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
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.
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)
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
An efficient and straightforward strategy for the synthesis of tetrasubstituted imidazoles from propargyl amines, sulfonyl azides, and terminal alkynes is described. N-sulfonyl ketenimine and aminoallene are believed to be the key intermediates for this two-step one-pot transformation.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
