ArticleNature communications2023
Structure of human drug transporters OATP1B1 and OATP1B3.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 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.
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Who cites it
56 citing papers in PubMed, 81 citations in OpenAlex.
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- Cyanopeptide Mixtures Induce Variable Synergistic and Antagonistic Effects Across Diverse Human Cell Lines.Environmental toxicology · 2026Article
- Combinatorial Treatment with Chlorogenic Acid and Cinnamaldehyde Disrupts Intracellular pH and Metabolic Transport in Breast Cancer Cells.Molecules (Basel, Switzerland) · 2026Article
- Quantification of Binding of Small Molecules to Native Kinases by Flow Cytometry Reveals Divergence from Biochemical Affinities.Journal of the American Chemical Society · 2026Article
- Regulation of organic anion transporting polypeptide 1B1 transport function by lysine deacetylase 6.Molecular pharmacology · 2026Article
- Loss of palmitoylation impacts the interaction between the organic anion transporting polypeptide (OATP) 1B1 and OATP1B3.Drug metabolism and disposition: the biological fate of chemicals · 2026Article
- Evaluating the Utility and Constraints of the Competitive Counter Flow (CCF) Assay in OATP1B1 Substrate Profiling.The AAPS journal · 2026Article
- Structural basis for prostaglandin and drug transport via SLCO2A1.Nature communications · 2026Article
- Discovery of compound candidates for the treatment of allergic diseases: integration of DFT analyses, molecular docking, molecular dynamics simulations, and ADMET profiling.BMC pharmacology & toxicology · 2026Article
- Impact of Efavirenz on Heme Protein Induction and Biomarkers: Insights From In Vitro Experiments and a Clinical Study.Clinical and translational science · 2026Article
- A conserved salt bridge network stabilizes the hepatic organic anion transporters OATP1B1 and OATP1B3.The Journal of biological chemistry · 2026Article
- Post-translational regulation of organic anion transporting polypeptide 1B3 transport function by lysine acetylation and lysine deacetylase 6 inhibition.Drug metabolism and disposition: the biological fate of chemicals · 2026Article
- Gd-EOB-DTPA-Enhanced Magnetic Resonance Imaging for Predicting Immunotherapy Response in Hepatocellular Carcinoma: A Systematic Review and Meta-Analysis.Liver cancer · 2026Review
- Review
- VARIDT 4.0: distribution variability of drug transporters.Nucleic acids research · 2026Article
- Resistance of first-line targeted drugs in hepatocellular carcinoma: the epigenetic regulation mechanisms.Cell death & disease · 2025Review
- Association Study of OATP1B3 Polymorphisms on Hepatic Uptake and Drug-Drug InteractionACS omega · 2025Article
- Determination of bioactive and anti-inflammatory molecules of Thymbra spicata L. from Mardin by GC-MS and LC-Orbitrap HRMS: a DFT, molecular docking, ADMET, biological target and activity study.BMC complementary medicine and therapies · 2025Article
- Article
- Chemical evaluation of arbequina extra virgin olive oil with in silico analysis of its key phenolic compounds targeting LDL metabolism.Scientific reports · 2025Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
Abstract
The organic anion transporting polypeptides OATP1B1 and OATP1B3 are membrane proteins that mediate uptake of drugs into the liver for subsequent conjugation and biliary excretion, a key step in drug elimination from the human body. Polymorphic variants of these transporters can cause reduced drug clearance and adverse drug effects such as statin-induced rhabdomyolysis, and co-administration of OATP substrates can lead to damaging drug-drug interaction. Despite their clinical relevance in drug disposition and pharmacokinetics, the structure and mechanism of OATPs are unknown. Here we present cryo-EM structures of human OATP1B1 and OATP1B3 bound to synthetic Fab fragments and in functionally distinct states. A single estrone-3-sulfate molecule is bound in a pocket located in the C-terminal half of OATP1B1. The shape and chemical nature of the pocket rationalize the preference for diverse organic anions and allow in silico docking of statins. The structure of OATP1B3 is determined in a drug-free state but reveals a bicarbonate molecule bound to the conserved signature motif and a histidine residue that is prevalent in OATPs exhibiting pH-dependent activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.