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N-(4-(benzyloxy)phenyl)formamide is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

479075-72-4

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479075-72-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 479075-72-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 4,7,9,0,7 and 5 respectively; the second part has 2 digits, 7 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 479075-72:
(8*4)+(7*7)+(6*9)+(5*0)+(4*7)+(3*5)+(2*7)+(1*2)=194
194 % 10 = 4
So 479075-72-4 is a valid CAS Registry Number.

479075-72-4Relevant academic research and scientific papers

Copper promoted aerobic oxidative c(sp3)-c(sp3) bond cleavage of n-(2-(pyridin-2-yl)-ethyl)anilines

Yu, Yang,Zhang, Yong,Sun, Chengyu,Shi, Lei,Wang, Wei,Li, Hao

, p. 2725 - 2732 (2020/03/11)

A strategy of aerobic oxidative C(sp3)-C(sp3) bond cleavage of N-ethylaniline derivatives bearing azaarenes for the synthesis of N-aryl formamides has been developed. This approach was carried out smoothly with the CuI/TEMPO/air system to give N-aryl formamides in yields of 50-90%. With this methodology, a mutagenically active compound was constructed in 90% yield. Moreover, the reaction also provided a one-pot synthetic tool for accessing a promoter of hematopoietic stem cells by difunctionalization in 61% yield.

Interaction of α-Thymidine Inhibitors with Thymidylate Kinase from Plasmodium falciparum

Chen, Mengshen,Sinha, Kaustubh,Rule, Gordon S.,Ly, Danith H.

, p. 2868 - 2875 (2018/05/14)

Plasmodium falciparum thymidylate kinase (PfTMK) is a critical enzyme in the de novo biosynthesis pathway of pyrimidine nucleotides. N-(5′-Deoxy-α-thymidin-5′-yl)-N′-[4-(2-chlorobenzyloxy)phenyl]urea was developed as an inhibitor of PfTMK and has been reported as an effective inhibitor of P. falciparum growth with an EC50 of 28 nM [Cui, H., et al. (2012) J. Med. Chem. 55, 10948-10957]. Using this compound as a scaffold, a number of derivatives were developed and, along with the original compound, were characterized in terms of their enzyme inhibition (Ki) and binding affinity (KD). Furthermore, the binding site of the synthesized compounds was investigated by a combination of mutagenesis and docking simulations. Although the reported compound is indicated to be highly effective in its inhibition of parasite growth, we observed significantly lower binding affinity and weaker inhibition of PfTMK than expected from the reported EC50. This suggests that significant structural optimization will be required for the use of this scaffold as an effective PfTMK inhibitor and that the inhibition of parasite growth is due to an off-target effect.

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