Molecules and Cells

Cited by CrossRef (12)

  1. Y. Gou, J. Li, O. Jackson-Weaver, J. Wu, T. Zhang, R. Gupta, I. Cho, T.V. Ho, Y. Chen, M. Li, S. Richard, J. Wang, Y. Chai, J. Xu. Protein Arginine Methyltransferase PRMT1 Is Essential for Palatogenesis. J Dent Res 2018;97:1510
    https://doi.org/10.1177/0022034518785164
  2. Jianlin Wang, Zhaoping Qiu, Yadi Wu. Ubiquitin Regulation: The Histone Modifying Enzyme′s Story. Cells 2018;7:118
    https://doi.org/10.3390/cells7090118
  3. Zhiwen Fan, Jianfei Li, Ping Li, Qing Ye, Huihui Xu, Xiaoyan Wu, Yong Xu. Protein arginine methyltransferase 1 (PRMT1) represses MHC II transcription in macrophages by methylating CIITA. Sci Rep 2017;7
    https://doi.org/10.1038/srep40531
  4. Ayad A. Al-Hamashi, Krystal Diaz, Rong Huang. Non-Histone Arginine Methylation by Protein Arginine Methyltransferases. CPPS 2020;21:699
    https://doi.org/10.2174/1389203721666200507091952
  5. Manami Hiraiwa, Kazuya Fukasawa, Takashi Iezaki, Hemragul Sabit, Tetsuhiro Horie, Kazuya Tokumura, Sayuki Iwahashi, Misato Murata, Masaki Kobayashi, Akane Suzuki, Gyujin Park, Katsuyuki Kaneda, Tomoki Todo, Atsushi Hirao, Mitsutoshi Nakada, Eiichi Hinoi. SMURF2 phosphorylation at Thr249 modifies glioma stemness and tumorigenicity by regulating TGF-β receptor stability. Commun Biol 2022;5
    https://doi.org/10.1038/s42003-021-02950-0
  6. Yu Zhu, Chao Yu, Shougang Zhuang. Protein arginine methyltransferase 1 mediates renal fibroblast activation and fibrogenesis through activation of Smad3 signaling. American Journal of Physiology-Renal Physiology 2020;318:F375
    https://doi.org/10.1152/ajprenal.00487.2019
  7. Qi Zhu, Dinghui Wang, Feng Liang, Xian Tong, Ziyun Liang, Xiaoyu Wang, Yaosheng Chen, Delin Mo. Protein arginine methyltransferase PRMT1 promotes adipogenesis by modulating transcription factors C/EBPβ and PPARγ. Journal of Biological Chemistry 2022;298:102309
    https://doi.org/10.1016/j.jbc.2022.102309
  8. Le Yu, Ling Dong, Hui Li, Zhaojian Liu, Zhong Luo, Guangjie Duan, Xiaotian Dai, Zhenghong Lin. Ubiquitination-mediated degradation of SIRT1 by SMURF2 suppresses CRC cell proliferation and tumorigenesis. Oncogene 2020;39:4450
    https://doi.org/10.1038/s41388-020-1298-0
  9. Longtao Yang, Wenwen Zhou, Hui Lin. Posttranslational Modifications of Smurfs: Emerging Regulation in Cancer. Front. Oncol. 2021;10
    https://doi.org/10.3389/fonc.2020.610663
  10. Yangjinming Bai, Ying Ying. The Post-translational Modifications of Smurf2 in TGF-β Signaling. Front. Mol. Biosci. 2020;7
    https://doi.org/10.3389/fmolb.2020.00128
  11. Lin Fu, Chun-Ping Cui, Xueli Zhang, Lingqiang Zhang. The functions and regulation of Smurfs in cancers. Seminars in Cancer Biology 2020;67:102
    https://doi.org/10.1016/j.semcancer.2019.12.023
  12. Melek Umay Tuz- Sasik, Elif Tugce Karoglu- Eravsar, Meric Kinali, Ayca Arslan- Ergul, Michelle M. Adams. Expression Levels of SMAD Specific E3 Ubiquitin Protein Ligase 2 (Smurf2) and its Interacting Partners Show Region-specific Alterations During Brain Aging. Neuroscience 2020;436:46
    https://doi.org/10.1016/j.neuroscience.2020.04.003