《人類NADPH sensor蛋白HSCARG調控機制研究》是鄭曉峰為項目負責人,北京大學為依託單位的重點項目。
基本介紹
- 中文名:人類NADPH sensor蛋白HSCARG調控機制研究
- 項目類別 :重點項目
- 項目負責人:鄭曉峰
- 依託單位 :北京大學
科研成果,項目摘要,
科研成果
序號 | 標題 | 類型 | 作者 |
---|---|---|---|
1 | The crystal structure of LidA, a translocated substrate of the Legionella pneumophila Type IV secretion system, reveals a novel folding. | 期刊論文 | Meng G|An X|Ye S|Liu Y|Zhu W|Zhang RG|Zheng XF| |
2 | HSCARG inhibits activation of NF-kappa B by interacting with I kappa B kinase-beta | 期刊論文 | Gan QN|Li TT|Hu B|Lian M|Zheng XF| |
3 | A CRM1-Dependent Nuclear Export Signal Controls Nucleocytoplasmic Translocation of HSCARG, Which Regulates NF-kappaB Activity | 期刊論文 | Zhang M|Hu B|Li T|Peng Y|Guan J|Lai S|Zheng XF| |
4 | hCINAP is a novel regulator of ribosomal protein-HDM2-p53 pathway by controlling NEDDylation of ribosomal protein S14 | 期刊論文 | Bai Dongmei|Ma Xinwei|Guan Junhong|Zheng Xiaofeng| |
5 | Structural and Functional Characterization of K339T Substitution Identified in the PB2 Subunit Cap-binding Pocket of Influenza A Virus | 期刊論文 | Liu Yong|Qin Kun|Meng Geng|Zhang Jinfang|Zhou Jianfang|Zhao Guangyu|Luo Ming|Zheng XF| |
6 | Human SI-CLP aggravates the inflammation of the arthritis and is a potential macrophage inflammatory regulator | 期刊論文 | Luo Ming|Zhao Wenming|Li Zhanguo|Zheng Xiaofeng| |
7 | Regulation of the HDM2-p53 pathway by ribosomal protein L6 in response to ribosomal stress | 期刊論文 | Bai, DM|Zhang JF|XIao WC|Zheng XF| |
8 | Crystallization and X-ray crystallographic analysis of the cap-binding domain of influenza A virus H1N1 polymerase subunit PB2 | 期刊論文 | Liu Y|Meng G|Luo M|Zheng XF| |
9 | Tip-to-tip interaction in the crystal packing of PACSIN 2 is important in regulating tubulation activity. | 期刊論文 | Bai X|Zheng XF| |
10 | HSCARG inhibits NADPH oxidase activity through regulation of the expression of p47phox. | 期刊論文 | Xiao WC|Peng YY|Li Z|Zheng XF| |
11 | Rigidity of Wedge Loop in PACSIN 3 Protein Is a Key Factor in Dictating Diameters of Tubules | 期刊論文 | Bai X|Meng G|Luo M|Zheng XF| |
項目摘要
HSCARG是我們新識別的人類NADPH sensor,我們已有結果表明它能感應細胞內氧化還原狀態的變化,發生核易位,並通過構象的改變來行使多種調節功能,是連線NADPH信號調控與一氧化氮信號通路的一個關鍵調控蛋白。HSCARG能夠通過泛素化-蛋白酶體降解途徑來調控細胞內COMMD1和NFkB的水平,是細胞生長必需的蛋白。但是,HSCARG調控細胞生長的分子機制仍有待於研究。本課題將結合生物化學、分子生物學、細胞生物學以及結構研究等多種手段,深入研究HSCARG感應細胞內氧化還原狀態的變化發生核易位的分子機制和它在入核後的調控作用;了解HSCARG調節不同蛋白泛素化的分子機制;尋找更多與HSCARG相互作用的蛋白,確定HSCARG參與的細胞信號傳導通路。這些研究有助於我們深入了解NADPH sensor在細胞調控網路中新的調控功能,對揭示NADPH sensor與疾病發生機制具有重要意義。