- Synthesis and in vitro evaluation of a selective antagonist and the corresponding radioligand for the prostaglandin D2 receptor CRTH2
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Synthesis and preliminary in vitro biological evaluation of a selective high-affinity CRTH2 antagonist is described. The stability of an N-benzyl group facilitated synthesis of the corresponding radioligand by tritiation of a brominated precursor. The com
- Ulven, Trond,Gallen, Michael J.,Nielsen, Mads C.,Merten, Nicole,Schmidt, Carola,Mohr, Klaus,Traenkle, Christian,Kostenis, Evi
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- Diastereoselective tricyclization/dimerization of yne-indoles catalyzed by a Au(III) complex featuring an L2/Z-type ligand
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In order to investigate catalyst activation via a (Au → B)8 interaction, Au(DPB)X3 (DPB = diphosphine-borane) featuring an L2/Z ligand was synthesized. The resulting cationic catalyst was utilized for the unprecedented diastereoselective tricyclization/dimerization of yne-indoles.
- Murakami, Ryo,Tanishima, Hiroto,Naito, Daisuke,Kawamitsu, Hikari,Kamo, Ryoya,Uchida, Ayaka,Kawasaki, Kazuki,Kiyohara, Chihiro,Matsuo, Motoki,Maeda, Kakeru,Inagaki, Fuyuhiko
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supporting information
(2021/07/28)
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- Synthesis, molecular docking, and QSAR study of sulfonamide-based indoles as aromatase inhibitors
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Thirty four of indoles bearing sulfonamides (11–44) were synthesized and evaluated for their anti-aromatase activities. Interestingly, all indole derivatives inhibited the aromatase with IC50 range of 0.7–15.3 μM. Indoles (27–36) exerted higher aromatase inhibitory activity than that of ketoconazole. The phenoxy analogs 28 and 34 with methoxy group were shown to be the most potent compounds with sub-micromolar IC50 values (i.e., 0.7 and 0.8 μM, respectively) without affecting to the normal cell line. Molecular docking demonstrated that the indoles 28, 30 and 34 could occupy the same binding site on the aromatase pocket and share several binding residues with those of the natural substrate (androstenedione), which suggested the competitive binding could be the mode of inhibition of the compounds. The most potent analog 28 could mimic H-bond interactions of the natural androstenedione with MET374 and ASP309 residues on the aromatase. QSAR model also revealed that the para-phenoxy indole (28) affords the higher value of electronegativity descriptor MATS6e as well as the higher inhibitory activity compared with that of the ortho-phenoxy compound (34). The study highlighted a series of promising indoles to be potentially developed as novel aromatase inhibitors for therapeutics.
- Pingaew, Ratchanok,Mandi, Prasit,Prachayasittikul, Veda,Prachayasittikul, Supaluk,Ruchirawat, Somsak,Prachayasittikul, Virapong
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p. 1604 - 1615
(2017/11/17)
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- Oxidative Fragmentations and Skeletal Rearrangements of Oxindole Derivatives
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An oxidative sequence for the conversion of oxindoles to structurally distinct heterocyclic scaffolds and aniline derivatives is disclosed by the combination of a copper-catalyzed C-H peroxidation and subsequent base-mediated fragmentation reaction. In contrast to classic enzymatic (i.e., kynurenine pathway) and biomimetic methods (i.e., Witkop-Winterfeldt oxidation) for oxidative indole cleavage, this protocol allows for the incorporation of external nucleophiles. The new transformation displays broad functional group tolerance and is applicable to tryptophan derivatives, opening potential new avenues for postsynthetic modification of polypeptides, bioconjugation, and unnatural amino acid synthesis.
- Klare, Hendrik F. T.,Goldberg, Alexander F. G.,Duquette, Douglas C.,Stoltz, Brian M.
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supporting information
p. 988 - 991
(2017/03/14)
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- Inhibitors of 15-lipoxygenase
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The present invention provides inhibitors of 15-LO according to Formula I, pharmaceutical compositions containing such inhibitors and methods for treating diseases related to the 15-LO cascade using such compounds and compositions.
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Page/Page column 9
(2008/06/13)
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