Nicole Lucien

TL;DR: The study of this disease-causing mutation in KLF1 provides further insights into the roles of this transcription factor during erythropoiesis in humans.

TL;DR: expression studies in Xenopusoocytes demonstrated that the truncated proteins encoded by the spliced transcripts did not mediate a facilitated urea transport compared with the wild type Kidd/urea transporter protein and were not expressed on the oocyte's plasma membrane.

TL;DR: Transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.

TL;DR: Findings show that, at physiological expression levels, the HUT11A transporter confers urea permeability but not water permeability, and that the observedWater permeability is a feature of the red cell urea transporter when expressed at unphysiological high levels.

TL;DR: This article showed that the Jk(S291P) mutant was translated into a glycosylated component as efficiently as the wild-type Jk polypeptide (wt Jk) in the presence of microsomes, thus indicating that the S291P mutation has no effect on the N-glycosylation pattern of the JK protein.