Skip to main content

Research Repository

Advanced Search

All Outputs (4)

Alexander disease causing mutations in the C-terminal domain of GFAP are deleterious both to assembly and network formation with the potential to both activate caspase 3 and decrease cell viability (2011)
Journal Article
Chen, Y., Lim, S., Chen, M., Quinlan, R. A., & Perng, M. (2011). Alexander disease causing mutations in the C-terminal domain of GFAP are deleterious both to assembly and network formation with the potential to both activate caspase 3 and decrease cell viability. Experimental Cell Research, 317(16), 2252-2266. https://doi.org/10.1016/j.yexcr.2011.06.017

Evolution of the vertebrate beaded filament protein, Bfsp2; comparing the in vitro assembly properties of a “tailed” zebrafish Bfsp2 to its “tailless” human orthologue. (2011)
Journal Article
Qu, B., Landsbury, A., Schoenthaler, H. B., Dahm, R., Liu, Y., Clark, J. I., …Quinlan, R. A. (2012). Evolution of the vertebrate beaded filament protein, Bfsp2; comparing the in vitro assembly properties of a “tailed” zebrafish Bfsp2 to its “tailless” human orthologue. Experimental Eye Research, 94(1), 192-202. https://doi.org/10.1016/j.exer.2011.12.001

In bony fishes, Bfsp2 orthologues are predicted to possess a C-terminal tail domain, which is absent from avian, amphibian and mammalian Bfsp2 sequences. These sequences, are however, not conserved between fish species and therefore questions whether... Read More about Evolution of the vertebrate beaded filament protein, Bfsp2; comparing the in vitro assembly properties of a “tailed” zebrafish Bfsp2 to its “tailless” human orthologue..

Multiple Sites in alpha B-Crystallin Modulate Its Interactions with Desmin Filaments Assembled In Vitro (2011)
Journal Article
Houck, S. A., Landsbury, A., Clark, J. I., & Quinlan, R. A. (2011). Multiple Sites in alpha B-Crystallin Modulate Its Interactions with Desmin Filaments Assembled In Vitro. PLoS ONE, 6(11), Article e25859. https://doi.org/10.1371/journal.pone.0025859

The β3- and β8-strands and C-terminal residues 155–165 of αB-crystallin were identified by pin arrays as interaction sites for various client proteins including the intermediate filament protein desmin. Here we present data using 5 well-characterised... Read More about Multiple Sites in alpha B-Crystallin Modulate Its Interactions with Desmin Filaments Assembled In Vitro.

Homeostasis in the vertebrate lens: mechanisms of solute exchange (2011)
Journal Article
Dahm, R., van Marle, J., Quinlan, R. A., Prescott, A. R., & Vrensen, G. F. (2011). Homeostasis in the vertebrate lens: mechanisms of solute exchange. Philosophical Transactions of the Royal Society B: Biological Sciences, 366(1568), 1265-1277. https://doi.org/10.1098/rstb.2010.0299

The eye lens is avascular, deriving nutrients from the aqueous and vitreous humours. It is, however, unclear which mechanisms mediate the transfer of solutes between these humours and the lens' fibre cells (FCs). In this review, we integrate the publ... Read More about Homeostasis in the vertebrate lens: mechanisms of solute exchange.