737772-45-1Relevant academic research and scientific papers
Rational modification, synthesis and biological evaluation of 3,4-dihydroquinoxalin-2(1H)-one derivatives as potent and selective c-Jun N-terminal kinase 3 (JNK3) inhibitors
Dou, Xiaodong,Huang, Huixia,Jiang, Lan,Jiao, Ning,Jin, Hongwei,Liu, Zhenming,Zhang, Liangren,Zhang, Lihe,Zhu, Guiwang
, (2020/07/03)
The c-Jun N-terminal kinase 3 (JNK3) plays key roles in a wide range of diseases, including neurodegeneration diseases, inflammation diseases, cancers, cardiovascular diseases, and metabolic disorders. Previously, we have identified a lead compound, (Z)-3
PIPERIDINE CXCR7 RECEPTOR MODULATORS
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Page/Page column 132-134, (2018/02/28)
The present invention relates to piperidine derivatives of formula (I) wherein Ar1, Ar2, RAr1, R1, R2, and R3 are as described in the description, their preparation, to pharmaceutically acceptable salts thereof, and to their use as pharmaceuticals, to pharmaceutical compositions containing one or more compounds of formula (I), and especially to their use as CXCR7 receptor modulators.
THIOPHENE DERIVATIVES, THEIR MANUFACTURE AND USE AS PHARMACEUTICAL AGENTS
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Page/Page column 58, (2010/02/15)
Objects of the present invention are the compounds of formula (I), their pharmaceutically acceptable salts, enantiomeric forms, diastereoisomers and racemates, the preparation of the above-mentioned compounds, medicaments containing them and their manufac
Slow-binding inhibition of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase
Braga, Remi,Hecquet, Laurence,Blonski, Casimir
, p. 2965 - 2972 (2007/10/03)
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase is a key enzyme in the Entner-Doudoroff pathway of bacteria. It catalyzes the reversible production of KDPG from pyruvate and D-glyceraldehyde 3-phosphate through a class I Schiff base mechanism. On the basis of aldolase mechanistic pathway, various pyruvate analogues bearing β-diketo structures were designed and synthesized as potential inhibitors. Their capacity to inhibit aldolase catalyzed reaction by forming stabilized iminium ion or conjugated enamine were investigated by enzymatic kinetics and UV-vis difference spectroscopy. Depending of the substituent R (methyl or aromatic ring), a competitive or a slow-binding inhibition takes place. These results were examined on the basis of the three-dimensional structure of the enzyme.
