890086-97-2

Upstream product

• 87751-33-5 quinoline-3,4-diamine 
• 2099-63-0 anthranilic acid hydrochloride 
• 121845-92-9 2-<2-nitroethylideneamino>benzoic acid 
• 39061-97-7 4-chloro-3-nitroquinoline 
• 50332-66-6 3-nitro-quinolin-4-ol 
• 42606-33-7 3-nitro-4-aminoquinoline 
• 890086-92-7 2-cyclohexyl-1H-imidazo[4,5-c]quinoline 

Downstream Products

• 890087-03-3 4-chloro-2-cyclohexyl-1H-imidazo[4,5-c]quinoline 

Relevant academic research and scientific papers

Novel 2-and 4-Substituted 1H-Imidazo[4,5-c]quinolin-4-amine derivatives as allosteric modulators of the A3 adenosine receptor

4-Arylamino and 2- cycloalkyl (including amino substitution) modifications were made in a series of 1Himidazo[ 4,5-c]quinolin-4-amine derivatives as allosteric modulators of the human A3 adenosine receptor (AR). In addition to allosteric modula

A3 ADENOSINE RECEPTOR ALLOSTERIC MODULATORS

The present invention relates to allosteric modulation of A3 adenosine receptor (A3AR) and provides for the use of an A3 adenosine receptor modulator (A3RM),for the preparation of pharmaceutical compositions for

Structure-activity relationships of new 1H-imidazo[4,5-c]quinolin-4-amine derivatives as allosteric enhancers of the A3 adenosine receptor

1H-Imidazo[4,5-c]quinolin-4-amine derivatives have been synthesized as allosteric modulators of the human A3 adenosine receptor (AR). Structural modifications were made at the 4-amino and 2 positions. The compounds were tested in both binding and functional assays, and many were found to be allosteric enhancers of the action of A3AR agonists by several different criteria. First, a potentiation of the maximum efficacy of the agonist C1-IB-MECA was observed for numerous derivatives. Also, a number of these compounds decreased the rate of dissociation of the agonist [ 125I]I-AB-MECA from the A3AR. Most prominently, compound 43 (LUF6000) was found to enhance agonist efficacy in a functional assay by 45% and decrease dissociation rate similarly without influencing agonist potency. The structural requirements for allosteric enhancement at the A3AR were distinct from the requirements to inhibit equilibrium binding. Thus, we have prepared allosteric enhancers of the human A3AR that have an improved allosteric effect in comparison to the inhibition of equilibrium binding at the orthosteric site.