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1419221-77-4

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1419221-77-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1419221-77-4 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,1,9,2,2 and 1 respectively; the second part has 2 digits, 7 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 1419221-77:
(9*1)+(8*4)+(7*1)+(6*9)+(5*2)+(4*2)+(3*1)+(2*7)+(1*7)=144
144 % 10 = 4
So 1419221-77-4 is a valid CAS Registry Number.

1419221-77-4Relevant articles and documents

FUSED BICYCLIC COMPOUND FOR INHIBITING ACTIVITY OF TYROSINE KINASE

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Paragraph 0166; 0168, (2019/06/12)

A fused bicyclic compound having an effect in inhibition of the activity of a tyrosine kinase, and preparation and use thereof are disclosed. In particular, a compound of formula (I) or a pharmaceutically acceptable salt, a stereoisomer, a solvate, a hydr

Discovery of 8-Amino-imidazo[1,5-a]pyrazines as Reversible BTK Inhibitors for the Treatment of Rheumatoid Arthritis

Liu, Jian,Guiadeen, Deodial,Krikorian, Arto,Gao, Xiaolei,Wang, James,Boga, Sobhana Babu,Alhassan, Abdul-Basit,Yu, Younong,Vaccaro, Henry,Liu, Shilan,Yang, Chundao,Wu, Hao,Cooper, Alan,De Man, Jos,Kaptein, Allard,Maloney, Kevin,Hornak, Viktor,Gao, Ying-Duo,Fischmann, Thierry O.,Raaijmakers, Hans,Vu-Pham, Diep,Presland, Jeremy,Mansueto, My,Xu, Zangwei,Leccese, Erica,Zhang-Hoover, Jie,Knemeyer, Ian,Garlisi, Charles G.,Bays, Nathan,Stivers, Peter,Brandish, Philip E.,Hicks, Alexandra,Kim, Ronald,Kozlowski, Joseph A.

supporting information, p. 198 - 203 (2016/03/01)

Bruton's tyrosine kinase (BTK) is a Tec family kinase with a well-defined role in the B cell receptor (BCR) pathway. It has become an attractive kinase target for selective B cell inhibition and for the treatment of B cell related diseases. We report a series of compounds based on 8-amino-imidazo[1,5-a]pyrazine that are potent reversible BTK inhibitors with excellent kinase selectivity. Selectivity is achieved through specific interactions of the ligand with the kinase hinge and driven by aminopyridine hydrogen bondings with Ser538 and Asp539, and by hydrophobic interaction of trifluoropyridine in the back pocket. These interactions are evident in the X-ray crystal structure of the lead compounds 1 and 3 in the complex with the BTK enzyme. Our lead compounds show desirable PK profiles and efficacy in the preclinical rat collagen induced arthritis model.

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