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414900-55-3

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414900-55-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 414900-55-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 4,1,4,9,0 and 0 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 414900-55:
(8*4)+(7*1)+(6*4)+(5*9)+(4*0)+(3*0)+(2*5)+(1*5)=123
123 % 10 = 3
So 414900-55-3 is a valid CAS Registry Number.

414900-55-3Downstream Products

414900-55-3Relevant academic research and scientific papers

Identification and Electrophysiological Evaluation of 2-Methylbenzamide Derivatives as Nav1.1 Modulators

Crestey, Fran?ois,Frederiksen, Kristen,Jensen, Henrik S.,Dekermendjian, Kim,Larsen, Peter H.,Bastlund, Jesper F.,Lu, Dunguo,Liu, Henry,Yang, Charles R.,Grunnet, Morten,Svenstrup, Niels

, p. 1302 - 1308 (2015)

Voltage-gated sodium channels (Nav) are crucial to the initiation and propagation of action potentials (APs) in electrically excitable cells, and during the past decades they have received considerable attention due to their therapeutic potential. Here, we report for the first time the synthesis and the electrophysiological evaluation of 16 ligands based on a 2-methylbenzamide scaffold that have been identified as Nav1.1 modulators. Among these compounds, N,N′-(1,3-phenylene)bis(2-methylbenzamide) (3a) has been selected and evaluated in ex-vivo experiments in order to estimate the activation impact of such a compound profile. It appears that 3a increases the Nav1.1 channel activity although its overall impact remains moderate. Altogether, our preliminary results provide new insights into the development of small molecule activators targeting specifically Nav1.1 channels to design potential drugs for treating CNS diseases.

Potent and selective inhibitors of the TASK-1 potassium channel through chemical optimization of a bis-amide scaffold

Flaherty, Daniel P.,Simpson, Denise S.,Miller, Melissa,Maki, Brooks E.,Zou, Beiyan,Shi, Jie,Wu, Meng,McManus, Owen B.,Aubé, Jeffrey,Li, Min,Golden, Jennifer E.

, p. 3968 - 3973 (2014/09/03)

TASK-1 is a two-pore domain potassium channel that is important to modulating cell excitability, most notably in the context of neuronal pathways. In order to leverage TASK-1 for therapeutic benefit, its physiological role needs better characterization; however, designing selective inhibitors that avoid the closely related TASK-3 channel has been challenging. In this study, a series of bis-amide derived compounds were found to demonstrate improved TASK-1 selectivity over TASK-3 compared to reported inhibitors. Optimization of a marginally selective hit led to analog 35 which displays a TASK-1 IC 50 = 16 nM with 62-fold selectivity over TASK-3 in an orthogonal electrophysiology assay.

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