Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin αIIbβ 3 in native platelets than in liposomes

Journal of the American Chemical Society

Volumn 127, Issue 3, 2005, Pages 916-919

  Claasen, Birgit ^a   Axmann, Marco ^a   Meinecke, Robert ^a,b   Meyer, Bernd ^a  

^a UNIVERSITY OF HAMBURG   (Germany)

^b B Ingelheim Pharma GmbH/CO KG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; BLOOD; CELLS; CHEMICAL BONDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

LIPOSOMES; NATURAL MEMBRANES; RECEPTOR-LIGAND INTERACTIONS; SATURATION TRANSFER DOUBLE DIFFERENCE (STDD);

PROTEINS;

ARGININE; CELL SURFACE PROTEIN; CYCLOPEPTIDE; EPITOPE; G PROTEIN COUPLED RECEPTOR; GLYCINE; GLYCOPROTEIN; INTEGRIN; INTEGRIN ALPHA2BBETA3; LIPOSOME; MEMBRANE PROTEIN; PENTAPEPTIDE; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; HUMAN; HUMAN CELL; LIGAND BINDING; MAMMAL; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; SATURATION TRANSFER DOUBLE DIFFERENCE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; THROMBOCYTE;

BLOOD PLATELETS; EPITOPE MAPPING; EPITOPES; HUMANS; LIGANDS; LIPOSOMES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES, CYCLIC; PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX;

EID: 12444289530     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja044434w     Document Type: Article

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