Evidence map›Paper›PMID 26236235›Full record

ReviewFrontiers in pharmacology2015

Redox regulation of cGMP-dependent protein kinase Iα in the cardiovascular system.

Oleksandra Prysyazhna, Philip Eaton

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. An In Vivo Model of Estrogen Supplementation Concerning the Expression of CaJournal of cardiovascular development and disease · 2024
    Article
  3. New Therapeutics for Heart Failure: Focusing on cGMP Signaling.International journal of molecular sciences · 2023
    Review
  4. NADPH Oxidases in Pain Processing.Antioxidants (Basel, Switzerland) · 2022
    Review
  5. Review
  6. Review
  7. Review
  8. Oxidation of PKGIα mediates an endogenous adaptation to pulmonary hypertension.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. 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

2 authors at 1 institution in 1 country.

Oleksandra PrysyazhnaCardiovascular Division, King's College London, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital , London, UK.
Philip EatonCardiovascular Division, King's College London, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital , London, UK.
King's College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C503646/1British Heart Foundation FS/11/45/28859British Heart Foundation PG/10/98/28655British Heart Foundation PG/13/13/30018British Heart Foundation PG/15/26/31373British Heart Foundation RG/12/12/29872Medical Research Council G0600785Medical Research Council G0700320Medical Research Council G1000458Medical Research Council MR/K003232/1Medical Research Council MR/L009684/1
6 · The paper itself

Abstract

Elevated levels of oxidants in biological systems have been historically referred to as "oxidative stress," a choice of words that perhaps conveys an imbalanced view of reactive oxygen species in cells and tissues. The term stress suggests a harmful role, whereas a contemporary view is that oxidants are also crucial for the maintenance of homeostasis or adaptive signaling that can actually limit injury. This regulatory role for oxidants is achieved in part by them inducing oxidative post-translational modifications of proteins which may alter their function or interactions. Such mechanisms allow changes in cell oxidant levels to be coupled to regulated alterations in enzymatic function (i.e., signal transduction), which enables "redox signaling." In this review we focus on the role of cGMP-dependent protein kinase (PKG) Ia disulfide dimerisation, an oxidative modification that is induced by oxidants that directly activates the enzyme, discussing how this impacts on the cardiovascular system. Additionally, how this oxidative activation of PKG may coordinate with or differ from classical activation of this kinase by cGMP is also considered.

Indexed as

cardio-vascular systemcGMPdisulfide dimerisationoxidative modificationprotein kinase G

Identifiers

PMID26236235
PMCPMC4505079
OpenAlexW1481963648

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.