497819-04-2Relevant academic research and scientific papers
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)
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
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
