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1309687-06-6

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1309687-06-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1309687-06-6 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,3,0,9,6,8 and 7 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 1309687-06:
(9*1)+(8*3)+(7*0)+(6*9)+(5*6)+(4*8)+(3*7)+(2*0)+(1*6)=176
176 % 10 = 6
So 1309687-06-6 is a valid CAS Registry Number.

1309687-06-6Downstream Products

1309687-06-6Relevant academic research and scientific papers

Site-directed Mutagenesis of Key Residues Unveiled a Novel Allosteric Site on Human Adenosine Kinase for Pyrrolobenzoxa(thia)zepinone Non-Nucleoside Inhibitors

Savi, Lida,Brindisi, Margherita,Alfano, Gloria,Butini, Stefania,La Pietra, Valeria,Novellino, Ettore,Marinelli, Luciana,Lossani, Andrea,Focher, Federico,Cavella, Caterina,Campiani, Giuseppe,Gemma, Sandra

, p. 112 - 120 (2016)

Most nucleoside kinases, besides the catalytic domain, feature an allosteric domain which modulates their activity. Generally, non-substrate analogs, interacting with allosteric sites, represent a major opportunity for developing more selective and safer therapeutics. We recently developed a series of non-nucleoside non-competitive inhibitors of human adenosine kinase (hAK), based on a pyrrolobenzoxa(thia)zepinone scaffold. Based on computational analysis, we hypothesized the existence of a novel allosteric site on hAK, topographically distinct from the catalytic site. In this study, we have adopted a multidisciplinary approach including molecular modeling, biochemical studies, and site-directed mutagenesis to validate our hypothesis. Based on a three-dimensional model of interaction between hAK and our molecules, we designed, cloned, and expressed specific, single and double point mutants of hAK (Q74A, Q78A, H107A, K341A, F338A, and Q74A-F338A). Kinetic characterization of recombinant enzymes indicated that these mutations did not affect enzyme functioning; conversely, mutated enzymes are endowed of reduced susceptibility to our non-nucleoside inhibitors, while maintaining comparable affinity for nucleoside inhibitors to the wild-type enzyme. This study represents the first characterization and validation of a novel allosteric site in hAK and may pave the way to the development of novel selective and potent non-nucleoside inhibitors of hAK endowed with therapeutic potential.

Alkaloid induced asymmetric electrocarboxylation of 4-methylpropiophenone

Zhao, Shu-Feng,Zhu, Mei-Xia,Zhang, Kai,Wang, Huan,Lu, Jia-Xing

experimental part, p. 2702 - 2705 (2011/06/19)

The alkaloid-induced electrocarboxylation of 4-methylpropiophenone is examined in mild conditions. Comparative studies with several inductors indicate that the efficient enantiodiscrimination of the electrocarboxylation depends on the nucleophilic quinucl

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