Title : Conformationally constrained analogues of diacylglycerol (DAG). 23. Hydrophobic ligand-protein interactions versus ligand-lipid interactions of DAG-lactones with protein kinase C (PK-C).

Pub. Date : 2004 Sep 23

PMID : 15369389






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Hydrophobic ligand-protein interactions versus ligand-lipid interactions of DAG-lactones with protein kinase C (PK-C). Diglycerides proline rich transmembrane protein 2 Homo sapiens
2 Hydrophobic ligand-protein interactions versus ligand-lipid interactions of DAG-lactones with protein kinase C (PK-C). Diglycerides proline rich transmembrane protein 2 Homo sapiens
3 The constrained glycerol backbone of DAG-lactones, when combined with highly branched alkyl chains, has engendered a series of DAG-lactone ligands capable of binding protein kinase C (PK-C) with affinities that approximate those of phorbol esters. Diglycerides proline rich transmembrane protein 2 Homo sapiens
4 The constrained glycerol backbone of DAG-lactones, when combined with highly branched alkyl chains, has engendered a series of DAG-lactone ligands capable of binding protein kinase C (PK-C) with affinities that approximate those of phorbol esters. Diglycerides proline rich transmembrane protein 2 Homo sapiens