81216-14-0Relevant articles and documents
EPIGENETIC PROFILING METHOD
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Page/Page column 17; 18; 19, (2021/04/01)
A method for analyzing DNA comprises forming labelled DNA fragments by cleaving genomic DNA into DNA fragments, selectively functionalizing any non-methylated CpG sites present in the DNA with a linker comprising a hydrolysable moiety, and attaching a label to the linker. The method further comprises separating the labelled DNA fragments from any non-labelled DNA fragments, hydrolysing the hydrolysable moiety of the linker of the separated labelled DNA fragments so as to release the DNA fragments from the label, and sequencing the released DNA fragments.
Hydroaminoalkylation of Allenes
Bielefeld, Jens,Mannhaupt, Steffen,Schmidtmann, Marc,Doye, Sven
supporting information, p. 967 - 971 (2019/05/10)
The first examples of early-transition-metal-catalyzed hydroaminoalkylation reactions of allenes are reported. Initial studies performed with secondary aminoallenes led to the identification of a suitable titanium catalyst and revealed that under the reaction conditions, the initially formed hydroaminoalkylation products undergo an unexpected titanium-catalyzed rearrangement to form the thermodynamically more stable allylamines. The assumption that this rearrangement involves a reactive allylic cation intermediate provides a simple explanation of the fact that no successful early-transition-metal-catalyzed hydroaminoalkylations of allenes have previously been reported. As a result of the generation of the corresponding cation, the titanium-catalyzed intermolecular hydroaminoalkylation of propa-1,2-diene unexpectedly gives an aminocyclopentane product formed by incorporation of two equivalents of propa-1,2-diene.
Discovery of a Highly Selective Cell-Active Inhibitor of the Histone Lysine Demethylases KDM2/7
Gerken, Philip A.,Wolstenhulme, Jamie R.,Tumber, Anthony,Hatch, Stephanie B.,Zhang, Yijia,Müller, Susanne,Chandler, Shane A.,Mair, Barbara,Li, Fengling,Nijman, Sebastian M. B.,Konietzny, Rebecca,Szommer, Tamas,Yapp, Clarence,Fedorov, Oleg,Benesch, Justin L. P.,Vedadi, Masoud,Kessler, Benedikt M.,Kawamura, Akane,Brennan, Paul E.,Smith, Martin D.
supporting information, p. 15555 - 15559 (2017/12/02)
Histone lysine demethylases (KDMs) are of critical importance in the epigenetic regulation of gene expression, yet there are few selective, cell-permeable inhibitors or suitable tool compounds for these enzymes. We describe the discovery of a new class of inhibitor that is highly potent towards the histone lysine demethylases KDM2A/7A. A modular synthetic approach was used to explore the chemical space and accelerate the investigation of key structure–activity relationships, leading to the development of a small molecule with around 75-fold selectivity towards KDM2A/7A versus other KDMs, as well as cellular activity at low micromolar concentrations.