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

Journal of Molecular Recognition

Volumn 23, Issue 3, 2010, Pages 329-334

  Riechers, Alexander ^a   Grauer, Andreas ^a   Ritter, Stefan ^a   Sperl, Bianca ^b   Berg, Thorsten ^b   König, Burkhard ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Emission spectroscopy; Metal chelates; Molecular recognition; Phosphate binding; Protein binding; Protein protein interaction

Indexed keywords

CHECKPOINT KINASE 2; CHELATING AGENT; METAL; PEPTIDE; PROTEIN SERINE THREONINE KINASE; STAT1 PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN BINDING; SIGNAL TRANSDUCTION;

CHELATING AGENTS; HUMANS; METALS; MOLECULAR STRUCTURE; PEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES; SIGNAL TRANSDUCTION; STAT1 TRANSCRIPTION FACTOR;

EID: 77950687929     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.986     Document Type: Article

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