147688-34-4Relevant academic research and scientific papers
Orthogonal regioselective synthesis of N-alkyl-3-substituted tetrahydroindazolones
Kim, Jonghoon,Song, Heebum,Park, Seung Bum
supporting information; experimental part, p. 3815 - 3822 (2010/09/10)
A divergent strategy for the regioselective and orthogonal synthesis of complementary regioisomers of N-alkyl-3-substituted-tetrahydroindazolones 3 and 4 was achieved from. Boc-protected alkylhydrazmes 1. The robustness and sub-strate generality of this method were validated by synthesizing 3 and. 4 through the intra- and intermolecular condensation of 1 with various 2-acylcyclohexane-l,3-diones 2 and aldehydes, respectively.
CHEMOKINE RECEPTOR MODULATORS
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Page/Page column 582, (2008/12/07)
The invention provides compounds of Formula (I) and pharmaceutical compositions comprising compounds of Formula (I). These compounds are useful treating or preventing HIV infections, and in treating proliferative disorders such as inhibiting the metastasis of various cancers.
Pyrazolones as inhibitors of 11B-hydroxysteroid dehydrogenase
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Page/Page column 25, (2008/06/13)
Provided herein are compounds of the formula (I): as well as pharmaceutically acceptable salts thereof, wherein the substituents are as those disclosed in the specification. These compounds, and the pharmaceutical compositions containing them, are useful for the treatment of diseases such as, for example, type II diabetes mellitus and metabolic syndrome.
Novel semicarbazide-derived inhibitors of human dipeptidyl peptidase I (hDPPI)
Bondebjerg, Jon,Fuglsang, Henrik,Valeur, Kirsten Rosendal,Kaznelson, Dorte Wissing,Hansen, Johnny Arnsdorf,Pedersen, Rene Orup,Krogh, Berit Olsen,Jensen, Bo Skaaning,Lauritzen, Conni,Petersen, Gitte,Pedersen, John,Naerum, Lars
, p. 4408 - 4424 (2007/10/03)
Human dipeptidyl peptidase I (hDPPI, cathepsin C, EC 3.4.14.1) is a novel putative drug target for the treatment of inflammatory diseases. Using 1 as a starting point (IC50 > 10 μM), we have improved potency by more than 500-fold and successfully identified novel inhibitors of DPPI via screening of a one-bead-two-compounds library of semicarbazide derivatives. Selected compounds were shown to inhibit intracellular DPPI in RBL-2H3 cells. These compounds were further characterized for adverse effects on HepG2 cells (cytotoxicity and viability) and their metabolic stability in rat liver microsomes was estimated. One of the most potent inhibitors, 8 (IC50 = 31 ± 3 nM; Ki = 45 ± 2 nM, competitive inhibition), is selective for DPPI over other cysteine and serine proteases, has a half-life of 24 min in rat liver microsomes, shows approximately 50% inhibition of intracellular DPPI at 20 μM and is noncytotoxic.
New Synthesis of 1,1-Substituted Hydrazines by Alkylation of N-Acyl- or N-alkyloxycarbonylaminophthalimide Using the Mitsunobu Protocol
Brosse, Nicolas,Pinto, Maria-Fatima,Jamart-Gregoire, Brigitte
, p. 4370 - 4374 (2007/10/03)
N-acyl- and N-alkoxycarbonylaminophthalimides are prepared using a convenient reaction and are efficiently used as acid partners in Mitsunobu reaction. This reaction allows them to be alkylated by primary, secondary or benzyl groups. Comparison of the reactivities and pKa values of these N-substituted aminophthalimides suggest that the success of the Mitsunobu reaction in this case seems to be governed more by steric than by electronic effects. A final dephthaloylation step results in an efficient method for the preparation of 1,1-substituted hydrazines.
N-tert-butoxycarbonylaminophthalimide, a versatile reagent for the conversion of alcohols into alkylated tert-butylcarbazates or hydrazines via the Mitsunobu protocol
Brosse, Nicolas,Pinto, Maria-Fatima,Jamart-Grégoire, Brigitte
, p. 205 - 207 (2007/10/03)
An efficient two-step method has been developed for the conversion of alcohols to substituted hydrazines. The use of N-tert- butoxycarbonylaminophthalimide as an acid partner in Mitsunobu reactions with a variety of alcohols permits the synthesis of the corresponding monoalkylated tert-butylcarbazates and hydrazines.
