chemistry, 1, 73-81

    Fig. 1. An array of fibril morphologies formed from similar protein sequences. With thanks to Claire Sarell for this image.

    Fig. 2. IMS-MS reveals oligomeric intermediates in ?2m amyloid assembly. With thanks to David Smith for this image.

  2. Membrane protein folding mechanisms and role of chaperones and the BAM complex

    Although we have learned much about protein folding mechanisms in recent years, principally through the development of new methods and studies of simple and experimentally tractable systems, our understanding of how proteins fold rapidly and efficiently to their unique native conformation both in vitro and in vivo remains an exciting challenge. In order to develop new and more detailed models of protein folding, we have studied the folding of the small helical bacterial immunity proteins (principally Im7 and Im9) for the last decade.  By combining stopped flow methods, ultra-rapid mixing experiments, single molecule fluorescence (FRET) and NMR analysis we have shown that Im7 folds through an intermediate that is on-pathway to the native state and has a distorted three helical structure stabilised in a large part by non-native inter-helical interactions (Friel et al, 2009, Nature Struct. Mol. Biol. 16, 318-324).

    Combined with molecular dynamics simulations (in collaboration with Emanuele Paci (Astbury Centre for Structural Molecular Biology), Michele Vendruscolo (University of Cambridge) and Joerg Gsponer (University of British Columbia, Canada)) this work culminated in the description of the entire folding landscape of Im7 in atomistic detail (Fig. 3), placing Im7 amongst the best studied examples of how a protein folds.

    Our most recent research on protein folding has now moved to the challenging field of membrane protein folding, focusing on bacterial outer membrane (OM) proteins. In collaboration with Dr David Brockwell (Astbury Centre for Structural Molecular Biology), we are investigating how OM proteins are able to cross the inner membrane, traverse the periplasm (aided by chaperones) and assemble into bacterial outer membrane. Our first inroads into this field (published and highlighted: Huysmans et al, 2010, PNAS 107, 4099-4104)exploited phi-value analysis to reveal a structural model of the transition state for folding of the E.coli outer membrane protein, PagP. The results revealed a complex, tilted insertion mechanism, previously predicted for membrane insertion of this class of proteins (Fig. 4). They also revealed that PagP folds on parallel folding pathways, the portioning between which depends on the lipid-to-protein ratio and the nature of the lipid. These results highlight the complexity of studying membrane protein folding in which both the sequence of the protein chain and environment of the lipid bilayer are crucial in determining the progress of folding. Moreover they highlight potentials of classical protein folding methods for the analysis of how this class of proteins folds.  Current work is now building on these first insights by exploring the role of the molecular chaperones SKP and SurA and the BAM complex in assisting the folding of OM proteins: Nature Structural and Molecular Biology (2016) and Nature Communications (2016).

    Fig. 3 The folding mechanism of Im7 (Friel et al., Nature Struct. and Molec. Biol. (2009))

    Fig. 4 Folding of the OM protein PagP (Husymans et al., PNAS (2010)). Thanks to Gerard Husymans for creating this image.

  3. Stabilising proteins of therapeutic and industrial interest against aggregation

    Most recently, we have exploited our fundamental knowledge of Im7 folding to practical benefits, by developing a system using directed evolution that is able to select for proteins with enhanced stability in vivo whilst avoiding any evolutionary pressure for function. Combining our skills with the microbiological expertise of Jim Bardwell (Michigan) we developed a ?-lactamase host-guest system to select for new Im7 sequences with enhanced stability. The resulting sequences were then analysed for their stability, folding and functional properties. The results (published in Molecular Cell in 2009) showed that the vast majority of mutations that enhance stability occur in residues that are required for function. In addition, we found that several of these residues were those we had identified previously as forming non-native interactions during folding. These results support the view that protein sequences are highly frustrated (i.e. function compromises stability and folding capability). They also demonstrate the utility of the ?-lactamase system we had developed to generate proteins that retain function, but are optimised for stability. Further developing this system has enabled us to use the split ?-lactamase system to screen for protein sequences that are aggregation-prone and to screen for small molecules able to protect proteins from aggregation:

    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.

    Our current efforts are focused on developing this, and other approaches (including fragment-based and other design strategies), to screen for protein sequence hot spots that cause aggregation of proteins, particularly those of interest and relevance to the biopharmaceutical industry, as well as to screen for small molecules able to arrest their aggregation.

    Finally, in collaboration with Dr David Brockwell (Astbury Centre for Structural Molecular Biology) and Dr Nikil Kapur (School of Mechanical Engineering, University of Leeds), we are examining how flow fields enhance, or cause, aggregation by flow-induced protein deformations (PNAS, 2017).

    Fig. 5. A bipartite assembly for screening for proteins with enhanced stability. From Foit et al. Mol. Cell (2009)

  4. Method development (MS, NMR, single molecule methods)

    Major developments in instrumentation have played a key role in increasing in our understanding of folding and aggregation mechanisms to date. Future developments in these fields will also require innovative approaches that cross the boundaries between disciplines. We have been involved in many exciting collaborations to fulfil this aim. To date we have built apparatus capable of measuring fast reactions in folding using ultra-rapid mixing detected by fluorescence, and, together with Roman Tuma (Astbury Centre for Structural Molecular Biology), instruments capable of single molecule measurements using both FRET and FCS. Developing MS methods continues to be an aim of our laboratory (in collaboration with Professors Alison Ashcroft and Frank Sobott (both of the Astbury Centre for Structural Molecular Biology)). In addition, developments in NMR methods remain a mainstay of our laboratory activities, whilst, in collaboration with David Brockwell (Astbury Centre for Structural Molecular Biology), we are involved in some very exciting developments in the use of the AFM for force measurements of protein unfolding and protein binding. More information about these projects can be found on the websites of our collaborators on their Astbury web pages.

For further details about the Radford laboratory, people involved, molecular images and available opportunities please see


Faculty Research and Innovation

Studentship information

Undergraduate project topics:

  • Protein folding and disease
    Keywords: Amyloid plaques, electron microscopy, protein misfolding, protein engineering, drug design (Laboratory)
  • Novel approaches to the study of single molecule protein folding
    Keywords: Atomic force microscopy, fluorescence, mutagenesis, protein engineering (Laboratory)
  • Exploring the key features of protein folding using protein engineering
    Keywords: PCR, protein expression, protein folding, circular dichroism (CD), structure elucidation (Laboratory)

Postgraduate studentship areas:

  • Mechanisms of Protein Folding and Misfolding in vitro and in vivo

See also:

Modules taught

BIOC2301 - Intermediate Integrated Biochemistry
BIOC3111/12 B - Protein Dynamics
BIOC3160 - Laboratory/Literature/Computing Research Project
BIOC3221/22/BIOL3210 b - ATU - Folding & Diseases
BIOL3399 - Extended Research Project Preparation
BIOL5382M - Extended Research Project
BIOL5394M - Specialised Research Topics and Skills
BIOW5905X - Membrane proteins

Centre membership: The Astbury Centre for Structural Molecular Biology

Group Leader Prof Sheena Radford, FMedSci, FRS  (Astbury Professor of Biophysics)

Mechanisms of protein folding and misfolding in vitro and in vivo 

Dr David Brockwell  (Associate Professor)

The effects of force on proteins and their complexes; extremophilic proteins; membrane protein folding and folding factors. 

Dr Antonio Calabrese  (Research Fellow)

Dr Matthew Iadanza  (Research Fellow)

Dr Matthew Jackson  (Research Fellow)

Dr Theodoros Karamanos  (Visiting Research Fellow)

Mr G Nasir Khan  (Research Lab Manager/ CD Facility Manager)

Dr Amit Kumar  (Research Fellow)

Dr Lydia Young  (Wellcome Trust ISSF Fellow)

Dr Esther Martin  (Visitor )

Mrs Helen McAllister  (PA to Professor Sheena Radford)

Dr Maya Pandya  (Research Fellow)


Lucy Barber (Primary supervisor) 50% FTE
Jessica Ebo (Primary supervisor) 50% FTE
Anna Higgins (Primary supervisor) 50% FTE
James Horne (Primary supervisor) 50% FTE
Julia Humes (Primary supervisor) 50% FTE
Hugh Smith (Primary supervisor) 50% FTE
Madeleine Brown (Co-supervisor) 50% FTE
Samuel Bunce (Co-supervisor) 33% FTE
Emma Cawood (Co-supervisor) 50% FTE
Chi Chau (Co-supervisor) 25% FTE
Owen Cornwell (Co-supervisor) 50% FTE
Michael Davies (Co-supervisor) 50% FTE
Chloe Dickinson (Co-supervisor) 50% FTE
Ciaran Doherty (Co-supervisor) 35% FTE
Sarah Good (Co-supervisor) 50% FTE
Maia Harvey (Co-supervisor) 30% FTE
Patrick Knight (Co-supervisor) 50% FTE
Atenas Posada Borbon (Co-supervisor) 50% FTE

Fessl T, Watkins D, Oatley P, Allen WJ, Corey RA, Horne J, Baldwin SA, Radford SE, Collinson I, Tuma R Dynamic action of the Sec machinery during initiation, protein translocation and termination. eLife 7, 2018
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Townsend D, Hughes E, Akien G, Stewart KL, Radford SE, Rochester D, Middleton DA Epigallocatechin-3-gallate remodels apolipoprotein A-I amyloid fibrils into soluble oligomers in the presence of heparin Journal of Biological Chemistry, 2018
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Willis LF, Kumar A, Dobson J, Bond NJ, Lowe D, Turner R, Radford SE, Kapur N, Brockwell DJ Using extensional flow to reveal diverse aggregation landscapes for three IgG1 molecules Biotechnology and Bioengineering 115 1216-1225, 2018
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Hethershaw EL, Adamson PJ, Smith KA, Goldsberry WN, Pease RJ, Radford SE, Grant PJ, Ariëns RAS, Maurer MC, Philippou H The role of barrels 1 and 2 in the enzymatic activity of factor XIII‐A Journal of Thrombosis and Haemostasis, 2018
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Berry A, Radford SE RICHARD NELSON PERHAM Biographical Memoirs of Fellows of the Royal Society, 2018

Doherty CPA, Young LM, Karamanos TK, Smith HI, Jackson MP, Radford SE, Brockwell DJ A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides. Protein science : a publication of the Protein Society, 2018
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Knight PD, Karamanos TK, Radford SE, Ashcroft AE Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1 European Journal of Mass Spectrometry 24 129-140, 2018
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Martin EM, Jackson MP, Gamerdinger M, Gense K, Karamonos TK, Humes JR, Deuerling E, Ashcroft AE, Radford SE Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins Journal of Biological Chemistry 293 8554-8568, 2018
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Calabrese AN, Radford SE Mass spectrometry-enabled structural biology of membrane proteins Methods, 2018
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Schiffrin B, Brockwell DJ, Radford SE Outer membrane protein folding from an energy landscape perspective BMC Biology 15, 2017
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Schiffrin B, Calabrese AN, Higgins AJ, Humes JR, Ashcroft AE, Kalli AC, Brockwell DJ, Radford SE Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding Journal of Molecular Biology 429 3776-3792, 2017
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Calabrese AN, Jackson SM, Jones LN, Beckstein O, Heinkel F, Gsponer J, Sharples D, Sans M, Kokkinidou M, Pearson AR, Radford SE, Ashcroft AE, Henderson PJF Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry Analytical Chemistry 89 8844-8852, 2017
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Devine PWA, Fisher HC, Calabrese AN, Whelan F, Higazi DR, Potts JR, Lowe DC, Radford SE, Ashcroft AE Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS Journal of The American Society for Mass Spectrometry 28 1855-1862, 2017
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Stewart KL, Hughes E, Yates EA, Middleton DA, Radford SE Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils Journal of Molecular Biology 429 2449-2462, 2017
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Young LM, Ashcroft AE, Radford SE Small molecule probes of protein aggregation Current Opinion in Chemical Biology 39 90-99, 2017
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Stewart KL, Radford SE Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation Biophysical Reviews 9 405-419, 2017
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Horne JE, Radford SE, Brockwell DJ Complementary cross-linking and fluorescence studies of outer membrane protein biogenesis in vitro, 2017

Radford SE The challenges and opportunities of understanding protein folding and misfolding in health and disease, 2017

Humes JR, Higgins AJ, Brockwell DJ, Radford SE Identifying the contributions of the different domains within SurA on outer member protein folding, 2017

Higgins AJ, Iadanza MG, Schiffrin B, Calabrese AN, Humes JR, Brockwell DJ, Ashcroft AE, Ranson NA, Radford SE Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM, 2017

Young LM, Tu LH, Raleigh D, Ashcroft AE, Radford SE Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers Chemical Science 8 5030-5040, 2017
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Dobson J, Kumar A, Willis LF, Tuma R, Higazi DR, Turner R, Lowe DC, Ashcroft AE, Radford SE, Kapur N, Brockwell DJ Inducing protein aggregation by extensional flow Proceedings of the National Academy of Sciences of the United States of America 114 4673-4678, 2017
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Horne JE, Brockwell DJ, Radford SE Fretting about Outer Membrane Protein Biogenesis. How Exactly do they Fold?, 2017

Watkinson TG, Calabrese AN, Ault JR, Radford SE, Ashcroft AE FPOP-LC-MS/MS Suggests Differences in Interaction Sites of Amphipols and Detergents with Outer Membrane Proteins Journal of the American Society for Mass Spectrometry 28 50-55, 2017
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Dobson CL, Devine PWA, Phillips JJ, Higazi DR, Lloyd C, Popovic B, Arnold J, Buchanan A, Lewis A, Goodman J, van der Walle CF, Thornton P, Vinall L, Lowne D, Aagaard A, Olsson LL, Ridderstad Wollberg A, Welsh F, Karamanos TK, Pashley CL, Iadanza MG, Ranson NA, Ashcroft AE, Kippen AD, Vaughan TJ, Radford SE, Lowe DC Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo Scientific Reports 6, 2016
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Iadanza MG, Higgins AJ, Schiffrin B, Calabrese AN, Brockwell DJ, Ashcroft AE, Radford SE, Ranson NA Lateral opening in the intactβ-barrel assembly machinery captured by cryo-EM Nature Communications 7, 2016
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Schiffrin B, Calabrese AN, Devine PWA, Harris SA, Ashcroft AE, Brockwell DJ, Radford SE Skp is a multivalent chaperone of outer-membrane proteins Nature Structural and Molecular Biology 23 786-793, 2016
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Stewart KL, Hughes E, Yates EA, Akien GR, Huang TY, Lima MA, Rudd TR, Guerrini M, Hung SC, Radford SE, Middleton DA Atomic Details of the Interactions of Glycosaminoglycans with Amyloid-β Fibrils Journal of the American Chemical Society 138 8328-8331, 2016
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Horne JE, Radford SE A growing toolbox of techniques for studyingβ-barrel outer membrane protein folding and biogenesis Biochemical Society Transactions 44 802-809, 2016
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Allen WJ, Corey RA, Oatley P, Sessions RB, Baldwin SA, Radford SE, Tuma R, Collinson I Two-way communication between SecY and SecA suggests a brownian ratchet mechanism for protein translocation eLife 5, 2016
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Young LM, Saunders JC, Mahood RA, Revill CH, Foster RJ, Ashcroft AE, Radford SE ESI-IMS-MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules. Methods 95 62-69, 2016
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Pashley CL, Hewitt EW, Radford SE Comparison of the aggregation of homologousβ<inf>2</inf>-microglobulin variants reveals protein solubility as a key determinant of amyloid formation Journal of Molecular Biology 428 631-643, 2016
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Iadanza MG, Jackson MP, Radford SE, Ranson NA MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images Scientific Reports 6, 2016
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Saunders JC, Young LM, Mahood RA, Jackson MP, Revill CH, Foster RJ, Smith DA, Ashcroft AE, Brockwell DJ, Radford SE An in vivo platform for identifying inhibitors of protein aggregation Nature Chemical Biology 12 94-101, 2016
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Stull F, Koldewey P, Humes JR, Radford SE, Bardwell JCA Substrate protein folds while it is bound to the ATP-independent chaperone Spy Nature Structural and Molecular Biology 23 53-58, 2016
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Watkinson TG, Calabrese AN, Giusti F, Zoonens M, Radford SE, Ashcroft AE Systematic analysis of the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry International Journal of Mass Spectrometry 391 54-61, 2015
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Rajabi K, Ashcroft AE, Radford SE Mass spectrometric methods to analyze the structural organization of macromolecular complexes. Methods (San Diego, Calif.) 89 13-21, 2015
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Calabrese AN, Ault JR, Radford SE, Ashcroft AE Using hydroxyl radical footprinting to explore the free energy landscape of protein folding. Methods 89 38-44, 2015
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Young LM, Mahood RA, Saunders JC, Tu LH, Raleigh DP, Radford SE, Ashcroft AE Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry. Analyst 140 6990-6999, 2015
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Karamanos TK, Kalverda AP, Thompson GS, Radford SE Mechanisms of amyloid formation revealed by solution NMR Progress in Nuclear Magnetic Resonance Spectroscopy 88-89 86-104, 2015
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Tipping KW, Karamanos TK, Jakhria T, Iadanza MG, Goodchild SC, Tuma R, Ranson NA, Hewitt EW, Radford SE pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers Proceedings of the National Academy of Sciences 112 5691-5696, 2015
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Scarff CA, Almeida B, Fraga J, Macedo-Ribeiro S, Radford SE, Ashcroft AE Examination of ataxin-3 (atx-3) aggregation by structural mass spectrometry techniques: A rationale for expedited aggregation upon polyglutamine (polyQ) expansion Molecular and Cellular Proteomics 14 1241-1253, 2015
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Farrance OE, Paci E, Radford SE, Brockwell DJ Extraction of accurate biomolecular parameters from single-molecule force spectroscopy experiments ACS Nano 9 1315-1324, 2015
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Chen Y, Radford SE, Brockwell DJ Force-induced remodelling of proteins and their complexes Current Opinion in Structural Biology 30 89-99, 2015
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Tu L-H, Young L, Wong AG, Ashcroft AE, Radford S, Raleigh DP Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactions Biochemistry 54 666-676, 2015
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Calabrese AN, Watkinson TG, Henderson PJF, Radford SE, Ashcroft AE Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase Analytical Chemistry 87 1118-1126, 2015
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Tipping KW, van Oosten-Hawle P, Hewitt EW, Radford SE Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease? Trends in Biochemical Sciences 40 719-727, 2015
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Scarff CA, Ashcroft AE, Radford SE Characterization of amyloid oligomers by electrospray ionization-ion mobility spectrometry-mass spectrometry (ESI-IMS-MS) In Methods in Molecular Biology, 2015
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Rajabi K, Reuther J, Deuerling E, Radford SE, Ashcroft AE A comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometry Protein Science 24 1282-1291, 2015
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Young LM, Saunders JC, Mahood RA, Revill CH, Foster RJ, Tu L-H, Raleigh DP, Radford SE, Ashcroft AE Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry Nature Chemistry 7 73-81, 2015
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Jakhria T, Hellewell AL, Porter MY, Jackson MP, Tipping KW, Xue WF, Radford SE, Hewitt EW β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes Journal of Biological Chemistry 289 35781-35794, 2014
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McMorran LM, Brockwell DJ, Radford SE Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date? Archives of Biochemistry and Biophysics 564 265-280, 2014
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Zhuravleva A, Radford SE How tric folds tricky proteins Cell 159 1251-1252, 2014
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Gershenson A, Gierasch LM, Pastore A, Radford SE Energy landscapes of functional proteins are inherently risky Nature Chemical Biology 10 884-891, 2014
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Giusti F, Rieger J, Catoire LJ, Qian S, Calabrese AN, Watkinson TG, Casiraghi M, Radford SE, Ashcroft AE, Popot J-L Synthesis, characterization and applications of a perdeuterated amphipol. J Membr Biol 247 909-924, 2014
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Sarell CJ, Karamanos TK, White SJ, Bunka DH, Kalverda AP, Thompson GS, Barker AM, Stockley PG, Radford SE Distinguishing closely related amyloid precursors using an RNA aptamer The Journal of Biological Chemistry 289 26859-26871, 2014
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Goodchild SC, Sheynis T, Thompson R, Tipping KW, Xue W-F, Ranson NA, Hewitt EW, Radford SE, Beales PA β-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH PLoS ONE 9, 2014
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Karamanos TK, Kalverda AP, Thompson GS, Radford SE Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly Molecular Cell 55 214-226, 2014
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Su Y, Eddy MT, Debelouchina GT, Andreas LB, Griffin RG, Sarell CJ, Pashley CL, Radford SE Secondary structure in the core of amyloid fibrils formed from humanβm and its truncated variant Δn6 Journal of the American Chemical Society 136 6313-6325, 2014
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Rimratchada S, Paci E, McLeish TCB, Radford SE The role of high-dimensional diffusive search, stabilization, and frustration in protein folding Biophysical Journal 106 1729-1740, 2014
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Preston GW, Radford SE, Wilson AJ, Ashcroft AE Analysis of amyloid nanostructures using photo-cross-linking: in situ comparison of three widely used photo-cross-linkers ACS Chemical Biology 9 761-768, 2014
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Leney AC, Pashley CL, Scarff CA, Radford SE, Ashcroft AE Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry Molecular BioSystems 10 412-420, 2014
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Young LM, Cao P, Raleigh DP, Ashcroft AE, Radford SE Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors Journal of the American Chemical Society 136 660-670, 2013
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Xue W-F, Radford SE An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior Biophysical Journal 105 2811-2819, 2013
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Figueiredo AM, Whittaker SB-M, Knowling SE, Radford SE, Moore GR Conformational dynamics is more important than helical propensity for the folding of the all alpha-helical protein Im7 Protein Science 22 1722-1738, 2013
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Sarell CJ, Stockley PG, Radford SE Assessing the causes and consequences of co-polymerization in amyloid formation Prion 7 359-368, 2013
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McMorran LM, Bartlett AI, Huysmans GHM, Radford SE, Brockwell DJ Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP. J Mol Biol 425 3178-3191, 2013
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Sheynis T, Friediger A, Xue W-F, Hellewell AL, Tipping KW, Hewitt EW, Radford SE, Jelinek R Aggregation modulators interfere with membrane interactions ofβ2-microglobulin fibrils Biophysical Journal 105 745-755, 2013
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Ndlovu H, Ashcroft AE, Radford SE, Harris SA Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects BEILSTEIN JOURNAL OF NANOTECHNOLOGY 4 429-440, 2013

Scarff CA, Sicorello A, Tome RJL, Macedo-Ribeiro S, Ashcroft AE, Radford SE A tale of a tail: Structural insights into the conformational properties of the polyglutamine protein ataxin-3 INTERNATIONAL JOURNAL OF MASS SPECTROMETRY 345 63-70, 2013

Woods LA, Radford SE, Ashcroft AE Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly. Biochim Biophys Acta 1834 1257-1268, 2013
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Sarell CJ, Woods LA, Su Y, Debelouchina GT, Ashcroft AE, Griffin RG, Stockley PG, Radford SE Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors. J Biol Chem 288 7327-7337, 2013
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Young L, Ndlovu H, Knapman TW, Harris SA, Radford SE, Ashcroft AE Monitoring oligomer formation from self-aggregating amylin peptides using ESI-IMS-MS International Journal for Ion Mobility Spectrometry 16 29-39, 2013
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Farrance OE, Hann E, Kaminska R, Housden NG, Derrington SR, Kleanthous C, Radford SE, Brockwell DJ A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein. PLoS Biol 11 e1001489-, 2013
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Young L, Ndlovu H, Knapman TW, Harris SA, Radford SE, Ashcroft AE Monitoring oligomer formation from self-aggregating amylin peptides using ESI-IMS-MS International Journal for Ion Mobility Spectrometry 1-11, 2013
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Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE, Middleton DA Site-specific identification of an Aβ fibril-heparin interaction site by using solid-state NMR spectroscopy Angewandte Chemie - International Edition 51 13140-13143, 2012
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Milanesi L, Sheynis T, Xue W-F, Orlova EV, Hellewell AL, Jelinek R, Hewitt EW, Radford SE, Saibil HR Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc Natl Acad Sci U S A 109 20455-20460, 2012
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Leney AC, McMorran LM, Radford SE, Ashcroft AE Amphipathic polymers enable the study of functional membrane proteins in the gas phase. Anal Chem 84 9841-9847, 2012
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Hodkinson JP, Radford SE, Ashcroft AE The role of conformational flexibility inβ<inf>2</inf>-microglobulin amyloid fibril formation at neutral pH Rapid Communications in Mass Spectrometry 26 1783-1792, 2012
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Radford SE, Weissman JS Special issue: the molecular and cellular mechanisms of amyloidosis. J Mol Biol 421 139-141, 2012

Preston GW, Radford SE, Ashcroft AE, Wilson AJ Covalent cross-linking within supramolecular peptide structures. Anal Chem 84 6790-6797, 2012
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Morrissey B, Leney AC, Rêgo AT, Phan G, Allen WJ, Verger D, Waksman G, Ashcroft AE, Radford SE The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS Molecular and Cellular Proteomics 11, 2012
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Kang L, Moriarty GM, Woods LA, Ashcroft AE, Radford SE, Baum J N-terminal acetylation ofα-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer Protein Science 21 911-917, 2012
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Huysmans GHM, Radford SE, Baldwin SA, Brockwell DJ Malleability of the folding mechanism of the outer membrane protein PagP: parallel pathways and the effect of membrane elasticity. J Mol Biol 416 453-464, 2012
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Pashley CL, Morgan GJ, Kalverda AP, Thompson GS, Kleanthous C, Radford SE Conformational properties of the unfolded state of Im7 in nondenaturing conditions. J Mol Biol 416 300-318, 2012
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Ndlovu H, Ashcroft AE, Radford SE, Harris SA Effect of sequence variation on the mechanical response of amyloid fibrils probed by steered molecular dynamics simulation. Biophys J 102 587-596, 2012
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Valette NM, Radford SE, Harris SA, Warriner SL Phosphorylation as a tool to modulate aggregation propensity and to predict fibril architecture. Chembiochem 13 271-281, 2012
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Eichner T, Radford SE Understanding the complex mechanisms ofβ2-microglobulin amyloid assembly. FEBS J 278 3868-3883, 2011
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Woods LA, Platt GW, Hellewell AL, Hewitt EW, Homans SW, Ashcroft AE, Radford SE Ligand binding to distinct states diverts aggregation of an amyloid-forming protein NAT CHEM BIOL 7 730-739, 2011

Smith DP, Woods LA, Radford SE, Ashcroft AE Structure and Dynamics of Oligomeric Intermediates in beta(2)-Microglobulin Self-Assembly BIOPHYS J 101 1238-1247, 2011

Eichner T, Radford SE A Diversity of Assembly Mechanisms of a Generic Amyloid Fold MOL CELL 43 8-18, 2011

Leney AC, Phan G, Allen W, Verger D, Waksman G, Radford SE, Ashcroft AE Second Order Rate Constants of Donor-Strand Exchange Reveal Individual Amino Acid Residues Important in Determining the Subunit Specificity of Pilus Biogenesis J AM SOC MASS SPECTR 22 1214-1223, 2011

Knowling S, Bartlett AI, Radford SE Dissecting key residues in folding and stability of the bacterial immunity protein 7 PROTEIN ENG DES SEL 24 517-523, 2011

Berryman JT, Radford SE, Harris SA Systematic Examination of Polymorphism in Amyloid Fibrils by Molecular-Dynamics Simulation BIOPHYS J 100 2234-2242, 2011

Teoh CL, Pham CLL, Todorova N, Hung A, Lincoln CN, Lees E, Lam YH, Binger KJ, Thomson NH, Radford SE, Smith TA, Muller SA, Engel A, Griffin MDW, Yarovsky I, Gooley PR, Howlett GJ A Structural Model for Apolipoprotein C-II Amyloid Fibrils: Experimental Characterization and Molecular Dynamics Simulations J MOL BIOL 405 1246-1266, 2011

Deville K, Gold VAM, Robson A, Whitehouse S, Sessions RB, Baldwin SA, Radford SE, Collinson I The Oligomeric State and Arrangement of the Active Bacterial Translocon J BIOL CHEM 286 4659-4669, 2011

Gilson MK, Radford SE Protein folding and binding: from biology to physics and back again CURR OPIN STRUC BIOL 21 1-3, 2011

Eichner T, Kalverda AP, Thompson GS, Homans SW, Radford SE Conformational Conversion during Amyloid Formation at Atomic Resolution MOL CELL 41 161-172, 2011

Porter MY, Routledge KE, Radford SE, Hewitt EW Characterization of the response of primary cells relevant to dialysis-related amyloidosis toβ2-microglobulin monomer and fibrils. PLoS One 6 e27353-, 2011
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Hoffmann A, Nettels D, Clark J, Borgia A, Radford SE, Clarke J, Schuler B Quantifying heterogeneity and conformational dynamics from single molecule FRET of diffusing molecules: recurrence analysis of single particles (RASP) PHYS CHEM CHEM PHYS 13 1857-1871, 2011

Chen MM, Bartlett AI, Nerenberg PS, Friel CT, Hackenberger CPR, Stultz CM, Radford SE, Imperiali B Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation P NATL ACAD SCI USA 107 22528-22533, 2010

Debelouchina GT, Platt GW, Bayro MJ, Radford SE, Griffin RG Intermolecular Alignment in beta(2)-Microglobulin Amyloid Fibrils J AM CHEM SOC 132 17077-17079, 2010

Valette NM, Radford SE, Harris SA, Warriner SL Studying peptide aggregation with a series of phosphopeptide variants ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY 240, 2010

Debelouchina GT, Platt GW, Bayro MJ, Radford SE, Griffin RG Magic Angle Spinning NMR Analysis of beta(2)-Microglobulin Amyloid Fibrils in Two Distinct Morphologies J AM CHEM SOC 132 10414-10423, 2010

Smith DP, Ashcroft AE, Radford SE Hemodialysis-Related Amyloidosis, 2010

Ladner CL, Chen M, Smith DP, Platt GW, Radford SE, Langen R Stacked Sets of Parallel, In-register beta-Strands of beta(2)-Microglobulin in Amyloid Fibrils Revealed by Site-directed Spin Labeling and Chemical Labeling J BIOL CHEM 285 17137-17147, 2010

Pugh SD, Gell C, Smith DA, Radford SE, Brockwell DJ Single-Molecule Studies of the Im7 Folding Landscape J MOL BIOL 398 132-145, 2010

Smith DP, Radford SE, Ashcroft AE Elongated oligomers in beta(2)-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry P NATL ACAD SCI USA 107 6794-6798, 2010

Bartlett AI, Radford SE Desolvation and Development of Specific Hydrophobic Core Packing during Im7 Folding J MOL BIOL 396 1329-1345, 2010

Huysmans GHM, Baldwin SA, Brockwell DJ, Radford SE The transition state for folding of an outer membrane protein P NATL ACAD SCI USA 107 4099-4104, 2010

Xue WF, Hellewell AL, Hewitt EW, Radford SE Fibril fragmentation in amyloid assembly and cytotoxicity When size matters PRION 4 20-25, 2010

Foit L, Morgan GJ, Kern MJ, Steimer LR, von Hacht AA, Titchmarsh J, Warriner SL, Radford SE, Bardwell JCA Optimizing Protein Stability In Vivo MOL CELL 36 861-871, 2009

Xue WF, Hellewell AL, Gosal WS, Homans SW, Hewitt EW, Radford SE Fibril Fragmentation Enhances Amyloid Cytotoxicity J BIOL CHEM 284 34272-34282, 2009

Grant CA, Brockwell DJ, Radford SE, Thomson NH Tuning the Elastic Modulus of Hydrated Collagen Fibrils BIOPHYS J 97 2985-2992, 2009

Sadler DP, Petrik E, Taniguchi Y, Pullen JR, Kawakami M, Radford SE, Brockwell DJ Identification of a Mechanical Rheostat in the Hydrophobic Core of Protein L J MOL BIOL 393 237-248, 2009

Knowling SE, Figueiredo AM, Whittaker SBM, Moore GR, Radford SE Amino Acid Insertion Reveals a Necessary Three-Helical Intermediate in the Folding Pathway of the Colicin E7 Immunity Protein Im7 J MOL BIOL 392 1074-1086, 2009

Platt GW, Radford SE Glimpses of the molecular mechanisms of beta(2)-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape FEBS LETT 583 2623-2629, 2009

Radford SE Structural insights into the self-assembly mechanism of amyloid fibrils ABSTR PAP AM CHEM S 238, 2009

Xue WF, Homans SW, Radford SE Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis Protein Engineering Design and Selection 22 489-496, 2009
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Berryman JT, Radford SE, Harris SA Thermodynamic Description of Polymorphism in Q- and N-Rich Peptide Aggregates Revealed by Atomistic Simulation BIOPHYS J 97 1-11, 2009

Routledge KE, Tartaglia GG, Platt GW, Vendrusco M, Radford SE Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming Protein J MOL BIOL 389 776-786, 2009

Bartlett AI, Radford SE An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms NAT STRUCT MOL BIOL 16 582-588, 2009

White HE, Hodgkinson JL, Jahn TR, Cohen-Krausz S, Gosal WS, Muller S, Orlova EV, Radford SE, Saibil HR Globular Tetramers of beta(2)-Microglobulin Assemble into Elaborate Amyloid Fibrils J MOL BIOL 389 48-57, 2009

Eichner T, Radford SE A Generic Mechanism of beta(2)-Microglobulin Amyloid Assembly at Neutral pH Involving a Specific Proline Switch J MOL BIOL 386 1312-1326, 2009

Friel CT, Smith DA, Vendruscolo M, Gsponer J, Radford SE The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints NAT STRUCT MOL BIOL 16 318-324, 2009

Debelouchina GT, Bayro MJ, Platt GW, Radford SE, Griffin RG Solid-state NMR Investigation of b2-Microglobulin Fibril Structure and Dynamics, 2009

Hodkinson JP, Jahn TR, Radford SE, Ashcroft AE HDX-ESI-MS Reveals Enhanced Conformational Dynamics of the Amyloidogenic Protein beta(2)-Microglobulin upon Release from the MHC-1 J AM SOC MASS SPECTR 20 278-286, 2009

Smith DP, Knapman TW, Campuzano I, Malham RW, Berryman JT, Radford SE, Ashcroft AE Deciphering drift time measurements from travelling wave ion mobility spectrometry-mass spectrometry studies EUR J MASS SPECTROM 15 113-130, 2009

Platt GW, Xue WF, Homans SW, Radford SE Probing Dynamics within Amyloid Fibrils Using a Novel Capping Method ANGEW CHEM INT EDIT 48 5705-5707, 2009

Madine J, Jack E, Stockley PG, Radford SE, Serpell LC, Middleton DA Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20-29 of Amylin Revealed by Solid-State NMR and X-ray Fiber Diffraction J AM CHEM SOC 130 14990-15001, 2008

Verger D, Rose RJ, Paci E, Costakes G, Daviter T, Hultgren S, Remaut H, Ashcroft AE, Radford SE, Waksman G Structural Determinants of Polymerization Reactivity of the P pilus Adaptor Subunit PapF STRUCTURE 16 1724-1731, 2008

Rose RJ, Verger D, Daviter T, Remaut H, Paci E, Waksman G, Ashcroft AE, Radford SE Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry P NATL ACAD SCI USA 105 12873-12878, 2008

Xue WF, Homans SW, Radford SE Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly P NATL ACAD SCI USA 105 8926-8931, 2008

Jahn TR, Tennent GA, Radford SE A common beta-sheet architecture underlies in vitro and in vivo beta(2)-microglobulin amyloid fibrils J BIOL CHEM 283 17279-17286, 2008

Platt GW, Routledge KE, Homans SW, Radford SE Fibril growth kinetics reveal a region of beta(2)-microglobulin important for nucleation and elongation of aggregation J MOL BIOL 378 251-263, 2008

Rose RJ, Welsh TS, Waksman G, Ashcroft AE, Radford SE, Paci E Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics J MOL BIOL 375 908-919, 2008

Jahn TR, Radford SE β<inf>2</inf>Microglobulin, 2008

Jahn TR, Radford SE Folding versus aggregation: Polypeptide conformations on competing pathways ARCH BIOCHEM BIOPHYS 469 100-117, 2008

Khatri BS, Byrne K, Kawakami M, Brockwell DJ, Smith DA, Radford SE, McLeish TCB Internal friction of single polypeptide chains at high stretch FARADAY DISCUSS 139 35-51, 2008

Smith DP, Anderson J, Plante J, Aschroft AE, Radford SE, Wilson AJ, Parker MJ Trifluoromethyldiazirine: an effective photo-induced cross-linking probe for exploring amyloid formation, 2008

Smith DP, Giles K, Bateman RH, Radford SE, Ashcroft AE Monitoring copopulated conformational states during protein folding events using Electrospray ionization-ion mobility spectrometry-mass spectrometry J AM SOC MASS SPECTR 18 2180-2190, 2007

Bunka DHJ, Mantle BJ, Morten IJ, Tennent GA, Radford SE, Stockley PG Production and characterization of RNA aptamers specific for amyloid fibril epitopes., 2007
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Bunka DHJ, Mantle BJ, Morten IJ, Tennent GA, Radford SE, Stockley PG Production and characterization of RNA aptamers specific for amyloid fibril epitopes J BIOL CHEM 282 34500-34509, 2007

Huysmans GHM, Radford SE, Brockwell DJ, Baldwin SA The N-terminal helix is a post-assembly clamp in the bacterial outer membrane protein PagP J MOL BIOL 373 529-540, 2007

Morten IJ, Gosal WS, Radford SE, Hewitt EW Investigation into the role of macrophages in the formation and degradation of beta(2)-microglobulin amyloid fibrils J BIOL CHEM 282 29691-29700, 2007

Nagalingam AC, Radford SE, Warriner SL Avoidance of epimerization in the synthesis of peptide thioesters using Fmoc protection SYNLETT 2517-2520, 2007

Morton VL, Friel CT, Allen LR, Paci E, Radford SE The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9 J MOL BIOL 371 554-568, 2007

Borysik AJ, Morten IJ, Radford SE, Hewitt EW Specific glycosaminoglycans promote unseeded amyloid formation from beta(2)-microglobulin under physiological conditions KIDNEY INT 72 174-181, 2007

Linse S, Cabaleiro-Lago C, Xue WF, Lynch I, Lindman S, Thulin E, Radford SE, Dawson KA Nucleation of protein fibrillation by nanoparticles P NATL ACAD SCI USA 104 8691-8696, 2007

Hann E, Kirkpatrick N, Kleanthous C, Smith DA, Radford SE, Brockwell DJ The effect of protein complexation on the mechanical stability of Im9 BIOPHYS J 92 L79-L81, 2007

Whittaker SBM, Spence GR, Grossmann JG, Radford SE, Moore GR NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7 J MOL BIOL 366 1001-1015, 2007

Brockwell DJ, Radford SE Intermediates: ubiquitous species on folding energy landscapes? CURR OPIN STRUC BIOL 17 30-37, 2007

Mathai M, Radford SE, Holland P Progressive glycosylation of albumin and its effect on the binding of homocysteine may be a key step in the pathogenesis of vascular damage in diabetes mellitus MED HYPOTHESES 69 166-172, 2007

Le Duff CS, Whittaker SBM, Radford SE, Moore GR Characterisation of the conformational properties of urea-unfolded Im7: Implications for the early stages of protein folding J MOL BIOL 364 824-835, 2006

Smith AM, Jahn TR, Ashcroft AE, Radford SE Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry J MOL BIOL 364 9-19, 2006

Radford SE BIOL 7 - Life on a knife edge: Tipping the balance between folding and aggregation ABSTR PAP AM CHEM S 232 897-897, 2006

Tezuka-Kawakami T, Gell C, Brockwell DJ, Radford SE, Smith DA Urea-induced unfolding of the immunity protein Im9 monitored by spFRET BIOPHYS J 91 L42-L44, 2006

Kawakami M, Byrne K, Brockwell DJ, Radford SE, Smith DA Viscoelastic study of the mechanical unfolding of a protein by AFM BIOPHYS J 91 L16-L18, 2006

Jack E, Newsome M, Stockley PG, Radford SE, Middleton DA The organization of aromatic side groups in an amyloid fibril probed by solid-state H-2 and F-19 NMR spectroscopy J AM CHEM SOC 128 8098-8099, 2006

Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism MOL CELL 22 831-842, 2006

Radford SE GroEL: More than just a folding cage CELL 125 831-833, 2006

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Jahn TR, Parker MJ, Homans SW, Radford SE Amyloid formation under physiological conditions proceeds via a native-like folding intermediate NAT STRUCT MOL BIOL 13 195-201, 2006

Cobos ES, Radford SE Sulfate-induced effects in the on-pathway intermediate of the bacterial immunity protein Im7 BIOCHEMISTRY-US 45 2274-2282, 2006

Myers SL, Jones S, Jahn TR, Morten IJ, Tennent GA, Hewitt EW, Radford SE A systematic study of the effect of physiological factors on beta 2-microglobulin amyloid formation at neutral pH BIOCHEMISTRY-US 45 2311-2321, 2006

Gsponer J, Hopearuoho H, Whittaker SBM, Spence GR, Moore GR, Paci E, Radford SE, Vendruscolo M Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7 P NATL ACAD SCI USA 103 99-104, 2006

West DK, Brockwell DJ, Olmsted PD, Radford SE, Paci E Mechanical resistance of proteins explained using simple molecular models BIOPHYS J 90 287-297, 2006

Masca S, Rodriguez-Mendieta IR, Friel CT, Radford SE, Smith DAM A detailed evaluation of the performance of microfluidic T-mixers using fluorescence and ultra-violet resonance Raman spectroscopy Review of Scientific Instruments 77, 2006

Morten IJ, Radford SE, Hewitt EW Investigation into the role of lysosomes in dialysis related amyloidosis IMMUNOLOGY 116 63-63, 2005

Jahn TR, Radford SE The Yin and Yang of protein folding FEBS Journal 272 5962-5970, 2005
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Radford SE, Gosal WS, Platt GW Towards an understanding of the structural molecular mechanism of beta(2)-microglobulin amyloid formation in vitro BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1753 51-63, 2005

Hackenberger CPR, Friel CT, Radford SE, Imperiali B Semisynthesis of a glycosylated lm7 analogue for protein folding studies Journal of the American Chemical Society 127 12882-12889, 2005
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Gosal WS, Morten IJ, Hewitt EW, Smith DA, Thomson NH, Radford SE Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J Mol Biol 351 850-864, 2005
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Brockwell DJ, Beddard GS, Paci E, West DK, Olmsted PD, Smith DA, Radford SE Mechanically unfolding the small, topologically simple protein L BIOPHYS J 89 506-519, 2005

Kawakami M, Byrne K, Khatri BS, McLeish TCB, Radford SE, Smith DAM Viscoelastic measurements of single molecules on a millisecond time scale by magnetically driven oscillation of an atomic force microscope Langmuir 21 4765-4722, 2005
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Rodriguez-Mendieta IR, Spence GR, Gell C, Radford SE, Smith DA Ultraviolet resonance Raman studies reveal the environment of tryptophan and tyrosine residues in the native and partially folded states of the E colicin-binding immunity protein Im7 BIOCHEMISTRY-US 44 3306-3315, 2005

Maxwell KL, Wildes D, Zarrine-Afsar A, de los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ERG, Bemporad F, Qiu LL, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai YW, Hagen SJ, Serrano L, Oliveberg M, Raleigh DP, Wittung-Stafshede P, Radford SE, Jackson SE, Sosnick TR, Marqusee S, Davidson AR, Plaxco KW Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins Protein Science 14 602-616, 2005
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Plattt GW, McParland VJ, Kalverda AP, Homans SW, Radford SE Dynamics in the unfolded state of beta(2)-microglobulin studied by NMR J MOL BIOL 346 279-294, 2005

Cranz-Mileva S, Friel CT, Radford SE Helix stability and hydrophobicity in the folding mechanism of the bacterial immunity protein Im9 PROTEIN ENG DES SEL 18 41-50, 2005

Friel CT, Beddard GS, Radford SE Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design J MOL BIOL 342 261-273, 2004

Kawakami M, Byrne K, Khatri B, McLeish TCB, Radford SE, Smith DAM Viscoelastic Properties of Single Polysaccharide Molecules Determined by Analysis of Thermally Driven Oscillations of an Atomic Force Microscope Cantilever Langmuir 20 9299-9303, 2004
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Spence GR, Capaldi AP, Radford SE Trapping the on-pathway folding intermediate of Im7 at equilibrium J MOL BIOL 341 215-226, 2004

Borysik AJH, Radford SE, Ashcroft AE Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J Biol Chem 279 27069-27077, 2004
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Gidalevitz T, Biswas C, Ding H, Schneidman-Duhovny D, Wolfson HJ, Stevens F, Radford SE, Argon Y Identification of the N-terminal peptide binding site of glucose-regulated protein 94 Journal of Biological Chemistry 279 16543-16552, 2004
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Dimitriadis G, Drysdale A, Myers JK, Arora P, Radford SE, Oas TG, Smith DA Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump P NATL ACAD SCI USA 101 3809-3814, 2004

Gorski SA, Le Duff CS, Capaldi AP, Kalverda AP, Beddard GS, Moore GR, Radford SE Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7 J MOL BIOL 337 183-193, 2004

Paci E, Friel CT, Lindorff-Larsen K, Radford SE, Karplus M, Vendruscolo M Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints PROTEINS 54 513-525, 2004

Jahn T, Radford SE In Amyloid proteins: The beta sheet conformation and disease In Beta-2 - microglobulin amyloidosis, 2004

Morton IJ, Hewitt E, Radford SE Protein misfolding, aggregation and combinational disease In Beta-2 - microglobulin and dialysis - related amyloidosis, 2004

Borysik AJH, Read P, Little DR, Bateman RH, Radford SE, Ashcroft AE Separation of beta(2)-microglobulin conformers by high-field asymmetric waveform ion mobility spectrometry (FAIMS) coupled to electrospray ionisation mass spectrometry RAPID COMMUN MASS SP 18 2229-2234, 2004


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Siepen JA, Radford SE, Westhead DR Beta edge strands in protein structure prediction and aggregation. Protein Sci 12 2348-2359, 2003
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Brockwell DJ, Paci E, Zinober RC, Beddard GS, Olmsted PD, Smith DA, Perham RN, Radford SE Erratum: Pulling geometry defines the mechanical resistance of aβ-sheet protein (Nature Structural Biology (2003) 10 (731-737)) Nature Structural Biology 10 872-, 2003

Siepen JA, Radford SE, Westhead DR β edge strands in protein structure prediction and aggregation Protein Science 12 2348-2359, 2003
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Brockwell DJ, Paci E, Zinober RC, Beddard GS, Olmsted PD, Smith DA, Perham RN, Radford SE Pulling geometry defines the mechanical resistance of a beta-sheet protein. Nat Struct Biol 10 731-737, 2003
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Aggeli A, Bell M, Carrick LM, Fishwick CWG, Harding R, Mawer PJ, Radford SE, Strong AE, Boden N pH as a trigger of peptide beta-sheet self-assembly and reversible switching between nematic and isotropic phases J AM CHEM SOC 125 9619-9628, 2003

Smith DP, Jones S, Serpell LC, Sunde M, Radford SE A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation J MOL BIOL 330 943-954, 2003

Kad NM, Myers SL, Smith DP, Smith DAM, Radford SE, Thomson NH Hierarchical Assembly of&beta;<sub>2</sub>-Microglobulin Amyloid In Vitro Revealed by Atomic Force Microscopy Journal of Molecular Biology 330 785-797, 2003
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Best RB, Brockwell DJ, Toca-Herrera JL, Blake AW, Smith DA, Radford SE, Clarke J Force mode atomic force microscopy as a tool for protein folding studies ANAL CHIM ACTA 479 87-105, 2003

Jones S, Manning J, Kad NM, Radford SE Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro. J Mol Biol 325 249-257, 2003
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Friel CT, Capaldi AP, Radford SE Structural Analysis of the Rate-limiting Transition States in the Folding of 1m7 and 1m9: Similarities and Differences in the Folding of Homologous Proteins Journal of Molecular Biology 326 293-305, 2003

Smith DAM, Brockwell DJ, Zinober RC, Blake AW, Beddard GS, Olmsted PD, Radford SE Unfolding dynamics of proteins under applied force Philosophical Transactions of the Royal Society of London, Series A: Mathematical, Physical and Engineering Sciences 361 739-740, 2003

Radford SE Co-translocational misfolding in the ER of living cells Nature Structural Biology 10 153-154, 2003

Jones S, Smith DP, Radford SE Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH Journal of Molecular Biology 330 935-941, 2003

Zinober RC, Brockwell DJ, Beddard GS, Blake AW, Olmsted PD, Radford SE, Smith DA Mechanically unfolding proteins: The effect of unfolding history and the supramolecular scaffold PROTEIN SCI 11 2759-2765, 2002

Brockwell DJ, Beddard GS, Clarkson J, Zinober RC, Blake AW, Trinick J, Olmsted PD, Smith DAM, Radford SE The Effect of Core Destabilization on the Mechanical Resistance of I27 Biophysical Journal 83 458-472, 2002

Trinh CH, Smith DP, Kalverda AP, Phillips SEV, Radford SE Crystal structure of monomeric humanß-2-microglobulin reveals clues to its amyloidogenic properties Proceedings of the National Academy of Sciences of the United States of America 99 9771-9776, 2002

Bousset L, Thomson NH, Radford SE, Melki R The yeast prion Ure2p retains its nativeá-helical conformation upon assembly into protein fibrils in vitro The EMBO Journal 21 2903-2911, 2002
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Ashcroft AE, Brinker A, Coyle J, Weber F, Kaiser M, Moroder L, Jaeger J, Parsons MR, Hayer-Hartl M, Hartl F, Radford SE Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain: A Study using electrospray ionization mass spectrometry and fluorescence binding studies Journal of Biological Chemistry 277 33115-33126, 2002

McParland VJ, Kalverda AP, Homans SW, Radford SE Structural properties of an amyloid precursor of&beta;<sub>2</sub>-microglobulin Nature Structural Biology 9 326-331, 2002

Capaldi AP, Kleanthous C, Radford SE Im7 folding mechanism: misfolding on a path to the native state. Nat Struct Biol 9 209-216, 2002
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Capaldi AP, Radford SE An unfolding story Trends in Biochemical Sciences 26 753-, 2001

Kad NM, Thomson NH, Smith DP, Smith DA, Radford SE β<inf>2</inf>-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro Journal of Molecular Biology 313 559-571, 2001
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Gorski SA, Capaldi AP, Kleanthous C, Radford SE Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9. J Mol Biol 312 849-863, 2001
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Smith DP, Radford SE Role of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitro. Protein Sci 10 1775-1784, 2001
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Reader JS, Van Nuland NAJ, Thompson GS, Ferguson SJ, Dobson CM, Radford SE A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding PROTEIN SCI 10 1216-1224, 2001

Ferguson N, Li W, Capaldi AP, Kleanthous C, Radford SE Using chimeric immunity proteins to explore the energy landscape for alpha-helical protein folding Journal of Molecular Biology 307 393-405, 2001

Kad NM, Thomson NH, Smith DP, Smith DA, Radford SE beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro Journal of Molecular Biology 313 559-571, 2001

Gell C, Brockwell DJ, Beddard GS, Radford SE, Kalvarda A, Smith DAM Accurate use of single molecule fluorescence correlation spectroscopy to determine molecular diffusion times Single Molecules 2 177-182, 2001

Kad NM, Radford SE Partial unfolding as a precursor of amyloidosis: a discussion of the occurrence, role and implications In Molecular Chaperones in the Cell, 2001

Capaldi AP, Shastry MCR, Kleanthous C, Roder H, Radford SE Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate NAT STRUCT BIOL 8 68-72, 2001

Radford SE Protein folding: progress made and promises ahead TRENDS BIOCHEM SCI 25 611-618, 2000

Smith DA, Radford SE Protein folding: Pulling back the frontiers CURR BIOL 10 R662-R664, 2000

McParland VJ, Kad NM, Kalverda AP, Brown A, Kirwin-Jones P, Hunter MG, Sunde M, Radford SE Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. Biochemistry 39 8735-8746, 2000
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Jones S, Reader JS, Healy M, Capaldi AP, Ashcroft AE, Kalverda AP, Smith DA, Radford SE Partially unfolded species populated during equilibrium denaturation of the beta-sheet protein Y74W apo-pseudoazurin. Biochemistry 39 5672-5682, 2000
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Thompson GS, Leung YC, Ferguson SJ, Radford SE, Redfield C The structure and dynamics in solution of Cu(I) pseudoazurin from Paracoccus pantotrophus. Protein Sci 9 846-858, 2000
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Argent RH, Parrott AM, Day PJ, Roberts LM, Stockley PG, Lord JM, Radford SE Ribosome-mediated folding of partially unfolded ricin A-chain J BIOL CHEM 275 9263-9269, 2000

Thompson GS, Radford SE The solution structure and backbone dynamics of Cu(I) pseudoazurin from Paracoccus pantotropus. Protein Science 846-858, 2000

Dobson CM, Radford SE Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme Journal of Molecular Biology 193-210, 2000

Brockwell DJ, Smith DAM, Radford SE Protein folding mechanisms: new methods and emerging ideas Current Opinion in Structural Biology 16-25, 2000

Coyle J, Texter FL, Ashcroft AE, Masselos D, Robinson CV, Radford SE GroEL accellerates the refolding of hen lysozyme without changing its folding mechanism Nature Structural Biology 6 683-690, 1999
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Kleanthous C, Kuhlmann UC, Pommer AJ, Ferguson N, Radford SE, Moore GR, James R, Hemmings AM Structural and mechanistic basis of immunity toward endonuclease colicins Nature Structural Biology 6 243-251, 1999

Radford SE Effecient enzyme inhibition by a protein that does not bind at the active site. Nature Structural Biology 233-242, 1999

Capaldi AP, Radford SE The Greek key protein pseudozurin folds through an obligate on-pathway intermediate Journal of Molecular Biology 1621-1632, 1999

Radford SE, Dobson CM From computer simulation to human disease: Emerging themes in protein folding Cell 97 291-296, 1999

Capaldi AP, Radford SE Rapid folding with and without populated intermediates in the homologous four helix proteins Im7 and Im9. Journal of Molecular Biology 1597-1608, 1999

Kulkarni SK, Ashcroft AE, Carey M, Masselos D, Robinson CV, Radford SE A near-native state on the slow refolding pathway of hen lysozyme. Protein Sci 8 35-44, 1999
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Capaldi AP, Radford SE Kinetic studies of beta-sheet protein folding. Curr Opin Struct Biol 8 86-92, 1998
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Radford SE The origin of the alpha-domain intermediate in folding of hen lysozyme Journal of Molecular Biology 997-1005, 1998

Radford SE Probing the structure of GroEL-bound substrate protein by mass spectrometry Methods in Enzymology 296-313, 1998

Radford SE What's new in protein folding? EMBO workshop: protein folding and misfolding inside and outside the cell. Fold Des 3 R59-R63, 1998

Robinson CV, Gross M, Radford SE Probing conformations of GroEL-bound substrate proteins by mass spectrometry. Methods Enzymol 290 296-313, 1998

Aggeli A, Bell M, Boden N, Keen JN, McLeish TCB, Nyrkova I, Radford SE, Semenov A Engineering of peptide beta-sheet nanotapes J MATER CHEM 7 1135-1145, 1997

Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CCF, Pepys MB Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis Nature 385 787-793, 1997
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Coyle JE, Jaeger J, Gross M, Robinson CV, Radford SE Structural and mechanistic consequences of polypeptide binding by GroEL FOLD DES 2 R93-R104, 1997

Aggeli A, Bell M, Boden N, Keen JN, Knowles PF, McLeish TCB, Pitkeathly M, Radford SE Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes Nature 386 259-262, 1997

Aggeli A, Boden N, McLeish TCB, Radford SE Self-assembly of peptides into polymeric beta-sheet tapes Abstracts of Papers of the American Chemical Society 213 pp.568-, 1997

Radford SE Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry Protein Science 1316-1324, 1997

Radford SE Fast and slow tracks in lysozyme folding: insight into the role of subdomains in the folding process Journal of Molecular Biology 1068-1074, 1997

Lu H, Radford SE Accelleration of the folding of hen lysozyme by trifluoroethanol Journal of Molecular Biology 112-117, 1997

Radford SE The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream putative regulatory sequences and over-expression in Escherichia coli. Biochemical Journal 699-705, 1997

Radford SE Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Protein Science 2506-2513, 1996

Yang JJ, van den Berg B, Pitkeathly M, Smith LJ, Bolin KA, Keiderling TA, Redfield C, Dobson CM, Radford SE Native-like secondary structure in a peptide from the alpha-domain of hen lysozyme. Fold Des 1 473-484, 1996
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Miranker A, Robinson CV, Radford SE, Dobson CM Investigation of protein folding by mass spectrometry. FASEB J 10 93-101, 1996
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Williams PA, Fülöp V, Leung YC, Chan C, Moir JW, Howlett G, Ferguson SJ, Radford SE, Hajdu J Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase. Nat Struct Biol 2 975-982, 1995
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Yang JJ, Buck M, Pitkeathly M, Kotik M, Haynie DT, Dobson CM, Radford SE Conformational properties of four peptides spanning the sequence of hen lysozyme. J Mol Biol 252 483-491, 1995
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Robinson CV, Radford SE Weighing the evidence for structure: electrospray ionization mass spectrometry of proteins. Structure 3 861-865, 1995


Chan C, Willis AC, Robinson CV, Aplin RT, Radford SE, Ferguson SJ The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha. Biochem J 308 ( Pt 2) 585-590, 1995
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Radford SE, Dobson CM Insights into protein folding using physical techniques: studies of lysozyme and alpha-lactalbumin. Philos Trans R Soc Lond B Biol Sci 348 17-25, 1995
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Gregoriou M, Jones PF, Timms JF, Yang JJ, Radford SE, Rees AR Physicochemical characterization of the cytoplasmic domain of the epidermal growth factor receptor and evidence for conformational changes associated with its activation by ammonium sulphate. Biochem J 306 ( Pt 3) 667-678, 1995
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Kotik M, Radford SE, Dobson CM Comparison of the refolding of hen lysozyme from dimethyl sulfoxide and guanidinium chloride. Biochemistry 34 1714-1724, 1995
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Robinson CV, Gross M, Eyles SJ, Ewbank JJ, Mayhew M, Hartl FU, Dobson CM, Radford SE Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry. Nature 372 646-651, 1994
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Hadfield AT, Harvey DJ, Archer DB, MacKenzie DA, Jeenes DJ, Radford SE, Lowe G, Dobson CM, Johnson LN Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product. J Mol Biol 243 856-872, 1994
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Eyles SJ, Radford SE, Robinson CV, Dobson CM Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme. Biochemistry 33 13038-13048, 1994
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Yang JJ, Pikeathly M, Radford SE Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme. Biochemistry 33 7345-7353, 1994
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Hooke SD, Radford SE, Dobson CM The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme. Biochemistry 33 5867-5876, 1994
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Itzhaki LS, Evans PA, Dobson CM, Radford SE Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry 33 5212-5220, 1994
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Buck M, Radford SE, Dobson CM Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea. J Mol Biol 237 247-254, 1994
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Aplin RT, Leung YC, Radford SE, Robinson CV, Waley SG β-lactamases: Probing the mechanism of action by Electrospray Ionisation Mass Spectrometry (ESI MS) Techniques in Protein Chemistry 5 39-47, 1994
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Dobson CM, Evans PA, Radford SE Understanding how proteins fold: the lysozyme story so far. Trends Biochem Sci 19 31-37, 1994
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Miranker A, Robinson CV, Radford SE, Aplin RT, Dobson CM Detection of transient protein folding populations by mass spectrometry. Science 262 896-900, 1993
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Buck M, Radford SE, Dobson CM A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. Biochemistry 32 669-678, 1993
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Radford SE, Buck M, Topping KD, Dobson CM, Evans PA Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins 14 237-248, 1992
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Radford SE, Dobson CM, Evans PA The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358 302-307, 1992
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Lumb KJ, Aplin RT, Radford SE, Archer DB, Jeenes DJ, Lambert N, MacKenzie DA, Dobson CM, Lowe G A study of D52S hen lysozyme-GlcNAc oligosaccharide complexes by NMR spectroscopy and electrospray mass spectrometry. FEBS Lett 296 153-157, 1992
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Miranker A, Radford SE, Karplus M, Dobson CM Demonstration by NMR of folding domains in lysozyme. Nature 349 633-636, 1991
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Broadhurst RW, Dobson CM, Hore PJ, Radford SE, Rees ML A photochemically induced dynamic nuclear polarization study of denatured states of lysozyme. Biochemistry 30 405-412, 1991
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Radford SE, Woolfson DN, Martin SR, Lowe G, Dobson CM A three-disulphide derivative of hen lysozyme. Structure, dynamics and stability. Biochem J 273(Pt 1) 211-217, 1991
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Radford SE, Perham RN, Ullrich SJ, Appella E Antibodies against an inter-domain segment of polypeptide chain inhibit active-site coupling in the pyruvate dehydrogenase multienzyme complex. FEBS letters 250 336-340, 1989
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Radford SE, Laue ED, Perham RN, Martin SR, Appella E Conformational flexibility and folding of synthetic peptides representing an interdomain segment of polypeptide chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. The Journal of biological chemistry 264 767-775, 1989
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Miles JS, Guest JR, Radford SE, Perham RN Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineering. Journal of molecular biology 202 97-106, 1988
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Texter FL, Radford SE, Laue ED, Perham RN, Miles JS, Guest JR Site-directed mutagenesis and 1H NMR spectroscopy of an interdomain segment in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Biochemistry 27 289-296, 1988
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Radford SE, Laue ED, Perham RN, Miles JS, Guest JR Segmental structure and protein domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Genetic reconstruction in vitro and 1H-n.m.r. spectroscopy. The Biochemical journal 247 641-649, 1987
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Miles JS, Guest JR, Radford SE, Perham RN A mutant pyruvate dehydrogenase complex of Escherichia coli deleted in the (alanine + proline)-rich region of the acetyltransferase component. Biochimica et biophysica acta 913 117-121, 1987
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Perham RN, Packman LC, Radford SE 2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning and halfway there. Biochemical Society symposium 54 67-81, 1987
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Radford SE, Hodkinson JP, Ashcroft AE Protein Misfolding and Toxicity in Dialysis-Related Amyloidosis In Non-fibrillar amyloidogenic protein assemblies - common cytotoxins underlying degenerative disease