Sodium/iodide cotransporter

[1]. Sylvaine Huc-Brandt, et al. Characterisation of the purified human sodium/iodide symporter reveals that the protein is mainly present in a dimeric form and permits the detailed study of a native C-terminal fragment. Biochim Biophys Acta. 2011 Jan;1808(1):65-77. [Content Brief]

[2]. Rebecca J Thompson, et al. Dimerization of the Sodium/Iodide Symporter. Thyroid. 2019 Oct;29(10):1485-1498. [Content Brief]

[3]. J Van Sande, et al. Anion selectivity by the sodium iodide symporter. Endocrinology. 2003 Jan;144(1):247-52. [Content Brief]

[4]. P A Smanik, et al. Cloning of the human sodium lodide symporter. Biochem Biophys Res Commun. 1996 Sep 13;226(2):339-45. [Content Brief]

[5]. Shih-Lu Wu, et al. Histidine residue at position 226 is critical for iodide uptake activity of human sodium/iodide symporter. J Endocrinol. 2008 Nov;199(2):213-9. [Content Brief]

[6]. Susanna C Concilio, et al. Inter-species variation in monovalent anion substrate selectivity and inhibitor sensitivity in the sodium iodide symporter (NIS). PLoS One. 2020 Feb 21;15(2):e0229085. [Content Brief]

[7]. T Saito, et al. Increased expression of the Na+/I- symporter in cultured human thyroid cells exposed to thyrotropin and in Graves' thyroid tissue. J Clin Endocrinol Metab. 1997 Oct;82(10):3331-6. [Content Brief]

[8]. Manal Dayem, et al. Comparison of expressed human and mouse sodium/iodide symporters reveals differences in transport properties and subcellular localization. J Endocrinol. 2008 Apr;197(1):95-109. [Content Brief]