Evidence map›Paper›PMID 21296873›Full record

ReviewThe Journal of biological chemistry2011

A unified view of cystic fibrosis transmembrane conductance regulator (CFTR) gating: combining the allosterism of a ligand-gated channel with the enzymatic activity of an ATP-binding cassette (ABC) transporter.

Kevin L Kirk, Wei Wang

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. TMEM16 proteins: CaInternational journal of molecular medicine · 2024
    Review
  2. Article
  3. Article
  4. G551D mutation impairs PKA-dependent activation of CFTR channel that can be restored by novel GOF mutations.American journal of physiology. Lung cellular and molecular physiology · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. A synonymous codon change alters the drug sensitivity of ΔF508 cystic fibrosis transmembrane conductance regulator.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Concise Guide to PHARMACOLOGY 2013/14: ion channels.British journal of pharmacology · 2013
    Article
  17. The silent codon change I507-ATC->ATT contributes to the severity of the ΔF508 CFTR channel dysfunction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  18. Targeting a genetic defect: cystic fibrosis transmembrane conductance regulator modulators in cystic fibrosis.European respiratory review : an official journal of the European Respiratory Society · 2013
    Review
  19. The CFTR ion channel: gating, regulation, and anion permeation.Cold Spring Harbor perspectives in medicine · 2013
    Article
  20. CFTR mutations altering CFTR fragmentation.The Biochemical journal · 2013
    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

2 authors at 1 institution in 1 country.

Kevin L KirkDepartment of Physiology and Biophysics and the Gregory Fleming James Cystic Fibrosis Research Center, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA. klkirk@uab.edu
Wei Wang
University of Alabama at Birmingham · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique ion channel in that its gating is coupled to an intrinsic enzymatic activity (ATP hydrolysis). This enzymatic activity derives from the evolutionary origin of CFTR as an ATP-binding cassette transporter. CFTR gating is distinct from that of a typical ligand-gated channel because its ligand (ATP) is usually consumed during the gating cycle. However, recent findings indicate that CFTR gating exhibits allosteric properties that are common to conventional ligand-gated channels (e.g. unliganded openings and constitutive mutations). Here, we provide a unified view of CFTR gating that combines the allosterism of a ligand-gated channel with its unique enzymatic activity.

Indexed as

Adenosine TriphosphateAllosteric RegulationAnimalsATP-Binding Cassette TransportersCystic Fibrosis Transmembrane Conductance RegulatorHumansHydrolysisIon Channel GatingMutationAdenosine TriphosphateATP-Binding Cassette TransportersCFTR protein, humanCystic Fibrosis Transmembrane Conductance Regulator

Identifiers

PMID21296873
PMCPMC3075628
OpenAlexW2050735029

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.