59484-42-3Relevant articles and documents
Bromination of α-Diazo Phenylacetate Derivatives Using Cobalt(II) Bromide
Wang, Haifeng,Sun, Xiangli,Hu, Manman,Zhang, Xiaoyi,Xie, Lele,Gu, Shuangxi
supporting information, p. 3347 - 3351 (2020/07/04)
A method for the bromination of α-diazo phenylacetate derivatives using cobalt(II) bromide is described. This bromination reaction features a short reaction time, broad substrate scope, operational simplicity, acid-free conditions, and gram-scalability. (Figure presented.).
Easily assembled, modular N,O-chelating ligands for Ta(V) complexation: A comparative study of ligand effects in hydroaminoalkylation with N-methylaniline and 4-methoxy-N-methylaniline
Garcia, Pierre,Payne, Philippa R.,Chong, Eugene,Webster, Ruth L.,Barron, Benedict J.,Behrle, Andrew C.,Schmidt, Joseph A.R.,Schafer, Laurel L.
, p. 5737 - 5743 (2013/07/11)
The influence of structurally related N,O-chelating ligands with additional heteroatoms (N, O, P, S) on the reactivity of in situ generated tantalum complexes for the hydroaminoalkylation of amines has been explored. Reactivity was probed by evaluating the catalytic ability of these N,O-chelating systems with N-methylaniline and 4-methoxy-N-methylaniline substrates. Enhanced reactivity is observed with amide proligands bearing an ortho-methoxyphenyl group on the nitrogen. 4-Methoxy-N-methylaniline is found to be more prone to undergo C-H functionalization via hydroaminoalkylation than N-methylaniline. The use of the related substrate 2-methoxy-N-methylaniline is not tolerated, and instead C(sp3)-O bond cleavage was observed.
4-Hydroxythiazole Inhibitors of 5-Lipoxygenase
Kerdesky, Francis A. J.,Holms, James H.,Moore, Jimmie L.,Bell, Randy L.,Dyer, Richard D.,et al.
, p. 2158 - 2165 (2007/10/02)
4-Hydroxythiazoles have been identified as potent inhibitors of 5-lipoxygenase in vitro exhibiting IC50's of less than 1 μM.An investigation of structure-activity relationships showed that the most potent inhibitors of this series are the 5-phenyl derivatives.The corresponding thiazolidin-4-one analogues were found to be relatively inactive.The 4-hydroxythiazoles were active inhibitors against 5-lipoxygenase in both intact rat polymorphonuclear leukocytes and human whole blood.The compounds were also selective inhibitors of 5-lipoxygenase, displaying only weak activity against other related enzymes, cyclooxygenase and 12- and 15-lipoxygenase.