Journal article
Systematic interpretation of cyclic nucleotide binding studies using KinetXBase

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Schweinsberg, S.; Moll, D.; Burghardt, N.; Hahnefeld, C.; Schwede, F.; Zimmermann, B.; Drewianka, S.; Werner, L.; Kleinjung, F.; Genieser, H.; Schuchhardt, J.; Herberg, F.
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Functional proteomics aims to describe cellular protein networks in depth based on the quantification of molecular interactions. in order to study the interaction of adenosine-3',5'-cydic monophosphate (cAMP), a general second messenger involved in several intracellular signalling networks, with one of its respective target proteins, the regulatory (R) subunit of cAMP dependent protein kinase (PKA), a number of different methods was employed. These include fluorescence polarisation (FP), isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), amplified luminescence proximity homogeneous assay (ALPHA-screen), radioligand binding or activity-based assays. Kinetic, thermodynamic and equilibrium binding data of a variety of cAMP derivatives to several cAMP binding domains were integrated in a single database system, we called KinetXBase, allowing for very distinct data formats. KineffBase is a practical data handling system for molecular interaction data of any kind, providing a synopsis of data derived from different technologies. This supports ongoing efforts in the bioinformatics community to devise formal concepts for a unified representation of interaction data, in order to enable their exchange and easy comparison. KinetXBase was applied here to analyse complex cAMP binding data and highly site-specific cAMP analogues could be identified. The software package is free for download by academic users.

Last updated on 2019-25-07 at 11:38

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