SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation.
By Ryuji Hamamoto, G. Toyokawa, Makoto Nakakido, K. Ueda, Yusuke Nakamura. 2014
93 citations recorded by the source corpus.
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- Takehiro Suzuki
- Lianhua Piao
- Ryuji Hamamoto
- Yusuke Nakamura
- N. Dohmae
- Rui Wang
- Jae-Hyun Park
- Xiaolan Deng
Citations in the corpus
- Critical roles of SMYD2-mediated β-catenin methylation for nuclear translocation and activation of Wnt signaling (2017, background): “Our group has reported critical roles of SMYD2-mediated methylation in tumorigenesis as a methyltransferase [6-9].”
- PRMT6 increases cytoplasmic localization of p21CDKN1A in cancer cells through arginine methylation and makes more resistant to cytotoxic agents (2015, background): “Even though whether PRMT6 methylates p21 in the nucleus or in the cytoplasm is still unknown, the present results imply that PRMT6 may play an important role in the functional regulation of not only histone proteins but also non-histone proteins as other histone methyltransferases [28–34].”
- Dysregulation of AKT Pathway by SMYD2-Mediated Lysine Methylation on PTEN (2015, unknown): “Our present and previous studies demonstrated that SMYD2 is mainly localized in the cytoplasm (Figure 2A) [21,29,42], implying that the functionally important substrates of SMYD2 in human tumorigenesis may not be histone proteins but non-histone cytoplasmic proteins.”
- 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].”