121942-75-4Relevant articles and documents
New non-symmetrical choline kinase inhibitors
Schiaffino-Ortega, Santiago,López-Cara, Luisa Carlota,Ríos-Marco, Pablo,Carrasco-Jimenez, Maria Paz,Gallo, Miguel A.,Espinosa, Antonio,Marco, Carmen,Entrena, Antonio
, p. 7146 - 7154 (2013)
Identification of novel and selective anticancer agents remains an important and challenging goal in pharmacological research. Choline kinase (ChoK) is the first enzyme in the CDP-choline pathway that synthesizes phosphatidylcholine (PC), the major phosph
Convenient synthesis of deazaflavin cofactor FO and its activity in F420-dependent NADP reductase
Hossain, Mohammad S.,Le, Cuong Q.,Joseph, Ebenezer,Nguyen, Toan Q.,Johnson-Winters, Kayunta,Foss, Frank W.
, p. 5082 - 5085 (2015)
F420 and FO are phenolic 5-deazaflavin cofactors that complement nicotinamide and flavin redox coenzymes in biochemical oxidoreductases and photocatalytic systems. Specifically, these 5-deazaflavins lack the single electron reactivity with O2 of riboflavin-derived coenzymes (FMN and FAD), and, in general, have a more negative redox potential than NAD(P)+. For example, F420-dependent NADP+ oxidoreductase (Fno) is critical to the conversion of CO2 to CH4 by methanogenic archaea, while FO functions as a light-harvesting agent in DNA repair. The preparation of these cofactors is an obstacle to their use in biochemical studies and biotechnology. Here, a convenient synthesis of FO was achieved by improving the redox stability of synthetic intermediates containing a polar, electron-rich aminophenol fragment. Improved yields and simplified purification techniques for FO are described. Additionally, Fno activity was restored with FO in the absence of F420. Investigating the FO-dependent NADP+/NADPH redox process by stopped-flow spectrophotometry, steady state kinetics were defined as having a Km of 4.00 ± 0.39 μM and a kcat of 5.27 ± 0.14 s-1. The preparation of FO should enable future biochemical studies and novel uses of F420 mimics.
Structure-activity relationships of natural quinone vegfrecine analogs with potent activity against VEGFR-1 and -2 tyrosine kinases
Adachi, Hayamitsu,Nosaka, Chisato,Atsumi, Sonoko,Nakae, Koichi,Umezawa, Yoji,Sawa, Ryuichi,Kubota, Yumiko,Nakane, Chie,Shibuya, Masabumi,Nishimura, Yoshio
, p. 734 - 742 (2021/07/25)
A series of analogs of vegfrecine, a natural quinone vascular endothelial growth factor receptor (VEGFR) tyrosine kinase inhibitor, was synthesized via oxidative amination of 2,5-dihydroxybenzamide with functionalized arylamine followed by ammonolysis and
SUBSTITUTED AMIDE COMPOUNDS USEFUL AS FARNESOID X RECEPTOR MODULATORS
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Page/Page column 204; 205, (2020/08/28)
Disclosed are compounds of Formula (I): or a stereoisomer, a tautomer, or a pharmaceutically acceptable salt or solvate thereof, wherein Q is: (i) halo, cyano, hydroxyl, NRxRx, C(O)OH, C(O)NH2, C1-6 alkyl substituted with zero to 6 R1a, or P(O)R1cR1c; or (ii) L R1; and A, X1, X2, X3, X4, Z1, Z2, R1, R1a, R1c, R2, R3a, R3b, Rx, L, a, b, and d are defined herein. Also disclosed are methods of using these compounds to modulate the activity of farnesoid X receptor (FXR); pharmaceutical compositions comprising these compounds; and methods of treating a disease, disorder, or condition associated with FXR dysregulation, such as pathological fibrosis, transplant rejection, cancer, osteoporosis, and inflammatory disorders, by using the compounds and pharmaceutical compositions.
Small-Molecule Covalent Modification of Conserved Cysteine Leads to Allosteric Inhibition of the TEAD?Yap Protein-Protein Interaction
Bum-Erdene, Khuchtumur,Zhou, Donghui,Gonzalez-Gutierrez, Giovanni,Ghozayel, Mona K.,Si, Yubing,Xu, David,Shannon, Harlan E.,Bailey, Barbara J.,Corson, Timothy W.,Pollok, Karen E.,Wells, Clark D.,Meroueh, Samy O.
, p. 378 - 13,389 (2019/03/19)
The Hippo pathway coordinates extracellular signals onto the control of tissue homeostasis and organ size. Hippo signaling primarily regulates the ability of Yap1 to bind and co-activate TEA domain (TEAD) transcription factors. Yap1 tightly binds to TEAD4
