Unique ligand selectivity of the GPR92/LPA5 lysophosphatidate receptor indicates role in human platelet activation

Journal of Biological Chemistry

Volumn 284, Issue 25, 2009, Pages 17304-17319

  Williams, Jesica R ^a   Khandoga, Anna L ^b   Goyal, Pankaj ^b   Fells, James I ^a   Perygin, Donna H ^a   Siess, Wolfgang ^b   Parrill, Abby L ^a   Tigyi, Gabor ^c   Fujiwara, Yuko ^c  

^a University of Memphis   (United States)

^b UNIVERSITY OF MUNICH   (Germany)

^c UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL DIFFERENTIATION; G PROTEIN COUPLED RECEPTORS; GENE FAMILIES; GENE RECEPTORS; GLYCEROL PHOSPHATE; IN-SILICO SCREENING; LIGAND RECOGNITION; LYSOPHOSPHATIDIC ACID; PHARMACOPHORE MODELS; PLATELET ACTIVATION; RANK ORDER; RECEPTOR ACTIVATION; SELECTIVE INHIBITION; SITE DIRECTED MUTAGENESIS; STRUCTURE-ACTIVITY RELATIONSHIPS;

BLOOD SUBSTITUTES; GLYCEROL; PHOSPHOLIPIDS; PLATELETS; SELF ASSEMBLY; SYNTHETIC APERTURES;

LIGANDS;

ALKYLGLYCEROL PHOSPHATE; ARACHIDONOYLGLYCINE; ARGININE; CYCLIC PHOSPHATIDIC ACID; FARNESYL DIPHOSPHATE; FARNESYL PHOSPHATE; GLYCINE; LIGAND; LYSOPHOSPHATIDIC ACID; LYSOPHOSPHATIDIC ACID 5; LYSOPHOSPHATIDIC ACID RECEPTOR; LYSOPHOSPHOLIPID RECEPTOR; OCTADECENYL PHOSPHATE; PHOSPHATE; PHOSPHATIDIC ACID; PROLINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CHEMICAL MUTAGENESIS; COMPUTER MODEL; CONTROLLED STUDY; HUMAN; HUMAN CELL; LIGAND BINDING; MOLECULAR RECOGNITION; NONHUMAN; PHARMACOPHORE; PRIORITY JOURNAL; PROTEIN INTERACTION; RECEPTOR GENE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; THROMBOCYTE ACTIVATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CALCIUM SIGNALING; HUMANS; LIGANDS; LYSOPHOSPHOLIPIDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLATELET ACTIVATION; RECEPTORS, LYSOPHOSPHATIDIC ACID; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 67650514340     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.003194     Document Type: Article

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