Evidence map›Paper›PMID 28939645›Full record

ReviewPhysiological genomics2017

Cyclooxygenase 2: protein-protein interactions and posttranslational modifications.

Anna Alexanian, Andrey Sorokin

Open access · greenAbstract readReview
In one paragraph

Review in Physiological genomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

40 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Intracellular NADJournal of cellular and molecular medicine · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
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  13. AMD1, a cardiotoxicity target for Maduramicin.BMC pharmacology & toxicology · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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.

Anna AlexanianCardiovascular Center and Department of Medicine, Medical College of Wisconsin, Milwaukee, Wisconsin.
Andrey SorokinCardiovascular Center and Department of Medicine, Medical College of Wisconsin, Milwaukee, Wisconsin sorokin@mcw.edu.ORCID http://orcid.org/0000-0002-5660-0190
Medical College of Wisconsin · US

Funding

Endothelin Signaling and Actions in Renal MesangiumR01DK098159 · NIDDK · MEDICAL COLLEGE OF WISCONSIN · PI SOROKIN, ANDREY · 2013 to 2016
$1.3M
Posttranslational regulation of Cox-2 activityR03CA182114 · NCI · MEDICAL COLLEGE OF WISCONSIN · PI SOROKIN, ANDREY · 2014 to 2015
$153k
NCI NIH HHS R03 CA182114NIDDK NIH HHS R01 DK098159
6 · The paper itself

Abstract

Numerous studies implicate the cyclooxygenase 2 (COX2) enzyme and COX2-derived prostanoids in various human diseases, and thus, much effort has been made to uncover the regulatory mechanisms of this enzyme. COX2 has been shown to be regulated at both the transcriptional and posttranscriptional levels, leading to the development of nonsteroidal anti-inflammatory drugs (NSAIDs) and selective COX2 inhibitors (COXIBs), which inhibit the COX2 enzyme through direct targeting. Recently, evidence of posttranslational regulation of COX2 enzymatic activity by s-nitrosylation, glycosylation, and phosphorylation has also been presented. Additionally, posttranslational regulators that actively downregulate COX2 expression by facilitating increased proteasome degradation of this enzyme have also been reported. Moreover, recent data identified proteins, located in close proximity to COX2 enzyme, that serve as posttranslational modulators of COX2 function, upregulating its enzymatic activity. While the precise mechanisms of the protein-protein interaction between COX2 and these regulatory proteins still need to be addressed, it is likely these interactions could regulate COX2 activity either as a result of conformational changes of the enzyme or by impacting subcellular localization of COX2 and thus affecting its interactions with regulatory proteins, which further modulate its activity. It is possible that posttranslational regulation of COX2 enzyme by such proteins could contribute to manifestation of different diseases. The uncovering of posttranslational regulation of COX2 enzyme will promote the development of more efficient therapeutic strategies of indirectly targeting the COX2 enzyme, as well as provide the basis for the generation of novel diagnostic tools as biomarkers of disease.

Indexed as

Protein Interaction MapsProtein Processing, Post-TranslationalAnimalsCyclooxygenase 2DiseaseHumansModels, BiologicalProtein BindingCyclooxygenase 2cyclooxygenaseELMO1Fynprostanoidsprotein-protein interactions

Identifiers

PMID28939645
PMCPMC5792139
OpenAlexW2759822706

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.