175692-06-5Relevant articles and documents
ANTIBACTERIAL AGENT
-
Paragraph 0124, (2020/06/16)
PROBLEM TO BE SOLVED: To provide an antibacterial agent having antibacterial property on bacteria selected from a group consisting of Methylobacterium bacteria, Sphingomonas bacteria, and Escherichia coil. SOLUTION: There is provided an antibacterial agen
Access to variously substituted 5,6,7,8-tetrahydro-3H-quinazolin-4-ones via Diels-Alder adducts of phenyl vinyl sulfone to cyclobutene-annelated pyrimidinones
Dalai, Suryakanta,Belov, Vladimir N.,Nizamov, Shamil,Rauch, Karsten,Finsinger, Dirk,De Meijere, Armin
, p. 2753 - 2765 (2007/10/03)
Under basic conditions (Et3N, dioxane), the aromatic amidines 4 and also S-methylisothiourea 4g cleanly undergo Michael addition to methyl 2-chloro-2-cyclopropylideneacetate (5), followed by intramolecular nucleophilic substitution, cyclopropyl
TETRAHYDRO- AND DIHYDROQUINAZOLINONES
-
Page/Page column 62; 63; 74, (2010/11/23)
The present invention relates to the use of tetrahydro- and dihydroquinazolinones of formula (I) as protein kinase activators or inhibitors, a method for their manufacture, their use for the preparation of a medicament for the treatment of diseases, their
Syntheses and selective inhibitory activities of terphenyl-bisamidines for serine proteases
Von Der Saal, Wolfgang,Engh, Richard A.,Eichinger, Andreas,Gabriel, Bernhard,Kucznierz, Ralf,Sauer, Juergen
, p. 73 - 82 (2007/10/02)
Biphenyl nitriles 5a-c, terphenyl dinitriles 11a-d, and naphthalene-bis(benzonitrile) 11e were prepared by palladium-catalyzed cross coupling reactions and subsequently converted to biphenyl amidines 8a-c and bis(benzamidines) 4a-e. Among the biphenyl amidines 8 only the meta-derivative 8b inhibits factor Xa and trypsin (K(i) = 10 μM). The terphenyl bisamidine 4c does not inhibit factor Xa, trypsin, thrombin, and plasmin, while 4a and 4d are almost equipotent inhibitors of theses enzymes (K(i) 1-6 μM), and 4b and 4e are selective for trypsin (K(i) = 0.2 and 0.3 μM; but K(i) > 1 μM for factor Xa, thrombin, and plasmin). X-ray analysis of crystals of 4b complexed with bovine trypsin revealed a unique binding mode: one benzamidino group binds in the S1 site to the side chain carboxylate of Arg 189. The central phenyl group is twisted away from the S2/S3 sites and the second amidino group contacts the Asn 143 side chain.