35763-22-5Relevant articles and documents
Synthesis and molecular docking of 1,2,3-triazole-based sulfonamides as aromatase inhibitors
Pingaew, Ratchanok,Prachayasittikul, Veda,Mandi, Prasit,Nantasenamat, Chanin,Prachayasittikul, Supaluk,Ruchirawat, Somsak,Prachayasittikul, Virapong
, p. 3472 - 3480 (2015/08/03)
Abstract A series of 1,4-disubstituted-1,2,3-triazoles (13-35) containing sulfonamide moiety were synthesized and evaluated for their aromatase inhibitory effects. Most triazoles with open-chain sulfonamide showed significant aromatase inhibitory activity
Synthesis and cytotoxicity of novel N-sulfonyl-1,2,3,4- tetrahydroisoquinoline thiosemicarbazone derivatives
Pingaew, Ratchanok,Prachayasittikul, Supaluk,Ruchirawat, Somsak,Prachayasittikul, Virapong
, p. 267 - 277 (2013/03/13)
The modified Pictet-Spengler reaction of phenylethylbenzene sulfonamide with a commercially available glyoxal to construct 1-benzoyl- and 1-acetyl-1,2,3,4-tetrahydroisoquinolines 9a-n has been reported. The reaction could be accomplished, regardless of th
Design, synthesis and early structure-activity relationship of farnesyltransferase inhibitors which mimic both the peptidic and the prenylic substrate
Schlitzer, Martin,Boehm, Markus,Sattler, Isabel,Dahse, Hans-Martin
, p. 1991 - 2006 (2007/10/03)
Inhibition of the farnesylation of ras proteins has been identified as a promising target in tumor therapy. Only a few farnesyltransferase inhibitors are bisubstrate analogues displaying features of both substrates, the farnesylpyrophosphate and the C-terminal CAAX-tetrapeptide sequence of the ras protein. These known bisubstrate analogues consist of an AAX-tripeptide and a farnesyl residue connected through various linkers. We have developed a class of novel compounds that mimic a bisubstrate inhibitor structure and that differ from the known ones by lacking peptidic or farnesylic substructures. Long chain fatty acids and aryl-substituted carboxylic acids were used as farnesyl surrogates. These structures were linked to isoleucine amide, benzoic acid amide, N-substituted aminobenzenesulfonamides and N(α)-aryl-substituted methionine derivatives, respectively, which function as AA- or AAX-mimetics. Copyright (C) 2000 Elsevier Science Ltd.
