Outputs (4)

Independent Membrane Binding Properties of the Caspase Generated Fragments of the Beaded Filament Structural Protein 1 (BFSP1) Involves an Amphipathic Helix (2023)
Journal Article
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

Background: BFSP1 (beaded filament structural protein 1) is a plasma membrane, Aqua- 21 porin 0 (AQP0/MIP)-associated intermediate filament protein expressed in the eye lens. BFSP1 is 22 myristoylated, a post-translation modification that requires ca... Read More about Independent Membrane Binding Properties of the Caspase Generated Fragments of the Beaded Filament Structural Protein 1 (BFSP1) Involves an Amphipathic Helix.

Three-dimensional data capture and analysis of intact eye lenses evidences emmetropia-associated changes and strain-dependent differences in epithelial cell organization (2020)
Journal Article
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

Organ and tissue development are highly coordinated processes; lens growth and functional integration into the eye (emmetropia) is a robust example. An epithelial monolayer covers the anterior hemisphere of the lens, and its organization is the key t... Read More about Three-dimensional data capture and analysis of intact eye lenses evidences emmetropia-associated changes and strain-dependent differences in epithelial cell organization.

BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability (2019)
Journal Article
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

BFSP1 (beaded filament structural protein 1, filensin) is a cytoskeletal protein expressed in the eye lens. It binds AQP0 in vitro and its C-terminal sequences have been suggested to regulate the water channel activity of AQP0. A myristoylated fragme... Read More about BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability.

Cataractogenic load – a concept to study the contribution of ionizing radiation to accelerated aging in the eye lens (2019)
Journal Article
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

Ionizing radiation (IR) damages DNA and other macromolecules, including proteins and lipids. Most cell types can repair DNA damage and cycle continuously their macromolecules as a mechanism to remove defective proteins and lipids. In those cells that... Read More about Cataractogenic load – a concept to study the contribution of ionizing radiation to accelerated aging in the eye lens.