58794-09-5Relevant articles and documents
CEREBLON LIGANDS AND BIFUNCTIONAL COMPOUNDS COMPRISING THE SAME
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Paragraph 1054; 1055; 1056; 10567, (2018/08/20)
The description relates to cereblon E3 ligase binding compounds, including bifunctional compounds comprising the same, which find utility as modulators of targeted ubiquitination, especially inhibitors of a variety of polypeptides and other proteins which are degraded and/or otherwise inhibited by bifunctional compounds according to the present disclosure. In particular, the description provides compounds, which contain on one end a ligand which binds to the cereblon E3 ubiquitin ligase and on the other end a moiety which binds a target protein such that the target protein is placed in proximity to the ubiquitin ligase to effect degradation (and inhibition) of that protein. Compounds can be synthesized that exhibit a broad range of pharmacological activities consistent with the degradation/inhibition of targeted polypeptides of nearly any type.
ANGIOGENESIS INHIBITORS
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Page/Page column 68, (2010/11/05)
Compounds of Structural Formula I or pharmaceutically acceptable salts thereof, are effective inhibitors of angiogenesis:
Discovery of potent and practical antiangiogenic agents inspired by cortistatin A
Czako, Barbara,Kuerti, Laszlo,Mammoto, Akiko,Ingber, Donald E.,Corey
supporting information; experimental part, p. 9014 - 9019 (2009/12/04)
The discovery that cortistatins A and J show noteworthy antiangiogenic activity prompted an investigation of the possibility that simpler and much more easily made compounds based on a steroid core might have useful bioactivity. These studies have led to
3,5-Disubstituted quinolines as novel c-Jun N-terminal kinase inhibitors
Jiang, Rong,Duckett, Derek,Chen, Weiming,Habel, Jeff,Ling, Yuan Yuan,LoGrasso, Philip,Kamenecka, Theodore M.
, p. 6378 - 6382 (2008/09/16)
The structure-based design and synthesis of a novel series of c-Jun N-terminal kinase (JNK) inhibitors with selectivity against p38 is reported. The unique structure of 3,5-disubstituted quinolines (2) was developed from the previously reported 4-(2,7-phenanthrolin-9-yl)phenol (1). The X-ray crystal structure of 16a in JNK3 reveals an unexpected binding mode for this new scaffold with protein.