388622-16-0Relevant academic research and scientific papers
Design, Synthesis, and Characterization of Novel sn-1 Heterocyclic DAG-Lactones as PKC Activators
Elhalem, Eleonora,Bellomo, Ana,Cooke, Mariana,Scravaglieri, Antonella,Pearce, Larry V.,Peach, Megan L.,Gandolfi Donadío, Lucía,Kazanietz, Marcelo G.,Comin, María J.
, p. 11418 - 11431 (2021/08/03)
DAG-lactones represent useful templates for the design of potent and selective C1 domain ligands for PKC isozymes. The ester moiety at the sn-1 position, a common feature in this template, is relevant for C1 domain interactions, but it represents a labile
Conformationally constrained analogues of diacylglycerol (DAG). 28. DAG-dioxolanones reveal a new additional interaction site in the C1b domain of PKCδ
Choi, Yongseok,Pu, Yongmei,Peach, Megan L.,Kang, Ji-Hye,Lewin, Nancy E.,Sigano, Dina M.,Garfield, Susan H.,Blumberg, Peter M.,Marquez, Victor E.
, p. 3465 - 3481 (2008/02/09)
Diacylglycerol (DAG) lactones have provided a powerful platform for structural exploration of the interactions between ligands and the C1 domains of protein kinase C (PKC). In this study, we report that DAG-dioxolanones, novel derivatives of DAG-lactones,
Branched diacylglycerol-lactones as potent protein kinase C ligands and α-secretase activators
Lee, Jeewoo,Kang, Ji-Hye,Han, Kee-Chung,Kim, Yerim,Kim, Su Yeon,Youn, Hae-Suk,Mook-Jung, Inhee,Kim, Hee,Han, Jee Hye Lo,Ha, Hee Jin,Kim, Young Ho,Marquez, Victor E.,Lewin, Nancy E.,Pearce, Larry V.,Lundberg, Daniel J.,Blumberg, Peter M.
, p. 2028 - 2036 (2007/10/03)
Using as our lead structure a potent PKC ligand (1) that we had previously described, we investigated a series of branched DAG-lactones to optimize the scaffold for PKC binding affinity and reduced lipophilicity, and we examined the potential utility of s
Conformationally constrained analogues of diacylglycerol. 19. Synthesis and protein kinase C binding affinity of diacylglycerol lactones bearing an N-hydroxylamide side chain
Choi, Yongseok,Kang, Ji-Hye,Lewin, Nancy E.,Blumberg, Peter M.,Lee, Jeewoo,Marquez, Victor E.
, p. 2790 - 2793 (2007/10/03)
The structures of N-hydroxylamides la and lb, previously reported by Lee et al. in J. Med. Chem. 2001, 44, 4309-4312 as strong protein kinase C (PK-C) ligands, were incorrect and correspond instead to esters 2a and 2b, respectively. Here, we report the sy
