Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells
By F. P. Silva, Ryuji Hamamoto, M. Kunizaki, M. Tsuge, Y. Nakamura, Yoichi Furukawa. 2008
59 citations recorded by the source corpus.
Subfields: Molecular Biology
How researchers see this paper
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In Molecular Biology
- Ryuji Hamamoto
- Yusuke Nakamura
- N. Dohmae
- Takehiro Suzuki
- S. Hayami
- Lianhua Piao
- Bruce A. J. Ponder
- Makoto Nakakido
Citations in the corpus
- SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells (2015, methodology): “In vitro methyltransferase assays were performed as described previously [7, 44-50].”
- SMYD3-mediated lysine methylation in the PH domain is critical for activation of AKT1 (2016, unknown): “SET and MYND domain-containing protein 3 (SMYD3) is a protein lysine methyltransferase, involved in colorectal cancer, hepatocellular carcinoma and breast cancer [10–14].”
- Overexpression of the JmjC histone demethylase KDM5B in human carcinogenesis: involvement in the proliferation of cancer cells through the E2F/RB pathway (2010, background): “We previously reported that SMYD3, a histone methyltransferase, stimulates cell proliferation through its methyltransferase activity and plays a crucial role in human carcinogenesis [6-10].”