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Porous polymers by emulsion templating. (2005)
Journal Article
Barbetta, A., Carnachan, R., Smith, K., Zhao, C., Cameron, N., Kataky, R., …Swan, M. (2005). Porous polymers by emulsion templating. Macromolecular Symposia, 226(1), 203-212. https://doi.org/10.1002/masy.200550819

Highly porous and permeable polymers are produced by polymerisation of the continuous phase of high internal phase emulsions (HIPEs). The morphology and properties of the resulting PolyHIPE materials can be varied, allowing the materials to be optimi... Read More about Porous polymers by emulsion templating..

Modular nanometer-scale structuring of gel fibres by sequential self-organization (2005)
Journal Article
Applegarth, L., Clark, N., Richardson, A., Parker, A., Radosavljevic-Evans, I., Goeta, A., …Steed, J. (2005). Modular nanometer-scale structuring of gel fibres by sequential self-organization. Chemical Communications, 5423-5425

Ag(I) and Cu(II) complexes of a series of simple bis( urea) ligands form soft metallogels. X-ray crystallographic results suggests that the gels' structure is based on hydrogen bonding to counter anions and thus suggests a route to tunable gel rheolo... Read More about Modular nanometer-scale structuring of gel fibres by sequential self-organization.

Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb (2005)
Journal Article
Dias-Gunasekara, S., Gubbens, J., van Lith, M., Dunne, C., Williams, J., Kataky, R., …Benham, A. (2005). Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb. Journal of Biological Chemistry, 280(38), 33066-33075. https://doi.org/10.1074/jbc.m505023200

Endoplasmic reticulum oxidoreductases (Eros) are essential for the formation of disulfide bonds. Understanding disulfide bond catalysis in mammals is important because of the involvement of protein misfolding in conditions such as diabetes, arthritis... Read More about Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb.

Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells (2004)
Journal Article
Perng, M., Wen, S., van den Ijssel, P., Prescott, A., & Quinlan, R. (2004). Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells. Molecular Biology of the Cell, 15(5), 2335-2346. https://doi.org/10.1091/mbc.e03-12-0893

The R120G mutation in alphaB-crystallin causes desmin-related myopathy. There have been a number of mechanisms proposed to explain the disease process, from altered protein processing to loss of chaperone function. Here, we show that the mutation alt... Read More about Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells.