Publikationsserver
Publizieren: oa@ur.de
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Dissertationen: dissertationen@ur.de
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Publikationsserver
Publizieren: oa@ur.de
0941 943 -4239 oder -69394
Dissertationen: dissertationen@ur.de
0941 943 -3904
Forschungsdaten: datahub@ur.de
0941 943 -5707
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 ...
Publikationsserver
Publizieren: oa@ur.de
0941 943 -4239 oder -69394
Dissertationen: dissertationen@ur.de
0941 943 -3904
Forschungsdaten: datahub@ur.de
0941 943 -5707
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