@article{TCR11930,
author = {Alba Maiques-Diaz and Tim C. P. Somervaille},
title = {Inhibit a kinase to degrade a histone demethylase: a candidate therapeutic approach in glioblastoma},
journal = {Translational Cancer Research},
volume = {6},
number = {Suppl 1},
year = {2017},
keywords = {},
abstract = {Lysine-specific histone demethylase 1A (KDM1A; more commonly known as LSD1), the first enzyme discovered to possess histone demethylase activity, removes monomethyl and dimethyl groups from histone H3 lysine 4 (H3K4) (1). It is generally considered a transcription repressor being a key component of corepressor complexes such as CoREST and NuRD (2-4). High level expression of KDM1A protein is observed in multiple cancer types, including poor prognosis sub-groups of prostate, lung, brain and breast cancer, as well as in certain hematological malignancies. Pharmacologic inhibitors of KDM1A are currently in early phase clinical trials (4).},
issn = {2219-6803}, url = {https://tcr.amegroups.org/article/view/11930}
}