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The Lipidation Profile of Aquaporin-0 Correlates with The Acyl Composition of Phosphoethanolamine Lipids in Lens Membranes (2016)
Journal Article
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

The lens fiber major intrinsic protein (otherwise known as aquaporin-0 (AQP0), MIP26 and MP26) has been examined by mass spectrometry (MS) in order to determine the speciation of acyl modifications to the side chains of lysine residues and the N-term... Read More about The Lipidation Profile of Aquaporin-0 Correlates with The Acyl Composition of Phosphoethanolamine Lipids in Lens Membranes.

A Gramicidin Analogue that Exhibits Redox Potential Dependent Cation Influx (2007)
Journal Article
Jackson, T., Sanderson, J., & Kataky, R. (2008). A Gramicidin Analogue that Exhibits Redox Potential Dependent Cation Influx. Sensors and Actuators B: Chemical, 130(2), 630-637. https://doi.org/10.1016/j.snb.2007.10.019

A synthetic analogue of gramicidin A, gram-2-(nicotinamidyl)ethyl carbamate (gAN) was found to regulate the influx of potassium ions depending on its redox state. At potentials less than −0.52 (±0.05) V, the nicotinamide group in gAN is reduced and a... Read More about A Gramicidin Analogue that Exhibits Redox Potential Dependent Cation Influx.