Evidence map›Paper›PMID 26774606›Full record

ReviewAdvances in biological regulation2016

Membrane and inhibitor interactions of intracellular phospholipases A2.

Varnavas D Mouchlis, Edward A Dennis

Open access · greenAbstract readReview
In one paragraph

Review in Advances in biological regulation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Review
  9. Article
  10. Edema Induced by aInternational journal of molecular sciences · 2018
    Article
  11. Phospholipid subcellular localization and dynamics.The Journal of biological chemistry · 2018
    Review
  12. Article
  13. Review of four major distinct types of human phospholipase AAdvances in biological regulation · 2018
    Review
  14. Article
  15. Article
  16. Articular inflammation induced by an enzymatically-inactive Lys49 phospholipase AThe journal of venomous animals and toxins including tropical diseases · 2017
    Article
  17. Article
  18. Article
  19. 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.

Varnavas D MouchlisDepartment of Pharmacology and Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.
Edward A DennisDepartment of Pharmacology and Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: edennis@ucsd.edu.
University of California, San Diego · US

Funding

ACTION OF LIPOLYTIC ENZYMESR01GM020501 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 1985 to 2020
$7.3M
NIGMS NIH HHS R01 GM020501
6 · The paper itself

Abstract

Studying phospholipases A2 (PLA2s) is a challenging task since they act on membrane-like aggregated substrates and not on monomeric phospholipids. Multidisciplinary approaches that include hydrogen/deuterium exchange mass spectrometry (DXMS) and computational techniques have been employed with great success in order to address important questions about the mode of interactions of PLA2 enzymes with membranes, phospholipid substrates and inhibitors. Understanding the interactions of PLA2s is crucial since these enzymes are the upstream regulators of the eicosanoid pathway liberating free arachidonic acid (AA) and other polyunsaturated fatty acids (PUFA). The liberation of AA by PLA2 enzymes sets off a cascade of molecular events that involves downstream regulators such as cyclooxygenase (COX) and lipoxygenase (LOX) metabolites leading to inflammation. Aspirin and other nonsteroidal anti-inflammatory drugs (NSAIDs) work by inhibiting COX, while Zileuton inhibits LOX and both rely on PLA2 enzymes to provide them with AA. That means PLA2 enzymes can potentially also be targeted to diminish inflammation at an earlier point in the process. In this review we describe extensive efforts reported in the past to define the interactions of PLA2 enzymes with membranes, substrate phospholipids and inhibitors using DXMS, molecular docking, and molecular dynamics (MD) simulations.

Indexed as

AnimalsAnti-Inflammatory Agents, Non-SteroidalArachidonic AcidAspirinCell MembraneEukaryotic CellsGene Expression RegulationHumansHydroxyureaLipoxygenaseModels, MolecularMolecular Docking SimulationMolecular Dynamics SimulationPhospholipases A2PhospholipidsProstaglandin-Endoperoxide SynthasesAnti-Inflammatory Agents, Non-SteroidalArachidonic AcidAspirinHydroxyureaLipoxygenasePhospholipases A2PhospholipidsProstaglandin-Endoperoxide SynthaseszileutonAllosteric regulationCatalytic cycleDXMSEicosanoid pathwayMolecular dynamics simulationsPAPCPhospholipase A(2)

Identifiers

PMID26774606
PMCPMC4884535
OpenAlexW2199729762

What OpenQuestion holds

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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.