Evidence map›Paper›PMID 37823914›Full record

ArticleThe Journal of membrane biology2023

Role of Hydrophobic Amino-Acid Side-Chains in the Narrow Selectivity Filter of the CFTR Chloride Channel Pore in Conductance and Selectivity.

Paul Linsdell

Erratum issuedAbstract readLegislation
PubMed Publisher
In one paragraph

Article in The Journal of membrane biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Paul LinsdellDepartment of Physiology & Biophysics, Dalhousie University, PO Box 15000, Halifax, NS, B3H 4R2, Canada. paul.linsdell@dal.ca.ORCID 0000-0001-6257-6273

Funding

Natural Sciences and Engineering Research Council of Canada RGPIN/05124-2017
6 · The paper itself

Abstract

Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel. Structural analysis of CFTR has identified a narrow, hydrophobic region close to the extracellular end of the open channel pore that may function as a selectivity filter. The present study combines comprehensive mutagenesis of hydrophobic amino-acid side-chains within the selectivity filter with functional evaluation of channel Cl

Indexed as

Chloride ChannelsCystic Fibrosis Transmembrane Conductance RegulatorAmino AcidsAnionsMutationAmino AcidsAnionsChloride ChannelsCystic Fibrosis Transmembrane Conductance RegulatorAnion selectivityChloride channelCystic fibrosis transmembrane conductance regulatorIon permeation

Identifiers

PMID37823914

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.