Professor Elizabeth Bromley's Outputs (4)

The binding of thioflavin-T to amyloid fibrils: localisation and implications (2005)
Journal Article
Krebs, M., Bromley, E., & Donald, A. (2005). The binding of thioflavin-T to amyloid fibrils: localisation and implications. Journal of Structural Biology, 149(1), 30-37. https://doi.org/10.1016/j.jsb.2004.08.002

Amyloid fibrils are a polymeric form of protein, involving a continuous P-sheet with the strands perpendicular to the long axis of the fibril. Although typically implicated in diseases such as Alzheimer's disease and the transmissible spongiform ence... Read More about The binding of thioflavin-T to amyloid fibrils: localisation and implications.

Aggregation across the length-scales in beta-lactoglobulin (2005)
Journal Article
Bromley, E., Krebs, M., & Donald, A. (2005). Aggregation across the length-scales in beta-lactoglobulin. Faraday Discussions, 128, 13-27

The protein beta-lactoglobulin (BLG) has been widely studied, in large part because of its importance to the food industry. Following denaturation during heating, under different conditions of pH it has been found to form either particulate (around t... Read More about Aggregation across the length-scales in beta-lactoglobulin.

The mechanism of amyloid spherulite formation by bovine insulin (2005)
Journal Article
Krebs, M., Bromley, E., Rogers, S., & Donald, A. (2005). The mechanism of amyloid spherulite formation by bovine insulin. Biophysical Journal, 88(3), 2013-2021

The formation of amyloid-containing spherulite-like structures has been observed in some instances of amyloid diseases, as well as in amyloid fibril-containing solutions in vitro. In this article we describe the structure and kinetics of bovine insul... Read More about The mechanism of amyloid spherulite formation by bovine insulin.

L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers (2005)
Journal Article
Keetch, C., Bromley, E., McCammon, M., Wang, N., Christodoulou, J., & Robinson, C. (2005). L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers. Journal of Biological Chemistry, 280(50), 41667-41674

Transthyretin is a tetrameric protein associated with the commonest form of systemic amyloid disease. Using isotopically labeled proteins and mass spectrometry, we compared subunit exchange in wild-type transthyretin with that of the variant associat... Read More about L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers.