Small Molecule Inhibition of Ligand-Stimulated RAGE-DIAPH1 Signal Transduction

The receptor for advanced glycation endproducts (RAGE) binds diverse ligands linked to chronic inflammation and disease. NMR spectroscopy and x-ray crystallization studies of the extracellular domains of RAGE indicate that RAGE ligands bind by distinct charge- and hydrophobicity-dependent mechanisms...

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Veröffentlicht in:	Scientific reports 2016-03, Vol.6 (1), p.22450-22450, Article 22450
Hauptverfasser:	Manigrasso, Michaele B., Pan, Jinhong, Rai, Vivek, Zhang, Jinghua, Reverdatto, Sergey, Quadri, Nosirudeen, DeVita, Robert J., Ramasamy, Ravichandran, Shekhtman, Alexander, Schmidt, Ann Marie
Format:	Artikel
Sprache:	eng
Schlagworte:	13/106 13/21 38/47 38/90 49/98 631/92/507 64/60 692/308/153 Adaptor Proteins, Signal Transducing - antagonists & inhibitors Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Advanced glycosylation end products Alzheimer's disease Animals Crystallization Diabetes mellitus Drug development Gene expression Glycosylation Humanities and Social Sciences Humans Hydrophobicity Intracellular signalling Ligands Magnetic resonance spectroscopy Mice multidisciplinary Neurodegenerative diseases NMR Nuclear magnetic resonance Protein interaction Receptor for Advanced Glycation End Products - antagonists & inhibitors Receptor for Advanced Glycation End Products - metabolism Science Science (multidisciplinary) Signal transduction Signal Transduction - drug effects Spectroscopy
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