Staff profile

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. Here his interest in the cytoskeleton and particularly intermediate filaments in astrocytes, cardiomyocytes and the lens led to the discovery of the functionally important interaction of the small heat shock protein chaperones with intermediate filaments and its role in mediating the biomechanical properties of cells. In the lens, these proteins are key to its function as an optical element the eye. The strong correlation between structure and function in this tissue provides the platform for current research interests to model lens cell organization in 3 and 4 dimensions and integrating the cytoskeletal and chaperone functions into a scaled model of this tissue.

The eye lens is a tissue in which its cell structure and cell organisation is intimately linked to function. The lens epithelium is a single layer of cells covering the anterior portion of the lens and underlying the anterior lens capsule. It is the cells of the lens epithelium that cause complications after cataract surgery and it is also those that are damaged by ionising radiation and this damage then manifests itself as lens opacities and eventually cataract. The lens epithelial cells form the lens fibre cells by cell differentiation. This is restricted to those epithelial cells at the very equator of the lens. The lens grows, albeit slowly, throughout life. To ensure that there is a continual supply of lens epithelial cells to differentiate into fibre cells, a cell proliferation zone is adjacent to the lens equator. The geometrical order of the lens originates in the epithelium and is manifested in fibre cell differentiation. The differentiating lens fibre cells undergo massive (~1000X) elongation so that eventually the ends of these cells from opposing lens quadrants touch to form the lens sutures. This exemplifies the precise arrangement of the lens fibre cells required to produce a functional lens that is capable of refracting focused images onto the retina. The epithelial cells outside of the equatorial and proliferative zones have the potential to proliferate, but they appear quiescent. This is called the central zone. The epithelial cells retain the potential for proliferation. We are investigating how ionising radiation causes lens opacities and cataract. We predict that it is damage to the cells in the lens epithelium and disturbance to their patterns of cell proliferation and differentiation, but important questions remain. For instance: Are some cells more sensitive than others to (low dose) ionising radiation? Is there a threshold dose? How does radiation damage to the lens epithelium cause the posterior subcapsular cataract that is so typical of radiation damage to the lens? 

The mouse is an excellent animal model because of the wealth of genetic and molecular tools to dissect out the mechanistic detail of low dose radiation effects. The lens is very accessible and easy to dissect. My laboratory has developed both mounting techniques and lens explant culturing techniques that has allowed us to link cell position in the epithelium to metric data (length, cross-sectional area; proliferation and apoptotic status). We can therefore detect the earliest signs of ionising radiation damage to the lens epithelium through changes in cell proliferation, cell death or cell metrics. Real time imaging of the developing eye lens would also be helpful to populate our knowledge base in terms of cell positioning, division planes and other organelle dynamics within the developing lens, but this is more easily achieved using zebrafish. With colleagues (Professor John Girkin, Dr Robert Pal, Dr Boguslaw Obara, Dr Junjie Wu) in Durham University Biophysical Sciences Institute, we are using multidisciplinary approaches to reach this goal so that in future, mouse and zebrafish systems can complement each other. This has led also to important research collaborations with Dr Kislon Voitchovsky and Dr Margarita Staykova (Physics), Dr John Sanderson and Dr Jackie Mosely (Chemistry) on lens membranes, their lipids and associated proteins, so that we connect our studies on the mechanistic details of lens function and cataractogenesis with our modelling of the lens.

We are currently investigating Electronic Lab Notebooks to standardise protocols, communicate results with collaborators and favour SciNote for ease of use and accessibility (https://scinote.net/)

• Aquaporin 0 structure and function
• animal cell biology
• cataract and amyloidosis
• inherited human diseases caused by mutant cytoskeletal proteins, particularly cataract, cardiomyopathy and neuropathies
• membrane domains and their association with protein chaperones and intermediate filaments
• motor neurone disease
• protein chaperones
• the cytoskeleton
• the eye lens and the ageing process

• 2016: Invited speaker at the the GRC on Intermediate Filaments:
• 2016: Chair Elect for the 2020 GRC on Intermediate Filaments: Elected along with Jan Lammerding to Chair the 2020 Gordon Research Conference on Intermediate Filaments
• 2015: Fight for Sight Trustee:
• 2013: Appointment to the Editorial Board of the Journal of Biological Chemistry: Apponitment by invitation only
• 2011: Appointed Affiliate Faculty to Department of Biological Structure at the UNiversity of Washington, Seattle: After my sabbatical year in this Department and the collaboration initiated I was appointed to the faculty as an affiliate member. Professor John I. Clark is Departmental Chair
• 2009: Section Editor for Experimental Eye Research: Section Editor for the leading international eye research journal, Experimental Eye Research

Chapter in book

• Perng, M., Huang, Y., & Quinlan, R. (2016). Purification of Protein Chaperones and Their Functional Assays with Intermediate Filaments. In A. Sonnenberg, & K. Wilson (Eds.), Intermediate Filament Associated Proteins (155-175). Elsevier. https://doi.org/10.1016/bs.mie.2015.07.025

Conference Paper

• Zinov'ev, N., Jahoda, C., Quinlan, R., & Chamberlain, J. (2007). Terahertz spectroscopy of stem cells.

Journal Article

• Pérez-Sala, D., & Quinlan, R. A. (2024). The redox-responsive roles of intermediate filaments in cellular stress detection, integration and mitigation. Current Opinion in Cell Biology, 86, Article 102283. https://doi.org/10.1016/j.ceb.2023.102283
• Berry, V., Ionides, A., Georgiou, M., Quinlan, R. A., & Michaelides, M. (2023). Multimorbidity due to novel pathogenic variants in theWFS1/RP1/NOD2genes: autosomal dominant congenital lamellar cataract, retinitis pigmentosa and Crohn’s disease in a British family. BMJ Open Ophthalmology, 8(1), Article e001252. https://doi.org/10.1136/bmjophth-2023-001252
• Jarrin, M., Kalligeraki, A. A., Uwineza, A., Cawood, C. S., Brown, A. P., Ward, E. N., …Quinlan, R. A. (2023). Independent Membrane Binding Properties of the Caspase Generated Fragments of the Beaded Filament Structural Protein 1 (BFSP1) Involves an Amphipathic Helix. Cells, https://doi.org/10.3390/cells12121580
• Uwineza, A., Cummins, I., Jarrin, M., Kalligeraki, A. K., Barnard, S., Mol, M., …Quinlan, R. A. (2023). Identification and quantification of ionising radiation-induced oxysterol formation in membranes of lens fibre cells. Advances in Redox Research, 7, Article 100057. https://doi.org/10.1016/j.arres.2022.100057
• Berry, V., Ionides, A., Pontikos, N., Moore, A. T., Quinlan, R. A., & Michaelides, M. (2022). Variants in PAX6, PITX3 and HSF4 causing autosomal dominant congenital cataracts. Eye, 36(8), 1694-1701. https://doi.org/10.1038/s41433-021-01711-x
• Quinlan, P. R., Figeuredo, G., Mongan, N., Jordan, L. B., Bray, S. E., Sreseli, R., …Quinlan, R. A. (2022). Cluster analyses of the TCGA and a TMA dataset using the coexpression of HSP27 and CRYAB improves alignment with clinical-pathological parameters of breast cancer and suggests different epichaperome influences for each sHSP. Cell Stress and Chaperones, 27(2), 177-188. https://doi.org/10.1007/s12192-022-01258-0
• Berry, V., Fujinami, K., Mochizuki, K., Iwata, T., Pontikos, N., Quinlan, R. A., & Michaelides, M. (2022). A recurrent variant in LIM2 causes an isolated congenital sutural/lamellar cataract in a Japanese family. Ophthalmic Genetics, 43(5), 622-626. https://doi.org/10.1080/13816810.2022.2090010
• Pawliczek, D., Fuchs, H., Gailus-Durner, V., de Angelis, M. H., Quinlan, R., Graw, J., & Dalke, C. (2022). On the Nature of Murine Radiation-Induced Subcapsular Cataracts: Optical Coherence Tomography-Based Fine Classification, In Vivo Dynamics and Impact on Visual Acuity. Radiation research, 197(1), 7-21. https://doi.org/10.1667/rade-20-00163.1
• Quinlan, R. A., & Clark, J. I. (2022). Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens. Journal of Biological Chemistry, 298(11), Article 102537. https://doi.org/10.1016/j.jbc.2022.102537
• Berry, V., Pontikos, N., Ionides, A., Kalitzeos, A., Quinlan, R. A., & Michaelides, M. (2022). Pathogenic variants in the CYP21A2 gene cause isolated autosomal dominant congenital posterior polar cataracts. Ophthalmic Genetics, 43(2), 218-223. https://doi.org/10.1080/13816810.2021.1998556
• Wu, W., Lois, N., Prescott, A. R., Brown, A. P., Van Gerwen, V., Tassignon, M., …Quinlan, R. A. (2021). The importance of the epithelial fibre cell interface to lens regeneration in an in vivo rat model and in a human bag-in-the-lens (BiL) sample. Experimental Eye Research, 213, Article 108808. https://doi.org/10.1016/j.exer.2021.108808
• Vasconcelos, M. H., Alcaro, S., Arechavala-Gomeza, V., Baumbach, J., Borges, F., Brevini, T. A., …Riganti, C. (2021). Joining European Scientific Forces to Face Pandemics. Trends in Microbiology, 29(2), 92-97. https://doi.org/10.1016/j.tim.2020.10.008
• Barnard, S., Uwineza, A., Kalligeraki, A., McCarron, R., Kruse, F., Ainsbury, E., & Quinlan, R. (2021). Lens Epithelial Cell Proliferation in Response to Ionizing Radiation. Radiation research, 197(1), 92-99. https://doi.org/10.1667/rade-20-00294.1
• Berry, V., Ionides, A., Pontikos, N., Moghul, I., Moore, A. T., Quinlan, R. A., & Michaelides, M. (2020). Whole Exome Sequencing Reveals Novel and Recurrent Disease-Causing Variants in Lens Specific Gap Junctional Protein Encoding Genes Causing Congenital Cataract. Genes, 11(5), Article 512. https://doi.org/10.3390/genes11050512
• Berry, V., Pontikos, N., Dudakova, L., Moore, A. T., Quinlan, R., Liskova, P., & Michaelides, M. (2020). A novel missense mutation in LIM2 causing isolated autosomal dominant congenital cataract. Ophthalmic Genetics, 41(2), 131-134. https://doi.org/10.1080/13816810.2020.1737950
• Kalligeraki, A. A., Isted, A., Pal, R., Saunter, C., Girkin, J., Jarrin, M., …Quinlan, R. A. (2020). Three-dimensional data capture and analysis of intact eye lenses evidences emmetropia-associated changes and strain-dependent differences in epithelial cell organization. Scientific Reports, 10, Article 16898. https://doi.org/10.1038/s41598-020-73625-9
• Berry, V., Ionides, A., Pontikos, N., Georgiou, M., Yu, J., Ocaka, L. A., …Michaelides, M. (2020). The genetic landscape of crystallins in congenital cataract. Orphanet Journal of Rare Diseases, 15, Article 333. https://doi.org/10.1186/s13023-020-01613-3
• Battaglia, R. A., Beltran, A. S., Delic, S., Dumitru, R., Robinson, J. A., Kabiraj, P., …Snider, N. T. (2019). Site-specific phosphorylation and caspase cleavage of GFAP are new markers of Alexander Disease severity. eLife, 8, Article e47789. https://doi.org/10.7554/elife.47789
• Tapodi, A., Clemens, D., Uwineza, A., Goldberg, M., Thinon, E., Heal, W., …Quinlan, R. (2019). BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability. Experimental Eye Research, 185, Article 107585. https://doi.org/10.1016/j.exer.2019.02.001
• Uwineza, A., Kalligeraki, A. A., Hamada, N., Jarrin, M., & Quinlan, R. A. (2019). Cataractogenic load – a concept to study the contribution of ionizing radiation to accelerated aging in the eye lens. Mutation Research/Reviews in Mutation Research, 779, 68-81. https://doi.org/10.1016/j.mrrev.2019.02.004
• Barnard, S., McCarron, R., Moquet, J., Quinlan, R., & Ainsbury, E. (2019). Inverse dose-rate effect of ionising radiation on residual 53BP1 foci in the eye lens. Scientific Reports, 9, Article 10418. https://doi.org/10.1038/s41598-019-46893-3
• Gorter, R. P., Nutma, E., Jahreiβ, M., de Jonge, J. C., Quinlan, R., van der Valk, P., …Amor, S. (2018). Heat shock proteins are differentially expressed in brain and spinal cord: implications for multiple sclerosis. Clinical and Experimental Immunology, 194(2), 137-152. https://doi.org/10.1111/cei.13186
• Young, L., Jarrin, M., Saunter, C., Quinlan, R., & Girkin, J. (2018). Non-invasive in vivo quantification of the developing optical properties and graded index of the embryonic eye lens using SPIM. Biomedical Optics Express, 9(5), 2176-2188. https://doi.org/10.1364/boe.9.002176
• Quinlan, R., Schwartz, N., Windoffer, R., Richardson, C., Hawkins, T., Broussard, J., …Leube, R. (2017). A rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks. Journal of Cell Science, 130(20), 3437-3445. https://doi.org/10.1242/jcs.202168
• Sharma, S., Conover, G., Elliott, J., Perng, M., Herrmann, H., & Quinlan, R. (2017). αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments. Cell Stress and Chaperones, 22(4), 613-626. https://doi.org/10.1007/s12192-017-0788-7
• Carver, J., Grosas, A., Ecroyd, H., & Quinlan, R. (2017). The functional roles of the unstructured N- and C-terminal regions in alphaB-crystallin and other mammalian small heat-shock proteins. Cell Stress and Chaperones, 22(4), 627-638. https://doi.org/10.1007/s12192-017-0789-6
• Forssell-Aronsson, E., & Quinlan, R. (2017). The impact of circadian rhythms on medical imaging and radiotherapy regimes for the paediatric patient. Radiation Protection Dosimetry, 173(1-3), 16-20. https://doi.org/10.1093/rpd/ncw328
• Ricci, M., Quinlan, R., & Voïtchovsky, K. (2017). Sub-nanometre mapping of the aquaporin-water interface with multifrequency atomic force microscopy. Soft Matter, 13(1), 187-195. https://doi.org/10.1039/c6sm00751a
• Zeraik, A., Staykova, M., Fontes, M., Nemuraitė, I., Quinlan, R., Araújo, A., & DeMarco, R. (2016). Biophysical dissection of schistosome septins: Insights into oligomerization and membrane binding. Biochimie, 131, 96-105. https://doi.org/10.1016/j.biochi.2016.09.014
• Ismail, V. S., Mosely, J. A., Tapodi, A., Quinlan, R. A., & Sanderson, J. M. (2016). The Lipidation Profile of Aquaporin-0 Correlates with The Acyl Composition of Phosphoethanolamine Lipids in Lens Membranes. BBA - Biomembranes, 1858(11), 2763-2768. https://doi.org/10.1016/j.bbamem.2016.06.026
• Barnes, S., & Quinlan, R. (2016). Small molecules, both dietary and endogenous, influence the onset of lens cataracts. Experimental Eye Research, 156, 87-94. https://doi.org/10.1016/j.exer.2016.03.024
• Barnard, S., Ainsbury, E., Quinlan, R., & Buffler, S. (2016). Radiation protection of the eye lens in medical workers—basis and impact of the ICRP recommendations. British Journal of Radiology, 89(1060), Article 20151034. https://doi.org/10.1259/bjr.20151034
• Quinlan, R. (2015). A new dawn for cataracts. Science, 350(6261), 636-637. https://doi.org/10.1126/science.aad6303
• Wu, J., Wu, W., Tholozan, F., Saunter, C., Girkin, J., & Quinlan, R. (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), https://doi.org/10.1098/rsif.2015.0391
• Bouffler, S., Peters, S., Gilvin, P., Slack, K., Markiewicz, E., Quinlan, R., …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. https://doi.org/10.1177/0146645314560693
• Markiewicz, E., Barnard, S., Haines, J., Coster, M., Geel, O. V., Wu, W., …Quinlan, R. A. (2015). Nonlinear ionizing radiation-induced changes in eye lens cell proliferation, cyclin D1 expression and lens shape. Open Biology, 5, Article 150011. https://doi.org/10.1098/rsob.150011
• Quinlan, R., Bromley, E., & 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. https://doi.org/10.1016/j.ceb.2014.12.010
• Wu, W., Tholozan, F., Goldberg, M., Bowen, L., Wu, J., & Quinlan, R. (2014). A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells. Experimental Eye Research, 120, 10-14. https://doi.org/10.1016/j.exer.2013.12.004
• Chen, M., Hagemann, T., Quinlan, R., Messing, A., & Perng, M. (2013). Caspase cleavage of GFAP produces an assembly-compromised proteolytic fragment that promotes filament aggregation. Conversations about pedagogy and teaching underpinned by research enquiry, 5(5), https://doi.org/10.1042/an20130032
• Quinlan, R., & Ellis, R. (2013). Chaperones: needed for both the good times and the bad times. Philosophical Transactions of the Royal Society B: Biological Sciences, 368(1617), Article 20130091. https://doi.org/10.1098/rstb.2013.0091
• Elliott, J., Der Perng, M., Prescott, A., Jansen, K., Koenderink, G., & Quinlan, R. (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), Article 20120375. https://doi.org/10.1098/rstb.2012.0375
• Quinlan, R., 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), Article 20120327. https://doi.org/10.1098/rstb.2012.0327
• 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
• 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
• 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
• 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
• Tang, G., Perng, M., Wilk, S., Quinlan, R., & Goldman, J. (2010). Oligomers of mutant glial fibrillary acidic protein (GFAP) Inhibit the proteasome system in alexander disease astrocytes, and the small heat shock protein αB-crystallin reverses the inhibition. Journal of Biological Chemistry, 285(14), 10527-10537. https://doi.org/10.1074/jbc.m109.067975
• Sugiyama, Y., Akimoto, K., Robinson, M. L., Ohno, S., & Quinlan, R. A. (2009). A cell polarity protein aPKCλ is required for eye lens formation and growth. Developmental Biology, 336(2), 246-256. https://doi.org/10.1016/j.ydbio.2009.10.010
• Gorog, D. A., Jabr, R. I., Tanno, M., Sarafraz, N., Clark, J. E., Fisher, S. G., …Heads, R. J. (2009). MAPKAPK-2 modulates p38-MAPK localization and small heat shock protein phosphorylation but does not mediate the injury associated with p38-MAPK activation during myocardial ischemia. Cell Stress and Chaperones, 14(5), 477-489. https://doi.org/10.1007/s12192-009-0101-5
• Middeldorp, J., Kamphuis, W., Sluijs, J. A., Achoui, D., Leenaars, C. H., Feenstra, M. G., …Hol, E. M. (2009). Intermediate filament transcription in astrocytes is repressed by proteasome inhibition. FASEB Journal, 23(8), 2710-2726. https://doi.org/10.1096/fj.08-127696
• Song, S., Landsbury, A., Dahm, R., Liu, Y., Zhang, Q., & Quinlan, R. A. (2009). Functions of the intermediate filament cytoskeleton in the eye lens. Journal of Clinical Investigation, 119(7), 1837-1848. https://doi.org/10.1172/jci38277
• Sreseli, R., Quinlan, P., Quinlan, R., Hadad, S., Bray, S., Kellock, D., …Thompson, A. (2009). ASSOCIATION OF AB-CRYSTALLIN, VIMENTIN WITH POOR PROGNOSIS IN PRIMARY BREAST CANCER. Annals of Oncology, 20,
• Sreseli, R., Quinlan, P., Quinlan, R., Bray, S., Kellok, D., Baker, L., …Thompson, A. (2009). NF-kB Complex Activation and Association of alpha B-Crystallin and Vimentin with Poor Prognosis in Primary Breast Cancer. Cancer Research, 69(24), Article 2143
• Quinlan, P., Sreseli, R., Quinlan, R., Hadad, S., Bray, S., Kernohan, N., …Thompson, A. (2009). alpha B-crystallin, vimentin and increased p53 expression levels in breast cancer is associated with poor prognosis. Cancer Research, 69(2 Suppl), 321S-322S. https://doi.org/10.1158/0008-5472.sabcs-5070
• Saunter, C. D., Perng, M. D., Love, G. D., & Quinlan, R. A. (2009). Stochastically determined directed movement explains the dominant small-scale mitochondrial movements within non- neuronal tissue culture cells. FEBS Letters, 583(8), 1267-1273. https://doi.org/10.1016/j.febslet.2009.02.041
• Perng, M., Wen, S., Gibbon, T., Middeldorp, J., Sluijs, J., Hol, E. M., & Quinlan, R. A. (2008). Glial Fibrillary Acidic Protein Filaments Can Tolerate the Incorporation of Assembly-compromised GFAP-delta, but with Consequences for Filament Organization and alpha B-Crystallin Association. Molecular Biology of the Cell, 19(10), 4521-4533. https://doi.org/10.1091/mbc.e08-03-0284
• Sugiyama, Y., Prescott, A. R., Tholozan, F. M., Ohno, S., & Quinlan, R. A. (2008). Expression and localisation of apical junctional complex proteins in lens epithelial cells. Experimental Eye Research, 87(1), 64-70. https://doi.org/10.1016/j.exer.2008.03.017
• Hayes, V. H., Devlin, G., & Quinlan, R. A. (2008). Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells. Journal of Biological Chemistry, 283(16), 10500-10512. https://doi.org/10.1074/jbc.m706453200
• Srinivasan, R., Forman, S., Quinlan, R., Ohanian, J., & Ohanian, V. (2008). Regulation of contractility by Hsp27 and Hic-5 in rat mesenteric small arteries. American Journal of Physiology - Heart and Circulatory Physiology, 294(2), H961-H969. https://doi.org/10.1152/ajpheart.00939.2007
• Tholozan, F., Gribbon, C., Li, Z., Goldberg, M., Prescott, A., McKie, N., & Quinlan, R. (2007). FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability. Molecular Biology of the Cell, 18(11), 4222-4231. https://doi.org/10.1091/mbc.e06-05-0416
• Tholozan, F., & Quinlan, R. (2007). Lens cells: More than meets the eye. International Journal of Biochemistry and Cell Biology, 39(10), 1754-1759
• Dahm, R., Procter, J., Ireland, M., Lo, W., Mogensen, M., Quinlan, R., & Prescott, A. (2007). Reorganization of centrosomal marker proteins coincides with epithelial cell differentiation in the vertebrate lens. Experimental Cell Research, 85(5), 696-713. https://doi.org/10.1016/j.exer.2007.07.022
• Quinlan, R., Brenner, M., Goldman, J., & Messing, A. (2007). GFAP and its role in Alexander disease. Experimental Cell Research, 313(10), 2077-87
• Perng, M., Zhang, Q., & Quinlan, R. (2007). Insights into the beaded filament of the eye lens. Experimental Cell Research, 313(10), 2180-8
• Tholozan, F., Sanderson, J., & Quinlan, R. (2007). Focus on Molecules : FoxE3. Experimental Eye Research, 84, 799-800. https://doi.org/10.1016/j.exer.2006.01.022
• Perng, M., Su, M., Wen, S., Li, R., Gibbon, T., Prescott, A., …Quinlan, R. (2006). The Alexander disease-causing Glial Fibrillary Acidic Protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alphaB-crystallin and HSP27. American Journal of Human Genetics, 79(2), 197-213. https://doi.org/10.1086/504411
• Rose, K., Gourdie, R., Prescott, A., Quinlan, R., Crouch, R., & Schey, K. (2006). The C terminus of lens aquaporin 0 interacts with the cytoskeletalproteins filensin and CP49. Investigative Ophthalmology & Visual Science, 47(4), 1562-1570
• Pigaga, V., & Quinlan, R. (2006). Lenticular chaperones suppress the aggregation of the cataract-causingmutant T5P gamma C-crystallin. Experimental Cell Research, 312(1), 51-62
• Kabir, A., Cao, X., Gorog, D., Tanno, M., Bassi, R., Bellahcene, M., …Marber, M. (2005). Antimycin A induced cardioprotection is dependent on pre-ischemicp38-MAPK activation but independent of MKK3. Journal of Molecular and Cellular Cardiology, 39(4), 709-717
• Quinlan, R., & Straughan, B. (2005). Decay bounds in a model for aggregation of microglia: application toAlzheimer's disease senile plaques. Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences, 461(2061), 2887-2897
• Hsiao, V., Tian, R., Long, H., Perng, M., Brenner, M., Quinlan, R., & Goldman, J. (2005). Alexander-disease mutation of GFAP causes filament disorganization anddecreased solubility of GFAP. Journal of Cell Science, 118(9), 2057-2065
• Treweek, T., Rekas, A., Lindner, R., Walker, M., Aquilina, J., Robinson, C., …Carver, J. (2005). R120G alpha B-crystallin promotes the unfolding of reducedalpha-lactalbumin and is inherently unstable. The FEBS Journal, 272(3), 711-724
• Golenhofen, N., Perng, M., Quinlan, R., & Drenckhahn, D. (2004). Comparison of the small heat shock proteins alpha B-crystallin, MKBP,HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochemistry and Cell Biology, 122(5), 415-425
• Gorog, D., Tanno, M., Fisher, S., Bin Cao, X., Bellahcene, M., Kabir, A., …Marber, M. (2004). MAPKAPK-2 and serine phospharylation of HSP25/27 and alpha B-crystallindo not increase myocardial resistance to infarction. Circulation, 110(17), 67-67
• 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
• Owens, D., Wilson, N., Hill, A., Rugg, E., Porter, R., Hutcheson, A., …Lane, E. (2004). Human keratin 8 mutations that disturb filament assembly observed ininflammatory bowel disease patients. Journal of Cell Science, 117(10), 1989-1999
• Sandilands, A., Wang, X., Hutcheson, A., James, J., Prescott, A., Wegener, A., …Quinlan, R. (2004). Bfsp2 mutation found in mouse 129 strains causes the loss of CP49 andinduces vimentin-dependent changes in the lens fibre cell cytoskeleton. Experimental Eye Research, 78(1), 109-123
• Gorog, D., Tanno, M., Cao, X., Bellahcene, M., Bassi, R., Kabir, A., …Marber, M. (2004). Inhibition of p38 MAPK activity falls to attenuate contractiledysfunction in a mouse model of low-flow ischemia. Cardiovascular Research, 61(1), 123-131
• Tanno, M., Gorog, D., Bellahcene, M., Cao, X., Quinlan, R., & Marber, M. (2003). Tumor necrosis factor-induced protection of the murine heart isindependent of p38-MAPK activation. Journal of Molecular and Cellular Cardiology, 35(12), 1523-1527
• Fischer, R., Quinlan, R., & Fowler, V. (2003). Tropomodulin binds to filensin intermediate filaments. FEBS Letters, 547(1-3), 228-232
• van den IJssel, P., Wheelock, R., Prescott, A., Russell, P., & Quinlan, R. (2003). Nuclear speckle localisation of the small heat shock protein alphaB-crystallin and its inhibition by the R120G cardiomyopathy-linkedmutation. Experimental Cell Research, 287(2), 249-261
• Sandilands, A., Prescott, A., Wegener, A., Zoltoski, R., Hutcheson, A., Masaki, S., …Quinlan, R. (2003). Knockout of the intermediate filament protein CP49 destabilises thelens fibre cell cytoskeleton and decreases lens optical quality, butdoes not induce cataract. Experimental Eye Research, 76(3), 385-391
• Markiewicz, E., Dechat, T., Foisner, R., Quinlan, R., & Hutchison, C. (2002). Lamin A/C binding protein LAP2 alpha is required for nuclear anchorageof retinoblastoma protein. Molecular Biology of the Cell, 13(12), 4401-4413. https://doi.org/10.1091/mbc.e02-07-0450
• Negre-Aminou, P., van Leeuwen, R., van Thiel, G., van den IJssel, P., de Jong, W., Quinlan, R., & Cohen, L. (2002). Differential effect of simvastatin on activation of Rac(1) vs.activation of the heat shock protein 27-mediated pathway upon oxidativestress, in human smooth muscle cells. Biochemical Pharmacology, 64(10), 1483-1491
• Sandilands, A., Hutcheson, A., Long, H., Prescott, A., Vrensen, G., Löster, J., …Quinlan, R. (2002). Altered aggregation properties of mutant gamma-crystallins cause inherited cataract. The EMBO Journal, 21(22), 6005-6014. https://doi.org/10.1093/emboj/cdf609
• Gribbon, C., Dahm, R., Prescott, A., & Quinlan, R. (2002). Association of the nuclear matrix component NuMA with the Cajal bodyand nuclear speckle compartments during transitions in transcriptionalactivity in lens cell differentiation. European Journal of Cell Biology, 81(10), 557-566. https://doi.org/10.1078/0171-9335-00275
• Masaki, S., Yonezawa, S., & Quinlan, R. (2002). Localization of two conserved cis-acting enhancer regions for thefilensin gene promoter that direct lens-specific expression. Experimental Eye Research, 75(3), 295-305
• Berry, V., Francis, P., Reddy, M., Collyer, D., Vithana, E., MacKay, I., …Quinlan, R. (2002). Theoretical considerations regarding the study "Alpha-B crystallin gene(CRYAB) mutation causes dominant congenital posterior polar cataract inhumans" - Reply. American Journal of Human Genetics, 71(3), 685-686
• Verschuure, P., Croes, Y., van den IJssel, P., Quinlan, R., de Jong, W., & Boelens, W. (2002). Translocation of small heat shock proteins to the actin cytoskeletonupon proteasomal inhibition. Journal of Molecular and Cellular Cardiology, 34(2), 117-128
• Berry, V., Francis, P., Reddy, M., Collyer, D., Vithana, E., MacKay, I., …Quinlan, R. (2001). Alpha-b crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. American Journal of Human Genetics, 69(5), 1141-1145. https://doi.org/10.1086/324158
• Martin, J., Avkiran, M., Quinlan, R., Cohen, P., & Marber, M. (2001). Antiischemic effects of SB203580 are mediated through the inhibition ofp38 alpha mitogen-activated protein kinase - Evidence from ectopicexpression of an inhibition-resistant kinase. Circulation Research, 89(9), 750-752
• Kleinjan, D., Seawright, A., Schedl, A., Quinlan, R., Danes, S., & van Heyningen, V. (2001). Aniridia-associated translocations, DNase hypersensitivity, sequencecomparison and transgenic analysis redefine the functional domain ofPAX6. Human Molecular Genetics, 10(19), 2049-2059
• Venables, R., McLean, S., Luny, D., Moteleb, E., Morley, S., Quinlan, R., …Hutchison, C. (2001). Expression of individual lamins in basal cell carcinomas of the skin. British Journal of Cancer, 84(4), 512-519. https://doi.org/10.1054/bjoc.2000.1632
• Lengler, J., Krausz, E., Tomarev, S., Prescott, A., Quinlan, R., & Graw, J. (2001). Antagonistic action of Six3 and Prox1 at the gamma-crystallin promoter. Nucleic Acids Research, 29(2), 515-526
• Carter, J., McLean, W., West, S., & Quinlan, R. (2000). Mapping of the human CP49 gene and identification of an intragenicpolymorphic marker to allow genetic linkage analysis in autosomaldominant congenital cataract. Biochemical and Biophysical Research Communications, 270(2), 432-436
• Ireland, M., Wallace, P., Sandilands, A., Poosch, M., Kasper, M., Graw, J., …Quinlan, R. (2000). Up-regulation of novel intermediate filament proteins in primary fibercells: An indicator of all vertebrate lens fiber differentiation?
• Der Perng, M., Muchowski, P., van den IJssel, P., Wu, G., Hutcheson, A., Clark, J., & Quinlan, R. (1999). The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction withintermediate filaments in vitro. Journal of Biological Chemistry, 274(47), 33235-33243. https://doi.org/10.1074/jbc.274.47.33235
• Perng, M., Cairns, L., van den IJssel, P., Prescott, A., Hutcheson, A., & Quinlan, R. (1999). Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin. Journal of Cell Science, 112(13), 2099-2112
• Dahm, R., Van Marle, J., Prescott, A., & Quinlan, R. (1999). Gap junctions containing alpha 8-connexin (MP70) in the adult mammalianlens epithelium suggests a re-evaluation of its role in the lens. Experimental Eye Research, 69(1), 45-56
• Eyers, P., van den Ijssel, P., Quinlan, R., Goedert, M., & Cohen, P. (1999). Use of a drug-resistant mutant of stress-activated protein kinase2a/p38 to validate the in vivo specificity of SE 203580. FEBS Letters, 451(2), 191-196
• Porter, R., Hutcheson, A., Rugg, E., Quinlan, R., & Lane, E. (1998). cDNA Cloning, Expression, and Assembly Characteristics of Mouse Keratin 16. Journal of Biological Chemistry, 273(48), 32265-32272. https://doi.org/10.1074/jbc.273.48.32265
• Klopp, N., Loster, J., Lutz, R., Neuhaauser-Klaus, A., Prescott, A., Pretsch, W., …Graw, J. (1998). Three murine cataract mutants (Cat2) are defective in differentgamma-crystallin genes. Genomics, 52(2), 152-158
• Masaki, S., Kamachi, Y., Quinlan, R., Yonezawa, S., & Kondoh, H. (1998). Identification and functional analysis of the mouse lens filensin genepromoter. Gene, 214(1-2), 77-86
• Dahm, R., Gribbon, C., Quinlan, R., & Prescott, A. (1998). Changes in the nucleolar and coiled body compartments precede laminaand chromatin reorganization during fibre cell denucleation in thebovine lens. European Journal of Cell Biology, 75(3), 237-246. https://doi.org/10.1016/s0171-9335%2898%2980118-0
• Masaki, S., & Quinlan, R. (1997). Gene structure and sequence comparisons of the eye lens specificprotein, filensin, from rat and mouse: implications for proteinclassification and assembly. Gene, 201(1-2), 11-20
• Pugh, G., Coates, P., Lane, E., Raymond, Y., & Quinlan, R. (1997). Distinct nuclear assembly pathways for lamins A and C lead to theirincrease during quiescence in Swiss 3T3 cells. Journal of Cell Science, 110, 2483-2493
• Dyer, J., Kill, I., Pugh, G., Quinlan, R., Lane, E., & Hutchison, C. (1997). Cell cycle changes in A-type lamin associations detected in humandermal fibroblasts using monoclonal antibodies. Chromosome Research, 5(6), 383-394
• Krausz, E., Augusteyn, R., Quinlan, R., Reddan, J., Russell, P., Sax, C., & Graw, J. (1996). Expression of crystallins, Pax6, filensin, CP49, MIP, and MP20 inlens-derived cell lines. Investigative Ophthalmology & Visual Science, 37(10), 2120-2128
• Chou, Y., Opal, P., Quinlan, R., & Goldman, R. (1996). The relative roles of specific N- and C-terminal phosphorylation sitesin the disassembly of intermediate filament in mitotic BHK-21 cells. Journal of Cell Science, 109, 817-826
• Sandilands, A., Prescott, A., Hutcheson, A., QUINLAN, R., Casselman, J., & Fitzgerald, P. (1995). FILENSIN IS PROTEOLYTICALLY PROCESSED DURING LENS FIBERCELL-DIFFERENTIATION BY MULTIPLE INDEPENDENT PATHWAYS. European Journal of Cell Biology, 67(3), 238-253
• Sandilands, A., Prescott, A., Carter, J., Hutcheson, A., QUINLAN, R., Richards, J., & Fitzgerald, P. (1995). VIMENTIN AND CP49 FILENSIN FORM DISTINCT NETWORKS IN THE LENS WHICH AREINDEPENDENTLY MODULATED DURING LENS FIBER CELL-DIFFERENTIATION. Journal of Cell Science, 108, 1397-1406
• Carter, J., Hutcheson, A., & QUINLAN, R. (1995). IN-VITRO STUDIES ON THE ASSEMBLY PROPERTIES OF THE LENS PROTEINS CP49,CP115 - COASSEMBLY WITH ALPHA-CRYSTALLIN BUT NOT WITH VIMENTIN. Experimental Eye Research, 60(2), 181-192
• Ralton, J., Lu, X., Hutcheson, A., & QUINLAN, R. (1994). IDENTIFICATION OF 2 N-TERMINAL NON-ALPHA-HELICAL DOMAIN MOTIFSIMPORTANT IN THE ASSEMBLY OF GLIAL FIBRILLARY ACIDIC PROTEIN. Journal of Cell Science, 107, 1935-1948
• Nicholl, I., & QUINLAN, R. (1994). CHAPERONE ACTIVITY OF ALPHA-CRYSTALLINS MODULATES INTERMEDIATE FILAMENTASSEMBLY. The EMBO Journal, 13(4), 945-953
• Lu, X., QUINLAN, R., Steel, J., & Lane, E. (1993). NETWORK INCORPORATION OF INTERMEDIATE FILAMENT MOLECULES DIFFERSBETWEEN PREEXISTING AND NEWLY ASSEMBLING FILAMENTS. Experimental Cell Research, 208(1), 218-225
• QUINLAN, R., Carter, J., Hutcheson, A., & Campbell, D. (1992). THE 53KDA POLYPEPTIDE COMPONENT OF THE BOVINE FIBER CELL CYTOSKELETONIS DERIVED FROM THE 115KDA BEADED FILAMENT PROTEIN - EVIDENCE FOR AFIBER CELL SPECIFIC INTERMEDIATE FILAMENT PROTEIN. Current Eye Research, 11(9), 909-921
• Moir, R., QUINLAN, R., & Stewart, M. (1990). EXPRESSION AND CHARACTERIZATION OF HUMAN LAMIN-C. FEBS Letters, 268(1), 301-305
• Stewart, M., QUINLAN, R., & Moir, R. (1989). MOLECULAR-INTERACTIONS IN PARACRYSTALS OF A FRAGMENT CORRESPONDING TOTHE ALPHA-HELICAL COILED-COIL ROD PORTION OF GLIAL FIBRILLARY ACIDICPROTEIN - EVIDENCE FOR AN ANTIPARALLEL PACKING OF MOLECULES ANDPOLYMORPHISM RELATED TO INTERMEDIATE FILAMENT STRUCTURE. Journal of Cell Biology, 109(1), 225-234
• QUINLAN, R., Moir, R., & Stewart, M. (1989). EXPRESSION IN ESCHERICHIA-COLI OF FRAGMENTS OF GLIAL FIBRILLARY ACIDICPROTEIN - CHARACTERIZATION, ASSEMBLY PROPERTIES AND PARACRYSTALFORMATION. Journal of Cell Science, 93, 71-83
• Little, M., QUINLAN, R., Rohricht, C., & Diez, J. (1987). STRUCTURAL DIFFERENCES BETWEEN BLOOD-PLATELET TUBULIN AND OTHERMAMMALIAN TUBULINS. Biochimica et biophysica acta, 916(1), 83-88
• QUINLAN, R., & Stewart, M. (1987). CRYSTALLINE TUBES OF MYOSIN SUBFRAGMENT-2 SHOWING THE COILED-COIL ANDMOLECULAR INTERACTION GEOMETRY. Journal of Cell Biology, 105(1), 403-415
• QUINLAN, R., Hatzfeld, M., Franke, W., Lustig, A., Schulthess, T., & Engel, J. (1986). CHARACTERIZATION OF DIMER SUBUNITS OF INTERMEDIATE FILAMENT PROTEINS. Journal of Molecular Biology, 192(2), 337-349
• Soellner, P., QUINLAN, R., & Franke, W. (1985). IDENTIFICATION OF A DISTINCT SOLUBLE SUBUNIT OF AN INTERMEDIATEFILAMENT PROTEIN - TETRAMERIC VIMENTIN FROM LIVING CELLS. Proceedings of the National Academy of Sciences, 82(23), 7929-7933
• Little, M., Luduena, R., QUINLAN, R., Ponstingl, H., Krauhs, E., & Raff, E. (1984). SOME ASPECTS OF TUBULIN STRUCTURE AND TISSUE-SPECIFICITY. Journal of submicroscopic cytology and pathology, 16(1), 11-13
• Bowden, P., QUINLAN, R., Breitkreutz, D., & Fusenig, N. (1984). PROTEOLYTIC MODIFICATION OF ACIDIC AND BASIC KERATINS DURING TERMINALDIFFERENTIATION OF MOUSE AND HUMAN-EPIDERMIS. European journal of biochemistry (Internet), 142(1), 29-36. https://doi.org/10.1111/j.1432-1033.1984.tb08246.x
• QUINLAN, R., Cohlberg, J., Schiller, D., Hatzfeld, M., & Franke, W. (1984). HETEROTYPIC TETRAMER (A2D2) COMPLEXES OF NON-EPIDERMAL KERATINSISOLATED FROM CYTOSKELETONS OF RAT HEPATOCYTES AND HEPATOMA-CELLS. Journal of Molecular Biology, 178(2), 365-388
• QUINLAN, R., & Franke, W. (1983). MOLECULAR-INTERACTIONS IN INTERMEDIATE-SIZED FILAMENTS REVEALED BYCHEMICAL CROSS-LINKING - HETEROPOLYMERS OF VIMENTIN AND GLIAL FILAMENTPROTEIN IN CULTURED HUMAN GLIOMA-CELLS. European journal of biochemistry (Internet), 132(3), 477-484. https://doi.org/10.1111/j.1432-1033.1983.tb07386.x
• Little, M., QUINLAN, R., Hoffman, E., & Luduena, R. (1983). IDENTIFICATION AND CHARACTERIZATION OF AXOPODIAL TUBULINS FROMECHINOSPHAERIUM-NUCLEOFILUM. European Journal of Cell Biology, 31(1), 55-61
• Quinlan, R., & Franke, W. (1982). Heteropolymer Filaments of Vimentin and Desmin in Vascular Smooth Muscle Tissue and Cultured Baby Hamster Kidney Cells Demonstrated by Chemical Crosslinking. Proceedings of the National Academy of Sciences, 79(11), 3452-3456. https://doi.org/10.1073/pnas.79.11.3452