S E Radford
Affiliation: University of Leeds
- 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. ..
- ..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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..