@inbook{8625a743fd224e7cba1f32adafcdd261,
title = "KDM5 Lysine Demethylases in Pathogenesis, from Basic Science Discovery to the Clinic",
abstract = "The histone lysine demethylase 5 (KDM5) family proteins are Fe2+ and α-ketoglutarate-dependent dioxygenases, with jumonji C (JmjC) domain as their catalytic core and several plant homeodomains (PHDs) to bind different histone methylation marks. These enzymes are capable of demethylating tri-, di- and mono-methylated lysine 4 in histone H3 (H3K4me3/2/1), the key epigenetic marks for active chromatin. Thus, this H3K4 demethylase family plays critical roles in cell fate determination during development as well as malignant transformation. KDM5 demethylases have both oncogenic and tumor suppressive functions in a cancer type-dependent manner. In solid tumors, KDM5A/B are generally oncogenic, whereas KDM5C/D have tumor suppressive roles. Their involvement in de-differentiation, cancer metastasis, drug resistance, and tumor immunoevasion indicated that KDM5 family proteins are promising drug targets for cancer therapy. Significant efforts from both academia and industry have led to the development of potent and selective KDM5 inhibitors for preclinical experiments and phase I clinical trials. However, a better understanding of the roles of KDM5 demethylases in different physiological and pathological conditions is critical for further developing KDM5 modulators for clinical applications.",
keywords = "Antitumor immunity, Cancer, Drug resistance, Histone demethylase, Jumonji, KDM5, Stem cell",
author = "Zhang, {Shang Min} and Jian Cao and Qin Yan",
note = "Publisher Copyright: {\textcopyright} Springer Nature Switzerland AG 2023.",
year = "2023",
doi = "10.1007/978-3-031-38176-8_6",
language = "English (US)",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer",
pages = "113--137",
booktitle = "Advances in Experimental Medicine and Biology",
}