ReviewFEBS letters2020
The role of the degenerate nucleotide binding site in type I ABC exporters.
Review in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 60 citations in OpenAlex.
- ABCG2 transporter: Structural and functional associations with gout (Review).International journal of molecular medicine · 2026Review
- Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.Journal of chemical theory and computation · 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
- A RareJournal of clinical medicine · 2025Article
- A fluorescent probe for the enzymatic activity of KbioRxiv : the preprint server for biology · 2025Article
- Genome-wide identification analysis of the ATP-binding cassette transporter family and expression analysis under methyl jasmonate treatment in Panax ginseng.BMC plant biology · 2025Article
- Structure and mechanism of a mycobacterial isoniazid efflux pump MsRv1273c/72c with a degenerate nucleotide-binding site.Nature communications · 2025Article
- Membrane-dependent dynamics and dual translocation mechanisms of ABCB4: Insights from molecular dynamics simulations.Computational and structural biotechnology journal · 2025Article
- A novel ABCC9 variant in a Greek family with Cantu syndrome affecting multiple generations highlights the functional role of the SUR2B NBD1.American journal of medical genetics. Part A · 2024Article
- Substrate-Induced Structural Dynamics and Evolutionary Linkage of Siderophore-Iron ABC Transporters ofMedicina (Kaunas, Lithuania) · 2024Article
- An in vitro set-up to study Pdr5-mediated substrate translocation.Protein science : a publication of the Protein Society · 2024Article
- Structural basis of prostaglandin efflux by MRP4.Nature structural & molecular biology · 2024Article
- Genome wide structural prediction of ABC transporter systems inFrontiers in microbiology · 2024Article
- Article
- Asymmetric conformations and lipid interactions shape the ATP-coupled cycle of a heterodimeric ABC transporter.Nature communications · 2023Article
- Dissecting the conformational complexity and mechanism of a bacterial heme transporter.Nature chemical biology · 2023Article
- How Cryo-EM Has Expanded Our Understanding of Membrane Transporters.Drug metabolism and disposition: the biological fate of chemicals · 2023Review
- Synergistic Inhibitory Effect of Quercetin and Cyanidin-3O-Sophoroside on ABCB1.International journal of molecular sciences · 2023Article
- The Alternating Access Mechanism in Mammalian Multidrug Resistance Transporters and Their Bacterial Homologs.Membranes · 2023Article
- Deep mutational scan of a drug efflux pump reveals its structure-function landscape.Nature chemical biology · 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
3 authors at 2 institutions in 2 countries.
Funding
Abstract
ATP-binding cassette (ABC) transporters are fascinating molecular machines that are capable of transporting a large variety of chemically diverse compounds. The energy required for translocation is derived from binding and hydrolysis of ATP. All ABC transporters share a basic architecture and are composed of two transmembrane domains and two nucleotide binding domains (NBDs). The latter harbor all conserved sequence motifs that hallmark the ABC transporter superfamily. The NBDs form the nucleotide binding sites (NBSs) in their interface. Transporters with two active NBSs are called canonical transporters, while ABC exporters from eukaryotic organisms, including humans, frequently have a degenerate NBS1 containing noncanonical residues that strongly impair ATP hydrolysis. Here, we summarize current knowledge on degenerate ABC transporters. By integrating structural information with biophysical and biochemical evidence of asymmetric function, we develop a model for the transport cycle of degenerate ABC transporters. We will elaborate on the unclear functional advantages of a degenerate NBS.
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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.