Dr Simon Easterbrook-Smith
Senior Lecturer G08 - Biochemistry and Microbiology Building
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Formation of amyloid is causally linked to currently un-curable diseases like Alzheimer’s disease, Parkinson’s disease, familial amyloid polyneuropathy and Type II diabetes. Therefore, a deeper understanding of how amyloid forms will contribute to the knowledge base needed for devising improved therapies for these diseases; this is the overall goal of our work.
We are particularly interesting in addressing the question of the extent to which amyloid formation in vivo may be modulated by other species, including metal ions, other macromolecules (such as glycosaminoglycans) and molecular assemblages (such as phospholipids in cell membranes) as well as by extra-cellular chaperones.
We are particularly interesting in addressing the question of the extent to which amyloid formation in vivo may be modulated by other species, including metal ions, other macromolecules (such as glycosaminoglycans) and molecular assemblages (such as phospholipids in cell membranes) as well as by extra-cellular chaperones.
- Wilkinson-White, L, Easterbrook-Smith, S. A dye-binding assay for measurement of the binding of Cu(II) to proteins. Journal of inorganic biochemistry. 2008; 102:1831-8 [Abstract]
- Wilkinson-White, L, Easterbrook-Smith, S. Characterization of the Binding of Cu(II) and Zn(II) to Transthyretin: Effects on Amyloid Formation. Biochemistry. 2007; 46:9123-32 [Abstract]
- Stewart, E, Aquilina, J, Easterbrook-Smith, S, Murphy-Durland, D, Jacobsen, C, Moestrup, S, Wilson, M. Effects of glycosylation on the structure and function of the extracellular chaperone clusterin. Biochemistry. 2007; 46:1412-1422 [Abstract]
- Yerbury, J, Rybchyn, M, Easterbrook-Smith, S, Henriques, C, Wilson, M. The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin. Biochemistry. 2005; 44:10914-25 [Abstract]
Glycoproteins; Molecular Chaperones; Protein Folding