ArticleFrontiers in microbiology2017
The C-terminal Six Amino Acids of the FNT Channel FocA Are Required for Formate Translocation But Not Homopentamer Integrity.
Article in Frontiers in microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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
4 citing papers in PubMed, 9 citations in OpenAlex.
- Conserved hydrophilic checkpoints tune FocA-mediated formate:HNature communications · 2025Article
- Hydrogen production in the presence of oxygen byMicrobiology (Reading, England) · 2022Article
- Potential virus-mediated nitrogen cycling in oxygen-depleted oceanic waters.The ISME journal · 2021Article
- Is the E. coli Homolog of the Formate/Nitrite Transporter Family an Anion Channel? A Computational Study.Biophysical journal · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FocA is the archetype of the pentameric formate-nitrite transporter (FNT) superfamily of channels, members of which translocate small organic and inorganic anions across the cytoplasmic membrane of microorganisms. The N- and C-termini of each protomer are cytoplasmically oriented. A Y-L-R motif is found immediately after transmembrane helix 6 at the C-terminus of FNT proteins related to FocA, or those with a role in formate translocation. Previous
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