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426828-08-2

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426828-08-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 426828-08-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 4,2,6,8,2 and 8 respectively; the second part has 2 digits, 0 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 426828-08:
(8*4)+(7*2)+(6*6)+(5*8)+(4*2)+(3*8)+(2*0)+(1*8)=162
162 % 10 = 2
So 426828-08-2 is a valid CAS Registry Number.

426828-08-2Relevant academic research and scientific papers

Redox-active magnetic resonance imaging contrast agents: Studies with thiol-bearing 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetracetic acid derivatives

Jagadish, Bhumasamudram,Guntle, Gerald P.,Zhao, Dezheng,Gokhale, Vijay,Ozumerzifon, Tarik J.,Ahad, Ali M.,Mash, Eugene A.,Raghunand, Natarajan

, p. 10378 - 10386 (2013/02/23)

The synthesis and structure-activity relationships of a homologous series of 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid gadolinium(III) complexes bearing thiol-terminated alkyl side chains from three to nine carbons in length are reported. The observed binding with human serum albumin (HSA) of the compounds having C-3 through C-7 side chain lengths was inhibited by homocysteine in a manner consistent with single-site binding. The observed binding with HSA of the compounds having C-8 and C-9 side chain lengths was only partly inhibited by homocysteine, consistent with multisite binding. The binding affinity of the C-7 compound could be related to the HSA oxidation state. 2D 1H-1H NMR TOCSY provided evidence of covalent binding of the europium analog of the C-6 compound to HSA-Cys34. The longitudinal water-proton MRI relaxivities of the gadolinium complexes at 7 T increased upon binding to HSA. On the basis of these results, the C-6 and C-7 compounds were identified as promising redox-sensitive MRI contrast agents.

Structure-activity relationship of S-trityl-L-cysteine analogues as inhibitors of the human mitotic kinesin Eg5

DeBonis, Salvatore,Skoufias, Dimitrios A.,Indorato, Rose-Laure,Liger, Fran?ois,Marquet, Bernard,Laggner, Christian,Joseph, Beno?t,Kozielski, Frank

, p. 1115 - 1125 (2008/09/20)

The human kinesin Eg5 is a potential drug target for cancer chemotherapy. Eg5 specific inhibitors cause cells to block in mitosis with a characteristic monoastral spindle phenotype. Prolonged metaphase block eventually leads to apoptotic cell death. S-trityl-L-cysteine (STLC) is a tight-binding inhibitor of Eg5 that prevents mitotic progression. It has proven antitumor activity as shown in the NCI 60 tumor cell line screen. It is of considerable interest to define the minimum chemical structure that is essential for Eg5 inhibition and to develop more potent STLC analogues. An initial structure-activity relationship study on a series of STLC analogues reveals the minimal skeleton necessary for Eg5 inhibition as well as indications of how to obtain more potent analogues. The most effective compounds investigated with substitutions at the para-position of one phenyl ring have an estimated Kiapp of 100 nM in vitro and induce mitotic arrest with an EC50 of 200 nM.

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