Self-funded students: International or domestic self-funded or scholarship/fellowship PhD students are always welcome to apply. International students must have a good command of both written and spoken English. In addition to University fees, laboratory fees will be required if you are self-funded. Applications can be made throughout the year.
The project builds upon a successful collaboration between Dr Eric Hewitt and Professor Sheena Radford. Below are some of their recent publications that are relevant to this project.
Xue, WF, Hellewell, AL, Gosal, WS, Homans, SW, Hewitt, EW, Radford, SE (2009) Fibril fragmentation enhances amyloid toxicity. J. Biol Chem. 284, 34272-82
Porter MY, Routledge KE, Radford SE, Hewitt EW. (2011). Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.PLoS One. 6:e27353.
Goodchild SC, Sheynis T, Thompson R, Tipping KW, Xue WF, Ranson NA, Beales PA, Hewitt EW, Radford SE. (2014) β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH. PLoS One. 9, e104492.
Jakhria, T, Hellewell, AL, Porter, MY, Jackson, M, Tipping, KW, Xue, WF Radford, SE, Hewitt, EW (2014). β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes. J. Biol. Chem. 289, 35781-94
Tipping KW, Karamanos TK, Jakhria T, Iadanza MG, Goodchild SC, Tuma R, Ranson NA, Hewitt EW, Radford SE. (2015). pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proc Natl Acad Sci U S A. 112:5691-6.
Tipping KW, van Oosten-Hawle P, Hewitt EW and Radford, SE. (2015) Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease? Trends in Biochemical Sciences 40, 719-727
FTE Category A staff submitted: 60.90
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