Molecules and Cells

Cited by CrossRef (29)

  1. Xiao-Lei Huang, Li Zhang, Yu Duan, Yu-Jie Wang, Jiu-Hua Zhao, Jing Wang. E3 ubiquitin ligase: A potential regulator in fibrosis and systemic sclerosis. Cellular Immunology 2016;306-307:1
    https://doi.org/10.1016/j.cellimm.2016.07.003
  2. Li-ping Wang, Jia-nan Geng, Bo Sun, Cheng-bo Sun, Yan Shi, Xiao-yan Yu. MiR-92b-3p is Induced by Advanced Glycation End Products and Involved in the Pathogenesis of Diabetic Nephropathy. Evidence-Based Complementary and Alternative Medicine 2020;2020:1
    https://doi.org/10.1155/2020/6050874
  3. Jinlu Ma, Mengjiao Cai, Yaqi Mo, Joshua S. Fried, Xinyue Tan, Yuan Ma, Jie Chen, Suxia Han, Bo Xu. The SPOP-ITCH Signaling Axis Protects Against Prostate Cancer Metastasis. Front. Oncol. 2021;11
    https://doi.org/10.3389/fonc.2021.658230
  4. Hong-Yang Luo, Jie-Ying Zhu, Min Chen, Wang-Jing Mu, Liang Guo. Krüppel-like factor 10 (KLF10) as a critical signaling mediator: Versatile functions in physiological and pathophysiological processes. Genes & Diseases 2023;10:915
    https://doi.org/10.1016/j.gendis.2022.06.005
  5. A S Chandhoke, K Karve, S Dadakhujaev, S Netherton, L Deng, S Bonni. The ubiquitin ligase Smurf2 suppresses TGFβ-induced epithelial–mesenchymal transition in a sumoylation-regulated manner. Cell Death Differ 2016;23:876
    https://doi.org/10.1038/cdd.2015.152
  6. Natania S Field, Emily K Moser, Paula M Oliver. Itch regulation of innate and adaptive immune responses in mice and humans. 2020;108:353
    https://doi.org/10.1002/JLB.3MIR0320-272R
  7. Zhiwei Li, Guanwen Li, Yunfei Li, Yujie Luo, Yuhan Jiang, Ziyu Zhang, Ziyi Zhou, Shengde Liu, Chen Wu, Fuping You. Deubiquitinase OTUD6A Regulates Innate Immune Response via Targeting UBC13. Viruses 2023;15:1761
    https://doi.org/10.3390/v15081761
  8. Yihao Li, Chao Cui, Feng Xie, Szymon Kiełbasa, Hailiang Mei, Maarten van Dinther, Hans van Dam, Andreas Bauer, Long Zhang, Peter ten Dijke. VprBP mitigates TGF-β and Activin signaling by promoting Smurf1-mediated type I receptor degradation. 2020;12:138
    https://doi.org/10.1093/jmcb/mjz057
  9. Xinggang Wang, Christian De Geyter, Zanhui Jia, Ya Peng, Hong Zhang. HECTD1 regulates the expression of SNAIL: Implications for epithelial‑mesenchymal transition. Int J Oncol 2020
    https://doi.org/10.3892/ijo.2020.5002
  10. Nishi Kumari, Patrick William Jaynes, Azad Saei, Prasanna Vasudevan Iyengar, John Lalith Charles Richard, Pieter Johan Adam Eichhorn. The roles of ubiquitin modifying enzymes in neoplastic disease. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 2017;1868:456
    https://doi.org/10.1016/j.bbcan.2017.09.002
  11. Emily K. Moser, Paula M. Oliver. Regulation of autoimmune disease by the E3 ubiquitin ligase Itch. Cellular Immunology 2019;340:103916
    https://doi.org/10.1016/j.cellimm.2019.04.004
  12. Jente van Staalduinen, David Baker, Peter ten Dijke, Hans van Dam. Epithelial–mesenchymal-transition-inducing transcription factors: new targets for tackling chemoresistance in cancer?. Oncogene 2018;37:6195
    https://doi.org/10.1038/s41388-018-0378-x
  13. Xuan Shu, Shenyou Shu, Hongqiu Cheng. A novel lncRNA‐mediated trans‐regulatory mechanism in the development of cleft palate in mouse. Molec Gen & Gen Med 2019;7
    https://doi.org/10.1002/mgg3.522
  14. Nikol Baloghova, Tomas Lidak, Lukas Cermak. Ubiquitin Ligases Involved in the Regulation of Wnt, TGF-β, and Notch Signaling Pathways and Their Roles in Mouse Development and Homeostasis. Genes 2019;10:815
    https://doi.org/10.3390/genes10100815
  15. Andrea Rodríguez-Alonso, Alba Casas-Pais, Daniel Roca-Lema, Begoña Graña, Gabriela Romay, Angélica Figueroa. Regulation of Epithelial–Mesenchymal Plasticity by the E3 Ubiquitin-Ligases in Cancer. Cancers 2020;12:3093
    https://doi.org/10.3390/cancers12113093
  16. Xiangwei Xiao, Shane Fischbach, Tina Zhang, Congde Chen, Qingfeng Sheng, Ray Zimmerman, Sneha Patnaik, Joseph Fusco, Yungching Ming, Ping Guo, Chiyo Shiota, Krishna Prasadan, Nupur Gangopadhyay, Sohail Z. Husain, Henry Dong, George K. Gittes. SMAD3/Stat3 Signaling Mediates β-Cell Epithelial-Mesenchymal Transition in Chronic Pancreatitis–Related Diabetes. 2017;66:2646
    https://doi.org/10.2337/db17-0537
  17. Shanez Haouari, Patrick Vourc’h, Médéric Jeanne, Sylviane Marouillat, Charlotte Veyrat-Durebex, Débora Lanznaster, Frédéric Laumonnier, Philippe Corcia, Hélène Blasco, Christian R. Andres. The Roles of NEDD4 Subfamily of HECT E3 Ubiquitin Ligases in Neurodevelopment and Neurodegeneration. IJMS 2022;23:3882
    https://doi.org/10.3390/ijms23073882
  18. Arun Upadhyay, Ayeman Amanullah, Deepak Chhangani, Ribhav Mishra, Amit Mishra. Selective multifaceted E3 ubiquitin ligases barricade extreme defense: Potential therapeutic targets for neurodegeneration and ageing. Ageing Research Reviews 2015;24:138
    https://doi.org/10.1016/j.arr.2015.07.009
  19. Peter F. Renz, Daniel Spies, Panagiota Tsikrika, Anton Wutz, Tobias A. Beyer, Constance Ciaudo. Inhibition of FGF and TGF-β Pathways in hESCs Identify STOX2 as a Novel SMAD2/4 Cofactor. Biology 2020;9:470
    https://doi.org/10.3390/biology9120470
  20. Aiqin Sun, Xianyan Tian, Yifei Chen, Wannian Yang, Qiong Lin. Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer. Pathol. Oncol. Res. 2023;29
    https://doi.org/10.3389/pore.2023.1610931
  21. Sarah Kit Leng Lui, Prasanna Vasudevan Iyengar, Patrick Jaynes, Zul Fazreen Bin Adam Isa, Brendan Pang, Tuan Zea Tan, Pieter Johan Adam Eichhorn. USP 26 regulates TGF ‐β signaling by deubiquitinating and stabilizing SMAD 7 . EMBO Reports 2017;18:797
    https://doi.org/10.15252/embr.201643270
  22. Hui Yuan, Jiyu Xu, Xiaoyi Xu, Tielei Gao, Yuehong Wang, Yuqi Fan, Jing Hu, Yiying Shao, Bingbing Zhao, Hongzhu Li, Jian Sun, Changqing Xu. Calhex231 Alleviates High Glucose-Induced Myocardial Fibrosis via Inhibiting Itch-Ubiquitin Proteasome Pathway in Vitro. Biological & Pharmaceutical Bulletin 2019;42:1337
    https://doi.org/10.1248/bpb.b19-00090
  23. Charlotte de Ceuninck van Capelle, Maureen Spit, Peter ten Dijke. Current perspectives on inhibitory SMAD7 in health and disease. Critical Reviews in Biochemistry and Molecular Biology 2020;55:691
    https://doi.org/10.1080/10409238.2020.1828260
  24. Shufen He, Jianqi Xue, Pengxiu Cao, Jianyuan Hou, Yan Cui, Jing Chang, Liying Huang, Yu Han, Xianglin Duan, Ke Tan, Yumei Fan. JNK/Itch Axis Mediates the Lipopolysaccharide-Induced Ubiquitin–Proteasome–Dependent Degradation of Ferritin Light Chain in Murine Macrophage Cells. Inflammation 2022;45:1089
    https://doi.org/10.1007/s10753-021-01603-y
  25. Yiming Tu, Lei Xu, Jia Xu, Zhongyuan Bao, Wei Tian, Yangfan Ye, Guangchi Sun, Zong Miao, Honglu Chao, Yongping You, Ning Liu, Jing Ji. Loss of deubiquitylase USP2 triggers development of glioblastoma via TGF-β signaling. Oncogene 2022;41:2597
    https://doi.org/10.1038/s41388-022-02275-0
  26. Yiping Hu, Juan He, Lianhua He, Bihua Xu, Qingwen Wang. Expression and function of Smad7 in autoimmune and inflammatory diseases. J Mol Med 2021;99:1209
    https://doi.org/10.1007/s00109-021-02083-1
  27. Li Tang, Xue-Mei Yi, Jia Chen, Fu-Juan Chen, Wei Lou, Yun-Lu Gao, Jing Zhou, Li-Na Su, Xin Xu, Jia-Qing Lu, Jun Ma, Ning Yu, Yang-Feng Ding. Ubiquitin ligase UBE3C promotes melanoma progression by increasing epithelial-mesenchymal transition in melanoma cells. Oncotarget 2016;7:15738
    https://doi.org/10.18632/oncotarget.7393
  28. Yasuyuki Gen, Kohichiroh Yasui, Tomoko Kitaichi, Naoto Iwai, Kei Terasaki, Osamu Dohi, Hikaru Hashimoto, Hayato Fukui, Yutaka Inada, Akifumi Fukui, Masayasu Jo, Michihisa Moriguchi, Taichiro Nishikawa, Atushi Umemura, Kanji Yamaguchi, Hiroyuki Konishi, Yuji Naito, Yoshito Itoh. ASPP2 suppresses invasion and TGF-β1-induced epithelial–mesenchymal transition by inhibiting Smad7 degradation mediated by E3 ubiquitin ligase ITCH in gastric cancer. Cancer Letters 2017;398:52
    https://doi.org/10.1016/j.canlet.2017.04.002
  29. Paola Pontrelli, Francesca Conserva, Massimo Papale, Annarita Oranger, Mariagrazia Barozzino, Grazia Vocino, Maria Teres. Rocchetti, Margherita Gigante, Giuseppe Castellano, Michele Rossini, Simona Simone, Luigi Laviola, Francesco Giorgino, Giuseppe Grandaliano, Salvatore Paolo, Loreto Gesualdo. Lysine 63 ubiquitination is involved in the progression of tubular damage in diabetic nephropathy. FASEB j. 2017;31:308
    https://doi.org/10.1096/fj.201600382rr