14228-23-0Relevant articles and documents
Synthesis, structure evaluation, spectroscopic and antibacterial investigation of metal complexes with 2-(pyridin-4-yl)quinoline-4-carboxylic acid
Zhang, Long,Man, Zhong-Wei,Zhang, Yan,Hong, Jing,Guo, Meng-Ran,Qin, Jie
, p. 891 - 898 (2016/12/18)
Four metal complexes based on quinoline carboxylate ligand from 2-(pyridin-4-yl)quinoline-4-carboxylic acid (HL), {[ML2(H2O)2]·2H2O}n (M = MnII, 1; M = CoII, 2; M = CdII, 3) and {[Ag2L2(H2O)2]·3H2O}n (4) have been synthesized under hydrothermal conditions. Their structures were determined by elemental analyses, IR spectra, and further characterized by single-crystal X-ray diffraction analysis. Complexes 1-3 feature a 1D chain structure which is further linked together to construct the 3D supramolecular network through hydrogen bonds. Complex 4 exhibits a 3D configuration. The fluorescent behavior and antibacterial activities of these compounds have been investigated.
Design of small molecule inhibitors of acetyl-CoA carboxylase 1 and 2 showing reduction of hepatic malonyl-CoA levels in vivo in obese Zucker rats
Bengtsson, Christoffer,Blaho, Stefan,Saitton, David Blomberg,Brickmann, Kay,Broddefalk, Johan,Davidsson, ?jvind,Drmota, Tomas,Folmer, Rutger,Hallberg, Kenth,Hallén, Stefan,Hovland, Ragnar,Isin, Emre,Johannesson, Petra,Kull, Bengt,Larsson, Lars-Olof,L?fgren, Lars,Nilsson, Kristina E.,Noeske, Tobias,Oakes, Nick,Plowright, Alleyn T.,Schnecke, Volker,Sthlberg, Pernilla,S?rme, Pernilla,Wan, Hong,Wellner, Eric,?ster, Linda
experimental part, p. 3039 - 3053 (2011/06/27)
Inhibition of acetyl-CoA carboxylases has the potential for modulating long chain fatty acid biosynthesis and mitochondrial fatty acid oxidation. Hybridization of weak inhibitors of ACC2 provided a novel, moderately potent but lipophilic series. Optimization led to compounds 33 and 37, which exhibit potent inhibition of human ACC2, 10-fold selectivity over inhibition of human ACC1, good physical and in vitro ADME properties and good bioavailability. X-ray crystallography has shown this series binding in the CT-domain of ACC2 and revealed two key hydrogen bonding interactions. Both 33 and 37 lower levels of hepatic malonyl-CoA in vivo in obese Zucker rats.
NEW ACETYL COENZYME A CARBOXYLASE (ACC) INHIBITORS AND USES IN TREATMENTS OF OBESITY AND DIABETES MELLITUS - 087
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Page/Page column 220, (2009/07/25)
The present invention relates to Acetyl Coenzyme A Carboxylase (ACC) inhibitors according to formula (I), or an enantiomer thereof, or a pharmaceutically acceptable salt thereof, where R1, R2, R3, R4, R5, E, L, Z and n are as defined herein, to processes for preparing such compounds, to pharmaceutical compositions containing them, to the use of such inhibitors and to methods for th eir therapeutic use, particularly in the treatments of obesity and diabetes mellitus.