P. J. Eswari Pandaranayaka

TL;DR: This is the first study demonstrating that the p.Cys134Trp mutant does not have a strong impact on FOXL2 localization, solubility, and transactivation abilities on a panel of proven target promoters, behaving neither as a dominant-negative nor as a loss-of-function mutation.

TL;DR: It is found that the localization of the side chain of each amino acid strongly correlated with the impact of its mutation on FOXL2 transactivation capacity, and a similar correlation can be found for BPES mutations associated or not with ovarian dysfunction.

TL;DR: In this article, the expression of normal and mutant myocilin (Gly367Arg) in cultured trabecular meshwork (TM) cells was examined and confocal microscopic analysis was used to determine the cellular localization.

TL;DR: The over expression and purification of the human myocilin in E. coli was reported here and the protein purity and folding were confirmed using electrophoresis, immunoblotting and fluorescence spectroscopy.

TL;DR: It is suggested that polymorphisms in the myocilin genomic region that cause synonymous codon changes or those that occur in the intron regions can possibly lead to altered myocILin protein products through altered intron–exon splicing.