ArticleStructure (London, England : 1993)2018
Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The trial behind it
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Who cites it
32 citing papers in PubMed, 78 citations in OpenAlex.
- Structural basis of glucosinolate recognition and transport by plant GTR1.Cell discovery · 2026Article
- Conformational Landscape of the Di- and Tripeptide Permease A Transport Cycle.Journal of chemical information and modeling · 2025Article
- Energetics of substrate transport in proton-dependent oligopeptide transporters.Communications chemistry · 2024Article
- Structural basis for antibiotic transport and inhibition in PepT2.Nature communications · 2024Article
- Article
- MFSD1 with its accessory subunit GLMP functions as a general dipeptide uniporter in lysosomes.Nature cell biology · 2024Article
- Structural basis for antibiotic transport and inhibition in PepT2, the mammalian proton-coupled peptide transporter.Research square · 2024Article
- Orphan lysosomal solute carrier MFSD1 facilitates highly selective dipeptide transport.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular Insights to the Structure-Interaction Relationships of Human Proton-Coupled Oligopeptide Transporters (PepTs).Pharmaceutics · 2023Review
- Cryo-EM structure of antibacterial efflux transporter QacA from Staphylococcus aureus reveals a novel extracellular loop with allosteric role.The EMBO journal · 2023Article
- Discovery of a glutathione utilization pathway in Francisella that shows functional divergence between environmental and pathogenic species.Cell host & microbe · 2023Article
- Transporter-Mediated Drug Delivery.Molecules (Basel, Switzerland) · 2023Review
- Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport.Structure (London, England : 1993) · 2022Article
- Peptide transporter structure reveals binding and action mechanism of a potent PEPT1 and PEPT2 inhibitor.Communications chemistry · 2022Article
- Cryo-EM Structure of an Atypical Proton-Coupled Peptide Transporter: Di- and Tripeptide Permease C.Frontiers in molecular biosciences · 2022Article
- Systemic tryptophan homeostasis.Frontiers in molecular biosciences · 2022Review
- Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes.Science advances · 2021Article
- The making of a potent L-lactate transport inhibitor.Communications chemistry · 2021Article
- Engineering and functional characterization of a proton-driven β-lactam antibiotic translocation module for bionanotechnological applications.Scientific reports · 2021Article
- Cryo-EM structure of PepT2 reveals structural basis for proton-coupled peptide and prodrug transport in mammals.Science advances · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proton-dependent oligopeptide transporters (POTs) are important for uptake of dietary di- and tripeptides in many organisms, and in humans are also involved in drug absorption. These transporters accept a wide range of substrates, but the structural basis for how different peptide side chains are accommodated has so far remained obscure. Twenty-eight peptides were screened for binding to PepT
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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.