Quinlan, Roy Andrew - Durham University - School of Biological and Biomedical Science

个人简介

Professor Roy Quinlan joined the University of Durham in 2001 and was one of those responsible for founding the Biophysical Sciences Institute, which was then established in 2007. He is a Biochemistry graduate and PhD from the University of Kent where he worked on microtubules with Professor Keith Gull FRS, before taking up an Alexander von Humboldt fellowship at the German Cancer Research Centre to work on Intermediate Filaments with Professor Werner Franke in 1981. He joined Dr Murray Stewart at the LMB Cambridge determining the coiled coil pitch of myosin LS2, but continued to investigate structural aspects of GFAP and lamins. In 1988, he was appointed as a lecturer to the Department of Biochemistry in Dundee.

研究领域

Animal cell biology Cataract and amyloidosis Inherited human diseases caused by mutant cytoskeletal proteins, particularly cataract, cardiomyopathy and neuropathies Motor neurone disease Protein chaperones The cytoskeleton The eye lens and the ageing process

近期论文

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Barnard, S., Ainsbury, E.A., Quinlan, R.A. & Buffler, S. (2016). Radiation protection of the eye lens in medical workers—basis and impact of the ICRP recommendations. The British Journal of Radiology 89(1060): 20151034. Barnes, S. & Quinlan, R.A. (2016). Small molecules, both dietary and endogenous, influence the onset of lens cataracts. Experimental Eye Research Ricci, M., Quinlan, R. A. & Vo?tchovsky, K. (2016). Sub-nanometre mapping of the aquaporin-water interface with multifrequency atomic force microscopy. Soft Matter (advance online publication). Ismail, Vian S., Mosely, Jackie A., Tapodi, Antal Quinlan, Roy A. & Sanderson, John M. (2016). The Lipidation Profile of Aquaporin-0 Correlates with The Acyl Composition of Phosphoethanolamine Lipids in Lens Membranes. Biochimica et Biophysica Acta (BBA) - Biomembranes 1858(11): 2763-2768. Wu, J.J., Wu, W., Tholozan, F.M., Saunter, C.D., Girkin, J.M. & Quinlan, R.A. (2015). A dimensionless ordered pull-through model of the mammalian lens epithelium evidences scaling across species and explains the age-dependent changes in cell density in the human lens. Journal of The Royal Society Interface 12(108): 20150391. Quinlan, R.A. (2015). A new dawn for cataracts. Science 350(6261): 636-637. Quinlan, R.A., Bromley, E.H. & Pohl, E. (2015). A silk purse from a sow’s ear – bioinspired materials based on α-helical coiled coils. Current opinion in cell biology 32: 131-137. Markiewicz, Ewa, Barnard, Stephen, Haines, Jackie, Coster, Margaret, Geel, Orry van, Wu, Weiju, Richards, Shane, Ainsbury, Elizabeth, Rothkamm, Kai, Bouffler, Simon & Quinlan, Roy A. (2015). Nonlinear ionizing radiation-induced changes in eye lens cell proliferation, cyclin D1 expression and lens shape. Open biology 5: 150011. Bouffler, S., Peters, S., Gilvin, P., Slack, K., Markiewicz, E.M., Quinlan, R.A., Gillan, J., Coster, M., Barnard, S., Rothkamm, K. & Ainsbury, E. (2015). The lens of the eye: exposures in the UK medical sector and mechanistic studies of radiation effects. Annals of the ICRP 44(1 Suppl): 84-90. Wu, W., Tholozan, F.M., Goldberg, M.W., Bowen, L., Wu, J.J. & Quinlan, R.A (2014). A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells. Experimental Eye Research 120: 10-14. Chen, M.H., Hagemann, T.L., Quinlan, R.A., Messing, A. & Perng, M.-D. (2013). Caspase cleavage of GFAP produces an assembly-compromised proteolytic fragment that promotes filament aggregation. ASN Neuro 5(5): 293-308. Quinlan, R.A., Zhang, Y., Lansbury, A., Williamson, I., Pohl, E. & Sun, F. (2013). Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the I–X–I motif and introduction of the substitution, R107G in the a-crystallin domain. Philosophical Transactions of the Royal Society B: Biological Sciences 368(1617): 20120327. Quinlan, R.A. & Ellis, R.J. (2013). Chaperones: needed for both the good times and the bad times. Philosophical Transactions of the Royal Society B: Biological Sciences 368(1617): 20130091. Elliott, JL, Der Perng, M Prescott, AR, Jansen, KA, Koenderink, GH & Quinlan, RA. (2013). The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability. Philosophical Transactions of the Royal Society B: Biological Sciences 368(1617): 20120375. Qu, Bo, Landsbury, Andrew, Schoenthaler, Helia Berrit, Dahm, Ralf, Liu, Yizhi, Clark, John I., Prescott, Alan R. & Quinlan, Roy 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. Chen, Yi-Song, Lim, Suh-Ciuan, Chen, Mei-Hsuan, Quinlan, Roy A. & Perng, Ming-Der (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. Dahm, Ralf, van Marle, Jan, Quinlan, Roy A., Prescott, Alan R. & Vrensen, Gijs F. J. M. (2011). Homeostasis in the vertebrate lens: mechanisms of solute exchange. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES 366(1568): 1265-1277. Houck, Scott A., Landsbury, Andrew, Clark, John I. & Quinlan, Roy A. (2011). Multiple Sites in alpha B-Crystallin Modulate Its Interactions with Desmin Filaments Assembled In Vitro. PLOS ONE 6(11): e25859. Tang,G Perng, MD, Wilk, S, Quinlan, R & Goldman, JE (2010). Oligomers of mutant glial fibrillary acidic protein (GFAP) Inhibit the proteasome system in alexander disease astrocytes, and the small heat shock protein alphaB-crystallin reverses the inhibition. Journal of Biological Chemistry 285(14): 10527. Sugiyama, Yuki, Akimoto, Kazunori, Robinson, Michael L., Ohno, Shigeo & Quinlan, Roy A. (2009). A cell polarity protein aPKC lambda is required for eye lens formation and growth. Developmental Biology 336(2): 246-256.