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| 1 | Magnetic Fe_3O_4-Reduced Graphene Oxide Nanocomposites-Based Electrochemical Biosensing显示文摘An electrochemical biosensing platform was developed based on glucose oxidase(GOx)/Fe3O4-reduced graphene oxide(Fe3O4-RGO) nanosheets loaded on the magnetic glassy carbon electrode(MGCE).With the advantages of the magnetism, conductivity and biocompatibility of the Fe3O4-RGO nanosheets, the nanocomposites could be facilely adhered to the electrode surface by magnetically controllable assembling and beneficial to achieve the direct redox reactions and electrocatalytic behaviors of GOx immobilized into the nanocomposites. The biosensor exhibited good electrocatalytic activity, high sensitivity and stability. The current response is linear over glucose concentration ranging from 0.05 to 1.5 m M with a low detection limit of0.15 μM. Meanwhile, validation of the applicability of the biosensor was carried out by determining glucose in serum samples. The proposed protocol is simple, inexpensive and convenient, which shows great potential in biosensing application. | Lili Yu Hui Wu Beina Wu Ziyi Wang Hongmei Cao Congying Fu Nengqin Jia | 2014 | Nano-Micro Letters2014，6，3： | 4 |
| 2 | NAMPT-targeting PROTAC promotes antitumor immunity via suppressing myeloid-derived suppressor cell expansion显示文摘Nicotinamide phosphoribosyl transferase(NAMPT) is considered as a promising target for cancer therapy given its critical engagement in cancer metabolism and inflammation.However,therapeutic benefit of NAMPT enzymatic inhibitors appears very limited,likely due to the failure to intervene nonenzymatic functions of NAMPT.Herein,we show that NAMPT dampens antitumor immunity by promoting the expansion of tumor infiltrating myeloid derived suppressive cells(MDSCs) via a mechanism independent of its enzymatic activity.Using proteolysis-targeting chimera(PROTAC) technology,PROTAC A7 is identified as a potent and selective degrader of NAMPT,which degrades intracellular NAMPT(iNAMPT) via the ubiquitin-proteasome system,and in turn decreases the secretion of extracellular NAMPT(eNAMPT),the major player of the non-enzymatic activity of NAMPT.In vivo,PROTAC A7 efficiently degrades NAMPT,inhibits tumor infiltrating MDSCs,and boosts antitumor efficacy.Of note,the anticancer activity of PROTAC A7 is superior to NAMPT enzymatic inhibitors that fail to achieve the same impact on MDSCs.Together,our findings uncover the new role of enzymatically-independent function of NAMPT in remodeling the immunosuppressive tumor microenvironment,and reports the first NAMPT PROTAC A7 that is able to block the pro-tumor function of both iNAMPT and eNAMPT,pointing out a new direction for the development of NAMPT-targeted therapies. | Ying Wu Congying Pu Yixian Fu Guoqiang Dong Min Huang Chunquan Sheng | 2022 | Acta Pharmaceutica Sinica B2022，12，6： | 3 |
| 3 | Crystal structure of human Gadd45 reveals an active dimer显示文摘The human Gadd45 protein family plays critical roles in DNA repair,negative growth control,genomic stability,cell cycle checkpoints and apoptosis.Here we report the crystal structure of human Gadd45,revealing a unique dimer formed via a bundle of four parallel helices,involving the most conserved residues among the Gadd45 isoforms.Mutational analysis of human Gadd45 identified a conserved,highly acidic patch in the central region of the dimer for interaction with the proliferating cell nuclear antigen(PCNA),p21 and cdc2,suggesting that the parallel dimer is the active form for the interaction.Cellular assays indicate that:(1)dimerization of Gadd45 is necessary for apoptosis as well as growth inhibition,and that cell growth inhibition is caused by both cell cycle arrest and apoptosis;(2)a conserved and highly acidic patch on the dimer surface,including the important residues Glu87 and Asp89,is a putative interface for binding proteins related to the cell cycle,DNA repair and apoptosis.These results reveal the mechanism of self-association by Gadd45 proteins and the importance of this self-association for their biological function. | Wenzheng Zhang Sheng Fu Xuefeng Liu Xuelian Zhao Wenchi Zhang Wei Peng Congying Wu Yuanyuan Li Xuemei Li Mark Bartlam Zong-Hao Zeng Qimin Zhan Zihe Rao | 2011 | Protein & Cell2011，2，10： | 1 |
| 4 | Crystal structure of human Gadd45γreveals an active dimer显示文摘Erratum to:Protein Cell 2011,2(10):814-826 DOI 10.1007/s13238-011-1090-6 Due to typesetting errors,“gadd45”should be“Gadd45γ”in the following places:the article title,the 2^(nd),4^(th) and 5^(th) Gadd45 in the ABSTRACT,the KEYWORDS,the first subti-tle of“RESULTS AND DISCUSSION”section,the legend of Figure 1,the“data collection and processing”of MATERIALS AND METHODS section. | Wenzheng Zhang Sheng Fu Xuefeng Liu Xuelian Zhao Wenchi Zhang Wei Peng Congying Wu Yuanyuan Li Xuemei Li Mark Bartlam Zong-Hao Zeng Qimin Zhan Zihe Rao | 2012 | Protein & Cell2012，3，3： | 0 |
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