Riechers, A. and Grauer, A. and Ritter , S. and Sperl, B. and Berg, T. and König, Burkhard (2010) Binding of phosphorylated peptides and inhibition of their interaction with disease-relevant human proteins by synthetic metal-chelate receptors. Journal of Molecular Recognition (23), pp. 329-334.
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The modulation of biological signal transduction pathways by masking phosphorylated amino acid residues represents a viable route toward pharmacologic protein regulation. Binding of phosphorylated amino acid residues has been achieved with synthetic metal-chelate receptors. The affinity and selectivity of such receptors can be enhanced if combined with a second binding site. We demonstrate this ...
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|Institutions:||Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König|
|Keywords:||metal-chelates; emission spectroscopy; protein binding; phosphate binding; protein–protein interaction; molecular recognition|
|Dewey Decimal Classification:||500 Science > 540 Chemistry & allied sciences|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited on:||05 Jul 2010 15:25|
|Last modified:||26 Oct 2010 09:38|