ArticleBritish journal of pharmacology2006
Multiple drugbinding sites on the R482G isoform of the ABCG2 transporter.
Article in British journal of pharmacology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 107 citations in OpenAlex.
- ABCB1 and ABCG2 Regulation at the Blood-Brain Barrier: Potential New Targets to Improve Brain Drug Delivery.Pharmacological reviews · 2023Review
- Article
- Analysis of Sequence Divergence in Mammalian ABCGs Predicts a Structural Network of Residues That Underlies Functional Divergence.International journal of molecular sciences · 2021Article
- The transport pathway in the ABCG2 protein and its regulation revealed by molecular dynamics simulations.Cellular and molecular life sciences : CMLS · 2021Article
- Overexpression of ABCG2 Confers Resistance to MLN7243, a Ubiquitin-Activating Enzyme (UAE) Inhibitor.Frontiers in cell and developmental biology · 2021Article
- Review
- Application of fluorescence correlation spectroscopy to study substrate binding in styrene maleic acid lipid copolymer encapsulated ABCG2.Biochimica et biophysica acta. Biomembranes · 2020Article
- ABCG2 transports anticancer drugs via a closed-to-open switch.Nature communications · 2020Article
- ABCG2 requires a single aromatic amino acid to "clamp" substrates and inhibitors into the binding pocket.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- 3D structure of the transporter ABCG2-What's new?British journal of pharmacology · 2020Review
- Residues contributing to drug transport by ABCG2 are localised to multiple drug-binding pockets.The Biochemical journal · 2018Article
- Structure-function relationships in ABCG2: insights from molecular dynamics simulations and molecular docking studies.Scientific reports · 2017Article
- PharmGKB summary: very important pharmacogene information for ABCG2.Pharmacogenetics and genomics · 2017Review
- The structure of the human ABC transporter ABCG2 reveals a novel mechanism for drug extrusion.Scientific reports · 2017Article
- Dual Modulation of Human P-Glycoprotein and ABCG2 with Prodrug Dimers of the Atypical Antipsychotic Agent Paliperidone in a Model of the Blood-Brain Barrier.Molecular pharmaceutics · 2017Article
- The multidrug transporter ABCG2: still more questions than answers.Biochemical Society transactions · 2016Review
- Providing a molecular mechanism for P-glycoprotein; why would I bother?Biochemical Society transactions · 2015Review
- Identification of residues in ABCG2 affecting protein trafficking and drug transport, using co-evolutionary analysis of ABCG sequences.Bioscience reports · 2015Article
- Role of the breast cancer resistance protein (BCRP/ABCG2) in drug transport--an update.The AAPS journal · 2015Review
- Human ABC transporter ABCG2/BCRP expression in chemoresistance: basic and clinical perspectives for molecular cancer therapeutics.Pharmacogenomics and personalized medicine · 2014Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
BACKGROUND & PURPOSE: Drug-resistant cancer cells frequently display efflux pumps such as P-glycoprotein (P-gp), the multidrug resistance associated protein (MRP1) or the transporter ABCG2. These transporters are each capable of mediating the active efflux of numerous anticancer drugs and display relatively distinct substrate preferences. The last, most recently discovered member, ABCG2, plays a major role in resistance in several types of cancer and the precise pharmacology of this multidrug transporter remain unresolved as does the nature of substrate binding. EXPERIMENTAL APPROACH: Plasma membranes from insect cells expressing ABCG2 were used to characterise binding of [3H]daunomycin to the multidrug transporter. The kinetics of association and dissociation for this substrate and several other compounds were also determined in this experimental system. KEY
resultsThe dissociation constant for [3H]daunomycin binding was 564 +/- 57 nM and a Hill slope of 1.4 suggested cooperative binding. Doxorubicin, prazosin and daunomycin completely displaced the binding of radioligand, while mitoxantrone and Hoechst 33342 produced only a partial displacement. Analysis of the dissociation rates revealed that [3H]daunomycin and doxorubicin bind to multiple sites on the transporter.
conclusionsBoth kinetic and equilibrium data support the presence of at least two symmetric drug binding sites on ABCG2, which is distinct from the asymmetry observed for P-gp. The data provide the first molecular details underlying the mechanism by which this transporter is capable of interacting with multiple substrates.
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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.