PMID

Data

Article Title

Organization

Binding mode prediction of aplysiatoxin, a potent agonist of protein kinase C, through molecular simulation and structure-activity study on simplified analogs of the receptor-recognition domain.

Ehime University

Diacylglycerol lactones targeting the structural features that distinguish the atypical C1 domains of protein kinase C¿ and¿ from typical C1 domains.

National Cancer Institute-Bethesda

Structural basis of binding of high-affinity ligands to protein kinase C: prediction of the binding modes through a new molecular dynamics method and evaluation by site-directed mutagenesis.

Georgetown University Medical Center

Conformationally constrained analogues of diacylglycerol (DAG). 28. DAG-dioxolanones reveal a new additional interaction site in the C1b domain of PKC delta.

National Cancer Institute-Frederick

New bivalent PKC ligands linked by a carbon spacer: enhancement in binding affinity.

Georgetown University Medical Center

Synthesis and biological activities of simplified aplysiatoxin analogs focused on the CH/? interaction.

Kyoto University

Structural basis of RasGRP binding to high-affinity PKC ligands.

Georgetown University Medical Center

Probing the binding of indolactam-V to protein kinase C through site-directed mutagenesis and computational docking simulations.

Georgetown University Medical Center