ArticleeLife2020
Characterization of the kinetic cycle of an ABC transporter by single-molecule and cryo-EM analyses.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 93 citations in OpenAlex.
- Plant ABCC1 orthologs from agronomically relevant species reveal conserved principles of detoxification transport.Phytochemistry · 2026Article
- ATP-driven conformational dynamics reveal hidden intermediates in a heterodimeric ABC transporter.eLife · 2026Article
- Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.Nature communications · 2026Article
- Multi-State Structural Genomics Enables Large-Scale, Mechanistic, and Context-Specific Classification of ABCC6 Genetic Variants Implicated in Calcification Diseases.International journal of molecular sciences · 2026Article
- Substrate recognition diversity and transport dynamics of ABCC1.Nature communications · 2025Article
- Nucleotide-dependent conformational changes direct peptide export by the transporter associated with antigen processing.Immunity · 2025Article
- DDX27 in cancer: molecular mechanisms, clinical implications, and therapeutic potential.Journal of translational medicine · 2025Review
- ABCG2 Transporter: From Structure to Function-Current Insights and Open Questions.International journal of molecular sciences · 2025Review
- Mechanism of human α3β GlyR regulation by intracellular M3/M4 loop phosphorylation and 2,6-di-tert-butylphenol interaction.Nature communications · 2025Article
- Conformational equilibrium of an ABC transporter analyzed by luminescence resonance energy transfer.Biophysical journal · 2025Article
- Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2.Nature communications · 2025Article
- Specificity and tunability of efflux pumps: A new role for the proton gradient?PLoS computational biology · 2025Article
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- Progress in Research of Nanotherapeutics for Overcoming Multidrug Resistance in Cancer.International journal of molecular sciences · 2024Review
- Structural View of Cryo-Electron Microscopy-Determined ATP-Binding Cassette Transporters in Human Multidrug Resistance.Biomolecules · 2024Review
- Transport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain.Nature communications · 2024Article
- Deciphering the functional role of clinical mutations in ABCB1, ABCC1, and ABCG2 ABC transporters in endometrial cancer.Frontiers in pharmacology · 2024Article
- Asymmetric conformations and lipid interactions shape the ATP-coupled cycle of a heterodimeric ABC transporter.Nature communications · 2023Article
- Article
- Placing steroid hormones within the human ABCC3 transporter reveals a compatible amphiphilic substrate-binding pocket.The EMBO journal · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
ATP-binding cassette (ABC) transporters are molecular pumps ubiquitous across all kingdoms of life. While their structures have been widely reported, the kinetics governing their transport cycles remain largely unexplored. Multidrug resistance protein 1 (MRP1) is an ABC exporter that extrudes a variety of chemotherapeutic agents and native substrates. Previously, the structures of MRP1 were determined in an inward-facing (IF) or outward-facing (OF) conformation. Here, we used single-molecule fluorescence spectroscopy to track the conformational changes of bovine MRP1 (bMRP1) in real time. We also determined the structure of bMRP1 under active turnover conditions. Our results show that substrate stimulates ATP hydrolysis by accelerating the IF-to-OF transition. The rate-limiting step of the transport cycle is the dissociation of the nucleotide-binding-domain dimer, while ATP hydrolysis per se does not reset MRP1 to the resting state. The combination of structural and kinetic data illustrates how different conformations of MRP1 are temporally linked and how substrate and ATP alter protein dynamics to achieve active transport.
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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.