Evidence map›Paper›PMID 27449280›Full record

ArticleeLife2016

Mechanistic signs of double-barreled structure in a fluoride ion channel.

Nicholas B Last, Ludmila Kolmakova-Partensky, Tania Shane, Christopher Miller

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Biocatalytic synthesis of 2-fluoro-3-hydroxypropionic acid.Frontiers in bioengineering and biotechnology · 2022
    Article
  9. An outer-pore gate modulates the pharmacology of the TMEM16A channel.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Membrane Exporters of Fluoride Ion.Annual review of biochemistry · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. A CLC-type FNature structural & molecular biology · 2018
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Nicholas B LastDepartment of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, United States.
Ludmila Kolmakova-PartenskyDepartment of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, United States.
Tania ShaneDepartment of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, United States.
Christopher MillerDepartment of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, United States.ORCID 0000-0002-0273-8653

Funding

Mechanisms of Biological Fluoride Resistance ExportersR01GM107023 · NIGMS · BRANDEIS UNIVERSITY · PI MILLER, CHRISTOPHER · 2014 to 2017
$1.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM107023
6 · The paper itself

Abstract

The Fluc family of F(-) ion channels protects prokaryotes and lower eukaryotes from the toxicity of environmental F(-). In bacteria, these channels are built as dual-topology dimers whereby the two subunits assemble in antiparallel transmembrane orientation. Recent crystal structures suggested that Fluc channels contain two separate ion-conduction pathways, each with two F(-) binding sites, but no functional correlates of this unusual architecture have been reported. Experiments here fill this gap by examining the consequences of mutating two conserved F(-)-coordinating phenylalanine residues. Substitution of each phenylalanine specifically extinguishes its associated F(-) binding site in crystal structures and concomitantly inhibits F(-) permeation. Functional analysis of concatemeric channels, which permit mutagenic manipulation of individual pores, show that each pore can be separately inactivated without blocking F(-) conduction through its symmetry-related twin. The results strongly support dual-pathway architecture of Fluc channels.

Indexed as

Amino Acid SubstitutionBinding SitesCrystallography, X-RayDNA Mutational AnalysisEscherichia coliFluoridesIon ChannelsModels, BiologicalModels, MolecularMutant ProteinsPermeabilityPhenylalanineProtein ConformationFluoridesIon ChannelsMutant ProteinsPhenylalaninebiophysicsE. colifluoride ion channelmembrane protein architecturepermeationstructural biology

Identifiers

PMID27449280
PMCPMC4969038

What OpenQuestion holds

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Registered trials

None linked

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.