Evidence map›Paper›PMID 16839566›Full record

ReviewJournal of molecular and cellular cardiology2007

Regulation of endothelial and myocardial NO synthesis by multi-site eNOS phosphorylation.

Peter F Mount, Bruce E Kemp, David A Power

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular and cellular cardiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 214 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
214citing papers in PubMed, 1 pooled it
13.6field-weighted citation impact, top 1% 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

214 citing papers in PubMed, 1 synthesis or guideline pooled it, 491 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Trial
  4. Dietary phosphorus acutely impairs endothelial function.Journal of the American Society of Nephrology : JASN · 2009
    Trial
  5. Article
  6. Article
  7. The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025
    Review
  8. Review
  9. Review
  10. Article
  11. Subcellular Localization Guides eNOS Function.International journal of molecular sciences · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Acta pharmaceutica Sinica. B · 2024
    Review

154 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Peter F MountDepartment of Nephrology, Austin Health, Studley Road, Heidelberg 3084, Victoria, Australia. Peter.Mount@nh.org.au
Bruce E Kemp
David A Power
Austin Health · AUHealth Sciences and Nutrition · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The controlled regulation of nitric oxide (NO) synthesis in endothelial cells and cardiomyocytes by the endothelial form of nitric oxide synthase (eNOS or NOS3) is essential for cardiovascular health. In recent years, a picture of complex and precise regulation of eNOS activity involving multi-site phosphorylation of specific serine and threonine residues has emerged. Regulation of endothelial NO synthesis by multi-site eNOS phosphorylation occurs in response to a wide variety of humoral, mechanical and pharmacological stimuli. This regulation involves numerous kinases and phosphatases, as well as interactions with other aspects of eNOS regulation such as Ca(2+) flux, protein-protein interactions and regulation of subcellular localization. Phosphorylation of eNOS-Ser(1177) close to the carboxy-terminal is a critical requirement for eNOS activation. In addition, phosphorylation of eNOS-Ser(633) in the flavin mononucleotide (FMN) binding domain also increases eNOS activity and appears particularly important for the maintenance of NO synthesis after initial activation by Ca(2+) flux and Ser(1177) phosphorylation. In contrast, NO synthesis is inhibited by phosphorylation of eNOS-Thr(495), which interferes with the binding of calmodulin to the eNOS calmodulin-binding domain. Regulated phosphorylation of eNOS also occurs at eNOS-Ser(114) and eNOS-Ser(615); however, the functions of these phosphorylation sites remain controversial. This review summarizes the present knowledge of the regulation of NO synthesis by multi-site eNOS phosphorylation and its relationship to other mechanisms of eNOS regulation. This progress in understanding important mechanisms controlling endothelial NO synthesis creates new opportunities to understand and potentially treat cardiovascular diseases characterized by deficient NO synthesis.

Indexed as

Protein Processing, Post-TranslationalAnimalsCardiovascular DiseasesEndothelium, VascularHumansMyocardiumNitric OxideNitric Oxide Synthase Type IIIPhosphorylationNitric OxideNitric Oxide Synthase Type IIINOS3 protein, human

Identifiers

PMID16839566
OpenAlexW2047770461

What OpenQuestion holds

Textmetadata
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.