ReviewFrontiers in pharmacology2024
The enigmatic SLC26A6 multifunctional anion transporter: recent advances in structure-function relationship, pathophysiological significance and novel pharmacological inhibitors.
Review in Frontiers in pharmacology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- The ZBTB16/CUL3/ROC1 ubiquitin ligase drives the degradation of pathogenic pendrin (SLC26A4) protein variants.Journal of biomedical science · 2026Article
- Epithelial plasma membrane transporters as drug targets.Physiological reviews · 2026Review
- Lipid transporters E-Syt3 and ORP5 regulate epithelial ion transport by controlling phosphatidylserine enrichment at ER/PM junctions.The EMBO journal · 2025Article
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Authors and funding
1 author.
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Abstract
SLC26A6, a member of the SLC26 family of multifunctional anion transporters, has been particularly enigmatic because of its multiple modes of transport, its expression in organs that are difficult to study physiologically, and the lack of specific antibodies and inhibitors. This has recently changed. SLC26A6 is expressed in the human pancreas, kidney, intestine, heart and some other organs and is involved in fluid absorption, anion secretion, regulation of intracellular pH and elimination of waste products such as oxalate. This review will focus on three topics: Firstly, a molecular structure of human SLC26A6 has recently been obtained by cryo-electron microscopy. Structure-function studies of the reconstituted SLC26A6 in proteoliposomes suggested a 1:1 stoichiometry, resulting in electroneutral Cl
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