1346951-99-2Relevant academic research and scientific papers
Potent non-hydroxamate inhibitors of histone deacetylase-8: Role and scope of an isoindolin-2-yl linker with an α-amino amide as the zinc-binding unit
Chan, A. W. Edith,Greenwood, Simon O. R.,Hansen, D. Flemming,Marson, Charles M.
supporting information, (2020/01/22)
A series of potent inhibitors of histone deacetylase-8 (HDAC8) is described that contains an α-amino amide zinc-binding unit and a substituted isoindolinyl capping group. The presence of a 2,4-dichlorophenyl unit located in the acetate-release cavity was
Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors
Whitehead, Lewis,Dobler, Markus R.,Radetich, Branko,Zhu, Yanyi,Atadja, Peter W.,Claiborne, Tavina,Grob, Jonathan E.,McRiner, Andrew,Pancost, Margaret R.,Patnaik, Anup,Shao, Wenlin,Shultz, Michael,Tichkule, Ritesh,Tommasi, Ruben A.,Vash, Brian,Wang, Ping,Stams, Travis
experimental part, p. 4626 - 4634 (2011/09/12)
Herein we report the discovery of a family of novel yet simple, amino-acid derived class I HDAC inhibitors that demonstrate isoform selectivity via access to the internal acetate release channel. Isoform selectivity criteria is discussed on the basis of X
