31420-66-3Relevant articles and documents
USE OF T-TYPE CALCIUM CHANNEL BLOCKER FOR TREATING PRURITUS
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Paragraph 0186-0188; 0228-0230, (2022/02/19)
A medicament for treating or preventing pruritus is provided. For the medicament for treating or preventing pruritus, a compound having a blocking action on Cav3.2T-type calcium channels represented by General Formulas (I) to (VI), a tautomer of the compo
Cyclopropane-1,2-dicarboxylic acids as new tools for the biophysical investigation of O-acetylserine sulfhydrylases by fluorimetric methods and saturation transfer difference (STD) NMR
Annunziato, Giannamaria,Pieroni, Marco,Benoni, Roberto,Campanini, Barbara,Pertinhez, Thelma A.,Pecchini, Chiara,Bruno, Agostino,Magalh?es, Joana,Bettati, Stefano,Franko, Nina,Mozzarelli, Andrea,Costantino, Gabriele
, p. 78 - 87 (2016/12/23)
Cysteine is a building block for many biomolecules that are crucial for living organisms. O-Acetylserine sulfhydrylase (OASS), present in bacteria and plants but absent in mammals, catalyzes the last step of cysteine biosynthesis. This enzyme has been dee
Conformationally restrained carbamoylcholine homologues. Synthesis, pharmacology at neuronal nicotinic acetylcholine receptors and biostructural considerations
De La Fuente Revenga, Mario,Balle, Thomas,Jensen, Anders A.,Fr?lund, Bente
, p. 352 - 362 (2015/09/01)
Exploration of small selective ligands for the nicotinic acetylcholine receptors (nAChRs) based on acetylcholine (ACh) has led to the development of potent agonists with clear preference for the α4β2 nAChR, the most prevalent nAChR subtype in the central nervous system. In this work we present the continuation of these efforts aimed at increasing this subtype selectivity by introduction of conformational restriction in the carbamoylcholine homologue, 3-(dimethylaminobutyl) dimethylcarbamate (DMABC). Our results highlight the importance of the N-carbamoyl substitution in α4β2-subtype selectivity. Moreover, we have confirmed the non-linear conformation of DMABC bound to nAChRs suggested by recent crystal structures of the compound in complex with the Lymnaea stagnalis ACh binding protein.