1225280-80-7Relevant academic research and scientific papers
The structure-activity relationships of L3MBTL3 inhibitors: Flexibility of the dimer interface
Camerino, Michelle A.,Zhong, Nan,Dong, Aiping,Dickson, Bradley M.,James, Lindsey I.,Baughman, Brandi M.,Norris, Jacqueline L.,Kireev, Dmitri B.,Janzen, William P.,Arrowsmith, Cheryl H.,Frye, Stephen V.
supporting information, p. 1501 - 1507 (2013/11/19)
We recently reported the discovery of UNC1215, a potent and selective chemical probe for the L3MBTL3 methyllysine reader domain. In this article, we describe the development of structure-activity relationships (SAR) of a second series of potent L3MBTL3 antagonists which evolved from the structure of the chemical probe UNC1215. These compounds are selective for L3MBTL3 against a panel of methyllysine reader proteins, particularly the related MBT family proteins, L3MBTL1 and MBTD1. A co-crystal structure of L3MBTL3 and one of the most potent compounds suggests that the L3MBTL3 dimer rotates about the dimer interface to accommodate ligand binding.
FUSED PYRAZINE DERIVATIVES AS KINASE INHIBITORS
-
Page/Page column 58-59, (2010/06/11)
A series of quinoxaline derivatives, and analogues thereof, which are functionalised further by a substituted phenyl or pyridinyl moiety, being selective inhibitors of PO kinase enzymes, are accordingly of benefit in medicine, for example in the treatment of inflammatory, autoimmune, cardiovascular, neurodegenerative, metabolic, oncological, nociceptive or ophthalmic conditions.
