228410-36-4Relevant academic research and scientific papers
Orally bioavailable factor Xa inhibitors containing alpha-substituted gem-dimethyl P4 moieties
Orwat, Michael J.,Qiao, Jennifer X.,He, Kan,Rendina, Alan R.,Luettgen, Joseph M.,Rossi, Karen A.,Xin, Baomin,Knabb, Robert M.,Wexler, Ruth R.,Lam, Patrick Y.S.,Pinto, Donald J.P.
, p. 3341 - 3345 (2014/07/22)
In an effort to identify a potential back-up to apixaban (Eliquis), we explored a series of diversified P4 moieties. Several analogs with substituted gem-dimethyl moieties replacing the terminal lactam of apixaban were identified which demonstrated potent
COMPOUNDS USEFUL AS PHOSPHOTYROSINE MIMICS
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Page 15, (2010/02/07)
New uses are disclosed for compositions containing compounds of formula (I) wherein A, B, C, G, Q and R are defined herein. The compositions inhibit the binding of tyrosine kinase-dependent regulatory proteins to their native phosphotyrosine-containing li
1,1-DISUBSTITUTED CYCLOALKYL DERIVATIVES AS FACTOR XA INHIBITORS
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Page 367-368, (2010/02/05)
The present application describes 1,1-disubstituted cycloalkyl compounds and derivatives thereof, or pharmaceutically acceptable salt forms thereof, which are useful as inhibitors of factor Xa.
Nonpeptidic, monocharged, cell permeable ligands for the p56lck SH2 domain
Proudfoot,Betageri,Cardozo,Gilmore,Glynn,Hickey,Jakes,Kabcenell,Kirrane,Tibolla,Lukas,Patel,Sharma,Yazdanian,Moss,Beaulieu,Cameron,Ferland,Gauthier,Gillard,Gorys,Poirier,Rancourt,Wernic,Montse
, p. 2421 - 2431 (2007/10/03)
p56lck is a member of the src family of tyrosine kinases and plays a critical role in the signal transduction events that lead to T cell activation. Ligands for the p56lck SH2 domain have the potential to disrupt the interaction of p56lck with its substra
Compounds useful as phosphotyrosine mimics
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, (2008/06/13)
Disclosed are compositions containing compounds of the formula (I) below wherein A,B,C,G,Q and R are defined herein. The compounds are useful as phosphotyrosine mimics that, when incorporated into an appropriate molecular structure, inhibit the binding of
