A study of the lipid-mediated dimerization of the RAGE TM+JM domains by molecular dynamic simulations
Author:
Funder
National Natural Science Foundation of China
Fundamental Research Funds for the Central Universities
CHEMCLOUDCOMPUTING
Publisher
Elsevier BV
Subject
General Chemistry
Reference17 articles.
1. The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
2. RAGE Mediates a Novel Proinflammatory Axis
3. Hexameric Calgranulin C (S100A12) Binds to the Receptor for Advanced Glycated End Products (RAGE) Using Symmetric Hydrophobic Target-binding Patches
4. Homodimerization Is Essential for the Receptor for Advanced Glycation End Products (RAGE)-mediated Signal Transduction
5. Interaction of the RAGE Cytoplasmic Domain with Diaphanous-1 Is Required for Ligand-stimulated Cellular Migration through Activation of Rac1 and Cdc42
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