The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3.
By M. Kunizaki, Ryuji Hamamoto, F. P. Silva, K. Yamaguchi, T. Nagayasu, M. Shibuya, Yusuke Nakamura, Yoichi Furukawa. 2007
149 citations recorded by the source corpus.
Subfields: Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
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
- Protein lysine methyltransferase SMYD3 is involved in tumorigenesis through regulation of HER2 homodimerization (2017, background): “the possible functions of methylation on these proteins were discussed [16, 17].”
- Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B (2012, unknown): “IB: HA (AURKB) HA–AURKB – – + – + – FLAG–AURKB-[1-200] FLAG–AURKB-[201-344]”
- 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): “In addition to histone proteins, SMYD3 methylates Vascular Endothelial Growth Factor Receptor 1 (VEGFR1) and Mitogen Activated Protein Kinase 2 (MAP3K2) [15, 16].”
- 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].”