Aufsatz in einer Fachzeitschrift
Systematic interpretation of cyclic nucleotide binding studies using KinetXBase
Details zur Publikation
Autor(inn)en: | Schweinsberg, S.; Moll, D.; Burghardt, N.; Hahnefeld, C.; Schwede, F.; Zimmermann, B.; Drewianka, S.; Werner, L.; Kleinjung, F.; Genieser, H.; Schuchhardt, J.; Herberg, F. |
Publikationsjahr: | 2008 |
Zeitschrift: | Proteomics: Proteomics and Systems Biology |
Seitenbereich: | 1212-1220 |
Jahrgang/Band : | 8 |
Erste Seite: | 1212 |
Letzte Seite: | 1220 |
ISSN: | 1615-9853 |
DOI-Link der Erstveröffentlichung: |
Zusammenfassung, Abstract
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.
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.
