ArticlePloS one2018
Blocking the interaction between S100A9 protein and RAGE V domain using S100A12 protein.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 17 citations in OpenAlex.
- Brain targeting and trafficking of extracellular vesicles in central nervous system diseases: a therapeutic roadmap.Nanomedicine (London, England) · 2026Review
- Virtual Probing on the Influence of CaCell biochemistry and biophysics · 2025Article
- Binding of Pro-Inflammatory Proteins S100A8 or S100A9 to Amyloid-β Peptide Suppresses Its Fibrillation.Biomolecules · 2025Article
- In silico pentapeptide design for the inhibition between S100 calcium-binding A9 (S100A9) proteins.Journal of molecular modeling · 2025Article
- Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.International journal of molecular sciences · 2022Article
- Key Genes Associated With Non-Alcoholic Fatty Liver Disease and Polycystic Ovary Syndrome.Frontiers in molecular biosciences · 2022Article
- Pathophysiology of RAGE in inflammatory diseases.Frontiers in immunology · 2022Review
- Discerning the promising binding sites of S100/calgranulins and their therapeutic potential in atherosclerosis.Expert opinion on therapeutic patents · 2021Review
- Development of anti-thrombotic vaccine against human S100A9 in rhesus monkey.Scientific reports · 2021Article
- S100P Interacts with p53 while Pentamidine Inhibits This Interaction.Biomolecules · 2021Article
- Differential expression and role of S100 proteins in chronic rhinosinusitis.Current opinion in allergy and clinical immunology · 2020Review
- S100A12 in Digestive Diseases and Health: A Scoping Review.Gastroenterology research and practice · 2020Article
- Development of Predictive Models for Identifying Potential S100A9 Inhibitors Based on Machine Learning Methods.Frontiers in chemistry · 2019Article
- Lysozyme as the anti-proliferative agent to block the interaction between S100A6 and the RAGE V domain.PloS one · 2019Article
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
The proteins S100A9 and S100A12 are associated with the human S100 calcium-binding protein family. These proteins promote interaction with target proteins and alter their conformation when they bind to calcium ions in EF-hand motifs. The V domain of RAGE (Receptor for Advanced Glycation End products) is crucial for S100A9 binding. The binding of RAGE with S100 family proteins aids in cell proliferation. In this report, we demonstrate that S100A12 protein hinders the binding of S100A9 with the RAGE V-domain. We used fluorescence and NMR spectroscopy to analyze the interaction of S100A9 with S100A12. The binary complex models of S100A9-S100A12 were developed using data obtained from 1H-15N HSQC NMR titrations and the HADDOCK program. We overlaid the complex models of S100A9-S100A12 with the same orientation of S100A9 and the RAGE V-domain. This complex showed that S100A12 protein blocks the interaction between S100A9 and the RAGE V-domain. It means S100A12 may be used as an antagonist for S100A9. The results could be favorable for developing anti-cancer drugs based on S100 family proteins.
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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.