497819-05-3Relevant 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
Exploring the influence of indololactone structure on selectivity for binding to the C1 domains of PKCα, PKCε, and RasGRP
Elhalem, Eleonora,Donadío, Lucía Gandolfi,Zhou, Xiaoling,Lewin, Nancy E.,Garcia, Lia C.,Lai, Christopher C.,Kelley, James A.,Peach, Megan L.,Blumberg, Peter M.,Comin, María J.
, p. 2971 - 2980 (2017/05/29)
C1 domain-containing proteins, such as protein kinase C (PKC), have a central role in cellular signal transduction. Their involvement in many diseases, including cancer, cardiovascular disease, and immunological and neurological disorders has been extensi
Diacylglycerol lactones targeting the structural features that distinguish the atypical C1 domains of protein kinase C Ζ and ι from typical C1 domains
Pu, Yongmei,Kang, Ji-Hye,Sigano, Dina M.,Peach, Megan L.,Lewin, Nancy E.,Marquez, Victor E.,Blumberg, Peter M.
, p. 3835 - 3844 (2014/05/20)
To explore the feasibility of developing ligands targeted to the atypical C1 domains of protein kinase C Ζ and ι, we have prepared diacylglycerol lactones substituted with hydrophilic groups on their side chains, which potentially could interact with the
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,
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
