6951-34-4Relevant academic research and scientific papers
Mammalian metabolism of phencyclidine
Baker,Wohlford,Bradbury,Wirth
, p. 666 - 669 (1981)
In dogs, the major metabolite of phencyclidine was found to be 5-[N-(1'-phenylcyclohexyl) amino]pentanoic acid (1). The γ-aminobutyric acid like metabolite was also pharmacologically evaluated to determine if the purported GABA-ergic mediated effects of p
Templated assembly of medium cyclic ethers: Via exo-trig nucleophilic cyclization of cyclopropenes
Alnasleh, Bassam K.,Rubina, Marina,Rubin, Michael
supporting information, p. 7494 - 7496 (2016/06/14)
A novel method for the assembly of medium heterocycles via an intramolecular nucleophilic addition to cyclopropenes generated in situ from the corresponding bromocyclopropanes is described. The exo-trig nucleophilic cyclizations were shown to proceed very
Indirect monoalkylation of primary and secondary amines by reductive decyanation of α-aminonitriles with sodium cyanoborohydride-mercury bis(trifluoroacetate)
Sassaman, Mark B.
, p. 10835 - 10840 (2007/10/03)
Secondary and tertiary amines are prepared from α-aminonitriles by selective reductive cleavage of the cyanide moiety. The α-aminonitriles in this case, function as 'masked' imine or iminium ions and are 'unmasked' by mercury(II) in the presence of sodium cyanoborohydride to obtain the reduced product. Secondary amines may be prepared indirectly from primary amines in good yield without danger of over alkylation.
Inhibitors of Cyclic AMP Phosphodiesterase. 2. Structural Variations of N-Cyclohexyl-N-methyl-4-quinazolin-7-yl)oxy>butyramide (RS-82856)
Venuti, Michael C.,Jones, Gordon H.,Alvarez, Robert,Bruno, John J.
, p. 303 - 318 (2007/10/02)
A series of analogues of the cyclic AMP phosphodiesterase (PDE) inhibitor N-cyclohexyl-N-methyl-4-quinazolin-7-yl)oxy>butyramide (RS-82856, 1) was prepared by systematic variation of the side-chain substituent, length, position, connecting atom, and the parent heterocycle itself.The compounds were evaluated as inhibitors of cyclic AMP phosphodiesterase from both human platelets and rat or dog heart tissue and as inhibitors of ADP-induced platelet aggregation.Structure-activity correlations for the analogue series revealed significant limitations on the steric bulk of substituents on the 1,2,3,5-tetrahydroimidazoquinaazolin-2-one heterocycle and the position and length of the side-chain.As inhibitors of cyclic AMP phosphodiesterase (PDE), potency steadily increased with increasingly lipophilic side chains.In platelet aggregation inhibition studies, however, a maximum in activity was reached with 1, while more lipophilic compounds were significantly less active.Major changes in the heterocycle itself, represented by isomeric and other carbonyl variations, also decreased activity.The molecular features defined by this series of analogues of 1 correlate to a high degree with current understanding of thr chemical and topographical requirements of the active site of the FIII (type IV) form of cyclic AMP PDE.Selective inhibition of this enzyme has been proposed as the principal component of the positive inotropic action of a number of cardiotonic agents.
