Evidence map›Paper›PMID 20006941›Full record

ReviewBiophysical journal2009

The TMEM16 protein family: a new class of chloride channels?

Luis J V Galietta

Open access · bronzeAbstract readReview
In one paragraph

Review in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

64 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
  2. Lipid scrambling is a general feature of protein insertases.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Lipid scrambling is a general feature of protein insertases.bioRxiv : the preprint server for biology · 2023
    Article
  4. Review
  5. Article
  6. Review
  7. Specific PIPCommunications biology · 2021
    Article
  8. Molecular mechanism of TMEM16A regulation: role of CaMKII and PP1/PP2A.American journal of physiology. Cell physiology · 2019
    Article
  9. Article
  10. Dextran sulfate sodium-induced chronic colitis attenuates CaAmerican journal of physiology. Cell physiology · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The CaNature communications · 2016
    Article
  16. Article
  17. Exposure of phosphatidylserine on the cell surface.Cell death and differentiation · 2016
    Review
  18. Article
  19. Article
  20. Review

4 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Luis J V GaliettaLaboratory of Molecular Genetics, Istituto Giannina Gaslini, Genoa, Italy. galietta@unige.it
Istituto Giannina Gaslini · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cl(-) channels play important roles in many physiological processes, including transepithelial ion absorption and secretion, smooth and skeletal muscle contraction, neuronal excitability, sensory perception, and cell volume regulation. The molecular identity of many types of Cl(-) channels is still unknown. Recently, three research groups have arrived independently at the identification of TMEM16A (also known as anoctamin-1) as a membrane protein strongly related to the activity of Ca(2+)-activated Cl(-) channels (CaCCs). Site-specific mutagenesis of TMEM16A alters the properties of the channels, thus suggesting that TMEM16A forms, at least in part, the CaCC. TMEM16A is a member of a family that includes nine other membrane proteins. All TMEM16 proteins have a similar structure, with eight putative transmembrane domains and cytosolic amino- and carboxy-termini. TMEM16B expression also evokes the appearance of CaCCs, but with biophysical characteristics (voltage dependence, unitary conductance) different from those associated to TMEM16A. The roles of the other TMEM16 proteins are still unknown. The study of TMEM16 proteins may lead to identification of novel molecular mechanisms underlying ion transport and channel gating by voltage and Ca(2+).

Indexed as

Chloride ChannelsAmino Acid SequenceAnimalsChlorineElectric ConductivityHumansMolecular Sequence DataChloride ChannelsChlorine

Identifiers

PMID20006941
PMCPMC2793353
OpenAlexW1984140289

What OpenQuestion holds

Textmetadata
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.