Evidence map›Paper›PMID 40717023›Full record

ReviewThe FEBS journal2025

Posttranslational modifications of phosphodiesterase type 4 enzymes represent novel points for therapeutic targeting.

Madihah Hussain, Gonzalo S Tejeda, George S Baillie

Abstract readReview
In one paragraph

Review in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

3 authors.

Madihah HussainSchool of Cardiovascular and Metabolic Health, College of Medical Veterinary and Life Sciences, University of Glasgow, UK.
Gonzalo S TejedaSchool of Cardiovascular and Metabolic Health, College of Medical Veterinary and Life Sciences, University of Glasgow, UK.
George S BaillieSchool of Cardiovascular and Metabolic Health, College of Medical Veterinary and Life Sciences, University of Glasgow, UK.ORCID https://orcid.org/0000-0003-2469-6316

Funding

British Heart Foundation SP/16/3/32317Medical Research Council MR/y00364/1
6 · The paper itself

Abstract

Cyclic AMP is a second messenger that is produced in response to the activation of many G-protein-coupled receptors. As each receptor type is linked to a transient but distinct physiological outcome, the activation of cAMP effector proteins is highly compartmentalized by the action of phosphodiesterases (PDEs). Phosphodiesterase type 4 (PDE4) enzymes are expressed as 25 different isoforms, and the function of each protein is linked to its cellular location(s). Fine-tuning of cAMP dynamics in space and time is underpinned by PDE4 activity shifts or PDE4 translocations that are driven by posttranslational modifications. As 'omics' technology improves, we are now learning more about these PDE4 events, and we can link them to diseases where aberrant cAMP signaling is causative. Additionally, recent advances allow us to pinpoint specific PDE4 modifications with targeted therapies that will lessen the chances of side effects. This review charts all known PDE4 modifications and links them to innovative existing pharmaceutical concepts or possible future therapeutic developments.

Indexed as

Cyclic Nucleotide Phosphodiesterases, Type 4Phosphodiesterase 4 InhibitorsProtein Processing, Post-TranslationalAnimalsCyclic AMPHumansMolecular Targeted TherapySignal TransductionCyclic AMPCyclic Nucleotide Phosphodiesterases, Type 4Phosphodiesterase 4 Inhibitorscyclic AMPphosphodiesterase type 4posttranslational modification

Identifiers

PMID40717023
PMCPMC12699188

What Socratic 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 Socratic graph.