67688-28-2Relevant academic research and scientific papers
Optimization of TRPV6 calcium channel inhibitors using a 3D ligand-based virtual screening method
Simonin, Céline,Awale, Mahendra,Brand, Michael,Van Deursen, Ruud,Schwartz, Julian,Fine, Michael,Kovacs, Gergely,H?fliger, Pascal,Gyimesi, Gergely,Sithampari, Abilashan,Charles, Roch-Philippe,Hediger, Matthias A.,Reymond, Jean-Louis
supporting information, p. 14748 - 14752 (2016/02/05)
Herein, we report the discovery of the first potent and selective inhibitor of TRPV6, a calcium channel overexpressed in breast and prostate cancer, and its use to test the effect of blocking TRPV6-mediated Ca2+-influx on cell growth. The inhib
New methylene homologation method for cyclic ketones
Liu, Huaqing,Sun, Chunrui,Lee, Nam-Kyu,Henry, Roger F.,Lee, Daesung
supporting information, p. 11889 - 11893 (2012/10/29)
Teaching new tricks to an old dog: By intercepting adducts between ketones and lithium trimethylsilyldiazomethane, a new Tiffeneau-Demjanov type methylene homologation could be realized in a single-step operation. Among proton sources and Lewis acids, silica gel was found to be the most effective reagent for the protonation of intermediates and their subsequent ring expansion (see scheme). Copyright
Side Chain Hydroxylation of Aromatic Compounds by Fungi. Part 5. Exploring the Benzylic Hydroxylase of Mortierella isabellina
Holland, Herbert L.,Kindermann, Maik,Kumaresan, Sudalaiyandi,Stefanac, Tomislav
, p. 1353 - 1364 (2007/10/02)
The active site topography of the hydroxylase enzyme of Mortierella isabellina ATCC 42613, which carries out the benzylic hydroxylation of toluene, ethylbenzene, and related compounds, has been explored.Operating in a whole cell biotransformation mode, this enzyme shows selectivity in substrate processing based on the nature, position and size of substituent side chains close to the site of hydroxylation.The results of determination of the yield and stereochemistry of hydroxylation of over twenty substrates and potential substrates, together with previously reported data, have been used to propose an active site model for the benzylic hydroxylase enzyme.
