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- W4319304503 endingPage "103519" @default.
- W4319304503 startingPage "103519" @default.
- W4319304503 abstract "Histone methylation is the most common histone modification and a highly dynamic regulator of gene transcription. Methylation of lysine residues can alter the structure of chromatin, helping to regulate DNA-based nuclear activities. Lysine demethylases control and maintain epigenetic factors that affect chromatin structure and cell characteristics. A variety of diseases, including malignant tumors, are connected to their dysregulation. Advances in biochemistry and pathogenesis have prompted the discovery of small molecule inhibitors and tool compounds that disrupt lysine demethylation. In this review, we focus on JmjC-domain-containing histone lysine demethylases (KDM2-7), discussing their structures and biological roles, representative inhibitors, and therapeutic potential in cancer therapy, and aiming to provide unique insights into the development of JmjC-KDM inhibitors." @default.
- W4319304503 created "2023-02-07" @default.
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- W4319304503 date "2023-05-01" @default.
- W4319304503 modified "2023-10-11" @default.
- W4319304503 title "Development of JmjC-domain-containing histone demethylase (KDM2-7) inhibitors for cancer therapy" @default.
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- W4319304503 doi "https://doi.org/10.1016/j.drudis.2023.103519" @default.
- W4319304503 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36754142" @default.
- W4319304503 hasPublicationYear "2023" @default.
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