Evidence map›Paper›PMID 24646234›Full record

ReviewBiochemical Society transactions2014

The cAMP-binding Popdc proteins have a redundant function in the heart.

Thomas Brand, Subreena L Simrick, Kar Lai Poon, Roland F R Schindler

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. TheBiology · 2025
    Article
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  13. The genetic basis for inherited forms of sinoatrial dysfunction and atrioventricular node dysfunction.Journal of interventional cardiac electrophysiology : an international journal of arrhythmias and pacing · 2015
    Review
  14. Review
  15. The Popeye Domain Containing Genes and cAMP Signaling.Journal of cardiovascular development and disease · 2014
    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 1 institution in 2 countries.

Thomas Brand*Heart Science Centre, National Heart and Lung Institute, Imperial College, Hill End Road, Harefield UB9 6JH, U.K.
Subreena L Simrick*Heart Science Centre, National Heart and Lung Institute, Imperial College, Hill End Road, Harefield UB9 6JH, U.K.
Kar Lai Poon*Heart Science Centre, National Heart and Lung Institute, Imperial College, Hill End Road, Harefield UB9 6JH, U.K.
Roland F R Schindler*Heart Science Centre, National Heart and Lung Institute, Imperial College, Hill End Road, Harefield UB9 6JH, U.K.
Harefield Hospital · GB

Funding

Medical Research Council MR/J010383/1
6 · The paper itself

Abstract

Popdc (Popeye-domain-containing) genes encode membrane-bound proteins and are abundantly present in cardiac myocytes and in skeletal muscle fibres. Functional analysis of Popdc1 (Bves) and Popdc2 in mice and of popdc2 in zebrafish revealed an overlapping role for proper electrical conduction in the heart and maintaining structural integrity of skeletal muscle. Popdc proteins mediate cAMP signalling and modulate the biological activity of interacting proteins. The two-pore channel TREK-1 interacts with all three Popdc proteins. In Xenopus oocytes, the presence of Popdc proteins causes an enhanced membrane transport leading to an increase in TREK-1 current, which is blocked when cAMP levels are increased. Another important Popdc-interacting protein is caveolin 3, and the loss of Popdc1 affects caveolar size. Thus a family of membrane-bound cAMP-binding proteins has been identified, which modulate the subcellular localization of effector proteins involved in organizing signalling complexes and assuring proper membrane physiology of cardiac myocytes.

Indexed as

AnimalsArrhythmias, CardiacCaveolin 3HumansMuscle ProteinsMyocardiumPotassium Channels, Tandem Pore DomainCaveolin 3Muscle Proteinspotassium channel protein TREK-1Potassium Channels, Tandem Pore Domain

Identifiers

PMID24646234
PMCPMC4080823
OpenAlexW2009603488

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.