ArticleJournal of medicinal chemistry2016
Development of Potent and Selective Inhibitors for Group VIA Calcium-Independent Phospholipase A2 Guided by Molecular Dynamics and Structure-Activity Relationships.
Article in Journal of medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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.
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.
Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- Specificity mechanism of Group VIA calcium-independent phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2025Article
- Next generation thiazolyl ketone inhibitors of cytosolic phospholipase ANature communications · 2025Article
- The mechanism of allosteric regulation of calcium-independent phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Catalytic Asymmetric Difluoroalkylation Using In Situ Generated Difluoroenol Species as the Privileged Synthon.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Membrane Association Allosterically Regulates Phospholipase AAccounts of chemical research · 2022Article
- Vitamin E functions by association with a novel binding site on the 67 kDa laminin receptor activating diacylglycerol kinase.The Journal of nutritional biochemistry · 2022Article
- Outtakes from My Journey through the World of LIPID MAPS.Molecules (Basel, Switzerland) · 2022Article
- Allosteric regulation by membranes and hydrophobic subsites in phospholipase AThe Journal of biological chemistry · 2022Review
- Each phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2022Article
- α-Ketoheterocycles Able to Inhibit the Generation of Prostaglandin EBiomolecules · 2021Article
- Omega-3 versus Omega-6 fatty acid availability is controlled by hydrophobic site geometries of phospholipase AJournal of lipid research · 2021Article
- Rescue of Hepatic Phospholipid Remodeling Defectin iPLA2β-Null Mice Attenuates Obese but Not Non-Obese Fatty Liver.Biomolecules · 2020Review
- Lipidomics-based assays coupled with computational approaches can identify novel phospholipase AAdvances in biological regulation · 2020Article
- iPLABiochimica et biophysica acta. Molecular and cell biology of lipids · 2019Review
- Small-molecule inhibitors as potential therapeutics and as tools to understand the role of phospholipases ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2019Review
- Phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2019Review
- β-Lactones: A Novel Class of CaJournal of medicinal chemistry · 2019Article
- Substrate-Specific Inhibition Constants for Phospholipase AJournal of medicinal chemistry · 2019Article
- Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.Journal of the American Chemical Society · 2018Article
- Review of four major distinct types of human phospholipase AAdvances in biological regulation · 2018Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The development of inhibitors for phospholipase A2 (PLA2) is important in elucidating the enzymes implication in various biological pathways. PLA2 enzymes are an important pharmacological target implicated in various inflammatory diseases. Computational chemistry, organic synthesis, and in vitro assays were employed to develop potent and selective inhibitors for group VIA calcium-independent PLA2. A set of fluoroketone inhibitors was studied for their binding mode with two human cytosolic PLA2 enzymes: group IVA cPLA2 and group VIA iPLA2. New compounds were synthesized and assayed toward three major PLA2s. This study led to the development of four potent and selective thioether fluoroketone inhibitors as well as a thioether keto-1,2,4-oxadiazole inhibitor for GVIA iPLA2, which will serve as lead compounds for future development and studies. The keto-1,2,4-oxadiazole functionality with a thioether is a novel structure, and it will be used as a lead to develop inhibitors with higher potency and selectivity toward GVIA iPLA2.
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What OpenQuestion holds
Registered trials
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.