S E Radford


Affiliation: University of Leeds
Country: UK


  1. Young L, Tu L, Raleigh D, Ashcroft A, Radford S. Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers. Chem Sci. 2017;8:5030-5040 pubmed publisher
    ..The results demonstrate that co-polymerization of IAPP sequences radically alters the rate of amyloid assembly by altering the conformational properties of the mixed oligomers that form. ..
  2. Shen K, Gamerdinger M, Chan R, Gense K, Martin E, Sachs N, et al. Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related Proteinopathies. Mol Cell. 2019;: pubmed publisher
    ..In sum, NAC is a potent suppressor of aggregation and proteotoxicity of mutant PolyQ-expanded proteins associated with human diseases like Huntington's disease and spinocerebellar ataxias. ..
  3. Humes J, Schiffrin B, Calabrese A, Higgins A, Westhead D, Brockwell D, et al. The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT. J Mol Biol. 2019;: pubmed publisher
  4. Iadanza M, Silvers R, Boardman J, Smith H, Karamanos T, Debelouchina G, et al. The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nat Commun. 2018;9:4517 pubmed publisher
    ..The results provide insights into the mechanisms of fibril formation and the commonalities and differences within the amyloid fold in different protein sequences. ..
  5. Iadanza M, Jackson M, Hewitt E, Ranson N, Radford S. A new era for understanding amyloid structures and disease. Nat Rev Mol Cell Biol. 2018;19:755-773 pubmed publisher
    ..These molecular insights will aid in understanding the development and spread of amyloid diseases and are inspiring new strategies for therapeutic intervention. ..
  6. Martin E, Jackson M, Gamerdinger M, Gense K, Karamonos T, Humes J, et al. Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins. J Biol Chem. 2018;293:8554-8568 pubmed publisher
    ..Specifically, they reveal the ability of NAC to exploit its conformational plasticity to bind a repertoire of substrates with unrelated sequences and structures, independently of actively translating ribosomes. ..
  7. Chen Y, Radford S, Brockwell D. Force-induced remodelling of proteins and their complexes. Curr Opin Struct Biol. 2015;30:89-99 pubmed publisher
    ..Where appropriate, therefore, force measurements should be integrated with other experimental approaches to understand the physiological context of the system under study. ..
  8. Calabrese A, Ault J, Radford S, Ashcroft A. Using hydroxyl radical footprinting to explore the free energy landscape of protein folding. Methods. 2015;89:38-44 pubmed publisher
  9. Rajabi K, Ashcroft A, Radford S. Mass spectrometric methods to analyze the structural organization of macromolecular complexes. Methods. 2015;89:13-21 pubmed publisher
    ..g. side-chain microsolvation, HDX and ion mobility spectrometry are discussed. Together, the approaches place MS as a powerful methodology for an ever growing plethora of structural applications. ..

More Information


  1. Scarff C, Ashcroft A, Radford S. Characterization of Amyloid Oligomers by Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry (ESI-IMS-MS). Methods Mol Biol. 2016;1345:115-32 pubmed publisher
    ..This enables information about the range of oligomeric species populated en route to amyloid formation and the mode of oligomer growth to be obtained. ..
  2. Zhuravleva A, Radford S. How TriC folds tricky proteins. Cell. 2014;159:1251-2 pubmed publisher
    ..and Freund et al., a new class of TRiC substrate is identified, and how the chaperonin exploits its different subunits to extend its substrate repertoire and direct productive folding is revealed. ..
  3. Karamanos T, Kalverda A, Thompson G, Radford S. Mechanisms of amyloid formation revealed by solution NMR. Prog Nucl Magn Reson Spectrosc. 2015;88-89:86-104 pubmed publisher
    ..Together, these topics highlight the power and potential of NMR to provide atomic level information about the molecular mechanisms of one of the most fascinating problems in structural biology. ..
  4. Young L, Mahood R, Saunders J, Tu L, Raleigh D, Radford S, et al. Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry. Analyst. 2015;140:6990-9 pubmed publisher
  5. Young L, Saunders J, Mahood R, Revill C, Foster R, Ashcroft A, et al. ESI-IMS-MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules. Methods. 2016;95:62-9 pubmed publisher
    ..Here, we demonstrate these advances using self-assembly of Aβ40 as an example, and reveal two new inhibitors of Aβ40 fibrillation. ..
  6. Tipping K, Karamanos T, Jakhria T, Iadanza M, Goodchild S, Tuma R, et al. pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proc Natl Acad Sci U S A. 2015;112:5691-6 pubmed publisher
    ..The results demonstrate how pH can modulate the deleterious effects of preformed amyloid aggregates and suggest why endocytic trafficking through acidic compartments may be a key factor in amyloid disease. ..
  7. Pashley C, Hewitt E, Radford S. Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation. J Mol Biol. 2016;428:631-643 pubmed publisher
  8. Horne J, Radford S. A growing toolbox of techniques for studying ?-barrel outer membrane protein folding and biogenesis. Biochem Soc Trans. 2016;44:802-9 pubmed publisher
    ..In this review we discuss old, new and emerging techniques used to examine the process of OMP folding and biogenesis in vitro and describe some of the insights and new questions these techniques have revealed. ..
  9. Watkinson T, Calabrese A, Ault J, Radford S, Ashcroft A. FPOP-LC-MS/MS Suggests Differences in Interaction Sites of Amphipols and Detergents with Outer Membrane Proteins. J Am Soc Mass Spectrom. 2017;28:50-55 pubmed publisher
    ..Graphical Abstract ᅟ. ..
  10. Tipping K, van Oosten Hawle P, Hewitt E, Radford S. Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease?. Trends Biochem Sci. 2015;40:719-27 pubmed publisher
    ..Thus, a greater understanding of amyloid fibre biology could enhance prospects of developing therapeutic interventions against this devastating class of protein-misfolding disorders. ..
  11. Schiffrin B, Brockwell D, Radford S. Outer membrane protein folding from an energy landscape perspective. BMC Biol. 2017;15:123 pubmed publisher
    ..We also highlight the role of chaperones and the β-barrel assembly machinery (BAM) in assisting OMP folding in vivo and discuss proposed mechanisms by which this fascinating machinery may catalyse OMP folding. ..
  12. Stewart K, Radford S. Amyloid plaques beyond A?: a survey of the diverse modulators of amyloid aggregation. Biophys Rev. 2017;9:405-419 pubmed publisher
    ..Since no protein acts in isolation, the interplay of these diverse molecules may differentiate disease onset, progression, and severity, and thus are worth careful consideration. ..
  13. Young L, Ashcroft A, Radford S. Small molecule probes of protein aggregation. Curr Opin Chem Biol. 2017;39:90-99 pubmed publisher
    ..Such probes form a powerful platform with which to better define the mechanisms of structural conversion into amyloid fibrils and may provide the much-needed stepping stone for future development of successful therapeutic agents. ..
  14. Stewart K, Hughes E, Yates E, Middleton D, Radford S. Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils. J Mol Biol. 2017;429:2449-2462 pubmed publisher
    ..Differences in GAG binding to fibrils with distinct sequence and/or structure may thus contribute to the diverse etiology and progression of amyloid diseases. ..
  15. Schiffrin B, Calabrese A, Higgins A, Humes J, Ashcroft A, Kalli A, et al. Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding. J Mol Biol. 2017;429:3776-3792 pubmed publisher
  16. Karamanos T, Kalverda A, Thompson G, Radford S. Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. Mol Cell. 2014;55:214-26 pubmed publisher
    ..The results highlight the complexity of interactions early in amyloid assembly and reveal atomic-level information about species barriers in amyloid formation. ..