Evidence map›Paper›PMID 29694855›Full record

ArticleBiophysical journal2018

Structure of Transmembrane Helix 8 and Possible Membrane Defects in CFTR.

Valentina Corradi, Ruo-Xu Gu, Paola Vergani, D Peter Tieleman

Open access · bronzeAbstract readLetter
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.3field-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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Structural basis for CFTR inhibition by CFTRProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Molecular dynamics study of ClCellular and molecular life sciences : CMLS · 2023
    Article
  5. Review
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Discovering the chloride pathway in the CFTR channel.Cellular and molecular life sciences : CMLS · 2020
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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

4 authors at 2 institutions in 2 countries.

Valentina CorradiCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
Ruo-Xu GuCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
Paola VerganiResearch Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom.
D Peter TielemanCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada. Electronic address: tieleman@ucalgary.ca.
University of Calgary · CAUniversity College London · GB

Funding

CIHR MFE-140949Medical Research Council G0501200
6 · The paper itself

Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) is an ion channel that regulates the flow of anions across epithelia. Mutations in CFTR cause cystic fibrosis. CFTR belongs to the ATP-binding cassette transporter superfamily, and gating is controlled by phosphorylation and ATP binding and hydrolysis. Recently obtained ATP-free and ATP-bound structures of zebrafish CFTR revealed an unwound segment of transmembrane helix (TM) 8, which appears to be a unique feature of CFTR not present in other ATP-binding cassette transporter structures. Here, using μs-long molecular dynamics simulations, we investigate the interactions formed by this TM8 segment with nearby helices in both ATP-free and ATP-bound states. We highlight ATP-dependent interactions as well as the structural role of TM8 in maintaining the functional architecture of the pore via interactions common to both the ATP-bound and ATP-free state. The results of the molecular dynamics simulations are discussed in the context of the gating mechanism of CFTR.

Indexed as

Adenosine TriphosphateCell MembraneCystic Fibrosis Transmembrane Conductance RegulatorModels, MolecularProtein Conformation, alpha-HelicalAdenosine TriphosphateCystic Fibrosis Transmembrane Conductance Regulator

Identifiers

PMID29694855
PMCPMC5936993
OpenAlexW2768809900

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.