Evidence map›Paper›PMID 40283209›Full record

ReviewLife (Basel, Switzerland)2025

Redox Regulation of cAMP-Dependent Protein Kinase and Its Role in Health and Disease.

Ese S Ekhator, Marco Fazzari, Robert H Newman

Abstract readReview
In one paragraph

Review in Life (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. 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.

Ese S EkhatorDepartment of Biology, North Carolina A&T State University, Greensboro, NC 27411, USA.ORCID 0000-0002-4931-9739
Marco FazzariDepartment of Pharmacology and Chemical Biology, University of Pittsburgh, Pittsburgh, PA 15261, USA.ORCID 0000-0002-4051-4431
Robert H NewmanDepartment of Biology, North Carolina A&T State University, Greensboro, NC 27411, USA.ORCID 0000-0002-3865-0266

Funding

Nitro-nitrate fatty acid derivatives as novel cGMP-dependent and cGMP-independent signaling mediatorsR01HL162787 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Marco Fazzari · 2023 to 2026
$2.4M
Biochemical and Cellular Analysis of Redox Modification on Protein Kinase Substrate SelectionSC1GM130545 · NIGMS · NORTH CAROLINA AGRI & TECH ST UNIV · PI NEWMAN, ROBERT HOWARD · 2018 to 2021
$1.4M
Redox regulation of protein kinase function: biochemical mechanisms and cellular consequencesR35GM153737 · NIGMS · NORTH CAROLINA AGRI & TECH ST UNIV · PI Robert Howard Newman · 2024 to 2026
$1.1M
NHLBI NIH HHS R01 HL162787NIGMS NIH HHS R35 GM153737NIGMS NIH HHS SC1 GM130545NIH HHS 1R35GM153737-01A1
6 · The paper itself

Abstract

Protein kinase A (PKA) is a key regulator of cellular signaling that regulates key physiological processes such as metabolism, cell proliferation, and neuronal function. While its activation by the second messenger 3',5'-cyclic adenosine triphosphate (cAMP) is well characterized, recent research highlights additional regulatory mechanisms, particularly oxidative post-translational modifications, that influence PKA's structure, activity, and substrate specificity. Both the regulatory and catalytic subunits of PKA are susceptible to redox modifications, which have been shown to play important roles in the regulation of key cellular functions, including cardiac contractility, lipid metabolism, and the immune response. Likewise, redox-dependent modulation of PKA signaling has been implicated in numerous diseases, including cardiovascular disorders, diabetes, and neurodegenerative conditions, making it a potential therapeutic target. However, the mechanisms of crosstalk between redox- and PKA-dependent signaling remain poorly understood. This review examines the structural and functional regulation of PKA, with a focus on redox-dependent modifications and their impact on PKA-dependent signaling. A deeper understanding of these mechanisms may provide new strategies for targeting oxidative stress in disease and restoring balanced PKA signaling in cells.

Indexed as

cAMP-dependent protein kinase (PKA)glutathionylationoxidationprotein kinasereactive oxygen species (ROS)redox-dependent signaling

Identifiers

PMID40283209
PMCPMC12029036

What OpenQuestion holds

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Registered trials

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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.