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
(2008)
Journal Article
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
All Outputs (134)
Expression and localisation of apical junctional complex proteins in lens epithelial cells (2008)
Journal Article
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 (2008)
Journal Article
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.m706453200Here we investigate the effects of a myopathy-causing mutation in αB-crystallin, Q151X, upon its structure and function. This mutation removes the C-terminal domain of αB-crystallin, which is expected to compromise both its oligomerization and chaper... Read More about Truncation of αB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells.
Lens cells: More than meets the eye (2007)
Journal Article
Tholozan, F., & Quinlan, R. (2007). Lens cells: More than meets the eye. International Journal of Biochemistry and Cell Biology, 39(10), 1754-1759Lens cells originate from the head ectoderm and differentiate into an avascular organ constituted from two contiguous cell subpopulations of very different morphology. Lens cells, together with corneal cells, are responsible for the transmission and... Read More about Lens cells: More than meets the eye.
Insights into the beaded filament of the eye lens (2007)
Journal Article
Perng, M., Zhang, Q., & Quinlan, R. (2007). Insights into the beaded filament of the eye lens. Experimental Cell Research, 313(10), 2180-8Filensin (BFSP1) and CP49 (BFSP2) represent two members of the IF protein superfamily that are thus far exclusively expressed in the eye lens. Mutations in both proteins cause lens cataract and careful consideration of the detail of these cataract ph... Read More about Insights into the beaded filament of the eye lens.
Focus on Molecules : FoxE3 (2007)
Journal Article
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
GFAP and its role in Alexander disease (2007)
Journal Article
Quinlan, R., Brenner, M., Goldman, J., & Messing, A. (2007). GFAP and its role in Alexander disease. Experimental Cell Research, 313(10), 2077-87Here we review how GFAP mutations cause Alexander disease. The current data suggest that a combination of events cause the disease. These include: (i) the accumulation of GFAP and the formation of characteristic aggregates, called Rosenthal fibers, (... Read More about GFAP and its role in Alexander disease.
Regulation of contractility by Hsp27 and Hic-5 in rat mesenteric small arteries. (2007)
Journal Article
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.00939.2007The regulation of small artery contractility by vasoconstrictors is important for vascular function, and actin cytoskeleton remodeling is required for contraction. p38 MAPK and tyrosine kinases are implicated in actin polymerization and contraction t... Read More about Regulation of contractility by Hsp27 and Hic-5 in rat mesenteric small arteries..
Reorganization of centrosomal marker proteins coincides with epithelial cell differentiation in the vertebrate lens (2007)
Journal Article
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.2007.07.022The differentiation of epithelial cells in the vertebrate lens involves a series of changes that includes the degradation of all intracellular organelles and a dramatic elongation of the cells. The latter is accompanied by a substantial remodelling o... Read More about Reorganization of centrosomal marker proteins coincides with epithelial cell differentiation in the vertebrate lens.
FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability (2007)
Journal Article
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.e06-05-0416The lens is an avascular tissue, separated from the aqueous and vitreous humors by its own extracellular matrix, the lens capsule. Here we demonstrate that the lens capsule is a source of essential survival factors for lens epithelial cells. Primary... Read More about FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability.
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 (2006)
Journal Article
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/10.1086/504411Here, we describe the early events in the disease pathogenesis of Alexander disease. This is a rare and usually fatal neurodegenerative disorder whose pathological hallmark is the abundance of protein aggregates in astrocytes. These aggregates, terme... Read More about 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.
The C terminus of lens aquaporin 0 interacts with the cytoskeletalproteins filensin and CP49 (2006)
Journal Article
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 (2006)
Journal Article
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 (2005)
Journal Article
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
Decay bounds in a model for aggregation of microglia: application toAlzheimer's disease senile plaques (2005)
Journal Article
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 (2005)
Journal Article
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 (2005)
Journal Article
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
Comparison of the small heat shock proteins alpha B-crystallin, MKBP,HSP25, HSP20, and cvHSP in heart and skeletal muscle (2004)
Journal Article
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 (2004)
Journal Article
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
Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells (2004)
Journal Article
Perng, M., Wen, S., van den Ijssel, P., Prescott, A., & Quinlan, R. (2004). Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells. Molecular Biology of the Cell, 15(5), 2335-2346. https://doi.org/10.1091/mbc.e03-12-0893The R120G mutation in alphaB-crystallin causes desmin-related myopathy. There have been a number of mechanisms proposed to explain the disease process, from altered protein processing to loss of chaperone function. Here, we show that the mutation alt... Read More about Desmin aggregate formation by R120G alpha B-crystallin is caused by altered filament interactions and is dependent upon network status in cells.