ArticleACS omega2022
Mutation in Transmembrane Domain 8 of Human Urate Transporter 1 Disrupts Uric Acid Recognition and Transport.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
The trial behind it
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Who cites it
4 citing papers in PubMed.
- A novel method for screening antihyperuricemic drugs by combining aptamer sensor array, exonuclease III-DNA walker and linear discriminant analysis.Journal of pharmaceutical analysis · 2026Article
- Uric Acid-Degrading Lacticaseibacillus paracasei CPU202306 Ameliorates Hyperuricemia by Regulating Uric Acid Metabolism and Intestinal Microecology in Mice.Probiotics and antimicrobial proteins · 2026Article
- Mechanisms of urate transport and uricosuric drugs inhibition in human URAT1.Nature communications · 2025Article
- Transport mechanism and structural pharmacology of human urate transporter URAT1.Cell research · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human urate transporter 1 (hURAT1) is the most pivotal therapeutic target for hyperuricemia. Due to a lack of crystal structure information, the atomic structure of URAT1 is not clearly understood. In this study, a multiple sequence alignment was performed, and K393, a positively charged residue in transmembrane domain (TMD) 8, was observed to be highly conserved in organic anion transporters (OATs). K393 was substituted with a positively, negatively, and neutrally charged amino acid via site-directed mutagenesis and then used to transfect HEK293 cells. Reverse transcription-quantitative polymerase chain reaction (RT-qPCR) and enzyme-linked immunosorbent assay (ELISA) analyses indicated that mutants of K393 showed mRNA and protein expression levels similar to those in the WT group. The nonpositively charged mutants K393A, K393D, and K393E eliminated 70-80% of
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Registered trials
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