Startseite UB

Binding of phosphorylated peptides and inhibition of their interaction with disease-relevant human proteins by synthetic metal-chelate receptors

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.

Full text not available from this repository.

at publisher (via DOI)

at PubMed


Abstract

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 ...

plus


Export bibliographical data



Item Type:Article
Date:2010
Institutions:Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König
Projects:DFG
Identification Number:
ValueType
10.1002/jmr.986DOI
19728300PubMed ID
Keywords:metal-chelates; emission spectroscopy; protein binding; phosphate binding; protein–protein interaction; molecular recognition
Subjects:500 Science > 540 Chemistry & allied sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Regina Hoheisel
Deposited On:05 Jul 2010 15:25
Last Modified:26 Oct 2010 09:38
Item ID:15677
Owner Only: item control page
  1. University

University Library

Publication Server

Contact person
Gernot Deinzer

Telefon 0941 943-2759
Contact