Highly functionalized terpyridines as competitive inhibitors of AKAP-PKA interactions
Autor: | Schäfer, G, Milić, J, Eldahshan, A, Götz, F, Zühlke, K, Schillinger, C, Kreuchwig, A, Elkins, J, Abdul Azeez, K, Oder, A, Moutty, M, Masada, N, Beerbaum, M, Schlegel, B, Niquet, S, Schmieder, P, Krause, G, von Kries, J, Cooper, D, Knapp, S, Rademann, J, Rosenthal, W, Klussmann, E |
---|---|
Jazyk: | angličtina |
Rok vydání: | 2013 |
Předmět: |
endocrine system
Binding Sites Pyridines A Kinase Anchor Proteins Helix Mimetics protein–protein interactions Binding Competitive Cyclic AMP-Dependent Protein Kinases Communications Protein Structure Tertiary Molecular Docking Simulation HEK293 Cells AKAP Cardiovascular and Metabolic Diseases Humans Protein Interaction Domains and Motifs protein kinase A Suzuki coupling terpyridines peptide mimetics Protein Kinase Inhibitors |
Zdroj: | Angewandte Chemie (International Ed. in English) |
Popis: | A good fit: Interactions between A-kinase anchoring proteins (AKAPs) and protein kinaseA (PKA) play key roles in a plethora of physiologically relevant processes whose dysregulation causes or is associated with diseases such as heart failure. Terpyridines have been developed as α-helix mimetics for the inhibition of such interactions and are the first biologically active, nonpeptidic compounds that block the AKAP binding site of PKA. © 2013 The Authors. Published by Wiley-VCH Verlag GmbH and Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
Databáze: | OpenAIRE |
Externí odkaz: |