Journal of ovarian research, 6(1), 75-75 (2013-10-30)
Lysine-specific demethylase 1 (LSD1, also known as KDM1A and AOF2) is a chromatin-modifying activity that catalyzes the removal of methyl groups from lysine residues in histone and non-histone proteins, regulating gene transcription. LSD1 is overexpressed in several cancer types, and
Journal of the American Chemical Society, 134(27), 11146-11152 (2012-06-06)
(15)N-Propargylcholine has been synthesized and hydrogenated with para-H(2). Through the application of a field cycling procedure, parahydrogen spin order is transferred to the (15)N resonance. Among the different isomers formed upon hydrogenation of (15)N-propargylcholine, only the nontransposed derivative contributes to
The Journal of organic chemistry, 78(4), 1687-1692 (2013-02-01)
The reaction of propargylic carbonates with 4-hydroxy-2-pyrones in the presence of a palladium catalyst is described. By the choice of the reaction temperature, two types of the substituted furo[3,2-c]pyran-4-one derivatives were regioselectively synthesized, respectively.
Glioma development is a multistep process, involving alterations in genetic and epigenetic mechanisms. Understanding the mechanisms and enzymes that promote epigenetic changes in gliomas are urgently needed to identify novel therapeutic targets. We examined the role of histone demethylase KDM1
Our previous studies demonstrated that lysine-specific demethylase 1 (LSD1) and histone deacetylases (HDACs) closely interact in controlling growth of breast cancer cells. However, the underlying mechanisms are largely unknown. In this study, we showed that knockdown of LSD1 expression (LSD1-KD)
