ArticleFrontiers in molecular biosciences2022
Cryo-EM Structure of an Atypical Proton-Coupled Peptide Transporter: Di- and Tripeptide Permease C.
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- In silico directed evolution of humanized peptide transporters via computational epistatic rescue.Molecular diversity · 2026Article
- Structural basis of glucosinolate recognition and transport by plant GTR1.Cell discovery · 2026Article
- Structural basis for antibiotic transport and inhibition in PepT2.Nature communications · 2024Article
- Structural basis for antibiotic transport and inhibition in PepT2, the mammalian proton-coupled peptide transporter.Research square · 2024Article
- Molecular basis of TASL recruitment by the peptide/histidine transporter 1, PHT1.Nature communications · 2023Article
- Functional Characterization of the Putative POT fromBiology · 2023Article
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Authors and funding
7 authors.
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Abstract
Proton-coupled Oligopeptide Transporters (POTs) of the Major Facilitator Superfamily (MFS) mediate the uptake of short di- and tripeptides in all phyla of life. POTs are thought to constitute the most promiscuous class of MFS transporters, with the potential to transport more than 8400 unique substrates. Over the past two decades, transport assays and biophysical studies have shown that various orthologues and paralogues display differences in substrate selectivity. The
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