13160-59-3

Usage

InChI:InChI=1/C12H11N3O/c13-10-5-3-9(4-6-10)12(16)15-11-2-1-7-14-8-11/h1-8H,13H2,(H,15,16)

Upstream product

• 13313-18-3 4-nitro-N-(pyridin-3-yl)benzamide 
• 66493-39-8 4-(N-tert-butoxycarbonyl)aminobenzoic acid 
• 462-08-8 pyridin-3-ylamine 
• 1326565-88-1 C₁₇H₁₉N₃O₃ 

Downstream Products

• 1173207-71-0 4-({[4-(3-ethyl-7-morpholin-4-yl-3H-[1,2,3]triazolo[4,5-d]pyrimidin-5-yl)phenyl]carbamoyl}amino)-N-pyridin-3-ylbenzamide 
• 909504-92-3 C₁₉H₁₅N₃O₂ 
• 1552311-69-9 C₂₀H₁₇N₃O₂ 
• 1552311-71-3 C₁₉H₁₄ClN₃O₂ 
• 1552311-74-6 C₂₃H₂₃N₃O₂ 
• 831214-35-8 C₁₃H₁₃N₃O₃S 
• 838260-50-7 C₁₈H₁₅N₃O₃S 
• 831204-81-0 C₁₉H₁₇N₃O₃S 
• 1552311-73-5 C₁₈H₁₄ClN₃O₃S 
• 1552311-75-7 C₂₂H₂₃N₃O₃S 
• 1229653-23-9 C₂₀H₁₅F₃N₄O₂ 

Relevant academic research and scientific papers

Towards the development of non-enediyne approaches for mimicking enediyne chemistry: Design, synthesis and activity of a 1,4-bisdiazonium compound

1,4-bisdiazonium compounds, whichmay be precursors of aryl 1,4-diradicals, have the potential to mimic the DNA cleaving activity of the enediyne antibiotics. To this end, the ability to generate and activate 1,4-bisdiazonium compounds in good yield (e.g.,

Fragment-based design of 3-aminopyridine-derived amides as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT)

The fragment-based identification of two novel and potent biochemical inhibitors of the nicotinamide phosphoribosyltransferase (NAMPT) enzyme is described. These compounds (51 and 63) incorporate an amide moiety derived from 3-aminopyridine, and are thus structurally distinct from other known anti-NAMPT agents. Each exhibits potent inhibition of NAMPT biochemical activity (IC 50 = 19 and 15 nM, respectively) as well as robust antiproliferative properties in A2780 cell culture experiments (IC50 = 121 and 99 nM, respectively). However, additional biological studies indicate that only inhibitor 51 exerts its A2780 cell culture effects via a NAMPT-mediated mechanism. The crystal structures of both 51 and 63 in complex with NAMPT are also independently described.

Exploration of secondary and tertiary pharmacophores in unsymmetrical N,N′-diaryl urea inhibitors of soluble epoxide hydrolase

The impact of various secondary and tertiary pharmacophores on in vitro potency of soluble epoxide hydrolase (sEH) inhibitors based on the unsymmetrical urea scaffold 1 is discussed. N,N′-Diaryl urea inhibitors of soluble epoxide hydrolase exhibit subtle variations in inhibitory potency depending on the secondary pharmacophore but tolerate considerable structural variation in the second linker/tertiary pharmacophore fragment.