ArticleJournal of the American Chemical Society2009
Location of inhibitors bound to group IVA phospholipase A2 determined by molecular dynamics and deuterium exchange mass spectrometry.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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
37 citing papers in PubMed, 62 citations in OpenAlex.
- Conformational Dynamics and Activation of Membrane-Associated Human Group IVA Cytosolic Phospholipase AThe journal of physical chemistry letters · 2025Article
- A Lipidomic Approach to Studying the Downregulation of Free Fatty Acids by Cytosolic Phospholipase ABiomolecules · 2025Article
- Synthesis, activity and metabolic stability of propan-2-one substituted tetrazolylalkanoic acids as dual inhibitors of cytosolic phospholipase ARSC medicinal chemistry · 2023Article
- Functions and mechanisms of cytosolic phospholipase ANeural regeneration research · 2023Review
- Membrane Association Allosterically Regulates Phospholipase AAccounts of chemical research · 2022Article
- Allosteric regulation by membranes and hydrophobic subsites in phospholipase AThe Journal of biological chemistry · 2022Review
- The Alpha Keto Amide Moiety as a Privileged Motif in Medicinal Chemistry: Current Insights and Emerging Opportunities.Journal of medicinal chemistry · 2021Review
- Omega-3 versus Omega-6 fatty acid availability is controlled by hydrophobic site geometries of phospholipase AJournal of lipid research · 2021Article
- 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
- Dynamic structural biology at the protein membrane interface.The Journal of biological chemistry · 2019Review
- Substrate-Specific Inhibition Constants for Phospholipase AJournal of medicinal chemistry · 2019Article
- Dimerization interface of osteoprotegerin revealed by hydrogen-deuterium exchange mass spectrometry.The Journal of biological chemistry · 2018Article
- Article
- Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.Journal of the American Chemical Society · 2018Article
- Hydrogen-deuterium exchange reveals long-range dynamical allostery in soybean lipoxygenase.The Journal of biological chemistry · 2018Article
- A New Generation of Arachidonic Acid Analogues as Potential Neurological Agent Targeting Cytosolic Phospholipase AScientific reports · 2017Article
- 2-Oxoesters: A Novel Class of Potent and Selective Inhibitors of Cytosolic Group IVA Phospholipase AScientific reports · 2017Article
- Analyses of Calcium-Independent Phospholipase AMethods in enzymology · 2017Article
- Liberating Chiral Lipid Mediators, Inflammatory Enzymes, and LIPID MAPS from Biological Grease.The Journal of biological chemistry · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
An analysis of group IVA (GIVA) phospholipase A(2) (PLA(2)) inhibitor binding was conducted using a combination of deuterium exchange mass spectrometry (DXMS) and molecular dynamics (MD). Models of the GIVA PLA(2) inhibitors pyrrophenone and the 2-oxoamide AX007 docked into the protein were designed on the basis of deuterium exchange results, and extensive molecular dynamics simulations were run to determine protein-inhibitor contacts. The models show that both inhibitors interact with key residues that also exhibit changes in deuterium exchange upon inhibitor binding. Pyrrophenone is bound to the protein through numerous hydrophobic residues located distal from the active site, while the oxoamide is bound mainly through contacts near the active site. We also show differences in protein dynamics around the active site between the two inhibitor-bound complexes. This combination of computational and experimental methods is useful in defining more accurate inhibitor binding sites and can be used in the generation of better inhibitors against GIVA PLA(2).
Indexed as
Identifiers
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.