Evidence map›Paper›PMID 19332488›Full record

ReviewThe Journal of physiology2009

Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation.

Tzyh-Chang Hwang, David N Sheppard

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

95 citing papers in PubMed, 164 citations in OpenAlex.

  1. CFTR IVS8 Poly-T Variation Affects Severity of Acute Pancreatitis in Women.Journal of gastrointestinal surgery : official journal of the Society for Surgery of the Alimentary Tract · 2019
    Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Exon-skipping antisense oligonucleotides for cystic fibrosis therapy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Precision Medicine Based on CFTR Genotype for People with Cystic Fibrosis.Pharmacogenomics and personalized medicine · 2022
    Review
  9. Article
  10. Review
  11. Clinical and molecular characterization of the R751L-CFTR mutation.American journal of physiology. Lung cellular and molecular physiology · 2021
    Article
  12. Review
  13. 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
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

35 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

2 authors at 2 institutions in 2 countries.

Tzyh-Chang HwangDepartment of Medical Pharmacology and Physiology, and Dalton Cardiovascular Research Center, University of Missouri-Columbia, Columbia, MO 65211, USA. hwangt@health.missouri.edu
David N Sheppard
University of Bristol · GBUniversity of Missouri Health System · US

Funding

MOLECULAR PATHOPHYSIOLOGY OF CYSTIC FIBROSISR01DK055835 · NIDDK · UNIVERSITY OF MISSOURI-COLUMBIA · PI HWANG, TZYH-CHANG · 1999 to 2022
$6.1M
GATING OF CFTR CL CHANNELS BY ATP HYDROLYSISR01HL053445 · NHLBI · UNIVERSITY OF MISSOURI-COLUMBIA · PI HWANG, TZYH-CHANG · 2001 to 2009
$2.3M
Biotechnology and Biological Sciences Research Council BB/C517517/1NHLBI NIH HHS R01 HL053445NHLBI NIH HHS R01HL53445NIDDK NIH HHS R01 DK055835NIDDK NIH HHS R01DK55835
6 · The paper itself

Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) plays a fundamental role in fluid and electrolyte transport across epithelial tissues. Based on its structure, function and regulation, CFTR is an ATP-binding cassette (ABC) transporter. These transporters are assembled from two membrane-spanning domains (MSDs) and two nucleotide-binding domains (NBDs). In the vast majority of ABC transporters, the NBDs form a common engine that utilises the energy of ATP hydrolysis to pump a wide spectrum of substrates through diverse transmembrane pathways formed by the MSDs. By contrast, in CFTR the MSDs form a pathway for passive anion flow that is gated by cycles of ATP binding and hydrolysis by the NBDs. Here, we consider how the interaction of ATP with two ATP-binding sites, formed by the NBDs, powers conformational changes in CFTR structure to gate the channel pore. We explore how conserved sequences from both NBDs form ATP-binding sites at the interface of an NBD dimer and highlight the distinct roles that each binding site plays during the gating cycle. Knowledge of how ATP gates the CFTR Cl- channel is critical for understanding CFTR's physiological role, its malfunction in disease and the mechanism of action of small molecules that modulate CFTR channel gating.

Indexed as

Adenosine TriphosphateAnimalsBinding SitesCystic Fibrosis Transmembrane Conductance RegulatorHumansIon Channel GatingModels, MolecularProtein Interaction Domains and MotifsProtein MultimerizationAdenosine TriphosphateCystic Fibrosis Transmembrane Conductance Regulator

Identifiers

PMID19332488
PMCPMC2697289
OpenAlexW1524370537

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.