Published in Sci Rep on March 03, 2016
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The 1.5 Å crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding. J Biol Chem (2010) 1.16
Design and structure of peptide and peptidomimetic antagonists of protein-protein interaction. Curr Protein Pept Sci (2005) 1.16
Site-specific blockade of RAGE-Vd prevents amyloid-beta oligomer neurotoxicity. J Neurosci (2008) 1.15
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Critical role of RAGE and HMGB1 in inflammatory heart disease. Proc Natl Acad Sci U S A (2015) 0.87
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RAGE Mediates the Pro-Migratory Response of Extracellular S100A4 in Human Thyroid Cancer Cells. Thyroid (2015) 0.82
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Deletion of bone-marrow-derived receptor for AGEs (RAGE) improves renal function in an experimental mouse model of diabetes. Diabetologia (2014) 0.79
The role of receptor for advanced glycation end products in airway inflammation in CF and CF related diabetes. Sci Rep (2015) 0.77
NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment. J Biomol NMR (2012) 0.77
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