Evidence map›Paper›PMID 39322437›Full record

ReviewAnnual review of pharmacology and toxicology2025

Phosphodiesterases: Evolving Concepts and Implications for Human Therapeutics.

Evan D Kelly, Mark J Ranek, Manling Zhang, David A Kass, Grace K Muller

Abstract readReview
In one paragraph

Review in Annual review of pharmacology and toxicology, 2025. 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
–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

7 citing papers in PubMed.

  1. Regulation of Translation by PKA Signaling Pathway.International journal of molecular sciences · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Distinct cAMP Regulation in Scleroderma Lung and Skin Myofibroblasts Governs Their Dedifferentiation via p38α Inhibition.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  7. 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

5 authors.

Evan D KellyDepartment of Cell and Molecular Physiology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA; email: gmuller@luc.edu.
Mark J RanekDivision of Cardiology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Manling ZhangDivision of Cardiology, Veterans Affairs Pittsburgh Healthcare System, Pittsburgh, Pennsylvania, USA.
David A KassDivision of Cardiology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Grace K MullerDepartment of Cell and Molecular Physiology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA; email: gmuller@luc.edu.

Funding

Intersection of Obesity and Heart Failure with Preserved Ejection FractionR35HL166565 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI David Alan Kass · 2023 to 2026
$4.1M
Chip phosphorylation stimulates the degradation of mutant transthyretin to attenuate cardiac amyloidosisR01HL169273 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI Mark John Ranek · 2024 to 2026
$2.1M
Phosphodiesterase 1 (PDE1) Regulation of Myocardial Calcium and FunctionR01HL171586 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI Grace Kim Muller · 2024 to 2026
$1.9M
The Role of GCN5L1 Mediated Mitochondria to Nucleus Retrograde Cardiac Metabolism Reprogramming in Exercise and Heart FailureK08HL157616 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHANG, MANLING · 2021 to 2025
$802k
Chip phosphorylation stimulates the degradation of mutant transthyretin to attenuate cardiac amyloidosisR56HL169273 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI RANEK, MARK JOHN · 2023 to 2023
$670k
American Heart Association-American Stroke Association 20TPA35500008 - MARK RANEKNHLBI NIH HHS K08 HL157616NHLBI NIH HHS R01 HL169273NHLBI NIH HHS R01 HL171586NHLBI NIH HHS R35 HL166565NHLBI NIH HHS R56 HL169273
6 · The paper itself

Abstract

Phosphodiesterases (PDEs) are a superfamily of enzymes that hydrolyze cyclic nucleotides. While the 11 PDE subfamilies share common features, key differences confer signaling specificity. The differences include substrate selectivity, enzymatic activity regulation, tissue expression, and subcellular localization. Selective inhibitors of each subfamily have elucidated the protean role of PDEs in normal cell function. PDEs are also linked to diseases, some of which affect the immune, cardiac, and vascular systems. Selective PDE inhibitors are clinically used to treat these specific disorders. Ongoing preclinical studies and clinical trials are likely to lead to the approval of additional PDE-targeting drugs for therapy in human disease. In this review, we discuss the structure and function of PDEs and examine current and evolving therapeutic uses of PDE inhibitors, highlighting their mechanisms and innovative applications that could further leverage this crucial family of enzymes in clinical settings.

Indexed as

Phosphodiesterase InhibitorsPhosphoric Diester HydrolasesAnimalsHumansSignal TransductionPhosphodiesterase InhibitorsPhosphoric Diester Hydrolases2′,3′-cyclic-nucleotide phosphodiesterasescompartmentalized signalingcyclic nucleotidessecond messenger systemssignal transductiontherapeutics

Identifiers

PMID39322437
PMCPMC12757971

What OpenQuestion holds

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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.