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您的检索式：作者名="TongHui Jiang"
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| 1 | Nuclear Aurora kinase A switches m^(6)A reader YTHDC1 to enhance an oncogenic RNA splicing of tumor suppressor RBM4显示文摘Aberrant RNA splicing produces alternative isoforms of genes to facilitate tumor progression,yet how this process is regulated by oncogenic signal remains largely unknown.Here,we unveil that non-canonical activation of nuclear AURKA promotes an oncogenic RNA splicing of tumor suppressor RBM4 directed by m^(6)A reader YTHDC1 in lung cancer.Nuclear translocation of AURKA is a prerequisite for RNA aberrant splicing,specifically triggering RBM4 splicing from the full isoform(RBM4-FL)to the short isoform(RBM4-S)in a kinase-independent manner. | SiSi Li YangFan Qi JiaChuan Yu YuChao Hao Bin He MengJuan Zhang ZhenWei Dai TongHui Jiang SuYi Li Fang Huang Ning Chen Jing Wang MengYing Yang DaPeng Liang Fan An JinYao Zhao WenJun Fan YuJia Pan ZiQian Deng YuanYuan Luo Tao Guo Fei Peng ZhiJie Hou ChunLi Wang FeiMeng Zheng LingZhi Xu Jie Xu QingPing Wen BiLian Jin Yang Wang Quentin Liu | 2022 | Signal Transduction and Targeted Therapy2022，7，5： | 4 |
| 2 | Identification of Cinobufagin and Resibufogenin as Inhibitors of Enterovirus 71 Infection显示文摘 | CHEN Jiawen XU Lin SUN Shiyang ZHANG Huafei MA Tonghui SU Weiheng JIANG Chunlai | 2014 | Chemical Research in Chinese Universities2014，30，6： | 1 |
| 3 | Importance of NPA motifs in the expression and function of water channel aquaporin-1显示文摘The asparagine-proline-alanine sequences (NPA motifs) are highly conserved in aquaporin water channel family. Crystallographic studies of AQP1 structure demonstrated that the two NPA motifs are in the narrow central constriction of the channel, serving to bind water molecules for selective and effi-cient water passage. To investigate the importance of the two NPA motifs in the structure, function and biogenesis of aquaporin water channels, we generated AQP1 mutations with NPA1 deletion, NPA2 de-letion and NPA1,2 double deletion. The coding sequences of the three mutated cDNAs were subcloned into the mammalian expression vector pcDNA3.1 to form expression plasmids. We established stably transfected CHO cell lines expressing these AQP1 mutants. Immunofluorescence indicated that all the three mutated AQP1 proteins are expressed normally on the plasma membrane of stably transfected CHO cells, suggesting that deletion of NPA motifs does not influence the expression and intracellular processing of AQP1. Functional analysis demonstrated that NPA1 or NPA2 deletion reduced AQP1 water permeability by 49.6% and 46.7%, respectively, while NPA1,2 double deletion had little effect on AQP1 water permeability. These results provide evidence that NPA motifs are important for water per-meation but not essential for the expression, intracellular processing and the basic structure of AQP1 water channel. | JIANG Yong MA TongHui | 2007 | Chinese Science Bulletin2007，52，6： | 1 |
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