Staff profile

I joined the University of Durham in 2001 as the foundation chair in Biomedical Sciences.  Since October 2020 I have held an Emeritus position as Professor of Biomedical Sciences at the University of Durham. I have also held an affiliate Professorship at the Department of Neurobiology and Biophysics at the University of Washington in Seattle since 2010. I spent a sabbatical year in the Department of Biophysics, hosted by Professor John I Clark, and we continue to collaborate on eye lens transparency, optical function and aging due to our common interest in the cytoskeleton, protein chaperones and protein phase separation mechanisms.  

My other interests are regionally based and have been greatly influenced by my service on grant panels and as a trustee to the charity, Fight for Sight. This charity is the most important UK charity dedicated to eye research and social change research into vision loss. I am working with Professors David Steel (South Tyneside and Sunderland Foundation Trust) and Matt Campbell (University of Sunderland) and others to form and launch an institute dedicated to ophthalmic research and innovation. This institute will capitalise on the ability of eye health data to detect and inform on both eye and systemic diseases such as cardiovascular disease, stroke and neurodegenerative diseases and so help change the poor health metrics in our region. I enjoy working with regional partners such as the Sunderland City Council, the Beacon of Light and the Sunderland and County Durham Royal Society for the Blind.

I am originally a Biochemistry graduate and PhD from the University of Kent where I worked on microtubules with Professor Keith Gull FRS, before taking up an Alexander von Humboldt fellowship in 1981 at the German Cancer Research Centre to work on Intermediate Filaments with Professor Werner Franke. I discovered that keratins, GFAP, vimentin and desmin all form dimeric coiled coils that further self-associate to form tetrameric units, which could also be isolated from the soluble fraction of cells. In 1985 I returned to the UK on a MRC fellowship to work with Dr Murray Stewart at the LMB Cambridge.  Here I determined the coiled coil pitch of myosin LS2 and continued my studies on the paracrystal assembly properties of GFAP and nuclear lamins. In 1988, I was appointed as a lecturer to the Department of Biochemistry in Dundee. This allowed me to form a research team focused on vimentin, GFAP and desmin. We discovered that these intermediate filament proteins interacted with small heat shock protein chaperones and this led to the concept of intermediate filaments are bone fide components of the cellular stress response (see image above). In the eye, there are two other intermediate filament proteins called BFSP1 and BFSP2. Both are key to the optical function of the lens, which we discovered through gene knockout in a mouse model. Emmetropia establishment depends on this lens cytoskeleton and lens transparency, as regulated by water channels, also depends upon the cytoskeleton. The most dramatic biological feature of the eye lens though, is its ability to function for decades, and in some animals, for centuries, without significant biomolecular replacement. The eye lens is an aging exemplar par excellence as it accumulates ageing-mediated damage and adjusts its protein organisation to maintain its function.

• 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

• Purification of Protein Chaperones and Their Functional Assays with Intermediate Filaments.
  
  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 (pp. 155-175). Elsevier. https://doi.org/10.1016/bs.mie.2015.07.025

Conference Paper

• Terahertz spectroscopy of stem cells
  
  Zinov’ev, N., Jahoda, C., Quinlan, R., & Chamberlain, J. (2007). Terahertz spectroscopy of stem cells. Presented at 2007 JOINT 32ND INTERNATIONAL CONFERENCE ON INFRARED AND MILLIMETER WAVES AND 15TH INTERNATIONAL CONFERENCE ON TERAHERTZ ELECTRONICS, VOLS 1 AND 2.

Journal Article

• Multimorbidity Through the Lens of the Eye: Pathogenic Variants for Multiple Systemic Disorders Found in an Autosomal Dominant Congenital Cataract Cohort
  
  Berry, V., Ponnekanti, M. B., Aychoua, N., Ionides, A., Tsika, C., Quinlan, R. A., & Michaelides, M. (2025). Multimorbidity Through the Lens of the Eye: Pathogenic Variants for Multiple Systemic Disorders Found in an Autosomal Dominant Congenital Cataract Cohort. Genes, 16(5), Article 604. https://doi.org/10.3390/genes16050604
• Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro
  
  Young, N., Gui, Z., Mustafa, S., Papa, K., Jessop, E., Ruddell, E., Bevington, L., Quinlan, R. A., Benham, A. M., Goldberg, M. W., Obara, B., & Karakesisoglou, I. (2024). Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro. Cells, 13(11), Article 906. https://doi.org/10.3390/cells13110906
• The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.
  
  Al-Ansari, M., Fitzsimons, T., Wei, W., Goldberg, M. W., Kunieda, T., & Quinlan, R. A. (2024). The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone. Cell Stress and Chaperones, 29(1), 51-65. https://doi.org/10.1016/j.cstres.2023.12.001
• The redox-responsive roles of intermediate filaments in cellular stress detection, integration and mitigation
  
  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
• A novel frameshift variant in BCOR causes congenital nuclear cataract
  
  Berry, V., Ponnekanti, M. B., Pontikos, N., Quinlan, R. A., & Michaelides, M. (2024). A novel frameshift variant in BCOR causes congenital nuclear cataract. Ophthalmic Genetics, 45(6), 591-595. https://doi.org/10.1080/13816810.2024.2373248
• Evaluation of cataract formation in fish exposed to environmental radiation at Chernobyl and Fukushima
  
  Lerebours, A., Regini, J., Quinlan, R. A., Wada, T., Pierscionek, B., Devonshire, M., Kalligeraki, A. A., Uwineza, A., Young, L., Girkin, J. M., Warwick, P., Smith, K., Hoshino, M., Uesugi, K., Yagi, N., Terrill, N., Shebanova, O., Snow, T., & Smith, J. T. (2023). Evaluation of cataract formation in fish exposed to environmental radiation at Chernobyl and Fukushima. Science of The Total Environment, 902, Article 165957. https://doi.org/10.1016/j.scitotenv.2023.165957
• Independent Membrane Binding Properties of the Caspase Generated Fragments of the Beaded Filament Structural Protein 1 (BFSP1) Involves an Amphipathic Helix
  
  Jarrin, M., Kalligeraki, A. A., Uwineza, A., Cawood, C. S., Brown, A. P., Ward, E. N., Le, K., Freitag-Pohl, S., Pohl, E., Kiss, B., Tapodi, A., & 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, 12(12), Article 1580. https://doi.org/10.3390/cells12121580
• Identification and quantification of ionising radiation-induced oxysterol formation in membranes of lens fibre cells
  
  Uwineza, A., Cummins, I., Jarrin, M., Kalligeraki, A. K., Barnard, S., Mol, M., Degani, G., Altomare, A. A., Aldini, G., Schreurs, A., Balschun, D., Ainsbury, E. A., Dias, I. H., & 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
• 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
  
  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
• Variants in PAX6, PITX3 and HSF4 causing autosomal dominant congenital cataracts
  
  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
• 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
  
  Quinlan, P. R., Figeuredo, G., Mongan, N., Jordan, L. B., Bray, S. E., Sreseli, R., Ashfield, A., Mitsch, J., van den Ijssel, P., Thompson, A. M., & 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
• A recurrent variant in LIM2 causes an isolated congenital sutural/lamellar cataract in a Japanese family
  
  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
• Pathogenic variants in the CYP21A2 gene cause isolated autosomal dominant congenital posterior polar cataracts
  
  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
• On the Nature of Murine Radiation-Induced Subcapsular Cataracts: Optical Coherence Tomography-Based Fine Classification, In Vivo Dynamics and Impact on Visual Acuity
  
  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
• Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens
  
  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
• 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
  
  Wu, W., Lois, N., Prescott, A. R., Brown, A. P., Van Gerwen, V., Tassignon, M., Richards, S. A., Saunter, C., Jarrin, 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
• Joining European Scientific Forces to Face Pandemics
  
  Vasconcelos, M. H., Alcaro, S., Arechavala-Gomeza, V., Baumbach, J., Borges, F., Brevini, T. A., Rivas, J. D. L., Devaux, Y., Hozak, P., Keinänen-Toivola, M. M., Lattanzi, G., Mohr, T., Murovska, M., Prusty, B. K., Quinlan, R. A., Pérez-Sala, D., Scheibenbogen, C., Schmidt, H. H., Silveira, I., … 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
• Lens Epithelial Cell Proliferation in Response to Ionizing Radiation
  
  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
• Whole Exome Sequencing Reveals Novel and Recurrent Disease-Causing Variants in Lens Specific Gap Junctional Protein Encoding Genes Causing Congenital Cataract
  
  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
• Three-dimensional data capture and analysis of intact eye lenses evidences emmetropia-associated changes and strain-dependent differences in epithelial cell organization
  
  Kalligeraki, A. A., Isted, A., Pal, R., Saunter, C., Girkin, J., Jarrin, M., Uwineza, A., Obara, B., & 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
• A novel missense mutation in LIM2 causing isolated autosomal dominant congenital cataract
  
  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
• The genetic landscape of crystallins in congenital cataract
  
  Berry, V., Ionides, A., Pontikos, N., Georgiou, M., Yu, J., Ocaka, L. A., Moore, A. T., Quinlan, R. 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
• Site-specific phosphorylation and caspase cleavage of GFAP are new markers of Alexander Disease severity
  
  Battaglia, R. A., Beltran, A. S., Delic, S., Dumitru, R., Robinson, J. A., Kabiraj, P., Herring, L. E., Madden, V. J., Ravinder, N., Willems, E., Newman, R. A., Quinlan, R. A., Goldman, J. E., Perng, M., Inagaki, M., & 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
• BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability
  
  Tapodi, A., Clemens, D., Uwineza, A., Goldberg, M., Thinon, E., Heal, W., Tate, E., Nemeth-Cahalan, K., Vorontsova, I., Jarrin, M., Hall, J., & 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
• Cataractogenic load – a concept to study the contribution of ionizing radiation to accelerated aging in the eye lens
  
  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, 779, 68-81. https://doi.org/10.1016/j.mrrev.2019.02.004
• Inverse dose-rate effect of ionising radiation on residual 53BP1 foci in the eye lens
  
  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
• Heat shock proteins are differentially expressed in brain and spinal cord: implications for multiple sclerosis
  
  Gorter, R. P., Nutma, E., Jahreiβ M., de Jonge, J. C., Quinlan, R., van der Valk, P., van Noort, J. M., Baron, W., & 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
• Non-invasive in vivo quantification of the developing optical properties and graded index of the embryonic eye lens using SPIM
  
  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
• A rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks
  
  Quinlan, R., Schwartz, N., Windoffer, R., Richardson, C., Hawkins, T., Broussard, J., Green, K., & 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
• αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments
  
  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
• The functional roles of the unstructured N- and C-terminal regions in alphaB-crystallin and other mammalian small heat-shock proteins
  
  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
• The impact of circadian rhythms on medical imaging and radiotherapy regimes for the paediatric patient
  
  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
• Sub-nanometre mapping of the aquaporin-water interface with multifrequency atomic force microscopy
  
  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
• Biophysical dissection of schistosome septins: Insights into oligomerization and membrane binding
  
  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
• The Lipidation Profile of Aquaporin-0 Correlates with The Acyl Composition of Phosphoethanolamine Lipids in Lens Membranes
  
  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
• Small molecules, both dietary and endogenous, influence the onset of lens cataracts
  
  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
• Radiation protection of the eye lens in medical workers—basis and impact of the ICRP recommendations
  
  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
• A new dawn for cataracts
  
  Quinlan, R. (2015). A new dawn for cataracts. Science, 350(6261), 636-637. https://doi.org/10.1126/science.aad6303
• 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
  
  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
• The lens of the eye: exposures in the UK medical sector and mechanistic studies of radiation effects
  
  Bouffler, S., Peters, S., Gilvin, P., Slack, K., Markiewicz, E., Quinlan, R., 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. https://doi.org/10.1177/0146645314560693
• Nonlinear ionizing radiation-induced changes in eye lens cell proliferation, cyclin D1 expression and lens shape
  
  Markiewicz, E., Barnard, S., Haines, J., Coster, M., Geel, O. van, Wu, W., Richards, S., Ainsbury, E., Rothkamm, K., Bouffler, S., & 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
• A silk purse from a sow’s ear – bioinspired materials based on α-helical coiled coils
  
  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
• A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells
  
  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
• Caspase cleavage of GFAP produces an assembly-compromised proteolytic fragment that promotes filament aggregation
  
  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. ASN NEURO, 5(5). https://doi.org/10.1042/an20130032
• The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability
  
  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
• Chaperones: needed for both the good times and the bad times
  
  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
• 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
  
  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
• Evolution of the vertebrate beaded filament protein, Bfsp2; comparing the in vitro assembly properties of a “tailed” zebrafish Bfsp2 to its “tailless” human orthologue.
  
  Qu, B., Landsbury, A., Schoenthaler, H. B., Dahm, R., Liu, Y., Clark, J. I., Prescott, A. R., & 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
• Multiple Sites in alpha B-Crystallin Modulate Its Interactions with Desmin Filaments Assembled In Vitro
  
  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
• Homeostasis in the vertebrate lens: mechanisms of solute exchange
  
  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
• 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
  
  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
• 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
  
  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
• A cell polarity protein aPKCλ is required for eye lens formation and growth
  
  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
• 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
  
  Gorog, D. A., Jabr, R. I., Tanno, M., Sarafraz, N., Clark, J. E., Fisher, S. G., Cao, X. B., Bellahcene, M., Dighe, K., Kabir, A. M., Quinlan, R. A., Kato, K., Gaestel, M., Marber, M. S., & 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 \& CHAPERONES, 14(5), 477-489. https://doi.org/10.1007/s12192-009-0101-5
• Intermediate filament transcription in astrocytes is repressed by proteasome inhibition
  
  Middeldorp, J., Kamphuis, W., Sluijs, J. A., Achoui, D., Leenaars, C. H., Feenstra, M. G., van Tijn, P., Fischer, D. F., Berkers, C., Ovaa, H., Quinlan, R. A., & 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
• Functions of the intermediate filament cytoskeleton in the eye lens
  
  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
• ASSOCIATION OF AB-CRYSTALLIN, VIMENTIN WITH POOR PROGNOSIS IN PRIMARY BREAST CANCER
  
  Sreseli, R., Quinlan, P., Quinlan, R., Hadad, S., Bray, S., Kellock, D., Baker, L., Purdie, C., Jordan, L., & Thompson, A. (2009). ASSOCIATION OF AB-CRYSTALLIN, VIMENTIN WITH POOR PROGNOSIS IN PRIMARY BREAST CANCER. Annals of Oncology, 20.
• alpha B-crystallin, vimentin and increased p53 expression levels in breast cancer is associated with poor prognosis
  
  Quinlan, P., Sreseli, R., Quinlan, R., Hadad, S., Bray, S., Kernohan, N., Kellock, D., Baker, L., Purdie, C., Jordan, L., & 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
• Stochastically determined directed movement explains the dominant small-scale mitochondrial movements within non- neuronal tissue culture cells
  
  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
• NF-kB Complex Activation and Association of alpha B-Crystallin and Vimentin with Poor Prognosis in Primary Breast Cancer
  
  Sreseli, R., Quinlan, P., Quinlan, R., Bray, S., Kellok, D., Baker, L., Jordan, L., Purdie, C., & 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.
• 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
  
  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
• Expression and localisation of apical junctional complex proteins in lens epithelial cells
  
  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
• Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells
  
  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
• Regulation of contractility by Hsp27 and Hic-5 in rat mesenteric small arteries.
  
  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
• FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability
  
  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
• Insights into the beaded filament of the eye lens
  
  Perng, M., Zhang, Q., & Quinlan, R. (2007). Insights into the beaded filament of the eye lens. Experimental Cell Research, 313(10), 2180-8.
• GFAP and its role in Alexander disease
  
  Quinlan, R., Brenner, M., Goldman, J., & Messing, A. (2007). GFAP and its role in Alexander disease. Experimental Cell Research, 313(10), 2077-87.
• Lens cells: More than meets the eye
  
  Tholozan, F., & Quinlan, R. (2007). Lens cells: More than meets the eye. International Journal of Biochemistry and Cell Biology, 39(10), 1754-1759.
• Focus on Molecules : FoxE3
  
  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
• Reorganization of centrosomal marker proteins coincides with epithelial cell differentiation in the vertebrate lens
  
  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
• 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
  
  Perng, M., Su, M., Wen, S., Li, R., Gibbon, T., Prescott, A., Brenner, M., & 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
• The C terminus of lens aquaporin 0 interacts with the cytoskeletalproteins filensin and CP49
  
  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.
• Lenticular chaperones suppress the aggregation of the cataract-causingmutant T5P gamma C-crystallin
  
  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.
• Antimycin A induced cardioprotection is dependent on pre-ischemicp38-MAPK activation but independent of MKK3
  
  Kabir, A., Cao, X., Gorog, D., Tanno, M., Bassi, R., Bellahcene, M., Quinlan, R., Davis, R., Flavell, R., Shattock, 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.
• Decay bounds in a model for aggregation of microglia: application toAlzheimer's disease senile plaques
  
  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.
• Alexander-disease mutation of GFAP causes filament disorganization anddecreased solubility of GFAP
  
  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.
• R120G alpha B-crystallin promotes the unfolding of reducedalpha-lactalbumin and is inherently unstable
  
  Treweek, T., Rekas, A., Lindner, R., Walker, M., Aquilina, J., Robinson, C., Horwitz, J., Perng, M., Quinlan, R., & Carver, J. (2005). R120G alpha B-crystallin promotes the unfolding of reducedalpha-lactalbumin and is inherently unstable. FEBS Journal, 272(3), 711-724.
• Comparison of the small heat shock proteins alpha B-crystallin, MKBP,HSP25, HSP20, and cvHSP in heart and skeletal muscle
  
  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.
• MAPKAPK-2 and serine phospharylation of HSP25/27 and alpha B-crystallindo not increase myocardial resistance to infarction
  
  Gorog, D., Tanno, M., Fisher, S., Bin Cao, X., Bellahcene, M., Kabir, A., Quinlan, R., Kato, K., & 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.
• Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells
  
  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
• Human keratin 8 mutations that disturb filament assembly observed ininflammatory bowel disease patients
  
  Owens, D., Wilson, N., Hill, A., Rugg, E., Porter, R., Hutcheson, A., Quinlan, R., van Heel, D., Parkes, M., Jewell, D., Campbell, S., Ghosh, S., Satsangi, J., & Lane, E. (2004). Human keratin 8 mutations that disturb filament assembly observed ininflammatory bowel disease patients. Journal of Cell Science, 117(10), 1989-1999.
• Inhibition of p38 MAPK activity falls to attenuate contractiledysfunction in a mouse model of low-flow ischemia
  
  Gorog, D., Tanno, M., Cao, X., Bellahcene, M., Bassi, R., Kabir, A., Dighe, K., Quinlan, R., & 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.
• Bfsp2 mutation found in mouse 129 strains causes the loss of CP49 andinduces vimentin-dependent changes in the lens fibre cell cytoskeleton
  
  Sandilands, A., Wang, X., Hutcheson, A., James, J., Prescott, A., Wegener, A., Pekny, M., Gong, X., & 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.
• Tumor necrosis factor-induced protection of the murine heart isindependent of p38-MAPK activation
  
  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.
• Tropomodulin binds to filensin intermediate filaments
  
  Fischer, R., Quinlan, R., & Fowler, V. (2003). Tropomodulin binds to filensin intermediate filaments. FEBS Letters, 547(1-3), 228-232.
• Nuclear speckle localisation of the small heat shock protein alphaB-crystallin and its inhibition by the R120G cardiomyopathy-linkedmutation
  
  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.
• Knockout of the intermediate filament protein CP49 destabilises thelens fibre cell cytoskeleton and decreases lens optical quality, butdoes not induce cataract
  
  Sandilands, A., Prescott, A., Wegener, A., Zoltoski, R., Hutcheson, A., Masaki, S., Kuszak, J., & 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.
• Lamin A/C binding protein LAP2 alpha is required for nuclear anchorageof retinoblastoma protein
  
  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
• 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
  
  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.
• Altered aggregation properties of mutant gamma-crystallins cause inherited cataract
  
  Sandilands, A., Hutcheson, A., Long, H., Prescott, A., Vrensen, G., Löster, J., Klopp, N., Lutz, R., Graw, J., Masaki, S., Dobson, C., MacPhee, C., & Quinlan, R. (2002). Altered aggregation properties of mutant gamma-crystallins cause inherited cataract. EMBO Journal, 21(22), 6005-6014. https://doi.org/10.1093/emboj/cdf609
• Association of the nuclear matrix component NuMA with the Cajal bodyand nuclear speckle compartments during transitions in transcriptionalactivity in lens cell differentiation
  
  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
• Theoretical considerations regarding the study "Alpha-B crystallin gene(CRYAB) mutation causes dominant congenital posterior polar cataract inhumans" - Reply
  
  Berry, V., Francis, P., Reddy, M., Collyer, D., Vithana, E., MacKay, I., Dawson, G., Carey, A., Moore, A., Bhattacharya, S., & 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.
• Localization of two conserved cis-acting enhancer regions for thefilensin gene promoter that direct lens-specific expression
  
  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.
• Translocation of small heat shock proteins to the actin cytoskeletonupon proteasomal inhibition
  
  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.
• Alpha-b crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans
  
  Berry, V., Francis, P., Reddy, M., Collyer, D., Vithana, E., MacKay, I., Dawson, G., Carey, A., Moore, A., Bhattacharya, S., & 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
• Antiischemic effects of SB203580 are mediated through the inhibition ofp38 alpha mitogen-activated protein kinase - Evidence from ectopicexpression of an inhibition-resistant kinase
  
  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.
• Aniridia-associated translocations, DNase hypersensitivity, sequencecomparison and transgenic analysis redefine the functional domain ofPAX6
  
  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.
• Expression of individual lamins in basal cell carcinomas of the skin
  
  Venables, R., McLean, S., Luny, D., Moteleb, E., Morley, S., Quinlan, R., Lane, E., & 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
• Antagonistic action of Six3 and Prox1 at the gamma-crystallin promoter
  
  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.
• Mapping of the human CP49 gene and identification of an intragenicpolymorphic marker to allow genetic linkage analysis in autosomaldominant congenital cataract
  
  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.
• Up-regulation of novel intermediate filament proteins in primary fibercells: An indicator of all vertebrate lens fiber differentiation?
  
  Ireland, M., Wallace, P., Sandilands, A., Poosch, M., Kasper, M., Graw, J., Liu, A., Maisel, H., Prescott, A., Hutcheson, A., Goebel, D., & Quinlan, R. (2000). Up-regulation of novel intermediate filament proteins in primary fibercells: An indicator of all vertebrate lens fiber differentiation? Anatomical Record, 258(1), 25-33.
• The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction withintermediate filaments in vitro
  
  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
• Gap junctions containing alpha 8-connexin (MP70) in the adult mammalianlens epithelium suggests a re-evaluation of its role in the lens
  
  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.
• Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin
  
  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.
• Use of a drug-resistant mutant of stress-activated protein kinase2a/p38 to validate the in vivo specificity of SE 203580
  
  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.
• cDNA Cloning, Expression, and Assembly Characteristics of Mouse Keratin 16
  
  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
• Three murine cataract mutants (Cat2) are defective in differentgamma-crystallin genes
  
  Klopp, N., Loster, J., Lutz, R., Neuhaauser-Klaus, A., Prescott, A., Pretsch, W., Quinlan, R., Sandilands, A., Vrensen, G., & Graw, J. (1998). Three murine cataract mutants (Cat2) are defective in differentgamma-crystallin genes. Genomics, 52(2), 152-158.
• Identification and functional analysis of the mouse lens filensin genepromoter
  
  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.
• Changes in the nucleolar and coiled body compartments precede laminaand chromatin reorganization during fibre cell denucleation in thebovine lens
  
  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
• Gene structure and sequence comparisons of the eye lens specificprotein, filensin, from rat and mouse: implications for proteinclassification and assembly
  
  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.
• Distinct nuclear assembly pathways for lamins A and C lead to theirincrease during quiescence in Swiss 3T3 cells
  
  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.
• Cell cycle changes in A-type lamin associations detected in humandermal fibroblasts using monoclonal antibodies
  
  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.
• Expression of crystallins, Pax6, filensin, CP49, MIP, and MP20 inlens-derived cell lines
  
  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.
• The relative roles of specific N- and C-terminal phosphorylation sitesin the disassembly of intermediate filament in mitotic BHK-21 cells
  
  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.
• FILENSIN IS PROTEOLYTICALLY PROCESSED DURING LENS FIBERCELL-DIFFERENTIATION BY MULTIPLE INDEPENDENT PATHWAYS
  
  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.
• VIMENTIN AND CP49 FILENSIN FORM DISTINCT NETWORKS IN THE LENS WHICH AREINDEPENDENTLY MODULATED DURING LENS FIBER CELL-DIFFERENTIATION
  
  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.
• IN-VITRO STUDIES ON THE ASSEMBLY PROPERTIES OF THE LENS PROTEINS CP49,CP115 - COASSEMBLY WITH ALPHA-CRYSTALLIN BUT NOT WITH VIMENTIN
  
  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.
• IDENTIFICATION OF 2 N-TERMINAL NON-ALPHA-HELICAL DOMAIN MOTIFSIMPORTANT IN THE ASSEMBLY OF GLIAL FIBRILLARY ACIDIC PROTEIN
  
  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.
• CHAPERONE ACTIVITY OF ALPHA-CRYSTALLINS MODULATES INTERMEDIATE FILAMENTASSEMBLY
  
  Nicholl, I., & QUINLAN, R. (1994). CHAPERONE ACTIVITY OF ALPHA-CRYSTALLINS MODULATES INTERMEDIATE FILAMENTASSEMBLY. EMBO Journal, 13(4), 945-953.
• NETWORK INCORPORATION OF INTERMEDIATE FILAMENT MOLECULES DIFFERSBETWEEN PREEXISTING AND NEWLY ASSEMBLING FILAMENTS
  
  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.
• 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
  
  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.
• EXPRESSION AND CHARACTERIZATION OF HUMAN LAMIN-C
  
  Moir, R., QUINLAN, R., & Stewart, M. (1990). EXPRESSION AND CHARACTERIZATION OF HUMAN LAMIN-C. FEBS Letters, 268(1), 301-305.
• 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
  
  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.
• EXPRESSION IN ESCHERICHIA-COLI OF FRAGMENTS OF GLIAL FIBRILLARY ACIDICPROTEIN - CHARACTERIZATION, ASSEMBLY PROPERTIES AND PARACRYSTALFORMATION
  
  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.
• STRUCTURAL DIFFERENCES BETWEEN BLOOD-PLATELET TUBULIN AND OTHERMAMMALIAN TUBULINS
  
  Little, M., QUINLAN, R., Rohricht, C., & Diez, J. (1987). STRUCTURAL DIFFERENCES BETWEEN BLOOD-PLATELET TUBULIN AND OTHERMAMMALIAN TUBULINS. BBA - Biochimica et Biophysica Acta, 916(1), 83-88.
• CRYSTALLINE TUBES OF MYOSIN SUBFRAGMENT-2 SHOWING THE COILED-COIL ANDMOLECULAR INTERACTION GEOMETRY
  
  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.
• CHARACTERIZATION OF DIMER SUBUNITS OF INTERMEDIATE FILAMENT PROTEINS
  
  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.
• IDENTIFICATION OF A DISTINCT SOLUBLE SUBUNIT OF AN INTERMEDIATEFILAMENT PROTEIN - TETRAMERIC VIMENTIN FROM LIVING CELLS
  
  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 Of The United States Of America, 82(23), 7929-7933.
• HETEROTYPIC TETRAMER (A2D2) COMPLEXES OF NON-EPIDERMAL KERATINSISOLATED FROM CYTOSKELETONS OF RAT HEPATOCYTES AND HEPATOMA-CELLS
  
  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.
• SOME ASPECTS OF TUBULIN STRUCTURE AND TISSUE-SPECIFICITY
  
  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.
• PROTEOLYTIC MODIFICATION OF ACIDIC AND BASIC KERATINS DURING TERMINALDIFFERENTIATION OF MOUSE AND HUMAN-EPIDERMIS
  
  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, 142(1), 29-36. https://doi.org/10.1111/j.1432-1033.1984.tb08246.x
• IDENTIFICATION AND CHARACTERIZATION OF AXOPODIAL TUBULINS FROMECHINOSPHAERIUM-NUCLEOFILUM
  
  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.
• MOLECULAR-INTERACTIONS IN INTERMEDIATE-SIZED FILAMENTS REVEALED BYCHEMICAL CROSS-LINKING - HETEROPOLYMERS OF VIMENTIN AND GLIAL FILAMENTPROTEIN IN CULTURED HUMAN GLIOMA-CELLS
  
  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, 132(3), 477-484. https://doi.org/10.1111/j.1432-1033.1983.tb07386.x
• Heteropolymer Filaments of Vimentin and Desmin in Vascular Smooth Muscle Tissue and Cultured Baby Hamster Kidney Cells Demonstrated by Chemical Crosslinking.
  
  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