89840-80-2Relevant articles and documents
Potent and selective N-(4-sulfamoylphenyl)thiourea-based GPR55 agonists
Yrj?l?, Sari,Parkkari, Teija,Navia-Paldanius, Dina,Laitinen, Tuomo,Kaczor, Agnieszka A.,Kokkola, Tarja,Adusei-Mensah, Frank,Savinainen, Juha R.,Laitinen, Jarmo T.,Poso, Antti,Alexander, Amy,Penman, June,Stott, Lisa,Anskat, Marie,Irving, Andrew J.,Nevalainen, Tapio J.
, p. 119 - 132 (2015/11/24)
To date, many known G protein-coupled receptor 55 (GPR55) ligands are those identified among the cannabinoids. In order to further study the function of GPR55, new potent and selective ligands are needed. In this study, we utilized the screening results from PubChem bioassay AID 1961 which reports the results of Image-based HTS for Selective Agonists of GPR55. Three compounds, CID1792579, CID1252842 and CID1011163, were further evaluated and used as a starting point to create a series of nanomolar potency GPR55 agonists with N-(4-sulfamoylphenyl)thiourea scaffold. The GPR55 activity of the compounds were screened by using a commercial β-arrestin PathHunter assay and the potential compounds were further evaluated by using a recombinant HEK cell line exhibiting GPR55-mediated effects on calcium signalling. The designed compounds were not active when tested against various endocannabinoid targets (CB1R, CB2R, FAAH, MGL, ABHD6 and ABHD12), indicating compounds' selectivity for the GPR55. Finally, structure-activity relationships of these compounds were explored.
PROCESS FOR THE PREPARATION OF SULFONAMIDES USEFUL AS RETROVIRAL PROTEASE INHIBITORS
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Page/Page column 20, (2013/03/26)
The present invention relates to a process for the preparation of sulfonamides useful as retroviral protease inhibitors.
Discovery of CGS 27023A, a non, peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits
MacPherson, Lawrence J.,Bayburt, Erol K.,Capparelli, Michael P.,Carroll, Brian J.,Goldstein, Robert,Justice, Michael R.,Zhu, Lijuan,Hu, Shou-Ih,Melton, Richard A.,Fryer, Lynn,Goldberg, Ron L.,Doughty, John R.,Spirito, Salvatore,Blancuzzi, Vincent,Wilson, Doug,O'Byrne, Elizabeth M.,Ganu, Vishwas,Parker, David T.
, p. 2525 - 2532 (2007/10/03)
Structure-activity relationships of a lead hydroxamic acid inhibitor of recombinant human stromelysin were systematically defined by taking advantage of a concise synthesis that allowed diverse functionality to be explored at each position in a template. An ex vivo rat model and an in vivo rabbit model of stromelysin-induced cartilage degradation were used to further optimize these analogs for oral activity and duration of action. The culmination of these modifications resulted in CGS 27023A, a potent, orally active stromelysin inhibitor that blocks the erosion of cartilage matrix.