Evidence map›Paper›PMID 32102849›Full record

ArticleThe Journal of biological chemistry2020

Protein kinase A phosphorylation potentiates cystic fibrosis transmembrane conductance regulator gating by relieving autoinhibition on the stimulatory C terminus of the regulatory domain.

Jeng-Haur Chen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Review
  5. Review
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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 3 countries.

Jeng-Haur ChenCollege of Chemistry and Life Sciences, Zhejiang Normal University, Jinhua, Zhejiang Province 321004, China jeng-haur-chen@zjnu.edu.cn.ORCID 0000-0001-6756-6939
University of Iowa · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel activated by protein kinase A (PKA) phosphorylation on the regulatory (R) domain. Phosphorylation at several R domain residues stimulates ATP-dependent channel openings and closings, termed channel gating. To explore the protein segment responsible for channel potentiation and PKA-dependent activation, deletion mutations were constructed by removing one to three protein segments of the R domain including residues 708-759 (ΔR

Indexed as

Adenosine TriphosphateCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorDeoxyadenosinesDiphosphatesHumansMembrane PotentialsMutagenesis, Site-DirectedPhosphorylationProtein Domains2'-deoxyribose-N6-cyclopentyladenosineAdenosine TriphosphateCFTR protein, humanCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorDeoxyadenosinesDiphosphatesdiphosphoric acidchannel activationchloride channelcystic fibrosiscystic fibrosis transmembrane conductance regulator (CFTR)phosphorylation

Identifiers

PMID32102849
PMCPMC7135986
OpenAlexW3006850052

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.