Evidence map›Paper›PMID 24489780›Full record

ArticlePloS one2014

Activation and inhibition of TMEM16A calcium-activated chloride channels.

Yu-Li Ni, Ai-Seon Kuan, Tsung-Yu Chen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Distinct modulation of calcium-activated chloride channel TMEM16A by drug-binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Polymodal Control of TMEM16x Channels and Scramblases.International journal of molecular sciences · 2022
    Review
  9. Review
  10. Divalent Cation Modulation of Ion Permeation in TMEM16 Proteins.International journal of molecular sciences · 2021
    Article
  11. Article
  12. Article
  13. Structure-Function of TMEM16 Ion Channels and Lipid Scramblases.Advances in experimental medicine and biology · 2021
    Article
  14. Review
  15. An Additional CaCell reports · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Molecular basis of PIPNature communications · 2019
    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 1 institution in 1 country.

Yu-Li NiDepartment of Neurology, Center for Neuroscience, University of California Davis, Davis, California, United States of America.
Ai-Seon KuanDepartment of Neurology, Center for Neuroscience, University of California Davis, Davis, California, United States of America.
Tsung-Yu ChenDepartment of Neurology, Center for Neuroscience, University of California Davis, Davis, California, United States of America.
University of California, Davis · US

Funding

Molecular Physiology of CLC Chloride ChannelsR01GM065447 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CHEN, TSUNG-YU · 2003 to 2018
$3.9M
NIGMS NIH HHS R01 GM065447NIGMS NIH HHS R01GM065447
6 · The paper itself

Abstract

Calcium-activated chloride channels (CaCC) encoded by family members of transmembrane proteins of unknown function 16 (TMEM16) have recently been intensely studied for functional properties as well as their physiological roles as chloride channels in various tissues. One technical hurdle in studying these channels is the well-known channel rundown that frequently impairs the precision of electrophysiological measurements for the channels. Using experimental protocols that employ fast-solution exchange, we circumvented the problem of channel rundown by normalizing the Ca(2+)-induced current to the maximally-activated current obtained within a time period in which the channel rundown was negligible. We characterized the activation of the TMEM16A-encoded CaCC (also called ANO1) by Ca(2+), Sr(2+), and Ba(2+), and discovered that Mg(2+) competes with Ca(2+) in binding to the divalent-cation binding site without activating the channel. We also studied the permeability of the ANO1 pore for various anions and found that the anion occupancy in the pore-as revealed by the permeability ratios of these anions-appeared to be inversely correlated with the apparent affinity of the ANO1 inhibition by niflumic acid (NFA). On the other hand, the NFA inhibition was neither affected by the degree of the channel activation nor influenced by the types of divalent cations used for the channel activation. These results suggest that the NFA inhibition of ANO1 is likely mediated by altering the pore function but not through changing the channel gating. Our study provides a precise characterization of ANO1 and documents factors that can affect divalent cation activation and NFA inhibition of ANO1.

Indexed as

AnimalsAnoctamin-1BariumBinding, CompetitiveCalciumCations, DivalentChloride ChannelsChloridesGene ExpressionHEK293 CellsHumansIon Channel GatingIon TransportMagnesiumMembrane PotentialsMiceANO1 protein, mouseAnoctamin-1BariumCalciumCations, DivalentChloride ChannelsChloridesMagnesiumNiflumic AcidRecombinant Fusion Proteins

Identifiers

PMID24489780
PMCPMC3906059
OpenAlexW2014374660

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.