Chemical and biochemical perspectives of protein lysine methylation

M Luo - Chemical reviews, 2018 - ACS Publications
Protein lysine methylation is a distinct posttranslational modification that causes minimal
changes in the size and electrostatic status of lysine residues. Lysine methylation plays …

Epigenetic modulators as therapeutic agents in cancer

E Patnaik, C Madu, Y Lu - International Journal of Molecular Sciences, 2023 - mdpi.com
Epigenetics play a crucial role in gene regulation and cellular processes. Most importantly,
its dysregulation can contribute to the development of tumors. Epigenetic modifications, such …

The role of nuclear receptor–binding SET domain family histone lysine methyltransferases in cancer

RL Bennett, A Swaroop… - Cold Spring …, 2017 - perspectivesinmedicine.cshlp.org
The nuclear receptor–binding SET Domain (NSD) family of histone H3 lysine 36
methyltransferases is comprised of NSD1, NSD2 (MMSET/WHSC1), and NSD3 (WHSC1L1) …

Recent advances in nuclear receptor-binding SET domain 2 (NSD2) inhibitors: An update and perspectives

L Zhang, X Zha - European Journal of Medicinal Chemistry, 2023 - Elsevier
Nuclear receptor-binding SET domain 2 (NSD2) is a histone lysine methyltransferase
(HKMTase), which is mainly responsible for the di-methylation of lysine residues on …

Approaching the catalytic mechanism of protein lysine methyltransferases by biochemical and simulation techniques

P Schnee, J Pleiss, A Jeltsch - Critical Reviews in Biochemistry and …, 2024 - Taylor & Francis
Protein lysine methyltransferases (PKMTs) transfer up to three methyl groups to the side
chains of lysine residues in proteins and fulfill important regulatory functions by controlling …

The role of methyltransferase NSD2 as a potential oncogene in human solid tumors

R Chen, Y Chen, W Zhao, C Fang, W Zhou… - OncoTargets and …, 2020 - Taylor & Francis
Malignant solid tumors are the leading cause of death in humans, and epigenetic regulation
plays a significant role in studying the mechanism of human solid tumors. Recently, histone …

Structural insights into stimulation of Ash1L's H3K36 methyltransferase activity through Mrg15 binding

P Hou, C Huang, CP Liu, N Yang, T Yu, Y Yin, B Zhu… - Structure, 2019 - cell.com
The evolutionarily conserved Trithorax group protein Ash1 is a SET domain histone
methyltransferase that mono-and dimethylates lysine 36 of histone H3 (H3K36). Ash1 forms …

The transition-state structure for human MAT2A from isotope effects

RS Firestone, VL Schramm - Journal of the American Chemical …, 2017 - ACS Publications
Human methionine S-adenosyltransferase (MAT2A) catalyzes the formation of S-
adenosylmethionine (SAM) from ATP and methionine. Synthetic lethal genetic analysis has …

NSD 2 promotes ventricular remodelling mediated by the regulation of H3K36me2

X Zhou, R Zhu, X Wu, H Xu, Y Li, Q Xu… - Journal of Cellular …, 2019 - Wiley Online Library
Histone lysine methylation plays an important role in the regulation of ventricular
remodelling. NSD 2 is involved in many types of tumours through enhancing H3K36me2 …

Identification of potential methyltransferase NSD2 enzymatic inhibitors through a multi-step structure-based drug design

Y Shen, Y Zhang, T Wu, L Zhang, BD Belviso - Molecular Diversity, 2024 - Springer
Reversing aberrant protein methylation levels is widely recognized as a key focus in cancer
therapy. As an essential lysine methylation regulator, NSD2 (Nuclear receptor-binding SET …