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ethyl (E)-4-bromo-3-hydroxycinnamate is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

540779-38-2

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540779-38-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 540779-38-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 5,4,0,7,7 and 9 respectively; the second part has 2 digits, 3 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 540779-38:
(8*5)+(7*4)+(6*0)+(5*7)+(4*7)+(3*9)+(2*3)+(1*8)=172
172 % 10 = 2
So 540779-38-2 is a valid CAS Registry Number.

540779-38-2Relevant academic research and scientific papers

Inhibition of IκB kinase-β and IκB kinase-α by heterocyclic adamantyl arotinoids

García-Rodríguez, José,Pérez-Rodríguez, Santiago,Ortiz, María A.,Pereira, Raquel,De Lera, Angel R.,Piedrafita, F. Javier

, p. 1285 - 1302 (2014/03/21)

We recently reported on a series of retinoid-related molecules containing an adamantyl group, a.k.a. adamantyl arotinoids (AdArs), that showed significant cancer cell growth inhibitory activity and activated RXRα (NR2B1) in transient transfection assays while devoid of RAR transactivation capacity. We have now explored whether these AdArs could also bind and inhibit IKKβ, a known target that mediates the induction of apoptosis and cancer cell growth inhibition by related AdArs containing a chalcone functional group. In addition, we have prepared and evaluated novel AdArs that incorporate a central heterocyclic ring connecting the adamantyl-phenol and the carboxylic acid at the polar termini. Our results indicate that the majority of the RXRα activating compounds lacked IKKβ inhibitory activity. In contrast, the novel heterocyclic AdArs containing a thiazole or pyrazine ring linked to a benzoic acid motif were potent inhibitors of both IKKα and IKKβ, which in most cases paralleled significant growth inhibitory and apoptosis inducing activities.

Antagonist analogue of 6-[3′-(1-adamantyl)-4′-hydroxyphenyl]-2- naphthalenecarboxylic acid (AHPN) family of apoptosis inducers that effectively blocks AHPN-induced apoptosis but not cell-cycle arrest

Dawson, Marcia I.,Harris, Danni L.,Liu, Gang,Hobbs, Peter D.,Lange, Christopher W.,Jong, Ling,Bruey-Sedano, Nathalie,James, Sharon Y.,Zhang, Xiao-Kun,Peterson, Valerie J.,Leid, Mark,Farhana, Lulu,Rishi, Arun K.,Fontana, Joseph A.

, p. 3518 - 3536 (2007/10/03)

The retinoid 6-[3′-(1-adamantyl)-4′-hydroxyphenyl]-2- naphthalenecarboxylic acid (AHPN) and its active analogues induce cell-cycle arrest and programmed cell death (apoptosis) in cancer cells independently of retinoic acid receptor (RAR) interaction. Its analogue, (E)-4-[3′-(1- adamantyl)-4′-hydroxyphenyl]-3-(3′-acetamidopropyloxy)cinnamic acid (3-A-AHPC) selectively antagonized cell apoptotic events (TR3/nur77/NGFI-B expression and nuclear-to-mitochondrial translocation) but not the proliferative events (cell-cycle arrest and p21WAF1/CIP1 expression) induced by proapoptotic AHPN and its analogues. The syntheses of 3-A-AHPC and proapoptotic (E)-6-[3′-(1-adamantyl)-4′-hydroxyphenyl]-5- chloronaphthalenecarboxylic acid (5-Cl-AHPN) are described. Computational studies on AHPN, AHPC, and three substituted analogues (5-Cl-AHPN, 3-Cl-AHPC, and 3-A-AHPC) suggested reasons for their diametric effects on RAR activation. Density functional theory studies indicated that the 1-adamantyl (1-Ad) groups of the AHPN and AHPC configurations assumed positions that were nearly planar with the aromatic rings of their polar termini. In contrast, in the configurations of the substituted analogues having chloro and 3-acetamidopropyloxy groups, rather than a hydrogen, ortho to the diaryl bonds, the diaryl bond torsion angles increased so that the 1-Ad groups were oriented out of this plane. Docking and molecular dynamics of AHPN, AHPC, and these substituted analogues in the RARγ ligand-binding domain illustrated how specific substituents on the AHPN and AHPC scaffolds modulated the positions and dynamics of the 1-Ad groups. As a result, the position of RARγ helix H12 in forming the coactivator-binding site was impacted in a manner consistent with the experimental effect of each analogue on RARγ transcriptional activation.

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