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41445-88-9

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41445-88-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 41445-88-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,1,4,4 and 5 respectively; the second part has 2 digits, 8 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 41445-88:
(7*4)+(6*1)+(5*4)+(4*4)+(3*5)+(2*8)+(1*8)=109
109 % 10 = 9
So 41445-88-9 is a valid CAS Registry Number.

41445-88-9Relevant articles and documents

Lewis acid- and cationic lithium-mediated diastereoselective aldol-type reaction based on a double chiral recognition manner for the asymmetric synthesis of α-substituted serines

Sano,Liu,Takebayashi,Kobayashi,Tabata,Shiro,Nagao

, p. 4101 - 4104 (1995)

Diastereoselective aldol-type reaction of ethyl (5R or 5S)-3,6-diethoxy-2,5-dihydro-5-isopropyl-2-pyrazinecarboxylate (5) with chiral aldehyde 7 was investigated by using Sn(OSO2CF3)2-N-ethylpiperizine, MgBr2-Et

HETEROCYCLIC UREA DERIVATIVES AND METHODS OF USE THEREOF

-

Page/Page column 92, (2010/12/29)

Compounds of formula (IA) and their pharmaceutically acceptable salts are described. Processes for their preparation, pharmaceutical compositions containing them, their use as medicaments and their use in the treatment of bacterial infections are also described.

Preparation and structure-activity relationship of novel P1/P1'- substituted cyclic urea-based human immunodeficiency virus type-1 protease inhibitors

Nugiel,Jacobs,Worley,Patel,Kaltenbach III,Meyer,Jadhav,De Lucca,Smyser,Klabe,Bacheler,Rayner,Seitz

, p. 2156 - 2169 (2007/10/03)

A series of novel P1/P1'-substituted cyclic urea-based HIV-1 protease inhibitors was prepared. Three different synthetic schemes were used to assemble these compounds. The first approach uses amino acid-based starting materials and was originally used to prepare DMP 323. The other two approaches use L-tartaric acid or L-mannitol as the starting material. The required four contiguous R,S,S,R centers of the cyclic urea scaffold are introduced using substrate control methodology. Each approach has specific advantages based on the desired P1/P1' substituent. Designing analogs based on the enzyme's natural substrates provided compounds with reduced activity. Attempts at exploiting hydrogen bond sites in the S1/S1' pocket, suggested by molecular modeling studies, were not fruitful. Several analogs had better binding affinity compared to our initial leads. Modulating the compound's physical properties led to a 10-fold improvement in translation resulting in better overall antiviral activity.

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