%0 Journal Article
%1 Schweinsberg:2008:Proteomics:18338824
%A Schweinsberg, S.
%A Moll, D.
%A Burghardt, N. C.
%A Hahnefeld, C.
%A Schwede, F.
%A Zimmermann, B.
%A Drewianka, S.
%A Werner, L.
%A Kleinjung, F.
%A Genieser, H. G.
%A Schuchhardt, J.
%A Herberg, F. W.
%D 2008
%J Proteomics
%K herberg myown
%N 6
%P 1212-1220
%T Systematic interpretation of cyclic nucleotide binding studies using KinetXBase
%U http://www.ncbi.nlm.nih.gov/pubmed/18338824
%V 8
%X 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'-cyclic 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. KinetXBase 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.