1001185-40-5

Upstream product

• 79463-77-7 N-cyanodiphenylcarbonimidate 
• 106-49-0 p-toluidine 

Downstream Products

• 3929-18-8 N-p-tolyl-1H-[1,2,4]triazole-3,5-diamine 

Relevant academic research and scientific papers

DIHYDRO-CYCLOPENTA-ISOQUINOLINE SULFONAMIDES DERIVATIVES

The present invention relates to dihydro‐cyclopenta‐isoquinoline derivatives of formula (I): processes for preparing them, pharmaceutical compositions containing them and their use in treating disorders caused by IgE (such as allergic responses, non‐allergic mast cell responses or certain autoimmune responses), and in particular, disorders caused by the interaction of IgE with the FcεRI receptor.

TETRAHYDROBENZO-QUINOLINE SULFONAMIDES DERIVATIVE COMPOUNDS

The present invention relates to tetrahydrobenzo-isoquinoline sulfonamides derivatives of formula (I), processes for preparing them, pharmaceutical compositions containing them and their use in treating disorders caused by IgE (such as allergic responses,

THIOPHENE DERIVATIVES FOR THE TREATMENT OF DISORDERS CAUSED BY IGE

Thiophene derivatives of formula (I) and a pharmaceutically acceptable salt thereof are provided. These compounds have utility for the treatment or prevention of disorders caused by IgE, such as allergy, type 1 hypersensitivity or familiar sinus inflammation.

A comparative study of fragment screening methods on the p38α kinase: New methods, new insights

The stress-activated kinase p38α was used to evaluate a fragment-based drug discovery approach using the BioFocus fragment library. Compounds were screened by surface plasmon resonance (SPR) on a Biacore T100 against p38α and two selectivity targets. A sub-set of our library was the focus of detailed follow-up analyses that included hit confirmation, affinity determination on 24 confirmed, selective hits and competition assays of these hits with respect to a known ATP binding site inhibitor. In addition, functional activity against p38α was assessed in a biochemical assay using a mobility shift platform (LC3000, Caliper LifeSciences). A selection of fragments was also evaluated using fluorescence lifetime (FLEXYTE) and microscale thermophoresis (Nanotemper) technologies. A good correlation between the data for the different assays was found. Crystal structures were solved for four of the small molecules complexed to p38α. Interestingly, as determined both by X-ray analysis and SPR competition experiments, three of the complexes involved the fragment at the ATP binding site, while the fourth compound bound in a distal site that may offer potential as a novel drug target site. A first round of optimization around the remotely bound fragment has led to the identification of a series of triazole-containing compounds. This approach could form the basis for developing novel and active p38α inhibitors. More broadly, it illustrates the power of combining a range of biophysical and biochemical techniques to the discovery of fragments that facilitate the development of novel modulators of kinase and other drug targets.