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Elife|September 26, 2019
Structural mapping of oligomeric intermediates in an amyloid assembly pathwayTheodoros K Karamanos, Matthew P Jackson, Antonio N Calabrese, et al.Molecular & Cellular Proteomics : MCP|February 3, 2007
Organelle proteomics: identification of the exocytic machinery associated with the natural killer cell secretory lysosomeTammy M Casey, Josephine L Meade, Eric W HewittJournal of Molecular Biology|January 19, 2016
Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationClare L Pashley, Eric W Hewitt, Sheena E RadfordFrontiers in Molecular Neuroscience|December 16, 2020
Modulation of β-Amyloid Fibril Formation in Alzheimer's Disease by Microglia and InfectionMadeleine R Brown, Sheena E Radford, Eric W HewittJournal of Virology|April 17, 2009
Kaposi's sarcoma-associated herpesvirus RTA promotes degradation of the Hey1 repressor protein through the ubiquitin proteasome pathwayFaye Gould, Sally M Harrison, Eric W Hewitt, et al.Nano Letters|June 20, 2020
Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State NanoporeChalmers C Chau, Sheena E Radford, Eric W Hewitt, et al.Trends in Biochemical Sciences|September 10, 2002
Powering the peptide pump: TAP crosstalk with energetic nucleotidesPeter M van Endert, Loredana Saveanu, Eric W Hewitt, et al.Prion|March 23, 2010
Fibril fragmentation in amyloid assembly and cytotoxicity: when size mattersWei-Feng Xue, Andrew L Hellewell, Eric W Hewitt, et al.The Journal of Biological Chemistry|August 10, 2007
Investigation into the role of macrophages in the formation and degradation of beta2-microglobulin amyloid fibrilsIsobel J Morten, Walraj S Gosal, Sheena E Radford, et al.Plos One|November 19, 2011
Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrilsMorwenna Y Porter, Katy E Routledge, Sheena E Radford, et al.Pageof 5