1431163-17-5 Usage
General Description
3-Iodo-6-methoxy-1-methyl-1H-indazole is a chemical compound that belongs to the indazole family. It is characterized by the presence of a methyl group on the 1-position, a methoxy group on the 6-position, and an iodo group on the 3-position of the indazole ring. 3-Iodo-6-methoxy-1-methyl-1H-indazole has potential applications in the field of medicinal chemistry, as it exhibits pharmacological properties that make it suitable for use in the development of pharmaceutical drugs. Its unique chemical structure and reactivity make it a valuable building block for the synthesis of new compounds with potentially beneficial biological activities. The compound's properties make it an interesting target for further research and potential drug development.
Check Digit Verification of cas no
The CAS Registry Mumber 1431163-17-5 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,3,1,1,6 and 3 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 1431163-17:
(9*1)+(8*4)+(7*3)+(6*1)+(5*1)+(4*6)+(3*3)+(2*1)+(1*7)=115
115 % 10 = 5
So 1431163-17-5 is a valid CAS Registry Number.
1431163-17-5Relevant articles and documents
Strategic use of conformational bias and structure based design to identify potent JAK3 inhibitors with improved selectivity against the JAK family and the kinome
Lynch, Stephen M.,Devicente, Javier,Hermann, Johannes C.,Jaime-Figueroa, Saul,Jin, Sue,Kuglstatter, Andreas,Li, Hongju,Lovey, Allen,Menke, John,Niu, Linghao,Patel, Vaishali,Roy, Douglas,Soth, Michael,Steiner, Sandra,Tivitmahaisoon, Parcharee,Vu, Minh Diem,Yee, Calvin
, p. 2793 - 2800 (2013/07/05)
Using a structure based design approach we have identified a series of indazole substituted pyrrolopyrazines, which are potent inhibitors of JAK3. Intramolecular electronic repulsion was used as a strategy to induce a strong conformational bias within the ligand. Compounds bearing this conformation participated in a favorable hydrophobic interaction with a cysteine residue in the JAK3 binding pocket, which imparted high selectivity versus the kinome and improved selectivity within the JAK family.
