ArticlePloS one2017
Alpha conotoxin-BuIA globular isomer is a competitive antagonist for oleoyl-L-alpha-lysophosphatidic acid binding to LPAR6; A molecular dynamics study.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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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.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Review
- High-Throughput Prediction and Design of Novel Conopeptides for Biomedical Research and Development.Biodesign research · 2022Article
- Role of lysophosphatidic acid and its receptors in health and disease: novel therapeutic strategies.Signal transduction and targeted therapy · 2021Review
- Graph-Directed Approach for Downselecting Toxins for Experimental Structure Determination.Marine drugs · 2020Article
- Nature-Derived Peptides: A Growing Niche for GPCR Ligand Discovery.Trends in pharmacological sciences · 2019Review
- Snails In Silico: A Review of Computational Studies on the Conopeptides.Marine drugs · 2019Review
- Regulation of tumor cell - Microenvironment interaction by the autotaxin-lysophosphatidic acid receptor axis.Advances in biological regulation · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysophosphatidic acid receptor 6 (LPAR6) is a G-protein coupled receptor (GPCR) involved in hair development and cytoskeleton formation in mammals. Its proliferation is implicated in several forms of cancer including liver cancer, squamous cell carcinoma and metastatic prostate cancer. Current study emphasizes the isolation of competitive non-lipid and stable peptide antagonists for Lysophosphatidic acid ligand. A total of 148 conotoxin structures were characterized for their binding abilities against LPAR6. Subsequently, top 10 conotoxins were selected on the basis of binding energy values, residual contributions and conformational cluster saturations. BuIA (a member of Alpha- conotoxins family), contryphan-R and contryphan-Lo (Synthetic class) conotoxins, exhibiting efficient binding parameters were subjected to molecular dynamics simulation assays and topology analysis. We propose that BuIA might be a potent antagonist due to its predominant binding at the extracellular region of LPAR6. Current study provides a backbone for understanding structural and functional insights of LPAR6 and findings of this study may be helpful in designing novel therapeutic targets for the treatment of cancers caused by elevated LPAR6 expression.
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