Evidence map›Paper›PMID 24036509›Full record

ArticleNature chemical biology2013

Fluoride-dependent interruption of the transport cycle of a CLC Cl-/H+ antiporter.

Hyun-Ho Lim, Randy B Stockbridge, Christopher Miller

Abstract read
In one paragraph

Article in Nature chemical biology, 2013. 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
2.2field-weighted citation impact, top 12% of its field
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, 44 citations in OpenAlex.

  1. Article
  2. CLCEnvironmental microbiology · 2026
    Article
  3. Article
  4. Review
  5. Fluoride Ion Binding and Translocation in the CLCThe journal of physical chemistry. B · 2024
    Article
  6. Fluoride Transport and Inhibition Across CLC Transporters.Handbook of experimental pharmacology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Membrane Exporters of Fluoride Ion.Annual review of biochemistry · 2021
    Review
  12. Article
  13. Article
  14. Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC ClProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. A CLC-type FNature structural & molecular biology · 2018
    Article
  17. Multiscale Kinetic Modeling Reveals an Ensemble of ClJournal of the American Chemical Society · 2018
    Article
  18. Review
  19. Article
  20. The Origin of Coupled Chloride and Proton Transport in a ClJournal of the American Chemical Society · 2016
    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

3 authors at 2 institutions in 1 country.

Hyun-Ho Lim1] Department of Biochemistry, Brandeis University, Waltham, Massachusetts, USA. [2] Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts, USA. [3].
Randy B Stockbridge
Christopher Miller
Brandeis University · USHoward Hughes Medical Institute · US

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

Cl(-)/H(+) antiporters of the CLC superfamily transport anions across biological membranes in varied physiological contexts. These proteins are weakly selective among anions commonly studied, including Cl(-), Br(-), I(-), NO3(-) and SCN(-), but they seem to be very selective against F(-). The recent discovery of a new CLC clade of F(-)/H(+) antiporters, which are highly selective for F(-) over Cl(-), led us to investigate the mechanism of Cl(-)-over-F(-) selectivity by a CLC Cl(-)/H(+) antiporter, CLC-ec1. By subjecting purified CLC-ec1 to anion transport measurements, electrophysiological recording, equilibrium ligand-binding studies and X-ray crystallography, we show that F(-) binds in the Cl(-) transport pathway with affinity similar to Cl(-) but stalls the transport cycle. Examination of various mutant antiporters implies a 'lock-down' mechanism of F(-) inhibition, in which F(-), by virtue of its unique hydrogen-bonding chemistry, greatly retards a proton-linked conformational change essential for the transport cycle of CLC-ec1.

Indexed as

AntiportersChloride ChannelsChlorineCrystallography, X-RayFluoridesHydrogenLigandsModels, MolecularAntiportersChloride ChannelsChlorineFluoridesHydrogenLigands

Identifiers

PMID24036509
PMCPMC3805709
OpenAlexW2078752919

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.