92611-10-4Relevant articles and documents
Switching Lysophosphatidylserine G Protein-Coupled Receptor Agonists to Antagonists by Acylation of the Hydrophilic Serine Amine
Sayama, Misa,Uwamizu, Akiharu,Ikubo, Masaya,Chen, Luying,Yan, Ge,Otani, Yuko,Inoue, Asuka,Aoki, Junken,Ohwada, Tomohiko
, p. 10059 - 10101 (2021/07/28)
Three human G protein-coupled receptors (GPCRs)—GPR34/LPS1, P2Y10/LPS2, and GPR174/LPS3—are activated specifically by lysophosphatidylserine (LysoPS), an endogenous hydrolysis product of a cell membrane component, phosphatidylserine (PS). LysoPS consists of-serine, glycerol, and fatty acid moieties connected by phosphodiester and ester linkages. We previously generated potent and selective GPCR agonists by modification of the three modules and the ester linkage. Here, we show that a novel modification of the hydrophilic serine moiety, that is, N-acylations of the serine amine, converted a GPR174 agonist to potent GPR174 antagonists. Structural exploration of the amide functionality provided access to a range of activities from agonist to partial agonist to antagonist. The present study would provide a new strategy for the development of lysophospholipid receptor antagonists.
CYCLIC NUCLEOTIDE ANALOGS
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Page/Page column 58-59, (2012/07/13)
Disclosed herein are cyclic nucleotide analogs, methods of synthesizing cyclic nucleotide analogs and methods of treating diseases and/or conditions such as viral infections, cancer, and/or parasitic diseases with cyclic nucleotide analogs.
A chemical model for the enzymatic mono de-alkylation of (methyl and ethyl) parathion by glutathione-S-transferase
Maturano, Marie Dolores,Bongibault, Véronique,Willson, Michèle,Klaébé, Alain,Fournier, Didier
, p. 17241 - 17246 (2007/10/03)
The NMR study of the reaction of methylparathion with thiol (glutathione) and a tertiary amine shows unambiguously a sequential transfer of the methyl group firstly to the amine and secondly to the thiol. The reaction stops after a single demethylation. This observation may account for regiospecificity of some glutathione S-transferases.