1135344-52-3Relevant academic research and scientific papers
Crystal transformation in Mn(ii) metal-organic frameworks based on a one-dimensional chain precursor
Fan, Yong,Gong, Yiran,Jiang, Yansong,Liu, Rui,Wang, Li,Xu, Jianing
, p. 9540 - 9546 (2021)
The solvothermal reaction of Mn(ii) salts and 5-((4′-(tetrazol-5′′-yl)benzyl)oxy)isophthalic acid (H3L) affords an Mn(ii) based coordination polymer Mn(H2L)2(H2O)2(1), which possesses a one-dimensiona
A two-dimensional manganese coordination polymer: Crystal structure, proton conductivity and catalytic property
Cao, Yexia,Li, Huiqing,Yin, Aiping
, (2021/10/22)
Herein, we report a new Manganese coordination polymer, Mn3L2(H2O)4·2H2O (1), based on the 4′-(1-H-tetrazol-5-yl)-[1,1′-biphenyl]-3,5-dicarboxylic acid (H3L) ligand under solvothermal condi
Manganese-organic framework assembled by 5-((4′-(tetrazol-5″-yl)benzyl)oxy)isophthalic acid: A solvent-free catalyst for the formation of carbon–carbon bond
Jiang, Yansong,Xu, Jianing,Zhu, Ziqian,Jiang, Changwei,Ma, Lin,Wang, Hui,Wang, Li,Fan, Yong
supporting information, (2020/05/25)
A new three-dimensional manganese-based metal–organic framework Mn4L2(HL)(H2O)5, (1), based on semi-rigid 5-((4′-(tetrazol-5′’-yl)benzyl)oxy)isophthalic acid ligand (H3L) have been prepared and charac
Discovery of the First in Vivo Active Inhibitors of the Soluble Epoxide Hydrolase Phosphatase Domain
Kramer, Jan S.,Woltersdorf, Stefano,Duflot, Thomas,Hiesinger, Kerstin,Lillich, Felix F.,Kn?ll, Felix,Wittmann, Sandra K.,Klingler, Franca-M.,Brunst, Steffen,Chaikuad, Apirat,Morisseau, Christophe,Hammock, Bruce D.,Buccellati, Carola,Sala, Angelo,Rovati, G. Enrico,Leuillier, Matthieu,Fraineau, Sylvain,Rondeaux, Julie,Hernandez-Olmos, Victor,Heering, Jan,Merk, Daniel,Pogoryelov, Denys,Steinhilber, Dieter,Knapp, Stefan,Bellien, Jeremy,Proschak, Ewgenij
, p. 8443 - 8460 (2019/10/16)
The emerging pharmacological target soluble epoxide hydrolase (sEH) is a bifunctional enzyme exhibiting two different catalytic activities that are located in two distinct domains. Although the physiological role of the C-terminal hydrolase domain is well-investigated, little is known about its phosphatase activity, located in the N-terminal phosphatase domain of sEH (sEH-P). Herein we report the discovery and optimization of the first inhibitor of human and rat sEH-P that is applicable in vivo. X-ray structure analysis of the sEH phosphatase domain complexed with an inhibitor provides insights in the molecular basis of small-molecule sEH-P inhibition and helps to rationalize the structure-activity relationships. 4-(4-(3,4-Dichlorophenyl)-5-phenyloxazol-2-yl)butanoic acid (22b, SWE101) has an excellent pharmacokinetic and pharmacodynamic profile in rats and enables the investigation of the physiological and pathophysiological role of sEH-P in vivo.
A tricyclic aluminum alkoxide catalyst for aldehyde trimethylsilylcyanation
Raders, Steven M.,Verkade, John G.
supporting information; experimental part, p. 5317 - 5321 (2009/12/06)
Trimethylsilylcyanation of aldehydes is efficiently accomplished with a low concentration of catalyst 1 under mild conditions in acetonitrile. This protocol tolerates a variety of electron-rich, neutral, and deficient aryl, heterocyclic, and alkyl aldehyd
