1093211-85-8Relevant articles and documents
Preclinical Characterization of the FAAH Inhibitor JNJ-42165279
Keith, John M.,Jones, William M.,Tichenor, Mark,Liu, Jing,Seierstad, Mark,Palmer, James A.,Webb, Michael,Karbarz, Mark,Scott, Brian P.,Wilson, Sandy J.,Luo, Lin,Wennerholm, Michelle L.,Chang, Leon,Rizzolio, Michele,Rynberg, Raymond,Chaplan, Sandra R.,Breitenbucher, J. Guy
, p. 1204 - 1208 (2015)
The pre-clinical characterization of the aryl piperazinyl urea inhibitor of fatty acid amide hydrolase (FAAH) JNJ-42165279 is described. JNJ-42165279 covalently inactivates the FAAH enzyme, but is highly selective with regard to other enzymes, ion channel
Reductive amination by continuous-flow hydrogenation: Direct and scalable synthesis of a benzylpiperazine
Liu, Jing,Fitzgerald, Anne E.,Mani, Neelakandha S.
, p. 2469 - 2473 (2012/09/08)
A benzylpiperazine was prepared directly from the corresponding benzaldehyde and piperazine on a continuous-flow hydrogenation apparatus. The synthesis was protecting group free, safe, and environmentally friendly. Large-scale synthesis under flow hydrogenation conditions was also demonstrated. Georg Thieme Verlag Stuttgart · New York.
HETEROARYL-SUBSTITUTED UREA MODULATORS OF FATTY ACID AMIDE HYDROLASE
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Page/Page column 33, (2009/01/24)
Certain heteroaryl-substituted piperidinyl and piperazinyl urea compounds are described, which are useful as FAAH inhibitors. Such compounds may be used in pharmaceutical compositions and methods for the treatment of disease states, disorders, and conditi