1431081-01-4Relevant articles and documents
Selective Inhibition of Histone Deacetylase 10: Hydrogen Bonding to the Gatekeeper Residue is Implicated
Géraldy, Magalie,Morgen, Michael,Sehr, Peter,Steimbach, Raphael R.,Moi, Davide,Ridinger, Johannes,Oehme, Ina,Witt, Olaf,Malz, Mona,Nogueira, Mauro S.,Koch, Oliver,Gunkel, Nikolas,Miller, Aubry K.
, p. 4426 - 4443 (2019/05/17)
The discovery of isozyme-selective histone deacetylase (HDAC) inhibitors is critical for understanding the biological functions of individual HDACs and for validating HDACs as drug targets. The isozyme HDAC10 contributes to chemotherapy resistance and has
Potent and selective HDAC6 inhibitory activity of N-(4- hydroxycarbamoylbenzyl)-1,2,4,9-tetrahydro-3-thia-9-azafluorenes as novel sulfur analogues of Tubastatin A
De Vreese, Rob,Verhaeghe, Tom,Desmet, Tom,D'Hooghe, Matthias
supporting information, p. 3775 - 3777 (2013/05/22)
Eight N-(4-hydroxycarbamoylbenzyl)-1,2,4,9-tetrahydro-3-thia-9-azafluorenes were efficiently prepared as sulfur analogues of Tubastatin A and thus evaluated as new HDAC6 inhibitors. All compounds exhibited potency against HDAC6, and four of them were active in the nanomolar range (IC50 = 1.9-22 nM). Further analysis revealed that the sulfone derivatives (designated as Tubathians) are superior to their non-oxidized sulfide analogues, and the two most active sulfones showed good to excellent HDAC6 selectivity compared to all other HDAC isoform classes.
