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 (3)
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.