1380411-49-3Relevant academic research and scientific papers
Synthesis and biological evaluation of diaryl urea derivatives designed as potential anticarcinoma agents using de novo structure-based lead optimization approach
Azimian, Fereshteh,Dastmalchi, Siavoush,Hamzeh-Mivehroud, Maryam,Hemmati, Salar,Shahbazi Mojarrad, Javid
, (2020/07/13)
To develop inhibitors blocking VEGFR2 and the Raf/MEK/ERK mitogen-activated protein kinase signaling pathway new compounds based on sorafenib were designed, synthesized and biologically evaluated. Using de novo design method, a library of new ligands was
Antimetastatic effect of sulfamate carbonic anhydrase IX inhibitors in breast carcinoma xenografts
Gieling, Roben G.,Babur, Muhammad,Mamnani, Lupti,Burrows, Natalie,Telfer, Brian A.,Carta, Fabrizio,Winum, Jean-Yves,Scozzafava, Andrea,Supuran, Claudiu T.,Williams, Kaye J.
experimental part, p. 5591 - 5600 (2012/08/28)
A panel of compounds belonging to the underexposed sulfamate class of carbonic anhydrase (CA, EC 4.2.1.1) inhibitors was generated that displayed high specificity at nanomolar levels for the tumor-associated CA IX/XII isoforms. Three of the specific CA IX
Ureido-substituted sulfamates show potent carbonic anhydrase IX inhibitory and antiproliferative activities against breast cancer cell lines
Winum, Jean-Yves,Carta, Fabrizio,Ward, Carol,Mullen, Peter,Harrison, David,Langdon, Simon P.,Cecchi, Alessandro,Scozzafava, Andrea,Kunkler, Ian,Supuran, Claudiu T.
supporting information; experimental part, p. 4681 - 4685 (2012/07/31)
A series of 50 sulfamates were obtained by reacting 4-aminophenol with isocyanates followed by sulfamoylation. Most of the new compounds were nanomolar inhibitors of the tumor-associated carbonic anhydrase (CA, EC 4.2.1.1) isoforms IX and XII, whereas the
