Evidence map›Paper›PMID 24907600›Full record

ReviewBiochemical pharmacology2014

Secretory phospholipase A2 enzymes as pharmacological targets for treatment of disease.

Nhat D Quach, Robert D Arnold, Brian S Cummings

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 177 citations in OpenAlex.

  1. Group IIA Secretory Phospholipase AArteriosclerosis, thrombosis, and vascular biology · 2019
    Trial
  2. Article
  3. Review
  4. Secreted phospholipase PLA2G5 acts as a hemolytic factor in sepsis.The Journal of clinical investigation · 2026
    Article
  5. Phospholipases ABiomolecules · 2025
    Review
  6. Review
  7. Review
  8. Unraveling snake venom phospholipase APharmacological reports : PR · 2023
    Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Subversion of host cell signaling: The arsenal of Rickettsial species.Frontiers in cellular and infection microbiology · 2022
    Review
  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

3 authors at 2 institutions in 1 country.

Nhat D QuachPharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, United States.
Robert D ArnoldDepartment of Drug Discovery & Development, Harrison School of Pharmacy, Auburn University, Auburn, AL 36849-5503, United States.
Brian S CummingsPharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, United States. Electronic address: bsc@rx.uga.edu.
University of Georgia · USAuburn University · US

Funding

Secretory Phospholipases sPLA2 and their Receptors for Delivering NanoparticlesR01EB016100 · NIBIB · AUBURN UNIVERSITY AT AUBURN · PI ARNOLD, ROBERT D · 2013 to 2016
$1.3M
sPLA2 Selective Degradation of NanoparticlesR21EB008153 · NIBIB · UNIVERSITY OF GEORGIA · PI ARNOLD, ROBERT D, CUMMINGS, BRIAN S · 2009 to 2010
$408k
NIBIB NIH HHS R01EB0116100NIBIB NIH HHS R01 EB016100NIBIB NIH HHS R21 EB008153NIBIB NIH HHS R21EB08153
6 · The paper itself

Abstract

Phospholipase A2 (PLA2) cleave phospholipids preferentially at the sn-2 position, liberating free fatty acids and lysophospholipids. They are classified into six main groups based on size, location, function, substrate specificity and calcium requirement. These classes include secretory PLA2 (sPLA2), cytosolic (cPLA2), Ca(2+)-independent (iPLA2), platelet activating factor acetylhydrolases (PAF-AH), lysosomal PLA2 (LyPLA2) and adipose specific PLA2 (AdPLA2). It is hypothesized that PLA2 can serve as pharmacological targets for the therapeutic treatment of several diseases, including cardiovascular diseases, atherosclerosis, immune disorders and cancer. Special emphasis has been placed on inhibitors of sPLA2 isoforms as pharmacological moieties, mostly due to the fact that these enzymes are activated during inflammatory events and because their expression is increased in several diseases. This review focuses on understanding how sPLA2 isoform expression is altered during disease progression and the possible therapeutic interventions to specifically target sPLA2 isoforms, including new approaches using nano-particulate-based strategies.

Indexed as

Amino Acid SequenceCardiovascular DiseasesEnzyme InhibitorsHumansInflammationMolecular Sequence DataNeoplasmsPhospholipases A2, SecretorySepsisSequence Homology, Amino AcidEnzyme InhibitorsPhospholipases A2, SecretoryCell signalingInteractomesLiposomesNanoparticlesPhospholipase A(2) receptorSecretory phospholipase A(2)

Identifiers

PMID24907600
PMCPMC4104246
OpenAlexW2027387500

What OpenQuestion holds

Textmetadata
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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.