ReviewCurrent opinion in structural biology2013
Ion selectivity and gating mechanisms of FNT channels.
Review in Current opinion in structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
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Who cites it
14 citing papers in PubMed.
- A two-membrane gateway for monocarboxylates couples host glycolysis tobioRxiv : the preprint server for biology · 2026Article
- Structure of Chlamydomonas reinhardtii LciA guided the engineering of FNT family proteins to gain bicarbonate transport activity.Nature plants · 2026Article
- Comparison of ion selectivities of nitrite channel NirC and water channel aquaporin.World journal of microbiology & biotechnology · 2023Article
- Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel.MicrobiologyOpen · 2022Article
- A single amino acid exchange converts FocA into a unidirectional efflux channel for formate.Microbiology (Reading, England) · 2022Article
- Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Is the E. coli Homolog of the Formate/Nitrite Transporter Family an Anion Channel? A Computational Study.Biophysical journal · 2020Article
- Energetics and mechanism of anion permeation across formate-nitrite transporters.Scientific reports · 2017Article
- Mechanism of formate-nitrite transporters by dielectric shift of substrate acidity.The EMBO journal · 2017Article
- The C-terminal Six Amino Acids of the FNT Channel FocA Are Required for Formate Translocation But Not Homopentamer Integrity.Frontiers in microbiology · 2017Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- The glycyl-radical enzyme 2-ketobutyrate formate-lyase, TdcE, interacts specifically with the formate-translocating FNT-channel protein FocA.Biochemistry and biophysics reports · 2016Article
- Pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation.Journal of molecular biology · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The phospholipid bilayer has evolved to be a protective and selective barrier by which the cell maintains high concentrations of life sustaining organic and inorganic material. As gatekeepers responsible for an immense amount of bidirectional chemical traffic between the cytoplasm and extracellular milieu, ion channels have been studied in detail since their postulated existence nearly three-quarters of a century ago. Over the past fifteen years, we have begun to understand how selective permeability can be achieved for both cationic and anionic ions. Our mechanistic knowledge has expanded recently with studies of a large family of anion channels, the Formate Nitrite Transport (FNT) family. This family has proven amenable to structural studies at a resolution high enough to reveal intimate details of ion selectivity and gating. With five representative members having yielded a total of 15 crystal structures, this family represents one of the richest sources of structural information for anion channels.
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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.